data_9CH0
# 
_entry.id   9CH0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9CH0         pdb_00009ch0 10.2210/pdb9ch0/pdb 
WWPDB D_1000285493 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-29 
2 'Structure model' 1 1 2025-02-05 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Derived calculations' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' pdbx_struct_assembly      
2 2 'Structure model' pdbx_struct_assembly_gen  
3 2 'Structure model' pdbx_struct_assembly_prop 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CH0 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (no cofactor)' 9CGW 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA) heteromeric complex (with SAH)' 7LTE unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM mutant Y58F) and RiPP precursor (SonA) heteromeric complex (no cofactor)' 
7LTF unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM mutant Y93F) and RiPP precursor (SonA) heteromeric complex (no cofactor)' 
7LTH unspecified 
PDB 
;Structure of the heteromeric complex between the alpha-N-methyltransferase (SonM) and a truncated construct of the RiPP precursor (SonA) (with SAM)
;
7LTR unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM mutant R67A) and RiPP precursor (SonA) heteromeric complex (with SAH)' 7LTS 
unspecified 
PDB 
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA with QSY deletion) heteromeric complex (bound to SAM)' 
8T1T unspecified 
PDB 
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA with QSY deletion) heteromeric complex (bound to SAH)' 
8T1S unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mffreema@umn.edu 
_pdbx_contact_author.name_first         Michael 
_pdbx_contact_author.name_last          Freeman 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0491-9618 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Crone, K.K.'   1 ? 
'Labonte, J.W.' 2 ? 
'Elias, M.'     3 ? 
'Freeman, M.F.' 4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Protein Sci.' 
_citation.journal_id_ASTM           PRCIEI 
_citation.journal_id_CSD            0795 
_citation.journal_id_ISSN           1469-896X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            34 
_citation.language                  ? 
_citation.page_first                e70021 
_citation.page_last                 e70021 
_citation.title                     
'alpha-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/pro.70021 
_citation.pdbx_database_id_PubMed   39840790 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Crone, K.K.'   1 0000-0001-9888-4710 
primary 'Labonte, J.W.' 2 ?                   
primary 'Elias, M.H.'   3 0000-0003-0406-7539 
primary 'Freeman, M.F.' 4 0000-0002-0491-9618 
# 
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 'TP-methylase family protein'                                                      29068.326 4   ? ?    ? ? 
2 polymer     man 'Extradiol ring-cleavage dioxygenase LigAB LigA subunit domain-containing protein' 8869.756  2   ? I65W ? ? 
3 polymer     man 'Extradiol ring-cleavage dioxygenase LigAB LigA subunit domain-containing protein' 8855.729  2   ? I65W ? ? 
4 non-polymer man S-ADENOSYL-L-HOMOCYSTEINE                                                          384.411   4   ? ?    ? ? 
5 non-polymer syn 'ZINC ION'                                                                         65.409    2   ? ?    ? ? 
6 water       nat water                                                                              18.015    170 ? ?    ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDLG
;
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDLG
;
A,C,H,J ? 
2 'polypeptide(L)' no yes 
;MHHHHHHMSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSY(MLE)VWSHGN
GD
;
MHHHHHHMSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYLVWSHGNGD B,D     ? 
3 'polypeptide(L)' no no  MHHHHHHMSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYLVWSHGNGD 
MHHHHHHMSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYLVWSHGNGD I,K     ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 S-ADENOSYL-L-HOMOCYSTEINE SAH 
5 'ZINC ION'                ZN  
6 water                     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   GLY n 
1 3   SER n 
1 4   LEU n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   GLY n 
1 9   THR n 
1 10  GLY n 
1 11  LEU n 
1 12  GLN n 
1 13  LEU n 
1 14  ALA n 
1 15  GLY n 
1 16  GLN n 
1 17  ILE n 
1 18  SER n 
1 19  VAL n 
1 20  LEU n 
1 21  SER n 
1 22  ARG n 
1 23  SER n 
1 24  TYR n 
1 25  ILE n 
1 26  GLU n 
1 27  HIS n 
1 28  ALA n 
1 29  ASP n 
1 30  ILE n 
1 31  VAL n 
1 32  PHE n 
1 33  SER n 
1 34  LEU n 
1 35  LEU n 
1 36  PRO n 
1 37  ASP n 
1 38  GLY n 
1 39  PHE n 
1 40  SER n 
1 41  GLN n 
1 42  ARG n 
1 43  TRP n 
1 44  LEU n 
1 45  THR n 
1 46  LYS n 
1 47  LEU n 
1 48  ASN n 
1 49  PRO n 
1 50  ASN n 
1 51  VAL n 
1 52  ILE n 
1 53  ASN n 
1 54  LEU n 
1 55  GLN n 
1 56  GLN n 
1 57  PHE n 
1 58  TYR n 
1 59  ALA n 
1 60  GLN n 
1 61  ASN n 
1 62  GLY n 
1 63  GLU n 
1 64  VAL n 
1 65  LYS n 
1 66  ASN n 
1 67  ARG n 
1 68  ARG n 
1 69  ASP n 
1 70  THR n 
1 71  TYR n 
1 72  GLU n 
1 73  GLN n 
1 74  MET n 
1 75  VAL n 
1 76  ASN n 
1 77  ALA n 
1 78  ILE n 
1 79  LEU n 
1 80  ASP n 
1 81  ALA n 
1 82  VAL n 
1 83  ARG n 
1 84  ALA n 
1 85  GLY n 
1 86  LYS n 
1 87  LYS n 
1 88  THR n 
1 89  VAL n 
1 90  CYS n 
1 91  ALA n 
1 92  LEU n 
1 93  TYR n 
1 94  GLY n 
1 95  HIS n 
1 96  PRO n 
1 97  GLY n 
1 98  VAL n 
1 99  PHE n 
1 100 ALA n 
1 101 CYS n 
1 102 VAL n 
1 103 SER n 
1 104 HIS n 
1 105 MET n 
1 106 ALA n 
1 107 ILE n 
1 108 THR n 
1 109 ARG n 
1 110 ALA n 
1 111 LYS n 
1 112 ALA n 
1 113 GLU n 
1 114 GLY n 
1 115 PHE n 
1 116 SER n 
1 117 ALA n 
1 118 LYS n 
1 119 MET n 
1 120 GLU n 
1 121 PRO n 
1 122 GLY n 
1 123 ILE n 
1 124 SER n 
1 125 ALA n 
1 126 GLU n 
1 127 ALA n 
1 128 CYS n 
1 129 LEU n 
1 130 TRP n 
1 131 ALA n 
1 132 ASP n 
1 133 LEU n 
1 134 GLY n 
1 135 ILE n 
1 136 ASP n 
1 137 PRO n 
1 138 GLY n 
1 139 ASN n 
1 140 SER n 
1 141 GLY n 
1 142 HIS n 
1 143 GLN n 
1 144 SER n 
1 145 PHE n 
1 146 GLU n 
1 147 ALA n 
1 148 SER n 
1 149 GLN n 
1 150 PHE n 
1 151 MET n 
1 152 PHE n 
1 153 PHE n 
1 154 ASN n 
1 155 HIS n 
1 156 VAL n 
1 157 PRO n 
1 158 ASP n 
1 159 PRO n 
1 160 THR n 
1 161 THR n 
1 162 HIS n 
1 163 LEU n 
1 164 LEU n 
1 165 LEU n 
1 166 TRP n 
1 167 GLN n 
1 168 ILE n 
1 169 ALA n 
1 170 ILE n 
1 171 ALA n 
1 172 GLY n 
1 173 GLU n 
1 174 HIS n 
1 175 THR n 
1 176 LEU n 
1 177 THR n 
1 178 GLN n 
1 179 PHE n 
1 180 HIS n 
1 181 THR n 
1 182 SER n 
1 183 SER n 
1 184 ASP n 
1 185 ARG n 
1 186 LEU n 
1 187 GLN n 
1 188 ILE n 
1 189 LEU n 
1 190 VAL n 
1 191 GLU n 
1 192 GLN n 
1 193 LEU n 
1 194 ASN n 
1 195 GLN n 
1 196 TRP n 
1 197 TYR n 
1 198 PRO n 
1 199 LEU n 
1 200 ASP n 
1 201 HIS n 
1 202 GLU n 
1 203 VAL n 
1 204 VAL n 
1 205 ILE n 
1 206 TYR n 
1 207 GLU n 
1 208 ALA n 
1 209 ALA n 
1 210 ASN n 
1 211 LEU n 
1 212 PRO n 
1 213 ILE n 
1 214 GLN n 
1 215 ALA n 
1 216 PRO n 
1 217 ARG n 
1 218 ILE n 
1 219 GLU n 
1 220 ARG n 
1 221 LEU n 
1 222 PRO n 
1 223 LEU n 
1 224 ALA n 
1 225 ASN n 
1 226 LEU n 
1 227 PRO n 
1 228 GLN n 
1 229 ALA n 
1 230 HIS n 
1 231 LEU n 
1 232 MET n 
1 233 PRO n 
1 234 ILE n 
1 235 SER n 
1 236 THR n 
1 237 LEU n 
1 238 LEU n 
1 239 ILE n 
1 240 PRO n 
1 241 PRO n 
1 242 ALA n 
1 243 LYS n 
1 244 LYS n 
1 245 LEU n 
1 246 GLU n 
1 247 TYR n 
1 248 ASN n 
1 249 TYR n 
1 250 ALA n 
1 251 ILE n 
1 252 LEU n 
1 253 ALA n 
1 254 LYS n 
1 255 LEU n 
1 256 GLY n 
1 257 ILE n 
1 258 GLY n 
1 259 PRO n 
1 260 GLU n 
1 261 ASP n 
1 262 LEU n 
1 263 GLY n 
2 1   MET n 
2 2   HIS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   MET n 
2 9   SER n 
2 10  GLY n 
2 11  LEU n 
2 12  SER n 
2 13  ASP n 
2 14  PHE n 
2 15  PHE n 
2 16  THR n 
2 17  GLN n 
2 18  LEU n 
2 19  GLY n 
2 20  GLN n 
2 21  ASP n 
2 22  ALA n 
2 23  GLN n 
2 24  LEU n 
2 25  MET n 
2 26  GLU n 
2 27  ASP n 
2 28  TYR n 
2 29  LYS n 
2 30  GLN n 
2 31  ASN n 
2 32  PRO n 
2 33  GLU n 
2 34  ALA n 
2 35  VAL n 
2 36  MET n 
2 37  ARG n 
2 38  ALA n 
2 39  HIS n 
2 40  GLY n 
2 41  LEU n 
2 42  THR n 
2 43  ASP n 
2 44  GLU n 
2 45  GLN n 
2 46  ILE n 
2 47  ASN n 
2 48  ALA n 
2 49  VAL n 
2 50  MET n 
2 51  THR n 
2 52  GLY n 
2 53  ASP n 
2 54  MET n 
2 55  GLU n 
2 56  LYS n 
2 57  LEU n 
2 58  LYS n 
2 59  THR n 
2 60  LEU n 
2 61  SER n 
2 62  GLY n 
2 63  ASP n 
2 64  SER n 
2 65  SER n 
2 66  TYR n 
2 67  GLN n 
2 68  SER n 
2 69  TYR n 
2 70  MLE n 
2 71  VAL n 
2 72  TRP n 
2 73  SER n 
2 74  HIS n 
2 75  GLY n 
2 76  ASN n 
2 77  GLY n 
2 78  ASP n 
3 1   MET n 
3 2   HIS n 
3 3   HIS n 
3 4   HIS n 
3 5   HIS n 
3 6   HIS n 
3 7   HIS n 
3 8   MET n 
3 9   SER n 
3 10  GLY n 
3 11  LEU n 
3 12  SER n 
3 13  ASP n 
3 14  PHE n 
3 15  PHE n 
3 16  THR n 
3 17  GLN n 
3 18  LEU n 
3 19  GLY n 
3 20  GLN n 
3 21  ASP n 
3 22  ALA n 
3 23  GLN n 
3 24  LEU n 
3 25  MET n 
3 26  GLU n 
3 27  ASP n 
3 28  TYR n 
3 29  LYS n 
3 30  GLN n 
3 31  ASN n 
3 32  PRO n 
3 33  GLU n 
3 34  ALA n 
3 35  VAL n 
3 36  MET n 
3 37  ARG n 
3 38  ALA n 
3 39  HIS n 
3 40  GLY n 
3 41  LEU n 
3 42  THR n 
3 43  ASP n 
3 44  GLU n 
3 45  GLN n 
3 46  ILE n 
3 47  ASN n 
3 48  ALA n 
3 49  VAL n 
3 50  MET n 
3 51  THR n 
3 52  GLY n 
3 53  ASP n 
3 54  MET n 
3 55  GLU n 
3 56  LYS n 
3 57  LEU n 
3 58  LYS n 
3 59  THR n 
3 60  LEU n 
3 61  SER n 
3 62  GLY n 
3 63  ASP n 
3 64  SER n 
3 65  SER n 
3 66  TYR n 
3 67  GLN n 
3 68  SER n 
3 69  TYR n 
3 70  LEU n 
3 71  VAL n 
3 72  TRP n 
3 73  SER n 
3 74  HIS n 
3 75  GLY n 
3 76  ASN n 
3 77  GLY n 
3 78  ASP n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 263 ? ? SO_1478 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 78  ? ? SO_1479 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 78  ? ? SO_1479 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 263 ? ? SO_1478 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                   ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                  ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'           ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                  ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                 ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'           ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                   ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                 ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                     ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                   ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                    ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                ? 'C5 H11 N O2 S'   149.211 
MLE 'L-peptide linking' n N-METHYLLEUCINE           ? 'C7 H15 N O2'     145.199 
PHE 'L-peptide linking' y PHENYLALANINE             ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                   ? 'C5 H9 N O2'      115.130 
SAH non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE ? 'C14 H20 N6 O5 S' 384.411 
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 
ZN  non-polymer         . 'ZINC ION'                ? 'Zn 2'            65.409  
# 
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   1   ?   ?   ?   A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  GLN 16  16  16  GLN GLN A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  HIS 27  27  27  HIS HIS A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  TRP 43  43  43  TRP TRP A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  TYR 58  58  58  TYR TYR A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  MET 74  74  74  MET MET A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  LYS 86  86  86  LYS LYS A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  CYS 90  90  90  CYS CYS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  HIS 95  95  95  HIS HIS A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 MET 105 105 105 MET MET A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 TRP 130 130 130 TRP TRP A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 HIS 142 142 142 HIS HIS A . n 
A 1 143 GLN 143 143 143 GLN GLN A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 PHE 145 145 145 PHE PHE A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 MET 151 151 151 MET MET A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 ASN 154 154 154 ASN ASN A . n 
A 1 155 HIS 155 155 155 HIS HIS A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 HIS 162 162 162 HIS HIS A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 TRP 166 166 166 TRP TRP A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 ILE 168 168 168 ILE ILE A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 HIS 174 174 174 HIS HIS A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 GLN 178 178 178 GLN GLN A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 THR 181 181 181 THR THR A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 GLN 195 195 195 GLN GLN A . n 
A 1 196 TRP 196 196 196 TRP TRP A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 HIS 201 201 201 HIS HIS A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 GLN 214 214 214 GLN GLN A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 PRO 216 216 216 PRO PRO A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ASN 225 225 225 ASN ASN A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 HIS 230 230 230 HIS HIS A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 MET 232 232 232 MET MET A . n 
A 1 233 PRO 233 233 233 PRO PRO A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 ILE 239 239 239 ILE ILE A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 TYR 247 247 247 TYR TYR A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 TYR 249 249 249 TYR TYR A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 ILE 257 257 257 ILE ILE A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 PRO 259 259 259 PRO PRO A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
B 2 1   MET 1   -6  ?   ?   ?   B . n 
B 2 2   HIS 2   -5  ?   ?   ?   B . n 
B 2 3   HIS 3   -4  ?   ?   ?   B . n 
B 2 4   HIS 4   -3  ?   ?   ?   B . n 
B 2 5   HIS 5   -2  ?   ?   ?   B . n 
B 2 6   HIS 6   -1  ?   ?   ?   B . n 
B 2 7   HIS 7   0   ?   ?   ?   B . n 
B 2 8   MET 8   1   ?   ?   ?   B . n 
B 2 9   SER 9   2   ?   ?   ?   B . n 
B 2 10  GLY 10  3   3   GLY GLY B . n 
B 2 11  LEU 11  4   4   LEU LEU B . n 
B 2 12  SER 12  5   5   SER SER B . n 
B 2 13  ASP 13  6   6   ASP ASP B . n 
B 2 14  PHE 14  7   7   PHE PHE B . n 
B 2 15  PHE 15  8   8   PHE PHE B . n 
B 2 16  THR 16  9   9   THR THR B . n 
B 2 17  GLN 17  10  10  GLN GLN B . n 
B 2 18  LEU 18  11  11  LEU LEU B . n 
B 2 19  GLY 19  12  12  GLY GLY B . n 
B 2 20  GLN 20  13  13  GLN GLN B . n 
B 2 21  ASP 21  14  14  ASP ASP B . n 
B 2 22  ALA 22  15  15  ALA ALA B . n 
B 2 23  GLN 23  16  16  GLN GLN B . n 
B 2 24  LEU 24  17  17  LEU LEU B . n 
B 2 25  MET 25  18  18  MET MET B . n 
B 2 26  GLU 26  19  19  GLU GLU B . n 
B 2 27  ASP 27  20  20  ASP ASP B . n 
B 2 28  TYR 28  21  21  TYR TYR B . n 
B 2 29  LYS 29  22  22  LYS LYS B . n 
B 2 30  GLN 30  23  23  GLN GLN B . n 
B 2 31  ASN 31  24  24  ASN ASN B . n 
B 2 32  PRO 32  25  25  PRO PRO B . n 
B 2 33  GLU 33  26  26  GLU GLU B . n 
B 2 34  ALA 34  27  27  ALA ALA B . n 
B 2 35  VAL 35  28  28  VAL VAL B . n 
B 2 36  MET 36  29  29  MET MET B . n 
B 2 37  ARG 37  30  30  ARG ARG B . n 
B 2 38  ALA 38  31  31  ALA ALA B . n 
B 2 39  HIS 39  32  32  HIS HIS B . n 
B 2 40  GLY 40  33  33  GLY GLY B . n 
B 2 41  LEU 41  34  34  LEU LEU B . n 
B 2 42  THR 42  35  35  THR THR B . n 
B 2 43  ASP 43  36  36  ASP ASP B . n 
B 2 44  GLU 44  37  37  GLU GLU B . n 
B 2 45  GLN 45  38  38  GLN GLN B . n 
B 2 46  ILE 46  39  39  ILE ILE B . n 
B 2 47  ASN 47  40  40  ASN ASN B . n 
B 2 48  ALA 48  41  41  ALA ALA B . n 
B 2 49  VAL 49  42  42  VAL VAL B . n 
B 2 50  MET 50  43  43  MET MET B . n 
B 2 51  THR 51  44  44  THR THR B . n 
B 2 52  GLY 52  45  45  GLY GLY B . n 
B 2 53  ASP 53  46  46  ASP ASP B . n 
B 2 54  MET 54  47  47  MET MET B . n 
B 2 55  GLU 55  48  48  GLU GLU B . n 
B 2 56  LYS 56  49  49  LYS LYS B . n 
B 2 57  LEU 57  50  50  LEU LEU B . n 
B 2 58  LYS 58  51  51  LYS LYS B . n 
B 2 59  THR 59  52  52  THR THR B . n 
B 2 60  LEU 60  53  53  LEU LEU B . n 
B 2 61  SER 61  54  ?   ?   ?   B . n 
B 2 62  GLY 62  55  ?   ?   ?   B . n 
B 2 63  ASP 63  56  ?   ?   ?   B . n 
B 2 64  SER 64  57  ?   ?   ?   B . n 
B 2 65  SER 65  58  ?   ?   ?   B . n 
B 2 66  TYR 66  59  ?   ?   ?   B . n 
B 2 67  GLN 67  60  ?   ?   ?   B . n 
B 2 68  SER 68  61  61  SER SER B . n 
B 2 69  TYR 69  62  62  TYR TYR B . n 
B 2 70  MLE 70  63  63  MLE MLE B . n 
B 2 71  VAL 71  64  64  VAL VAL B . n 
B 2 72  TRP 72  65  65  TRP TRP B . n 
B 2 73  SER 73  66  66  SER SER B . n 
B 2 74  HIS 74  67  67  HIS HIS B . n 
B 2 75  GLY 75  68  ?   ?   ?   B . n 
B 2 76  ASN 76  69  ?   ?   ?   B . n 
B 2 77  GLY 77  70  ?   ?   ?   B . n 
B 2 78  ASP 78  71  ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   GLY 2   2   2   GLY GLY C . n 
C 1 3   SER 3   3   3   SER SER C . n 
C 1 4   LEU 4   4   4   LEU LEU C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   THR 9   9   9   THR THR C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  LEU 11  11  11  LEU LEU C . n 
C 1 12  GLN 12  12  12  GLN GLN C . n 
C 1 13  LEU 13  13  13  LEU LEU C . n 
C 1 14  ALA 14  14  14  ALA ALA C . n 
C 1 15  GLY 15  15  15  GLY GLY C . n 
C 1 16  GLN 16  16  16  GLN GLN C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  SER 18  18  18  SER SER C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  LEU 20  20  20  LEU LEU C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  ARG 22  22  22  ARG ARG C . n 
C 1 23  SER 23  23  23  SER SER C . n 
C 1 24  TYR 24  24  24  TYR TYR C . n 
C 1 25  ILE 25  25  25  ILE ILE C . n 
C 1 26  GLU 26  26  26  GLU GLU C . n 
C 1 27  HIS 27  27  27  HIS HIS C . n 
C 1 28  ALA 28  28  28  ALA ALA C . n 
C 1 29  ASP 29  29  29  ASP ASP C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  PHE 32  32  32  PHE PHE C . n 
C 1 33  SER 33  33  33  SER SER C . n 
C 1 34  LEU 34  34  34  LEU LEU C . n 
C 1 35  LEU 35  35  35  LEU LEU C . n 
C 1 36  PRO 36  36  36  PRO PRO C . n 
C 1 37  ASP 37  37  37  ASP ASP C . n 
C 1 38  GLY 38  38  38  GLY GLY C . n 
C 1 39  PHE 39  39  39  PHE PHE C . n 
C 1 40  SER 40  40  40  SER SER C . n 
C 1 41  GLN 41  41  41  GLN GLN C . n 
C 1 42  ARG 42  42  42  ARG ARG C . n 
C 1 43  TRP 43  43  43  TRP TRP C . n 
C 1 44  LEU 44  44  44  LEU LEU C . n 
C 1 45  THR 45  45  45  THR THR C . n 
C 1 46  LYS 46  46  46  LYS LYS C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  ASN 48  48  48  ASN ASN C . n 
C 1 49  PRO 49  49  49  PRO PRO C . n 
C 1 50  ASN 50  50  50  ASN ASN C . n 
C 1 51  VAL 51  51  51  VAL VAL C . n 
C 1 52  ILE 52  52  52  ILE ILE C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  LEU 54  54  54  LEU LEU C . n 
C 1 55  GLN 55  55  55  GLN GLN C . n 
C 1 56  GLN 56  56  56  GLN GLN C . n 
C 1 57  PHE 57  57  57  PHE PHE C . n 
C 1 58  TYR 58  58  58  TYR TYR C . n 
C 1 59  ALA 59  59  59  ALA ALA C . n 
C 1 60  GLN 60  60  60  GLN GLN C . n 
C 1 61  ASN 61  61  61  ASN ASN C . n 
C 1 62  GLY 62  62  62  GLY GLY C . n 
C 1 63  GLU 63  63  63  GLU GLU C . n 
C 1 64  VAL 64  64  64  VAL VAL C . n 
C 1 65  LYS 65  65  65  LYS LYS C . n 
C 1 66  ASN 66  66  66  ASN ASN C . n 
C 1 67  ARG 67  67  67  ARG ARG C . n 
C 1 68  ARG 68  68  68  ARG ARG C . n 
C 1 69  ASP 69  69  69  ASP ASP C . n 
C 1 70  THR 70  70  70  THR THR C . n 
C 1 71  TYR 71  71  71  TYR TYR C . n 
C 1 72  GLU 72  72  72  GLU GLU C . n 
C 1 73  GLN 73  73  73  GLN GLN C . n 
C 1 74  MET 74  74  74  MET MET C . n 
C 1 75  VAL 75  75  75  VAL VAL C . n 
C 1 76  ASN 76  76  76  ASN ASN C . n 
C 1 77  ALA 77  77  77  ALA ALA C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  LEU 79  79  79  LEU LEU C . n 
C 1 80  ASP 80  80  80  ASP ASP C . n 
C 1 81  ALA 81  81  81  ALA ALA C . n 
C 1 82  VAL 82  82  82  VAL VAL C . n 
C 1 83  ARG 83  83  83  ARG ARG C . n 
C 1 84  ALA 84  84  84  ALA ALA C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  LYS 86  86  86  LYS LYS C . n 
C 1 87  LYS 87  87  87  LYS LYS C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  VAL 89  89  89  VAL VAL C . n 
C 1 90  CYS 90  90  90  CYS CYS C . n 
C 1 91  ALA 91  91  91  ALA ALA C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  TYR 93  93  93  TYR TYR C . n 
C 1 94  GLY 94  94  94  GLY GLY C . n 
C 1 95  HIS 95  95  95  HIS HIS C . n 
C 1 96  PRO 96  96  96  PRO PRO C . n 
C 1 97  GLY 97  97  97  GLY GLY C . n 
C 1 98  VAL 98  98  98  VAL VAL C . n 
C 1 99  PHE 99  99  99  PHE PHE C . n 
C 1 100 ALA 100 100 100 ALA ALA C . n 
C 1 101 CYS 101 101 101 CYS CYS C . n 
C 1 102 VAL 102 102 102 VAL VAL C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 HIS 104 104 104 HIS HIS C . n 
C 1 105 MET 105 105 105 MET MET C . n 
C 1 106 ALA 106 106 106 ALA ALA C . n 
C 1 107 ILE 107 107 107 ILE ILE C . n 
C 1 108 THR 108 108 108 THR THR C . n 
C 1 109 ARG 109 109 109 ARG ARG C . n 
C 1 110 ALA 110 110 110 ALA ALA C . n 
C 1 111 LYS 111 111 111 LYS LYS C . n 
C 1 112 ALA 112 112 112 ALA ALA C . n 
C 1 113 GLU 113 113 113 GLU GLU C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 PHE 115 115 115 PHE PHE C . n 
C 1 116 SER 116 116 116 SER SER C . n 
C 1 117 ALA 117 117 117 ALA ALA C . n 
C 1 118 LYS 118 118 118 LYS LYS C . n 
C 1 119 MET 119 119 119 MET MET C . n 
C 1 120 GLU 120 120 120 GLU GLU C . n 
C 1 121 PRO 121 121 121 PRO PRO C . n 
C 1 122 GLY 122 122 122 GLY GLY C . n 
C 1 123 ILE 123 123 123 ILE ILE C . n 
C 1 124 SER 124 124 124 SER SER C . n 
C 1 125 ALA 125 125 125 ALA ALA C . n 
C 1 126 GLU 126 126 126 GLU GLU C . n 
C 1 127 ALA 127 127 127 ALA ALA C . n 
C 1 128 CYS 128 128 128 CYS CYS C . n 
C 1 129 LEU 129 129 129 LEU LEU C . n 
C 1 130 TRP 130 130 130 TRP TRP C . n 
C 1 131 ALA 131 131 131 ALA ALA C . n 
C 1 132 ASP 132 132 132 ASP ASP C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 GLY 134 134 134 GLY GLY C . n 
C 1 135 ILE 135 135 135 ILE ILE C . n 
C 1 136 ASP 136 136 136 ASP ASP C . n 
C 1 137 PRO 137 137 137 PRO PRO C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 SER 140 140 140 SER SER C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 HIS 142 142 142 HIS HIS C . n 
C 1 143 GLN 143 143 143 GLN GLN C . n 
C 1 144 SER 144 144 144 SER SER C . n 
C 1 145 PHE 145 145 145 PHE PHE C . n 
C 1 146 GLU 146 146 146 GLU GLU C . n 
C 1 147 ALA 147 147 147 ALA ALA C . n 
C 1 148 SER 148 148 148 SER SER C . n 
C 1 149 GLN 149 149 149 GLN GLN C . n 
C 1 150 PHE 150 150 150 PHE PHE C . n 
C 1 151 MET 151 151 151 MET MET C . n 
C 1 152 PHE 152 152 152 PHE PHE C . n 
C 1 153 PHE 153 153 153 PHE PHE C . n 
C 1 154 ASN 154 154 154 ASN ASN C . n 
C 1 155 HIS 155 155 155 HIS HIS C . n 
C 1 156 VAL 156 156 156 VAL VAL C . n 
C 1 157 PRO 157 157 157 PRO PRO C . n 
C 1 158 ASP 158 158 158 ASP ASP C . n 
C 1 159 PRO 159 159 159 PRO PRO C . n 
C 1 160 THR 160 160 160 THR THR C . n 
C 1 161 THR 161 161 161 THR THR C . n 
C 1 162 HIS 162 162 162 HIS HIS C . n 
C 1 163 LEU 163 163 163 LEU LEU C . n 
C 1 164 LEU 164 164 164 LEU LEU C . n 
C 1 165 LEU 165 165 165 LEU LEU C . n 
C 1 166 TRP 166 166 166 TRP TRP C . n 
C 1 167 GLN 167 167 167 GLN GLN C . n 
C 1 168 ILE 168 168 168 ILE ILE C . n 
C 1 169 ALA 169 169 169 ALA ALA C . n 
C 1 170 ILE 170 170 170 ILE ILE C . n 
C 1 171 ALA 171 171 171 ALA ALA C . n 
C 1 172 GLY 172 172 172 GLY GLY C . n 
C 1 173 GLU 173 173 173 GLU GLU C . n 
C 1 174 HIS 174 174 174 HIS HIS C . n 
C 1 175 THR 175 175 175 THR THR C . n 
C 1 176 LEU 176 176 176 LEU LEU C . n 
C 1 177 THR 177 177 177 THR THR C . n 
C 1 178 GLN 178 178 178 GLN GLN C . n 
C 1 179 PHE 179 179 179 PHE PHE C . n 
C 1 180 HIS 180 180 180 HIS HIS C . n 
C 1 181 THR 181 181 181 THR THR C . n 
C 1 182 SER 182 182 182 SER SER C . n 
C 1 183 SER 183 183 183 SER SER C . n 
C 1 184 ASP 184 184 184 ASP ASP C . n 
C 1 185 ARG 185 185 185 ARG ARG C . n 
C 1 186 LEU 186 186 186 LEU LEU C . n 
C 1 187 GLN 187 187 187 GLN GLN C . n 
C 1 188 ILE 188 188 188 ILE ILE C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 VAL 190 190 190 VAL VAL C . n 
C 1 191 GLU 191 191 191 GLU GLU C . n 
C 1 192 GLN 192 192 192 GLN GLN C . n 
C 1 193 LEU 193 193 193 LEU LEU C . n 
C 1 194 ASN 194 194 194 ASN ASN C . n 
C 1 195 GLN 195 195 195 GLN GLN C . n 
C 1 196 TRP 196 196 196 TRP TRP C . n 
C 1 197 TYR 197 197 197 TYR TYR C . n 
C 1 198 PRO 198 198 198 PRO PRO C . n 
C 1 199 LEU 199 199 199 LEU LEU C . n 
C 1 200 ASP 200 200 200 ASP ASP C . n 
C 1 201 HIS 201 201 201 HIS HIS C . n 
C 1 202 GLU 202 202 202 GLU GLU C . n 
C 1 203 VAL 203 203 203 VAL VAL C . n 
C 1 204 VAL 204 204 204 VAL VAL C . n 
C 1 205 ILE 205 205 205 ILE ILE C . n 
C 1 206 TYR 206 206 206 TYR TYR C . n 
C 1 207 GLU 207 207 207 GLU GLU C . n 
C 1 208 ALA 208 208 208 ALA ALA C . n 
C 1 209 ALA 209 209 209 ALA ALA C . n 
C 1 210 ASN 210 210 210 ASN ASN C . n 
C 1 211 LEU 211 211 211 LEU LEU C . n 
C 1 212 PRO 212 212 212 PRO PRO C . n 
C 1 213 ILE 213 213 213 ILE ILE C . n 
C 1 214 GLN 214 214 214 GLN GLN C . n 
C 1 215 ALA 215 215 215 ALA ALA C . n 
C 1 216 PRO 216 216 216 PRO PRO C . n 
C 1 217 ARG 217 217 217 ARG ARG C . n 
C 1 218 ILE 218 218 218 ILE ILE C . n 
C 1 219 GLU 219 219 219 GLU GLU C . n 
C 1 220 ARG 220 220 220 ARG ARG C . n 
C 1 221 LEU 221 221 221 LEU LEU C . n 
C 1 222 PRO 222 222 222 PRO PRO C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 ASN 225 225 225 ASN ASN C . n 
C 1 226 LEU 226 226 226 LEU LEU C . n 
C 1 227 PRO 227 227 227 PRO PRO C . n 
C 1 228 GLN 228 228 228 GLN GLN C . n 
C 1 229 ALA 229 229 229 ALA ALA C . n 
C 1 230 HIS 230 230 230 HIS HIS C . n 
C 1 231 LEU 231 231 231 LEU LEU C . n 
C 1 232 MET 232 232 232 MET MET C . n 
C 1 233 PRO 233 233 233 PRO PRO C . n 
C 1 234 ILE 234 234 234 ILE ILE C . n 
C 1 235 SER 235 235 235 SER SER C . n 
C 1 236 THR 236 236 236 THR THR C . n 
C 1 237 LEU 237 237 237 LEU LEU C . n 
C 1 238 LEU 238 238 238 LEU LEU C . n 
C 1 239 ILE 239 239 239 ILE ILE C . n 
C 1 240 PRO 240 240 240 PRO PRO C . n 
C 1 241 PRO 241 241 241 PRO PRO C . n 
C 1 242 ALA 242 242 242 ALA ALA C . n 
C 1 243 LYS 243 243 243 LYS LYS C . n 
C 1 244 LYS 244 244 244 LYS LYS C . n 
C 1 245 LEU 245 245 245 LEU LEU C . n 
C 1 246 GLU 246 246 246 GLU GLU C . n 
C 1 247 TYR 247 247 247 TYR TYR C . n 
C 1 248 ASN 248 248 248 ASN ASN C . n 
C 1 249 TYR 249 249 249 TYR TYR C . n 
C 1 250 ALA 250 250 250 ALA ALA C . n 
C 1 251 ILE 251 251 251 ILE ILE C . n 
C 1 252 LEU 252 252 252 LEU LEU C . n 
C 1 253 ALA 253 253 253 ALA ALA C . n 
C 1 254 LYS 254 254 254 LYS LYS C . n 
C 1 255 LEU 255 255 255 LEU LEU C . n 
C 1 256 GLY 256 256 256 GLY GLY C . n 
C 1 257 ILE 257 257 257 ILE ILE C . n 
C 1 258 GLY 258 258 258 GLY GLY C . n 
C 1 259 PRO 259 259 259 PRO PRO C . n 
C 1 260 GLU 260 260 260 GLU GLU C . n 
C 1 261 ASP 261 261 261 ASP ASP C . n 
C 1 262 LEU 262 262 262 LEU LEU C . n 
C 1 263 GLY 263 263 263 GLY GLY C . n 
D 2 1   MET 1   -6  ?   ?   ?   D . n 
D 2 2   HIS 2   -5  ?   ?   ?   D . n 
D 2 3   HIS 3   -4  ?   ?   ?   D . n 
D 2 4   HIS 4   -3  ?   ?   ?   D . n 
D 2 5   HIS 5   -2  ?   ?   ?   D . n 
D 2 6   HIS 6   -1  ?   ?   ?   D . n 
D 2 7   HIS 7   0   ?   ?   ?   D . n 
D 2 8   MET 8   1   ?   ?   ?   D . n 
D 2 9   SER 9   2   ?   ?   ?   D . n 
D 2 10  GLY 10  3   ?   ?   ?   D . n 
D 2 11  LEU 11  4   4   LEU LEU D . n 
D 2 12  SER 12  5   5   SER SER D . n 
D 2 13  ASP 13  6   6   ASP ASP D . n 
D 2 14  PHE 14  7   7   PHE PHE D . n 
D 2 15  PHE 15  8   8   PHE PHE D . n 
D 2 16  THR 16  9   9   THR THR D . n 
D 2 17  GLN 17  10  10  GLN GLN D . n 
D 2 18  LEU 18  11  11  LEU LEU D . n 
D 2 19  GLY 19  12  12  GLY GLY D . n 
D 2 20  GLN 20  13  13  GLN GLN D . n 
D 2 21  ASP 21  14  14  ASP ASP D . n 
D 2 22  ALA 22  15  15  ALA ALA D . n 
D 2 23  GLN 23  16  16  GLN GLN D . n 
D 2 24  LEU 24  17  17  LEU LEU D . n 
D 2 25  MET 25  18  18  MET MET D . n 
D 2 26  GLU 26  19  19  GLU GLU D . n 
D 2 27  ASP 27  20  20  ASP ASP D . n 
D 2 28  TYR 28  21  21  TYR TYR D . n 
D 2 29  LYS 29  22  22  LYS LYS D . n 
D 2 30  GLN 30  23  23  GLN GLN D . n 
D 2 31  ASN 31  24  24  ASN ASN D . n 
D 2 32  PRO 32  25  25  PRO PRO D . n 
D 2 33  GLU 33  26  26  GLU GLU D . n 
D 2 34  ALA 34  27  27  ALA ALA D . n 
D 2 35  VAL 35  28  28  VAL VAL D . n 
D 2 36  MET 36  29  29  MET MET D . n 
D 2 37  ARG 37  30  30  ARG ARG D . n 
D 2 38  ALA 38  31  31  ALA ALA D . n 
D 2 39  HIS 39  32  32  HIS HIS D . n 
D 2 40  GLY 40  33  33  GLY GLY D . n 
D 2 41  LEU 41  34  34  LEU LEU D . n 
D 2 42  THR 42  35  35  THR THR D . n 
D 2 43  ASP 43  36  36  ASP ASP D . n 
D 2 44  GLU 44  37  37  GLU GLU D . n 
D 2 45  GLN 45  38  38  GLN GLN D . n 
D 2 46  ILE 46  39  39  ILE ILE D . n 
D 2 47  ASN 47  40  40  ASN ASN D . n 
D 2 48  ALA 48  41  41  ALA ALA D . n 
D 2 49  VAL 49  42  42  VAL VAL D . n 
D 2 50  MET 50  43  43  MET MET D . n 
D 2 51  THR 51  44  44  THR THR D . n 
D 2 52  GLY 52  45  45  GLY GLY D . n 
D 2 53  ASP 53  46  46  ASP ASP D . n 
D 2 54  MET 54  47  47  MET MET D . n 
D 2 55  GLU 55  48  48  GLU GLU D . n 
D 2 56  LYS 56  49  49  LYS LYS D . n 
D 2 57  LEU 57  50  50  LEU LEU D . n 
D 2 58  LYS 58  51  51  LYS LYS D . n 
D 2 59  THR 59  52  52  THR THR D . n 
D 2 60  LEU 60  53  ?   ?   ?   D . n 
D 2 61  SER 61  54  ?   ?   ?   D . n 
D 2 62  GLY 62  55  ?   ?   ?   D . n 
D 2 63  ASP 63  56  ?   ?   ?   D . n 
D 2 64  SER 64  57  ?   ?   ?   D . n 
D 2 65  SER 65  58  ?   ?   ?   D . n 
D 2 66  TYR 66  59  ?   ?   ?   D . n 
D 2 67  GLN 67  60  ?   ?   ?   D . n 
D 2 68  SER 68  61  ?   ?   ?   D . n 
D 2 69  TYR 69  62  ?   ?   ?   D . n 
D 2 70  MLE 70  63  ?   ?   ?   D . n 
D 2 71  VAL 71  64  ?   ?   ?   D . n 
D 2 72  TRP 72  65  ?   ?   ?   D . n 
D 2 73  SER 73  66  ?   ?   ?   D . n 
D 2 74  HIS 74  67  ?   ?   ?   D . n 
D 2 75  GLY 75  68  ?   ?   ?   D . n 
D 2 76  ASN 76  69  ?   ?   ?   D . n 
D 2 77  GLY 77  70  ?   ?   ?   D . n 
D 2 78  ASP 78  71  ?   ?   ?   D . n 
E 1 1   MET 1   1   ?   ?   ?   H . n 
E 1 2   GLY 2   2   2   GLY GLY H . n 
E 1 3   SER 3   3   3   SER SER H . n 
E 1 4   LEU 4   4   4   LEU LEU H . n 
E 1 5   VAL 5   5   5   VAL VAL H . n 
E 1 6   CYS 6   6   6   CYS CYS H . n 
E 1 7   VAL 7   7   7   VAL VAL H . n 
E 1 8   GLY 8   8   8   GLY GLY H . n 
E 1 9   THR 9   9   9   THR THR H . n 
E 1 10  GLY 10  10  10  GLY GLY H . n 
E 1 11  LEU 11  11  11  LEU LEU H . n 
E 1 12  GLN 12  12  12  GLN GLN H . n 
E 1 13  LEU 13  13  13  LEU LEU H . n 
E 1 14  ALA 14  14  14  ALA ALA H . n 
E 1 15  GLY 15  15  15  GLY GLY H . n 
E 1 16  GLN 16  16  16  GLN GLN H . n 
E 1 17  ILE 17  17  17  ILE ILE H . n 
E 1 18  SER 18  18  18  SER SER H . n 
E 1 19  VAL 19  19  19  VAL VAL H . n 
E 1 20  LEU 20  20  20  LEU LEU H . n 
E 1 21  SER 21  21  21  SER SER H . n 
E 1 22  ARG 22  22  22  ARG ARG H . n 
E 1 23  SER 23  23  23  SER SER H . n 
E 1 24  TYR 24  24  24  TYR TYR H . n 
E 1 25  ILE 25  25  25  ILE ILE H . n 
E 1 26  GLU 26  26  26  GLU GLU H . n 
E 1 27  HIS 27  27  27  HIS HIS H . n 
E 1 28  ALA 28  28  28  ALA ALA H . n 
E 1 29  ASP 29  29  29  ASP ASP H . n 
E 1 30  ILE 30  30  30  ILE ILE H . n 
E 1 31  VAL 31  31  31  VAL VAL H . n 
E 1 32  PHE 32  32  32  PHE PHE H . n 
E 1 33  SER 33  33  33  SER SER H . n 
E 1 34  LEU 34  34  34  LEU LEU H . n 
E 1 35  LEU 35  35  35  LEU LEU H . n 
E 1 36  PRO 36  36  36  PRO PRO H . n 
E 1 37  ASP 37  37  37  ASP ASP H . n 
E 1 38  GLY 38  38  38  GLY GLY H . n 
E 1 39  PHE 39  39  39  PHE PHE H . n 
E 1 40  SER 40  40  40  SER SER H . n 
E 1 41  GLN 41  41  41  GLN GLN H . n 
E 1 42  ARG 42  42  42  ARG ARG H . n 
E 1 43  TRP 43  43  43  TRP TRP H . n 
E 1 44  LEU 44  44  44  LEU LEU H . n 
E 1 45  THR 45  45  45  THR THR H . n 
E 1 46  LYS 46  46  46  LYS LYS H . n 
E 1 47  LEU 47  47  47  LEU LEU H . n 
E 1 48  ASN 48  48  48  ASN ASN H . n 
E 1 49  PRO 49  49  49  PRO PRO H . n 
E 1 50  ASN 50  50  50  ASN ASN H . n 
E 1 51  VAL 51  51  51  VAL VAL H . n 
E 1 52  ILE 52  52  52  ILE ILE H . n 
E 1 53  ASN 53  53  53  ASN ASN H . n 
E 1 54  LEU 54  54  54  LEU LEU H . n 
E 1 55  GLN 55  55  55  GLN GLN H . n 
E 1 56  GLN 56  56  56  GLN GLN H . n 
E 1 57  PHE 57  57  57  PHE PHE H . n 
E 1 58  TYR 58  58  58  TYR TYR H . n 
E 1 59  ALA 59  59  59  ALA ALA H . n 
E 1 60  GLN 60  60  60  GLN GLN H . n 
E 1 61  ASN 61  61  61  ASN ASN H . n 
E 1 62  GLY 62  62  62  GLY GLY H . n 
E 1 63  GLU 63  63  63  GLU GLU H . n 
E 1 64  VAL 64  64  64  VAL VAL H . n 
E 1 65  LYS 65  65  65  LYS LYS H . n 
E 1 66  ASN 66  66  66  ASN ASN H . n 
E 1 67  ARG 67  67  67  ARG ARG H . n 
E 1 68  ARG 68  68  68  ARG ARG H . n 
E 1 69  ASP 69  69  69  ASP ASP H . n 
E 1 70  THR 70  70  70  THR THR H . n 
E 1 71  TYR 71  71  71  TYR TYR H . n 
E 1 72  GLU 72  72  72  GLU GLU H . n 
E 1 73  GLN 73  73  73  GLN GLN H . n 
E 1 74  MET 74  74  74  MET MET H . n 
E 1 75  VAL 75  75  75  VAL VAL H . n 
E 1 76  ASN 76  76  76  ASN ASN H . n 
E 1 77  ALA 77  77  77  ALA ALA H . n 
E 1 78  ILE 78  78  78  ILE ILE H . n 
E 1 79  LEU 79  79  79  LEU LEU H . n 
E 1 80  ASP 80  80  80  ASP ASP H . n 
E 1 81  ALA 81  81  81  ALA ALA H . n 
E 1 82  VAL 82  82  82  VAL VAL H . n 
E 1 83  ARG 83  83  83  ARG ARG H . n 
E 1 84  ALA 84  84  84  ALA ALA H . n 
E 1 85  GLY 85  85  85  GLY GLY H . n 
E 1 86  LYS 86  86  86  LYS LYS H . n 
E 1 87  LYS 87  87  87  LYS LYS H . n 
E 1 88  THR 88  88  88  THR THR H . n 
E 1 89  VAL 89  89  89  VAL VAL H . n 
E 1 90  CYS 90  90  90  CYS CYS H . n 
E 1 91  ALA 91  91  91  ALA ALA H . n 
E 1 92  LEU 92  92  92  LEU LEU H . n 
E 1 93  TYR 93  93  93  TYR TYR H . n 
E 1 94  GLY 94  94  94  GLY GLY H . n 
E 1 95  HIS 95  95  95  HIS HIS H . n 
E 1 96  PRO 96  96  96  PRO PRO H . n 
E 1 97  GLY 97  97  97  GLY GLY H . n 
E 1 98  VAL 98  98  98  VAL VAL H . n 
E 1 99  PHE 99  99  99  PHE PHE H . n 
E 1 100 ALA 100 100 100 ALA ALA H . n 
E 1 101 CYS 101 101 101 CYS CYS H . n 
E 1 102 VAL 102 102 102 VAL VAL H . n 
E 1 103 SER 103 103 103 SER SER H . n 
E 1 104 HIS 104 104 104 HIS HIS H . n 
E 1 105 MET 105 105 105 MET MET H . n 
E 1 106 ALA 106 106 106 ALA ALA H . n 
E 1 107 ILE 107 107 107 ILE ILE H . n 
E 1 108 THR 108 108 108 THR THR H . n 
E 1 109 ARG 109 109 109 ARG ARG H . n 
E 1 110 ALA 110 110 110 ALA ALA H . n 
E 1 111 LYS 111 111 111 LYS LYS H . n 
E 1 112 ALA 112 112 112 ALA ALA H . n 
E 1 113 GLU 113 113 113 GLU GLU H . n 
E 1 114 GLY 114 114 114 GLY GLY H . n 
E 1 115 PHE 115 115 115 PHE PHE H . n 
E 1 116 SER 116 116 116 SER SER H . n 
E 1 117 ALA 117 117 117 ALA ALA H . n 
E 1 118 LYS 118 118 118 LYS LYS H . n 
E 1 119 MET 119 119 119 MET MET H . n 
E 1 120 GLU 120 120 120 GLU GLU H . n 
E 1 121 PRO 121 121 121 PRO PRO H . n 
E 1 122 GLY 122 122 122 GLY GLY H . n 
E 1 123 ILE 123 123 123 ILE ILE H . n 
E 1 124 SER 124 124 124 SER SER H . n 
E 1 125 ALA 125 125 125 ALA ALA H . n 
E 1 126 GLU 126 126 126 GLU GLU H . n 
E 1 127 ALA 127 127 127 ALA ALA H . n 
E 1 128 CYS 128 128 128 CYS CYS H . n 
E 1 129 LEU 129 129 129 LEU LEU H . n 
E 1 130 TRP 130 130 130 TRP TRP H . n 
E 1 131 ALA 131 131 131 ALA ALA H . n 
E 1 132 ASP 132 132 132 ASP ASP H . n 
E 1 133 LEU 133 133 133 LEU LEU H . n 
E 1 134 GLY 134 134 134 GLY GLY H . n 
E 1 135 ILE 135 135 135 ILE ILE H . n 
E 1 136 ASP 136 136 136 ASP ASP H . n 
E 1 137 PRO 137 137 137 PRO PRO H . n 
E 1 138 GLY 138 138 138 GLY GLY H . n 
E 1 139 ASN 139 139 139 ASN ASN H . n 
E 1 140 SER 140 140 140 SER SER H . n 
E 1 141 GLY 141 141 141 GLY GLY H . n 
E 1 142 HIS 142 142 142 HIS HIS H . n 
E 1 143 GLN 143 143 143 GLN GLN H . n 
E 1 144 SER 144 144 144 SER SER H . n 
E 1 145 PHE 145 145 145 PHE PHE H . n 
E 1 146 GLU 146 146 146 GLU GLU H . n 
E 1 147 ALA 147 147 147 ALA ALA H . n 
E 1 148 SER 148 148 148 SER SER H . n 
E 1 149 GLN 149 149 149 GLN GLN H . n 
E 1 150 PHE 150 150 150 PHE PHE H . n 
E 1 151 MET 151 151 151 MET MET H . n 
E 1 152 PHE 152 152 152 PHE PHE H . n 
E 1 153 PHE 153 153 153 PHE PHE H . n 
E 1 154 ASN 154 154 154 ASN ASN H . n 
E 1 155 HIS 155 155 155 HIS HIS H . n 
E 1 156 VAL 156 156 156 VAL VAL H . n 
E 1 157 PRO 157 157 157 PRO PRO H . n 
E 1 158 ASP 158 158 158 ASP ASP H . n 
E 1 159 PRO 159 159 159 PRO PRO H . n 
E 1 160 THR 160 160 160 THR THR H . n 
E 1 161 THR 161 161 161 THR THR H . n 
E 1 162 HIS 162 162 162 HIS HIS H . n 
E 1 163 LEU 163 163 163 LEU LEU H . n 
E 1 164 LEU 164 164 164 LEU LEU H . n 
E 1 165 LEU 165 165 165 LEU LEU H . n 
E 1 166 TRP 166 166 166 TRP TRP H . n 
E 1 167 GLN 167 167 167 GLN GLN H . n 
E 1 168 ILE 168 168 168 ILE ILE H . n 
E 1 169 ALA 169 169 169 ALA ALA H . n 
E 1 170 ILE 170 170 170 ILE ILE H . n 
E 1 171 ALA 171 171 171 ALA ALA H . n 
E 1 172 GLY 172 172 172 GLY GLY H . n 
E 1 173 GLU 173 173 173 GLU GLU H . n 
E 1 174 HIS 174 174 174 HIS HIS H . n 
E 1 175 THR 175 175 175 THR THR H . n 
E 1 176 LEU 176 176 176 LEU LEU H . n 
E 1 177 THR 177 177 177 THR THR H . n 
E 1 178 GLN 178 178 178 GLN GLN H . n 
E 1 179 PHE 179 179 179 PHE PHE H . n 
E 1 180 HIS 180 180 180 HIS HIS H . n 
E 1 181 THR 181 181 181 THR THR H . n 
E 1 182 SER 182 182 182 SER SER H . n 
E 1 183 SER 183 183 183 SER SER H . n 
E 1 184 ASP 184 184 184 ASP ASP H . n 
E 1 185 ARG 185 185 185 ARG ARG H . n 
E 1 186 LEU 186 186 186 LEU LEU H . n 
E 1 187 GLN 187 187 187 GLN GLN H . n 
E 1 188 ILE 188 188 188 ILE ILE H . n 
E 1 189 LEU 189 189 189 LEU LEU H . n 
E 1 190 VAL 190 190 190 VAL VAL H . n 
E 1 191 GLU 191 191 191 GLU GLU H . n 
E 1 192 GLN 192 192 192 GLN GLN H . n 
E 1 193 LEU 193 193 193 LEU LEU H . n 
E 1 194 ASN 194 194 194 ASN ASN H . n 
E 1 195 GLN 195 195 195 GLN GLN H . n 
E 1 196 TRP 196 196 196 TRP TRP H . n 
E 1 197 TYR 197 197 197 TYR TYR H . n 
E 1 198 PRO 198 198 198 PRO PRO H . n 
E 1 199 LEU 199 199 199 LEU LEU H . n 
E 1 200 ASP 200 200 200 ASP ASP H . n 
E 1 201 HIS 201 201 201 HIS HIS H . n 
E 1 202 GLU 202 202 202 GLU GLU H . n 
E 1 203 VAL 203 203 203 VAL VAL H . n 
E 1 204 VAL 204 204 204 VAL VAL H . n 
E 1 205 ILE 205 205 205 ILE ILE H . n 
E 1 206 TYR 206 206 206 TYR TYR H . n 
E 1 207 GLU 207 207 207 GLU GLU H . n 
E 1 208 ALA 208 208 208 ALA ALA H . n 
E 1 209 ALA 209 209 209 ALA ALA H . n 
E 1 210 ASN 210 210 210 ASN ASN H . n 
E 1 211 LEU 211 211 211 LEU LEU H . n 
E 1 212 PRO 212 212 212 PRO PRO H . n 
E 1 213 ILE 213 213 213 ILE ILE H . n 
E 1 214 GLN 214 214 214 GLN GLN H . n 
E 1 215 ALA 215 215 215 ALA ALA H . n 
E 1 216 PRO 216 216 216 PRO PRO H . n 
E 1 217 ARG 217 217 217 ARG ARG H . n 
E 1 218 ILE 218 218 218 ILE ILE H . n 
E 1 219 GLU 219 219 219 GLU GLU H . n 
E 1 220 ARG 220 220 220 ARG ARG H . n 
E 1 221 LEU 221 221 221 LEU LEU H . n 
E 1 222 PRO 222 222 222 PRO PRO H . n 
E 1 223 LEU 223 223 223 LEU LEU H . n 
E 1 224 ALA 224 224 224 ALA ALA H . n 
E 1 225 ASN 225 225 225 ASN ASN H . n 
E 1 226 LEU 226 226 226 LEU LEU H . n 
E 1 227 PRO 227 227 227 PRO PRO H . n 
E 1 228 GLN 228 228 228 GLN GLN H . n 
E 1 229 ALA 229 229 229 ALA ALA H . n 
E 1 230 HIS 230 230 230 HIS HIS H . n 
E 1 231 LEU 231 231 231 LEU LEU H . n 
E 1 232 MET 232 232 232 MET MET H . n 
E 1 233 PRO 233 233 233 PRO PRO H . n 
E 1 234 ILE 234 234 234 ILE ILE H . n 
E 1 235 SER 235 235 235 SER SER H . n 
E 1 236 THR 236 236 236 THR THR H . n 
E 1 237 LEU 237 237 237 LEU LEU H . n 
E 1 238 LEU 238 238 238 LEU LEU H . n 
E 1 239 ILE 239 239 239 ILE ILE H . n 
E 1 240 PRO 240 240 240 PRO PRO H . n 
E 1 241 PRO 241 241 241 PRO PRO H . n 
E 1 242 ALA 242 242 242 ALA ALA H . n 
E 1 243 LYS 243 243 243 LYS LYS H . n 
E 1 244 LYS 244 244 244 LYS LYS H . n 
E 1 245 LEU 245 245 245 LEU LEU H . n 
E 1 246 GLU 246 246 246 GLU GLU H . n 
E 1 247 TYR 247 247 247 TYR TYR H . n 
E 1 248 ASN 248 248 248 ASN ASN H . n 
E 1 249 TYR 249 249 249 TYR TYR H . n 
E 1 250 ALA 250 250 250 ALA ALA H . n 
E 1 251 ILE 251 251 251 ILE ILE H . n 
E 1 252 LEU 252 252 252 LEU LEU H . n 
E 1 253 ALA 253 253 253 ALA ALA H . n 
E 1 254 LYS 254 254 254 LYS LYS H . n 
E 1 255 LEU 255 255 255 LEU LEU H . n 
E 1 256 GLY 256 256 256 GLY GLY H . n 
E 1 257 ILE 257 257 257 ILE ILE H . n 
E 1 258 GLY 258 258 258 GLY GLY H . n 
E 1 259 PRO 259 259 259 PRO PRO H . n 
E 1 260 GLU 260 260 260 GLU GLU H . n 
E 1 261 ASP 261 261 261 ASP ASP H . n 
E 1 262 LEU 262 262 262 LEU LEU H . n 
E 1 263 GLY 263 263 263 GLY GLY H . n 
F 3 1   MET 1   -6  ?   ?   ?   I . n 
F 3 2   HIS 2   -5  ?   ?   ?   I . n 
F 3 3   HIS 3   -4  ?   ?   ?   I . n 
F 3 4   HIS 4   -3  ?   ?   ?   I . n 
F 3 5   HIS 5   -2  ?   ?   ?   I . n 
F 3 6   HIS 6   -1  ?   ?   ?   I . n 
F 3 7   HIS 7   0   ?   ?   ?   I . n 
F 3 8   MET 8   1   ?   ?   ?   I . n 
F 3 9   SER 9   2   ?   ?   ?   I . n 
F 3 10  GLY 10  3   3   GLY GLY I . n 
F 3 11  LEU 11  4   4   LEU LEU I . n 
F 3 12  SER 12  5   5   SER SER I . n 
F 3 13  ASP 13  6   6   ASP ASP I . n 
F 3 14  PHE 14  7   7   PHE PHE I . n 
F 3 15  PHE 15  8   8   PHE PHE I . n 
F 3 16  THR 16  9   9   THR THR I . n 
F 3 17  GLN 17  10  10  GLN GLN I . n 
F 3 18  LEU 18  11  11  LEU LEU I . n 
F 3 19  GLY 19  12  12  GLY GLY I . n 
F 3 20  GLN 20  13  13  GLN GLN I . n 
F 3 21  ASP 21  14  14  ASP ASP I . n 
F 3 22  ALA 22  15  15  ALA ALA I . n 
F 3 23  GLN 23  16  16  GLN GLN I . n 
F 3 24  LEU 24  17  17  LEU LEU I . n 
F 3 25  MET 25  18  18  MET MET I . n 
F 3 26  GLU 26  19  19  GLU GLU I . n 
F 3 27  ASP 27  20  20  ASP ASP I . n 
F 3 28  TYR 28  21  21  TYR TYR I . n 
F 3 29  LYS 29  22  22  LYS LYS I . n 
F 3 30  GLN 30  23  23  GLN GLN I . n 
F 3 31  ASN 31  24  24  ASN ASN I . n 
F 3 32  PRO 32  25  25  PRO PRO I . n 
F 3 33  GLU 33  26  26  GLU GLU I . n 
F 3 34  ALA 34  27  27  ALA ALA I . n 
F 3 35  VAL 35  28  28  VAL VAL I . n 
F 3 36  MET 36  29  29  MET MET I . n 
F 3 37  ARG 37  30  30  ARG ARG I . n 
F 3 38  ALA 38  31  31  ALA ALA I . n 
F 3 39  HIS 39  32  32  HIS HIS I . n 
F 3 40  GLY 40  33  33  GLY GLY I . n 
F 3 41  LEU 41  34  34  LEU LEU I . n 
F 3 42  THR 42  35  35  THR THR I . n 
F 3 43  ASP 43  36  36  ASP ASP I . n 
F 3 44  GLU 44  37  37  GLU GLU I . n 
F 3 45  GLN 45  38  38  GLN GLN I . n 
F 3 46  ILE 46  39  39  ILE ILE I . n 
F 3 47  ASN 47  40  40  ASN ASN I . n 
F 3 48  ALA 48  41  41  ALA ALA I . n 
F 3 49  VAL 49  42  42  VAL VAL I . n 
F 3 50  MET 50  43  43  MET MET I . n 
F 3 51  THR 51  44  44  THR THR I . n 
F 3 52  GLY 52  45  45  GLY GLY I . n 
F 3 53  ASP 53  46  46  ASP ASP I . n 
F 3 54  MET 54  47  47  MET MET I . n 
F 3 55  GLU 55  48  48  GLU GLU I . n 
F 3 56  LYS 56  49  49  LYS LYS I . n 
F 3 57  LEU 57  50  50  LEU LEU I . n 
F 3 58  LYS 58  51  51  LYS LYS I . n 
F 3 59  THR 59  52  52  THR THR I . n 
F 3 60  LEU 60  53  53  LEU LEU I . n 
F 3 61  SER 61  54  ?   ?   ?   I . n 
F 3 62  GLY 62  55  ?   ?   ?   I . n 
F 3 63  ASP 63  56  ?   ?   ?   I . n 
F 3 64  SER 64  57  ?   ?   ?   I . n 
F 3 65  SER 65  58  ?   ?   ?   I . n 
F 3 66  TYR 66  59  ?   ?   ?   I . n 
F 3 67  GLN 67  60  ?   ?   ?   I . n 
F 3 68  SER 68  61  ?   ?   ?   I . n 
F 3 69  TYR 69  62  ?   ?   ?   I . n 
F 3 70  LEU 70  63  63  LEU LEU I . n 
F 3 71  VAL 71  64  64  VAL VAL I . n 
F 3 72  TRP 72  65  65  TRP TRP I . n 
F 3 73  SER 73  66  66  SER SER I . n 
F 3 74  HIS 74  67  ?   ?   ?   I . n 
F 3 75  GLY 75  68  ?   ?   ?   I . n 
F 3 76  ASN 76  69  ?   ?   ?   I . n 
F 3 77  GLY 77  70  ?   ?   ?   I . n 
F 3 78  ASP 78  71  ?   ?   ?   I . n 
G 1 1   MET 1   1   ?   ?   ?   J . n 
G 1 2   GLY 2   2   2   GLY GLY J . n 
G 1 3   SER 3   3   3   SER SER J . n 
G 1 4   LEU 4   4   4   LEU LEU J . n 
G 1 5   VAL 5   5   5   VAL VAL J . n 
G 1 6   CYS 6   6   6   CYS CYS J . n 
G 1 7   VAL 7   7   7   VAL VAL J . n 
G 1 8   GLY 8   8   8   GLY GLY J . n 
G 1 9   THR 9   9   9   THR THR J . n 
G 1 10  GLY 10  10  10  GLY GLY J . n 
G 1 11  LEU 11  11  11  LEU LEU J . n 
G 1 12  GLN 12  12  12  GLN GLN J . n 
G 1 13  LEU 13  13  13  LEU LEU J . n 
G 1 14  ALA 14  14  14  ALA ALA J . n 
G 1 15  GLY 15  15  15  GLY GLY J . n 
G 1 16  GLN 16  16  16  GLN GLN J . n 
G 1 17  ILE 17  17  17  ILE ILE J . n 
G 1 18  SER 18  18  18  SER SER J . n 
G 1 19  VAL 19  19  19  VAL VAL J . n 
G 1 20  LEU 20  20  20  LEU LEU J . n 
G 1 21  SER 21  21  21  SER SER J . n 
G 1 22  ARG 22  22  22  ARG ARG J . n 
G 1 23  SER 23  23  23  SER SER J . n 
G 1 24  TYR 24  24  24  TYR TYR J . n 
G 1 25  ILE 25  25  25  ILE ILE J . n 
G 1 26  GLU 26  26  26  GLU GLU J . n 
G 1 27  HIS 27  27  27  HIS HIS J . n 
G 1 28  ALA 28  28  28  ALA ALA J . n 
G 1 29  ASP 29  29  29  ASP ASP J . n 
G 1 30  ILE 30  30  30  ILE ILE J . n 
G 1 31  VAL 31  31  31  VAL VAL J . n 
G 1 32  PHE 32  32  32  PHE PHE J . n 
G 1 33  SER 33  33  33  SER SER J . n 
G 1 34  LEU 34  34  34  LEU LEU J . n 
G 1 35  LEU 35  35  35  LEU LEU J . n 
G 1 36  PRO 36  36  36  PRO PRO J . n 
G 1 37  ASP 37  37  37  ASP ASP J . n 
G 1 38  GLY 38  38  38  GLY GLY J . n 
G 1 39  PHE 39  39  39  PHE PHE J . n 
G 1 40  SER 40  40  40  SER SER J . n 
G 1 41  GLN 41  41  41  GLN GLN J . n 
G 1 42  ARG 42  42  42  ARG ARG J . n 
G 1 43  TRP 43  43  43  TRP TRP J . n 
G 1 44  LEU 44  44  44  LEU LEU J . n 
G 1 45  THR 45  45  45  THR THR J . n 
G 1 46  LYS 46  46  46  LYS LYS J . n 
G 1 47  LEU 47  47  47  LEU LEU J . n 
G 1 48  ASN 48  48  48  ASN ASN J . n 
G 1 49  PRO 49  49  49  PRO PRO J . n 
G 1 50  ASN 50  50  50  ASN ASN J . n 
G 1 51  VAL 51  51  51  VAL VAL J . n 
G 1 52  ILE 52  52  52  ILE ILE J . n 
G 1 53  ASN 53  53  53  ASN ASN J . n 
G 1 54  LEU 54  54  54  LEU LEU J . n 
G 1 55  GLN 55  55  55  GLN GLN J . n 
G 1 56  GLN 56  56  56  GLN GLN J . n 
G 1 57  PHE 57  57  57  PHE PHE J . n 
G 1 58  TYR 58  58  58  TYR TYR J . n 
G 1 59  ALA 59  59  59  ALA ALA J . n 
G 1 60  GLN 60  60  60  GLN GLN J . n 
G 1 61  ASN 61  61  61  ASN ASN J . n 
G 1 62  GLY 62  62  62  GLY GLY J . n 
G 1 63  GLU 63  63  63  GLU GLU J . n 
G 1 64  VAL 64  64  64  VAL VAL J . n 
G 1 65  LYS 65  65  65  LYS LYS J . n 
G 1 66  ASN 66  66  66  ASN ASN J . n 
G 1 67  ARG 67  67  67  ARG ARG J . n 
G 1 68  ARG 68  68  68  ARG ARG J . n 
G 1 69  ASP 69  69  69  ASP ASP J . n 
G 1 70  THR 70  70  70  THR THR J . n 
G 1 71  TYR 71  71  71  TYR TYR J . n 
G 1 72  GLU 72  72  72  GLU GLU J . n 
G 1 73  GLN 73  73  73  GLN GLN J . n 
G 1 74  MET 74  74  74  MET MET J . n 
G 1 75  VAL 75  75  75  VAL VAL J . n 
G 1 76  ASN 76  76  76  ASN ASN J . n 
G 1 77  ALA 77  77  77  ALA ALA J . n 
G 1 78  ILE 78  78  78  ILE ILE J . n 
G 1 79  LEU 79  79  79  LEU LEU J . n 
G 1 80  ASP 80  80  80  ASP ASP J . n 
G 1 81  ALA 81  81  81  ALA ALA J . n 
G 1 82  VAL 82  82  82  VAL VAL J . n 
G 1 83  ARG 83  83  83  ARG ARG J . n 
G 1 84  ALA 84  84  84  ALA ALA J . n 
G 1 85  GLY 85  85  85  GLY GLY J . n 
G 1 86  LYS 86  86  86  LYS LYS J . n 
G 1 87  LYS 87  87  87  LYS LYS J . n 
G 1 88  THR 88  88  88  THR THR J . n 
G 1 89  VAL 89  89  89  VAL VAL J . n 
G 1 90  CYS 90  90  90  CYS CYS J . n 
G 1 91  ALA 91  91  91  ALA ALA J . n 
G 1 92  LEU 92  92  92  LEU LEU J . n 
G 1 93  TYR 93  93  93  TYR TYR J . n 
G 1 94  GLY 94  94  94  GLY GLY J . n 
G 1 95  HIS 95  95  95  HIS HIS J . n 
G 1 96  PRO 96  96  96  PRO PRO J . n 
G 1 97  GLY 97  97  97  GLY GLY J . n 
G 1 98  VAL 98  98  98  VAL VAL J . n 
G 1 99  PHE 99  99  99  PHE PHE J . n 
G 1 100 ALA 100 100 100 ALA ALA J . n 
G 1 101 CYS 101 101 101 CYS CYS J . n 
G 1 102 VAL 102 102 102 VAL VAL J . n 
G 1 103 SER 103 103 103 SER SER J . n 
G 1 104 HIS 104 104 104 HIS HIS J . n 
G 1 105 MET 105 105 105 MET MET J . n 
G 1 106 ALA 106 106 106 ALA ALA J . n 
G 1 107 ILE 107 107 107 ILE ILE J . n 
G 1 108 THR 108 108 108 THR THR J . n 
G 1 109 ARG 109 109 109 ARG ARG J . n 
G 1 110 ALA 110 110 110 ALA ALA J . n 
G 1 111 LYS 111 111 111 LYS LYS J . n 
G 1 112 ALA 112 112 112 ALA ALA J . n 
G 1 113 GLU 113 113 113 GLU GLU J . n 
G 1 114 GLY 114 114 114 GLY GLY J . n 
G 1 115 PHE 115 115 115 PHE PHE J . n 
G 1 116 SER 116 116 116 SER SER J . n 
G 1 117 ALA 117 117 117 ALA ALA J . n 
G 1 118 LYS 118 118 118 LYS LYS J . n 
G 1 119 MET 119 119 119 MET MET J . n 
G 1 120 GLU 120 120 120 GLU GLU J . n 
G 1 121 PRO 121 121 121 PRO PRO J . n 
G 1 122 GLY 122 122 122 GLY GLY J . n 
G 1 123 ILE 123 123 123 ILE ILE J . n 
G 1 124 SER 124 124 124 SER SER J . n 
G 1 125 ALA 125 125 125 ALA ALA J . n 
G 1 126 GLU 126 126 126 GLU GLU J . n 
G 1 127 ALA 127 127 127 ALA ALA J . n 
G 1 128 CYS 128 128 128 CYS CYS J . n 
G 1 129 LEU 129 129 129 LEU LEU J . n 
G 1 130 TRP 130 130 130 TRP TRP J . n 
G 1 131 ALA 131 131 131 ALA ALA J . n 
G 1 132 ASP 132 132 132 ASP ASP J . n 
G 1 133 LEU 133 133 133 LEU LEU J . n 
G 1 134 GLY 134 134 134 GLY GLY J . n 
G 1 135 ILE 135 135 135 ILE ILE J . n 
G 1 136 ASP 136 136 136 ASP ASP J . n 
G 1 137 PRO 137 137 137 PRO PRO J . n 
G 1 138 GLY 138 138 138 GLY GLY J . n 
G 1 139 ASN 139 139 139 ASN ASN J . n 
G 1 140 SER 140 140 140 SER SER J . n 
G 1 141 GLY 141 141 141 GLY GLY J . n 
G 1 142 HIS 142 142 142 HIS HIS J . n 
G 1 143 GLN 143 143 143 GLN GLN J . n 
G 1 144 SER 144 144 144 SER SER J . n 
G 1 145 PHE 145 145 145 PHE PHE J . n 
G 1 146 GLU 146 146 146 GLU GLU J . n 
G 1 147 ALA 147 147 147 ALA ALA J . n 
G 1 148 SER 148 148 148 SER SER J . n 
G 1 149 GLN 149 149 149 GLN GLN J . n 
G 1 150 PHE 150 150 150 PHE PHE J . n 
G 1 151 MET 151 151 151 MET MET J . n 
G 1 152 PHE 152 152 152 PHE PHE J . n 
G 1 153 PHE 153 153 153 PHE PHE J . n 
G 1 154 ASN 154 154 154 ASN ASN J . n 
G 1 155 HIS 155 155 155 HIS HIS J . n 
G 1 156 VAL 156 156 156 VAL VAL J . n 
G 1 157 PRO 157 157 157 PRO PRO J . n 
G 1 158 ASP 158 158 158 ASP ASP J . n 
G 1 159 PRO 159 159 159 PRO PRO J . n 
G 1 160 THR 160 160 160 THR THR J . n 
G 1 161 THR 161 161 161 THR THR J . n 
G 1 162 HIS 162 162 162 HIS HIS J . n 
G 1 163 LEU 163 163 163 LEU LEU J . n 
G 1 164 LEU 164 164 164 LEU LEU J . n 
G 1 165 LEU 165 165 165 LEU LEU J . n 
G 1 166 TRP 166 166 166 TRP TRP J . n 
G 1 167 GLN 167 167 167 GLN GLN J . n 
G 1 168 ILE 168 168 168 ILE ILE J . n 
G 1 169 ALA 169 169 169 ALA ALA J . n 
G 1 170 ILE 170 170 170 ILE ILE J . n 
G 1 171 ALA 171 171 171 ALA ALA J . n 
G 1 172 GLY 172 172 172 GLY GLY J . n 
G 1 173 GLU 173 173 173 GLU GLU J . n 
G 1 174 HIS 174 174 174 HIS HIS J . n 
G 1 175 THR 175 175 175 THR THR J . n 
G 1 176 LEU 176 176 176 LEU LEU J . n 
G 1 177 THR 177 177 177 THR THR J . n 
G 1 178 GLN 178 178 178 GLN GLN J . n 
G 1 179 PHE 179 179 179 PHE PHE J . n 
G 1 180 HIS 180 180 180 HIS HIS J . n 
G 1 181 THR 181 181 181 THR THR J . n 
G 1 182 SER 182 182 182 SER SER J . n 
G 1 183 SER 183 183 183 SER SER J . n 
G 1 184 ASP 184 184 184 ASP ASP J . n 
G 1 185 ARG 185 185 185 ARG ARG J . n 
G 1 186 LEU 186 186 186 LEU LEU J . n 
G 1 187 GLN 187 187 187 GLN GLN J . n 
G 1 188 ILE 188 188 188 ILE ILE J . n 
G 1 189 LEU 189 189 189 LEU LEU J . n 
G 1 190 VAL 190 190 190 VAL VAL J . n 
G 1 191 GLU 191 191 191 GLU GLU J . n 
G 1 192 GLN 192 192 192 GLN GLN J . n 
G 1 193 LEU 193 193 193 LEU LEU J . n 
G 1 194 ASN 194 194 194 ASN ASN J . n 
G 1 195 GLN 195 195 195 GLN GLN J . n 
G 1 196 TRP 196 196 196 TRP TRP J . n 
G 1 197 TYR 197 197 197 TYR TYR J . n 
G 1 198 PRO 198 198 198 PRO PRO J . n 
G 1 199 LEU 199 199 199 LEU LEU J . n 
G 1 200 ASP 200 200 200 ASP ASP J . n 
G 1 201 HIS 201 201 201 HIS HIS J . n 
G 1 202 GLU 202 202 202 GLU GLU J . n 
G 1 203 VAL 203 203 203 VAL VAL J . n 
G 1 204 VAL 204 204 204 VAL VAL J . n 
G 1 205 ILE 205 205 205 ILE ILE J . n 
G 1 206 TYR 206 206 206 TYR TYR J . n 
G 1 207 GLU 207 207 207 GLU GLU J . n 
G 1 208 ALA 208 208 208 ALA ALA J . n 
G 1 209 ALA 209 209 209 ALA ALA J . n 
G 1 210 ASN 210 210 210 ASN ASN J . n 
G 1 211 LEU 211 211 211 LEU LEU J . n 
G 1 212 PRO 212 212 212 PRO PRO J . n 
G 1 213 ILE 213 213 213 ILE ILE J . n 
G 1 214 GLN 214 214 214 GLN GLN J . n 
G 1 215 ALA 215 215 215 ALA ALA J . n 
G 1 216 PRO 216 216 216 PRO PRO J . n 
G 1 217 ARG 217 217 217 ARG ARG J . n 
G 1 218 ILE 218 218 218 ILE ILE J . n 
G 1 219 GLU 219 219 219 GLU GLU J . n 
G 1 220 ARG 220 220 220 ARG ARG J . n 
G 1 221 LEU 221 221 221 LEU LEU J . n 
G 1 222 PRO 222 222 222 PRO PRO J . n 
G 1 223 LEU 223 223 223 LEU LEU J . n 
G 1 224 ALA 224 224 224 ALA ALA J . n 
G 1 225 ASN 225 225 225 ASN ASN J . n 
G 1 226 LEU 226 226 226 LEU LEU J . n 
G 1 227 PRO 227 227 227 PRO PRO J . n 
G 1 228 GLN 228 228 228 GLN GLN J . n 
G 1 229 ALA 229 229 229 ALA ALA J . n 
G 1 230 HIS 230 230 230 HIS HIS J . n 
G 1 231 LEU 231 231 231 LEU LEU J . n 
G 1 232 MET 232 232 232 MET MET J . n 
G 1 233 PRO 233 233 233 PRO PRO J . n 
G 1 234 ILE 234 234 234 ILE ILE J . n 
G 1 235 SER 235 235 235 SER SER J . n 
G 1 236 THR 236 236 236 THR THR J . n 
G 1 237 LEU 237 237 237 LEU LEU J . n 
G 1 238 LEU 238 238 238 LEU LEU J . n 
G 1 239 ILE 239 239 239 ILE ILE J . n 
G 1 240 PRO 240 240 240 PRO PRO J . n 
G 1 241 PRO 241 241 241 PRO PRO J . n 
G 1 242 ALA 242 242 242 ALA ALA J . n 
G 1 243 LYS 243 243 243 LYS LYS J . n 
G 1 244 LYS 244 244 244 LYS LYS J . n 
G 1 245 LEU 245 245 245 LEU LEU J . n 
G 1 246 GLU 246 246 246 GLU GLU J . n 
G 1 247 TYR 247 247 247 TYR TYR J . n 
G 1 248 ASN 248 248 248 ASN ASN J . n 
G 1 249 TYR 249 249 249 TYR TYR J . n 
G 1 250 ALA 250 250 250 ALA ALA J . n 
G 1 251 ILE 251 251 251 ILE ILE J . n 
G 1 252 LEU 252 252 252 LEU LEU J . n 
G 1 253 ALA 253 253 253 ALA ALA J . n 
G 1 254 LYS 254 254 254 LYS LYS J . n 
G 1 255 LEU 255 255 255 LEU LEU J . n 
G 1 256 GLY 256 256 256 GLY GLY J . n 
G 1 257 ILE 257 257 257 ILE ILE J . n 
G 1 258 GLY 258 258 258 GLY GLY J . n 
G 1 259 PRO 259 259 259 PRO PRO J . n 
G 1 260 GLU 260 260 260 GLU GLU J . n 
G 1 261 ASP 261 261 261 ASP ASP J . n 
G 1 262 LEU 262 262 262 LEU LEU J . n 
G 1 263 GLY 263 263 263 GLY GLY J . n 
H 3 1   MET 1   -6  ?   ?   ?   K . n 
H 3 2   HIS 2   -5  ?   ?   ?   K . n 
H 3 3   HIS 3   -4  ?   ?   ?   K . n 
H 3 4   HIS 4   -3  ?   ?   ?   K . n 
H 3 5   HIS 5   -2  ?   ?   ?   K . n 
H 3 6   HIS 6   -1  ?   ?   ?   K . n 
H 3 7   HIS 7   0   ?   ?   ?   K . n 
H 3 8   MET 8   1   ?   ?   ?   K . n 
H 3 9   SER 9   2   ?   ?   ?   K . n 
H 3 10  GLY 10  3   ?   ?   ?   K . n 
H 3 11  LEU 11  4   4   LEU LEU K . n 
H 3 12  SER 12  5   5   SER SER K . n 
H 3 13  ASP 13  6   6   ASP ASP K . n 
H 3 14  PHE 14  7   7   PHE PHE K . n 
H 3 15  PHE 15  8   8   PHE PHE K . n 
H 3 16  THR 16  9   9   THR THR K . n 
H 3 17  GLN 17  10  10  GLN GLN K . n 
H 3 18  LEU 18  11  11  LEU LEU K . n 
H 3 19  GLY 19  12  12  GLY GLY K . n 
H 3 20  GLN 20  13  13  GLN GLN K . n 
H 3 21  ASP 21  14  14  ASP ASP K . n 
H 3 22  ALA 22  15  15  ALA ALA K . n 
H 3 23  GLN 23  16  16  GLN GLN K . n 
H 3 24  LEU 24  17  17  LEU LEU K . n 
H 3 25  MET 25  18  18  MET MET K . n 
H 3 26  GLU 26  19  19  GLU GLU K . n 
H 3 27  ASP 27  20  20  ASP ASP K . n 
H 3 28  TYR 28  21  21  TYR TYR K . n 
H 3 29  LYS 29  22  22  LYS LYS K . n 
H 3 30  GLN 30  23  23  GLN GLN K . n 
H 3 31  ASN 31  24  24  ASN ASN K . n 
H 3 32  PRO 32  25  25  PRO PRO K . n 
H 3 33  GLU 33  26  26  GLU GLU K . n 
H 3 34  ALA 34  27  27  ALA ALA K . n 
H 3 35  VAL 35  28  28  VAL VAL K . n 
H 3 36  MET 36  29  29  MET MET K . n 
H 3 37  ARG 37  30  30  ARG ARG K . n 
H 3 38  ALA 38  31  31  ALA ALA K . n 
H 3 39  HIS 39  32  32  HIS HIS K . n 
H 3 40  GLY 40  33  33  GLY GLY K . n 
H 3 41  LEU 41  34  34  LEU LEU K . n 
H 3 42  THR 42  35  35  THR THR K . n 
H 3 43  ASP 43  36  36  ASP ASP K . n 
H 3 44  GLU 44  37  37  GLU GLU K . n 
H 3 45  GLN 45  38  38  GLN GLN K . n 
H 3 46  ILE 46  39  39  ILE ILE K . n 
H 3 47  ASN 47  40  40  ASN ASN K . n 
H 3 48  ALA 48  41  41  ALA ALA K . n 
H 3 49  VAL 49  42  42  VAL VAL K . n 
H 3 50  MET 50  43  43  MET MET K . n 
H 3 51  THR 51  44  44  THR THR K . n 
H 3 52  GLY 52  45  45  GLY GLY K . n 
H 3 53  ASP 53  46  46  ASP ASP K . n 
H 3 54  MET 54  47  47  MET MET K . n 
H 3 55  GLU 55  48  48  GLU GLU K . n 
H 3 56  LYS 56  49  49  LYS LYS K . n 
H 3 57  LEU 57  50  50  LEU LEU K . n 
H 3 58  LYS 58  51  51  LYS LYS K . n 
H 3 59  THR 59  52  52  THR THR K . n 
H 3 60  LEU 60  53  ?   ?   ?   K . n 
H 3 61  SER 61  54  ?   ?   ?   K . n 
H 3 62  GLY 62  55  ?   ?   ?   K . n 
H 3 63  ASP 63  56  ?   ?   ?   K . n 
H 3 64  SER 64  57  ?   ?   ?   K . n 
H 3 65  SER 65  58  ?   ?   ?   K . n 
H 3 66  TYR 66  59  ?   ?   ?   K . n 
H 3 67  GLN 67  60  ?   ?   ?   K . n 
H 3 68  SER 68  61  61  SER SER K . n 
H 3 69  TYR 69  62  62  TYR TYR K . n 
H 3 70  LEU 70  63  63  LEU LEU K . n 
H 3 71  VAL 71  64  64  VAL VAL K . n 
H 3 72  TRP 72  65  ?   ?   ?   K . n 
H 3 73  SER 73  66  ?   ?   ?   K . n 
H 3 74  HIS 74  67  ?   ?   ?   K . n 
H 3 75  GLY 75  68  ?   ?   ?   K . n 
H 3 76  ASN 76  69  ?   ?   ?   K . n 
H 3 77  GLY 77  70  ?   ?   ?   K . n 
H 3 78  ASP 78  71  ?   ?   ?   K . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 SAH ? ? SAH ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ZN  ? ? ZN  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
I 4 SAH 1  301 301 SAH SAH A . 
J 5 ZN  1  302 1   ZN  ZN  A . 
K 4 SAH 1  301 301 SAH SAH C . 
L 4 SAH 1  301 301 SAH SAH H . 
M 5 ZN  1  302 1   ZN  ZN  H . 
N 4 SAH 1  301 301 SAH SAH J . 
O 6 HOH 1  401 183 HOH HOH A . 
O 6 HOH 2  402 192 HOH HOH A . 
O 6 HOH 3  403 73  HOH HOH A . 
O 6 HOH 4  404 6   HOH HOH A . 
O 6 HOH 5  405 2   HOH HOH A . 
O 6 HOH 6  406 116 HOH HOH A . 
O 6 HOH 7  407 37  HOH HOH A . 
O 6 HOH 8  408 50  HOH HOH A . 
O 6 HOH 9  409 23  HOH HOH A . 
O 6 HOH 10 410 42  HOH HOH A . 
O 6 HOH 11 411 242 HOH HOH A . 
O 6 HOH 12 412 243 HOH HOH A . 
O 6 HOH 13 413 88  HOH HOH A . 
O 6 HOH 14 414 45  HOH HOH A . 
O 6 HOH 15 415 48  HOH HOH A . 
O 6 HOH 16 416 74  HOH HOH A . 
O 6 HOH 17 417 92  HOH HOH A . 
O 6 HOH 18 418 133 HOH HOH A . 
O 6 HOH 19 419 229 HOH HOH A . 
O 6 HOH 20 420 101 HOH HOH A . 
O 6 HOH 21 421 153 HOH HOH A . 
O 6 HOH 22 422 230 HOH HOH A . 
O 6 HOH 23 423 193 HOH HOH A . 
O 6 HOH 24 424 206 HOH HOH A . 
O 6 HOH 25 425 180 HOH HOH A . 
O 6 HOH 26 426 204 HOH HOH A . 
O 6 HOH 27 427 136 HOH HOH A . 
O 6 HOH 28 428 65  HOH HOH A . 
P 6 HOH 1  101 203 HOH HOH B . 
P 6 HOH 2  102 86  HOH HOH B . 
P 6 HOH 3  103 15  HOH HOH B . 
P 6 HOH 4  104 125 HOH HOH B . 
P 6 HOH 5  105 9   HOH HOH B . 
P 6 HOH 6  106 201 HOH HOH B . 
Q 6 HOH 1  401 199 HOH HOH C . 
Q 6 HOH 2  402 122 HOH HOH C . 
Q 6 HOH 3  403 245 HOH HOH C . 
Q 6 HOH 4  404 84  HOH HOH C . 
Q 6 HOH 5  405 212 HOH HOH C . 
Q 6 HOH 6  406 14  HOH HOH C . 
Q 6 HOH 7  407 78  HOH HOH C . 
Q 6 HOH 8  408 123 HOH HOH C . 
Q 6 HOH 9  409 94  HOH HOH C . 
Q 6 HOH 10 410 246 HOH HOH C . 
Q 6 HOH 11 411 121 HOH HOH C . 
Q 6 HOH 12 412 39  HOH HOH C . 
Q 6 HOH 13 413 141 HOH HOH C . 
Q 6 HOH 14 414 8   HOH HOH C . 
Q 6 HOH 15 415 54  HOH HOH C . 
Q 6 HOH 16 416 174 HOH HOH C . 
Q 6 HOH 17 417 31  HOH HOH C . 
Q 6 HOH 18 418 32  HOH HOH C . 
Q 6 HOH 19 419 232 HOH HOH C . 
Q 6 HOH 20 420 155 HOH HOH C . 
Q 6 HOH 21 421 134 HOH HOH C . 
Q 6 HOH 22 422 89  HOH HOH C . 
Q 6 HOH 23 423 244 HOH HOH C . 
Q 6 HOH 24 424 108 HOH HOH C . 
Q 6 HOH 25 425 36  HOH HOH C . 
Q 6 HOH 26 426 105 HOH HOH C . 
Q 6 HOH 27 427 235 HOH HOH C . 
Q 6 HOH 28 428 145 HOH HOH C . 
Q 6 HOH 29 429 200 HOH HOH C . 
Q 6 HOH 30 430 182 HOH HOH C . 
Q 6 HOH 31 431 240 HOH HOH C . 
Q 6 HOH 32 432 239 HOH HOH C . 
Q 6 HOH 33 433 236 HOH HOH C . 
Q 6 HOH 34 434 77  HOH HOH C . 
R 6 HOH 1  101 11  HOH HOH D . 
R 6 HOH 2  102 90  HOH HOH D . 
R 6 HOH 3  103 34  HOH HOH D . 
R 6 HOH 4  104 172 HOH HOH D . 
R 6 HOH 5  105 160 HOH HOH D . 
R 6 HOH 6  106 205 HOH HOH D . 
R 6 HOH 7  107 76  HOH HOH D . 
R 6 HOH 8  108 114 HOH HOH D . 
R 6 HOH 9  109 216 HOH HOH D . 
R 6 HOH 10 110 237 HOH HOH D . 
R 6 HOH 11 111 202 HOH HOH D . 
R 6 HOH 12 112 194 HOH HOH D . 
R 6 HOH 13 113 238 HOH HOH D . 
S 6 HOH 1  401 64  HOH HOH H . 
S 6 HOH 2  402 149 HOH HOH H . 
S 6 HOH 3  403 158 HOH HOH H . 
S 6 HOH 4  404 38  HOH HOH H . 
S 6 HOH 5  405 185 HOH HOH H . 
S 6 HOH 6  406 109 HOH HOH H . 
S 6 HOH 7  407 5   HOH HOH H . 
S 6 HOH 8  408 70  HOH HOH H . 
S 6 HOH 9  409 209 HOH HOH H . 
S 6 HOH 10 410 208 HOH HOH H . 
S 6 HOH 11 411 139 HOH HOH H . 
S 6 HOH 12 412 210 HOH HOH H . 
S 6 HOH 13 413 118 HOH HOH H . 
S 6 HOH 14 414 234 HOH HOH H . 
S 6 HOH 15 415 27  HOH HOH H . 
S 6 HOH 16 416 40  HOH HOH H . 
S 6 HOH 17 417 104 HOH HOH H . 
S 6 HOH 18 418 135 HOH HOH H . 
S 6 HOH 19 419 41  HOH HOH H . 
S 6 HOH 20 420 20  HOH HOH H . 
S 6 HOH 21 421 1   HOH HOH H . 
S 6 HOH 22 422 24  HOH HOH H . 
S 6 HOH 23 423 83  HOH HOH H . 
S 6 HOH 24 424 51  HOH HOH H . 
S 6 HOH 25 425 63  HOH HOH H . 
S 6 HOH 26 426 164 HOH HOH H . 
S 6 HOH 27 427 60  HOH HOH H . 
S 6 HOH 28 428 241 HOH HOH H . 
S 6 HOH 29 429 62  HOH HOH H . 
S 6 HOH 30 430 150 HOH HOH H . 
S 6 HOH 31 431 161 HOH HOH H . 
S 6 HOH 32 432 169 HOH HOH H . 
S 6 HOH 33 433 211 HOH HOH H . 
S 6 HOH 34 434 197 HOH HOH H . 
S 6 HOH 35 435 195 HOH HOH H . 
S 6 HOH 36 436 196 HOH HOH H . 
S 6 HOH 37 437 157 HOH HOH H . 
S 6 HOH 38 438 190 HOH HOH H . 
T 6 HOH 1  101 163 HOH HOH I . 
T 6 HOH 2  102 4   HOH HOH I . 
T 6 HOH 3  103 29  HOH HOH I . 
T 6 HOH 4  104 56  HOH HOH I . 
T 6 HOH 5  105 221 HOH HOH I . 
T 6 HOH 6  106 61  HOH HOH I . 
T 6 HOH 7  107 207 HOH HOH I . 
U 6 HOH 1  401 222 HOH HOH J . 
U 6 HOH 2  402 18  HOH HOH J . 
U 6 HOH 3  403 17  HOH HOH J . 
U 6 HOH 4  404 75  HOH HOH J . 
U 6 HOH 5  405 25  HOH HOH J . 
U 6 HOH 6  406 129 HOH HOH J . 
U 6 HOH 7  407 53  HOH HOH J . 
U 6 HOH 8  408 12  HOH HOH J . 
U 6 HOH 9  409 106 HOH HOH J . 
U 6 HOH 10 410 147 HOH HOH J . 
U 6 HOH 11 411 46  HOH HOH J . 
U 6 HOH 12 412 167 HOH HOH J . 
U 6 HOH 13 413 68  HOH HOH J . 
U 6 HOH 14 414 215 HOH HOH J . 
U 6 HOH 15 415 112 HOH HOH J . 
U 6 HOH 16 416 96  HOH HOH J . 
U 6 HOH 17 417 85  HOH HOH J . 
U 6 HOH 18 418 13  HOH HOH J . 
U 6 HOH 19 419 16  HOH HOH J . 
U 6 HOH 20 420 110 HOH HOH J . 
U 6 HOH 21 421 124 HOH HOH J . 
U 6 HOH 22 422 3   HOH HOH J . 
U 6 HOH 23 423 120 HOH HOH J . 
U 6 HOH 24 424 175 HOH HOH J . 
U 6 HOH 25 425 30  HOH HOH J . 
U 6 HOH 26 426 119 HOH HOH J . 
U 6 HOH 27 427 47  HOH HOH J . 
U 6 HOH 28 428 52  HOH HOH J . 
U 6 HOH 29 429 178 HOH HOH J . 
U 6 HOH 30 430 226 HOH HOH J . 
U 6 HOH 31 431 87  HOH HOH J . 
U 6 HOH 32 432 127 HOH HOH J . 
U 6 HOH 33 433 184 HOH HOH J . 
U 6 HOH 34 434 144 HOH HOH J . 
U 6 HOH 35 435 35  HOH HOH J . 
U 6 HOH 36 436 186 HOH HOH J . 
U 6 HOH 37 437 198 HOH HOH J . 
U 6 HOH 38 438 191 HOH HOH J . 
V 6 HOH 1  101 97  HOH HOH K . 
V 6 HOH 2  102 170 HOH HOH K . 
V 6 HOH 3  103 220 HOH HOH K . 
V 6 HOH 4  104 189 HOH HOH K . 
V 6 HOH 5  105 187 HOH HOH K . 
V 6 HOH 6  106 188 HOH HOH K . 
# 
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 ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.01 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.41 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  89.95 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CH0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.130 
_cell.length_a_esd                 ? 
_cell.length_b                     108.020 
_cell.length_b_esd                 ? 
_cell.length_c                     58.590 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9CH0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CH0 
_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             2.17 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.33 
_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              5.5 
_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    '240 mM sodium malonate pH 5.5 with 14% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-16 
_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   1.033167 
_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                        'APS BEAMLINE 23-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033167 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CH0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               19.84 
_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                                     56305 
_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                           86.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.29 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.29 
_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                                0.134 
_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                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.2 
_reflns_shell.d_res_low                                     2.3 
_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                             6602 
_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                               0.476 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.935 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -7.77 
_refine.aniso_B[1][2]                            10.72 
_refine.aniso_B[1][3]                            0.63 
_refine.aniso_B[2][2]                            7.80 
_refine.aniso_B[2][3]                            -4.88 
_refine.aniso_B[3][3]                            -0.04 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.793 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.902 
_refine.correlation_coeff_Fo_to_Fc_free          0.901 
_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                                 9CH0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             19.84 
_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                     53537 
_refine.ls_number_reflns_R_free                  2767 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.82 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.29361 
_refine.ls_R_factor_R_free                       0.32685 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.29180 
_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                       0.128 
_refine.pdbx_overall_ESU_R_Free                  0.071 
_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                             8.389 
_refine.overall_SU_ML                            0.225 
_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                       2.20 
_refine_hist.d_res_low                        19.84 
_refine_hist.number_atoms_solvent             170 
_refine_hist.number_atoms_total               10132 
_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        9960 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_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' ? 0.002  0.012  10192 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.000  0.016  9617  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.849  1.810  13861 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.271  1.741  22143 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.812  5.000  1251  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.811  5.000  40    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.839 10.000 1668  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.038  0.200  1557  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  11920 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.000  0.020  2268  ? 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' ? 2.464  2.598  5053  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.462  2.598  5053  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.716  4.651  6290  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.716  4.652  6291  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.558  2.885  5139  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.558  2.886  5140  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.998  5.194  7572  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.162  28.05  11553 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.158  28.06  11543 ? 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                       2.2 
_refine_ls_shell.d_res_low                        2.255 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             178 
_refine_ls_shell.number_reflns_R_work             3473 
_refine_ls_shell.percent_reflns_obs               76.40 
_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                  0.357 
_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                  0.454 
# 
_struct.entry_id                     9CH0 
_struct.title                        
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (bound to SAH)' 
_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        9CH0 
_struct_keywords.text            'Alpha-N-methyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 1 ? 
F N N 3 ? 
G N N 1 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 4 ? 
O N N 6 ? 
P N N 6 ? 
Q N N 6 ? 
R N N 6 ? 
S N N 6 ? 
T N N 6 ? 
U N N 6 ? 
V N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q8EGW3_SHEON Q8EGW3 ? 1 
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDLG
;
1 
2 UNP Q8EGW2_SHEON Q8EGW2 ? 2 MSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYLVISHGNGD 1 
3 UNP Q8EGW2_SHEON Q8EGW2 ? 3 MSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYLVISHGNGD 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 9CH0 A 1 ? 263 ? Q8EGW3 1 ? 263 ? 1 263 
2 2 9CH0 B 8 ? 78  ? Q8EGW2 1 ? 71  ? 1 71  
3 1 9CH0 C 1 ? 263 ? Q8EGW3 1 ? 263 ? 1 263 
4 2 9CH0 D 8 ? 78  ? Q8EGW2 1 ? 71  ? 1 71  
5 1 9CH0 H 1 ? 263 ? Q8EGW3 1 ? 263 ? 1 263 
6 3 9CH0 I 8 ? 78  ? Q8EGW2 1 ? 71  ? 1 71  
7 1 9CH0 J 1 ? 263 ? Q8EGW3 1 ? 263 ? 1 263 
8 3 9CH0 K 8 ? 78  ? Q8EGW2 1 ? 71  ? 1 71  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
2 9CH0 MET B 1  ? UNP Q8EGW2 ?   ?  'initiating methionine' -6 1  
2 9CH0 HIS B 2  ? UNP Q8EGW2 ?   ?  'expression tag'        -5 2  
2 9CH0 HIS B 3  ? UNP Q8EGW2 ?   ?  'expression tag'        -4 3  
2 9CH0 HIS B 4  ? UNP Q8EGW2 ?   ?  'expression tag'        -3 4  
2 9CH0 HIS B 5  ? UNP Q8EGW2 ?   ?  'expression tag'        -2 5  
2 9CH0 HIS B 6  ? UNP Q8EGW2 ?   ?  'expression tag'        -1 6  
2 9CH0 HIS B 7  ? UNP Q8EGW2 ?   ?  'expression tag'        0  7  
2 9CH0 TRP B 72 ? UNP Q8EGW2 ILE 65 'engineered mutation'   65 8  
4 9CH0 MET D 1  ? UNP Q8EGW2 ?   ?  'initiating methionine' -6 9  
4 9CH0 HIS D 2  ? UNP Q8EGW2 ?   ?  'expression tag'        -5 10 
4 9CH0 HIS D 3  ? UNP Q8EGW2 ?   ?  'expression tag'        -4 11 
4 9CH0 HIS D 4  ? UNP Q8EGW2 ?   ?  'expression tag'        -3 12 
4 9CH0 HIS D 5  ? UNP Q8EGW2 ?   ?  'expression tag'        -2 13 
4 9CH0 HIS D 6  ? UNP Q8EGW2 ?   ?  'expression tag'        -1 14 
4 9CH0 HIS D 7  ? UNP Q8EGW2 ?   ?  'expression tag'        0  15 
4 9CH0 TRP D 72 ? UNP Q8EGW2 ILE 65 'engineered mutation'   65 16 
6 9CH0 MET I 1  ? UNP Q8EGW2 ?   ?  'initiating methionine' -6 17 
6 9CH0 HIS I 2  ? UNP Q8EGW2 ?   ?  'expression tag'        -5 18 
6 9CH0 HIS I 3  ? UNP Q8EGW2 ?   ?  'expression tag'        -4 19 
6 9CH0 HIS I 4  ? UNP Q8EGW2 ?   ?  'expression tag'        -3 20 
6 9CH0 HIS I 5  ? UNP Q8EGW2 ?   ?  'expression tag'        -2 21 
6 9CH0 HIS I 6  ? UNP Q8EGW2 ?   ?  'expression tag'        -1 22 
6 9CH0 HIS I 7  ? UNP Q8EGW2 ?   ?  'expression tag'        0  23 
6 9CH0 TRP I 72 ? UNP Q8EGW2 ILE 65 'engineered mutation'   65 24 
8 9CH0 MET K 1  ? UNP Q8EGW2 ?   ?  'initiating methionine' -6 25 
8 9CH0 HIS K 2  ? UNP Q8EGW2 ?   ?  'expression tag'        -5 26 
8 9CH0 HIS K 3  ? UNP Q8EGW2 ?   ?  'expression tag'        -4 27 
8 9CH0 HIS K 4  ? UNP Q8EGW2 ?   ?  'expression tag'        -3 28 
8 9CH0 HIS K 5  ? UNP Q8EGW2 ?   ?  'expression tag'        -2 29 
8 9CH0 HIS K 6  ? UNP Q8EGW2 ?   ?  'expression tag'        -1 30 
8 9CH0 HIS K 7  ? UNP Q8EGW2 ?   ?  'expression tag'        0  31 
8 9CH0 TRP K 72 ? UNP Q8EGW2 ILE 65 'engineered mutation'   65 32 
# 
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_and_software_defined_assembly PISA tetrameric 4 
2 author_and_software_defined_assembly PISA tetrameric 4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 11160 ? 
1 MORE         -108  ? 
1 'SSA (A^2)'  23870 ? 
2 'ABSA (A^2)' 11520 ? 
2 MORE         -111  ? 
2 'SSA (A^2)'  23800 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,I,J,K,O,P,Q,R 
2 1 E,F,G,H,L,M,N,S,T,U,V 
# 
_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 SER A 18  ? ALA A 28  ? SER A 18  ALA A 28  1 ? 11 
HELX_P HELX_P2  AA2 ASP A 37  ? ASN A 48  ? ASP A 37  ASN A 48  1 ? 12 
HELX_P HELX_P3  AA3 GLN A 55  ? TYR A 58  ? GLN A 55  TYR A 58  5 ? 4  
HELX_P HELX_P4  AA4 ASN A 66  ? GLY A 85  ? ASN A 66  GLY A 85  1 ? 20 
HELX_P HELX_P5  AA5 ALA A 100 ? GLU A 113 ? ALA A 100 GLU A 113 1 ? 14 
HELX_P HELX_P6  AA6 SER A 124 ? LEU A 133 ? SER A 124 LEU A 133 1 ? 10 
HELX_P HELX_P7  AA7 ALA A 147 ? PHE A 153 ? ALA A 147 PHE A 153 1 ? 7  
HELX_P HELX_P8  AA8 ILE A 168 ? ALA A 171 ? ILE A 168 ALA A 171 5 ? 4  
HELX_P HELX_P9  AA9 SER A 182 ? ASN A 194 ? SER A 182 ASN A 194 1 ? 13 
HELX_P HELX_P10 AB1 ALA A 224 ? ALA A 229 ? ALA A 224 ALA A 229 5 ? 6  
HELX_P HELX_P11 AB2 ASN A 248 ? LEU A 255 ? ASN A 248 LEU A 255 1 ? 8  
HELX_P HELX_P12 AB3 GLY A 258 ? LEU A 262 ? GLY A 258 LEU A 262 5 ? 5  
HELX_P HELX_P13 AB4 LEU B 11  ? ASP B 21  ? LEU B 4   ASP B 14  1 ? 11 
HELX_P HELX_P14 AB5 ASP B 21  ? ASN B 31  ? ASP B 14  ASN B 24  1 ? 11 
HELX_P HELX_P15 AB6 ASN B 31  ? HIS B 39  ? ASN B 24  HIS B 32  1 ? 9  
HELX_P HELX_P16 AB7 THR B 42  ? GLY B 52  ? THR B 35  GLY B 45  1 ? 11 
HELX_P HELX_P17 AB8 ASP B 53  ? LEU B 60  ? ASP B 46  LEU B 53  1 ? 8  
HELX_P HELX_P18 AB9 SER C 18  ? ALA C 28  ? SER C 18  ALA C 28  1 ? 11 
HELX_P HELX_P19 AC1 ASP C 37  ? ASN C 48  ? ASP C 37  ASN C 48  1 ? 12 
HELX_P HELX_P20 AC2 GLN C 55  ? TYR C 58  ? GLN C 55  TYR C 58  5 ? 4  
HELX_P HELX_P21 AC3 ASN C 66  ? GLY C 85  ? ASN C 66  GLY C 85  1 ? 20 
HELX_P HELX_P22 AC4 ALA C 100 ? GLU C 113 ? ALA C 100 GLU C 113 1 ? 14 
HELX_P HELX_P23 AC5 SER C 124 ? GLY C 134 ? SER C 124 GLY C 134 1 ? 11 
HELX_P HELX_P24 AC6 ALA C 147 ? PHE C 153 ? ALA C 147 PHE C 153 1 ? 7  
HELX_P HELX_P25 AC7 GLN C 167 ? ALA C 171 ? GLN C 167 ALA C 171 5 ? 5  
HELX_P HELX_P26 AC8 SER C 182 ? ASN C 194 ? SER C 182 ASN C 194 1 ? 13 
HELX_P HELX_P27 AC9 ALA C 224 ? ALA C 229 ? ALA C 224 ALA C 229 5 ? 6  
HELX_P HELX_P28 AD1 ASN C 248 ? LEU C 255 ? ASN C 248 LEU C 255 1 ? 8  
HELX_P HELX_P29 AD2 GLY C 258 ? LEU C 262 ? GLY C 258 LEU C 262 5 ? 5  
HELX_P HELX_P30 AD3 SER D 12  ? ASP D 21  ? SER D 5   ASP D 14  1 ? 10 
HELX_P HELX_P31 AD4 ASP D 21  ? ASN D 31  ? ASP D 14  ASN D 24  1 ? 11 
HELX_P HELX_P32 AD5 ASN D 31  ? HIS D 39  ? ASN D 24  HIS D 32  1 ? 9  
HELX_P HELX_P33 AD6 THR D 42  ? THR D 51  ? THR D 35  THR D 44  1 ? 10 
HELX_P HELX_P34 AD7 ASP D 53  ? THR D 59  ? ASP D 46  THR D 52  1 ? 7  
HELX_P HELX_P35 AD8 SER E 18  ? ALA E 28  ? SER H 18  ALA H 28  1 ? 11 
HELX_P HELX_P36 AD9 GLY E 38  ? ASN E 48  ? GLY H 38  ASN H 48  1 ? 11 
HELX_P HELX_P37 AE1 GLN E 55  ? TYR E 58  ? GLN H 55  TYR H 58  5 ? 4  
HELX_P HELX_P38 AE2 ASN E 66  ? GLY E 85  ? ASN H 66  GLY H 85  1 ? 20 
HELX_P HELX_P39 AE3 ALA E 100 ? GLU E 113 ? ALA H 100 GLU H 113 1 ? 14 
HELX_P HELX_P40 AE4 SER E 124 ? LEU E 133 ? SER H 124 LEU H 133 1 ? 10 
HELX_P HELX_P41 AE5 ALA E 147 ? PHE E 153 ? ALA H 147 PHE H 153 1 ? 7  
HELX_P HELX_P42 AE6 GLN E 167 ? ALA E 171 ? GLN H 167 ALA H 171 5 ? 5  
HELX_P HELX_P43 AE7 SER E 182 ? ASN E 194 ? SER H 182 ASN H 194 1 ? 13 
HELX_P HELX_P44 AE8 ALA E 224 ? ALA E 229 ? ALA H 224 ALA H 229 5 ? 6  
HELX_P HELX_P45 AE9 ASN E 248 ? LEU E 255 ? ASN H 248 LEU H 255 1 ? 8  
HELX_P HELX_P46 AF1 GLY E 258 ? LEU E 262 ? GLY H 258 LEU H 262 5 ? 5  
HELX_P HELX_P47 AF2 LEU F 11  ? ASP F 21  ? LEU I 4   ASP I 14  1 ? 11 
HELX_P HELX_P48 AF3 ASP F 21  ? ASN F 31  ? ASP I 14  ASN I 24  1 ? 11 
HELX_P HELX_P49 AF4 ASN F 31  ? HIS F 39  ? ASN I 24  HIS I 32  1 ? 9  
HELX_P HELX_P50 AF5 THR F 42  ? GLY F 52  ? THR I 35  GLY I 45  1 ? 11 
HELX_P HELX_P51 AF6 ASP F 53  ? LEU F 60  ? ASP I 46  LEU I 53  1 ? 8  
HELX_P HELX_P52 AF7 SER G 18  ? HIS G 27  ? SER J 18  HIS J 27  1 ? 10 
HELX_P HELX_P53 AF8 ASP G 37  ? ASN G 48  ? ASP J 37  ASN J 48  1 ? 12 
HELX_P HELX_P54 AF9 GLN G 55  ? TYR G 58  ? GLN J 55  TYR J 58  5 ? 4  
HELX_P HELX_P55 AG1 ASN G 66  ? GLY G 85  ? ASN J 66  GLY J 85  1 ? 20 
HELX_P HELX_P56 AG2 ALA G 100 ? GLU G 113 ? ALA J 100 GLU J 113 1 ? 14 
HELX_P HELX_P57 AG3 SER G 124 ? GLY G 134 ? SER J 124 GLY J 134 1 ? 11 
HELX_P HELX_P58 AG4 ALA G 147 ? PHE G 153 ? ALA J 147 PHE J 153 1 ? 7  
HELX_P HELX_P59 AG5 GLN G 167 ? ALA G 171 ? GLN J 167 ALA J 171 5 ? 5  
HELX_P HELX_P60 AG6 SER G 182 ? ASN G 194 ? SER J 182 ASN J 194 1 ? 13 
HELX_P HELX_P61 AG7 ALA G 224 ? ALA G 229 ? ALA J 224 ALA J 229 5 ? 6  
HELX_P HELX_P62 AG8 ASN G 248 ? LEU G 255 ? ASN J 248 LEU J 255 1 ? 8  
HELX_P HELX_P63 AG9 GLY G 258 ? LEU G 262 ? GLY J 258 LEU J 262 5 ? 5  
HELX_P HELX_P64 AH1 SER H 12  ? ASP H 21  ? SER K 5   ASP K 14  1 ? 10 
HELX_P HELX_P65 AH2 ASP H 21  ? ASN H 31  ? ASP K 14  ASN K 24  1 ? 11 
HELX_P HELX_P66 AH3 ASN H 31  ? HIS H 39  ? ASN K 24  HIS K 32  1 ? 9  
HELX_P HELX_P67 AH4 THR H 42  ? THR H 51  ? THR K 35  THR K 44  1 ? 10 
HELX_P HELX_P68 AH5 ASP H 53  ? THR H 59  ? ASP K 46  THR K 52  1 ? 7  
# 
_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 ? B TYR 69  C   ? ? ? 1_555 B MLE 70  N   ? ? B TYR 62  B MLE 63  1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale2 covale both ? B MLE 70  C   ? ? ? 1_555 B VAL 71  N   ? ? B MLE 63  B VAL 64  1_555 ? ? ? ? ? ? ? 1.348 ? ? 
metalc1 metalc ?    ? A GLU 126 OE1 ? ? ? 1_555 J ZN  .   ZN  ? ? A GLU 126 A ZN  302 1_555 ? ? ? ? ? ? ? 2.584 ? ? 
metalc2 metalc ?    ? A GLU 126 OE2 ? ? ? 1_555 J ZN  .   ZN  ? ? A GLU 126 A ZN  302 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc3 metalc ?    ? J ZN  .   ZN  ? ? ? 1_555 C GLU 126 OE2 ? ? A ZN  302 C GLU 126 1_555 ? ? ? ? ? ? ? 2.213 ? ? 
metalc4 metalc ?    ? E GLU 126 OE2 ? ? ? 1_555 M ZN  .   ZN  ? ? H GLU 126 H ZN  302 1_555 ? ? ? ? ? ? ? 1.999 ? ? 
metalc5 metalc ?    ? E HIS 142 ND1 ? ? ? 1_555 M ZN  .   ZN  ? ? H HIS 142 H ZN  302 1_555 ? ? ? ? ? ? ? 2.644 ? ? 
metalc6 metalc ?    ? M ZN  .   ZN  ? ? ? 1_555 G GLU 126 OE2 ? ? H ZN  302 J GLU 126 1_555 ? ? ? ? ? ? ? 2.239 ? ? 
metalc7 metalc ?    ? M ZN  .   ZN  ? ? ? 1_555 G HIS 142 ND1 ? ? H ZN  302 J HIS 142 1_555 ? ? ? ? ? ? ? 2.638 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OE1 ? A GLU 126 ? A GLU 126 ? 1_555 ZN ? J ZN . ? A ZN 302 ? 1_555 OE2 ? A GLU 126 ? A GLU 126 ? 1_555 53.0  ? 
2 OE1 ? A GLU 126 ? A GLU 126 ? 1_555 ZN ? J ZN . ? A ZN 302 ? 1_555 OE2 ? C GLU 126 ? C GLU 126 ? 1_555 97.0  ? 
3 OE2 ? A GLU 126 ? A GLU 126 ? 1_555 ZN ? J ZN . ? A ZN 302 ? 1_555 OE2 ? C GLU 126 ? C GLU 126 ? 1_555 82.3  ? 
4 OE2 ? E GLU 126 ? H GLU 126 ? 1_555 ZN ? M ZN . ? H ZN 302 ? 1_555 ND1 ? E HIS 142 ? H HIS 142 ? 1_555 83.8  ? 
5 OE2 ? E GLU 126 ? H GLU 126 ? 1_555 ZN ? M ZN . ? H ZN 302 ? 1_555 OE2 ? G GLU 126 ? J GLU 126 ? 1_555 80.3  ? 
6 ND1 ? E HIS 142 ? H HIS 142 ? 1_555 ZN ? M ZN . ? H ZN 302 ? 1_555 OE2 ? G GLU 126 ? J GLU 126 ? 1_555 156.4 ? 
7 OE2 ? E GLU 126 ? H GLU 126 ? 1_555 ZN ? M ZN . ? H ZN 302 ? 1_555 ND1 ? G HIS 142 ? J HIS 142 ? 1_555 156.0 ? 
8 ND1 ? E HIS 142 ? H HIS 142 ? 1_555 ZN ? M ZN . ? H ZN 302 ? 1_555 ND1 ? G HIS 142 ? J HIS 142 ? 1_555 89.4  ? 
9 OE2 ? G GLU 126 ? J GLU 126 ? 1_555 ZN ? M ZN . ? H ZN 302 ? 1_555 ND1 ? G HIS 142 ? J HIS 142 ? 1_555 112.0 ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      MLE 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       70 
_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                       MLE 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        63 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_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                LEU 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        MLE 
_pdbx_modification_feature.type                               Methylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5  ? 
AA2 ? 10 ? 
AA3 ? 5  ? 
AA4 ? 5  ? 
AA5 ? 10 ? 
AA6 ? 5  ? 
# 
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  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? parallel      
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? parallel      
AA3 2 3  ? parallel      
AA3 3 4  ? parallel      
AA3 4 5  ? parallel      
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA5 1 2  ? anti-parallel 
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? parallel      
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? parallel      
AA6 2 3  ? parallel      
AA6 3 4  ? parallel      
AA6 4 5  ? 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 51  ? ASN A 53  ? VAL A 51  ASN A 53  
AA1 2  ILE A 30  ? LEU A 34  ? ILE A 30  LEU A 34  
AA1 3  LYS A 87  ? LEU A 92  ? LYS A 87  LEU A 92  
AA1 4  SER A 3   ? GLY A 8   ? SER A 3   GLY A 8   
AA1 5  SER A 116 ? MET A 119 ? SER A 116 MET A 119 
AA2 1  ARG A 217 ? PRO A 222 ? ARG A 217 PRO A 222 
AA2 2  GLU A 202 ? GLU A 207 ? GLU A 202 GLU A 207 
AA2 3  THR A 236 ? ILE A 239 ? THR A 236 ILE A 239 
AA2 4  HIS A 162 ? TRP A 166 ? HIS A 162 TRP A 166 
AA2 5  HIS A 142 ? GLU A 146 ? HIS A 142 GLU A 146 
AA2 6  HIS C 142 ? GLU C 146 ? HIS C 142 GLU C 146 
AA2 7  HIS C 162 ? TRP C 166 ? HIS C 162 TRP C 166 
AA2 8  THR C 236 ? ILE C 239 ? THR C 236 ILE C 239 
AA2 9  GLU C 202 ? GLU C 207 ? GLU C 202 GLU C 207 
AA2 10 ARG C 217 ? PRO C 222 ? ARG C 217 PRO C 222 
AA3 1  VAL C 51  ? ASN C 53  ? VAL C 51  ASN C 53  
AA3 2  ILE C 30  ? LEU C 34  ? ILE C 30  LEU C 34  
AA3 3  LYS C 87  ? LEU C 92  ? LYS C 87  LEU C 92  
AA3 4  SER C 3   ? GLY C 8   ? SER C 3   GLY C 8   
AA3 5  SER C 116 ? MET C 119 ? SER C 116 MET C 119 
AA4 1  VAL E 51  ? ASN E 53  ? VAL H 51  ASN H 53  
AA4 2  ILE E 30  ? LEU E 34  ? ILE H 30  LEU H 34  
AA4 3  LYS E 87  ? LEU E 92  ? LYS H 87  LEU H 92  
AA4 4  SER E 3   ? GLY E 8   ? SER H 3   GLY H 8   
AA4 5  SER E 116 ? MET E 119 ? SER H 116 MET H 119 
AA5 1  ARG E 217 ? PRO E 222 ? ARG H 217 PRO H 222 
AA5 2  GLU E 202 ? GLU E 207 ? GLU H 202 GLU H 207 
AA5 3  THR E 236 ? ILE E 239 ? THR H 236 ILE H 239 
AA5 4  HIS E 162 ? TRP E 166 ? HIS H 162 TRP H 166 
AA5 5  HIS E 142 ? GLU E 146 ? HIS H 142 GLU H 146 
AA5 6  HIS G 142 ? GLU G 146 ? HIS J 142 GLU J 146 
AA5 7  HIS G 162 ? TRP G 166 ? HIS J 162 TRP J 166 
AA5 8  THR G 236 ? ILE G 239 ? THR J 236 ILE J 239 
AA5 9  GLU G 202 ? GLU G 207 ? GLU J 202 GLU J 207 
AA5 10 ARG G 217 ? PRO G 222 ? ARG J 217 PRO J 222 
AA6 1  VAL G 51  ? ASN G 53  ? VAL J 51  ASN J 53  
AA6 2  ILE G 30  ? LEU G 34  ? ILE J 30  LEU J 34  
AA6 3  LYS G 87  ? LEU G 92  ? LYS J 87  LEU J 92  
AA6 4  SER G 3   ? GLY G 8   ? SER J 3   GLY J 8   
AA6 5  SER G 116 ? MET G 119 ? SER J 116 MET J 119 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O ILE A 52  ? O ILE A 52  N VAL A 31  ? N VAL A 31  
AA1 2 3  N PHE A 32  ? N PHE A 32  O VAL A 89  ? O VAL A 89  
AA1 3 4  O CYS A 90  ? O CYS A 90  N VAL A 7   ? N VAL A 7   
AA1 4 5  N LEU A 4   ? N LEU A 4   O SER A 116 ? O SER A 116 
AA2 1 2  O LEU A 221 ? O LEU A 221 N VAL A 203 ? N VAL A 203 
AA2 2 3  N VAL A 204 ? N VAL A 204 O LEU A 238 ? O LEU A 238 
AA2 3 4  O ILE A 239 ? O ILE A 239 N LEU A 163 ? N LEU A 163 
AA2 4 5  O LEU A 164 ? O LEU A 164 N GLN A 143 ? N GLN A 143 
AA2 5 6  N SER A 144 ? N SER A 144 O HIS C 142 ? O HIS C 142 
AA2 6 7  N GLN C 143 ? N GLN C 143 O HIS C 162 ? O HIS C 162 
AA2 7 8  N LEU C 163 ? N LEU C 163 O ILE C 239 ? O ILE C 239 
AA2 8 9  O LEU C 238 ? O LEU C 238 N VAL C 204 ? N VAL C 204 
AA2 9 10 N VAL C 203 ? N VAL C 203 O LEU C 221 ? O LEU C 221 
AA3 1 2  O ILE C 52  ? O ILE C 52  N VAL C 31  ? N VAL C 31  
AA3 2 3  N PHE C 32  ? N PHE C 32  O ALA C 91  ? O ALA C 91  
AA3 3 4  O CYS C 90  ? O CYS C 90  N VAL C 7   ? N VAL C 7   
AA3 4 5  N LEU C 4   ? N LEU C 4   O SER C 116 ? O SER C 116 
AA4 1 2  O ILE E 52  ? O ILE H 52  N VAL E 31  ? N VAL H 31  
AA4 2 3  N PHE E 32  ? N PHE H 32  O ALA E 91  ? O ALA H 91  
AA4 3 4  O CYS E 90  ? O CYS H 90  N VAL E 7   ? N VAL H 7   
AA4 4 5  N LEU E 4   ? N LEU H 4   O SER E 116 ? O SER H 116 
AA5 1 2  O LEU E 221 ? O LEU H 221 N VAL E 203 ? N VAL H 203 
AA5 2 3  N VAL E 204 ? N VAL H 204 O LEU E 238 ? O LEU H 238 
AA5 3 4  O ILE E 239 ? O ILE H 239 N LEU E 163 ? N LEU H 163 
AA5 4 5  O LEU E 164 ? O LEU H 164 N GLN E 143 ? N GLN H 143 
AA5 5 6  N SER E 144 ? N SER H 144 O HIS G 142 ? O HIS J 142 
AA5 6 7  N PHE G 145 ? N PHE J 145 O TRP G 166 ? O TRP J 166 
AA5 7 8  N LEU G 163 ? N LEU J 163 O ILE G 239 ? O ILE J 239 
AA5 8 9  O LEU G 238 ? O LEU J 238 N VAL G 204 ? N VAL J 204 
AA5 9 10 N VAL G 203 ? N VAL J 203 O LEU G 221 ? O LEU J 221 
AA6 1 2  O ILE G 52  ? O ILE J 52  N VAL G 31  ? N VAL J 31  
AA6 2 3  N PHE G 32  ? N PHE J 32  O ALA G 91  ? O ALA J 91  
AA6 3 4  O CYS G 90  ? O CYS J 90  N VAL G 7   ? N VAL J 7   
AA6 4 5  N LEU G 4   ? N LEU J 4   O SER G 116 ? O SER J 116 
# 
_pdbx_entry_details.entry_id                   9CH0 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   H HOH 404 ? ? O  H HOH 411 ? ? 2.05 
2 1 O   B GLN 13  ? ? O  B HOH 101 ? ? 2.12 
3 1 N   J ASN 61  ? ? O  J HOH 401 ? ? 2.12 
4 1 O   H ASP 261 ? ? O  H HOH 401 ? ? 2.14 
5 1 O   J HOH 413 ? ? O  J HOH 414 ? ? 2.14 
6 1 OE2 C GLU 207 ? ? OG C SER 235 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 CD2 A PHE 179 ? ? 1_555 CZ  C PHE 179 ? ? 1_554 1.75 
2 1 OE1 A GLN 178 ? ? 1_555 OE1 C GLN 178 ? ? 1_554 2.07 
# 
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 ALA A 14  ? ? 79.89   -38.91  
2  1 THR A 181 ? ? -107.57 -168.46 
3  1 PRO A 241 ? ? -38.97  151.05  
4  1 ASN B 24  ? ? -154.15 77.73   
5  1 TRP B 65  ? ? -147.25 -157.15 
6  1 ALA C 14  ? ? 78.62   -45.84  
7  1 LEU C 34  ? ? -159.09 76.95   
8  1 ASN C 61  ? ? 80.15   58.61   
9  1 ALA C 171 ? ? -51.55  108.81  
10 1 LEU C 176 ? ? 72.86   46.21   
11 1 ASN C 248 ? ? -102.11 73.35   
12 1 ALA H 14  ? ? 83.43   -36.58  
13 1 THR H 181 ? ? -109.99 -163.36 
14 1 ALA J 14  ? ? 77.83   -46.67  
15 1 LEU J 34  ? ? -160.51 87.88   
16 1 ASN J 61  ? ? 74.20   61.00   
17 1 PRO J 240 ? ? -59.24  170.14  
18 1 ASN J 248 ? ? -107.77 71.91   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     67 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.151 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    B 
_pdbx_struct_mod_residue.label_comp_id    MLE 
_pdbx_struct_mod_residue.label_seq_id     70 
_pdbx_struct_mod_residue.auth_asym_id     B 
_pdbx_struct_mod_residue.auth_comp_id     MLE 
_pdbx_struct_mod_residue.auth_seq_id      63 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   LEU 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 426 ? 5.91 . 
2 1 O ? A HOH 427 ? 5.92 . 
3 1 O ? A HOH 428 ? 7.11 . 
4 1 O ? J HOH 437 ? 6.00 . 
5 1 O ? J HOH 438 ? 6.14 . 
# 
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 1  ? A MET 1  
2   1 Y 1 B MET -6 ? B MET 1  
3   1 Y 1 B HIS -5 ? B HIS 2  
4   1 Y 1 B HIS -4 ? B HIS 3  
5   1 Y 1 B HIS -3 ? B HIS 4  
6   1 Y 1 B HIS -2 ? B HIS 5  
7   1 Y 1 B HIS -1 ? B HIS 6  
8   1 Y 1 B HIS 0  ? B HIS 7  
9   1 Y 1 B MET 1  ? B MET 8  
10  1 Y 1 B SER 2  ? B SER 9  
11  1 Y 1 B SER 54 ? B SER 61 
12  1 Y 1 B GLY 55 ? B GLY 62 
13  1 Y 1 B ASP 56 ? B ASP 63 
14  1 Y 1 B SER 57 ? B SER 64 
15  1 Y 1 B SER 58 ? B SER 65 
16  1 Y 1 B TYR 59 ? B TYR 66 
17  1 Y 1 B GLN 60 ? B GLN 67 
18  1 Y 1 B GLY 68 ? B GLY 75 
19  1 Y 1 B ASN 69 ? B ASN 76 
20  1 Y 1 B GLY 70 ? B GLY 77 
21  1 Y 1 B ASP 71 ? B ASP 78 
22  1 Y 1 C MET 1  ? C MET 1  
23  1 Y 1 D MET -6 ? D MET 1  
24  1 Y 1 D HIS -5 ? D HIS 2  
25  1 Y 1 D HIS -4 ? D HIS 3  
26  1 Y 1 D HIS -3 ? D HIS 4  
27  1 Y 1 D HIS -2 ? D HIS 5  
28  1 Y 1 D HIS -1 ? D HIS 6  
29  1 Y 1 D HIS 0  ? D HIS 7  
30  1 Y 1 D MET 1  ? D MET 8  
31  1 Y 1 D SER 2  ? D SER 9  
32  1 Y 1 D GLY 3  ? D GLY 10 
33  1 Y 1 D LEU 53 ? D LEU 60 
34  1 Y 1 D SER 54 ? D SER 61 
35  1 Y 1 D GLY 55 ? D GLY 62 
36  1 Y 1 D ASP 56 ? D ASP 63 
37  1 Y 1 D SER 57 ? D SER 64 
38  1 Y 1 D SER 58 ? D SER 65 
39  1 Y 1 D TYR 59 ? D TYR 66 
40  1 Y 1 D GLN 60 ? D GLN 67 
41  1 Y 1 D SER 61 ? D SER 68 
42  1 Y 1 D TYR 62 ? D TYR 69 
43  1 Y 1 D MLE 63 ? D MLE 70 
44  1 Y 1 D VAL 64 ? D VAL 71 
45  1 Y 1 D TRP 65 ? D TRP 72 
46  1 Y 1 D SER 66 ? D SER 73 
47  1 Y 1 D HIS 67 ? D HIS 74 
48  1 Y 1 D GLY 68 ? D GLY 75 
49  1 Y 1 D ASN 69 ? D ASN 76 
50  1 Y 1 D GLY 70 ? D GLY 77 
51  1 Y 1 D ASP 71 ? D ASP 78 
52  1 Y 1 H MET 1  ? E MET 1  
53  1 Y 1 I MET -6 ? F MET 1  
54  1 Y 1 I HIS -5 ? F HIS 2  
55  1 Y 1 I HIS -4 ? F HIS 3  
56  1 Y 1 I HIS -3 ? F HIS 4  
57  1 Y 1 I HIS -2 ? F HIS 5  
58  1 Y 1 I HIS -1 ? F HIS 6  
59  1 Y 1 I HIS 0  ? F HIS 7  
60  1 Y 1 I MET 1  ? F MET 8  
61  1 Y 1 I SER 2  ? F SER 9  
62  1 Y 1 I SER 54 ? F SER 61 
63  1 Y 1 I GLY 55 ? F GLY 62 
64  1 Y 1 I ASP 56 ? F ASP 63 
65  1 Y 1 I SER 57 ? F SER 64 
66  1 Y 1 I SER 58 ? F SER 65 
67  1 Y 1 I TYR 59 ? F TYR 66 
68  1 Y 1 I GLN 60 ? F GLN 67 
69  1 Y 1 I SER 61 ? F SER 68 
70  1 Y 1 I TYR 62 ? F TYR 69 
71  1 Y 1 I HIS 67 ? F HIS 74 
72  1 Y 1 I GLY 68 ? F GLY 75 
73  1 Y 1 I ASN 69 ? F ASN 76 
74  1 Y 1 I GLY 70 ? F GLY 77 
75  1 Y 1 I ASP 71 ? F ASP 78 
76  1 Y 1 J MET 1  ? G MET 1  
77  1 Y 1 K MET -6 ? H MET 1  
78  1 Y 1 K HIS -5 ? H HIS 2  
79  1 Y 1 K HIS -4 ? H HIS 3  
80  1 Y 1 K HIS -3 ? H HIS 4  
81  1 Y 1 K HIS -2 ? H HIS 5  
82  1 Y 1 K HIS -1 ? H HIS 6  
83  1 Y 1 K HIS 0  ? H HIS 7  
84  1 Y 1 K MET 1  ? H MET 8  
85  1 Y 1 K SER 2  ? H SER 9  
86  1 Y 1 K GLY 3  ? H GLY 10 
87  1 Y 1 K LEU 53 ? H LEU 60 
88  1 Y 1 K SER 54 ? H SER 61 
89  1 Y 1 K GLY 55 ? H GLY 62 
90  1 Y 1 K ASP 56 ? H ASP 63 
91  1 Y 1 K SER 57 ? H SER 64 
92  1 Y 1 K SER 58 ? H SER 65 
93  1 Y 1 K TYR 59 ? H TYR 66 
94  1 Y 1 K GLN 60 ? H GLN 67 
95  1 Y 1 K TRP 65 ? H TRP 72 
96  1 Y 1 K SER 66 ? H SER 73 
97  1 Y 1 K HIS 67 ? H HIS 74 
98  1 Y 1 K GLY 68 ? H GLY 75 
99  1 Y 1 K ASN 69 ? H ASN 76 
100 1 Y 1 K GLY 70 ? H GLY 77 
101 1 Y 1 K ASP 71 ? H ASP 78 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
HIS N      N  N N 137 
HIS CA     C  N S 138 
HIS C      C  N N 139 
HIS O      O  N N 140 
HIS CB     C  N N 141 
HIS CG     C  Y N 142 
HIS ND1    N  Y N 143 
HIS CD2    C  Y N 144 
HIS CE1    C  Y N 145 
HIS NE2    N  Y N 146 
HIS OXT    O  N N 147 
HIS H      H  N N 148 
HIS H2     H  N N 149 
HIS HA     H  N N 150 
HIS HB2    H  N N 151 
HIS HB3    H  N N 152 
HIS HD1    H  N N 153 
HIS HD2    H  N N 154 
HIS HE1    H  N N 155 
HIS HE2    H  N N 156 
HIS HXT    H  N N 157 
HOH O      O  N N 158 
HOH H1     H  N N 159 
HOH H2     H  N N 160 
ILE N      N  N N 161 
ILE CA     C  N S 162 
ILE C      C  N N 163 
ILE O      O  N N 164 
ILE CB     C  N S 165 
ILE CG1    C  N N 166 
ILE CG2    C  N N 167 
ILE CD1    C  N N 168 
ILE OXT    O  N N 169 
ILE H      H  N N 170 
ILE H2     H  N N 171 
ILE HA     H  N N 172 
ILE HB     H  N N 173 
ILE HG12   H  N N 174 
ILE HG13   H  N N 175 
ILE HG21   H  N N 176 
ILE HG22   H  N N 177 
ILE HG23   H  N N 178 
ILE HD11   H  N N 179 
ILE HD12   H  N N 180 
ILE HD13   H  N N 181 
ILE HXT    H  N N 182 
LEU N      N  N N 183 
LEU CA     C  N S 184 
LEU C      C  N N 185 
LEU O      O  N N 186 
LEU CB     C  N N 187 
LEU CG     C  N N 188 
LEU CD1    C  N N 189 
LEU CD2    C  N N 190 
LEU OXT    O  N N 191 
LEU H      H  N N 192 
LEU H2     H  N N 193 
LEU HA     H  N N 194 
LEU HB2    H  N N 195 
LEU HB3    H  N N 196 
LEU HG     H  N N 197 
LEU HD11   H  N N 198 
LEU HD12   H  N N 199 
LEU HD13   H  N N 200 
LEU HD21   H  N N 201 
LEU HD22   H  N N 202 
LEU HD23   H  N N 203 
LEU HXT    H  N N 204 
LYS N      N  N N 205 
LYS CA     C  N S 206 
LYS C      C  N N 207 
LYS O      O  N N 208 
LYS CB     C  N N 209 
LYS CG     C  N N 210 
LYS CD     C  N N 211 
LYS CE     C  N N 212 
LYS NZ     N  N N 213 
LYS OXT    O  N N 214 
LYS H      H  N N 215 
LYS H2     H  N N 216 
LYS HA     H  N N 217 
LYS HB2    H  N N 218 
LYS HB3    H  N N 219 
LYS HG2    H  N N 220 
LYS HG3    H  N N 221 
LYS HD2    H  N N 222 
LYS HD3    H  N N 223 
LYS HE2    H  N N 224 
LYS HE3    H  N N 225 
LYS HZ1    H  N N 226 
LYS HZ2    H  N N 227 
LYS HZ3    H  N N 228 
LYS HXT    H  N N 229 
MET N      N  N N 230 
MET CA     C  N S 231 
MET C      C  N N 232 
MET O      O  N N 233 
MET CB     C  N N 234 
MET CG     C  N N 235 
MET SD     S  N N 236 
MET CE     C  N N 237 
MET OXT    O  N N 238 
MET H      H  N N 239 
MET H2     H  N N 240 
MET HA     H  N N 241 
MET HB2    H  N N 242 
MET HB3    H  N N 243 
MET HG2    H  N N 244 
MET HG3    H  N N 245 
MET HE1    H  N N 246 
MET HE2    H  N N 247 
MET HE3    H  N N 248 
MET HXT    H  N N 249 
MLE N      N  N N 250 
MLE CN     C  N N 251 
MLE CA     C  N S 252 
MLE CB     C  N N 253 
MLE CG     C  N N 254 
MLE CD1    C  N N 255 
MLE CD2    C  N N 256 
MLE C      C  N N 257 
MLE O      O  N N 258 
MLE OXT    O  N N 259 
MLE H      H  N N 260 
MLE HN1    H  N N 261 
MLE HN2    H  N N 262 
MLE HN3    H  N N 263 
MLE HA     H  N N 264 
MLE HB2    H  N N 265 
MLE HB3    H  N N 266 
MLE HG     H  N N 267 
MLE HD11   H  N N 268 
MLE HD12   H  N N 269 
MLE HD13   H  N N 270 
MLE HD21   H  N N 271 
MLE HD22   H  N N 272 
MLE HD23   H  N N 273 
MLE HXT    H  N N 274 
PHE N      N  N N 275 
PHE CA     C  N S 276 
PHE C      C  N N 277 
PHE O      O  N N 278 
PHE CB     C  N N 279 
PHE CG     C  Y N 280 
PHE CD1    C  Y N 281 
PHE CD2    C  Y N 282 
PHE CE1    C  Y N 283 
PHE CE2    C  Y N 284 
PHE CZ     C  Y N 285 
PHE OXT    O  N N 286 
PHE H      H  N N 287 
PHE H2     H  N N 288 
PHE HA     H  N N 289 
PHE HB2    H  N N 290 
PHE HB3    H  N N 291 
PHE HD1    H  N N 292 
PHE HD2    H  N N 293 
PHE HE1    H  N N 294 
PHE HE2    H  N N 295 
PHE HZ     H  N N 296 
PHE HXT    H  N N 297 
PRO N      N  N N 298 
PRO CA     C  N S 299 
PRO C      C  N N 300 
PRO O      O  N N 301 
PRO CB     C  N N 302 
PRO CG     C  N N 303 
PRO CD     C  N N 304 
PRO OXT    O  N N 305 
PRO H      H  N N 306 
PRO HA     H  N N 307 
PRO HB2    H  N N 308 
PRO HB3    H  N N 309 
PRO HG2    H  N N 310 
PRO HG3    H  N N 311 
PRO HD2    H  N N 312 
PRO HD3    H  N N 313 
PRO HXT    H  N N 314 
SAH N      N  N N 315 
SAH CA     C  N S 316 
SAH CB     C  N N 317 
SAH CG     C  N N 318 
SAH SD     S  N N 319 
SAH C      C  N N 320 
SAH O      O  N N 321 
SAH OXT    O  N N 322 
SAH "C5'"  C  N N 323 
SAH "C4'"  C  N S 324 
SAH "O4'"  O  N N 325 
SAH "C3'"  C  N S 326 
SAH "O3'"  O  N N 327 
SAH "C2'"  C  N R 328 
SAH "O2'"  O  N N 329 
SAH "C1'"  C  N R 330 
SAH N9     N  Y N 331 
SAH C8     C  Y N 332 
SAH N7     N  Y N 333 
SAH C5     C  Y N 334 
SAH C6     C  Y N 335 
SAH N6     N  N N 336 
SAH N1     N  Y N 337 
SAH C2     C  Y N 338 
SAH N3     N  Y N 339 
SAH C4     C  Y N 340 
SAH HN1    H  N N 341 
SAH HN2    H  N N 342 
SAH HA     H  N N 343 
SAH HB1    H  N N 344 
SAH HB2    H  N N 345 
SAH HG1    H  N N 346 
SAH HG2    H  N N 347 
SAH HXT    H  N N 348 
SAH "H5'1" H  N N 349 
SAH "H5'2" H  N N 350 
SAH "H4'"  H  N N 351 
SAH "H3'"  H  N N 352 
SAH "HO3'" H  N N 353 
SAH "H2'"  H  N N 354 
SAH "HO2'" H  N N 355 
SAH "H1'"  H  N N 356 
SAH H8     H  N N 357 
SAH HN61   H  N N 358 
SAH HN62   H  N N 359 
SAH H2     H  N N 360 
SER N      N  N N 361 
SER CA     C  N S 362 
SER C      C  N N 363 
SER O      O  N N 364 
SER CB     C  N N 365 
SER OG     O  N N 366 
SER OXT    O  N N 367 
SER H      H  N N 368 
SER H2     H  N N 369 
SER HA     H  N N 370 
SER HB2    H  N N 371 
SER HB3    H  N N 372 
SER HG     H  N N 373 
SER HXT    H  N N 374 
THR N      N  N N 375 
THR CA     C  N S 376 
THR C      C  N N 377 
THR O      O  N N 378 
THR CB     C  N R 379 
THR OG1    O  N N 380 
THR CG2    C  N N 381 
THR OXT    O  N N 382 
THR H      H  N N 383 
THR H2     H  N N 384 
THR HA     H  N N 385 
THR HB     H  N N 386 
THR HG1    H  N N 387 
THR HG21   H  N N 388 
THR HG22   H  N N 389 
THR HG23   H  N N 390 
THR HXT    H  N N 391 
TRP N      N  N N 392 
TRP CA     C  N S 393 
TRP C      C  N N 394 
TRP O      O  N N 395 
TRP CB     C  N N 396 
TRP CG     C  Y N 397 
TRP CD1    C  Y N 398 
TRP CD2    C  Y N 399 
TRP NE1    N  Y N 400 
TRP CE2    C  Y N 401 
TRP CE3    C  Y N 402 
TRP CZ2    C  Y N 403 
TRP CZ3    C  Y N 404 
TRP CH2    C  Y N 405 
TRP OXT    O  N N 406 
TRP H      H  N N 407 
TRP H2     H  N N 408 
TRP HA     H  N N 409 
TRP HB2    H  N N 410 
TRP HB3    H  N N 411 
TRP HD1    H  N N 412 
TRP HE1    H  N N 413 
TRP HE3    H  N N 414 
TRP HZ2    H  N N 415 
TRP HZ3    H  N N 416 
TRP HH2    H  N N 417 
TRP HXT    H  N N 418 
TYR N      N  N N 419 
TYR CA     C  N S 420 
TYR C      C  N N 421 
TYR O      O  N N 422 
TYR CB     C  N N 423 
TYR CG     C  Y N 424 
TYR CD1    C  Y N 425 
TYR CD2    C  Y N 426 
TYR CE1    C  Y N 427 
TYR CE2    C  Y N 428 
TYR CZ     C  Y N 429 
TYR OH     O  N N 430 
TYR OXT    O  N N 431 
TYR H      H  N N 432 
TYR H2     H  N N 433 
TYR HA     H  N N 434 
TYR HB2    H  N N 435 
TYR HB3    H  N N 436 
TYR HD1    H  N N 437 
TYR HD2    H  N N 438 
TYR HE1    H  N N 439 
TYR HE2    H  N N 440 
TYR HH     H  N N 441 
TYR HXT    H  N N 442 
VAL N      N  N N 443 
VAL CA     C  N S 444 
VAL C      C  N N 445 
VAL O      O  N N 446 
VAL CB     C  N N 447 
VAL CG1    C  N N 448 
VAL CG2    C  N N 449 
VAL OXT    O  N N 450 
VAL H      H  N N 451 
VAL H2     H  N N 452 
VAL HA     H  N N 453 
VAL HB     H  N N 454 
VAL HG11   H  N N 455 
VAL HG12   H  N N 456 
VAL HG13   H  N N 457 
VAL HG21   H  N N 458 
VAL HG22   H  N N 459 
VAL HG23   H  N N 460 
VAL HXT    H  N N 461 
ZN  ZN     ZN N N 462 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LYS N     CA     sing N N 194 
LYS N     H      sing N N 195 
LYS N     H2     sing N N 196 
LYS CA    C      sing N N 197 
LYS CA    CB     sing N N 198 
LYS CA    HA     sing N N 199 
LYS C     O      doub N N 200 
LYS C     OXT    sing N N 201 
LYS CB    CG     sing N N 202 
LYS CB    HB2    sing N N 203 
LYS CB    HB3    sing N N 204 
LYS CG    CD     sing N N 205 
LYS CG    HG2    sing N N 206 
LYS CG    HG3    sing N N 207 
LYS CD    CE     sing N N 208 
LYS CD    HD2    sing N N 209 
LYS CD    HD3    sing N N 210 
LYS CE    NZ     sing N N 211 
LYS CE    HE2    sing N N 212 
LYS CE    HE3    sing N N 213 
LYS NZ    HZ1    sing N N 214 
LYS NZ    HZ2    sing N N 215 
LYS NZ    HZ3    sing N N 216 
LYS OXT   HXT    sing N N 217 
MET N     CA     sing N N 218 
MET N     H      sing N N 219 
MET N     H2     sing N N 220 
MET CA    C      sing N N 221 
MET CA    CB     sing N N 222 
MET CA    HA     sing N N 223 
MET C     O      doub N N 224 
MET C     OXT    sing N N 225 
MET CB    CG     sing N N 226 
MET CB    HB2    sing N N 227 
MET CB    HB3    sing N N 228 
MET CG    SD     sing N N 229 
MET CG    HG2    sing N N 230 
MET CG    HG3    sing N N 231 
MET SD    CE     sing N N 232 
MET CE    HE1    sing N N 233 
MET CE    HE2    sing N N 234 
MET CE    HE3    sing N N 235 
MET OXT   HXT    sing N N 236 
MLE N     CN     sing N N 237 
MLE N     CA     sing N N 238 
MLE N     H      sing N N 239 
MLE CN    HN1    sing N N 240 
MLE CN    HN2    sing N N 241 
MLE CN    HN3    sing N N 242 
MLE CA    CB     sing N N 243 
MLE CA    C      sing N N 244 
MLE CA    HA     sing N N 245 
MLE CB    CG     sing N N 246 
MLE CB    HB2    sing N N 247 
MLE CB    HB3    sing N N 248 
MLE CG    CD1    sing N N 249 
MLE CG    CD2    sing N N 250 
MLE CG    HG     sing N N 251 
MLE CD1   HD11   sing N N 252 
MLE CD1   HD12   sing N N 253 
MLE CD1   HD13   sing N N 254 
MLE CD2   HD21   sing N N 255 
MLE CD2   HD22   sing N N 256 
MLE CD2   HD23   sing N N 257 
MLE C     O      doub N N 258 
MLE C     OXT    sing N N 259 
MLE OXT   HXT    sing N N 260 
PHE N     CA     sing N N 261 
PHE N     H      sing N N 262 
PHE N     H2     sing N N 263 
PHE CA    C      sing N N 264 
PHE CA    CB     sing N N 265 
PHE CA    HA     sing N N 266 
PHE C     O      doub N N 267 
PHE C     OXT    sing N N 268 
PHE CB    CG     sing N N 269 
PHE CB    HB2    sing N N 270 
PHE CB    HB3    sing N N 271 
PHE CG    CD1    doub Y N 272 
PHE CG    CD2    sing Y N 273 
PHE CD1   CE1    sing Y N 274 
PHE CD1   HD1    sing N N 275 
PHE CD2   CE2    doub Y N 276 
PHE CD2   HD2    sing N N 277 
PHE CE1   CZ     doub Y N 278 
PHE CE1   HE1    sing N N 279 
PHE CE2   CZ     sing Y N 280 
PHE CE2   HE2    sing N N 281 
PHE CZ    HZ     sing N N 282 
PHE OXT   HXT    sing N N 283 
PRO N     CA     sing N N 284 
PRO N     CD     sing N N 285 
PRO N     H      sing N N 286 
PRO CA    C      sing N N 287 
PRO CA    CB     sing N N 288 
PRO CA    HA     sing N N 289 
PRO C     O      doub N N 290 
PRO C     OXT    sing N N 291 
PRO CB    CG     sing N N 292 
PRO CB    HB2    sing N N 293 
PRO CB    HB3    sing N N 294 
PRO CG    CD     sing N N 295 
PRO CG    HG2    sing N N 296 
PRO CG    HG3    sing N N 297 
PRO CD    HD2    sing N N 298 
PRO CD    HD3    sing N N 299 
PRO OXT   HXT    sing N N 300 
SAH N     CA     sing N N 301 
SAH N     HN1    sing N N 302 
SAH N     HN2    sing N N 303 
SAH CA    CB     sing N N 304 
SAH CA    C      sing N N 305 
SAH CA    HA     sing N N 306 
SAH CB    CG     sing N N 307 
SAH CB    HB1    sing N N 308 
SAH CB    HB2    sing N N 309 
SAH CG    SD     sing N N 310 
SAH CG    HG1    sing N N 311 
SAH CG    HG2    sing N N 312 
SAH SD    "C5'"  sing N N 313 
SAH C     O      doub N N 314 
SAH C     OXT    sing N N 315 
SAH OXT   HXT    sing N N 316 
SAH "C5'" "C4'"  sing N N 317 
SAH "C5'" "H5'1" sing N N 318 
SAH "C5'" "H5'2" sing N N 319 
SAH "C4'" "O4'"  sing N N 320 
SAH "C4'" "C3'"  sing N N 321 
SAH "C4'" "H4'"  sing N N 322 
SAH "O4'" "C1'"  sing N N 323 
SAH "C3'" "O3'"  sing N N 324 
SAH "C3'" "C2'"  sing N N 325 
SAH "C3'" "H3'"  sing N N 326 
SAH "O3'" "HO3'" sing N N 327 
SAH "C2'" "O2'"  sing N N 328 
SAH "C2'" "C1'"  sing N N 329 
SAH "C2'" "H2'"  sing N N 330 
SAH "O2'" "HO2'" sing N N 331 
SAH "C1'" N9     sing N N 332 
SAH "C1'" "H1'"  sing N N 333 
SAH N9    C8     sing Y N 334 
SAH N9    C4     sing Y N 335 
SAH C8    N7     doub Y N 336 
SAH C8    H8     sing N N 337 
SAH N7    C5     sing Y N 338 
SAH C5    C6     sing Y N 339 
SAH C5    C4     doub Y N 340 
SAH C6    N6     sing N N 341 
SAH C6    N1     doub Y N 342 
SAH N6    HN61   sing N N 343 
SAH N6    HN62   sing N N 344 
SAH N1    C2     sing Y N 345 
SAH C2    N3     doub Y N 346 
SAH C2    H2     sing N N 347 
SAH N3    C4     sing Y N 348 
SER N     CA     sing N N 349 
SER N     H      sing N N 350 
SER N     H2     sing N N 351 
SER CA    C      sing N N 352 
SER CA    CB     sing N N 353 
SER CA    HA     sing N N 354 
SER C     O      doub N N 355 
SER C     OXT    sing N N 356 
SER CB    OG     sing N N 357 
SER CB    HB2    sing N N 358 
SER CB    HB3    sing N N 359 
SER OG    HG     sing N N 360 
SER OXT   HXT    sing N N 361 
THR N     CA     sing N N 362 
THR N     H      sing N N 363 
THR N     H2     sing N N 364 
THR CA    C      sing N N 365 
THR CA    CB     sing N N 366 
THR CA    HA     sing N N 367 
THR C     O      doub N N 368 
THR C     OXT    sing N N 369 
THR CB    OG1    sing N N 370 
THR CB    CG2    sing N N 371 
THR CB    HB     sing N N 372 
THR OG1   HG1    sing N N 373 
THR CG2   HG21   sing N N 374 
THR CG2   HG22   sing N N 375 
THR CG2   HG23   sing N N 376 
THR OXT   HXT    sing N N 377 
TRP N     CA     sing N N 378 
TRP N     H      sing N N 379 
TRP N     H2     sing N N 380 
TRP CA    C      sing N N 381 
TRP CA    CB     sing N N 382 
TRP CA    HA     sing N N 383 
TRP C     O      doub N N 384 
TRP C     OXT    sing N N 385 
TRP CB    CG     sing N N 386 
TRP CB    HB2    sing N N 387 
TRP CB    HB3    sing N N 388 
TRP CG    CD1    doub Y N 389 
TRP CG    CD2    sing Y N 390 
TRP CD1   NE1    sing Y N 391 
TRP CD1   HD1    sing N N 392 
TRP CD2   CE2    doub Y N 393 
TRP CD2   CE3    sing Y N 394 
TRP NE1   CE2    sing Y N 395 
TRP NE1   HE1    sing N N 396 
TRP CE2   CZ2    sing Y N 397 
TRP CE3   CZ3    doub Y N 398 
TRP CE3   HE3    sing N N 399 
TRP CZ2   CH2    doub Y N 400 
TRP CZ2   HZ2    sing N N 401 
TRP CZ3   CH2    sing Y N 402 
TRP CZ3   HZ3    sing N N 403 
TRP CH2   HH2    sing N N 404 
TRP OXT   HXT    sing N N 405 
TYR N     CA     sing N N 406 
TYR N     H      sing N N 407 
TYR N     H2     sing N N 408 
TYR CA    C      sing N N 409 
TYR CA    CB     sing N N 410 
TYR CA    HA     sing N N 411 
TYR C     O      doub N N 412 
TYR C     OXT    sing N N 413 
TYR CB    CG     sing N N 414 
TYR CB    HB2    sing N N 415 
TYR CB    HB3    sing N N 416 
TYR CG    CD1    doub Y N 417 
TYR CG    CD2    sing Y N 418 
TYR CD1   CE1    sing Y N 419 
TYR CD1   HD1    sing N N 420 
TYR CD2   CE2    doub Y N 421 
TYR CD2   HD2    sing N N 422 
TYR CE1   CZ     doub Y N 423 
TYR CE1   HE1    sing N N 424 
TYR CE2   CZ     sing Y N 425 
TYR CE2   HE2    sing N N 426 
TYR CZ    OH     sing N N 427 
TYR OH    HH     sing N N 428 
TYR OXT   HXT    sing N N 429 
VAL N     CA     sing N N 430 
VAL N     H      sing N N 431 
VAL N     H2     sing N N 432 
VAL CA    C      sing N N 433 
VAL CA    CB     sing N N 434 
VAL CA    HA     sing N N 435 
VAL C     O      doub N N 436 
VAL C     OXT    sing N N 437 
VAL CB    CG1    sing N N 438 
VAL CB    CG2    sing N N 439 
VAL CB    HB     sing N N 440 
VAL CG1   HG11   sing N N 441 
VAL CG1   HG12   sing N N 442 
VAL CG1   HG13   sing N N 443 
VAL CG2   HG21   sing N N 444 
VAL CG2   HG22   sing N N 445 
VAL CG2   HG23   sing N N 446 
VAL OXT   HXT    sing N N 447 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R35GM133475 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7LTE 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CH0 
_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]   0.019183 
_atom_sites.fract_transf_matrix[1][2]   -0.000016 
_atom_sites.fract_transf_matrix[1][3]   0.001144 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009258 
_atom_sites.fract_transf_matrix[2][3]   0.000001 
_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]   0.017098 
_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  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . GLY A 1 2   ? 25.383  15.116  -6.181  1.00 16.39 ?  2   GLY A N     1 
ATOM   2     C  CA    . GLY A 1 2   ? 24.152  14.584  -6.795  1.00 17.24 ?  2   GLY A CA    1 
ATOM   3     C  C     . GLY A 1 2   ? 23.598  13.406  -5.998  1.00 20.12 ?  2   GLY A C     1 
ATOM   4     O  O     . GLY A 1 2   ? 24.350  12.591  -5.466  1.00 22.02 ?  2   GLY A O     1 
ATOM   5     N  N     . SER A 1 3   ? 22.266  13.330  -5.955  1.00 19.13 ?  3   SER A N     1 
ATOM   6     C  CA    . SER A 1 3   ? 21.556  12.414  -5.081  1.00 20.08 ?  3   SER A CA    1 
ATOM   7     C  C     . SER A 1 3   ? 20.276  11.965  -5.773  1.00 19.35 ?  3   SER A C     1 
ATOM   8     O  O     . SER A 1 3   ? 19.906  12.501  -6.815  1.00 16.42 ?  3   SER A O     1 
ATOM   9     C  CB    . SER A 1 3   ? 21.257  13.056  -3.752  1.00 21.07 ?  3   SER A CB    1 
ATOM   10    O  OG    . SER A 1 3   ? 20.592  14.299  -3.932  1.00 22.45 ?  3   SER A OG    1 
ATOM   11    N  N     . LEU A 1 4   ? 19.602  10.983  -5.174  1.00 18.31 ?  4   LEU A N     1 
ATOM   12    C  CA    . LEU A 1 4   ? 18.432  10.398  -5.797  1.00 16.22 ?  4   LEU A CA    1 
ATOM   13    C  C     . LEU A 1 4   ? 17.335  10.210  -4.758  1.00 13.59 ?  4   LEU A C     1 
ATOM   14    O  O     . LEU A 1 4   ? 17.581  9.709   -3.664  1.00 11.96 ?  4   LEU A O     1 
ATOM   15    C  CB    . LEU A 1 4   ? 18.836  9.078   -6.448  1.00 16.68 ?  4   LEU A CB    1 
ATOM   16    C  CG    . LEU A 1 4   ? 17.694  8.262   -7.057  1.00 17.70 ?  4   LEU A CG    1 
ATOM   17    C  CD1   . LEU A 1 4   ? 16.993  9.060   -8.143  1.00 17.39 ?  4   LEU A CD1   1 
ATOM   18    C  CD2   . LEU A 1 4   ? 18.213  6.939   -7.592  1.00 18.45 ?  4   LEU A CD2   1 
ATOM   19    N  N     . VAL A 1 5   ? 16.124  10.638  -5.124  1.00 14.36 ?  5   VAL A N     1 
ATOM   20    C  CA    . VAL A 1 5   ? 14.935  10.355  -4.342  1.00 14.00 ?  5   VAL A CA    1 
ATOM   21    C  C     . VAL A 1 5   ? 13.875  9.846   -5.312  1.00 12.90 ?  5   VAL A C     1 
ATOM   22    O  O     . VAL A 1 5   ? 13.514  10.535  -6.262  1.00 14.46 ?  5   VAL A O     1 
ATOM   23    C  CB    . VAL A 1 5   ? 14.399  11.554  -3.535  1.00 14.77 ?  5   VAL A CB    1 
ATOM   24    C  CG1   . VAL A 1 5   ? 13.195  11.152  -2.690  1.00 15.06 ?  5   VAL A CG1   1 
ATOM   25    C  CG2   . VAL A 1 5   ? 15.473  12.189  -2.660  1.00 14.63 ?  5   VAL A CG2   1 
ATOM   26    N  N     . CYS A 1 6   ? 13.407  8.621   -5.070  1.00 15.18 ?  6   CYS A N     1 
ATOM   27    C  CA    . CYS A 1 6   ? 12.321  8.046   -5.842  1.00 14.68 ?  6   CYS A CA    1 
ATOM   28    C  C     . CYS A 1 6   ? 11.024  8.207   -5.055  1.00 13.63 ?  6   CYS A C     1 
ATOM   29    O  O     . CYS A 1 6   ? 10.937  7.769   -3.911  1.00 14.36 ?  6   CYS A O     1 
ATOM   30    C  CB    . CYS A 1 6   ? 12.587  6.578   -6.150  1.00 17.14 ?  6   CYS A CB    1 
ATOM   31    S  SG    . CYS A 1 6   ? 14.119  6.303   -7.078  1.00 21.71 ?  6   CYS A SG    1 
ATOM   32    N  N     . VAL A 1 7   ? 10.028  8.848   -5.678  1.00 15.60 ?  7   VAL A N     1 
ATOM   33    C  CA    . VAL A 1 7   ? 8.747   9.084   -5.032  1.00 15.66 ?  7   VAL A CA    1 
ATOM   34    C  C     . VAL A 1 7   ? 7.630   8.516   -5.902  1.00 17.05 ?  7   VAL A C     1 
ATOM   35    O  O     . VAL A 1 7   ? 7.852   8.156   -7.056  1.00 19.14 ?  7   VAL A O     1 
ATOM   36    C  CB    . VAL A 1 7   ? 8.507   10.581  -4.754  1.00 15.39 ?  7   VAL A CB    1 
ATOM   37    C  CG1   . VAL A 1 7   ? 9.618   11.182  -3.903  1.00 14.47 ?  7   VAL A CG1   1 
ATOM   38    C  CG2   . VAL A 1 7   ? 8.320   11.383  -6.038  1.00 14.88 ?  7   VAL A CG2   1 
ATOM   39    N  N     . GLY A 1 8   ? 6.426   8.451   -5.323  1.00 20.18 ?  8   GLY A N     1 
ATOM   40    C  CA    . GLY A 1 8   ? 5.231   8.043   -6.045  1.00 18.57 ?  8   GLY A CA    1 
ATOM   41    C  C     . GLY A 1 8   ? 4.214   9.180   -6.115  1.00 20.29 ?  8   GLY A C     1 
ATOM   42    O  O     . GLY A 1 8   ? 4.188   10.049  -5.247  1.00 18.48 ?  8   GLY A O     1 
ATOM   43    N  N     . THR A 1 9   ? 3.377   9.156   -7.159  1.00 21.68 ?  9   THR A N     1 
ATOM   44    C  CA    . THR A 1 9   ? 2.358   10.174  -7.362  1.00 20.98 ?  9   THR A CA    1 
ATOM   45    C  C     . THR A 1 9   ? 0.967   9.568   -7.177  1.00 18.40 ?  9   THR A C     1 
ATOM   46    O  O     . THR A 1 9   ? -0.031  10.208  -7.501  1.00 17.65 ?  9   THR A O     1 
ATOM   47    C  CB    . THR A 1 9   ? 2.509   10.786  -8.756  1.00 21.45 ?  9   THR A CB    1 
ATOM   48    O  OG1   . THR A 1 9   ? 2.360   9.712   -9.680  1.00 25.25 ?  9   THR A OG1   1 
ATOM   49    C  CG2   . THR A 1 9   ? 3.855   11.453  -8.969  1.00 20.47 ?  9   THR A CG2   1 
ATOM   50    N  N     . GLY A 1 10  ? 0.901   8.336   -6.660  1.00 16.78 ?  10  GLY A N     1 
ATOM   51    C  CA    . GLY A 1 10  ? -0.370  7.649   -6.492  1.00 13.46 ?  10  GLY A CA    1 
ATOM   52    C  C     . GLY A 1 10  ? -1.047  7.406   -7.839  1.00 12.77 ?  10  GLY A C     1 
ATOM   53    O  O     . GLY A 1 10  ? -0.445  7.630   -8.887  1.00 11.49 ?  10  GLY A O     1 
ATOM   54    N  N     . LEU A 1 11  ? -2.306  6.957   -7.798  1.00 13.90 ?  11  LEU A N     1 
ATOM   55    C  CA    . LEU A 1 11  ? -3.072  6.671   -9.001  1.00 15.35 ?  11  LEU A CA    1 
ATOM   56    C  C     . LEU A 1 11  ? -3.821  7.918   -9.471  1.00 15.55 ?  11  LEU A C     1 
ATOM   57    O  O     . LEU A 1 11  ? -3.805  8.243   -10.657 1.00 15.42 ?  11  LEU A O     1 
ATOM   58    C  CB    . LEU A 1 11  ? -4.028  5.514   -8.716  1.00 17.70 ?  11  LEU A CB    1 
ATOM   59    C  CG    . LEU A 1 11  ? -3.429  4.109   -8.834  1.00 20.76 ?  11  LEU A CG    1 
ATOM   60    C  CD1   . LEU A 1 11  ? -3.109  3.819   -10.288 1.00 21.91 ?  11  LEU A CD1   1 
ATOM   61    C  CD2   . LEU A 1 11  ? -2.188  3.943   -7.977  1.00 23.11 ?  11  LEU A CD2   1 
ATOM   62    N  N     . GLN A 1 12  ? -4.477  8.611   -8.535  1.00 15.23 ?  12  GLN A N     1 
ATOM   63    C  CA    . GLN A 1 12  ? -5.347  9.726   -8.877  1.00 17.48 ?  12  GLN A CA    1 
ATOM   64    C  C     . GLN A 1 12  ? -4.520  10.979  -9.148  1.00 18.90 ?  12  GLN A C     1 
ATOM   65    O  O     . GLN A 1 12  ? -3.514  11.233  -8.489  1.00 20.08 ?  12  GLN A O     1 
ATOM   66    C  CB    . GLN A 1 12  ? -6.384  9.986   -7.783  1.00 17.18 ?  12  GLN A CB    1 
ATOM   67    C  CG    . GLN A 1 12  ? -7.681  9.198   -7.944  1.00 16.68 ?  12  GLN A CG    1 
ATOM   68    C  CD    . GLN A 1 12  ? -8.616  9.790   -8.979  1.00 17.07 ?  12  GLN A CD    1 
ATOM   69    O  OE1   . GLN A 1 12  ? -8.203  10.534  -9.876  1.00 15.99 ?  12  GLN A OE1   1 
ATOM   70    N  NE2   . GLN A 1 12  ? -9.894  9.458   -8.868  1.00 17.66 ?  12  GLN A NE2   1 
ATOM   71    N  N     . LEU A 1 13  ? -4.981  11.756  -10.132 1.00 19.48 ?  13  LEU A N     1 
ATOM   72    C  CA    . LEU A 1 13  ? -4.358  13.012  -10.514 1.00 17.89 ?  13  LEU A CA    1 
ATOM   73    C  C     . LEU A 1 13  ? -4.229  13.949  -9.313  1.00 16.85 ?  13  LEU A C     1 
ATOM   74    O  O     . LEU A 1 13  ? -5.211  14.244  -8.637  1.00 18.46 ?  13  LEU A O     1 
ATOM   75    C  CB    . LEU A 1 13  ? -5.214  13.638  -11.615 1.00 18.94 ?  13  LEU A CB    1 
ATOM   76    C  CG    . LEU A 1 13  ? -4.776  15.025  -12.094 1.00 19.13 ?  13  LEU A CG    1 
ATOM   77    C  CD1   . LEU A 1 13  ? -3.463  14.916  -12.845 1.00 19.81 ?  13  LEU A CD1   1 
ATOM   78    C  CD2   . LEU A 1 13  ? -5.840  15.692  -12.951 1.00 20.02 ?  13  LEU A CD2   1 
ATOM   79    N  N     . ALA A 1 14  ? -2.989  14.380  -9.054  1.00 15.78 ?  14  ALA A N     1 
ATOM   80    C  CA    . ALA A 1 14  ? -2.686  15.617  -8.347  1.00 15.15 ?  14  ALA A CA    1 
ATOM   81    C  C     . ALA A 1 14  ? -2.817  15.485  -6.829  1.00 13.64 ?  14  ALA A C     1 
ATOM   82    O  O     . ALA A 1 14  ? -2.018  16.064  -6.096  1.00 14.51 ?  14  ALA A O     1 
ATOM   83    C  CB    . ALA A 1 14  ? -3.553  16.741  -8.878  1.00 16.24 ?  14  ALA A CB    1 
ATOM   84    N  N     . GLY A 1 15  ? -3.824  14.750  -6.349  1.00 13.52 ?  15  GLY A N     1 
ATOM   85    C  CA    . GLY A 1 15  ? -4.158  14.787  -4.933  1.00 14.39 ?  15  GLY A CA    1 
ATOM   86    C  C     . GLY A 1 15  ? -3.555  13.635  -4.130  1.00 13.88 ?  15  GLY A C     1 
ATOM   87    O  O     . GLY A 1 15  ? -3.469  13.726  -2.909  1.00 14.81 ?  15  GLY A O     1 
ATOM   88    N  N     . GLN A 1 16  ? -3.136  12.556  -4.801  1.00 13.44 ?  16  GLN A N     1 
ATOM   89    C  CA    . GLN A 1 16  ? -2.890  11.303  -4.101  1.00 13.73 ?  16  GLN A CA    1 
ATOM   90    C  C     . GLN A 1 16  ? -1.414  11.147  -3.733  1.00 15.14 ?  16  GLN A C     1 
ATOM   91    O  O     . GLN A 1 16  ? -1.041  10.179  -3.071  1.00 12.63 ?  16  GLN A O     1 
ATOM   92    C  CB    . GLN A 1 16  ? -3.386  10.115  -4.924  1.00 13.46 ?  16  GLN A CB    1 
ATOM   93    C  CG    . GLN A 1 16  ? -3.635  8.863   -4.090  1.00 14.88 ?  16  GLN A CG    1 
ATOM   94    C  CD    . GLN A 1 16  ? -4.552  7.870   -4.768  1.00 14.57 ?  16  GLN A CD    1 
ATOM   95    O  OE1   . GLN A 1 16  ? -4.349  7.492   -5.927  1.00 15.15 ?  16  GLN A OE1   1 
ATOM   96    N  NE2   . GLN A 1 16  ? -5.584  7.448   -4.052  1.00 14.05 ?  16  GLN A NE2   1 
ATOM   97    N  N     . ILE A 1 17  ? -0.579  12.103  -4.149  1.00 15.84 ?  17  ILE A N     1 
ATOM   98    C  CA    . ILE A 1 17  ? 0.827   12.095  -3.776  1.00 16.83 ?  17  ILE A CA    1 
ATOM   99    C  C     . ILE A 1 17  ? 0.964   12.630  -2.351  1.00 17.09 ?  17  ILE A C     1 
ATOM   100   O  O     . ILE A 1 17  ? 0.130   13.407  -1.892  1.00 24.53 ?  17  ILE A O     1 
ATOM   101   C  CB    . ILE A 1 17  ? 1.666   12.909  -4.778  1.00 15.20 ?  17  ILE A CB    1 
ATOM   102   C  CG1   . ILE A 1 17  ? 3.166   12.787  -4.487  1.00 13.93 ?  17  ILE A CG1   1 
ATOM   103   C  CG2   . ILE A 1 17  ? 1.205   14.368  -4.814  1.00 15.48 ?  17  ILE A CG2   1 
ATOM   104   C  CD1   . ILE A 1 17  ? 4.052   13.616  -5.400  1.00 13.29 ?  17  ILE A CD1   1 
ATOM   105   N  N     . SER A 1 18  ? 2.024   12.187  -1.665  1.00 15.18 ?  18  SER A N     1 
ATOM   106   C  CA    . SER A 1 18  ? 2.385   12.673  -0.341  1.00 15.78 ?  18  SER A CA    1 
ATOM   107   C  C     . SER A 1 18  ? 2.649   14.175  -0.376  1.00 14.00 ?  18  SER A C     1 
ATOM   108   O  O     . SER A 1 18  ? 2.975   14.726  -1.424  1.00 13.75 ?  18  SER A O     1 
ATOM   109   C  CB    . SER A 1 18  ? 3.597   11.947  0.185   1.00 15.04 ?  18  SER A CB    1 
ATOM   110   O  OG    . SER A 1 18  ? 3.249   10.672  0.703   1.00 18.72 ?  18  SER A OG    1 
ATOM   111   N  N     . VAL A 1 19  ? 2.530   14.820  0.790   1.00 13.61 ?  19  VAL A N     1 
ATOM   112   C  CA    . VAL A 1 19  ? 2.855   16.230  0.928   1.00 14.53 ?  19  VAL A CA    1 
ATOM   113   C  C     . VAL A 1 19  ? 4.368   16.392  0.790   1.00 16.40 ?  19  VAL A C     1 
ATOM   114   O  O     . VAL A 1 19  ? 4.842   17.320  0.137   1.00 16.84 ?  19  VAL A O     1 
ATOM   115   C  CB    . VAL A 1 19  ? 2.338   16.783  2.271   1.00 14.79 ?  19  VAL A CB    1 
ATOM   116   C  CG1   . VAL A 1 19  ? 2.796   18.215  2.527   1.00 15.04 ?  19  VAL A CG1   1 
ATOM   117   C  CG2   . VAL A 1 19  ? 0.819   16.684  2.374   1.00 14.50 ?  19  VAL A CG2   1 
ATOM   118   N  N     . LEU A 1 20  ? 5.118   15.463  1.394   1.00 18.91 ?  20  LEU A N     1 
ATOM   119   C  CA    . LEU A 1 20  ? 6.571   15.514  1.360   1.00 16.40 ?  20  LEU A CA    1 
ATOM   120   C  C     . LEU A 1 20  ? 7.051   15.237  -0.063  1.00 14.68 ?  20  LEU A C     1 
ATOM   121   O  O     . LEU A 1 20  ? 7.918   15.942  -0.575  1.00 13.71 ?  20  LEU A O     1 
ATOM   122   C  CB    . LEU A 1 20  ? 7.194   14.534  2.355   1.00 15.09 ?  20  LEU A CB    1 
ATOM   123   C  CG    . LEU A 1 20  ? 8.717   14.639  2.511   1.00 15.69 ?  20  LEU A CG    1 
ATOM   124   C  CD1   . LEU A 1 20  ? 9.095   16.002  3.070   1.00 17.86 ?  20  LEU A CD1   1 
ATOM   125   C  CD2   . LEU A 1 20  ? 9.307   13.539  3.378   1.00 13.90 ?  20  LEU A CD2   1 
ATOM   126   N  N     . SER A 1 21  ? 6.472   14.212  -0.696  1.00 14.15 ?  21  SER A N     1 
ATOM   127   C  CA    . SER A 1 21  ? 6.912   13.779  -2.013  1.00 13.43 ?  21  SER A CA    1 
ATOM   128   C  C     . SER A 1 21  ? 6.711   14.898  -3.030  1.00 13.69 ?  21  SER A C     1 
ATOM   129   O  O     . SER A 1 21  ? 7.559   15.116  -3.894  1.00 15.67 ?  21  SER A O     1 
ATOM   130   C  CB    . SER A 1 21  ? 6.207   12.519  -2.441  1.00 12.28 ?  21  SER A CB    1 
ATOM   131   O  OG    . SER A 1 21  ? 6.610   11.422  -1.635  1.00 13.63 ?  21  SER A OG    1 
ATOM   132   N  N     . ARG A 1 22  ? 5.582   15.602  -2.915  1.00 12.53 ?  22  ARG A N     1 
ATOM   133   C  CA    . ARG A 1 22  ? 5.300   16.737  -3.777  1.00 13.33 ?  22  ARG A CA    1 
ATOM   134   C  C     . ARG A 1 22  ? 6.422   17.765  -3.644  1.00 12.71 ?  22  ARG A C     1 
ATOM   135   O  O     . ARG A 1 22  ? 6.873   18.338  -4.635  1.00 10.57 ?  22  ARG A O     1 
ATOM   136   C  CB    . ARG A 1 22  ? 3.953   17.369  -3.411  1.00 15.95 ?  22  ARG A CB    1 
ATOM   137   C  CG    . ARG A 1 22  ? 3.425   18.303  -4.490  1.00 18.76 ?  22  ARG A CG    1 
ATOM   138   C  CD    . ARG A 1 22  ? 2.228   19.131  -4.051  1.00 20.28 ?  22  ARG A CD    1 
ATOM   139   N  NE    . ARG A 1 22  ? 1.607   19.780  -5.211  1.00 21.27 ?  22  ARG A NE    1 
ATOM   140   C  CZ    . ARG A 1 22  ? 1.674   21.074  -5.501  1.00 22.93 ?  22  ARG A CZ    1 
ATOM   141   N  NH1   . ARG A 1 22  ? 2.319   21.908  -4.702  1.00 19.76 1  22  ARG A NH1   1 
ATOM   142   N  NH2   . ARG A 1 22  ? 1.092   21.529  -6.596  1.00 26.04 ?  22  ARG A NH2   1 
ATOM   143   N  N     . SER A 1 23  ? 6.867   17.990  -2.405  1.00 13.84 ?  23  SER A N     1 
ATOM   144   C  CA    . SER A 1 23  ? 7.891   18.983  -2.130  1.00 13.42 ?  23  SER A CA    1 
ATOM   145   C  C     . SER A 1 23  ? 9.208   18.556  -2.773  1.00 13.12 ?  23  SER A C     1 
ATOM   146   O  O     . SER A 1 23  ? 9.970   19.394  -3.249  1.00 13.48 ?  23  SER A O     1 
ATOM   147   C  CB    . SER A 1 23  ? 8.042   19.217  -0.647  1.00 12.52 ?  23  SER A CB    1 
ATOM   148   O  OG    . SER A 1 23  ? 9.149   20.064  -0.372  1.00 11.84 ?  23  SER A OG    1 
ATOM   149   N  N     . TYR A 1 24  ? 9.455   17.240  -2.796  1.00 14.82 ?  24  TYR A N     1 
ATOM   150   C  CA    . TYR A 1 24  ? 10.660  16.691  -3.397  1.00 14.26 ?  24  TYR A CA    1 
ATOM   151   C  C     . TYR A 1 24  ? 10.692  17.034  -4.884  1.00 15.11 ?  24  TYR A C     1 
ATOM   152   O  O     . TYR A 1 24  ? 11.721  17.467  -5.398  1.00 16.32 ?  24  TYR A O     1 
ATOM   153   C  CB    . TYR A 1 24  ? 10.777  15.178  -3.183  1.00 12.77 ?  24  TYR A CB    1 
ATOM   154   C  CG    . TYR A 1 24  ? 11.563  14.797  -1.936  1.00 11.80 ?  24  TYR A CG    1 
ATOM   155   C  CD1   . TYR A 1 24  ? 12.917  15.095  -1.831  1.00 10.79 ?  24  TYR A CD1   1 
ATOM   156   C  CD2   . TYR A 1 24  ? 10.963  14.126  -0.878  1.00 11.81 ?  24  TYR A CD2   1 
ATOM   157   C  CE1   . TYR A 1 24  ? 13.645  14.754  -0.704  1.00 11.48 ?  24  TYR A CE1   1 
ATOM   158   C  CE2   . TYR A 1 24  ? 11.682  13.777  0.254   1.00 11.55 ?  24  TYR A CE2   1 
ATOM   159   C  CZ    . TYR A 1 24  ? 13.026  14.090  0.341   1.00 11.00 ?  24  TYR A CZ    1 
ATOM   160   O  OH    . TYR A 1 24  ? 13.731  13.745  1.457   1.00 9.66  ?  24  TYR A OH    1 
ATOM   161   N  N     . ILE A 1 25  ? 9.563   16.826  -5.567  1.00 14.58 ?  25  ILE A N     1 
ATOM   162   C  CA    . ILE A 1 25  ? 9.452   17.168  -6.975  1.00 15.76 ?  25  ILE A CA    1 
ATOM   163   C  C     . ILE A 1 25  ? 9.696   18.667  -7.136  1.00 17.89 ?  25  ILE A C     1 
ATOM   164   O  O     . ILE A 1 25  ? 10.488  19.090  -7.977  1.00 16.87 ?  25  ILE A O     1 
ATOM   165   C  CB    . ILE A 1 25  ? 8.083   16.739  -7.535  1.00 15.69 ?  25  ILE A CB    1 
ATOM   166   C  CG1   . ILE A 1 25  ? 7.959   15.212  -7.605  1.00 14.70 ?  25  ILE A CG1   1 
ATOM   167   C  CG2   . ILE A 1 25  ? 7.824   17.392  -8.893  1.00 15.37 ?  25  ILE A CG2   1 
ATOM   168   C  CD1   . ILE A 1 25  ? 6.574   14.714  -7.979  1.00 14.01 ?  25  ILE A CD1   1 
ATOM   169   N  N     . GLU A 1 26  ? 9.023   19.458  -6.297  1.00 21.12 ?  26  GLU A N     1 
ATOM   170   C  CA    . GLU A 1 26  ? 9.056   20.908  -6.391  1.00 23.63 ?  26  GLU A CA    1 
ATOM   171   C  C     . GLU A 1 26  ? 10.496  21.420  -6.383  1.00 24.14 ?  26  GLU A C     1 
ATOM   172   O  O     . GLU A 1 26  ? 10.849  22.281  -7.187  1.00 23.47 ?  26  GLU A O     1 
ATOM   173   C  CB    . GLU A 1 26  ? 8.260   21.509  -5.232  1.00 25.30 ?  26  GLU A CB    1 
ATOM   174   C  CG    . GLU A 1 26  ? 8.085   23.022  -5.329  1.00 29.50 ?  26  GLU A CG    1 
ATOM   175   C  CD    . GLU A 1 26  ? 7.229   23.599  -4.216  1.00 32.12 ?  26  GLU A CD    1 
ATOM   176   O  OE1   . GLU A 1 26  ? 6.144   23.034  -3.964  1.00 33.51 ?  26  GLU A OE1   1 
ATOM   177   O  OE2   . GLU A 1 26  ? 7.640   24.611  -3.610  1.00 34.80 -1 26  GLU A OE2   1 
ATOM   178   N  N     . HIS A 1 27  ? 11.320  20.888  -5.472  1.00 26.16 ?  27  HIS A N     1 
ATOM   179   C  CA    . HIS A 1 27  ? 12.636  21.450  -5.205  1.00 27.94 ?  27  HIS A CA    1 
ATOM   180   C  C     . HIS A 1 27  ? 13.719  20.780  -6.052  1.00 26.03 ?  27  HIS A C     1 
ATOM   181   O  O     . HIS A 1 27  ? 14.862  21.231  -6.054  1.00 26.69 ?  27  HIS A O     1 
ATOM   182   C  CB    . HIS A 1 27  ? 12.964  21.367  -3.708  1.00 34.51 ?  27  HIS A CB    1 
ATOM   183   C  CG    . HIS A 1 27  ? 12.323  22.435  -2.884  1.00 36.90 ?  27  HIS A CG    1 
ATOM   184   N  ND1   . HIS A 1 27  ? 11.156  22.257  -2.172  1.00 40.27 ?  27  HIS A ND1   1 
ATOM   185   C  CD2   . HIS A 1 27  ? 12.705  23.698  -2.657  1.00 35.71 ?  27  HIS A CD2   1 
ATOM   186   C  CE1   . HIS A 1 27  ? 10.852  23.384  -1.544  1.00 38.68 ?  27  HIS A CE1   1 
ATOM   187   N  NE2   . HIS A 1 27  ? 11.779  24.273  -1.825  1.00 36.45 ?  27  HIS A NE2   1 
ATOM   188   N  N     . ALA A 1 28  ? 13.353  19.716  -6.777  1.00 24.73 ?  28  ALA A N     1 
ATOM   189   C  CA    . ALA A 1 28  ? 14.310  18.923  -7.534  1.00 23.93 ?  28  ALA A CA    1 
ATOM   190   C  C     . ALA A 1 28  ? 14.970  19.752  -8.634  1.00 25.07 ?  28  ALA A C     1 
ATOM   191   O  O     . ALA A 1 28  ? 14.371  20.685  -9.167  1.00 24.53 ?  28  ALA A O     1 
ATOM   192   C  CB    . ALA A 1 28  ? 13.619  17.711  -8.119  1.00 23.64 ?  28  ALA A CB    1 
ATOM   193   N  N     . ASP A 1 29  ? 16.212  19.378  -8.967  1.00 25.03 ?  29  ASP A N     1 
ATOM   194   C  CA    . ASP A 1 29  ? 16.940  19.948  -10.091 1.00 28.33 ?  29  ASP A CA    1 
ATOM   195   C  C     . ASP A 1 29  ? 16.373  19.397  -11.395 1.00 24.62 ?  29  ASP A C     1 
ATOM   196   O  O     . ASP A 1 29  ? 16.325  20.097  -12.403 1.00 23.39 ?  29  ASP A O     1 
ATOM   197   C  CB    . ASP A 1 29  ? 18.425  19.622  -10.023 1.00 28.80 ?  29  ASP A CB    1 
ATOM   198   C  CG    . ASP A 1 29  ? 19.241  20.410  -9.008  1.00 30.50 ?  29  ASP A CG    1 
ATOM   199   O  OD1   . ASP A 1 29  ? 18.764  21.478  -8.571  1.00 29.35 ?  29  ASP A OD1   1 
ATOM   200   O  OD2   . ASP A 1 29  ? 20.344  19.941  -8.655  1.00 39.18 -1 29  ASP A OD2   1 
ATOM   201   N  N     . ILE A 1 30  ? 15.959  18.126  -11.358 1.00 26.42 ?  30  ILE A N     1 
ATOM   202   C  CA    . ILE A 1 30  ? 15.495  17.428  -12.545 1.00 23.33 ?  30  ILE A CA    1 
ATOM   203   C  C     . ILE A 1 30  ? 14.608  16.265  -12.113 1.00 22.18 ?  30  ILE A C     1 
ATOM   204   O  O     . ILE A 1 30  ? 14.899  15.593  -11.125 1.00 21.56 ?  30  ILE A O     1 
ATOM   205   C  CB    . ILE A 1 30  ? 16.686  16.955  -13.399 1.00 25.41 ?  30  ILE A CB    1 
ATOM   206   C  CG1   . ILE A 1 30  ? 16.238  16.450  -14.769 1.00 26.78 ?  30  ILE A CG1   1 
ATOM   207   C  CG2   . ILE A 1 30  ? 17.510  15.904  -12.653 1.00 27.58 ?  30  ILE A CG2   1 
ATOM   208   C  CD1   . ILE A 1 30  ? 17.379  16.216  -15.743 1.00 26.69 ?  30  ILE A CD1   1 
ATOM   209   N  N     . VAL A 1 31  ? 13.526  16.040  -12.868 1.00 19.52 ?  31  VAL A N     1 
ATOM   210   C  CA    . VAL A 1 31  ? 12.564  14.999  -12.547 1.00 19.45 ?  31  VAL A CA    1 
ATOM   211   C  C     . VAL A 1 31  ? 12.445  14.036  -13.726 1.00 20.10 ?  31  VAL A C     1 
ATOM   212   O  O     . VAL A 1 31  ? 12.291  14.461  -14.870 1.00 19.67 ?  31  VAL A O     1 
ATOM   213   C  CB    . VAL A 1 31  ? 11.191  15.599  -12.184 1.00 18.48 ?  31  VAL A CB    1 
ATOM   214   C  CG1   . VAL A 1 31  ? 10.182  14.522  -11.804 1.00 17.31 ?  31  VAL A CG1   1 
ATOM   215   C  CG2   . VAL A 1 31  ? 11.304  16.640  -11.078 1.00 18.65 ?  31  VAL A CG2   1 
ATOM   216   N  N     . PHE A 1 32  ? 12.519  12.736  -13.418 1.00 19.47 ?  32  PHE A N     1 
ATOM   217   C  CA    . PHE A 1 32  ? 12.285  11.674  -14.385 1.00 19.05 ?  32  PHE A CA    1 
ATOM   218   C  C     . PHE A 1 32  ? 10.952  11.006  -14.059 1.00 18.00 ?  32  PHE A C     1 
ATOM   219   O  O     . PHE A 1 32  ? 10.800  10.400  -13.000 1.00 19.04 ?  32  PHE A O     1 
ATOM   220   C  CB    . PHE A 1 32  ? 13.454  10.686  -14.360 1.00 21.14 ?  32  PHE A CB    1 
ATOM   221   C  CG    . PHE A 1 32  ? 14.759  11.274  -14.881 1.00 23.86 ?  32  PHE A CG    1 
ATOM   222   C  CD1   . PHE A 1 32  ? 15.611  11.978  -14.038 1.00 24.10 ?  32  PHE A CD1   1 
ATOM   223   C  CD2   . PHE A 1 32  ? 15.121  11.132  -16.216 1.00 24.64 ?  32  PHE A CD2   1 
ATOM   224   C  CE1   . PHE A 1 32  ? 16.792  12.521  -14.518 1.00 26.29 ?  32  PHE A CE1   1 
ATOM   225   C  CE2   . PHE A 1 32  ? 16.306  11.675  -16.689 1.00 25.86 ?  32  PHE A CE2   1 
ATOM   226   C  CZ    . PHE A 1 32  ? 17.138  12.368  -15.840 1.00 26.17 ?  32  PHE A CZ    1 
ATOM   227   N  N     . SER A 1 33  ? 9.998   11.117  -14.990 1.00 15.45 ?  33  SER A N     1 
ATOM   228   C  CA    . SER A 1 33  ? 8.608   10.790  -14.719 1.00 14.32 ?  33  SER A CA    1 
ATOM   229   C  C     . SER A 1 33  ? 8.191   9.505   -15.430 1.00 15.28 ?  33  SER A C     1 
ATOM   230   O  O     . SER A 1 33  ? 8.679   9.199   -16.516 1.00 15.60 ?  33  SER A O     1 
ATOM   231   C  CB    . SER A 1 33  ? 7.709   11.929  -15.126 1.00 13.87 ?  33  SER A CB    1 
ATOM   232   O  OG    . SER A 1 33  ? 7.689   12.079  -16.539 1.00 12.69 ?  33  SER A OG    1 
ATOM   233   N  N     . LEU A 1 34  ? 7.271   8.772   -14.792 1.00 17.75 ?  34  LEU A N     1 
ATOM   234   C  CA    . LEU A 1 34  ? 6.525   7.705   -15.437 1.00 19.71 ?  34  LEU A CA    1 
ATOM   235   C  C     . LEU A 1 34  ? 5.091   7.742   -14.906 1.00 20.27 ?  34  LEU A C     1 
ATOM   236   O  O     . LEU A 1 34  ? 4.795   7.178   -13.854 1.00 19.99 ?  34  LEU A O     1 
ATOM   237   C  CB    . LEU A 1 34  ? 7.200   6.357   -15.188 1.00 19.58 ?  34  LEU A CB    1 
ATOM   238   C  CG    . LEU A 1 34  ? 6.883   5.255   -16.206 1.00 19.91 ?  34  LEU A CG    1 
ATOM   239   C  CD1   . LEU A 1 34  ? 7.432   5.619   -17.575 1.00 21.43 ?  34  LEU A CD1   1 
ATOM   240   C  CD2   . LEU A 1 34  ? 7.423   3.909   -15.762 1.00 20.52 ?  34  LEU A CD2   1 
ATOM   241   N  N     . LEU A 1 35  ? 4.214   8.422   -15.654 1.00 22.66 ?  35  LEU A N     1 
ATOM   242   C  CA    . LEU A 1 35  ? 2.892   8.808   -15.183 1.00 22.96 ?  35  LEU A CA    1 
ATOM   243   C  C     . LEU A 1 35  ? 1.820   8.223   -16.100 1.00 21.60 ?  35  LEU A C     1 
ATOM   244   O  O     . LEU A 1 35  ? 2.088   7.957   -17.269 1.00 22.42 ?  35  LEU A O     1 
ATOM   245   C  CB    . LEU A 1 35  ? 2.848   10.336  -15.167 1.00 24.32 ?  35  LEU A CB    1 
ATOM   246   C  CG    . LEU A 1 35  ? 3.373   11.039  -13.910 1.00 26.03 ?  35  LEU A CG    1 
ATOM   247   C  CD1   . LEU A 1 35  ? 4.587   10.381  -13.277 1.00 25.31 ?  35  LEU A CD1   1 
ATOM   248   C  CD2   . LEU A 1 35  ? 3.694   12.476  -14.279 1.00 27.44 ?  35  LEU A CD2   1 
ATOM   249   N  N     . PRO A 1 36  ? 0.572   8.016   -15.616 1.00 20.87 ?  36  PRO A N     1 
ATOM   250   C  CA    . PRO A 1 36  ? -0.453  7.327   -16.406 1.00 21.82 ?  36  PRO A CA    1 
ATOM   251   C  C     . PRO A 1 36  ? -0.899  7.998   -17.705 1.00 22.43 ?  36  PRO A C     1 
ATOM   252   O  O     . PRO A 1 36  ? -1.303  7.306   -18.637 1.00 23.22 ?  36  PRO A O     1 
ATOM   253   C  CB    . PRO A 1 36  ? -1.628  7.207   -15.410 1.00 21.32 ?  36  PRO A CB    1 
ATOM   254   C  CG    . PRO A 1 36  ? -0.985  7.342   -14.050 1.00 20.48 ?  36  PRO A CG    1 
ATOM   255   C  CD    . PRO A 1 36  ? 0.095   8.383   -14.273 1.00 20.26 ?  36  PRO A CD    1 
ATOM   256   N  N     . ASP A 1 37  ? -0.838  9.335   -17.772 1.00 23.53 ?  37  ASP A N     1 
ATOM   257   C  CA    . ASP A 1 37  ? -1.497  10.048  -18.855 1.00 25.05 ?  37  ASP A CA    1 
ATOM   258   C  C     . ASP A 1 37  ? -0.981  11.479  -18.985 1.00 25.04 ?  37  ASP A C     1 
ATOM   259   O  O     . ASP A 1 37  ? -0.059  11.889  -18.283 1.00 26.92 ?  37  ASP A O     1 
ATOM   260   C  CB    . ASP A 1 37  ? -3.003  10.050  -18.648 1.00 24.75 ?  37  ASP A CB    1 
ATOM   261   C  CG    . ASP A 1 37  ? -3.460  10.584  -17.299 1.00 24.54 ?  37  ASP A CG    1 
ATOM   262   O  OD1   . ASP A 1 37  ? -3.193  11.771  -17.017 1.00 22.50 ?  37  ASP A OD1   1 
ATOM   263   O  OD2   . ASP A 1 37  ? -4.066  9.802   -16.536 1.00 23.54 -1 37  ASP A OD2   1 
ATOM   264   N  N     . GLY A 1 38  ? -1.616  12.228  -19.897 1.00 22.25 ?  38  GLY A N     1 
ATOM   265   C  CA    . GLY A 1 38  ? -1.206  13.577  -20.251 1.00 20.68 ?  38  GLY A CA    1 
ATOM   266   C  C     . GLY A 1 38  ? -1.646  14.616  -19.221 1.00 19.68 ?  38  GLY A C     1 
ATOM   267   O  O     . GLY A 1 38  ? -1.050  15.687  -19.134 1.00 24.32 ?  38  GLY A O     1 
ATOM   268   N  N     . PHE A 1 39  ? -2.698  14.305  -18.455 1.00 19.45 ?  39  PHE A N     1 
ATOM   269   C  CA    . PHE A 1 39  ? -3.155  15.191  -17.396 1.00 20.42 ?  39  PHE A CA    1 
ATOM   270   C  C     . PHE A 1 39  ? -2.140  15.159  -16.258 1.00 21.86 ?  39  PHE A C     1 
ATOM   271   O  O     . PHE A 1 39  ? -1.728  16.201  -15.752 1.00 20.80 ?  39  PHE A O     1 
ATOM   272   C  CB    . PHE A 1 39  ? -4.553  14.803  -16.902 1.00 20.11 ?  39  PHE A CB    1 
ATOM   273   C  CG    . PHE A 1 39  ? -5.646  14.954  -17.950 1.00 20.65 ?  39  PHE A CG    1 
ATOM   274   C  CD1   . PHE A 1 39  ? -6.061  16.214  -18.366 1.00 19.77 ?  39  PHE A CD1   1 
ATOM   275   C  CD2   . PHE A 1 39  ? -6.263  13.840  -18.509 1.00 21.47 ?  39  PHE A CD2   1 
ATOM   276   C  CE1   . PHE A 1 39  ? -7.054  16.353  -19.322 1.00 19.40 ?  39  PHE A CE1   1 
ATOM   277   C  CE2   . PHE A 1 39  ? -7.258  13.986  -19.462 1.00 19.40 ?  39  PHE A CE2   1 
ATOM   278   C  CZ    . PHE A 1 39  ? -7.651  15.241  -19.866 1.00 19.12 ?  39  PHE A CZ    1 
ATOM   279   N  N     . SER A 1 40  ? -1.746  13.942  -15.872 1.00 22.18 ?  40  SER A N     1 
ATOM   280   C  CA    . SER A 1 40  ? -0.774  13.732  -14.813 1.00 21.29 ?  40  SER A CA    1 
ATOM   281   C  C     . SER A 1 40  ? 0.581   14.303  -15.222 1.00 21.77 ?  40  SER A C     1 
ATOM   282   O  O     . SER A 1 40  ? 1.387   14.665  -14.369 1.00 22.95 ?  40  SER A O     1 
ATOM   283   C  CB    . SER A 1 40  ? -0.667  12.268  -14.469 1.00 23.67 ?  40  SER A CB    1 
ATOM   284   O  OG    . SER A 1 40  ? 0.433   12.024  -13.604 1.00 27.67 ?  40  SER A OG    1 
ATOM   285   N  N     . GLN A 1 41  ? 0.817   14.381  -16.537 1.00 21.14 ?  41  GLN A N     1 
ATOM   286   C  CA    . GLN A 1 41  ? 2.089   14.840  -17.071 1.00 20.36 ?  41  GLN A CA    1 
ATOM   287   C  C     . GLN A 1 41  ? 2.128   16.367  -17.083 1.00 20.41 ?  41  GLN A C     1 
ATOM   288   O  O     . GLN A 1 41  ? 3.198   16.960  -16.964 1.00 19.19 ?  41  GLN A O     1 
ATOM   289   C  CB    . GLN A 1 41  ? 2.309   14.286  -18.479 1.00 20.91 ?  41  GLN A CB    1 
ATOM   290   C  CG    . GLN A 1 41  ? 3.762   14.321  -18.944 1.00 19.58 ?  41  GLN A CG    1 
ATOM   291   C  CD    . GLN A 1 41  ? 4.670   13.453  -18.099 1.00 20.48 ?  41  GLN A CD    1 
ATOM   292   O  OE1   . GLN A 1 41  ? 4.281   12.372  -17.643 1.00 25.55 ?  41  GLN A OE1   1 
ATOM   293   N  NE2   . GLN A 1 41  ? 5.886   13.925  -17.867 1.00 18.49 ?  41  GLN A NE2   1 
ATOM   294   N  N     . ARG A 1 42  ? 0.956   16.995  -17.240 1.00 22.76 ?  42  ARG A N     1 
ATOM   295   C  CA    . ARG A 1 42  ? 0.849   18.447  -17.233 1.00 21.84 ?  42  ARG A CA    1 
ATOM   296   C  C     . ARG A 1 42  ? 0.999   18.974  -15.810 1.00 19.42 ?  42  ARG A C     1 
ATOM   297   O  O     . ARG A 1 42  ? 1.691   19.962  -15.578 1.00 19.71 ?  42  ARG A O     1 
ATOM   298   C  CB    . ARG A 1 42  ? -0.501  18.934  -17.771 1.00 25.45 ?  42  ARG A CB    1 
ATOM   299   C  CG    . ARG A 1 42  ? -0.604  18.997  -19.287 1.00 28.91 ?  42  ARG A CG    1 
ATOM   300   C  CD    . ARG A 1 42  ? -2.013  19.374  -19.709 1.00 30.48 ?  42  ARG A CD    1 
ATOM   301   N  NE    . ARG A 1 42  ? -2.187  19.346  -21.164 1.00 30.47 ?  42  ARG A NE    1 
ATOM   302   C  CZ    . ARG A 1 42  ? -2.877  18.426  -21.829 1.00 34.97 ?  42  ARG A CZ    1 
ATOM   303   N  NH1   . ARG A 1 42  ? -3.372  17.376  -21.198 1.00 32.03 1  42  ARG A NH1   1 
ATOM   304   N  NH2   . ARG A 1 42  ? -3.045  18.549  -23.134 1.00 35.51 ?  42  ARG A NH2   1 
ATOM   305   N  N     . TRP A 1 43  ? 0.307   18.321  -14.872 1.00 19.11 ?  43  TRP A N     1 
ATOM   306   C  CA    . TRP A 1 43  ? 0.417   18.649  -13.461 1.00 19.19 ?  43  TRP A CA    1 
ATOM   307   C  C     . TRP A 1 43  ? 1.882   18.618  -13.026 1.00 19.80 ?  43  TRP A C     1 
ATOM   308   O  O     . TRP A 1 43  ? 2.354   19.547  -12.375 1.00 17.35 ?  43  TRP A O     1 
ATOM   309   C  CB    . TRP A 1 43  ? -0.445  17.688  -12.629 1.00 20.43 ?  43  TRP A CB    1 
ATOM   310   C  CG    . TRP A 1 43  ? -0.082  17.617  -11.169 1.00 21.98 ?  43  TRP A CG    1 
ATOM   311   C  CD1   . TRP A 1 43  ? -0.500  18.446  -10.170 1.00 24.97 ?  43  TRP A CD1   1 
ATOM   312   C  CD2   . TRP A 1 43  ? 0.763   16.628  -10.540 1.00 24.49 ?  43  TRP A CD2   1 
ATOM   313   N  NE1   . TRP A 1 43  ? 0.034   18.055  -8.971  1.00 24.41 ?  43  TRP A NE1   1 
ATOM   314   C  CE2   . TRP A 1 43  ? 0.809   16.942  -9.164  1.00 25.34 ?  43  TRP A CE2   1 
ATOM   315   C  CE3   . TRP A 1 43  ? 1.482   15.520  -11.003 1.00 25.81 ?  43  TRP A CE3   1 
ATOM   316   C  CZ2   . TRP A 1 43  ? 1.544   16.185  -8.255  1.00 26.72 ?  43  TRP A CZ2   1 
ATOM   317   C  CZ3   . TRP A 1 43  ? 2.206   14.772  -10.101 1.00 27.78 ?  43  TRP A CZ3   1 
ATOM   318   C  CH2   . TRP A 1 43  ? 2.234   15.101  -8.746  1.00 28.38 ?  43  TRP A CH2   1 
ATOM   319   N  N     . LEU A 1 44  ? 2.604   17.554  -13.397 1.00 22.19 ?  44  LEU A N     1 
ATOM   320   C  CA    . LEU A 1 44  ? 3.988   17.408  -12.974 1.00 22.47 ?  44  LEU A CA    1 
ATOM   321   C  C     . LEU A 1 44  ? 4.806   18.581  -13.505 1.00 22.97 ?  44  LEU A C     1 
ATOM   322   O  O     . LEU A 1 44  ? 5.615   19.160  -12.782 1.00 18.93 ?  44  LEU A O     1 
ATOM   323   C  CB    . LEU A 1 44  ? 4.595   16.084  -13.436 1.00 22.94 ?  44  LEU A CB    1 
ATOM   324   C  CG    . LEU A 1 44  ? 6.075   15.889  -13.086 1.00 19.98 ?  44  LEU A CG    1 
ATOM   325   C  CD1   . LEU A 1 44  ? 6.293   16.039  -11.590 1.00 20.63 ?  44  LEU A CD1   1 
ATOM   326   C  CD2   . LEU A 1 44  ? 6.591   14.544  -13.563 1.00 18.79 ?  44  LEU A CD2   1 
ATOM   327   N  N     . THR A 1 45  ? 4.584   18.908  -14.782 1.00 23.00 ?  45  THR A N     1 
ATOM   328   C  CA    . THR A 1 45  ? 5.385   19.893  -15.490 1.00 24.83 ?  45  THR A CA    1 
ATOM   329   C  C     . THR A 1 45  ? 5.170   21.276  -14.881 1.00 27.37 ?  45  THR A C     1 
ATOM   330   O  O     . THR A 1 45  ? 6.084   22.097  -14.874 1.00 26.61 ?  45  THR A O     1 
ATOM   331   C  CB    . THR A 1 45  ? 5.028   19.867  -16.975 1.00 26.11 ?  45  THR A CB    1 
ATOM   332   O  OG1   . THR A 1 45  ? 5.514   18.618  -17.457 1.00 25.38 ?  45  THR A OG1   1 
ATOM   333   C  CG2   . THR A 1 45  ? 5.675   20.997  -17.754 1.00 26.89 ?  45  THR A CG2   1 
ATOM   334   N  N     . LYS A 1 46  ? 3.953   21.530  -14.387 1.00 30.89 ?  46  LYS A N     1 
ATOM   335   C  CA    . LYS A 1 46  ? 3.657   22.772  -13.691 1.00 32.02 ?  46  LYS A CA    1 
ATOM   336   C  C     . LYS A 1 46  ? 4.373   22.783  -12.345 1.00 28.59 ?  46  LYS A C     1 
ATOM   337   O  O     . LYS A 1 46  ? 4.791   23.834  -11.867 1.00 25.12 ?  46  LYS A O     1 
ATOM   338   C  CB    . LYS A 1 46  ? 2.155   22.969  -13.454 1.00 39.11 ?  46  LYS A CB    1 
ATOM   339   C  CG    . LYS A 1 46  ? 1.383   23.621  -14.591 1.00 41.74 ?  46  LYS A CG    1 
ATOM   340   C  CD    . LYS A 1 46  ? 0.018   24.129  -14.142 1.00 46.67 ?  46  LYS A CD    1 
ATOM   341   C  CE    . LYS A 1 46  ? -0.465  25.302  -14.933 1.00 50.43 ?  46  LYS A CE    1 
ATOM   342   N  NZ    . LYS A 1 46  ? -1.560  25.985  -14.239 1.00 54.36 1  46  LYS A NZ    1 
ATOM   343   N  N     . LEU A 1 47  ? 4.502   21.601  -11.738 1.00 25.76 ?  47  LEU A N     1 
ATOM   344   C  CA    . LEU A 1 47  ? 5.112   21.487  -10.426 1.00 24.39 ?  47  LEU A CA    1 
ATOM   345   C  C     . LEU A 1 47  ? 6.613   21.748  -10.551 1.00 23.22 ?  47  LEU A C     1 
ATOM   346   O  O     . LEU A 1 47  ? 7.195   22.455  -9.732  1.00 23.96 ?  47  LEU A O     1 
ATOM   347   C  CB    . LEU A 1 47  ? 4.800   20.102  -9.865  1.00 26.46 ?  47  LEU A CB    1 
ATOM   348   C  CG    . LEU A 1 47  ? 4.436   20.045  -8.378  1.00 27.30 ?  47  LEU A CG    1 
ATOM   349   C  CD1   . LEU A 1 47  ? 4.251   18.596  -7.969  1.00 28.17 ?  47  LEU A CD1   1 
ATOM   350   C  CD2   . LEU A 1 47  ? 5.464   20.737  -7.501  1.00 25.59 ?  47  LEU A CD2   1 
ATOM   351   N  N     . ASN A 1 48  ? 7.224   21.183  -11.600 1.00 21.90 ?  48  ASN A N     1 
ATOM   352   C  CA    . ASN A 1 48  ? 8.627   21.413  -11.911 1.00 20.79 ?  48  ASN A CA    1 
ATOM   353   C  C     . ASN A 1 48  ? 8.808   21.283  -13.422 1.00 20.89 ?  48  ASN A C     1 
ATOM   354   O  O     . ASN A 1 48  ? 8.468   20.252  -13.998 1.00 21.22 ?  48  ASN A O     1 
ATOM   355   C  CB    . ASN A 1 48  ? 9.530   20.455  -11.138 1.00 21.71 ?  48  ASN A CB    1 
ATOM   356   C  CG    . ASN A 1 48  ? 11.000  20.774  -11.293 1.00 22.07 ?  48  ASN A CG    1 
ATOM   357   O  OD1   . ASN A 1 48  ? 11.436  21.211  -12.364 1.00 20.95 ?  48  ASN A OD1   1 
ATOM   358   N  ND2   . ASN A 1 48  ? 11.777  20.574  -10.238 1.00 22.85 ?  48  ASN A ND2   1 
ATOM   359   N  N     . PRO A 1 49  ? 9.328   22.317  -14.123 1.00 24.78 ?  49  PRO A N     1 
ATOM   360   C  CA    . PRO A 1 49  ? 9.438   22.266  -15.583 1.00 26.74 ?  49  PRO A CA    1 
ATOM   361   C  C     . PRO A 1 49  ? 10.591  21.436  -16.148 1.00 29.61 ?  49  PRO A C     1 
ATOM   362   O  O     . PRO A 1 49  ? 10.589  21.109  -17.332 1.00 27.45 ?  49  PRO A O     1 
ATOM   363   C  CB    . PRO A 1 49  ? 9.590   23.753  -15.923 1.00 26.62 ?  49  PRO A CB    1 
ATOM   364   C  CG    . PRO A 1 49  ? 10.392  24.298  -14.766 1.00 25.75 ?  49  PRO A CG    1 
ATOM   365   C  CD    . PRO A 1 49  ? 9.800   23.592  -13.556 1.00 24.66 ?  49  PRO A CD    1 
ATOM   366   N  N     . ASN A 1 50  ? 11.572  21.097  -15.305 1.00 32.25 ?  50  ASN A N     1 
ATOM   367   C  CA    . ASN A 1 50  ? 12.732  20.357  -15.777 1.00 31.55 ?  50  ASN A CA    1 
ATOM   368   C  C     . ASN A 1 50  ? 12.475  18.860  -15.613 1.00 27.87 ?  50  ASN A C     1 
ATOM   369   O  O     . ASN A 1 50  ? 13.061  18.215  -14.748 1.00 22.02 ?  50  ASN A O     1 
ATOM   370   C  CB    . ASN A 1 50  ? 14.014  20.796  -15.081 1.00 36.93 ?  50  ASN A CB    1 
ATOM   371   C  CG    . ASN A 1 50  ? 15.239  20.334  -15.834 1.00 38.52 ?  50  ASN A CG    1 
ATOM   372   O  OD1   . ASN A 1 50  ? 15.120  19.785  -16.935 1.00 43.43 ?  50  ASN A OD1   1 
ATOM   373   N  ND2   . ASN A 1 50  ? 16.419  20.555  -15.273 1.00 39.70 ?  50  ASN A ND2   1 
ATOM   374   N  N     . VAL A 1 51  ? 11.599  18.330  -16.474 1.00 26.24 ?  51  VAL A N     1 
ATOM   375   C  CA    . VAL A 1 51  ? 11.158  16.946  -16.410 1.00 26.21 ?  51  VAL A CA    1 
ATOM   376   C  C     . VAL A 1 51  ? 11.690  16.198  -17.629 1.00 28.07 ?  51  VAL A C     1 
ATOM   377   O  O     . VAL A 1 51  ? 11.721  16.745  -18.729 1.00 28.69 ?  51  VAL A O     1 
ATOM   378   C  CB    . VAL A 1 51  ? 9.619   16.866  -16.361 1.00 26.81 ?  51  VAL A CB    1 
ATOM   379   C  CG1   . VAL A 1 51  ? 9.112   15.446  -16.588 1.00 26.32 ?  51  VAL A CG1   1 
ATOM   380   C  CG2   . VAL A 1 51  ? 9.048   17.443  -15.071 1.00 26.72 ?  51  VAL A CG2   1 
ATOM   381   N  N     . ILE A 1 52  ? 12.100  14.943  -17.420 1.00 28.27 ?  52  ILE A N     1 
ATOM   382   C  CA    . ILE A 1 52  ? 12.378  14.034  -18.519 1.00 27.64 ?  52  ILE A CA    1 
ATOM   383   C  C     . ILE A 1 52  ? 11.440  12.837  -18.392 1.00 22.84 ?  52  ILE A C     1 
ATOM   384   O  O     . ILE A 1 52  ? 11.342  12.225  -17.331 1.00 21.13 ?  52  ILE A O     1 
ATOM   385   C  CB    . ILE A 1 52  ? 13.865  13.632  -18.554 1.00 32.07 ?  52  ILE A CB    1 
ATOM   386   C  CG1   . ILE A 1 52  ? 14.742  14.828  -18.939 1.00 32.62 ?  52  ILE A CG1   1 
ATOM   387   C  CG2   . ILE A 1 52  ? 14.094  12.440  -19.486 1.00 31.76 ?  52  ILE A CG2   1 
ATOM   388   C  CD1   . ILE A 1 52  ? 16.232  14.539  -18.954 1.00 36.13 ?  52  ILE A CD1   1 
ATOM   389   N  N     . ASN A 1 53  ? 10.733  12.541  -19.489 1.00 19.41 ?  53  ASN A N     1 
ATOM   390   C  CA    . ASN A 1 53  ? 9.671   11.549  -19.497 1.00 18.77 ?  53  ASN A CA    1 
ATOM   391   C  C     . ASN A 1 53  ? 10.256  10.195  -19.891 1.00 18.05 ?  53  ASN A C     1 
ATOM   392   O  O     . ASN A 1 53  ? 10.716  10.015  -21.016 1.00 15.41 ?  53  ASN A O     1 
ATOM   393   C  CB    . ASN A 1 53  ? 8.533   11.984  -20.415 1.00 18.39 ?  53  ASN A CB    1 
ATOM   394   C  CG    . ASN A 1 53  ? 7.342   11.058  -20.344 1.00 18.90 ?  53  ASN A CG    1 
ATOM   395   O  OD1   . ASN A 1 53  ? 7.418   9.987   -19.731 1.00 19.36 ?  53  ASN A OD1   1 
ATOM   396   N  ND2   . ASN A 1 53  ? 6.239   11.447  -20.967 1.00 18.57 ?  53  ASN A ND2   1 
ATOM   397   N  N     . LEU A 1 54  ? 10.225  9.251   -18.943 1.00 19.15 ?  54  LEU A N     1 
ATOM   398   C  CA    . LEU A 1 54  ? 10.810  7.932   -19.130 1.00 17.99 ?  54  LEU A CA    1 
ATOM   399   C  C     . LEU A 1 54  ? 10.004  7.127   -20.147 1.00 22.37 ?  54  LEU A C     1 
ATOM   400   O  O     . LEU A 1 54  ? 10.500  6.142   -20.691 1.00 22.96 ?  54  LEU A O     1 
ATOM   401   C  CB    . LEU A 1 54  ? 10.871  7.211   -17.784 1.00 18.00 ?  54  LEU A CB    1 
ATOM   402   C  CG    . LEU A 1 54  ? 11.820  7.814   -16.744 1.00 17.39 ?  54  LEU A CG    1 
ATOM   403   C  CD1   . LEU A 1 54  ? 11.647  7.166   -15.380 1.00 17.39 ?  54  LEU A CD1   1 
ATOM   404   C  CD2   . LEU A 1 54  ? 13.254  7.689   -17.224 1.00 15.79 ?  54  LEU A CD2   1 
ATOM   405   N  N     . GLN A 1 55  ? 8.757   7.541   -20.393 1.00 23.91 ?  55  GLN A N     1 
ATOM   406   C  CA    . GLN A 1 55  ? 7.878   6.802   -21.284 1.00 26.69 ?  55  GLN A CA    1 
ATOM   407   C  C     . GLN A 1 55  ? 8.583   6.581   -22.623 1.00 27.90 ?  55  GLN A C     1 
ATOM   408   O  O     . GLN A 1 55  ? 8.366   5.566   -23.281 1.00 29.20 ?  55  GLN A O     1 
ATOM   409   C  CB    . GLN A 1 55  ? 6.551   7.544   -21.456 1.00 26.92 ?  55  GLN A CB    1 
ATOM   410   C  CG    . GLN A 1 55  ? 5.376   6.660   -21.866 1.00 28.70 ?  55  GLN A CG    1 
ATOM   411   C  CD    . GLN A 1 55  ? 4.721   5.945   -20.703 1.00 29.04 ?  55  GLN A CD    1 
ATOM   412   O  OE1   . GLN A 1 55  ? 4.528   6.511   -19.621 1.00 29.69 ?  55  GLN A OE1   1 
ATOM   413   N  NE2   . GLN A 1 55  ? 4.368   4.686   -20.917 1.00 29.77 ?  55  GLN A NE2   1 
ATOM   414   N  N     . GLN A 1 56  ? 9.439   7.534   -23.012 1.00 25.90 ?  56  GLN A N     1 
ATOM   415   C  CA    . GLN A 1 56  ? 10.114  7.487   -24.301 1.00 28.81 ?  56  GLN A CA    1 
ATOM   416   C  C     . GLN A 1 56  ? 10.911  6.193   -24.464 1.00 31.70 ?  56  GLN A C     1 
ATOM   417   O  O     . GLN A 1 56  ? 11.159  5.768   -25.591 1.00 25.67 ?  56  GLN A O     1 
ATOM   418   C  CB    . GLN A 1 56  ? 11.084  8.654   -24.479 1.00 29.51 ?  56  GLN A CB    1 
ATOM   419   C  CG    . GLN A 1 56  ? 12.138  8.746   -23.381 1.00 31.57 ?  56  GLN A CG    1 
ATOM   420   C  CD    . GLN A 1 56  ? 13.413  9.421   -23.836 1.00 34.56 ?  56  GLN A CD    1 
ATOM   421   O  OE1   . GLN A 1 56  ? 13.739  10.537  -23.417 1.00 34.09 ?  56  GLN A OE1   1 
ATOM   422   N  NE2   . GLN A 1 56  ? 14.149  8.743   -24.705 1.00 39.46 ?  56  GLN A NE2   1 
ATOM   423   N  N     . PHE A 1 57  ? 11.325  5.580   -23.348 1.00 32.48 ?  57  PHE A N     1 
ATOM   424   C  CA    . PHE A 1 57  ? 12.237  4.445   -23.401 1.00 35.46 ?  57  PHE A CA    1 
ATOM   425   C  C     . PHE A 1 57  ? 11.469  3.150   -23.660 1.00 32.62 ?  57  PHE A C     1 
ATOM   426   O  O     . PHE A 1 57  ? 12.083  2.100   -23.834 1.00 29.38 ?  57  PHE A O     1 
ATOM   427   C  CB    . PHE A 1 57  ? 13.095  4.370   -22.133 1.00 35.51 ?  57  PHE A CB    1 
ATOM   428   C  CG    . PHE A 1 57  ? 14.126  5.488   -22.057 1.00 36.52 ?  57  PHE A CG    1 
ATOM   429   C  CD1   . PHE A 1 57  ? 15.288  5.437   -22.819 1.00 36.77 ?  57  PHE A CD1   1 
ATOM   430   C  CD2   . PHE A 1 57  ? 13.920  6.596   -21.244 1.00 39.14 ?  57  PHE A CD2   1 
ATOM   431   C  CE1   . PHE A 1 57  ? 16.218  6.463   -22.762 1.00 34.88 ?  57  PHE A CE1   1 
ATOM   432   C  CE2   . PHE A 1 57  ? 14.855  7.618   -21.189 1.00 38.32 ?  57  PHE A CE2   1 
ATOM   433   C  CZ    . PHE A 1 57  ? 16.001  7.550   -21.948 1.00 37.41 ?  57  PHE A CZ    1 
ATOM   434   N  N     . TYR A 1 58  ? 10.133  3.217   -23.691 1.00 33.57 ?  58  TYR A N     1 
ATOM   435   C  CA    . TYR A 1 58  ? 9.345   2.055   -24.070 1.00 34.13 ?  58  TYR A CA    1 
ATOM   436   C  C     . TYR A 1 58  ? 9.406   1.902   -25.587 1.00 35.43 ?  58  TYR A C     1 
ATOM   437   O  O     . TYR A 1 58  ? 9.581   2.880   -26.312 1.00 31.52 ?  58  TYR A O     1 
ATOM   438   C  CB    . TYR A 1 58  ? 7.880   2.104   -23.621 1.00 35.15 ?  58  TYR A CB    1 
ATOM   439   C  CG    . TYR A 1 58  ? 7.644   1.822   -22.143 1.00 37.70 ?  58  TYR A CG    1 
ATOM   440   C  CD1   . TYR A 1 58  ? 7.583   0.520   -21.658 1.00 36.12 ?  58  TYR A CD1   1 
ATOM   441   C  CD2   . TYR A 1 58  ? 7.463   2.859   -21.237 1.00 39.09 ?  58  TYR A CD2   1 
ATOM   442   C  CE1   . TYR A 1 58  ? 7.362   0.260   -20.315 1.00 37.05 ?  58  TYR A CE1   1 
ATOM   443   C  CE2   . TYR A 1 58  ? 7.241   2.612   -19.893 1.00 39.33 ?  58  TYR A CE2   1 
ATOM   444   C  CZ    . TYR A 1 58  ? 7.190   1.309   -19.430 1.00 38.20 ?  58  TYR A CZ    1 
ATOM   445   O  OH    . TYR A 1 58  ? 6.972   1.066   -18.105 1.00 42.89 ?  58  TYR A OH    1 
ATOM   446   N  N     . ALA A 1 59  ? 9.262   0.654   -26.045 1.00 34.22 ?  59  ALA A N     1 
ATOM   447   C  CA    . ALA A 1 59  ? 9.254   0.340   -27.463 1.00 36.02 ?  59  ALA A CA    1 
ATOM   448   C  C     . ALA A 1 59  ? 8.346   1.319   -28.202 1.00 34.31 ?  59  ALA A C     1 
ATOM   449   O  O     . ALA A 1 59  ? 7.185   1.494   -27.839 1.00 31.46 ?  59  ALA A O     1 
ATOM   450   C  CB    . ALA A 1 59  ? 8.811   -1.092  -27.668 1.00 37.73 ?  59  ALA A CB    1 
ATOM   451   N  N     . GLN A 1 60  ? 8.895   1.950   -29.243 1.00 35.44 ?  60  GLN A N     1 
ATOM   452   C  CA    . GLN A 1 60  ? 8.161   2.915   -30.044 1.00 41.33 ?  60  GLN A CA    1 
ATOM   453   C  C     . GLN A 1 60  ? 7.882   2.325   -31.424 1.00 46.70 ?  60  GLN A C     1 
ATOM   454   O  O     . GLN A 1 60  ? 8.736   1.658   -32.003 1.00 45.95 ?  60  GLN A O     1 
ATOM   455   C  CB    . GLN A 1 60  ? 8.978   4.202   -30.158 1.00 42.60 ?  60  GLN A CB    1 
ATOM   456   C  CG    . GLN A 1 60  ? 9.311   4.853   -28.819 1.00 44.05 ?  60  GLN A CG    1 
ATOM   457   C  CD    . GLN A 1 60  ? 8.137   5.583   -28.202 1.00 39.16 ?  60  GLN A CD    1 
ATOM   458   O  OE1   . GLN A 1 60  ? 7.619   6.557   -28.759 1.00 36.04 ?  60  GLN A OE1   1 
ATOM   459   N  NE2   . GLN A 1 60  ? 7.707   5.120   -27.038 1.00 38.29 ?  60  GLN A NE2   1 
ATOM   460   N  N     . ASN A 1 61  ? 6.674   2.583   -31.938 1.00 54.12 ?  61  ASN A N     1 
ATOM   461   C  CA    . ASN A 1 61  ? 6.292   2.194   -33.287 1.00 55.84 ?  61  ASN A CA    1 
ATOM   462   C  C     . ASN A 1 61  ? 6.423   0.683   -33.469 1.00 53.05 ?  61  ASN A C     1 
ATOM   463   O  O     . ASN A 1 61  ? 7.022   0.224   -34.439 1.00 59.13 ?  61  ASN A O     1 
ATOM   464   C  CB    . ASN A 1 61  ? 7.109   2.934   -34.340 1.00 59.39 ?  61  ASN A CB    1 
ATOM   465   C  CG    . ASN A 1 61  ? 7.049   4.433   -34.168 1.00 60.62 ?  61  ASN A CG    1 
ATOM   466   O  OD1   . ASN A 1 61  ? 5.958   5.014   -34.144 1.00 67.51 ?  61  ASN A OD1   1 
ATOM   467   N  ND2   . ASN A 1 61  ? 8.202   5.074   -34.047 1.00 60.11 ?  61  ASN A ND2   1 
ATOM   468   N  N     . GLY A 1 62  ? 5.854   -0.079  -32.529 1.00 49.07 ?  62  GLY A N     1 
ATOM   469   C  CA    . GLY A 1 62  ? 5.662   -1.511  -32.699 1.00 50.30 ?  62  GLY A CA    1 
ATOM   470   C  C     . GLY A 1 62  ? 6.974   -2.256  -32.934 1.00 45.54 ?  62  GLY A C     1 
ATOM   471   O  O     . GLY A 1 62  ? 7.002   -3.248  -33.660 1.00 41.07 ?  62  GLY A O     1 
ATOM   472   N  N     . GLU A 1 63  ? 8.053   -1.780  -32.304 1.00 42.97 ?  63  GLU A N     1 
ATOM   473   C  CA    . GLU A 1 63  ? 9.341   -2.446  -32.400 1.00 38.72 ?  63  GLU A CA    1 
ATOM   474   C  C     . GLU A 1 63  ? 9.422   -3.533  -31.333 1.00 36.19 ?  63  GLU A C     1 
ATOM   475   O  O     . GLU A 1 63  ? 8.848   -3.399  -30.255 1.00 35.90 ?  63  GLU A O     1 
ATOM   476   C  CB    . GLU A 1 63  ? 10.511  -1.478  -32.224 1.00 42.94 ?  63  GLU A CB    1 
ATOM   477   C  CG    . GLU A 1 63  ? 10.897  -1.239  -30.768 1.00 48.72 ?  63  GLU A CG    1 
ATOM   478   C  CD    . GLU A 1 63  ? 11.844  -0.068  -30.574 1.00 52.14 ?  63  GLU A CD    1 
ATOM   479   O  OE1   . GLU A 1 63  ? 11.422  1.075   -30.851 1.00 51.05 ?  63  GLU A OE1   1 
ATOM   480   O  OE2   . GLU A 1 63  ? 13.000  -0.295  -30.159 1.00 52.22 -1 63  GLU A OE2   1 
ATOM   481   N  N     . VAL A 1 64  ? 10.145  -4.607  -31.662 1.00 28.43 ?  64  VAL A N     1 
ATOM   482   C  CA    . VAL A 1 64  ? 10.431  -5.672  -30.719 1.00 27.38 ?  64  VAL A CA    1 
ATOM   483   C  C     . VAL A 1 64  ? 11.561  -5.203  -29.810 1.00 25.81 ?  64  VAL A C     1 
ATOM   484   O  O     . VAL A 1 64  ? 12.649  -4.871  -30.276 1.00 22.92 ?  64  VAL A O     1 
ATOM   485   C  CB    . VAL A 1 64  ? 10.789  -6.989  -31.433 1.00 27.91 ?  64  VAL A CB    1 
ATOM   486   C  CG1   . VAL A 1 64  ? 11.383  -8.017  -30.478 1.00 24.75 ?  64  VAL A CG1   1 
ATOM   487   C  CG2   . VAL A 1 64  ? 9.591   -7.569  -32.174 1.00 28.78 ?  64  VAL A CG2   1 
ATOM   488   N  N     . LYS A 1 65  ? 11.272  -5.173  -28.509 1.00 25.70 ?  65  LYS A N     1 
ATOM   489   C  CA    . LYS A 1 65  ? 12.212  -4.688  -27.516 1.00 26.27 ?  65  LYS A CA    1 
ATOM   490   C  C     . LYS A 1 65  ? 11.854  -5.323  -26.178 1.00 26.80 ?  65  LYS A C     1 
ATOM   491   O  O     . LYS A 1 65  ? 10.734  -5.178  -25.692 1.00 25.51 ?  65  LYS A O     1 
ATOM   492   C  CB    . LYS A 1 65  ? 12.155  -3.157  -27.463 1.00 27.04 ?  65  LYS A CB    1 
ATOM   493   C  CG    . LYS A 1 65  ? 13.171  -2.469  -26.562 1.00 25.55 ?  65  LYS A CG    1 
ATOM   494   C  CD    . LYS A 1 65  ? 12.999  -0.954  -26.517 1.00 25.61 ?  65  LYS A CD    1 
ATOM   495   C  CE    . LYS A 1 65  ? 14.053  -0.270  -25.703 1.00 24.78 ?  65  LYS A CE    1 
ATOM   496   N  NZ    . LYS A 1 65  ? 14.019  1.188   -25.858 1.00 21.90 1  65  LYS A NZ    1 
ATOM   497   N  N     . ASN A 1 66  ? 12.816  -6.056  -25.615 1.00 30.03 ?  66  ASN A N     1 
ATOM   498   C  CA    . ASN A 1 66  ? 12.678  -6.628  -24.289 1.00 33.11 ?  66  ASN A CA    1 
ATOM   499   C  C     . ASN A 1 66  ? 12.506  -5.493  -23.282 1.00 31.78 ?  66  ASN A C     1 
ATOM   500   O  O     . ASN A 1 66  ? 13.254  -4.519  -23.312 1.00 29.57 ?  66  ASN A O     1 
ATOM   501   C  CB    . ASN A 1 66  ? 13.878  -7.503  -23.949 1.00 34.09 ?  66  ASN A CB    1 
ATOM   502   C  CG    . ASN A 1 66  ? 13.561  -8.503  -22.865 1.00 34.84 ?  66  ASN A CG    1 
ATOM   503   O  OD1   . ASN A 1 66  ? 13.072  -8.126  -21.795 1.00 36.72 ?  66  ASN A OD1   1 
ATOM   504   N  ND2   . ASN A 1 66  ? 13.816  -9.777  -23.126 1.00 36.00 ?  66  ASN A ND2   1 
ATOM   505   N  N     . ARG A 1 67  ? 11.514  -5.631  -22.395 1.00 33.57 ?  67  ARG A N     1 
ATOM   506   C  CA    . ARG A 1 67  ? 11.239  -4.618  -21.387 1.00 37.08 ?  67  ARG A CA    1 
ATOM   507   C  C     . ARG A 1 67  ? 12.432  -4.477  -20.443 1.00 33.66 ?  67  ARG A C     1 
ATOM   508   O  O     . ARG A 1 67  ? 12.647  -3.405  -19.883 1.00 35.97 ?  67  ARG A O     1 
ATOM   509   C  CB    . ARG A 1 67  ? 9.934   -4.896  -20.627 1.00 38.25 ?  67  ARG A CB    1 
ATOM   510   C  CG    . ARG A 1 67  ? 8.712   -4.207  -21.221 1.00 43.08 ?  67  ARG A CG    1 
ATOM   511   C  CD    . ARG A 1 67  ? 7.508   -4.198  -20.284 1.00 42.12 ?  67  ARG A CD    1 
ATOM   512   N  NE    . ARG A 1 67  ? 6.986   -5.531  -19.962 1.00 45.10 ?  67  ARG A NE    1 
ATOM   513   C  CZ    . ARG A 1 67  ? 6.343   -6.331  -20.806 1.00 47.16 ?  67  ARG A CZ    1 
ATOM   514   N  NH1   . ARG A 1 67  ? 6.173   -5.975  -22.067 1.00 46.17 1  67  ARG A NH1   1 
ATOM   515   N  NH2   . ARG A 1 67  ? 5.872   -7.490  -20.381 1.00 45.70 ?  67  ARG A NH2   1 
ATOM   516   N  N     . ARG A 1 68  ? 13.209  -5.553  -20.267 1.00 33.88 ?  68  ARG A N     1 
ATOM   517   C  CA    . ARG A 1 68  ? 14.417  -5.476  -19.459 1.00 33.64 ?  68  ARG A CA    1 
ATOM   518   C  C     . ARG A 1 68  ? 15.297  -4.343  -19.982 1.00 34.61 ?  68  ARG A C     1 
ATOM   519   O  O     . ARG A 1 68  ? 15.947  -3.646  -19.205 1.00 33.73 ?  68  ARG A O     1 
ATOM   520   C  CB    . ARG A 1 68  ? 15.211  -6.788  -19.448 1.00 37.06 ?  68  ARG A CB    1 
ATOM   521   C  CG    . ARG A 1 68  ? 14.491  -7.982  -18.837 1.00 40.15 ?  68  ARG A CG    1 
ATOM   522   C  CD    . ARG A 1 68  ? 15.417  -9.173  -18.627 1.00 42.69 ?  68  ARG A CD    1 
ATOM   523   N  NE    . ARG A 1 68  ? 14.676  -10.410 -18.355 1.00 45.94 ?  68  ARG A NE    1 
ATOM   524   C  CZ    . ARG A 1 68  ? 14.482  -10.942 -17.154 1.00 46.13 ?  68  ARG A CZ    1 
ATOM   525   N  NH1   . ARG A 1 68  ? 14.897  -10.311 -16.068 1.00 47.79 1  68  ARG A NH1   1 
ATOM   526   N  NH2   . ARG A 1 68  ? 13.846  -12.094 -17.041 1.00 42.52 ?  68  ARG A NH2   1 
ATOM   527   N  N     . ASP A 1 69  ? 15.302  -4.164  -21.307 1.00 35.51 ?  69  ASP A N     1 
ATOM   528   C  CA    . ASP A 1 69  ? 16.184  -3.208  -21.958 1.00 34.49 ?  69  ASP A CA    1 
ATOM   529   C  C     . ASP A 1 69  ? 15.620  -1.796  -21.810 1.00 33.80 ?  69  ASP A C     1 
ATOM   530   O  O     . ASP A 1 69  ? 16.372  -0.824  -21.801 1.00 31.99 ?  69  ASP A O     1 
ATOM   531   C  CB    . ASP A 1 69  ? 16.443  -3.594  -23.406 1.00 33.49 ?  69  ASP A CB    1 
ATOM   532   C  CG    . ASP A 1 69  ? 17.358  -4.795  -23.601 1.00 38.66 ?  69  ASP A CG    1 
ATOM   533   O  OD1   . ASP A 1 69  ? 18.538  -4.702  -23.202 1.00 45.82 ?  69  ASP A OD1   1 
ATOM   534   O  OD2   . ASP A 1 69  ? 16.883  -5.815  -24.145 1.00 36.13 -1 69  ASP A OD2   1 
ATOM   535   N  N     . THR A 1 70  ? 14.292  -1.695  -21.701 1.00 31.86 ?  70  THR A N     1 
ATOM   536   C  CA    . THR A 1 70  ? 13.645  -0.425  -21.418 1.00 32.50 ?  70  THR A CA    1 
ATOM   537   C  C     . THR A 1 70  ? 14.038  0.021   -20.012 1.00 31.85 ?  70  THR A C     1 
ATOM   538   O  O     . THR A 1 70  ? 14.435  1.166   -19.810 1.00 33.35 ?  70  THR A O     1 
ATOM   539   C  CB    . THR A 1 70  ? 12.133  -0.577  -21.582 1.00 33.22 ?  70  THR A CB    1 
ATOM   540   O  OG1   . THR A 1 70  ? 11.929  -0.769  -22.979 1.00 38.76 ?  70  THR A OG1   1 
ATOM   541   C  CG2   . THR A 1 70  ? 11.356  0.639   -21.111 1.00 32.28 ?  70  THR A CG2   1 
ATOM   542   N  N     . TYR A 1 71  ? 13.948  -0.904  -19.049 1.00 27.33 ?  71  TYR A N     1 
ATOM   543   C  CA    . TYR A 1 71  ? 14.198  -0.583  -17.653 1.00 26.23 ?  71  TYR A CA    1 
ATOM   544   C  C     . TYR A 1 71  ? 15.659  -0.163  -17.486 1.00 28.14 ?  71  TYR A C     1 
ATOM   545   O  O     . TYR A 1 71  ? 15.945  0.831   -16.822 1.00 26.44 ?  71  TYR A O     1 
ATOM   546   C  CB    . TYR A 1 71  ? 13.762  -1.767  -16.782 1.00 23.12 ?  71  TYR A CB    1 
ATOM   547   C  CG    . TYR A 1 71  ? 12.296  -2.160  -16.937 1.00 22.74 ?  71  TYR A CG    1 
ATOM   548   C  CD1   . TYR A 1 71  ? 11.326  -1.218  -17.265 1.00 22.09 ?  71  TYR A CD1   1 
ATOM   549   C  CD2   . TYR A 1 71  ? 11.881  -3.475  -16.764 1.00 21.69 ?  71  TYR A CD2   1 
ATOM   550   C  CE1   . TYR A 1 71  ? 9.994   -1.571  -17.412 1.00 22.79 ?  71  TYR A CE1   1 
ATOM   551   C  CE2   . TYR A 1 71  ? 10.552  -3.841  -16.908 1.00 22.75 ?  71  TYR A CE2   1 
ATOM   552   C  CZ    . TYR A 1 71  ? 9.606   -2.887  -17.233 1.00 23.33 ?  71  TYR A CZ    1 
ATOM   553   O  OH    . TYR A 1 71  ? 8.293   -3.236  -17.377 1.00 23.56 ?  71  TYR A OH    1 
ATOM   554   N  N     . GLU A 1 72  ? 16.578  -0.911  -18.111 1.00 27.57 ?  72  GLU A N     1 
ATOM   555   C  CA    . GLU A 1 72  ? 18.001  -0.617  -18.032 1.00 31.08 ?  72  GLU A CA    1 
ATOM   556   C  C     . GLU A 1 72  ? 18.285  0.809   -18.498 1.00 28.70 ?  72  GLU A C     1 
ATOM   557   O  O     . GLU A 1 72  ? 19.166  1.476   -17.960 1.00 28.12 ?  72  GLU A O     1 
ATOM   558   C  CB    . GLU A 1 72  ? 18.810  -1.586  -18.894 1.00 35.63 ?  72  GLU A CB    1 
ATOM   559   C  CG    . GLU A 1 72  ? 20.314  -1.327  -18.857 1.00 35.74 ?  72  GLU A CG    1 
ATOM   560   C  CD    . GLU A 1 72  ? 20.921  -1.384  -17.466 1.00 38.50 ?  72  GLU A CD    1 
ATOM   561   O  OE1   . GLU A 1 72  ? 20.536  -2.288  -16.694 1.00 34.80 ?  72  GLU A OE1   1 
ATOM   562   O  OE2   . GLU A 1 72  ? 21.792  -0.541  -17.162 1.00 40.63 -1 72  GLU A OE2   1 
ATOM   563   N  N     . GLN A 1 73  ? 17.546  1.257   -19.518 1.00 29.87 ?  73  GLN A N     1 
ATOM   564   C  CA    . GLN A 1 73  ? 17.780  2.555   -20.129 1.00 30.01 ?  73  GLN A CA    1 
ATOM   565   C  C     . GLN A 1 73  ? 17.264  3.651   -19.200 1.00 26.32 ?  73  GLN A C     1 
ATOM   566   O  O     . GLN A 1 73  ? 17.968  4.620   -18.926 1.00 26.18 ?  73  GLN A O     1 
ATOM   567   C  CB    . GLN A 1 73  ? 17.119  2.605   -21.507 1.00 33.26 ?  73  GLN A CB    1 
ATOM   568   C  CG    . GLN A 1 73  ? 17.761  1.670   -22.527 1.00 35.86 ?  73  GLN A CG    1 
ATOM   569   C  CD    . GLN A 1 73  ? 16.941  1.506   -23.789 1.00 38.31 ?  73  GLN A CD    1 
ATOM   570   O  OE1   . GLN A 1 73  ? 15.891  2.134   -23.964 1.00 38.11 ?  73  GLN A OE1   1 
ATOM   571   N  NE2   . GLN A 1 73  ? 17.415  0.652   -24.683 1.00 36.00 ?  73  GLN A NE2   1 
ATOM   572   N  N     . MET A 1 74  ? 16.023  3.482   -18.732 1.00 25.11 ?  74  MET A N     1 
ATOM   573   C  CA    . MET A 1 74  ? 15.470  4.334   -17.695 1.00 23.22 ?  74  MET A CA    1 
ATOM   574   C  C     . MET A 1 74  ? 16.512  4.515   -16.592 1.00 22.29 ?  74  MET A C     1 
ATOM   575   O  O     . MET A 1 74  ? 16.968  5.629   -16.340 1.00 21.50 ?  74  MET A O     1 
ATOM   576   C  CB    . MET A 1 74  ? 14.185  3.728   -17.113 1.00 21.66 ?  74  MET A CB    1 
ATOM   577   C  CG    . MET A 1 74  ? 13.023  3.660   -18.093 1.00 21.53 ?  74  MET A CG    1 
ATOM   578   S  SD    . MET A 1 74  ? 11.526  2.950   -17.377 1.00 21.81 ?  74  MET A SD    1 
ATOM   579   C  CE    . MET A 1 74  ? 10.365  3.118   -18.740 1.00 20.77 ?  74  MET A CE    1 
ATOM   580   N  N     . VAL A 1 75  ? 16.893  3.402   -15.955 1.00 20.60 ?  75  VAL A N     1 
ATOM   581   C  CA    . VAL A 1 75  ? 17.778  3.422   -14.800 1.00 19.29 ?  75  VAL A CA    1 
ATOM   582   C  C     . VAL A 1 75  ? 19.031  4.231   -15.125 1.00 21.27 ?  75  VAL A C     1 
ATOM   583   O  O     . VAL A 1 75  ? 19.516  4.991   -14.290 1.00 22.29 ?  75  VAL A O     1 
ATOM   584   C  CB    . VAL A 1 75  ? 18.136  1.990   -14.355 1.00 19.19 ?  75  VAL A CB    1 
ATOM   585   C  CG1   . VAL A 1 75  ? 19.269  1.972   -13.335 1.00 17.77 ?  75  VAL A CG1   1 
ATOM   586   C  CG2   . VAL A 1 75  ? 16.920  1.245   -13.817 1.00 17.90 ?  75  VAL A CG2   1 
ATOM   587   N  N     . ASN A 1 76  ? 19.543  4.061   -16.348 1.00 23.54 ?  76  ASN A N     1 
ATOM   588   C  CA    . ASN A 1 76  ? 20.805  4.664   -16.748 1.00 25.22 ?  76  ASN A CA    1 
ATOM   589   C  C     . ASN A 1 76  ? 20.638  6.168   -16.954 1.00 22.88 ?  76  ASN A C     1 
ATOM   590   O  O     . ASN A 1 76  ? 21.576  6.929   -16.725 1.00 25.18 ?  76  ASN A O     1 
ATOM   591   C  CB    . ASN A 1 76  ? 21.369  4.006   -18.002 1.00 27.26 ?  76  ASN A CB    1 
ATOM   592   C  CG    . ASN A 1 76  ? 22.759  4.503   -18.319 1.00 26.15 ?  76  ASN A CG    1 
ATOM   593   O  OD1   . ASN A 1 76  ? 22.954  5.212   -19.312 1.00 27.96 ?  76  ASN A OD1   1 
ATOM   594   N  ND2   . ASN A 1 76  ? 23.729  4.159   -17.484 1.00 27.29 ?  76  ASN A ND2   1 
ATOM   595   N  N     . ALA A 1 77  ? 19.451  6.589   -17.404 1.00 21.79 ?  77  ALA A N     1 
ATOM   596   C  CA    . ALA A 1 77  ? 19.174  8.002   -17.604 1.00 22.07 ?  77  ALA A CA    1 
ATOM   597   C  C     . ALA A 1 77  ? 19.137  8.711   -16.251 1.00 21.41 ?  77  ALA A C     1 
ATOM   598   O  O     . ALA A 1 77  ? 19.732  9.773   -16.085 1.00 21.04 ?  77  ALA A O     1 
ATOM   599   C  CB    . ALA A 1 77  ? 17.880  8.183   -18.369 1.00 22.88 ?  77  ALA A CB    1 
ATOM   600   N  N     . ILE A 1 78  ? 18.438  8.100   -15.288 1.00 20.14 ?  78  ILE A N     1 
ATOM   601   C  CA    . ILE A 1 78  ? 18.344  8.632   -13.938 1.00 19.17 ?  78  ILE A CA    1 
ATOM   602   C  C     . ILE A 1 78  ? 19.752  8.849   -13.388 1.00 19.48 ?  78  ILE A C     1 
ATOM   603   O  O     . ILE A 1 78  ? 20.077  9.935   -12.913 1.00 20.33 ?  78  ILE A O     1 
ATOM   604   C  CB    . ILE A 1 78  ? 17.512  7.692   -13.043 1.00 18.34 ?  78  ILE A CB    1 
ATOM   605   C  CG1   . ILE A 1 78  ? 16.066  7.594   -13.530 1.00 16.33 ?  78  ILE A CG1   1 
ATOM   606   C  CG2   . ILE A 1 78  ? 17.580  8.116   -11.575 1.00 18.48 ?  78  ILE A CG2   1 
ATOM   607   C  CD1   . ILE A 1 78  ? 15.268  6.471   -12.892 1.00 16.11 ?  78  ILE A CD1   1 
ATOM   608   N  N     . LEU A 1 79  ? 20.585  7.806   -13.471 1.00 21.41 ?  79  LEU A N     1 
ATOM   609   C  CA    . LEU A 1 79  ? 21.907  7.817   -12.865 1.00 20.90 ?  79  LEU A CA    1 
ATOM   610   C  C     . LEU A 1 79  ? 22.806  8.836   -13.562 1.00 20.31 ?  79  LEU A C     1 
ATOM   611   O  O     . LEU A 1 79  ? 23.674  9.429   -12.926 1.00 19.42 ?  79  LEU A O     1 
ATOM   612   C  CB    . LEU A 1 79  ? 22.508  6.412   -12.901 1.00 20.87 ?  79  LEU A CB    1 
ATOM   613   C  CG    . LEU A 1 79  ? 22.164  5.502   -11.718 1.00 21.60 ?  79  LEU A CG    1 
ATOM   614   C  CD1   . LEU A 1 79  ? 22.847  5.986   -10.450 1.00 23.45 ?  79  LEU A CD1   1 
ATOM   615   C  CD2   . LEU A 1 79  ? 20.664  5.401   -11.504 1.00 23.14 ?  79  LEU A CD2   1 
ATOM   616   N  N     . ASP A 1 80  ? 22.601  9.026   -14.871 1.00 20.17 ?  80  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 80  ? 23.345  10.024  -15.624 1.00 22.24 ?  80  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 80  ? 23.177  11.402  -14.984 1.00 22.03 ?  80  ASP A C     1 
ATOM   619   O  O     . ASP A 1 80  ? 24.143  12.156  -14.886 1.00 19.72 ?  80  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 80  ? 22.954  10.040  -17.095 1.00 26.02 ?  80  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 80  ? 23.711  9.068   -17.990 1.00 28.23 ?  80  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 80  ? 24.553  8.312   -17.461 1.00 24.84 ?  80  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 80  ? 23.460  9.087   -19.215 1.00 29.55 -1 80  ASP A OD2   1 
ATOM   624   N  N     . ALA A 1 81  ? 21.952  11.737  -14.561 1.00 20.72 ?  81  ALA A N     1 
ATOM   625   C  CA    . ALA A 1 81  ? 21.707  13.024  -13.928 1.00 19.28 ?  81  ALA A CA    1 
ATOM   626   C  C     . ALA A 1 81  ? 22.379  13.060  -12.556 1.00 17.99 ?  81  ALA A C     1 
ATOM   627   O  O     . ALA A 1 81  ? 23.017  14.049  -12.202 1.00 17.07 ?  81  ALA A O     1 
ATOM   628   C  CB    . ALA A 1 81  ? 20.221  13.303  -13.831 1.00 18.16 ?  81  ALA A CB    1 
ATOM   629   N  N     . VAL A 1 82  ? 22.236  11.969  -11.795 1.00 18.01 ?  82  VAL A N     1 
ATOM   630   C  CA    . VAL A 1 82  ? 22.818  11.876  -10.464 1.00 18.81 ?  82  VAL A CA    1 
ATOM   631   C  C     . VAL A 1 82  ? 24.327  12.107  -10.564 1.00 19.14 ?  82  VAL A C     1 
ATOM   632   O  O     . VAL A 1 82  ? 24.877  12.945  -9.852  1.00 19.91 ?  82  VAL A O     1 
ATOM   633   C  CB    . VAL A 1 82  ? 22.478  10.526  -9.799  1.00 18.36 ?  82  VAL A CB    1 
ATOM   634   C  CG1   . VAL A 1 82  ? 23.179  10.342  -8.457  1.00 17.81 ?  82  VAL A CG1   1 
ATOM   635   C  CG2   . VAL A 1 82  ? 20.973  10.349  -9.628  1.00 18.33 ?  82  VAL A CG2   1 
ATOM   636   N  N     . ARG A 1 83  ? 24.977  11.378  -11.478 1.00 22.66 ?  83  ARG A N     1 
ATOM   637   C  CA    . ARG A 1 83  ? 26.425  11.402  -11.635 1.00 22.17 ?  83  ARG A CA    1 
ATOM   638   C  C     . ARG A 1 83  ? 26.924  12.798  -12.010 1.00 21.86 ?  83  ARG A C     1 
ATOM   639   O  O     . ARG A 1 83  ? 28.036  13.177  -11.647 1.00 19.87 ?  83  ARG A O     1 
ATOM   640   C  CB    . ARG A 1 83  ? 26.824  10.385  -12.710 1.00 24.85 ?  83  ARG A CB    1 
ATOM   641   C  CG    . ARG A 1 83  ? 26.753  8.933   -12.260 1.00 24.09 ?  83  ARG A CG    1 
ATOM   642   C  CD    . ARG A 1 83  ? 26.780  7.993   -13.454 1.00 24.94 ?  83  ARG A CD    1 
ATOM   643   N  NE    . ARG A 1 83  ? 26.453  6.605   -13.109 1.00 24.74 ?  83  ARG A NE    1 
ATOM   644   C  CZ    . ARG A 1 83  ? 26.044  5.702   -13.993 1.00 27.03 ?  83  ARG A CZ    1 
ATOM   645   N  NH1   . ARG A 1 83  ? 25.882  6.046   -15.259 1.00 25.97 1  83  ARG A NH1   1 
ATOM   646   N  NH2   . ARG A 1 83  ? 25.781  4.466   -13.608 1.00 25.86 ?  83  ARG A NH2   1 
ATOM   647   N  N     . ALA A 1 84  ? 26.103  13.544  -12.755 1.00 22.92 ?  84  ALA A N     1 
ATOM   648   C  CA    . ALA A 1 84  ? 26.457  14.880  -13.211 1.00 20.72 ?  84  ALA A CA    1 
ATOM   649   C  C     . ALA A 1 84  ? 26.445  15.862  -12.041 1.00 20.34 ?  84  ALA A C     1 
ATOM   650   O  O     . ALA A 1 84  ? 27.032  16.940  -12.123 1.00 20.33 ?  84  ALA A O     1 
ATOM   651   C  CB    . ALA A 1 84  ? 25.508  15.309  -14.308 1.00 21.65 ?  84  ALA A CB    1 
ATOM   652   N  N     . GLY A 1 85  ? 25.758  15.480  -10.959 1.00 20.01 ?  85  GLY A N     1 
ATOM   653   C  CA    . GLY A 1 85  ? 25.741  16.265  -9.735  1.00 21.43 ?  85  GLY A CA    1 
ATOM   654   C  C     . GLY A 1 85  ? 24.402  16.971  -9.527  1.00 21.52 ?  85  GLY A C     1 
ATOM   655   O  O     . GLY A 1 85  ? 24.341  18.003  -8.861  1.00 19.65 ?  85  GLY A O     1 
ATOM   656   N  N     . LYS A 1 86  ? 23.336  16.399  -10.095 1.00 20.57 ?  86  LYS A N     1 
ATOM   657   C  CA    . LYS A 1 86  ? 22.006  16.977  -9.995  1.00 22.05 ?  86  LYS A CA    1 
ATOM   658   C  C     . LYS A 1 86  ? 21.252  16.328  -8.838  1.00 20.10 ?  86  LYS A C     1 
ATOM   659   O  O     . LYS A 1 86  ? 21.296  15.112  -8.674  1.00 17.40 ?  86  LYS A O     1 
ATOM   660   C  CB    . LYS A 1 86  ? 21.197  16.755  -11.279 1.00 22.79 ?  86  LYS A CB    1 
ATOM   661   C  CG    . LYS A 1 86  ? 21.791  17.313  -12.565 1.00 24.28 ?  86  LYS A CG    1 
ATOM   662   C  CD    . LYS A 1 86  ? 20.971  16.947  -13.797 1.00 26.75 ?  86  LYS A CD    1 
ATOM   663   C  CE    . LYS A 1 86  ? 21.586  17.386  -15.087 1.00 27.47 ?  86  LYS A CE    1 
ATOM   664   N  NZ    . LYS A 1 86  ? 21.636  18.846  -15.192 1.00 30.00 1  86  LYS A NZ    1 
ATOM   665   N  N     . LYS A 1 87  ? 20.560  17.152  -8.042  1.00 20.48 ?  87  LYS A N     1 
ATOM   666   C  CA    . LYS A 1 87  ? 19.589  16.646  -7.087  1.00 17.16 ?  87  LYS A CA    1 
ATOM   667   C  C     . LYS A 1 87  ? 18.404  16.099  -7.879  1.00 16.62 ?  87  LYS A C     1 
ATOM   668   O  O     . LYS A 1 87  ? 17.572  16.860  -8.366  1.00 16.44 ?  87  LYS A O     1 
ATOM   669   C  CB    . LYS A 1 87  ? 19.176  17.732  -6.086  1.00 15.81 ?  87  LYS A CB    1 
ATOM   670   C  CG    . LYS A 1 87  ? 18.146  17.290  -5.057  1.00 15.77 ?  87  LYS A CG    1 
ATOM   671   C  CD    . LYS A 1 87  ? 17.854  18.316  -3.970  1.00 16.96 ?  87  LYS A CD    1 
ATOM   672   C  CE    . LYS A 1 87  ? 17.371  19.625  -4.501  1.00 17.71 ?  87  LYS A CE    1 
ATOM   673   N  NZ    . LYS A 1 87  ? 17.187  20.566  -3.395  1.00 20.26 1  87  LYS A NZ    1 
ATOM   674   N  N     . THR A 1 88  ? 18.350  14.768  -8.002  1.00 16.75 ?  88  THR A N     1 
ATOM   675   C  CA    . THR A 1 88  ? 17.498  14.111  -8.980  1.00 16.34 ?  88  THR A CA    1 
ATOM   676   C  C     . THR A 1 88  ? 16.316  13.456  -8.272  1.00 16.14 ?  88  THR A C     1 
ATOM   677   O  O     . THR A 1 88  ? 16.475  12.862  -7.208  1.00 17.71 ?  88  THR A O     1 
ATOM   678   C  CB    . THR A 1 88  ? 18.335  13.087  -9.748  1.00 18.89 ?  88  THR A CB    1 
ATOM   679   O  OG1   . THR A 1 88  ? 19.454  13.801  -10.264 1.00 19.95 ?  88  THR A OG1   1 
ATOM   680   C  CG2   . THR A 1 88  ? 17.570  12.434  -10.886 1.00 19.33 ?  88  THR A CG2   1 
ATOM   681   N  N     . VAL A 1 89  ? 15.131  13.564  -8.882  1.00 15.88 ?  89  VAL A N     1 
ATOM   682   C  CA    . VAL A 1 89  ? 13.932  12.948  -8.339  1.00 16.30 ?  89  VAL A CA    1 
ATOM   683   C  C     . VAL A 1 89  ? 13.337  12.031  -9.404  1.00 14.78 ?  89  VAL A C     1 
ATOM   684   O  O     . VAL A 1 89  ? 13.261  12.397  -10.573 1.00 14.17 ?  89  VAL A O     1 
ATOM   685   C  CB    . VAL A 1 89  ? 12.911  13.999  -7.860  1.00 14.86 ?  89  VAL A CB    1 
ATOM   686   C  CG1   . VAL A 1 89  ? 11.536  13.392  -7.600  1.00 14.76 ?  89  VAL A CG1   1 
ATOM   687   C  CG2   . VAL A 1 89  ? 13.409  14.742  -6.625  1.00 14.48 ?  89  VAL A CG2   1 
ATOM   688   N  N     . CYS A 1 90  ? 12.945  10.824  -8.988  1.00 15.89 ?  90  CYS A N     1 
ATOM   689   C  CA    . CYS A 1 90  ? 12.227  9.919   -9.867  1.00 16.62 ?  90  CYS A CA    1 
ATOM   690   C  C     . CYS A 1 90  ? 10.785  9.804   -9.378  1.00 15.44 ?  90  CYS A C     1 
ATOM   691   O  O     . CYS A 1 90  ? 10.535  9.347   -8.264  1.00 16.82 ?  90  CYS A O     1 
ATOM   692   C  CB    . CYS A 1 90  ? 12.926  8.567   -9.957  1.00 20.04 ?  90  CYS A CB    1 
ATOM   693   S  SG    . CYS A 1 90  ? 12.068  7.383   -11.027 1.00 25.12 ?  90  CYS A SG    1 
ATOM   694   N  N     . ALA A 1 91  ? 9.849   10.249  -10.224 1.00 13.58 ?  91  ALA A N     1 
ATOM   695   C  CA    . ALA A 1 91  ? 8.434   10.223  -9.898  1.00 13.26 ?  91  ALA A CA    1 
ATOM   696   C  C     . ALA A 1 91  ? 7.734   9.154   -10.731 1.00 14.33 ?  91  ALA A C     1 
ATOM   697   O  O     . ALA A 1 91  ? 7.618   9.278   -11.950 1.00 15.57 ?  91  ALA A O     1 
ATOM   698   C  CB    . ALA A 1 91  ? 7.822   11.590  -10.116 1.00 13.71 ?  91  ALA A CB    1 
ATOM   699   N  N     . LEU A 1 92  ? 7.281   8.101   -10.044 1.00 14.27 ?  92  LEU A N     1 
ATOM   700   C  CA    . LEU A 1 92  ? 6.547   7.012   -10.663 1.00 16.52 ?  92  LEU A CA    1 
ATOM   701   C  C     . LEU A 1 92  ? 5.120   7.037   -10.125 1.00 17.47 ?  92  LEU A C     1 
ATOM   702   O  O     . LEU A 1 92  ? 4.886   7.498   -9.010  1.00 19.17 ?  92  LEU A O     1 
ATOM   703   C  CB    . LEU A 1 92  ? 7.217   5.671   -10.363 1.00 18.53 ?  92  LEU A CB    1 
ATOM   704   C  CG    . LEU A 1 92  ? 8.689   5.522   -10.762 1.00 20.82 ?  92  LEU A CG    1 
ATOM   705   C  CD1   . LEU A 1 92  ? 9.126   4.090   -10.505 1.00 23.60 ?  92  LEU A CD1   1 
ATOM   706   C  CD2   . LEU A 1 92  ? 8.959   5.902   -12.207 1.00 21.47 ?  92  LEU A CD2   1 
ATOM   707   N  N     . TYR A 1 93  ? 4.171   6.531   -10.915 1.00 17.99 ?  93  TYR A N     1 
ATOM   708   C  CA    . TYR A 1 93  ? 2.783   6.526   -10.491 1.00 20.45 ?  93  TYR A CA    1 
ATOM   709   C  C     . TYR A 1 93  ? 2.628   5.493   -9.376  1.00 20.04 ?  93  TYR A C     1 
ATOM   710   O  O     . TYR A 1 93  ? 3.304   4.464   -9.372  1.00 23.85 ?  93  TYR A O     1 
ATOM   711   C  CB    . TYR A 1 93  ? 1.875   6.317   -11.708 1.00 23.84 ?  93  TYR A CB    1 
ATOM   712   C  CG    . TYR A 1 93  ? 1.856   4.904   -12.272 1.00 25.57 ?  93  TYR A CG    1 
ATOM   713   C  CD1   . TYR A 1 93  ? 0.994   3.948   -11.754 1.00 28.25 ?  93  TYR A CD1   1 
ATOM   714   C  CD2   . TYR A 1 93  ? 2.684   4.531   -13.325 1.00 25.79 ?  93  TYR A CD2   1 
ATOM   715   C  CE1   . TYR A 1 93  ? 0.960   2.659   -12.257 1.00 30.16 ?  93  TYR A CE1   1 
ATOM   716   C  CE2   . TYR A 1 93  ? 2.660   3.244   -13.837 1.00 26.50 ?  93  TYR A CE2   1 
ATOM   717   C  CZ    . TYR A 1 93  ? 1.795   2.306   -13.301 1.00 27.73 ?  93  TYR A CZ    1 
ATOM   718   O  OH    . TYR A 1 93  ? 1.763   1.036   -13.796 1.00 32.11 ?  93  TYR A OH    1 
ATOM   719   N  N     . GLY A 1 94  ? 1.756   5.809   -8.414  1.00 16.33 ?  94  GLY A N     1 
ATOM   720   C  CA    . GLY A 1 94  ? 1.519   4.957   -7.261  1.00 15.34 ?  94  GLY A CA    1 
ATOM   721   C  C     . GLY A 1 94  ? 2.732   4.919   -6.336  1.00 15.00 ?  94  GLY A C     1 
ATOM   722   O  O     . GLY A 1 94  ? 3.324   5.951   -6.029  1.00 14.49 ?  94  GLY A O     1 
ATOM   723   N  N     . HIS A 1 95  ? 3.088   3.708   -5.899  1.00 14.44 ?  95  HIS A N     1 
ATOM   724   C  CA    . HIS A 1 95  ? 4.216   3.509   -5.006  1.00 16.75 ?  95  HIS A CA    1 
ATOM   725   C  C     . HIS A 1 95  ? 5.436   3.163   -5.857  1.00 17.95 ?  95  HIS A C     1 
ATOM   726   O  O     . HIS A 1 95  ? 5.417   2.197   -6.618  1.00 19.61 ?  95  HIS A O     1 
ATOM   727   C  CB    . HIS A 1 95  ? 3.834   2.483   -3.930  1.00 17.57 ?  95  HIS A CB    1 
ATOM   728   C  CG    . HIS A 1 95  ? 4.899   2.197   -2.928  1.00 16.77 ?  95  HIS A CG    1 
ATOM   729   N  ND1   . HIS A 1 95  ? 6.242   2.219   -3.235  1.00 19.05 ?  95  HIS A ND1   1 
ATOM   730   C  CD2   . HIS A 1 95  ? 4.818   1.863   -1.634  1.00 15.91 ?  95  HIS A CD2   1 
ATOM   731   C  CE1   . HIS A 1 95  ? 6.941   1.911   -2.152  1.00 17.65 ?  95  HIS A CE1   1 
ATOM   732   N  NE2   . HIS A 1 95  ? 6.097   1.691   -1.168  1.00 17.27 ?  95  HIS A NE2   1 
ATOM   733   N  N     . PRO A 1 96  ? 6.530   3.952   -5.771  1.00 16.88 ?  96  PRO A N     1 
ATOM   734   C  CA    . PRO A 1 96  ? 7.637   3.839   -6.723  1.00 17.89 ?  96  PRO A CA    1 
ATOM   735   C  C     . PRO A 1 96  ? 8.368   2.498   -6.704  1.00 20.68 ?  96  PRO A C     1 
ATOM   736   O  O     . PRO A 1 96  ? 9.121   2.192   -7.626  1.00 20.48 ?  96  PRO A O     1 
ATOM   737   C  CB    . PRO A 1 96  ? 8.557   4.999   -6.304  1.00 17.67 ?  96  PRO A CB    1 
ATOM   738   C  CG    . PRO A 1 96  ? 8.265   5.183   -4.833  1.00 17.32 ?  96  PRO A CG    1 
ATOM   739   C  CD    . PRO A 1 96  ? 6.763   4.979   -4.742  1.00 17.46 ?  96  PRO A CD    1 
ATOM   740   N  N     . GLY A 1 97  ? 8.136   1.702   -5.654  1.00 19.94 ?  97  GLY A N     1 
ATOM   741   C  CA    . GLY A 1 97  ? 8.873   0.464   -5.463  1.00 23.12 ?  97  GLY A CA    1 
ATOM   742   C  C     . GLY A 1 97  ? 7.958   -0.755  -5.372  1.00 24.49 ?  97  GLY A C     1 
ATOM   743   O  O     . GLY A 1 97  ? 8.405   -1.830  -4.977  1.00 26.73 ?  97  GLY A O     1 
ATOM   744   N  N     . VAL A 1 98  ? 6.684   -0.589  -5.746  1.00 23.36 ?  98  VAL A N     1 
ATOM   745   C  CA    . VAL A 1 98  ? 5.746   -1.701  -5.756  1.00 24.30 ?  98  VAL A CA    1 
ATOM   746   C  C     . VAL A 1 98  ? 5.558   -2.158  -7.201  1.00 25.46 ?  98  VAL A C     1 
ATOM   747   O  O     . VAL A 1 98  ? 5.072   -1.401  -8.039  1.00 23.16 ?  98  VAL A O     1 
ATOM   748   C  CB    . VAL A 1 98  ? 4.395   -1.358  -5.095  1.00 22.88 ?  98  VAL A CB    1 
ATOM   749   C  CG1   . VAL A 1 98  ? 3.363   -2.460  -5.309  1.00 24.87 ?  98  VAL A CG1   1 
ATOM   750   C  CG2   . VAL A 1 98  ? 4.545   -1.058  -3.607  1.00 21.57 ?  98  VAL A CG2   1 
ATOM   751   N  N     . PHE A 1 99  ? 5.962   -3.405  -7.475  1.00 24.38 ?  99  PHE A N     1 
ATOM   752   C  CA    . PHE A 1 99  ? 5.865   -3.996  -8.802  1.00 23.61 ?  99  PHE A CA    1 
ATOM   753   C  C     . PHE A 1 99  ? 6.513   -3.078  -9.834  1.00 22.09 ?  99  PHE A C     1 
ATOM   754   O  O     . PHE A 1 99  ? 6.011   -2.932  -10.945 1.00 20.80 ?  99  PHE A O     1 
ATOM   755   C  CB    . PHE A 1 99  ? 4.410   -4.269  -9.190  1.00 24.91 ?  99  PHE A CB    1 
ATOM   756   C  CG    . PHE A 1 99  ? 3.847   -5.541  -8.575  1.00 24.64 ?  99  PHE A CG    1 
ATOM   757   C  CD1   . PHE A 1 99  ? 3.461   -5.575  -7.241  1.00 21.34 ?  99  PHE A CD1   1 
ATOM   758   C  CD2   . PHE A 1 99  ? 3.710   -6.699  -9.333  1.00 24.25 ?  99  PHE A CD2   1 
ATOM   759   C  CE1   . PHE A 1 99  ? 2.951   -6.735  -6.683  1.00 23.04 ?  99  PHE A CE1   1 
ATOM   760   C  CE2   . PHE A 1 99  ? 3.199   -7.856  -8.769  1.00 21.98 ?  99  PHE A CE2   1 
ATOM   761   C  CZ    . PHE A 1 99  ? 2.822   -7.872  -7.447  1.00 21.77 ?  99  PHE A CZ    1 
ATOM   762   N  N     . ALA A 1 100 ? 7.643   -2.482  -9.452  1.00 23.17 ?  100 ALA A N     1 
ATOM   763   C  CA    . ALA A 1 100 ? 8.342   -1.534  -10.299 1.00 27.25 ?  100 ALA A CA    1 
ATOM   764   C  C     . ALA A 1 100 ? 9.825   -1.561  -9.944  1.00 30.73 ?  100 ALA A C     1 
ATOM   765   O  O     . ALA A 1 100 ? 10.208  -1.210  -8.830  1.00 36.20 ?  100 ALA A O     1 
ATOM   766   C  CB    . ALA A 1 100 ? 7.745   -0.155  -10.128 1.00 28.40 ?  100 ALA A CB    1 
ATOM   767   N  N     . CYS A 1 101 ? 10.647  -1.980  -10.910 1.00 33.18 ?  101 CYS A N     1 
ATOM   768   C  CA    . CYS A 1 101 ? 12.022  -2.363  -10.638 1.00 35.33 ?  101 CYS A CA    1 
ATOM   769   C  C     . CYS A 1 101 ? 12.986  -1.240  -11.013 1.00 32.76 ?  101 CYS A C     1 
ATOM   770   O  O     . CYS A 1 101 ? 14.188  -1.350  -10.784 1.00 34.99 ?  101 CYS A O     1 
ATOM   771   C  CB    . CYS A 1 101 ? 12.380  -3.638  -11.394 1.00 34.24 ?  101 CYS A CB    1 
ATOM   772   S  SG    . CYS A 1 101 ? 12.414  -3.427  -13.193 1.00 31.99 ?  101 CYS A SG    1 
ATOM   773   N  N     . VAL A 1 102 ? 12.447  -0.161  -11.588 1.00 30.81 ?  102 VAL A N     1 
ATOM   774   C  CA    . VAL A 1 102 ? 13.266  0.942   -12.064 1.00 29.14 ?  102 VAL A CA    1 
ATOM   775   C  C     . VAL A 1 102 ? 13.829  1.714   -10.874 1.00 28.23 ?  102 VAL A C     1 
ATOM   776   O  O     . VAL A 1 102 ? 14.972  2.162   -10.911 1.00 34.53 ?  102 VAL A O     1 
ATOM   777   C  CB    . VAL A 1 102 ? 12.475  1.875   -13.000 1.00 29.56 ?  102 VAL A CB    1 
ATOM   778   C  CG1   . VAL A 1 102 ? 13.191  3.204   -13.207 1.00 28.14 ?  102 VAL A CG1   1 
ATOM   779   C  CG2   . VAL A 1 102 ? 12.173  1.204   -14.334 1.00 28.63 ?  102 VAL A CG2   1 
ATOM   780   N  N     . SER A 1 103 ? 13.016  1.875   -9.826  1.00 26.79 ?  103 SER A N     1 
ATOM   781   C  CA    . SER A 1 103 ? 13.427  2.642   -8.662  1.00 28.31 ?  103 SER A CA    1 
ATOM   782   C  C     . SER A 1 103 ? 14.442  1.854   -7.836  1.00 25.95 ?  103 SER A C     1 
ATOM   783   O  O     . SER A 1 103 ? 15.442  2.412   -7.393  1.00 25.62 ?  103 SER A O     1 
ATOM   784   C  CB    . SER A 1 103 ? 12.238  3.060   -7.834  1.00 28.32 ?  103 SER A CB    1 
ATOM   785   O  OG    . SER A 1 103 ? 11.497  4.079   -8.491  1.00 28.89 ?  103 SER A OG    1 
ATOM   786   N  N     . HIS A 1 104 ? 14.184  0.556   -7.640  1.00 25.92 ?  104 HIS A N     1 
ATOM   787   C  CA    . HIS A 1 104 ? 15.041  -0.271  -6.804  1.00 26.50 ?  104 HIS A CA    1 
ATOM   788   C  C     . HIS A 1 104 ? 16.426  -0.390  -7.438  1.00 22.42 ?  104 HIS A C     1 
ATOM   789   O  O     . HIS A 1 104 ? 17.434  -0.409  -6.736  1.00 20.01 ?  104 HIS A O     1 
ATOM   790   C  CB    . HIS A 1 104 ? 14.407  -1.642  -6.539  1.00 27.89 ?  104 HIS A CB    1 
ATOM   791   C  CG    . HIS A 1 104 ? 13.292  -1.633  -5.542  1.00 28.14 ?  104 HIS A CG    1 
ATOM   792   N  ND1   . HIS A 1 104 ? 13.483  -1.392  -4.199  1.00 26.94 ?  104 HIS A ND1   1 
ATOM   793   C  CD2   . HIS A 1 104 ? 11.976  -1.830  -5.697  1.00 27.88 ?  104 HIS A CD2   1 
ATOM   794   C  CE1   . HIS A 1 104 ? 12.316  -1.450  -3.573  1.00 27.74 ?  104 HIS A CE1   1 
ATOM   795   N  NE2   . HIS A 1 104 ? 11.388  -1.718  -4.463  1.00 26.95 ?  104 HIS A NE2   1 
ATOM   796   N  N     . MET A 1 105 ? 16.463  -0.460  -8.772  1.00 20.97 ?  105 MET A N     1 
ATOM   797   C  CA    . MET A 1 105 ? 17.712  -0.627  -9.498  1.00 20.38 ?  105 MET A CA    1 
ATOM   798   C  C     . MET A 1 105 ? 18.506  0.676   -9.463  1.00 19.43 ?  105 MET A C     1 
ATOM   799   O  O     . MET A 1 105 ? 19.711  0.662   -9.222  1.00 18.22 ?  105 MET A O     1 
ATOM   800   C  CB    . MET A 1 105 ? 17.446  -1.076  -10.940 1.00 23.24 ?  105 MET A CB    1 
ATOM   801   C  CG    . MET A 1 105 ? 17.042  -2.535  -11.048 1.00 24.76 ?  105 MET A CG    1 
ATOM   802   S  SD    . MET A 1 105 ? 16.273  -2.957  -12.624 1.00 28.26 ?  105 MET A SD    1 
ATOM   803   C  CE    . MET A 1 105 ? 17.643  -2.653  -13.748 1.00 29.78 ?  105 MET A CE    1 
ATOM   804   N  N     . ALA A 1 106 ? 17.818  1.800   -9.692  1.00 17.92 ?  106 ALA A N     1 
ATOM   805   C  CA    . ALA A 1 106 ? 18.448  3.108   -9.642  1.00 16.41 ?  106 ALA A CA    1 
ATOM   806   C  C     . ALA A 1 106 ? 19.050  3.344   -8.258  1.00 15.83 ?  106 ALA A C     1 
ATOM   807   O  O     . ALA A 1 106 ? 20.183  3.808   -8.145  1.00 17.07 ?  106 ALA A O     1 
ATOM   808   C  CB    . ALA A 1 106 ? 17.446  4.185   -9.997  1.00 17.20 ?  106 ALA A CB    1 
ATOM   809   N  N     . ILE A 1 107 ? 18.282  3.016   -7.214  1.00 13.81 ?  107 ILE A N     1 
ATOM   810   C  CA    . ILE A 1 107 ? 18.707  3.248   -5.842  1.00 14.97 ?  107 ILE A CA    1 
ATOM   811   C  C     . ILE A 1 107 ? 19.931  2.381   -5.539  1.00 15.27 ?  107 ILE A C     1 
ATOM   812   O  O     . ILE A 1 107 ? 20.931  2.873   -5.022  1.00 15.83 ?  107 ILE A O     1 
ATOM   813   C  CB    . ILE A 1 107 ? 17.548  2.999   -4.857  1.00 14.28 ?  107 ILE A CB    1 
ATOM   814   C  CG1   . ILE A 1 107 ? 16.506  4.129   -4.924  1.00 15.45 ?  107 ILE A CG1   1 
ATOM   815   C  CG2   . ILE A 1 107 ? 18.072  2.797   -3.434  1.00 15.12 ?  107 ILE A CG2   1 
ATOM   816   C  CD1   . ILE A 1 107 ? 15.374  4.012   -3.918  1.00 13.94 ?  107 ILE A CD1   1 
ATOM   817   N  N     . THR A 1 108 ? 19.837  1.090   -5.877  1.00 16.05 ?  108 THR A N     1 
ATOM   818   C  CA    . THR A 1 108 ? 20.900  0.125   -5.634  1.00 16.30 ?  108 THR A CA    1 
ATOM   819   C  C     . THR A 1 108 ? 22.201  0.583   -6.291  1.00 18.30 ?  108 THR A C     1 
ATOM   820   O  O     . THR A 1 108 ? 23.266  0.520   -5.681  1.00 20.78 ?  108 THR A O     1 
ATOM   821   C  CB    . THR A 1 108 ? 20.464  -1.235  -6.177  1.00 15.97 ?  108 THR A CB    1 
ATOM   822   O  OG1   . THR A 1 108 ? 19.512  -1.748  -5.252  1.00 15.55 ?  108 THR A OG1   1 
ATOM   823   C  CG2   . THR A 1 108 ? 21.619  -2.210  -6.311  1.00 18.16 ?  108 THR A CG2   1 
ATOM   824   N  N     . ARG A 1 109 ? 22.102  1.018   -7.550  1.00 18.56 ?  109 ARG A N     1 
ATOM   825   C  CA    . ARG A 1 109 ? 23.267  1.361   -8.349  1.00 20.20 ?  109 ARG A CA    1 
ATOM   826   C  C     . ARG A 1 109 ? 23.862  2.677   -7.853  1.00 20.82 ?  109 ARG A C     1 
ATOM   827   O  O     . ARG A 1 109 ? 25.078  2.860   -7.869  1.00 22.42 ?  109 ARG A O     1 
ATOM   828   C  CB    . ARG A 1 109 ? 22.839  1.422   -9.820  1.00 20.92 ?  109 ARG A CB    1 
ATOM   829   C  CG    . ARG A 1 109 ? 23.985  1.505   -10.818 1.00 23.10 ?  109 ARG A CG    1 
ATOM   830   C  CD    . ARG A 1 109 ? 23.513  1.410   -12.263 1.00 25.94 ?  109 ARG A CD    1 
ATOM   831   N  NE    . ARG A 1 109 ? 22.787  0.164   -12.536 1.00 27.31 ?  109 ARG A NE    1 
ATOM   832   C  CZ    . ARG A 1 109 ? 22.429  -0.257  -13.743 1.00 29.28 ?  109 ARG A CZ    1 
ATOM   833   N  NH1   . ARG A 1 109 ? 22.685  0.484   -14.807 1.00 30.71 1  109 ARG A NH1   1 
ATOM   834   N  NH2   . ARG A 1 109 ? 21.815  -1.418  -13.883 1.00 30.24 ?  109 ARG A NH2   1 
ATOM   835   N  N     . ALA A 1 110 ? 22.986  3.585   -7.409  1.00 20.13 ?  110 ALA A N     1 
ATOM   836   C  CA    . ALA A 1 110 ? 23.398  4.886   -6.906  1.00 18.89 ?  110 ALA A CA    1 
ATOM   837   C  C     . ALA A 1 110 ? 24.240  4.718   -5.644  1.00 17.76 ?  110 ALA A C     1 
ATOM   838   O  O     . ALA A 1 110 ? 25.287  5.345   -5.508  1.00 17.48 ?  110 ALA A O     1 
ATOM   839   C  CB    . ALA A 1 110 ? 22.181  5.747   -6.647  1.00 18.94 ?  110 ALA A CB    1 
ATOM   840   N  N     . LYS A 1 111 ? 23.768  3.870   -4.725  1.00 20.70 ?  111 LYS A N     1 
ATOM   841   C  CA    . LYS A 1 111 ? 24.473  3.620   -3.479  1.00 24.55 ?  111 LYS A CA    1 
ATOM   842   C  C     . LYS A 1 111 ? 25.863  3.062   -3.779  1.00 26.39 ?  111 LYS A C     1 
ATOM   843   O  O     . LYS A 1 111 ? 26.846  3.480   -3.172  1.00 28.48 ?  111 LYS A O     1 
ATOM   844   C  CB    . LYS A 1 111 ? 23.681  2.666   -2.576  1.00 23.42 ?  111 LYS A CB    1 
ATOM   845   C  CG    . LYS A 1 111 ? 22.483  3.280   -1.861  1.00 23.80 ?  111 LYS A CG    1 
ATOM   846   C  CD    . LYS A 1 111 ? 21.676  2.269   -1.054  1.00 25.68 ?  111 LYS A CD    1 
ATOM   847   C  CE    . LYS A 1 111 ? 20.406  2.833   -0.504  1.00 25.23 ?  111 LYS A CE    1 
ATOM   848   N  NZ    . LYS A 1 111 ? 20.659  3.901   0.465   1.00 26.89 1  111 LYS A NZ    1 
ATOM   849   N  N     . ALA A 1 112 ? 25.936  2.120   -4.726  1.00 26.53 ?  112 ALA A N     1 
ATOM   850   C  CA    . ALA A 1 112 ? 27.182  1.427   -5.013  1.00 27.42 ?  112 ALA A CA    1 
ATOM   851   C  C     . ALA A 1 112 ? 28.187  2.378   -5.660  1.00 26.36 ?  112 ALA A C     1 
ATOM   852   O  O     . ALA A 1 112 ? 29.380  2.087   -5.685  1.00 28.35 ?  112 ALA A O     1 
ATOM   853   C  CB    . ALA A 1 112 ? 26.920  0.214   -5.879  1.00 27.53 ?  112 ALA A CB    1 
ATOM   854   N  N     . GLU A 1 113 ? 27.705  3.515   -6.176  1.00 24.97 ?  113 GLU A N     1 
ATOM   855   C  CA    . GLU A 1 113 ? 28.591  4.508   -6.766  1.00 24.03 ?  113 GLU A CA    1 
ATOM   856   C  C     . GLU A 1 113 ? 28.848  5.627   -5.759  1.00 22.31 ?  113 GLU A C     1 
ATOM   857   O  O     . GLU A 1 113 ? 29.538  6.597   -6.066  1.00 21.98 ?  113 GLU A O     1 
ATOM   858   C  CB    . GLU A 1 113 ? 28.036  5.050   -8.084  1.00 28.48 ?  113 GLU A CB    1 
ATOM   859   C  CG    . GLU A 1 113 ? 27.788  3.955   -9.117  1.00 30.11 ?  113 GLU A CG    1 
ATOM   860   C  CD    . GLU A 1 113 ? 27.475  4.445   -10.519 1.00 31.48 ?  113 GLU A CD    1 
ATOM   861   O  OE1   . GLU A 1 113 ? 27.706  5.639   -10.804 1.00 34.01 ?  113 GLU A OE1   1 
ATOM   862   O  OE2   . GLU A 1 113 ? 26.987  3.624   -11.324 1.00 34.26 -1 113 GLU A OE2   1 
ATOM   863   N  N     . GLY A 1 114 ? 28.285  5.480   -4.555  1.00 21.53 ?  114 GLY A N     1 
ATOM   864   C  CA    . GLY A 1 114 ? 28.582  6.380   -3.452  1.00 21.28 ?  114 GLY A CA    1 
ATOM   865   C  C     . GLY A 1 114 ? 27.697  7.624   -3.457  1.00 19.21 ?  114 GLY A C     1 
ATOM   866   O  O     . GLY A 1 114 ? 28.053  8.636   -2.860  1.00 16.59 ?  114 GLY A O     1 
ATOM   867   N  N     . PHE A 1 115 ? 26.541  7.540   -4.127  1.00 19.20 ?  115 PHE A N     1 
ATOM   868   C  CA    . PHE A 1 115 ? 25.574  8.626   -4.122  1.00 17.23 ?  115 PHE A CA    1 
ATOM   869   C  C     . PHE A 1 115 ? 24.496  8.335   -3.088  1.00 17.86 ?  115 PHE A C     1 
ATOM   870   O  O     . PHE A 1 115 ? 24.218  7.178   -2.777  1.00 21.22 ?  115 PHE A O     1 
ATOM   871   C  CB    . PHE A 1 115 ? 24.953  8.822   -5.507  1.00 15.75 ?  115 PHE A CB    1 
ATOM   872   C  CG    . PHE A 1 115 ? 25.992  9.224   -6.541  1.00 15.53 ?  115 PHE A CG    1 
ATOM   873   C  CD1   . PHE A 1 115 ? 26.877  10.264  -6.283  1.00 16.61 ?  115 PHE A CD1   1 
ATOM   874   C  CD2   . PHE A 1 115 ? 26.128  8.521   -7.730  1.00 14.04 ?  115 PHE A CD2   1 
ATOM   875   C  CE1   . PHE A 1 115 ? 27.841  10.617  -7.210  1.00 17.21 ?  115 PHE A CE1   1 
ATOM   876   C  CE2   . PHE A 1 115 ? 27.097  8.876   -8.653  1.00 15.52 ?  115 PHE A CE2   1 
ATOM   877   C  CZ    . PHE A 1 115 ? 27.952  9.921   -8.391  1.00 16.73 ?  115 PHE A CZ    1 
ATOM   878   N  N     . SER A 1 116 ? 23.902  9.410   -2.563  1.00 14.84 ?  116 SER A N     1 
ATOM   879   C  CA    . SER A 1 116 ? 22.773  9.303   -1.659  1.00 16.41 ?  116 SER A CA    1 
ATOM   880   C  C     . SER A 1 116 ? 21.524  8.971   -2.467  1.00 15.57 ?  116 SER A C     1 
ATOM   881   O  O     . SER A 1 116 ? 21.239  9.612   -3.476  1.00 13.50 ?  116 SER A O     1 
ATOM   882   C  CB    . SER A 1 116 ? 22.582  10.569  -0.863  1.00 19.53 ?  116 SER A CB    1 
ATOM   883   O  OG    . SER A 1 116 ? 21.556  10.410  0.108   1.00 23.03 ?  116 SER A OG    1 
ATOM   884   N  N     . ALA A 1 117 ? 20.793  7.956   -2.008  1.00 15.45 ?  117 ALA A N     1 
ATOM   885   C  CA    . ALA A 1 117 ? 19.589  7.518   -2.687  1.00 15.56 ?  117 ALA A CA    1 
ATOM   886   C  C     . ALA A 1 117 ? 18.624  6.946   -1.660  1.00 14.84 ?  117 ALA A C     1 
ATOM   887   O  O     . ALA A 1 117 ? 19.033  6.244   -0.737  1.00 14.54 ?  117 ALA A O     1 
ATOM   888   C  CB    . ALA A 1 117 ? 19.934  6.503   -3.753  1.00 16.28 ?  117 ALA A CB    1 
ATOM   889   N  N     . LYS A 1 118 ? 17.341  7.267   -1.827  1.00 13.91 ?  118 LYS A N     1 
ATOM   890   C  CA    . LYS A 1 118 ? 16.318  6.695   -0.975  1.00 15.01 ?  118 LYS A CA    1 
ATOM   891   C  C     . LYS A 1 118 ? 14.982  6.675   -1.706  1.00 13.97 ?  118 LYS A C     1 
ATOM   892   O  O     . LYS A 1 118 ? 14.817  7.297   -2.753  1.00 13.95 ?  118 LYS A O     1 
ATOM   893   C  CB    . LYS A 1 118 ? 16.237  7.466   0.345   1.00 18.77 ?  118 LYS A CB    1 
ATOM   894   C  CG    . LYS A 1 118 ? 16.062  8.967   0.212   1.00 18.28 ?  118 LYS A CG    1 
ATOM   895   C  CD    . LYS A 1 118 ? 15.810  9.598   1.573   1.00 23.41 ?  118 LYS A CD    1 
ATOM   896   C  CE    . LYS A 1 118 ? 16.912  9.276   2.528   1.00 24.23 ?  118 LYS A CE    1 
ATOM   897   N  NZ    . LYS A 1 118 ? 18.175  9.867   2.078   1.00 29.25 1  118 LYS A NZ    1 
ATOM   898   N  N     . MET A 1 119 ? 14.047  5.922   -1.126  1.00 17.07 ?  119 MET A N     1 
ATOM   899   C  CA    . MET A 1 119 ? 12.715  5.749   -1.673  1.00 19.73 ?  119 MET A CA    1 
ATOM   900   C  C     . MET A 1 119 ? 11.706  6.297   -0.671  1.00 19.76 ?  119 MET A C     1 
ATOM   901   O  O     . MET A 1 119 ? 11.797  6.006   0.520   1.00 20.85 ?  119 MET A O     1 
ATOM   902   C  CB    . MET A 1 119 ? 12.425  4.264   -1.926  1.00 21.18 ?  119 MET A CB    1 
ATOM   903   C  CG    . MET A 1 119 ? 11.070  3.995   -2.558  1.00 21.54 ?  119 MET A CG    1 
ATOM   904   S  SD    . MET A 1 119 ? 10.790  2.246   -2.899  1.00 23.58 ?  119 MET A SD    1 
ATOM   905   C  CE    . MET A 1 119 ? 12.048  2.012   -4.163  1.00 23.84 ?  119 MET A CE    1 
ATOM   906   N  N     . GLU A 1 120 ? 10.762  7.103   -1.166  1.00 19.01 ?  120 GLU A N     1 
ATOM   907   C  CA    . GLU A 1 120 ? 9.652   7.575   -0.356  1.00 17.59 ?  120 GLU A CA    1 
ATOM   908   C  C     . GLU A 1 120 ? 8.405   6.782   -0.729  1.00 15.57 ?  120 GLU A C     1 
ATOM   909   O  O     . GLU A 1 120 ? 7.983   6.790   -1.884  1.00 14.14 ?  120 GLU A O     1 
ATOM   910   C  CB    . GLU A 1 120 ? 9.376   9.066   -0.550  1.00 17.03 ?  120 GLU A CB    1 
ATOM   911   C  CG    . GLU A 1 120 ? 10.462  9.965   0.031   1.00 18.23 ?  120 GLU A CG    1 
ATOM   912   C  CD    . GLU A 1 120 ? 10.648  9.812   1.529   1.00 19.75 ?  120 GLU A CD    1 
ATOM   913   O  OE1   . GLU A 1 120 ? 9.742   9.243   2.175   1.00 24.41 ?  120 GLU A OE1   1 
ATOM   914   O  OE2   . GLU A 1 120 ? 11.704  10.240  2.043   1.00 22.92 -1 120 GLU A OE2   1 
ATOM   915   N  N     . PRO A 1 121 ? 7.770   6.086   0.238   1.00 12.55 ?  121 PRO A N     1 
ATOM   916   C  CA    . PRO A 1 121 ? 6.587   5.284   -0.064  1.00 14.36 ?  121 PRO A CA    1 
ATOM   917   C  C     . PRO A 1 121 ? 5.490   6.166   -0.655  1.00 14.90 ?  121 PRO A C     1 
ATOM   918   O  O     . PRO A 1 121 ? 5.469   7.377   -0.448  1.00 14.79 ?  121 PRO A O     1 
ATOM   919   C  CB    . PRO A 1 121 ? 6.201   4.661   1.288   1.00 14.24 ?  121 PRO A CB    1 
ATOM   920   C  CG    . PRO A 1 121 ? 6.845   5.570   2.315   1.00 14.17 ?  121 PRO A CG    1 
ATOM   921   C  CD    . PRO A 1 121 ? 8.126   6.068   1.665   1.00 13.21 ?  121 PRO A CD    1 
ATOM   922   N  N     . GLY A 1 122 ? 4.598   5.532   -1.418  1.00 16.01 ?  122 GLY A N     1 
ATOM   923   C  CA    . GLY A 1 122 ? 3.469   6.210   -2.029  1.00 15.09 ?  122 GLY A CA    1 
ATOM   924   C  C     . GLY A 1 122 ? 2.239   5.312   -1.972  1.00 15.25 ?  122 GLY A C     1 
ATOM   925   O  O     . GLY A 1 122 ? 2.288   4.236   -1.379  1.00 13.33 ?  122 GLY A O     1 
ATOM   926   N  N     . ILE A 1 123 ? 1.145   5.761   -2.592  1.00 14.25 ?  123 ILE A N     1 
ATOM   927   C  CA    . ILE A 1 123 ? -0.104  5.020   -2.570  1.00 15.68 ?  123 ILE A CA    1 
ATOM   928   C  C     . ILE A 1 123 ? -0.171  4.155   -3.828  1.00 16.38 ?  123 ILE A C     1 
ATOM   929   O  O     . ILE A 1 123 ? 0.029   4.654   -4.934  1.00 18.03 ?  123 ILE A O     1 
ATOM   930   C  CB    . ILE A 1 123 ? -1.294  5.991   -2.435  1.00 16.44 ?  123 ILE A CB    1 
ATOM   931   C  CG1   . ILE A 1 123 ? -1.293  6.686   -1.063  1.00 16.64 ?  123 ILE A CG1   1 
ATOM   932   C  CG2   . ILE A 1 123 ? -2.621  5.283   -2.707  1.00 16.31 ?  123 ILE A CG2   1 
ATOM   933   C  CD1   . ILE A 1 123 ? -2.316  7.799   -0.915  1.00 16.71 ?  123 ILE A CD1   1 
ATOM   934   N  N     . SER A 1 124 ? -0.437  2.855   -3.649  1.00 16.01 ?  124 SER A N     1 
ATOM   935   C  CA    . SER A 1 124 ? -0.369  1.895   -4.741  1.00 17.04 ?  124 SER A CA    1 
ATOM   936   C  C     . SER A 1 124 ? -1.769  1.466   -5.176  1.00 16.87 ?  124 SER A C     1 
ATOM   937   O  O     . SER A 1 124 ? -2.755  1.768   -4.508  1.00 15.57 ?  124 SER A O     1 
ATOM   938   C  CB    . SER A 1 124 ? 0.451   0.692   -4.356  1.00 16.31 ?  124 SER A CB    1 
ATOM   939   O  OG    . SER A 1 124 ? -0.217  -0.070  -3.360  1.00 15.27 ?  124 SER A OG    1 
ATOM   940   N  N     . ALA A 1 125 ? -1.826  0.731   -6.293  1.00 17.49 ?  125 ALA A N     1 
ATOM   941   C  CA    . ALA A 1 125 ? -3.079  0.240   -6.845  1.00 17.29 ?  125 ALA A CA    1 
ATOM   942   C  C     . ALA A 1 125 ? -3.748  -0.714  -5.859  1.00 17.20 ?  125 ALA A C     1 
ATOM   943   O  O     . ALA A 1 125 ? -4.961  -0.904  -5.899  1.00 19.34 ?  125 ALA A O     1 
ATOM   944   C  CB    . ALA A 1 125 ? -2.828  -0.432  -8.179  1.00 15.51 ?  125 ALA A CB    1 
ATOM   945   N  N     . GLU A 1 126 ? -2.935  -1.311  -4.981  1.00 18.22 ?  126 GLU A N     1 
ATOM   946   C  CA    . GLU A 1 126 ? -3.410  -2.254  -3.983  1.00 18.29 ?  126 GLU A CA    1 
ATOM   947   C  C     . GLU A 1 126 ? -4.043  -1.493  -2.822  1.00 16.51 ?  126 GLU A C     1 
ATOM   948   O  O     . GLU A 1 126 ? -5.091  -1.881  -2.306  1.00 14.44 ?  126 GLU A O     1 
ATOM   949   C  CB    . GLU A 1 126 ? -2.226  -3.074  -3.476  1.00 20.88 ?  126 GLU A CB    1 
ATOM   950   C  CG    . GLU A 1 126 ? -2.628  -4.234  -2.573  1.00 21.95 ?  126 GLU A CG    1 
ATOM   951   C  CD    . GLU A 1 126 ? -1.479  -4.768  -1.738  1.00 23.05 ?  126 GLU A CD    1 
ATOM   952   O  OE1   . GLU A 1 126 ? -0.391  -5.005  -2.302  1.00 23.98 ?  126 GLU A OE1   1 
ATOM   953   O  OE2   . GLU A 1 126 ? -1.677  -4.951  -0.520  1.00 33.71 -1 126 GLU A OE2   1 
ATOM   954   N  N     . ALA A 1 127 ? -3.371  -0.417  -2.405  1.00 15.08 ?  127 ALA A N     1 
ATOM   955   C  CA    . ALA A 1 127 ? -3.934  0.519   -1.448  1.00 14.82 ?  127 ALA A CA    1 
ATOM   956   C  C     . ALA A 1 127 ? -5.314  0.955   -1.934  1.00 14.38 ?  127 ALA A C     1 
ATOM   957   O  O     . ALA A 1 127 ? -6.278  0.964   -1.172  1.00 14.71 ?  127 ALA A O     1 
ATOM   958   C  CB    . ALA A 1 127 ? -2.998  1.697   -1.279  1.00 13.69 ?  127 ALA A CB    1 
ATOM   959   N  N     . CYS A 1 128 ? -5.390  1.289   -3.226  1.00 14.27 ?  128 CYS A N     1 
ATOM   960   C  CA    . CYS A 1 128 ? -6.613  1.772   -3.848  1.00 14.82 ?  128 CYS A CA    1 
ATOM   961   C  C     . CYS A 1 128 ? -7.707  0.704   -3.802  1.00 16.10 ?  128 CYS A C     1 
ATOM   962   O  O     . CYS A 1 128 ? -8.866  1.022   -3.539  1.00 14.37 ?  128 CYS A O     1 
ATOM   963   C  CB    . CYS A 1 128 ? -6.328  2.242   -5.270  1.00 15.93 ?  128 CYS A CB    1 
ATOM   964   S  SG    . CYS A 1 128 ? -5.412  3.806   -5.340  1.00 17.85 ?  128 CYS A SG    1 
ATOM   965   N  N     . LEU A 1 129 ? -7.332  -0.557  -4.054  1.00 17.11 ?  129 LEU A N     1 
ATOM   966   C  CA    . LEU A 1 129 ? -8.280  -1.658  -4.143  1.00 15.68 ?  129 LEU A CA    1 
ATOM   967   C  C     . LEU A 1 129 ? -9.032  -1.815  -2.820  1.00 17.02 ?  129 LEU A C     1 
ATOM   968   O  O     . LEU A 1 129 ? -10.248 -1.646  -2.771  1.00 19.30 ?  129 LEU A O     1 
ATOM   969   C  CB    . LEU A 1 129 ? -7.516  -2.920  -4.550  1.00 16.68 ?  129 LEU A CB    1 
ATOM   970   C  CG    . LEU A 1 129 ? -8.342  -4.189  -4.789  1.00 15.19 ?  129 LEU A CG    1 
ATOM   971   C  CD1   . LEU A 1 129 ? -7.669  -5.079  -5.823  1.00 15.79 ?  129 LEU A CD1   1 
ATOM   972   C  CD2   . LEU A 1 129 ? -8.548  -4.961  -3.501  1.00 15.88 ?  129 LEU A CD2   1 
ATOM   973   N  N     . TRP A 1 130 ? -8.299  -2.130  -1.747  1.00 16.98 ?  130 TRP A N     1 
ATOM   974   C  CA    . TRP A 1 130 ? -8.876  -2.271  -0.418  1.00 19.28 ?  130 TRP A CA    1 
ATOM   975   C  C     . TRP A 1 130 ? -10.004 -1.263  -0.198  1.00 20.08 ?  130 TRP A C     1 
ATOM   976   O  O     . TRP A 1 130 ? -11.071 -1.623  0.294   1.00 19.69 ?  130 TRP A O     1 
ATOM   977   C  CB    . TRP A 1 130 ? -7.785  -2.094  0.646   1.00 20.71 ?  130 TRP A CB    1 
ATOM   978   C  CG    . TRP A 1 130 ? -6.602  -3.007  0.465   1.00 22.70 ?  130 TRP A CG    1 
ATOM   979   C  CD1   . TRP A 1 130 ? -5.289  -2.672  0.623   1.00 21.72 ?  130 TRP A CD1   1 
ATOM   980   C  CD2   . TRP A 1 130 ? -6.620  -4.406  0.104   1.00 24.04 ?  130 TRP A CD2   1 
ATOM   981   N  NE1   . TRP A 1 130 ? -4.489  -3.755  0.377   1.00 24.52 ?  130 TRP A NE1   1 
ATOM   982   C  CE2   . TRP A 1 130 ? -5.274  -4.832  0.059   1.00 24.74 ?  130 TRP A CE2   1 
ATOM   983   C  CE3   . TRP A 1 130 ? -7.627  -5.333  -0.186  1.00 26.38 ?  130 TRP A CE3   1 
ATOM   984   C  CZ2   . TRP A 1 130 ? -4.918  -6.139  -0.262  1.00 26.02 ?  130 TRP A CZ2   1 
ATOM   985   C  CZ3   . TRP A 1 130 ? -7.272  -6.627  -0.501  1.00 27.55 ?  130 TRP A CZ3   1 
ATOM   986   C  CH2   . TRP A 1 130 ? -5.936  -7.022  -0.539  1.00 24.86 ?  130 TRP A CH2   1 
ATOM   987   N  N     . ALA A 1 131 ? -9.740  0.003   -0.543  1.00 19.66 ?  131 ALA A N     1 
ATOM   988   C  CA    . ALA A 1 131 ? -10.660 1.099   -0.280  1.00 19.70 ?  131 ALA A CA    1 
ATOM   989   C  C     . ALA A 1 131 ? -11.878 1.012   -1.197  1.00 22.83 ?  131 ALA A C     1 
ATOM   990   O  O     . ALA A 1 131 ? -13.011 1.154   -0.745  1.00 25.82 ?  131 ALA A O     1 
ATOM   991   C  CB    . ALA A 1 131 ? -9.940  2.419   -0.451  1.00 19.42 ?  131 ALA A CB    1 
ATOM   992   N  N     . ASP A 1 132 ? -11.631 0.777   -2.489  1.00 23.66 ?  132 ASP A N     1 
ATOM   993   C  CA    . ASP A 1 132 ? -12.686 0.830   -3.487  1.00 22.40 ?  132 ASP A CA    1 
ATOM   994   C  C     . ASP A 1 132 ? -13.650 -0.340  -3.311  1.00 22.81 ?  132 ASP A C     1 
ATOM   995   O  O     . ASP A 1 132 ? -14.840 -0.198  -3.586  1.00 25.69 ?  132 ASP A O     1 
ATOM   996   C  CB    . ASP A 1 132 ? -12.112 0.913   -4.892  1.00 22.14 ?  132 ASP A CB    1 
ATOM   997   C  CG    . ASP A 1 132 ? -11.427 2.230   -5.222  1.00 20.97 ?  132 ASP A CG    1 
ATOM   998   O  OD1   . ASP A 1 132 ? -11.513 3.157   -4.390  1.00 25.27 ?  132 ASP A OD1   1 
ATOM   999   O  OD2   . ASP A 1 132 ? -10.809 2.315   -6.303  1.00 19.83 -1 132 ASP A OD2   1 
ATOM   1000  N  N     . LEU A 1 133 ? -13.145 -1.493  -2.855  1.00 20.25 ?  133 LEU A N     1 
ATOM   1001  C  CA    . LEU A 1 133 ? -14.005 -2.649  -2.658  1.00 21.38 ?  133 LEU A CA    1 
ATOM   1002  C  C     . LEU A 1 133 ? -14.236 -2.879  -1.169  1.00 23.36 ?  133 LEU A C     1 
ATOM   1003  O  O     . LEU A 1 133 ? -14.645 -3.966  -0.765  1.00 23.51 ?  133 LEU A O     1 
ATOM   1004  C  CB    . LEU A 1 133 ? -13.442 -3.904  -3.320  1.00 22.62 ?  133 LEU A CB    1 
ATOM   1005  C  CG    . LEU A 1 133 ? -13.278 -3.827  -4.839  1.00 22.00 ?  133 LEU A CG    1 
ATOM   1006  C  CD1   . LEU A 1 133 ? -11.971 -3.140  -5.182  1.00 24.12 ?  133 LEU A CD1   1 
ATOM   1007  C  CD2   . LEU A 1 133 ? -13.366 -5.203  -5.469  1.00 26.72 ?  133 LEU A CD2   1 
ATOM   1008  N  N     . GLY A 1 134 ? -13.972 -1.846  -0.365  1.00 22.98 ?  134 GLY A N     1 
ATOM   1009  C  CA    . GLY A 1 134 ? -14.258 -1.896  1.058   1.00 22.44 ?  134 GLY A CA    1 
ATOM   1010  C  C     . GLY A 1 134 ? -13.835 -3.234  1.657   1.00 22.94 ?  134 GLY A C     1 
ATOM   1011  O  O     . GLY A 1 134 ? -14.631 -3.903  2.313   1.00 20.44 ?  134 GLY A O     1 
ATOM   1012  N  N     . ILE A 1 135 ? -12.572 -3.600  1.410   1.00 28.09 ?  135 ILE A N     1 
ATOM   1013  C  CA    . ILE A 1 135 ? -11.983 -4.831  1.915   1.00 25.88 ?  135 ILE A CA    1 
ATOM   1014  C  C     . ILE A 1 135 ? -10.766 -4.496  2.773   1.00 29.51 ?  135 ILE A C     1 
ATOM   1015  O  O     . ILE A 1 135 ? -9.846  -3.821  2.316   1.00 29.87 ?  135 ILE A O     1 
ATOM   1016  C  CB    . ILE A 1 135 ? -11.565 -5.759  0.760   1.00 27.22 ?  135 ILE A CB    1 
ATOM   1017  C  CG1   . ILE A 1 135 ? -12.736 -6.120  -0.152  1.00 27.72 ?  135 ILE A CG1   1 
ATOM   1018  C  CG2   . ILE A 1 135 ? -10.862 -7.004  1.301   1.00 29.82 ?  135 ILE A CG2   1 
ATOM   1019  C  CD1   . ILE A 1 135 ? -12.321 -6.853  -1.415  1.00 27.56 ?  135 ILE A CD1   1 
ATOM   1020  N  N     . ASP A 1 136 ? -10.760 -5.006  4.009   1.00 29.26 ?  136 ASP A N     1 
ATOM   1021  C  CA    . ASP A 1 136 ? -9.594  -4.935  4.874   1.00 32.14 ?  136 ASP A CA    1 
ATOM   1022  C  C     . ASP A 1 136 ? -8.700  -6.144  4.604   1.00 32.77 ?  136 ASP A C     1 
ATOM   1023  O  O     . ASP A 1 136 ? -9.097  -7.278  4.861   1.00 26.76 ?  136 ASP A O     1 
ATOM   1024  C  CB    . ASP A 1 136 ? -10.016 -4.873  6.334   1.00 35.25 ?  136 ASP A CB    1 
ATOM   1025  C  CG    . ASP A 1 136 ? -8.887  -4.783  7.350   1.00 36.60 ?  136 ASP A CG    1 
ATOM   1026  O  OD1   . ASP A 1 136 ? -7.710  -4.821  6.929   1.00 35.94 ?  136 ASP A OD1   1 
ATOM   1027  O  OD2   . ASP A 1 136 ? -9.195  -4.674  8.556   1.00 34.85 -1 136 ASP A OD2   1 
ATOM   1028  N  N     . PRO A 1 137 ? -7.468  -5.952  4.076   1.00 32.98 ?  137 PRO A N     1 
ATOM   1029  C  CA    . PRO A 1 137 ? -6.563  -7.074  3.818   1.00 30.65 ?  137 PRO A CA    1 
ATOM   1030  C  C     . PRO A 1 137 ? -6.321  -7.943  5.050   1.00 35.18 ?  137 PRO A C     1 
ATOM   1031  O  O     . PRO A 1 137 ? -5.852  -9.073  4.931   1.00 37.69 ?  137 PRO A O     1 
ATOM   1032  C  CB    . PRO A 1 137 ? -5.263  -6.414  3.313   1.00 30.27 ?  137 PRO A CB    1 
ATOM   1033  C  CG    . PRO A 1 137 ? -5.404  -4.945  3.664   1.00 30.06 ?  137 PRO A CG    1 
ATOM   1034  C  CD    . PRO A 1 137 ? -6.895  -4.657  3.680   1.00 28.56 ?  137 PRO A CD    1 
ATOM   1035  N  N     . GLY A 1 138 ? -6.647  -7.406  6.230   1.00 33.83 ?  138 GLY A N     1 
ATOM   1036  C  CA    . GLY A 1 138 ? -6.459  -8.128  7.477   1.00 35.74 ?  138 GLY A CA    1 
ATOM   1037  C  C     . GLY A 1 138 ? -7.569  -9.151  7.707   1.00 32.70 ?  138 GLY A C     1 
ATOM   1038  O  O     . GLY A 1 138 ? -7.362  -10.152 8.389   1.00 30.90 ?  138 GLY A O     1 
ATOM   1039  N  N     . ASN A 1 139 ? -8.743  -8.887  7.124   1.00 33.99 ?  139 ASN A N     1 
ATOM   1040  C  CA    . ASN A 1 139 ? -9.928  -9.685  7.392   1.00 35.03 ?  139 ASN A CA    1 
ATOM   1041  C  C     . ASN A 1 139 ? -9.549  -11.162 7.325   1.00 26.94 ?  139 ASN A C     1 
ATOM   1042  O  O     . ASN A 1 139 ? -9.607  -11.862 8.332   1.00 24.24 ?  139 ASN A O     1 
ATOM   1043  C  CB    . ASN A 1 139 ? -11.078 -9.312  6.462   1.00 37.61 ?  139 ASN A CB    1 
ATOM   1044  C  CG    . ASN A 1 139 ? -12.419 -9.730  7.017   1.00 36.38 ?  139 ASN A CG    1 
ATOM   1045  O  OD1   . ASN A 1 139 ? -12.762 -9.373  8.149   1.00 47.78 ?  139 ASN A OD1   1 
ATOM   1046  N  ND2   . ASN A 1 139 ? -13.191 -10.476 6.241   1.00 32.87 ?  139 ASN A ND2   1 
ATOM   1047  N  N     . SER A 1 140 ? -9.143  -11.629 6.140   1.00 26.97 ?  140 SER A N     1 
ATOM   1048  C  CA    . SER A 1 140 ? -8.701  -13.007 5.995   1.00 24.60 ?  140 SER A CA    1 
ATOM   1049  C  C     . SER A 1 140 ? -7.307  -13.064 5.376   1.00 21.46 ?  140 SER A C     1 
ATOM   1050  O  O     . SER A 1 140 ? -6.863  -14.129 4.955   1.00 24.77 ?  140 SER A O     1 
ATOM   1051  C  CB    . SER A 1 140 ? -9.689  -13.820 5.198   1.00 22.71 ?  140 SER A CB    1 
ATOM   1052  O  OG    . SER A 1 140 ? -9.923  -13.238 3.923   1.00 23.06 ?  140 SER A OG    1 
ATOM   1053  N  N     . GLY A 1 141 ? -6.616  -11.919 5.338   1.00 17.77 ?  141 GLY A N     1 
ATOM   1054  C  CA    . GLY A 1 141 ? -5.252  -11.869 4.837   1.00 19.80 ?  141 GLY A CA    1 
ATOM   1055  C  C     . GLY A 1 141 ? -5.206  -11.757 3.314   1.00 18.90 ?  141 GLY A C     1 
ATOM   1056  O  O     . GLY A 1 141 ? -6.233  -11.845 2.645   1.00 17.84 ?  141 GLY A O     1 
ATOM   1057  N  N     . HIS A 1 142 ? -3.985  -11.622 2.783   1.00 20.14 ?  142 HIS A N     1 
ATOM   1058  C  CA    . HIS A 1 142 ? -3.754  -11.041 1.470   1.00 21.60 ?  142 HIS A CA    1 
ATOM   1059  C  C     . HIS A 1 142 ? -2.539  -11.674 0.793   1.00 21.27 ?  142 HIS A C     1 
ATOM   1060  O  O     . HIS A 1 142 ? -1.525  -11.918 1.442   1.00 20.23 ?  142 HIS A O     1 
ATOM   1061  C  CB    . HIS A 1 142 ? -3.518  -9.535  1.630   1.00 23.52 ?  142 HIS A CB    1 
ATOM   1062  C  CG    . HIS A 1 142 ? -2.743  -8.916  0.520   1.00 27.37 ?  142 HIS A CG    1 
ATOM   1063  N  ND1   . HIS A 1 142 ? -1.802  -7.932  0.735   1.00 30.77 ?  142 HIS A ND1   1 
ATOM   1064  C  CD2   . HIS A 1 142 ? -2.752  -9.140  -0.799  1.00 29.71 ?  142 HIS A CD2   1 
ATOM   1065  C  CE1   . HIS A 1 142 ? -1.271  -7.577  -0.425  1.00 33.40 ?  142 HIS A CE1   1 
ATOM   1066  N  NE2   . HIS A 1 142 ? -1.834  -8.298  -1.371  1.00 32.63 ?  142 HIS A NE2   1 
ATOM   1067  N  N     . GLN A 1 143 ? -2.641  -11.904 -0.523  1.00 23.95 ?  143 GLN A N     1 
ATOM   1068  C  CA    . GLN A 1 143 ? -1.525  -12.406 -1.311  1.00 26.28 ?  143 GLN A CA    1 
ATOM   1069  C  C     . GLN A 1 143 ? -1.443  -11.670 -2.648  1.00 21.59 ?  143 GLN A C     1 
ATOM   1070  O  O     . GLN A 1 143 ? -2.464  -11.412 -3.282  1.00 22.16 ?  143 GLN A O     1 
ATOM   1071  C  CB    . GLN A 1 143 ? -1.673  -13.894 -1.624  1.00 30.07 ?  143 GLN A CB    1 
ATOM   1072  C  CG    . GLN A 1 143 ? -1.776  -14.795 -0.399  1.00 36.27 ?  143 GLN A CG    1 
ATOM   1073  C  CD    . GLN A 1 143 ? -2.154  -16.215 -0.757  1.00 38.32 ?  143 GLN A CD    1 
ATOM   1074  O  OE1   . GLN A 1 143 ? -1.383  -17.162 -0.558  1.00 43.64 ?  143 GLN A OE1   1 
ATOM   1075  N  NE2   . GLN A 1 143 ? -3.347  -16.372 -1.311  1.00 39.17 ?  143 GLN A NE2   1 
ATOM   1076  N  N     . SER A 1 144 ? -0.212  -11.374 -3.080  1.00 18.45 ?  144 SER A N     1 
ATOM   1077  C  CA    . SER A 1 144 ? 0.033   -10.727 -4.360  1.00 17.66 ?  144 SER A CA    1 
ATOM   1078  C  C     . SER A 1 144 ? 1.078   -11.498 -5.161  1.00 17.22 ?  144 SER A C     1 
ATOM   1079  O  O     . SER A 1 144 ? 2.091   -11.930 -4.617  1.00 22.08 ?  144 SER A O     1 
ATOM   1080  C  CB    . SER A 1 144 ? 0.474   -9.296  -4.180  1.00 16.76 ?  144 SER A CB    1 
ATOM   1081  O  OG    . SER A 1 144 ? -0.633  -8.430  -3.978  1.00 17.80 ?  144 SER A OG    1 
ATOM   1082  N  N     . PHE A 1 145 ? 0.828   -11.638 -6.467  1.00 16.17 ?  145 PHE A N     1 
ATOM   1083  C  CA    . PHE A 1 145 ? 1.837   -12.133 -7.387  1.00 15.67 ?  145 PHE A CA    1 
ATOM   1084  C  C     . PHE A 1 145 ? 1.657   -11.472 -8.749  1.00 16.99 ?  145 PHE A C     1 
ATOM   1085  O  O     . PHE A 1 145 ? 0.535   -11.217 -9.183  1.00 17.77 ?  145 PHE A O     1 
ATOM   1086  C  CB    . PHE A 1 145 ? 1.785   -13.636 -7.679  1.00 14.19 ?  145 PHE A CB    1 
ATOM   1087  C  CG    . PHE A 1 145 ? 1.754   -14.569 -6.477  1.00 14.43 ?  145 PHE A CG    1 
ATOM   1088  C  CD1   . PHE A 1 145 ? 2.930   -14.988 -5.863  1.00 13.97 ?  145 PHE A CD1   1 
ATOM   1089  C  CD2   . PHE A 1 145 ? 0.547   -15.065 -5.999  1.00 13.47 ?  145 PHE A CD2   1 
ATOM   1090  C  CE1   . PHE A 1 145 ? 2.892   -15.856 -4.783  1.00 13.25 ?  145 PHE A CE1   1 
ATOM   1091  C  CE2   . PHE A 1 145 ? 0.515   -15.930 -4.918  1.00 13.40 ?  145 PHE A CE2   1 
ATOM   1092  C  CZ    . PHE A 1 145 ? 1.686   -16.325 -4.314  1.00 13.52 ?  145 PHE A CZ    1 
ATOM   1093  N  N     . GLU A 1 146 ? 2.784   -11.235 -9.424  1.00 17.47 ?  146 GLU A N     1 
ATOM   1094  C  CA    . GLU A 1 146 ? 2.773   -10.932 -10.844 1.00 17.41 ?  146 GLU A CA    1 
ATOM   1095  C  C     . GLU A 1 146 ? 2.222   -12.153 -11.580 1.00 18.92 ?  146 GLU A C     1 
ATOM   1096  O  O     . GLU A 1 146 ? 2.596   -13.284 -11.280 1.00 19.32 ?  146 GLU A O     1 
ATOM   1097  C  CB    . GLU A 1 146 ? 4.188   -10.538 -11.266 1.00 18.67 ?  146 GLU A CB    1 
ATOM   1098  C  CG    . GLU A 1 146 ? 4.232   -9.675  -12.523 1.00 18.43 ?  146 GLU A CG    1 
ATOM   1099  C  CD    . GLU A 1 146 ? 4.150   -10.436 -13.831 1.00 20.94 ?  146 GLU A CD    1 
ATOM   1100  O  OE1   . GLU A 1 146 ? 4.284   -11.679 -13.813 1.00 22.53 ?  146 GLU A OE1   1 
ATOM   1101  O  OE2   . GLU A 1 146 ? 3.946   -9.778  -14.873 1.00 20.50 -1 146 GLU A OE2   1 
ATOM   1102  N  N     . ALA A 1 147 ? 1.327   -11.905 -12.543 1.00 19.00 ?  147 ALA A N     1 
ATOM   1103  C  CA    . ALA A 1 147 ? 0.496   -12.941 -13.138 1.00 20.67 ?  147 ALA A CA    1 
ATOM   1104  C  C     . ALA A 1 147 ? 1.337   -13.957 -13.907 1.00 21.13 ?  147 ALA A C     1 
ATOM   1105  O  O     . ALA A 1 147 ? 1.016   -15.144 -13.934 1.00 21.75 ?  147 ALA A O     1 
ATOM   1106  C  CB    . ALA A 1 147 ? -0.534  -12.296 -14.039 1.00 20.56 ?  147 ALA A CB    1 
ATOM   1107  N  N     . SER A 1 148 ? 2.405   -13.473 -14.547 1.00 22.28 ?  148 SER A N     1 
ATOM   1108  C  CA    . SER A 1 148 ? 3.239   -14.303 -15.401 1.00 23.93 ?  148 SER A CA    1 
ATOM   1109  C  C     . SER A 1 148 ? 4.164   -15.172 -14.553 1.00 24.87 ?  148 SER A C     1 
ATOM   1110  O  O     . SER A 1 148 ? 4.386   -16.340 -14.866 1.00 21.05 ?  148 SER A O     1 
ATOM   1111  C  CB    . SER A 1 148 ? 4.013   -13.455 -16.378 1.00 26.39 ?  148 SER A CB    1 
ATOM   1112  O  OG    . SER A 1 148 ? 3.167   -12.980 -17.417 1.00 27.74 ?  148 SER A OG    1 
ATOM   1113  N  N     . GLN A 1 149 ? 4.698   -14.585 -13.477 1.00 24.33 ?  149 GLN A N     1 
ATOM   1114  C  CA    . GLN A 1 149 ? 5.557   -15.306 -12.553 1.00 23.36 ?  149 GLN A CA    1 
ATOM   1115  C  C     . GLN A 1 149 ? 4.748   -16.414 -11.888 1.00 22.47 ?  149 GLN A C     1 
ATOM   1116  O  O     . GLN A 1 149 ? 5.284   -17.471 -11.562 1.00 26.22 ?  149 GLN A O     1 
ATOM   1117  C  CB    . GLN A 1 149 ? 6.138   -14.365 -11.496 1.00 23.83 ?  149 GLN A CB    1 
ATOM   1118  C  CG    . GLN A 1 149 ? 7.215   -15.002 -10.624 1.00 23.26 ?  149 GLN A CG    1 
ATOM   1119  C  CD    . GLN A 1 149 ? 7.599   -14.153 -9.431  1.00 22.85 ?  149 GLN A CD    1 
ATOM   1120  O  OE1   . GLN A 1 149 ? 7.232   -14.446 -8.288  1.00 23.85 ?  149 GLN A OE1   1 
ATOM   1121  N  NE2   . GLN A 1 149 ? 8.336   -13.082 -9.686  1.00 24.66 ?  149 GLN A NE2   1 
ATOM   1122  N  N     . PHE A 1 150 ? 3.451   -16.152 -11.692 1.00 17.54 ?  150 PHE A N     1 
ATOM   1123  C  CA    . PHE A 1 150 ? 2.553   -17.110 -11.068 1.00 17.15 ?  150 PHE A CA    1 
ATOM   1124  C  C     . PHE A 1 150 ? 2.403   -18.323 -11.981 1.00 17.70 ?  150 PHE A C     1 
ATOM   1125  O  O     . PHE A 1 150 ? 2.131   -19.429 -11.518 1.00 20.17 ?  150 PHE A O     1 
ATOM   1126  C  CB    . PHE A 1 150 ? 1.177   -16.498 -10.789 1.00 16.01 ?  150 PHE A CB    1 
ATOM   1127  C  CG    . PHE A 1 150 ? 0.233   -17.455 -10.073 1.00 16.62 ?  150 PHE A CG    1 
ATOM   1128  C  CD1   . PHE A 1 150 ? -0.457  -18.436 -10.778 1.00 16.03 ?  150 PHE A CD1   1 
ATOM   1129  C  CD2   . PHE A 1 150 ? 0.055   -17.386 -8.696  1.00 15.48 ?  150 PHE A CD2   1 
ATOM   1130  C  CE1   . PHE A 1 150 ? -1.305  -19.315 -10.124 1.00 16.49 ?  150 PHE A CE1   1 
ATOM   1131  C  CE2   . PHE A 1 150 ? -0.796  -18.268 -8.049  1.00 15.86 ?  150 PHE A CE2   1 
ATOM   1132  C  CZ    . PHE A 1 150 ? -1.473  -19.229 -8.762  1.00 15.89 ?  150 PHE A CZ    1 
ATOM   1133  N  N     . MET A 1 151 ? 2.578   -18.091 -13.285 1.00 18.06 ?  151 MET A N     1 
ATOM   1134  C  CA    . MET A 1 151 ? 2.358   -19.114 -14.293 1.00 18.55 ?  151 MET A CA    1 
ATOM   1135  C  C     . MET A 1 151 ? 3.664   -19.850 -14.578 1.00 19.56 ?  151 MET A C     1 
ATOM   1136  O  O     . MET A 1 151 ? 3.656   -21.055 -14.816 1.00 20.33 ?  151 MET A O     1 
ATOM   1137  C  CB    . MET A 1 151 ? 1.828   -18.499 -15.594 1.00 18.79 ?  151 MET A CB    1 
ATOM   1138  C  CG    . MET A 1 151 ? 0.371   -18.082 -15.542 1.00 18.26 ?  151 MET A CG    1 
ATOM   1139  S  SD    . MET A 1 151 ? -0.251  -17.546 -17.149 1.00 19.28 ?  151 MET A SD    1 
ATOM   1140  C  CE    . MET A 1 151 ? -0.648  -19.111 -17.941 1.00 17.72 ?  151 MET A CE    1 
ATOM   1141  N  N     . PHE A 1 152 ? 4.781   -19.114 -14.541 1.00 19.64 ?  152 PHE A N     1 
ATOM   1142  C  CA    . PHE A 1 152 ? 6.061   -19.632 -14.993 1.00 19.42 ?  152 PHE A CA    1 
ATOM   1143  C  C     . PHE A 1 152 ? 6.800   -20.311 -13.843 1.00 23.49 ?  152 PHE A C     1 
ATOM   1144  O  O     . PHE A 1 152 ? 7.688   -21.130 -14.073 1.00 21.28 ?  152 PHE A O     1 
ATOM   1145  C  CB    . PHE A 1 152 ? 6.945   -18.521 -15.567 1.00 19.30 ?  152 PHE A CB    1 
ATOM   1146  C  CG    . PHE A 1 152 ? 6.360   -17.773 -16.757 1.00 19.97 ?  152 PHE A CG    1 
ATOM   1147  C  CD1   . PHE A 1 152 ? 5.405   -18.363 -17.578 1.00 21.07 ?  152 PHE A CD1   1 
ATOM   1148  C  CD2   . PHE A 1 152 ? 6.777   -16.481 -17.055 1.00 19.82 ?  152 PHE A CD2   1 
ATOM   1149  C  CE1   . PHE A 1 152 ? 4.879   -17.673 -18.660 1.00 22.32 ?  152 PHE A CE1   1 
ATOM   1150  C  CE2   . PHE A 1 152 ? 6.247   -15.797 -18.138 1.00 20.89 ?  152 PHE A CE2   1 
ATOM   1151  C  CZ    . PHE A 1 152 ? 5.301   -16.394 -18.938 1.00 21.98 ?  152 PHE A CZ    1 
ATOM   1152  N  N     . PHE A 1 153 ? 6.436   -19.955 -12.608 1.00 24.17 ?  153 PHE A N     1 
ATOM   1153  C  CA    . PHE A 1 153 ? 7.153   -20.441 -11.443 1.00 23.12 ?  153 PHE A CA    1 
ATOM   1154  C  C     . PHE A 1 153 ? 6.161   -21.095 -10.488 1.00 23.40 ?  153 PHE A C     1 
ATOM   1155  O  O     . PHE A 1 153 ? 4.951   -21.001 -10.679 1.00 23.53 ?  153 PHE A O     1 
ATOM   1156  C  CB    . PHE A 1 153 ? 7.939   -19.293 -10.802 1.00 23.59 ?  153 PHE A CB    1 
ATOM   1157  C  CG    . PHE A 1 153 ? 9.059   -18.742 -11.673 1.00 23.20 ?  153 PHE A CG    1 
ATOM   1158  C  CD1   . PHE A 1 153 ? 10.307  -19.356 -11.705 1.00 24.12 ?  153 PHE A CD1   1 
ATOM   1159  C  CD2   . PHE A 1 153 ? 8.866   -17.608 -12.455 1.00 24.33 ?  153 PHE A CD2   1 
ATOM   1160  C  CE1   . PHE A 1 153 ? 11.326  -18.853 -12.499 1.00 22.42 ?  153 PHE A CE1   1 
ATOM   1161  C  CE2   . PHE A 1 153 ? 9.889   -17.109 -13.246 1.00 22.73 ?  153 PHE A CE2   1 
ATOM   1162  C  CZ    . PHE A 1 153 ? 11.115  -17.731 -13.266 1.00 22.53 ?  153 PHE A CZ    1 
ATOM   1163  N  N     . ASN A 1 154 ? 6.698   -21.763 -9.464  1.00 29.19 ?  154 ASN A N     1 
ATOM   1164  C  CA    . ASN A 1 154 ? 5.881   -22.545 -8.556  1.00 29.44 ?  154 ASN A CA    1 
ATOM   1165  C  C     . ASN A 1 154 ? 5.400   -21.644 -7.423  1.00 28.71 ?  154 ASN A C     1 
ATOM   1166  O  O     . ASN A 1 154 ? 6.184   -21.207 -6.583  1.00 25.07 ?  154 ASN A O     1 
ATOM   1167  C  CB    . ASN A 1 154 ? 6.621   -23.786 -8.068  1.00 28.35 ?  154 ASN A CB    1 
ATOM   1168  C  CG    . ASN A 1 154 ? 7.087   -24.660 -9.210  1.00 29.54 ?  154 ASN A CG    1 
ATOM   1169  O  OD1   . ASN A 1 154 ? 6.320   -24.936 -10.140 1.00 25.16 ?  154 ASN A OD1   1 
ATOM   1170  N  ND2   . ASN A 1 154 ? 8.335   -25.102 -9.163  1.00 32.59 ?  154 ASN A ND2   1 
ATOM   1171  N  N     . HIS A 1 155 ? 4.093   -21.367 -7.444  1.00 27.07 ?  155 HIS A N     1 
ATOM   1172  C  CA    . HIS A 1 155 ? 3.418   -20.612 -6.404  1.00 24.74 ?  155 HIS A CA    1 
ATOM   1173  C  C     . HIS A 1 155 ? 2.109   -21.313 -6.061  1.00 25.88 ?  155 HIS A C     1 
ATOM   1174  O  O     . HIS A 1 155 ? 1.316   -21.623 -6.947  1.00 27.33 ?  155 HIS A O     1 
ATOM   1175  C  CB    . HIS A 1 155 ? 3.141   -19.176 -6.861  1.00 20.68 ?  155 HIS A CB    1 
ATOM   1176  C  CG    . HIS A 1 155 ? 4.357   -18.320 -6.950  1.00 16.44 ?  155 HIS A CG    1 
ATOM   1177  N  ND1   . HIS A 1 155 ? 5.196   -18.107 -5.878  1.00 15.80 ?  155 HIS A ND1   1 
ATOM   1178  C  CD2   . HIS A 1 155 ? 4.854   -17.599 -7.961  1.00 14.79 ?  155 HIS A CD2   1 
ATOM   1179  C  CE1   . HIS A 1 155 ? 6.174   -17.294 -6.246  1.00 14.94 ?  155 HIS A CE1   1 
ATOM   1180  N  NE2   . HIS A 1 155 ? 5.988   -16.976 -7.509  1.00 14.89 ?  155 HIS A NE2   1 
ATOM   1181  N  N     . VAL A 1 156 ? 1.907   -21.560 -4.765  1.00 27.66 ?  156 VAL A N     1 
ATOM   1182  C  CA    . VAL A 1 156 ? 0.664   -22.114 -4.260  1.00 32.22 ?  156 VAL A CA    1 
ATOM   1183  C  C     . VAL A 1 156 ? -0.042  -21.023 -3.461  1.00 32.74 ?  156 VAL A C     1 
ATOM   1184  O  O     . VAL A 1 156 ? 0.488   -20.547 -2.460  1.00 33.93 ?  156 VAL A O     1 
ATOM   1185  C  CB    . VAL A 1 156 ? 0.929   -23.363 -3.396  1.00 34.86 ?  156 VAL A CB    1 
ATOM   1186  C  CG1   . VAL A 1 156 ? -0.350  -23.926 -2.788  1.00 36.17 ?  156 VAL A CG1   1 
ATOM   1187  C  CG2   . VAL A 1 156 ? 1.669   -24.443 -4.176  1.00 38.40 ?  156 VAL A CG2   1 
ATOM   1188  N  N     . PRO A 1 157 ? -1.247  -20.579 -3.882  1.00 33.96 ?  157 PRO A N     1 
ATOM   1189  C  CA    . PRO A 1 157 ? -1.985  -19.559 -3.142  1.00 31.20 ?  157 PRO A CA    1 
ATOM   1190  C  C     . PRO A 1 157 ? -2.782  -20.194 -2.008  1.00 30.39 ?  157 PRO A C     1 
ATOM   1191  O  O     . PRO A 1 157 ? -3.223  -21.336 -2.122  1.00 31.17 ?  157 PRO A O     1 
ATOM   1192  C  CB    . PRO A 1 157 ? -2.883  -18.976 -4.241  1.00 29.64 ?  157 PRO A CB    1 
ATOM   1193  C  CG    . PRO A 1 157 ? -3.232  -20.185 -5.083  1.00 30.90 ?  157 PRO A CG    1 
ATOM   1194  C  CD    . PRO A 1 157 ? -1.969  -21.039 -5.081  1.00 32.41 ?  157 PRO A CD    1 
ATOM   1195  N  N     . ASP A 1 158 ? -2.947  -19.448 -0.913  1.00 27.24 ?  158 ASP A N     1 
ATOM   1196  C  CA    . ASP A 1 158 ? -3.892  -19.822 0.123   1.00 26.01 ?  158 ASP A CA    1 
ATOM   1197  C  C     . ASP A 1 158 ? -5.283  -19.380 -0.320  1.00 25.22 ?  158 ASP A C     1 
ATOM   1198  O  O     . ASP A 1 158 ? -5.530  -18.188 -0.483  1.00 22.34 ?  158 ASP A O     1 
ATOM   1199  C  CB    . ASP A 1 158 ? -3.533  -19.198 1.462   1.00 25.43 ?  158 ASP A CB    1 
ATOM   1200  C  CG    . ASP A 1 158 ? -4.489  -19.520 2.602   1.00 21.76 ?  158 ASP A CG    1 
ATOM   1201  O  OD1   . ASP A 1 158 ? -5.447  -20.285 2.366   1.00 22.70 ?  158 ASP A OD1   1 
ATOM   1202  O  OD2   . ASP A 1 158 ? -4.268  -19.004 3.715   1.00 18.78 -1 158 ASP A OD2   1 
ATOM   1203  N  N     . PRO A 1 159 ? -6.231  -20.317 -0.545  1.00 29.61 ?  159 PRO A N     1 
ATOM   1204  C  CA    . PRO A 1 159 ? -7.571  -19.946 -1.007  1.00 33.78 ?  159 PRO A CA    1 
ATOM   1205  C  C     . PRO A 1 159 ? -8.520  -19.353 0.035   1.00 34.34 ?  159 PRO A C     1 
ATOM   1206  O  O     . PRO A 1 159 ? -9.702  -19.171 -0.252  1.00 35.51 ?  159 PRO A O     1 
ATOM   1207  C  CB    . PRO A 1 159 ? -8.091  -21.287 -1.560  1.00 33.41 ?  159 PRO A CB    1 
ATOM   1208  C  CG    . PRO A 1 159 ? -7.431  -22.328 -0.685  1.00 33.06 ?  159 PRO A CG    1 
ATOM   1209  C  CD    . PRO A 1 159 ? -6.044  -21.772 -0.416  1.00 31.77 ?  159 PRO A CD    1 
ATOM   1210  N  N     . THR A 1 160 ? -8.008  -19.044 1.236   1.00 32.63 ?  160 THR A N     1 
ATOM   1211  C  CA    . THR A 1 160 ? -8.811  -18.399 2.265   1.00 28.01 ?  160 THR A CA    1 
ATOM   1212  C  C     . THR A 1 160 ? -8.522  -16.901 2.294   1.00 26.69 ?  160 THR A C     1 
ATOM   1213  O  O     . THR A 1 160 ? -9.159  -16.167 3.046   1.00 25.81 ?  160 THR A O     1 
ATOM   1214  C  CB    . THR A 1 160 ? -8.540  -18.988 3.650   1.00 26.78 ?  160 THR A CB    1 
ATOM   1215  O  OG1   . THR A 1 160 ? -7.187  -18.647 3.935   1.00 20.16 ?  160 THR A OG1   1 
ATOM   1216  C  CG2   . THR A 1 160 ? -8.757  -20.488 3.722   1.00 27.11 ?  160 THR A CG2   1 
ATOM   1217  N  N     . THR A 1 161 ? -7.541  -16.457 1.503   1.00 24.29 ?  161 THR A N     1 
ATOM   1218  C  CA    . THR A 1 161 ? -7.110  -15.070 1.550   1.00 24.96 ?  161 THR A CA    1 
ATOM   1219  C  C     . THR A 1 161 ? -7.602  -14.355 0.296   1.00 25.66 ?  161 THR A C     1 
ATOM   1220  O  O     . THR A 1 161 ? -8.079  -14.998 -0.636  1.00 25.51 ?  161 THR A O     1 
ATOM   1221  C  CB    . THR A 1 161 ? -5.589  -15.006 1.668   1.00 22.68 ?  161 THR A CB    1 
ATOM   1222  O  OG1   . THR A 1 161 ? -5.110  -15.407 0.389   1.00 31.20 ?  161 THR A OG1   1 
ATOM   1223  C  CG2   . THR A 1 161 ? -5.042  -15.913 2.755   1.00 23.55 ?  161 THR A CG2   1 
ATOM   1224  N  N     . HIS A 1 162 ? -7.489  -13.021 0.289   1.00 22.37 ?  162 HIS A N     1 
ATOM   1225  C  CA    . HIS A 1 162 ? -7.672  -12.258 -0.934  1.00 21.88 ?  162 HIS A CA    1 
ATOM   1226  C  C     . HIS A 1 162 ? -6.417  -12.390 -1.789  1.00 21.10 ?  162 HIS A C     1 
ATOM   1227  O  O     . HIS A 1 162 ? -5.319  -12.053 -1.350  1.00 18.25 ?  162 HIS A O     1 
ATOM   1228  C  CB    . HIS A 1 162 ? -8.035  -10.797 -0.642  1.00 23.95 ?  162 HIS A CB    1 
ATOM   1229  C  CG    . HIS A 1 162 ? -9.490  -10.623 -0.372  1.00 23.26 ?  162 HIS A CG    1 
ATOM   1230  N  ND1   . HIS A 1 162 ? -10.414 -10.530 -1.390  1.00 24.15 ?  162 HIS A ND1   1 
ATOM   1231  C  CD2   . HIS A 1 162 ? -10.188 -10.574 0.770   1.00 22.74 ?  162 HIS A CD2   1 
ATOM   1232  C  CE1   . HIS A 1 162 ? -11.626 -10.409 -0.868  1.00 23.31 ?  162 HIS A CE1   1 
ATOM   1233  N  NE2   . HIS A 1 162 ? -11.512 -10.432 0.442   1.00 22.75 ?  162 HIS A NE2   1 
ATOM   1234  N  N     . LEU A 1 163 ? -6.602  -12.888 -3.016  1.00 18.80 ?  163 LEU A N     1 
ATOM   1235  C  CA    . LEU A 1 163 ? -5.492  -13.139 -3.917  1.00 18.87 ?  163 LEU A CA    1 
ATOM   1236  C  C     . LEU A 1 163 ? -5.518  -12.134 -5.066  1.00 16.86 ?  163 LEU A C     1 
ATOM   1237  O  O     . LEU A 1 163 ? -6.544  -11.953 -5.718  1.00 19.81 ?  163 LEU A O     1 
ATOM   1238  C  CB    . LEU A 1 163 ? -5.545  -14.571 -4.444  1.00 15.77 ?  163 LEU A CB    1 
ATOM   1239  C  CG    . LEU A 1 163 ? -4.681  -14.844 -5.680  1.00 14.93 ?  163 LEU A CG    1 
ATOM   1240  C  CD1   . LEU A 1 163 ? -3.222  -14.562 -5.379  1.00 14.81 ?  163 LEU A CD1   1 
ATOM   1241  C  CD2   . LEU A 1 163 ? -4.851  -16.260 -6.203  1.00 14.71 ?  163 LEU A CD2   1 
ATOM   1242  N  N     . LEU A 1 164 ? -4.362  -11.511 -5.317  1.00 15.28 ?  164 LEU A N     1 
ATOM   1243  C  CA    . LEU A 1 164 ? -4.217  -10.568 -6.413  1.00 15.76 ?  164 LEU A CA    1 
ATOM   1244  C  C     . LEU A 1 164 ? -3.214  -11.090 -7.438  1.00 15.26 ?  164 LEU A C     1 
ATOM   1245  O  O     . LEU A 1 164 ? -2.154  -11.601 -7.082  1.00 17.53 ?  164 LEU A O     1 
ATOM   1246  C  CB    . LEU A 1 164 ? -3.775  -9.214  -5.864  1.00 16.43 ?  164 LEU A CB    1 
ATOM   1247  C  CG    . LEU A 1 164 ? -4.759  -8.532  -4.911  1.00 15.83 ?  164 LEU A CG    1 
ATOM   1248  C  CD1   . LEU A 1 164 ? -4.245  -7.167  -4.498  1.00 15.17 ?  164 LEU A CD1   1 
ATOM   1249  C  CD2   . LEU A 1 164 ? -6.117  -8.424  -5.571  1.00 17.46 ?  164 LEU A CD2   1 
ATOM   1250  N  N     . LEU A 1 165 ? -3.570  -10.927 -8.716  1.00 13.87 ?  165 LEU A N     1 
ATOM   1251  C  CA    . LEU A 1 165 ? -2.668  -11.185 -9.825  1.00 13.37 ?  165 LEU A CA    1 
ATOM   1252  C  C     . LEU A 1 165 ? -2.480  -9.886  -10.604 1.00 13.73 ?  165 LEU A C     1 
ATOM   1253  O  O     . LEU A 1 165 ? -3.380  -9.455  -11.321 1.00 14.53 ?  165 LEU A O     1 
ATOM   1254  C  CB    . LEU A 1 165 ? -3.225  -12.297 -10.713 1.00 13.21 ?  165 LEU A CB    1 
ATOM   1255  C  CG    . LEU A 1 165 ? -3.329  -13.688 -10.076 1.00 12.72 ?  165 LEU A CG    1 
ATOM   1256  C  CD1   . LEU A 1 165 ? -3.592  -14.745 -11.138 1.00 12.66 ?  165 LEU A CD1   1 
ATOM   1257  C  CD2   . LEU A 1 165 ? -2.085  -14.035 -9.277  1.00 12.24 ?  165 LEU A CD2   1 
ATOM   1258  N  N     . TRP A 1 166 ? -1.311  -9.257  -10.436 1.00 14.78 ?  166 TRP A N     1 
ATOM   1259  C  CA    . TRP A 1 166 ? -1.010  -8.006  -11.114 1.00 15.20 ?  166 TRP A CA    1 
ATOM   1260  C  C     . TRP A 1 166 ? -0.583  -8.303  -12.552 1.00 17.40 ?  166 TRP A C     1 
ATOM   1261  O  O     . TRP A 1 166 ? -0.138  -9.410  -12.853 1.00 15.09 ?  166 TRP A O     1 
ATOM   1262  C  CB    . TRP A 1 166 ? 0.085   -7.221  -10.373 1.00 15.33 ?  166 TRP A CB    1 
ATOM   1263  C  CG    . TRP A 1 166 ? -0.207  -6.873  -8.935  1.00 16.14 ?  166 TRP A CG    1 
ATOM   1264  C  CD1   . TRP A 1 166 ? -0.654  -7.700  -7.945  1.00 13.96 ?  166 TRP A CD1   1 
ATOM   1265  C  CD2   . TRP A 1 166 ? -0.050  -5.572  -8.323  1.00 14.81 ?  166 TRP A CD2   1 
ATOM   1266  N  NE1   . TRP A 1 166 ? -0.786  -7.010  -6.769  1.00 13.29 ?  166 TRP A NE1   1 
ATOM   1267  C  CE2   . TRP A 1 166 ? -0.425  -5.703  -6.968  1.00 15.14 ?  166 TRP A CE2   1 
ATOM   1268  C  CE3   . TRP A 1 166 ? 0.366   -4.318  -8.786  1.00 15.19 ?  166 TRP A CE3   1 
ATOM   1269  C  CZ2   . TRP A 1 166 ? -0.393  -4.629  -6.081  1.00 15.85 ?  166 TRP A CZ2   1 
ATOM   1270  C  CZ3   . TRP A 1 166 ? 0.396   -3.258  -7.907  1.00 15.08 ?  166 TRP A CZ3   1 
ATOM   1271  C  CH2   . TRP A 1 166 ? 0.022   -3.413  -6.573  1.00 15.48 ?  166 TRP A CH2   1 
ATOM   1272  N  N     . GLN A 1 167 ? -0.725  -7.302  -13.430 1.00 16.32 ?  167 GLN A N     1 
ATOM   1273  C  CA    . GLN A 1 167 ? -0.271  -7.394  -14.811 1.00 16.71 ?  167 GLN A CA    1 
ATOM   1274  C  C     . GLN A 1 167 ? -0.936  -8.580  -15.508 1.00 17.65 ?  167 GLN A C     1 
ATOM   1275  O  O     . GLN A 1 167 ? -0.307  -9.274  -16.303 1.00 17.93 ?  167 GLN A O     1 
ATOM   1276  C  CB    . GLN A 1 167 ? 1.258   -7.453  -14.855 1.00 17.60 ?  167 GLN A CB    1 
ATOM   1277  C  CG    . GLN A 1 167 ? 1.923   -6.154  -14.408 1.00 18.20 ?  167 GLN A CG    1 
ATOM   1278  C  CD    . GLN A 1 167 ? 3.406   -6.082  -14.703 1.00 18.06 ?  167 GLN A CD    1 
ATOM   1279  O  OE1   . GLN A 1 167 ? 4.062   -5.066  -14.443 1.00 14.78 ?  167 GLN A OE1   1 
ATOM   1280  N  NE2   . GLN A 1 167 ? 3.953   -7.155  -15.255 1.00 19.40 ?  167 GLN A NE2   1 
ATOM   1281  N  N     . ILE A 1 168 ? -2.226  -8.774  -15.218 1.00 21.15 ?  168 ILE A N     1 
ATOM   1282  C  CA    . ILE A 1 168 ? -3.010  -9.869  -15.769 1.00 20.44 ?  168 ILE A CA    1 
ATOM   1283  C  C     . ILE A 1 168 ? -3.129  -9.721  -17.287 1.00 20.83 ?  168 ILE A C     1 
ATOM   1284  O  O     . ILE A 1 168 ? -3.380  -10.701 -17.985 1.00 17.05 ?  168 ILE A O     1 
ATOM   1285  C  CB    . ILE A 1 168 ? -4.389  -9.922  -15.082 1.00 22.87 ?  168 ILE A CB    1 
ATOM   1286  C  CG1   . ILE A 1 168 ? -5.214  -11.133 -15.524 1.00 19.99 ?  168 ILE A CG1   1 
ATOM   1287  C  CG2   . ILE A 1 168 ? -5.153  -8.613  -15.289 1.00 24.21 ?  168 ILE A CG2   1 
ATOM   1288  C  CD1   . ILE A 1 168 ? -4.663  -12.466 -15.048 1.00 21.52 ?  168 ILE A CD1   1 
ATOM   1289  N  N     . ALA A 1 169 ? -2.941  -8.501  -17.800 1.00 22.06 ?  169 ALA A N     1 
ATOM   1290  C  CA    . ALA A 1 169 ? -3.147  -8.243  -19.218 1.00 24.63 ?  169 ALA A CA    1 
ATOM   1291  C  C     . ALA A 1 169 ? -2.030  -8.875  -20.047 1.00 26.57 ?  169 ALA A C     1 
ATOM   1292  O  O     . ALA A 1 169 ? -2.148  -8.979  -21.266 1.00 30.48 ?  169 ALA A O     1 
ATOM   1293  C  CB    . ALA A 1 169 ? -3.249  -6.755  -19.474 1.00 23.48 ?  169 ALA A CB    1 
ATOM   1294  N  N     . ILE A 1 170 ? -0.946  -9.293  -19.383 1.00 24.89 ?  170 ILE A N     1 
ATOM   1295  C  CA    . ILE A 1 170 ? 0.174   -9.912  -20.074 1.00 21.13 ?  170 ILE A CA    1 
ATOM   1296  C  C     . ILE A 1 170 ? 0.467   -11.279 -19.462 1.00 21.18 ?  170 ILE A C     1 
ATOM   1297  O  O     . ILE A 1 170 ? 1.564   -11.809 -19.624 1.00 17.71 ?  170 ILE A O     1 
ATOM   1298  C  CB    . ILE A 1 170 ? 1.423   -9.009  -20.052 1.00 19.54 ?  170 ILE A CB    1 
ATOM   1299  C  CG1   . ILE A 1 170 ? 1.714   -8.462  -18.654 1.00 22.01 ?  170 ILE A CG1   1 
ATOM   1300  C  CG2   . ILE A 1 170 ? 1.302   -7.884  -21.079 1.00 20.53 ?  170 ILE A CG2   1 
ATOM   1301  C  CD1   . ILE A 1 170 ? 3.002   -7.664  -18.563 1.00 21.37 ?  170 ILE A CD1   1 
ATOM   1302  N  N     . ALA A 1 171 ? -0.525  -11.846 -18.770 1.00 18.18 ?  171 ALA A N     1 
ATOM   1303  C  CA    . ALA A 1 171 ? -0.372  -13.147 -18.142 1.00 19.77 ?  171 ALA A CA    1 
ATOM   1304  C  C     . ALA A 1 171 ? 0.072   -14.175 -19.180 1.00 23.84 ?  171 ALA A C     1 
ATOM   1305  O  O     . ALA A 1 171 ? -0.683  -14.515 -20.089 1.00 21.85 ?  171 ALA A O     1 
ATOM   1306  C  CB    . ALA A 1 171 ? -1.669  -13.556 -17.481 1.00 22.25 ?  171 ALA A CB    1 
ATOM   1307  N  N     . GLY A 1 172 ? 1.310   -14.657 -19.030 1.00 24.88 ?  172 GLY A N     1 
ATOM   1308  C  CA    . GLY A 1 172 ? 1.822   -15.743 -19.847 1.00 26.61 ?  172 GLY A CA    1 
ATOM   1309  C  C     . GLY A 1 172 ? 2.487   -15.228 -21.120 1.00 29.01 ?  172 GLY A C     1 
ATOM   1310  O  O     . GLY A 1 172 ? 2.663   -15.980 -22.078 1.00 25.30 ?  172 GLY A O     1 
ATOM   1311  N  N     . GLU A 1 173 ? 2.848   -13.940 -21.118 1.00 29.50 ?  173 GLU A N     1 
ATOM   1312  C  CA    . GLU A 1 173 ? 3.537   -13.332 -22.245 1.00 27.79 ?  173 GLU A CA    1 
ATOM   1313  C  C     . GLU A 1 173 ? 5.035   -13.350 -21.955 1.00 26.18 ?  173 GLU A C     1 
ATOM   1314  O  O     . GLU A 1 173 ? 5.594   -12.376 -21.456 1.00 26.02 ?  173 GLU A O     1 
ATOM   1315  C  CB    . GLU A 1 173 ? 2.987   -11.931 -22.518 1.00 32.94 ?  173 GLU A CB    1 
ATOM   1316  C  CG    . GLU A 1 173 ? 3.588   -11.269 -23.755 1.00 38.17 ?  173 GLU A CG    1 
ATOM   1317  C  CD    . GLU A 1 173 ? 4.739   -10.316 -23.481 1.00 46.73 ?  173 GLU A CD    1 
ATOM   1318  O  OE1   . GLU A 1 173 ? 5.402   -9.900  -24.456 1.00 43.54 ?  173 GLU A OE1   1 
ATOM   1319  O  OE2   . GLU A 1 173 ? 4.962   -9.973  -22.299 1.00 54.59 -1 173 GLU A OE2   1 
ATOM   1320  N  N     . HIS A 1 174 ? 5.668   -14.477 -22.298 1.00 23.80 ?  174 HIS A N     1 
ATOM   1321  C  CA    . HIS A 1 174 ? 6.985   -14.832 -21.795 1.00 20.90 ?  174 HIS A CA    1 
ATOM   1322  C  C     . HIS A 1 174 ? 8.079   -14.018 -22.484 1.00 20.57 ?  174 HIS A C     1 
ATOM   1323  O  O     . HIS A 1 174 ? 9.211   -13.980 -22.003 1.00 19.51 ?  174 HIS A O     1 
ATOM   1324  C  CB    . HIS A 1 174 ? 7.237   -16.327 -22.015 1.00 22.41 ?  174 HIS A CB    1 
ATOM   1325  C  CG    . HIS A 1 174 ? 7.278   -16.684 -23.463 1.00 22.38 ?  174 HIS A CG    1 
ATOM   1326  N  ND1   . HIS A 1 174 ? 6.176   -17.123 -24.166 1.00 23.16 ?  174 HIS A ND1   1 
ATOM   1327  C  CD2   . HIS A 1 174 ? 8.283   -16.633 -24.344 1.00 22.54 ?  174 HIS A CD2   1 
ATOM   1328  C  CE1   . HIS A 1 174 ? 6.522   -17.341 -25.427 1.00 25.06 ?  174 HIS A CE1   1 
ATOM   1329  N  NE2   . HIS A 1 174 ? 7.798   -17.048 -25.557 1.00 25.33 ?  174 HIS A NE2   1 
ATOM   1330  N  N     . THR A 1 175 ? 7.741   -13.379 -23.610 1.00 18.16 ?  175 THR A N     1 
ATOM   1331  C  CA    . THR A 1 175 ? 8.734   -12.710 -24.439 1.00 22.28 ?  175 THR A CA    1 
ATOM   1332  C  C     . THR A 1 175 ? 9.103   -11.358 -23.833 1.00 26.32 ?  175 THR A C     1 
ATOM   1333  O  O     . THR A 1 175 ? 10.225  -10.887 -24.003 1.00 24.31 ?  175 THR A O     1 
ATOM   1334  C  CB    . THR A 1 175 ? 8.209   -12.540 -25.865 1.00 22.95 ?  175 THR A CB    1 
ATOM   1335  O  OG1   . THR A 1 175 ? 7.293   -11.450 -25.817 1.00 20.65 ?  175 THR A OG1   1 
ATOM   1336  C  CG2   . THR A 1 175 ? 7.529   -13.788 -26.398 1.00 22.14 ?  175 THR A CG2   1 
ATOM   1337  N  N     . LEU A 1 176 ? 8.146   -10.731 -23.143 1.00 31.33 ?  176 LEU A N     1 
ATOM   1338  C  CA    . LEU A 1 176 ? 8.338   -9.396  -22.598 1.00 34.08 ?  176 LEU A CA    1 
ATOM   1339  C  C     . LEU A 1 176 ? 8.555   -8.402  -23.738 1.00 35.26 ?  176 LEU A C     1 
ATOM   1340  O  O     . LEU A 1 176 ? 9.277   -7.423  -23.566 1.00 38.18 ?  176 LEU A O     1 
ATOM   1341  C  CB    . LEU A 1 176 ? 9.521   -9.354  -21.630 1.00 34.20 ?  176 LEU A CB    1 
ATOM   1342  C  CG    . LEU A 1 176 ? 9.528   -10.396 -20.508 1.00 41.44 ?  176 LEU A CG    1 
ATOM   1343  C  CD1   . LEU A 1 176 ? 10.788  -10.271 -19.665 1.00 41.58 ?  176 LEU A CD1   1 
ATOM   1344  C  CD2   . LEU A 1 176 ? 8.288   -10.265 -19.641 1.00 43.32 ?  176 LEU A CD2   1 
ATOM   1345  N  N     . THR A 1 177 ? 7.942   -8.655  -24.901 1.00 33.91 ?  177 THR A N     1 
ATOM   1346  C  CA    . THR A 1 177 ? 8.002   -7.694  -25.993 1.00 33.16 ?  177 THR A CA    1 
ATOM   1347  C  C     . THR A 1 177 ? 6.587   -7.276  -26.392 1.00 36.48 ?  177 THR A C     1 
ATOM   1348  O  O     . THR A 1 177 ? 6.420   -6.372  -27.208 1.00 34.88 ?  177 THR A O     1 
ATOM   1349  C  CB    . THR A 1 177 ? 8.767   -8.262  -27.189 1.00 30.60 ?  177 THR A CB    1 
ATOM   1350  O  OG1   . THR A 1 177 ? 7.914   -9.251  -27.756 1.00 28.81 ?  177 THR A OG1   1 
ATOM   1351  C  CG2   . THR A 1 177 ? 10.109  -8.863  -26.810 1.00 29.69 ?  177 THR A CG2   1 
ATOM   1352  N  N     . GLN A 1 178 ? 5.574   -7.937  -25.815 1.00 34.35 ?  178 GLN A N     1 
ATOM   1353  C  CA    . GLN A 1 178 ? 4.183   -7.650  -26.136 1.00 35.83 ?  178 GLN A CA    1 
ATOM   1354  C  C     . GLN A 1 178 ? 3.537   -6.861  -24.999 1.00 37.17 ?  178 GLN A C     1 
ATOM   1355  O  O     . GLN A 1 178 ? 4.008   -6.891  -23.863 1.00 33.69 ?  178 GLN A O     1 
ATOM   1356  C  CB    . GLN A 1 178 ? 3.365   -8.921  -26.371 1.00 36.62 ?  178 GLN A CB    1 
ATOM   1357  C  CG    . GLN A 1 178 ? 3.843   -9.779  -27.538 1.00 40.44 ?  178 GLN A CG    1 
ATOM   1358  C  CD    . GLN A 1 178 ? 3.534   -9.177  -28.892 1.00 42.99 ?  178 GLN A CD    1 
ATOM   1359  O  OE1   . GLN A 1 178 ? 2.991   -8.071  -28.999 1.00 35.00 ?  178 GLN A OE1   1 
ATOM   1360  N  NE2   . GLN A 1 178 ? 3.878   -9.904  -29.945 1.00 38.95 ?  178 GLN A NE2   1 
ATOM   1361  N  N     . PHE A 1 179 ? 2.437   -6.172  -25.328 1.00 38.70 ?  179 PHE A N     1 
ATOM   1362  C  CA    . PHE A 1 179 ? 1.734   -5.315  -24.387 1.00 41.14 ?  179 PHE A CA    1 
ATOM   1363  C  C     . PHE A 1 179 ? 0.564   -6.069  -23.764 1.00 35.45 ?  179 PHE A C     1 
ATOM   1364  O  O     . PHE A 1 179 ? -0.013  -5.615  -22.779 1.00 37.12 ?  179 PHE A O     1 
ATOM   1365  C  CB    . PHE A 1 179 ? 1.211   -4.059  -25.090 1.00 43.61 ?  179 PHE A CB    1 
ATOM   1366  C  CG    . PHE A 1 179 ? 2.284   -3.161  -25.692 1.00 56.18 ?  179 PHE A CG    1 
ATOM   1367  C  CD1   . PHE A 1 179 ? 3.415   -2.811  -24.964 1.00 61.87 ?  179 PHE A CD1   1 
ATOM   1368  C  CD2   . PHE A 1 179 ? 2.164   -2.682  -26.991 1.00 61.17 ?  179 PHE A CD2   1 
ATOM   1369  C  CE1   . PHE A 1 179 ? 4.389   -1.995  -25.518 1.00 63.75 ?  179 PHE A CE1   1 
ATOM   1370  C  CE2   . PHE A 1 179 ? 3.143   -1.870  -27.542 1.00 64.84 ?  179 PHE A CE2   1 
ATOM   1371  C  CZ    . PHE A 1 179 ? 4.252   -1.529  -26.805 1.00 66.02 ?  179 PHE A CZ    1 
ATOM   1372  N  N     . HIS A 1 180 ? 0.210   -7.213  -24.357 1.00 32.83 ?  180 HIS A N     1 
ATOM   1373  C  CA    . HIS A 1 180 ? -0.927  -7.986  -23.891 1.00 34.99 ?  180 HIS A CA    1 
ATOM   1374  C  C     . HIS A 1 180 ? -0.723  -9.450  -24.260 1.00 35.57 ?  180 HIS A C     1 
ATOM   1375  O  O     . HIS A 1 180 ? 0.158   -9.784  -25.049 1.00 27.05 ?  180 HIS A O     1 
ATOM   1376  C  CB    . HIS A 1 180 ? -2.240  -7.435  -24.461 1.00 36.73 ?  180 HIS A CB    1 
ATOM   1377  C  CG    . HIS A 1 180 ? -2.394  -7.610  -25.935 1.00 36.77 ?  180 HIS A CG    1 
ATOM   1378  N  ND1   . HIS A 1 180 ? -2.774  -8.804  -26.509 1.00 27.69 ?  180 HIS A ND1   1 
ATOM   1379  C  CD2   . HIS A 1 180 ? -2.217  -6.751  -26.949 1.00 37.55 ?  180 HIS A CD2   1 
ATOM   1380  C  CE1   . HIS A 1 180 ? -2.826  -8.659  -27.825 1.00 30.65 ?  180 HIS A CE1   1 
ATOM   1381  N  NE2   . HIS A 1 180 ? -2.492  -7.419  -28.115 1.00 33.70 ?  180 HIS A NE2   1 
ATOM   1382  N  N     . THR A 1 181 ? -1.557  -10.313 -23.677 1.00 36.58 ?  181 THR A N     1 
ATOM   1383  C  CA    . THR A 1 181 ? -1.440  -11.744 -23.887 1.00 32.26 ?  181 THR A CA    1 
ATOM   1384  C  C     . THR A 1 181 ? -2.594  -12.199 -24.778 1.00 26.65 ?  181 THR A C     1 
ATOM   1385  O  O     . THR A 1 181 ? -3.282  -11.371 -25.367 1.00 22.66 ?  181 THR A O     1 
ATOM   1386  C  CB    . THR A 1 181 ? -1.417  -12.448 -22.530 1.00 34.37 ?  181 THR A CB    1 
ATOM   1387  O  OG1   . THR A 1 181 ? -1.019  -13.787 -22.809 1.00 37.98 ?  181 THR A OG1   1 
ATOM   1388  C  CG2   . THR A 1 181 ? -2.760  -12.419 -21.823 1.00 34.68 ?  181 THR A CG2   1 
ATOM   1389  N  N     . SER A 1 182 ? -2.783  -13.519 -24.882 1.00 25.44 ?  182 SER A N     1 
ATOM   1390  C  CA    . SER A 1 182 ? -3.854  -14.086 -25.686 1.00 24.67 ?  182 SER A CA    1 
ATOM   1391  C  C     . SER A 1 182 ? -4.863  -14.794 -24.787 1.00 24.84 ?  182 SER A C     1 
ATOM   1392  O  O     . SER A 1 182 ? -4.558  -15.124 -23.644 1.00 20.55 ?  182 SER A O     1 
ATOM   1393  C  CB    . SER A 1 182 ? -3.314  -15.031 -26.732 1.00 24.56 ?  182 SER A CB    1 
ATOM   1394  O  OG    . SER A 1 182 ? -2.721  -16.175 -26.131 1.00 25.35 ?  182 SER A OG    1 
ATOM   1395  N  N     . SER A 1 183 ? -6.058  -15.041 -25.336 1.00 33.90 ?  183 SER A N     1 
ATOM   1396  C  CA    . SER A 1 183 ? -7.142  -15.679 -24.605 1.00 34.85 ?  183 SER A CA    1 
ATOM   1397  C  C     . SER A 1 183 ? -6.788  -17.130 -24.290 1.00 34.82 ?  183 SER A C     1 
ATOM   1398  O  O     . SER A 1 183 ? -7.335  -17.717 -23.359 1.00 34.81 ?  183 SER A O     1 
ATOM   1399  C  CB    . SER A 1 183 ? -8.435  -15.592 -25.377 1.00 33.20 ?  183 SER A CB    1 
ATOM   1400  O  OG    . SER A 1 183 ? -8.358  -16.336 -26.585 1.00 39.46 ?  183 SER A OG    1 
ATOM   1401  N  N     . ASP A 1 184 ? -5.876  -17.702 -25.083 1.00 39.61 ?  184 ASP A N     1 
ATOM   1402  C  CA    . ASP A 1 184 ? -5.430  -19.072 -24.888 1.00 39.16 ?  184 ASP A CA    1 
ATOM   1403  C  C     . ASP A 1 184 ? -4.560  -19.144 -23.635 1.00 37.25 ?  184 ASP A C     1 
ATOM   1404  O  O     . ASP A 1 184 ? -4.659  -20.095 -22.862 1.00 34.03 ?  184 ASP A O     1 
ATOM   1405  C  CB    . ASP A 1 184 ? -4.700  -19.583 -26.119 1.00 42.50 ?  184 ASP A CB    1 
ATOM   1406  C  CG    . ASP A 1 184 ? -3.423  -18.833 -26.466 1.00 43.74 ?  184 ASP A CG    1 
ATOM   1407  O  OD1   . ASP A 1 184 ? -2.383  -19.126 -25.838 1.00 48.76 ?  184 ASP A OD1   1 
ATOM   1408  O  OD2   . ASP A 1 184 ? -3.487  -17.941 -27.337 1.00 33.60 -1 184 ASP A OD2   1 
ATOM   1409  N  N     . ARG A 1 185 ? -3.702  -18.131 -23.455 1.00 31.61 ?  185 ARG A N     1 
ATOM   1410  C  CA    . ARG A 1 185 ? -2.900  -17.997 -22.249 1.00 36.40 ?  185 ARG A CA    1 
ATOM   1411  C  C     . ARG A 1 185 ? -3.812  -17.904 -21.030 1.00 33.37 ?  185 ARG A C     1 
ATOM   1412  O  O     . ARG A 1 185 ? -3.609  -18.599 -20.038 1.00 33.75 ?  185 ARG A O     1 
ATOM   1413  C  CB    . ARG A 1 185 ? -2.025  -16.738 -22.258 1.00 41.85 ?  185 ARG A CB    1 
ATOM   1414  C  CG    . ARG A 1 185 ? -0.536  -16.981 -22.451 1.00 48.34 ?  185 ARG A CG    1 
ATOM   1415  C  CD    . ARG A 1 185 ? -0.162  -17.438 -23.848 1.00 52.84 ?  185 ARG A CD    1 
ATOM   1416  N  NE    . ARG A 1 185 ? 1.291   -17.623 -23.927 1.00 59.26 ?  185 ARG A NE    1 
ATOM   1417  C  CZ    . ARG A 1 185 ? 1.976   -17.961 -25.011 1.00 63.85 ?  185 ARG A CZ    1 
ATOM   1418  N  NH1   . ARG A 1 185 ? 1.360   -18.117 -26.170 1.00 62.54 1  185 ARG A NH1   1 
ATOM   1419  N  NH2   . ARG A 1 185 ? 3.283   -18.132 -24.929 1.00 59.65 ?  185 ARG A NH2   1 
ATOM   1420  N  N     . LEU A 1 186 ? -4.804  -17.015 -21.121 1.00 32.36 ?  186 LEU A N     1 
ATOM   1421  C  CA    . LEU A 1 186 ? -5.726  -16.774 -20.026 1.00 29.04 ?  186 LEU A CA    1 
ATOM   1422  C  C     . LEU A 1 186 ? -6.470  -18.066 -19.685 1.00 29.89 ?  186 LEU A C     1 
ATOM   1423  O  O     . LEU A 1 186 ? -6.744  -18.336 -18.518 1.00 30.29 ?  186 LEU A O     1 
ATOM   1424  C  CB    . LEU A 1 186 ? -6.661  -15.630 -20.424 1.00 27.57 ?  186 LEU A CB    1 
ATOM   1425  C  CG    . LEU A 1 186 ? -6.051  -14.224 -20.366 1.00 29.58 ?  186 LEU A CG    1 
ATOM   1426  C  CD1   . LEU A 1 186 ? -6.979  -13.168 -20.946 1.00 27.65 ?  186 LEU A CD1   1 
ATOM   1427  C  CD2   . LEU A 1 186 ? -5.680  -13.865 -18.936 1.00 30.17 ?  186 LEU A CD2   1 
ATOM   1428  N  N     . GLN A 1 187 ? -6.767  -18.872 -20.712 1.00 26.82 ?  187 GLN A N     1 
ATOM   1429  C  CA    . GLN A 1 187 ? -7.455  -20.143 -20.535 1.00 25.16 ?  187 GLN A CA    1 
ATOM   1430  C  C     . GLN A 1 187 ? -6.575  -21.110 -19.745 1.00 22.06 ?  187 GLN A C     1 
ATOM   1431  O  O     . GLN A 1 187 ? -7.074  -21.895 -18.941 1.00 17.27 ?  187 GLN A O     1 
ATOM   1432  C  CB    . GLN A 1 187 ? -7.815  -20.769 -21.883 1.00 25.51 ?  187 GLN A CB    1 
ATOM   1433  C  CG    . GLN A 1 187 ? -8.577  -22.085 -21.764 1.00 26.39 ?  187 GLN A CG    1 
ATOM   1434  C  CD    . GLN A 1 187 ? -9.885  -21.945 -21.018 1.00 25.55 ?  187 GLN A CD    1 
ATOM   1435  O  OE1   . GLN A 1 187 ? -10.495 -20.871 -20.983 1.00 25.29 ?  187 GLN A OE1   1 
ATOM   1436  N  NE2   . GLN A 1 187 ? -10.338 -23.041 -20.425 1.00 28.82 ?  187 GLN A NE2   1 
ATOM   1437  N  N     . ILE A 1 188 ? -5.265  -21.059 -20.003 1.00 21.11 ?  188 ILE A N     1 
ATOM   1438  C  CA    . ILE A 1 188 ? -4.304  -21.889 -19.296 1.00 22.07 ?  188 ILE A CA    1 
ATOM   1439  C  C     . ILE A 1 188 ? -4.235  -21.443 -17.836 1.00 19.17 ?  188 ILE A C     1 
ATOM   1440  O  O     . ILE A 1 188 ? -4.123  -22.275 -16.938 1.00 18.50 ?  188 ILE A O     1 
ATOM   1441  C  CB    . ILE A 1 188 ? -2.933  -21.841 -19.999 1.00 23.60 ?  188 ILE A CB    1 
ATOM   1442  C  CG1   . ILE A 1 188 ? -2.986  -22.560 -21.350 1.00 27.04 ?  188 ILE A CG1   1 
ATOM   1443  C  CG2   . ILE A 1 188 ? -1.826  -22.407 -19.108 1.00 23.88 ?  188 ILE A CG2   1 
ATOM   1444  C  CD1   . ILE A 1 188 ? -1.742  -22.382 -22.201 1.00 28.47 ?  188 ILE A CD1   1 
ATOM   1445  N  N     . LEU A 1 189 ? -4.322  -20.127 -17.611 1.00 17.48 ?  189 LEU A N     1 
ATOM   1446  C  CA    . LEU A 1 189 ? -4.328  -19.570 -16.267 1.00 17.64 ?  189 LEU A CA    1 
ATOM   1447  C  C     . LEU A 1 189 ? -5.530  -20.110 -15.495 1.00 17.45 ?  189 LEU A C     1 
ATOM   1448  O  O     . LEU A 1 189 ? -5.387  -20.582 -14.370 1.00 19.24 ?  189 LEU A O     1 
ATOM   1449  C  CB    . LEU A 1 189 ? -4.339  -18.044 -16.346 1.00 17.02 ?  189 LEU A CB    1 
ATOM   1450  C  CG    . LEU A 1 189 ? -4.457  -17.297 -15.014 1.00 17.21 ?  189 LEU A CG    1 
ATOM   1451  C  CD1   . LEU A 1 189 ? -3.400  -17.755 -14.024 1.00 16.53 ?  189 LEU A CD1   1 
ATOM   1452  C  CD2   . LEU A 1 189 ? -4.364  -15.797 -15.246 1.00 15.88 ?  189 LEU A CD2   1 
ATOM   1453  N  N     . VAL A 1 190 ? -6.713  -20.035 -16.115 1.00 17.07 ?  190 VAL A N     1 
ATOM   1454  C  CA    . VAL A 1 190 ? -7.945  -20.514 -15.509 1.00 21.87 ?  190 VAL A CA    1 
ATOM   1455  C  C     . VAL A 1 190 ? -7.780  -21.974 -15.095 1.00 20.44 ?  190 VAL A C     1 
ATOM   1456  O  O     . VAL A 1 190 ? -8.137  -22.349 -13.981 1.00 18.78 ?  190 VAL A O     1 
ATOM   1457  C  CB    . VAL A 1 190 ? -9.145  -20.351 -16.462 1.00 24.98 ?  190 VAL A CB    1 
ATOM   1458  C  CG1   . VAL A 1 190 ? -10.364 -21.132 -15.982 1.00 26.77 ?  190 VAL A CG1   1 
ATOM   1459  C  CG2   . VAL A 1 190 ? -9.495  -18.885 -16.686 1.00 26.84 ?  190 VAL A CG2   1 
ATOM   1460  N  N     . GLU A 1 191 ? -7.254  -22.798 -16.006 1.00 20.21 ?  191 GLU A N     1 
ATOM   1461  C  CA    . GLU A 1 191 ? -7.142  -24.226 -15.756 1.00 22.59 ?  191 GLU A CA    1 
ATOM   1462  C  C     . GLU A 1 191 ? -6.181  -24.456 -14.594 1.00 21.18 ?  191 GLU A C     1 
ATOM   1463  O  O     . GLU A 1 191 ? -6.379  -25.360 -13.786 1.00 21.78 ?  191 GLU A O     1 
ATOM   1464  C  CB    . GLU A 1 191 ? -6.724  -24.960 -17.030 1.00 25.25 ?  191 GLU A CB    1 
ATOM   1465  C  CG    . GLU A 1 191 ? -7.798  -24.918 -18.113 1.00 27.16 ?  191 GLU A CG    1 
ATOM   1466  C  CD    . GLU A 1 191 ? -7.342  -25.382 -19.485 1.00 33.56 ?  191 GLU A CD    1 
ATOM   1467  O  OE1   . GLU A 1 191 ? -7.427  -24.572 -20.433 1.00 35.89 ?  191 GLU A OE1   1 
ATOM   1468  O  OE2   . GLU A 1 191 ? -6.909  -26.547 -19.610 1.00 35.07 -1 191 GLU A OE2   1 
ATOM   1469  N  N     . GLN A 1 192 ? -5.149  -23.612 -14.515 1.00 19.42 ?  192 GLN A N     1 
ATOM   1470  C  CA    . GLN A 1 192 ? -4.183  -23.673 -13.432 1.00 18.38 ?  192 GLN A CA    1 
ATOM   1471  C  C     . GLN A 1 192 ? -4.837  -23.235 -12.123 1.00 19.93 ?  192 GLN A C     1 
ATOM   1472  O  O     . GLN A 1 192 ? -4.686  -23.901 -11.101 1.00 20.11 ?  192 GLN A O     1 
ATOM   1473  C  CB    . GLN A 1 192 ? -2.988  -22.792 -13.791 1.00 16.85 ?  192 GLN A CB    1 
ATOM   1474  C  CG    . GLN A 1 192 ? -1.929  -22.704 -12.699 1.00 14.76 ?  192 GLN A CG    1 
ATOM   1475  C  CD    . GLN A 1 192 ? -0.845  -21.703 -13.028 1.00 14.57 ?  192 GLN A CD    1 
ATOM   1476  O  OE1   . GLN A 1 192 ? -0.986  -20.884 -13.944 1.00 13.66 ?  192 GLN A OE1   1 
ATOM   1477  N  NE2   . GLN A 1 192 ? 0.243   -21.752 -12.274 1.00 12.73 ?  192 GLN A NE2   1 
ATOM   1478  N  N     . LEU A 1 193 ? -5.557  -22.107 -12.159 1.00 19.66 ?  193 LEU A N     1 
ATOM   1479  C  CA    . LEU A 1 193 ? -6.227  -21.589 -10.977 1.00 20.11 ?  193 LEU A CA    1 
ATOM   1480  C  C     . LEU A 1 193 ? -7.276  -22.593 -10.499 1.00 18.95 ?  193 LEU A C     1 
ATOM   1481  O  O     . LEU A 1 193 ? -7.649  -22.586 -9.329  1.00 17.42 ?  193 LEU A O     1 
ATOM   1482  C  CB    . LEU A 1 193 ? -6.855  -20.223 -11.254 1.00 22.45 ?  193 LEU A CB    1 
ATOM   1483  C  CG    . LEU A 1 193 ? -5.898  -19.028 -11.332 1.00 23.07 ?  193 LEU A CG    1 
ATOM   1484  C  CD1   . LEU A 1 193 ? -6.652  -17.823 -11.865 1.00 23.98 ?  193 LEU A CD1   1 
ATOM   1485  C  CD2   . LEU A 1 193 ? -5.259  -18.697 -9.992  1.00 24.45 ?  193 LEU A CD2   1 
ATOM   1486  N  N     . ASN A 1 194 ? -7.742  -23.462 -11.405 1.00 22.97 ?  194 ASN A N     1 
ATOM   1487  C  CA    . ASN A 1 194 ? -8.792  -24.416 -11.077 1.00 24.62 ?  194 ASN A CA    1 
ATOM   1488  C  C     . ASN A 1 194 ? -8.300  -25.438 -10.051 1.00 23.11 ?  194 ASN A C     1 
ATOM   1489  O  O     . ASN A 1 194 ? -9.105  -26.195 -9.514  1.00 20.56 ?  194 ASN A O     1 
ATOM   1490  C  CB    . ASN A 1 194 ? -9.339  -25.124 -12.313 1.00 25.87 ?  194 ASN A CB    1 
ATOM   1491  C  CG    . ASN A 1 194 ? -10.676 -25.776 -12.051 1.00 30.32 ?  194 ASN A CG    1 
ATOM   1492  O  OD1   . ASN A 1 194 ? -11.304 -25.519 -11.017 1.00 29.94 ?  194 ASN A OD1   1 
ATOM   1493  N  ND2   . ASN A 1 194 ? -11.137 -26.609 -12.973 1.00 37.83 ?  194 ASN A ND2   1 
ATOM   1494  N  N     . GLN A 1 195 ? -6.989  -25.469 -9.774  1.00 24.11 ?  195 GLN A N     1 
ATOM   1495  C  CA    . GLN A 1 195 ? -6.465  -26.372 -8.757  1.00 28.12 ?  195 GLN A CA    1 
ATOM   1496  C  C     . GLN A 1 195 ? -7.045  -25.980 -7.399  1.00 29.28 ?  195 GLN A C     1 
ATOM   1497  O  O     . GLN A 1 195 ? -7.093  -26.798 -6.483  1.00 25.43 ?  195 GLN A O     1 
ATOM   1498  C  CB    . GLN A 1 195 ? -4.936  -26.381 -8.663  1.00 25.54 ?  195 GLN A CB    1 
ATOM   1499  C  CG    . GLN A 1 195 ? -4.224  -26.728 -9.967  1.00 28.39 ?  195 GLN A CG    1 
ATOM   1500  C  CD    . GLN A 1 195 ? -2.740  -26.425 -9.942  1.00 28.01 ?  195 GLN A CD    1 
ATOM   1501  O  OE1   . GLN A 1 195 ? -1.917  -27.232 -9.494  1.00 25.51 ?  195 GLN A OE1   1 
ATOM   1502  N  NE2   . GLN A 1 195 ? -2.381  -25.258 -10.457 1.00 26.63 ?  195 GLN A NE2   1 
ATOM   1503  N  N     . TRP A 1 196 ? -7.490  -24.720 -7.288  1.00 31.78 ?  196 TRP A N     1 
ATOM   1504  C  CA    . TRP A 1 196 ? -7.942  -24.159 -6.025  1.00 27.27 ?  196 TRP A CA    1 
ATOM   1505  C  C     . TRP A 1 196 ? -9.349  -23.574 -6.158  1.00 29.82 ?  196 TRP A C     1 
ATOM   1506  O  O     . TRP A 1 196 ? -10.199 -23.811 -5.303  1.00 30.73 ?  196 TRP A O     1 
ATOM   1507  C  CB    . TRP A 1 196 ? -6.944  -23.097 -5.537  1.00 26.37 ?  196 TRP A CB    1 
ATOM   1508  C  CG    . TRP A 1 196 ? -5.528  -23.598 -5.398  1.00 23.03 ?  196 TRP A CG    1 
ATOM   1509  C  CD1   . TRP A 1 196 ? -4.977  -24.197 -4.303  1.00 20.60 ?  196 TRP A CD1   1 
ATOM   1510  C  CD2   . TRP A 1 196 ? -4.478  -23.532 -6.390  1.00 21.23 ?  196 TRP A CD2   1 
ATOM   1511  N  NE1   . TRP A 1 196 ? -3.665  -24.510 -4.542  1.00 21.48 ?  196 TRP A NE1   1 
ATOM   1512  C  CE2   . TRP A 1 196 ? -3.330  -24.116 -5.811  1.00 20.96 ?  196 TRP A CE2   1 
ATOM   1513  C  CE3   . TRP A 1 196 ? -4.396  -23.044 -7.698  1.00 19.41 ?  196 TRP A CE3   1 
ATOM   1514  C  CZ2   . TRP A 1 196 ? -2.122  -24.222 -6.497  1.00 19.23 ?  196 TRP A CZ2   1 
ATOM   1515  C  CZ3   . TRP A 1 196 ? -3.200  -23.148 -8.374  1.00 20.84 ?  196 TRP A CZ3   1 
ATOM   1516  C  CH2   . TRP A 1 196 ? -2.080  -23.729 -7.781  1.00 19.97 ?  196 TRP A CH2   1 
ATOM   1517  N  N     . TYR A 1 197 ? -9.591  -22.812 -7.234  1.00 29.73 ?  197 TYR A N     1 
ATOM   1518  C  CA    . TYR A 1 197 ? -10.834 -22.071 -7.398  1.00 30.44 ?  197 TYR A CA    1 
ATOM   1519  C  C     . TYR A 1 197 ? -11.701 -22.724 -8.475  1.00 29.52 ?  197 TYR A C     1 
ATOM   1520  O  O     . TYR A 1 197 ? -11.220 -23.002 -9.571  1.00 29.69 ?  197 TYR A O     1 
ATOM   1521  C  CB    . TYR A 1 197 ? -10.499 -20.619 -7.760  1.00 29.19 ?  197 TYR A CB    1 
ATOM   1522  C  CG    . TYR A 1 197 ? -9.505  -19.932 -6.832  1.00 29.55 ?  197 TYR A CG    1 
ATOM   1523  C  CD1   . TYR A 1 197 ? -9.934  -19.236 -5.707  1.00 28.30 ?  197 TYR A CD1   1 
ATOM   1524  C  CD2   . TYR A 1 197 ? -8.138  -19.968 -7.086  1.00 27.55 ?  197 TYR A CD2   1 
ATOM   1525  C  CE1   . TYR A 1 197 ? -9.036  -18.607 -4.860  1.00 25.41 ?  197 TYR A CE1   1 
ATOM   1526  C  CE2   . TYR A 1 197 ? -7.230  -19.343 -6.247  1.00 27.26 ?  197 TYR A CE2   1 
ATOM   1527  C  CZ    . TYR A 1 197 ? -7.681  -18.662 -5.130  1.00 24.43 ?  197 TYR A CZ    1 
ATOM   1528  O  OH    . TYR A 1 197 ? -6.789  -18.043 -4.303  1.00 25.14 ?  197 TYR A OH    1 
ATOM   1529  N  N     . PRO A 1 198 ? -13.004 -22.987 -8.210  1.00 29.87 ?  198 PRO A N     1 
ATOM   1530  C  CA    . PRO A 1 198 ? -13.905 -23.511 -9.241  1.00 28.45 ?  198 PRO A CA    1 
ATOM   1531  C  C     . PRO A 1 198 ? -14.073 -22.531 -10.402 1.00 30.46 ?  198 PRO A C     1 
ATOM   1532  O  O     . PRO A 1 198 ? -13.563 -21.414 -10.350 1.00 27.62 ?  198 PRO A O     1 
ATOM   1533  C  CB    . PRO A 1 198 ? -15.227 -23.795 -8.495  1.00 27.44 ?  198 PRO A CB    1 
ATOM   1534  C  CG    . PRO A 1 198 ? -15.141 -22.977 -7.220  1.00 29.14 ?  198 PRO A CG    1 
ATOM   1535  C  CD    . PRO A 1 198 ? -13.662 -22.823 -6.904  1.00 28.75 ?  198 PRO A CD    1 
ATOM   1536  N  N     . LEU A 1 199 ? -14.788 -22.960 -11.451 1.00 35.41 ?  199 LEU A N     1 
ATOM   1537  C  CA    . LEU A 1 199 ? -14.838 -22.225 -12.707 1.00 34.51 ?  199 LEU A CA    1 
ATOM   1538  C  C     . LEU A 1 199 ? -15.844 -21.081 -12.598 1.00 35.85 ?  199 LEU A C     1 
ATOM   1539  O  O     . LEU A 1 199 ? -15.717 -20.069 -13.284 1.00 35.43 ?  199 LEU A O     1 
ATOM   1540  C  CB    . LEU A 1 199 ? -15.183 -23.167 -13.862 1.00 35.67 ?  199 LEU A CB    1 
ATOM   1541  C  CG    . LEU A 1 199 ? -14.138 -24.234 -14.207 1.00 36.98 ?  199 LEU A CG    1 
ATOM   1542  C  CD1   . LEU A 1 199 ? -14.626 -25.143 -15.324 1.00 36.72 ?  199 LEU A CD1   1 
ATOM   1543  C  CD2   . LEU A 1 199 ? -12.806 -23.609 -14.590 1.00 38.75 ?  199 LEU A CD2   1 
ATOM   1544  N  N     . ASP A 1 200 ? -16.839 -21.261 -11.723 1.00 35.05 ?  200 ASP A N     1 
ATOM   1545  C  CA    . ASP A 1 200 ? -17.902 -20.289 -11.533 1.00 35.54 ?  200 ASP A CA    1 
ATOM   1546  C  C     . ASP A 1 200 ? -17.554 -19.327 -10.397 1.00 34.43 ?  200 ASP A C     1 
ATOM   1547  O  O     . ASP A 1 200 ? -18.368 -18.479 -10.037 1.00 34.75 ?  200 ASP A O     1 
ATOM   1548  C  CB    . ASP A 1 200 ? -19.222 -20.991 -11.255 1.00 35.21 ?  200 ASP A CB    1 
ATOM   1549  C  CG    . ASP A 1 200 ? -19.223 -21.888 -10.025 1.00 32.95 ?  200 ASP A CG    1 
ATOM   1550  O  OD1   . ASP A 1 200 ? -18.160 -21.993 -9.377  1.00 27.69 ?  200 ASP A OD1   1 
ATOM   1551  O  OD2   . ASP A 1 200 ? -20.287 -22.468 -9.721  1.00 33.14 -1 200 ASP A OD2   1 
ATOM   1552  N  N     . HIS A 1 201 ? -16.344 -19.459 -9.838  1.00 31.35 ?  201 HIS A N     1 
ATOM   1553  C  CA    . HIS A 1 201 ? -15.917 -18.624 -8.724  1.00 29.02 ?  201 HIS A CA    1 
ATOM   1554  C  C     . HIS A 1 201 ? -15.853 -17.168 -9.177  1.00 27.02 ?  201 HIS A C     1 
ATOM   1555  O  O     . HIS A 1 201 ? -15.126 -16.838 -10.111 1.00 26.48 ?  201 HIS A O     1 
ATOM   1556  C  CB    . HIS A 1 201 ? -14.567 -19.101 -8.173  1.00 30.91 ?  201 HIS A CB    1 
ATOM   1557  C  CG    . HIS A 1 201 ? -14.051 -18.318 -7.007  1.00 26.97 ?  201 HIS A CG    1 
ATOM   1558  N  ND1   . HIS A 1 201 ? -14.440 -18.570 -5.709  1.00 26.82 ?  201 HIS A ND1   1 
ATOM   1559  C  CD2   . HIS A 1 201 ? -13.174 -17.305 -6.937  1.00 25.86 ?  201 HIS A CD2   1 
ATOM   1560  C  CE1   . HIS A 1 201 ? -13.818 -17.731 -4.893  1.00 25.33 ?  201 HIS A CE1   1 
ATOM   1561  N  NE2   . HIS A 1 201 ? -13.044 -16.953 -5.617  1.00 24.63 ?  201 HIS A NE2   1 
ATOM   1562  N  N     . GLU A 1 202 ? -16.622 -16.304 -8.505  1.00 27.14 ?  202 GLU A N     1 
ATOM   1563  C  CA    . GLU A 1 202 ? -16.643 -14.890 -8.837  1.00 24.08 ?  202 GLU A CA    1 
ATOM   1564  C  C     . GLU A 1 202 ? -15.232 -14.335 -8.662  1.00 23.05 ?  202 GLU A C     1 
ATOM   1565  O  O     . GLU A 1 202 ? -14.635 -14.478 -7.598  1.00 21.90 ?  202 GLU A O     1 
ATOM   1566  C  CB    . GLU A 1 202 ? -17.657 -14.142 -7.968  1.00 26.12 ?  202 GLU A CB    1 
ATOM   1567  C  CG    . GLU A 1 202 ? -17.850 -12.678 -8.359  1.00 29.35 ?  202 GLU A CG    1 
ATOM   1568  C  CD    . GLU A 1 202 ? -18.979 -11.982 -7.618  1.00 31.77 ?  202 GLU A CD    1 
ATOM   1569  O  OE1   . GLU A 1 202 ? -18.939 -11.958 -6.369  1.00 33.62 ?  202 GLU A OE1   1 
ATOM   1570  O  OE2   . GLU A 1 202 ? -19.898 -11.462 -8.286  1.00 29.77 -1 202 GLU A OE2   1 
ATOM   1571  N  N     . VAL A 1 203 ? -14.692 -13.735 -9.728  1.00 21.06 ?  203 VAL A N     1 
ATOM   1572  C  CA    . VAL A 1 203 ? -13.475 -12.950 -9.609  1.00 20.58 ?  203 VAL A CA    1 
ATOM   1573  C  C     . VAL A 1 203 ? -13.814 -11.512 -9.988  1.00 19.37 ?  203 VAL A C     1 
ATOM   1574  O  O     . VAL A 1 203 ? -14.923 -11.225 -10.436 1.00 18.88 ?  203 VAL A O     1 
ATOM   1575  C  CB    . VAL A 1 203 ? -12.285 -13.487 -10.429 1.00 20.82 ?  203 VAL A CB    1 
ATOM   1576  C  CG1   . VAL A 1 203 ? -11.804 -14.832 -9.898  1.00 21.07 ?  203 VAL A CG1   1 
ATOM   1577  C  CG2   . VAL A 1 203 ? -12.594 -13.566 -11.919 1.00 21.03 ?  203 VAL A CG2   1 
ATOM   1578  N  N     . VAL A 1 204 ? -12.845 -10.615 -9.791  1.00 18.27 ?  204 VAL A N     1 
ATOM   1579  C  CA    . VAL A 1 204 ? -13.077 -9.190  -9.945  1.00 17.30 ?  204 VAL A CA    1 
ATOM   1580  C  C     . VAL A 1 204 ? -11.969 -8.588  -10.799 1.00 17.44 ?  204 VAL A C     1 
ATOM   1581  O  O     . VAL A 1 204 ? -10.789 -8.753  -10.495 1.00 18.75 ?  204 VAL A O     1 
ATOM   1582  C  CB    . VAL A 1 204 ? -13.136 -8.491  -8.574  1.00 15.65 ?  204 VAL A CB    1 
ATOM   1583  C  CG1   . VAL A 1 204 ? -13.259 -6.979  -8.717  1.00 17.08 ?  204 VAL A CG1   1 
ATOM   1584  C  CG2   . VAL A 1 204 ? -14.253 -9.049  -7.701  1.00 15.25 ?  204 VAL A CG2   1 
ATOM   1585  N  N     . ILE A 1 205 ? -12.364 -7.870  -11.854 1.00 18.71 ?  205 ILE A N     1 
ATOM   1586  C  CA    . ILE A 1 205 ? -11.418 -7.067  -12.607 1.00 19.49 ?  205 ILE A CA    1 
ATOM   1587  C  C     . ILE A 1 205 ? -11.492 -5.634  -12.091 1.00 21.86 ?  205 ILE A C     1 
ATOM   1588  O  O     . ILE A 1 205 ? -12.499 -4.949  -12.263 1.00 20.22 ?  205 ILE A O     1 
ATOM   1589  C  CB    . ILE A 1 205 ? -11.663 -7.141  -14.124 1.00 18.98 ?  205 ILE A CB    1 
ATOM   1590  C  CG1   . ILE A 1 205 ? -11.543 -8.574  -14.650 1.00 20.10 ?  205 ILE A CG1   1 
ATOM   1591  C  CG2   . ILE A 1 205 ? -10.713 -6.191  -14.852 1.00 19.71 ?  205 ILE A CG2   1 
ATOM   1592  C  CD1   . ILE A 1 205 ? -11.999 -8.745  -16.088 1.00 20.51 ?  205 ILE A CD1   1 
ATOM   1593  N  N     . TYR A 1 206 ? -10.397 -5.203  -11.462 1.00 21.86 ?  206 TYR A N     1 
ATOM   1594  C  CA    . TYR A 1 206 ? -10.345 -3.916  -10.797 1.00 22.35 ?  206 TYR A CA    1 
ATOM   1595  C  C     . TYR A 1 206 ? -9.386  -2.997  -11.544 1.00 23.46 ?  206 TYR A C     1 
ATOM   1596  O  O     . TYR A 1 206 ? -8.312  -3.418  -11.967 1.00 23.64 ?  206 TYR A O     1 
ATOM   1597  C  CB    . TYR A 1 206 ? -9.910  -4.089  -9.339  1.00 23.63 ?  206 TYR A CB    1 
ATOM   1598  C  CG    . TYR A 1 206 ? -9.593  -2.773  -8.642  1.00 25.00 ?  206 TYR A CG    1 
ATOM   1599  C  CD1   . TYR A 1 206 ? -10.598 -2.004  -8.069  1.00 22.28 ?  206 TYR A CD1   1 
ATOM   1600  C  CD2   . TYR A 1 206 ? -8.290  -2.296  -8.567  1.00 25.61 ?  206 TYR A CD2   1 
ATOM   1601  C  CE1   . TYR A 1 206 ? -10.317 -0.803  -7.438  1.00 21.53 ?  206 TYR A CE1   1 
ATOM   1602  C  CE2   . TYR A 1 206 ? -7.996  -1.097  -7.940  1.00 25.76 ?  206 TYR A CE2   1 
ATOM   1603  C  CZ    . TYR A 1 206 ? -9.012  -0.349  -7.373  1.00 23.55 ?  206 TYR A CZ    1 
ATOM   1604  O  OH    . TYR A 1 206 ? -8.726  0.834   -6.754  1.00 23.99 ?  206 TYR A OH    1 
ATOM   1605  N  N     . GLU A 1 207 ? -9.805  -1.737  -11.696 1.00 20.25 ?  207 GLU A N     1 
ATOM   1606  C  CA    . GLU A 1 207 ? -8.932  -0.682  -12.179 1.00 22.96 ?  207 GLU A CA    1 
ATOM   1607  C  C     . GLU A 1 207 ? -9.236  0.597   -11.406 1.00 23.39 ?  207 GLU A C     1 
ATOM   1608  O  O     . GLU A 1 207 ? -10.328 1.150   -11.522 1.00 26.61 ?  207 GLU A O     1 
ATOM   1609  C  CB    . GLU A 1 207 ? -9.128  -0.424  -13.673 1.00 22.87 ?  207 GLU A CB    1 
ATOM   1610  C  CG    . GLU A 1 207 ? -9.114  -1.690  -14.525 1.00 21.94 ?  207 GLU A CG    1 
ATOM   1611  C  CD    . GLU A 1 207 ? -9.392  -1.434  -15.995 1.00 22.20 ?  207 GLU A CD    1 
ATOM   1612  O  OE1   . GLU A 1 207 ? -9.670  -0.270  -16.354 1.00 22.69 ?  207 GLU A OE1   1 
ATOM   1613  O  OE2   . GLU A 1 207 ? -9.327  -2.398  -16.786 1.00 21.82 -1 207 GLU A OE2   1 
ATOM   1614  N  N     . ALA A 1 208 ? -8.262  1.050   -10.612 1.00 22.33 ?  208 ALA A N     1 
ATOM   1615  C  CA    . ALA A 1 208 ? -8.365  2.315   -9.905  1.00 20.46 ?  208 ALA A CA    1 
ATOM   1616  C  C     . ALA A 1 208 ? -8.449  3.455   -10.914 1.00 17.73 ?  208 ALA A C     1 
ATOM   1617  O  O     . ALA A 1 208 ? -7.763  3.433   -11.933 1.00 17.74 ?  208 ALA A O     1 
ATOM   1618  C  CB    . ALA A 1 208 ? -7.174  2.486   -8.988  1.00 20.30 ?  208 ALA A CB    1 
ATOM   1619  N  N     . ALA A 1 209 ? -9.287  4.454   -10.622 1.00 17.16 ?  209 ALA A N     1 
ATOM   1620  C  CA    . ALA A 1 209 ? -9.401  5.614   -11.489 1.00 17.13 ?  209 ALA A CA    1 
ATOM   1621  C  C     . ALA A 1 209 ? -8.106  6.419   -11.431 1.00 16.69 ?  209 ALA A C     1 
ATOM   1622  O  O     . ALA A 1 209 ? -7.421  6.427   -10.412 1.00 19.02 ?  209 ALA A O     1 
ATOM   1623  C  CB    . ALA A 1 209 ? -10.597 6.450   -11.091 1.00 17.78 ?  209 ALA A CB    1 
ATOM   1624  N  N     . ASN A 1 210 ? -7.780  7.082   -12.546 1.00 15.60 ?  210 ASN A N     1 
ATOM   1625  C  CA    . ASN A 1 210 ? -6.614  7.947   -12.627 1.00 15.72 ?  210 ASN A CA    1 
ATOM   1626  C  C     . ASN A 1 210 ? -7.055  9.410   -12.634 1.00 16.20 ?  210 ASN A C     1 
ATOM   1627  O  O     . ASN A 1 210 ? -6.228  10.311  -12.501 1.00 13.54 ?  210 ASN A O     1 
ATOM   1628  C  CB    . ASN A 1 210 ? -5.765  7.615   -13.850 1.00 15.83 ?  210 ASN A CB    1 
ATOM   1629  C  CG    . ASN A 1 210 ? -5.148  6.239   -13.758 1.00 15.64 ?  210 ASN A CG    1 
ATOM   1630  O  OD1   . ASN A 1 210 ? -4.433  5.942   -12.795 1.00 15.15 ?  210 ASN A OD1   1 
ATOM   1631  N  ND2   . ASN A 1 210 ? -5.414  5.388   -14.738 1.00 15.43 ?  210 ASN A ND2   1 
ATOM   1632  N  N     . LEU A 1 211 ? -8.366  9.637   -12.785 1.00 16.68 ?  211 LEU A N     1 
ATOM   1633  C  CA    . LEU A 1 211 ? -8.915  10.983  -12.866 1.00 18.07 ?  211 LEU A CA    1 
ATOM   1634  C  C     . LEU A 1 211 ? -10.002 11.166  -11.809 1.00 17.36 ?  211 LEU A C     1 
ATOM   1635  O  O     . LEU A 1 211 ? -10.698 10.218  -11.452 1.00 15.61 ?  211 LEU A O     1 
ATOM   1636  C  CB    . LEU A 1 211 ? -9.470  11.245  -14.264 1.00 20.27 ?  211 LEU A CB    1 
ATOM   1637  C  CG    . LEU A 1 211 ? -8.456  11.306  -15.410 1.00 22.16 ?  211 LEU A CG    1 
ATOM   1638  C  CD1   . LEU A 1 211 ? -9.206  11.679  -16.675 1.00 23.46 ?  211 LEU A CD1   1 
ATOM   1639  C  CD2   . LEU A 1 211 ? -7.314  12.277  -15.154 1.00 24.39 ?  211 LEU A CD2   1 
ATOM   1640  N  N     . PRO A 1 212 ? -10.189 12.403  -11.292 1.00 17.25 ?  212 PRO A N     1 
ATOM   1641  C  CA    . PRO A 1 212 ? -11.163 12.658  -10.229 1.00 16.90 ?  212 PRO A CA    1 
ATOM   1642  C  C     . PRO A 1 212 ? -12.617 12.420  -10.634 1.00 20.73 ?  212 PRO A C     1 
ATOM   1643  O  O     . PRO A 1 212 ? -13.452 12.105  -9.789  1.00 19.64 ?  212 PRO A O     1 
ATOM   1644  C  CB    . PRO A 1 212 ? -10.904 14.126  -9.826  1.00 16.35 ?  212 PRO A CB    1 
ATOM   1645  C  CG    . PRO A 1 212 ? -10.160 14.738  -10.995 1.00 16.41 ?  212 PRO A CG    1 
ATOM   1646  C  CD    . PRO A 1 212 ? -9.433  13.602  -11.685 1.00 16.62 ?  212 PRO A CD    1 
ATOM   1647  N  N     . ILE A 1 213 ? -12.905 12.564  -11.933 1.00 22.84 ?  213 ILE A N     1 
ATOM   1648  C  CA    . ILE A 1 213 ? -14.259 12.441  -12.449 1.00 25.87 ?  213 ILE A CA    1 
ATOM   1649  C  C     . ILE A 1 213 ? -14.475 11.031  -12.992 1.00 27.76 ?  213 ILE A C     1 
ATOM   1650  O  O     . ILE A 1 213 ? -15.459 10.771  -13.682 1.00 30.03 ?  213 ILE A O     1 
ATOM   1651  C  CB    . ILE A 1 213 ? -14.533 13.516  -13.520 1.00 26.59 ?  213 ILE A CB    1 
ATOM   1652  C  CG1   . ILE A 1 213 ? -13.525 13.465  -14.676 1.00 28.13 ?  213 ILE A CG1   1 
ATOM   1653  C  CG2   . ILE A 1 213 ? -14.569 14.905  -12.882 1.00 27.89 ?  213 ILE A CG2   1 
ATOM   1654  C  CD1   . ILE A 1 213 ? -13.444 12.130  -15.393 1.00 29.86 ?  213 ILE A CD1   1 
ATOM   1655  N  N     . GLN A 1 214 ? -13.551 10.123  -12.661 1.00 26.85 ?  214 GLN A N     1 
ATOM   1656  C  CA    . GLN A 1 214 ? -13.596 8.761   -13.167 1.00 24.91 ?  214 GLN A CA    1 
ATOM   1657  C  C     . GLN A 1 214 ? -13.964 7.806   -12.037 1.00 22.67 ?  214 GLN A C     1 
ATOM   1658  O  O     . GLN A 1 214 ? -13.331 7.810   -10.983 1.00 23.04 ?  214 GLN A O     1 
ATOM   1659  C  CB    . GLN A 1 214 ? -12.246 8.353   -13.757 1.00 26.58 ?  214 GLN A CB    1 
ATOM   1660  C  CG    . GLN A 1 214 ? -12.211 6.924   -14.289 1.00 26.51 ?  214 GLN A CG    1 
ATOM   1661  C  CD    . GLN A 1 214 ? -10.831 6.476   -14.719 1.00 25.87 ?  214 GLN A CD    1 
ATOM   1662  O  OE1   . GLN A 1 214 ? -9.870  7.254   -14.723 1.00 25.16 ?  214 GLN A OE1   1 
ATOM   1663  N  NE2   . GLN A 1 214 ? -10.719 5.208   -15.086 1.00 24.06 ?  214 GLN A NE2   1 
ATOM   1664  N  N     . ALA A 1 215 ? -14.998 6.992   -12.270 1.00 20.02 ?  215 ALA A N     1 
ATOM   1665  C  CA    . ALA A 1 215 ? -15.321 5.899   -11.370 1.00 22.90 ?  215 ALA A CA    1 
ATOM   1666  C  C     . ALA A 1 215 ? -14.362 4.744   -11.633 1.00 21.60 ?  215 ALA A C     1 
ATOM   1667  O  O     . ALA A 1 215 ? -13.890 4.568   -12.754 1.00 19.85 ?  215 ALA A O     1 
ATOM   1668  C  CB    . ALA A 1 215 ? -16.761 5.473   -11.551 1.00 24.56 ?  215 ALA A CB    1 
ATOM   1669  N  N     . PRO A 1 216 ? -14.038 3.928   -10.606 1.00 22.12 ?  216 PRO A N     1 
ATOM   1670  C  CA    . PRO A 1 216 ? -13.167 2.769   -10.792 1.00 23.68 ?  216 PRO A CA    1 
ATOM   1671  C  C     . PRO A 1 216 ? -13.902 1.624   -11.481 1.00 22.76 ?  216 PRO A C     1 
ATOM   1672  O  O     . PRO A 1 216 ? -15.124 1.529   -11.403 1.00 27.11 ?  216 PRO A O     1 
ATOM   1673  C  CB    . PRO A 1 216 ? -12.779 2.431   -9.346  1.00 23.56 ?  216 PRO A CB    1 
ATOM   1674  C  CG    . PRO A 1 216 ? -14.017 2.796   -8.558  1.00 22.88 ?  216 PRO A CG    1 
ATOM   1675  C  CD    . PRO A 1 216 ? -14.497 4.081   -9.216  1.00 23.65 ?  216 PRO A CD    1 
ATOM   1676  N  N     . ARG A 1 217 ? -13.139 0.760   -12.156 1.00 23.29 ?  217 ARG A N     1 
ATOM   1677  C  CA    . ARG A 1 217 ? -13.695 -0.437  -12.761 1.00 21.20 ?  217 ARG A CA    1 
ATOM   1678  C  C     . ARG A 1 217 ? -13.695 -1.554  -11.722 1.00 20.73 ?  217 ARG A C     1 
ATOM   1679  O  O     . ARG A 1 217 ? -12.653 -1.888  -11.162 1.00 16.87 ?  217 ARG A O     1 
ATOM   1680  C  CB    . ARG A 1 217 ? -12.898 -0.843  -14.006 1.00 22.28 ?  217 ARG A CB    1 
ATOM   1681  C  CG    . ARG A 1 217 ? -13.465 -2.052  -14.736 1.00 21.76 ?  217 ARG A CG    1 
ATOM   1682  C  CD    . ARG A 1 217 ? -12.601 -2.465  -15.918 1.00 24.29 ?  217 ARG A CD    1 
ATOM   1683  N  NE    . ARG A 1 217 ? -13.124 -3.655  -16.599 1.00 24.70 ?  217 ARG A NE    1 
ATOM   1684  C  CZ    . ARG A 1 217 ? -12.484 -4.333  -17.545 1.00 23.12 ?  217 ARG A CZ    1 
ATOM   1685  N  NH1   . ARG A 1 217 ? -11.266 -3.976  -17.914 1.00 21.62 1  217 ARG A NH1   1 
ATOM   1686  N  NH2   . ARG A 1 217 ? -13.064 -5.376  -18.111 1.00 20.82 ?  217 ARG A NH2   1 
ATOM   1687  N  N     . ILE A 1 218 ? -14.884 -2.108  -11.465 1.00 24.46 ?  218 ILE A N     1 
ATOM   1688  C  CA    . ILE A 1 218 ? -15.045 -3.229  -10.554 1.00 26.71 ?  218 ILE A CA    1 
ATOM   1689  C  C     . ILE A 1 218 ? -15.970 -4.246  -11.218 1.00 31.27 ?  218 ILE A C     1 
ATOM   1690  O  O     . ILE A 1 218 ? -17.154 -4.323  -10.897 1.00 35.22 ?  218 ILE A O     1 
ATOM   1691  C  CB    . ILE A 1 218 ? -15.576 -2.761  -9.186  1.00 26.55 ?  218 ILE A CB    1 
ATOM   1692  C  CG1   . ILE A 1 218 ? -14.672 -1.689  -8.570  1.00 26.69 ?  218 ILE A CG1   1 
ATOM   1693  C  CG2   . ILE A 1 218 ? -15.774 -3.946  -8.240  1.00 25.31 ?  218 ILE A CG2   1 
ATOM   1694  C  CD1   . ILE A 1 218 ? -15.097 -1.232  -7.185  1.00 25.39 ?  218 ILE A CD1   1 
ATOM   1695  N  N     . GLU A 1 219 ? -15.403 -5.021  -12.148 1.00 30.92 ?  219 GLU A N     1 
ATOM   1696  C  CA    . GLU A 1 219 ? -16.175 -5.904  -13.006 1.00 26.28 ?  219 GLU A CA    1 
ATOM   1697  C  C     . GLU A 1 219 ? -16.095 -7.337  -12.488 1.00 24.05 ?  219 GLU A C     1 
ATOM   1698  O  O     . GLU A 1 219 ? -15.040 -7.967  -12.528 1.00 21.32 ?  219 GLU A O     1 
ATOM   1699  C  CB    . GLU A 1 219 ? -15.662 -5.790  -14.441 1.00 25.39 ?  219 GLU A CB    1 
ATOM   1700  C  CG    . GLU A 1 219 ? -16.445 -6.635  -15.441 1.00 26.55 ?  219 GLU A CG    1 
ATOM   1701  C  CD    . GLU A 1 219 ? -15.998 -6.431  -16.878 1.00 25.95 ?  219 GLU A CD    1 
ATOM   1702  O  OE1   . GLU A 1 219 ? -15.145 -5.548  -17.107 1.00 24.45 ?  219 GLU A OE1   1 
ATOM   1703  O  OE2   . GLU A 1 219 ? -16.494 -7.156  -17.767 1.00 26.11 -1 219 GLU A OE2   1 
ATOM   1704  N  N     . ARG A 1 220 ? -17.243 -7.833  -12.016 1.00 19.98 ?  220 ARG A N     1 
ATOM   1705  C  CA    . ARG A 1 220 ? -17.365 -9.168  -11.460 1.00 19.61 ?  220 ARG A CA    1 
ATOM   1706  C  C     . ARG A 1 220 ? -17.783 -10.146 -12.555 1.00 21.32 ?  220 ARG A C     1 
ATOM   1707  O  O     . ARG A 1 220 ? -18.654 -9.842  -13.367 1.00 21.74 ?  220 ARG A O     1 
ATOM   1708  C  CB    . ARG A 1 220 ? -18.396 -9.124  -10.328 1.00 22.13 ?  220 ARG A CB    1 
ATOM   1709  C  CG    . ARG A 1 220 ? -17.911 -8.400  -9.082  1.00 22.95 ?  220 ARG A CG    1 
ATOM   1710  C  CD    . ARG A 1 220 ? -19.061 -8.021  -8.165  1.00 24.35 ?  220 ARG A CD    1 
ATOM   1711  N  NE    . ARG A 1 220 ? -18.620 -7.060  -7.149  1.00 25.07 ?  220 ARG A NE    1 
ATOM   1712  C  CZ    . ARG A 1 220 ? -17.890 -7.366  -6.085  1.00 26.73 ?  220 ARG A CZ    1 
ATOM   1713  N  NH1   . ARG A 1 220 ? -17.640 -8.631  -5.794  1.00 29.77 1  220 ARG A NH1   1 
ATOM   1714  N  NH2   . ARG A 1 220 ? -17.441 -6.406  -5.298  1.00 22.49 ?  220 ARG A NH2   1 
ATOM   1715  N  N     . LEU A 1 221 ? -17.154 -11.326 -12.557 1.00 20.40 ?  221 LEU A N     1 
ATOM   1716  C  CA    . LEU A 1 221 ? -17.451 -12.357 -13.538 1.00 21.48 ?  221 LEU A CA    1 
ATOM   1717  C  C     . LEU A 1 221 ? -16.962 -13.703 -13.017 1.00 23.53 ?  221 LEU A C     1 
ATOM   1718  O  O     . LEU A 1 221 ? -16.020 -13.764 -12.229 1.00 21.87 ?  221 LEU A O     1 
ATOM   1719  C  CB    . LEU A 1 221 ? -16.807 -12.042 -14.889 1.00 23.92 ?  221 LEU A CB    1 
ATOM   1720  C  CG    . LEU A 1 221 ? -15.275 -12.025 -14.926 1.00 23.05 ?  221 LEU A CG    1 
ATOM   1721  C  CD1   . LEU A 1 221 ? -14.771 -12.086 -16.359 1.00 24.48 ?  221 LEU A CD1   1 
ATOM   1722  C  CD2   . LEU A 1 221 ? -14.705 -10.802 -14.225 1.00 23.98 ?  221 LEU A CD2   1 
ATOM   1723  N  N     . PRO A 1 222 ? -17.584 -14.821 -13.454 1.00 27.75 ?  222 PRO A N     1 
ATOM   1724  C  CA    . PRO A 1 222 ? -17.070 -16.153 -13.145 1.00 28.93 ?  222 PRO A CA    1 
ATOM   1725  C  C     . PRO A 1 222 ? -15.671 -16.308 -13.734 1.00 28.66 ?  222 PRO A C     1 
ATOM   1726  O  O     . PRO A 1 222 ? -15.360 -15.727 -14.772 1.00 28.22 ?  222 PRO A O     1 
ATOM   1727  C  CB    . PRO A 1 222 ? -18.095 -17.124 -13.761 1.00 30.28 ?  222 PRO A CB    1 
ATOM   1728  C  CG    . PRO A 1 222 ? -18.867 -16.288 -14.765 1.00 30.80 ?  222 PRO A CG    1 
ATOM   1729  C  CD    . PRO A 1 222 ? -18.807 -14.852 -14.270 1.00 28.69 ?  222 PRO A CD    1 
ATOM   1730  N  N     . LEU A 1 223 ? -14.835 -17.092 -13.048 1.00 28.35 ?  223 LEU A N     1 
ATOM   1731  C  CA    . LEU A 1 223 ? -13.441 -17.268 -13.419 1.00 25.81 ?  223 LEU A CA    1 
ATOM   1732  C  C     . LEU A 1 223 ? -13.327 -17.733 -14.870 1.00 25.36 ?  223 LEU A C     1 
ATOM   1733  O  O     . LEU A 1 223 ? -12.449 -17.280 -15.602 1.00 26.08 ?  223 LEU A O     1 
ATOM   1734  C  CB    . LEU A 1 223 ? -12.824 -18.268 -12.442 1.00 24.60 ?  223 LEU A CB    1 
ATOM   1735  C  CG    . LEU A 1 223 ? -11.394 -18.727 -12.741 1.00 23.16 ?  223 LEU A CG    1 
ATOM   1736  C  CD1   . LEU A 1 223 ? -10.415 -17.569 -12.795 1.00 22.11 ?  223 LEU A CD1   1 
ATOM   1737  C  CD2   . LEU A 1 223 ? -10.960 -19.742 -11.698 1.00 23.42 ?  223 LEU A CD2   1 
ATOM   1738  N  N     . ALA A 1 224 ? -14.222 -18.640 -15.274 1.00 24.55 ?  224 ALA A N     1 
ATOM   1739  C  CA    . ALA A 1 224 ? -14.191 -19.226 -16.605 1.00 27.43 ?  224 ALA A CA    1 
ATOM   1740  C  C     . ALA A 1 224 ? -14.214 -18.144 -17.684 1.00 28.51 ?  224 ALA A C     1 
ATOM   1741  O  O     . ALA A 1 224 ? -13.628 -18.326 -18.749 1.00 27.54 ?  224 ALA A O     1 
ATOM   1742  C  CB    . ALA A 1 224 ? -15.350 -20.187 -16.771 1.00 28.46 ?  224 ALA A CB    1 
ATOM   1743  N  N     . ASN A 1 225 ? -14.890 -17.023 -17.407 1.00 28.48 ?  225 ASN A N     1 
ATOM   1744  C  CA    . ASN A 1 225 ? -15.160 -16.019 -18.426 1.00 27.79 ?  225 ASN A CA    1 
ATOM   1745  C  C     . ASN A 1 225 ? -13.947 -15.117 -18.649 1.00 24.03 ?  225 ASN A C     1 
ATOM   1746  O  O     . ASN A 1 225 ? -13.925 -14.338 -19.598 1.00 21.71 ?  225 ASN A O     1 
ATOM   1747  C  CB    . ASN A 1 225 ? -16.382 -15.173 -18.081 1.00 28.24 ?  225 ASN A CB    1 
ATOM   1748  C  CG    . ASN A 1 225 ? -17.675 -15.938 -18.230 1.00 29.90 ?  225 ASN A CG    1 
ATOM   1749  O  OD1   . ASN A 1 225 ? -17.660 -17.165 -18.378 1.00 33.83 ?  225 ASN A OD1   1 
ATOM   1750  N  ND2   . ASN A 1 225 ? -18.800 -15.239 -18.186 1.00 30.24 ?  225 ASN A ND2   1 
ATOM   1751  N  N     . LEU A 1 226 ? -12.934 -15.235 -17.784 1.00 23.91 ?  226 LEU A N     1 
ATOM   1752  C  CA    . LEU A 1 226 ? -11.839 -14.278 -17.750 1.00 21.82 ?  226 LEU A CA    1 
ATOM   1753  C  C     . LEU A 1 226 ? -11.211 -14.130 -19.134 1.00 23.12 ?  226 LEU A C     1 
ATOM   1754  O  O     . LEU A 1 226 ? -10.935 -13.018 -19.578 1.00 22.59 ?  226 LEU A O     1 
ATOM   1755  C  CB    . LEU A 1 226 ? -10.804 -14.717 -16.717 1.00 21.97 ?  226 LEU A CB    1 
ATOM   1756  C  CG    . LEU A 1 226 ? -9.460  -13.984 -16.766 1.00 22.00 ?  226 LEU A CG    1 
ATOM   1757  C  CD1   . LEU A 1 226 ? -9.618  -12.514 -16.408 1.00 23.30 ?  226 LEU A CD1   1 
ATOM   1758  C  CD2   . LEU A 1 226 ? -8.458  -14.668 -15.852 1.00 23.10 ?  226 LEU A CD2   1 
ATOM   1759  N  N     . PRO A 1 227 ? -10.936 -15.247 -19.844 1.00 26.66 ?  227 PRO A N     1 
ATOM   1760  C  CA    . PRO A 1 227 ? -10.259 -15.195 -21.143 1.00 26.99 ?  227 PRO A CA    1 
ATOM   1761  C  C     . PRO A 1 227 ? -10.965 -14.371 -22.218 1.00 26.90 ?  227 PRO A C     1 
ATOM   1762  O  O     . PRO A 1 227 ? -10.336 -13.950 -23.187 1.00 25.63 ?  227 PRO A O     1 
ATOM   1763  C  CB    . PRO A 1 227 ? -10.180 -16.685 -21.524 1.00 25.93 ?  227 PRO A CB    1 
ATOM   1764  C  CG    . PRO A 1 227 ? -10.199 -17.404 -20.198 1.00 26.40 ?  227 PRO A CG    1 
ATOM   1765  C  CD    . PRO A 1 227 ? -11.221 -16.621 -19.402 1.00 25.80 ?  227 PRO A CD    1 
ATOM   1766  N  N     . GLN A 1 228 ? -12.273 -14.155 -22.045 1.00 26.65 ?  228 GLN A N     1 
ATOM   1767  C  CA    . GLN A 1 228 ? -13.050 -13.368 -22.988 1.00 29.96 ?  228 GLN A CA    1 
ATOM   1768  C  C     . GLN A 1 228 ? -13.051 -11.903 -22.554 1.00 32.29 ?  228 GLN A C     1 
ATOM   1769  O  O     . GLN A 1 228 ? -13.302 -11.012 -23.362 1.00 27.58 ?  228 GLN A O     1 
ATOM   1770  C  CB    . GLN A 1 228 ? -14.485 -13.884 -23.108 1.00 34.99 ?  228 GLN A CB    1 
ATOM   1771  C  CG    . GLN A 1 228 ? -14.628 -15.162 -23.930 1.00 37.95 ?  228 GLN A CG    1 
ATOM   1772  C  CD    . GLN A 1 228 ? -14.306 -16.419 -23.152 1.00 40.17 ?  228 GLN A CD    1 
ATOM   1773  O  OE1   . GLN A 1 228 ? -15.005 -16.784 -22.199 1.00 42.39 ?  228 GLN A OE1   1 
ATOM   1774  N  NE2   . GLN A 1 228 ? -13.248 -17.105 -23.561 1.00 41.22 ?  228 GLN A NE2   1 
ATOM   1775  N  N     . ALA A 1 229 ? -12.753 -11.673 -21.271 1.00 31.30 ?  229 ALA A N     1 
ATOM   1776  C  CA    . ALA A 1 229 ? -12.859 -10.353 -20.670 1.00 29.68 ?  229 ALA A CA    1 
ATOM   1777  C  C     . ALA A 1 229 ? -11.957 -9.355  -21.389 1.00 29.64 ?  229 ALA A C     1 
ATOM   1778  O  O     . ALA A 1 229 ? -10.937 -9.724  -21.966 1.00 32.98 ?  229 ALA A O     1 
ATOM   1779  C  CB    . ALA A 1 229 ? -12.518 -10.431 -19.198 1.00 28.99 ?  229 ALA A CB    1 
ATOM   1780  N  N     . HIS A 1 230 ? -12.361 -8.082  -21.338 1.00 29.58 ?  230 HIS A N     1 
ATOM   1781  C  CA    . HIS A 1 230 ? -11.550 -6.978  -21.822 1.00 29.27 ?  230 HIS A CA    1 
ATOM   1782  C  C     . HIS A 1 230 ? -10.634 -6.524  -20.687 1.00 30.15 ?  230 HIS A C     1 
ATOM   1783  O  O     . HIS A 1 230 ? -11.108 -6.122  -19.627 1.00 34.80 ?  230 HIS A O     1 
ATOM   1784  C  CB    . HIS A 1 230 ? -12.458 -5.863  -22.360 1.00 33.73 ?  230 HIS A CB    1 
ATOM   1785  C  CG    . HIS A 1 230 ? -11.739 -4.691  -22.944 1.00 35.86 ?  230 HIS A CG    1 
ATOM   1786  N  ND1   . HIS A 1 230 ? -11.056 -4.755  -24.139 1.00 38.49 ?  230 HIS A ND1   1 
ATOM   1787  C  CD2   . HIS A 1 230 ? -11.590 -3.436  -22.500 1.00 38.08 ?  230 HIS A CD2   1 
ATOM   1788  C  CE1   . HIS A 1 230 ? -10.523 -3.571  -24.403 1.00 36.68 ?  230 HIS A CE1   1 
ATOM   1789  N  NE2   . HIS A 1 230 ? -10.836 -2.754  -23.421 1.00 37.43 ?  230 HIS A NE2   1 
ATOM   1790  N  N     . LEU A 1 231 ? -9.320  -6.618  -20.920 1.00 26.54 ?  231 LEU A N     1 
ATOM   1791  C  CA    . LEU A 1 231 ? -8.324  -6.255  -19.925 1.00 25.88 ?  231 LEU A CA    1 
ATOM   1792  C  C     . LEU A 1 231 ? -7.438  -5.147  -20.485 1.00 24.30 ?  231 LEU A C     1 
ATOM   1793  O  O     . LEU A 1 231 ? -7.265  -5.029  -21.697 1.00 23.63 ?  231 LEU A O     1 
ATOM   1794  C  CB    . LEU A 1 231 ? -7.485  -7.468  -19.521 1.00 23.97 ?  231 LEU A CB    1 
ATOM   1795  C  CG    . LEU A 1 231 ? -8.243  -8.632  -18.876 1.00 23.93 ?  231 LEU A CG    1 
ATOM   1796  C  CD1   . LEU A 1 231 ? -7.405  -9.902  -18.850 1.00 24.59 ?  231 LEU A CD1   1 
ATOM   1797  C  CD2   . LEU A 1 231 ? -8.678  -8.253  -17.473 1.00 22.94 ?  231 LEU A CD2   1 
ATOM   1798  N  N     . MET A 1 232 ? -6.870  -4.352  -19.573 1.00 20.34 ?  232 MET A N     1 
ATOM   1799  C  CA    . MET A 1 232 ? -5.995  -3.248  -19.926 1.00 18.09 ?  232 MET A CA    1 
ATOM   1800  C  C     . MET A 1 232 ? -4.706  -3.362  -19.116 1.00 16.03 ?  232 MET A C     1 
ATOM   1801  O  O     . MET A 1 232 ? -4.667  -4.061  -18.106 1.00 13.18 ?  232 MET A O     1 
ATOM   1802  C  CB    . MET A 1 232 ? -6.680  -1.909  -19.633 1.00 20.81 ?  232 MET A CB    1 
ATOM   1803  C  CG    . MET A 1 232 ? -7.973  -1.702  -20.399 1.00 21.34 ?  232 MET A CG    1 
ATOM   1804  S  SD    . MET A 1 232 ? -7.705  -1.642  -22.181 1.00 26.44 ?  232 MET A SD    1 
ATOM   1805  C  CE    . MET A 1 232 ? -6.540  -0.276  -22.274 1.00 26.02 ?  232 MET A CE    1 
ATOM   1806  N  N     . PRO A 1 233 ? -3.607  -2.694  -19.533 1.00 14.77 ?  233 PRO A N     1 
ATOM   1807  C  CA    . PRO A 1 233 ? -2.346  -2.764  -18.791 1.00 16.22 ?  233 PRO A CA    1 
ATOM   1808  C  C     . PRO A 1 233 ? -2.475  -2.435  -17.305 1.00 18.70 ?  233 PRO A C     1 
ATOM   1809  O  O     . PRO A 1 233 ? -1.710  -2.947  -16.491 1.00 17.79 ?  233 PRO A O     1 
ATOM   1810  C  CB    . PRO A 1 233 ? -1.448  -1.761  -19.535 1.00 15.36 ?  233 PRO A CB    1 
ATOM   1811  C  CG    . PRO A 1 233 ? -2.010  -1.728  -20.939 1.00 14.99 ?  233 PRO A CG    1 
ATOM   1812  C  CD    . PRO A 1 233 ? -3.511  -1.878  -20.754 1.00 15.11 ?  233 PRO A CD    1 
ATOM   1813  N  N     . ILE A 1 234 ? -3.449  -1.584  -16.957 1.00 19.01 ?  234 ILE A N     1 
ATOM   1814  C  CA    . ILE A 1 234 ? -3.616  -1.129  -15.585 1.00 18.88 ?  234 ILE A CA    1 
ATOM   1815  C  C     . ILE A 1 234 ? -4.455  -2.134  -14.801 1.00 18.23 ?  234 ILE A C     1 
ATOM   1816  O  O     . ILE A 1 234 ? -4.627  -1.982  -13.594 1.00 17.51 ?  234 ILE A O     1 
ATOM   1817  C  CB    . ILE A 1 234 ? -4.245  0.277   -15.531 1.00 20.25 ?  234 ILE A CB    1 
ATOM   1818  C  CG1   . ILE A 1 234 ? -5.599  0.325   -16.249 1.00 21.79 ?  234 ILE A CG1   1 
ATOM   1819  C  CG2   . ILE A 1 234 ? -3.275  1.329   -16.066 1.00 20.31 ?  234 ILE A CG2   1 
ATOM   1820  C  CD1   . ILE A 1 234 ? -6.139  1.726   -16.477 1.00 23.09 ?  234 ILE A CD1   1 
ATOM   1821  N  N     . SER A 1 235 ? -4.967  -3.157  -15.492 1.00 17.74 ?  235 SER A N     1 
ATOM   1822  C  CA    . SER A 1 235 ? -5.922  -4.079  -14.901 1.00 17.06 ?  235 SER A CA    1 
ATOM   1823  C  C     . SER A 1 235 ? -5.241  -4.963  -13.860 1.00 17.51 ?  235 SER A C     1 
ATOM   1824  O  O     . SER A 1 235 ? -4.137  -5.455  -14.078 1.00 21.95 ?  235 SER A O     1 
ATOM   1825  C  CB    . SER A 1 235 ? -6.601  -4.907  -15.961 1.00 17.48 ?  235 SER A CB    1 
ATOM   1826  O  OG    . SER A 1 235 ? -7.414  -4.095  -16.796 1.00 15.21 ?  235 SER A OG    1 
ATOM   1827  N  N     . THR A 1 236 ? -5.921  -5.141  -12.724 1.00 18.65 ?  236 THR A N     1 
ATOM   1828  C  CA    . THR A 1 236 ? -5.515  -6.092  -11.704 1.00 17.35 ?  236 THR A CA    1 
ATOM   1829  C  C     . THR A 1 236 ? -6.668  -7.062  -11.479 1.00 16.92 ?  236 THR A C     1 
ATOM   1830  O  O     . THR A 1 236 ? -7.826  -6.652  -11.433 1.00 19.33 ?  236 THR A O     1 
ATOM   1831  C  CB    . THR A 1 236 ? -5.147  -5.365  -10.412 1.00 17.56 ?  236 THR A CB    1 
ATOM   1832  O  OG1   . THR A 1 236 ? -3.952  -4.647  -10.701 1.00 16.65 ?  236 THR A OG1   1 
ATOM   1833  C  CG2   . THR A 1 236 ? -4.918  -6.320  -9.254  1.00 18.09 ?  236 THR A CG2   1 
ATOM   1834  N  N     . LEU A 1 237 ? -6.332  -8.348  -11.343 1.00 14.09 ?  237 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 237 ? -7.319  -9.376  -11.072 1.00 13.26 ?  237 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 237 ? -7.323  -9.696  -9.580  1.00 14.85 ?  237 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 237 ? -6.286  -10.035 -9.014  1.00 14.30 ?  237 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 237 ? -7.004  -10.616 -11.907 1.00 11.39 ?  237 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 237 ? -7.980  -11.783 -11.738 1.00 12.01 ?  237 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 237 ? -9.364  -11.358 -12.198 1.00 11.32 ?  237 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 237 ? -7.520  -13.032 -12.472 1.00 13.01 ?  237 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 238 ? -8.504  -9.573  -8.960  1.00 17.91 ?  238 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 238 ? -8.720  -9.985  -7.582  1.00 19.54 ?  238 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 238 ? -9.457  -11.320 -7.581  1.00 21.79 ?  238 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 238 ? -10.518 -11.449 -8.187  1.00 26.73 ?  238 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 238 ? -9.521  -8.944  -6.799  1.00 19.28 ?  238 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 238 ? -9.928  -9.342  -5.374  1.00 19.22 ?  238 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 238 ? -8.795  -9.162  -4.375  1.00 19.82 ?  238 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 238 ? -11.155 -8.571  -4.921  1.00 19.36 ?  238 LEU A CD2   1 
ATOM   1850  N  N     . ILE A 1 239 ? -8.887  -12.304 -6.883  1.00 21.91 ?  239 ILE A N     1 
ATOM   1851  C  CA    . ILE A 1 239 ? -9.559  -13.573 -6.673  1.00 25.32 ?  239 ILE A CA    1 
ATOM   1852  C  C     . ILE A 1 239 ? -9.936  -13.680 -5.197  1.00 25.78 ?  239 ILE A C     1 
ATOM   1853  O  O     . ILE A 1 239 ? -9.074  -13.900 -4.349  1.00 30.95 ?  239 ILE A O     1 
ATOM   1854  C  CB    . ILE A 1 239 ? -8.661  -14.732 -7.146  1.00 23.39 ?  239 ILE A CB    1 
ATOM   1855  C  CG1   . ILE A 1 239 ? -8.238  -14.531 -8.606  1.00 22.71 ?  239 ILE A CG1   1 
ATOM   1856  C  CG2   . ILE A 1 239 ? -9.339  -16.084 -6.927  1.00 23.14 ?  239 ILE A CG2   1 
ATOM   1857  C  CD1   . ILE A 1 239 ? -7.244  -15.555 -9.122  1.00 24.41 ?  239 ILE A CD1   1 
ATOM   1858  N  N     . PRO A 1 240 ? -11.230 -13.499 -4.839  1.00 27.05 ?  240 PRO A N     1 
ATOM   1859  C  CA    . PRO A 1 240 ? -11.659 -13.556 -3.441  1.00 23.46 ?  240 PRO A CA    1 
ATOM   1860  C  C     . PRO A 1 240 ? -11.558 -14.970 -2.878  1.00 24.02 ?  240 PRO A C     1 
ATOM   1861  O  O     . PRO A 1 240 ? -11.576 -15.941 -3.632  1.00 20.23 ?  240 PRO A O     1 
ATOM   1862  C  CB    . PRO A 1 240 ? -13.117 -13.057 -3.492  1.00 23.80 ?  240 PRO A CB    1 
ATOM   1863  C  CG    . PRO A 1 240 ? -13.235 -12.374 -4.839  1.00 25.12 ?  240 PRO A CG    1 
ATOM   1864  C  CD    . PRO A 1 240 ? -12.345 -13.200 -5.751  1.00 25.67 ?  240 PRO A CD    1 
ATOM   1865  N  N     . PRO A 1 241 ? -11.453 -15.131 -1.539  1.00 25.09 ?  241 PRO A N     1 
ATOM   1866  C  CA    . PRO A 1 241 ? -11.424 -16.460 -0.932  1.00 25.74 ?  241 PRO A CA    1 
ATOM   1867  C  C     . PRO A 1 241 ? -12.388 -17.417 -1.625  1.00 28.36 ?  241 PRO A C     1 
ATOM   1868  O  O     . PRO A 1 241 ? -13.403 -16.994 -2.172  1.00 27.10 ?  241 PRO A O     1 
ATOM   1869  C  CB    . PRO A 1 241 ? -11.835 -16.151 0.513   1.00 25.94 ?  241 PRO A CB    1 
ATOM   1870  C  CG    . PRO A 1 241 ? -11.215 -14.797 0.775   1.00 26.47 ?  241 PRO A CG    1 
ATOM   1871  C  CD    . PRO A 1 241 ? -11.356 -14.049 -0.545  1.00 26.63 ?  241 PRO A CD    1 
ATOM   1872  N  N     . ALA A 1 242 ? -12.052 -18.709 -1.600  1.00 31.25 ?  242 ALA A N     1 
ATOM   1873  C  CA    . ALA A 1 242 ? -12.931 -19.731 -2.141  1.00 31.06 ?  242 ALA A CA    1 
ATOM   1874  C  C     . ALA A 1 242 ? -13.250 -20.764 -1.065  1.00 33.87 ?  242 ALA A C     1 
ATOM   1875  O  O     . ALA A 1 242 ? -14.036 -21.679 -1.299  1.00 28.35 ?  242 ALA A O     1 
ATOM   1876  C  CB    . ALA A 1 242 ? -12.288 -20.381 -3.346  1.00 31.81 ?  242 ALA A CB    1 
ATOM   1877  N  N     . LYS A 1 243 ? -12.636 -20.606 0.114   1.00 34.65 ?  243 LYS A N     1 
ATOM   1878  C  CA    . LYS A 1 243 ? -12.602 -21.683 1.088   1.00 42.46 ?  243 LYS A CA    1 
ATOM   1879  C  C     . LYS A 1 243 ? -12.836 -21.145 2.497   1.00 43.67 ?  243 LYS A C     1 
ATOM   1880  O  O     . LYS A 1 243 ? -12.527 -19.994 2.800   1.00 50.29 ?  243 LYS A O     1 
ATOM   1881  C  CB    . LYS A 1 243 ? -11.260 -22.419 0.986   1.00 46.57 ?  243 LYS A CB    1 
ATOM   1882  C  CG    . LYS A 1 243 ? -11.122 -23.661 1.859   1.00 51.09 ?  243 LYS A CG    1 
ATOM   1883  C  CD    . LYS A 1 243 ? -9.670  -24.082 2.059   1.00 58.28 ?  243 LYS A CD    1 
ATOM   1884  C  CE    . LYS A 1 243 ? -9.356  -24.509 3.462   1.00 63.93 ?  243 LYS A CE    1 
ATOM   1885  N  NZ    . LYS A 1 243 ? -9.596  -25.931 3.717   1.00 63.74 1  243 LYS A NZ    1 
ATOM   1886  N  N     . LYS A 1 244 ? -13.395 -22.017 3.342   1.00 38.70 ?  244 LYS A N     1 
ATOM   1887  C  CA    . LYS A 1 244 ? -13.632 -21.742 4.749   1.00 38.55 ?  244 LYS A CA    1 
ATOM   1888  C  C     . LYS A 1 244 ? -12.334 -21.921 5.531   1.00 45.82 ?  244 LYS A C     1 
ATOM   1889  O  O     . LYS A 1 244 ? -11.566 -22.846 5.273   1.00 45.61 ?  244 LYS A O     1 
ATOM   1890  C  CB    . LYS A 1 244 ? -14.743 -22.692 5.217   1.00 35.23 ?  244 LYS A CB    1 
ATOM   1891  C  CG    . LYS A 1 244 ? -14.481 -23.498 6.488   1.00 42.81 ?  244 LYS A CG    1 
ATOM   1892  C  CD    . LYS A 1 244 ? -15.168 -23.052 7.774   1.00 43.35 ?  244 LYS A CD    1 
ATOM   1893  C  CE    . LYS A 1 244 ? -16.663 -23.109 7.712   1.00 41.15 ?  244 LYS A CE    1 
ATOM   1894  N  NZ    . LYS A 1 244 ? -17.251 -21.776 7.560   1.00 42.76 1  244 LYS A NZ    1 
ATOM   1895  N  N     . LEU A 1 245 ? -12.100 -21.013 6.482   1.00 51.30 ?  245 LEU A N     1 
ATOM   1896  C  CA    . LEU A 1 245 ? -11.020 -21.173 7.438   1.00 51.94 ?  245 LEU A CA    1 
ATOM   1897  C  C     . LEU A 1 245 ? -11.267 -22.453 8.228   1.00 49.65 ?  245 LEU A C     1 
ATOM   1898  O  O     . LEU A 1 245 ? -12.337 -22.635 8.803   1.00 50.27 ?  245 LEU A O     1 
ATOM   1899  C  CB    . LEU A 1 245 ? -10.954 -19.949 8.350   1.00 49.56 ?  245 LEU A CB    1 
ATOM   1900  C  CG    . LEU A 1 245 ? -10.498 -18.648 7.682   1.00 49.37 ?  245 LEU A CG    1 
ATOM   1901  C  CD1   . LEU A 1 245 ? -10.872 -17.422 8.500   1.00 48.30 ?  245 LEU A CD1   1 
ATOM   1902  C  CD2   . LEU A 1 245 ? -9.000  -18.687 7.437   1.00 49.74 ?  245 LEU A CD2   1 
ATOM   1903  N  N     . GLU A 1 246 ? -10.274 -23.346 8.227   1.00 48.60 ?  246 GLU A N     1 
ATOM   1904  C  CA    . GLU A 1 246 ? -10.324 -24.527 9.069   1.00 49.62 ?  246 GLU A CA    1 
ATOM   1905  C  C     . GLU A 1 246 ? -9.559  -24.206 10.349  1.00 47.96 ?  246 GLU A C     1 
ATOM   1906  O  O     . GLU A 1 246 ? -8.515  -23.559 10.302  1.00 40.58 ?  246 GLU A O     1 
ATOM   1907  C  CB    . GLU A 1 246 ? -9.750  -25.746 8.343   1.00 52.17 ?  246 GLU A CB    1 
ATOM   1908  C  CG    . GLU A 1 246 ? -10.176 -25.860 6.881   1.00 54.88 ?  246 GLU A CG    1 
ATOM   1909  C  CD    . GLU A 1 246 ? -11.643 -26.153 6.616   1.00 51.45 ?  246 GLU A CD    1 
ATOM   1910  O  OE1   . GLU A 1 246 ? -12.000 -26.282 5.425   1.00 49.54 ?  246 GLU A OE1   1 
ATOM   1911  O  OE2   . GLU A 1 246 ? -12.426 -26.252 7.583   1.00 53.24 -1 246 GLU A OE2   1 
ATOM   1912  N  N     . TYR A 1 247 ? -10.098 -24.641 11.492  1.00 50.31 ?  247 TYR A N     1 
ATOM   1913  C  CA    . TYR A 1 247 ? -9.483  -24.340 12.772  1.00 51.07 ?  247 TYR A CA    1 
ATOM   1914  C  C     . TYR A 1 247 ? -8.148  -25.066 12.873  1.00 53.51 ?  247 TYR A C     1 
ATOM   1915  O  O     . TYR A 1 247 ? -8.060  -26.265 12.618  1.00 55.23 ?  247 TYR A O     1 
ATOM   1916  C  CB    . TYR A 1 247 ? -10.369 -24.707 13.965  1.00 50.25 ?  247 TYR A CB    1 
ATOM   1917  C  CG    . TYR A 1 247 ? -11.443 -23.669 14.245  1.00 49.77 ?  247 TYR A CG    1 
ATOM   1918  C  CD1   . TYR A 1 247 ? -11.132 -22.478 14.889  1.00 51.35 ?  247 TYR A CD1   1 
ATOM   1919  C  CD2   . TYR A 1 247 ? -12.761 -23.874 13.858  1.00 50.84 ?  247 TYR A CD2   1 
ATOM   1920  C  CE1   . TYR A 1 247 ? -12.099 -21.521 15.142  1.00 48.67 ?  247 TYR A CE1   1 
ATOM   1921  C  CE2   . TYR A 1 247 ? -13.739 -22.926 14.108  1.00 47.96 ?  247 TYR A CE2   1 
ATOM   1922  C  CZ    . TYR A 1 247 ? -13.407 -21.747 14.751  1.00 46.36 ?  247 TYR A CZ    1 
ATOM   1923  O  OH    . TYR A 1 247 ? -14.366 -20.808 14.999  1.00 53.93 ?  247 TYR A OH    1 
ATOM   1924  N  N     . ASN A 1 248 ? -7.117  -24.308 13.247  1.00 52.68 ?  248 ASN A N     1 
ATOM   1925  C  CA    . ASN A 1 248 ? -5.827  -24.885 13.570  1.00 51.31 ?  248 ASN A CA    1 
ATOM   1926  C  C     . ASN A 1 248 ? -5.935  -25.500 14.963  1.00 50.06 ?  248 ASN A C     1 
ATOM   1927  O  O     . ASN A 1 248 ? -5.392  -24.968 15.929  1.00 42.34 ?  248 ASN A O     1 
ATOM   1928  C  CB    . ASN A 1 248 ? -4.719  -23.846 13.452  1.00 49.95 ?  248 ASN A CB    1 
ATOM   1929  C  CG    . ASN A 1 248 ? -3.405  -24.468 13.048  1.00 45.46 ?  248 ASN A CG    1 
ATOM   1930  O  OD1   . ASN A 1 248 ? -2.982  -25.468 13.639  1.00 61.81 ?  248 ASN A OD1   1 
ATOM   1931  N  ND2   . ASN A 1 248 ? -2.759  -23.908 12.037  1.00 41.47 ?  248 ASN A ND2   1 
ATOM   1932  N  N     . TYR A 1 249 ? -6.669  -26.615 15.048  1.00 49.34 ?  249 TYR A N     1 
ATOM   1933  C  CA    . TYR A 1 249 ? -6.922  -27.281 16.315  1.00 49.98 ?  249 TYR A CA    1 
ATOM   1934  C  C     . TYR A 1 249 ? -5.588  -27.596 16.985  1.00 46.37 ?  249 TYR A C     1 
ATOM   1935  O  O     . TYR A 1 249 ? -5.469  -27.554 18.207  1.00 41.72 ?  249 TYR A O     1 
ATOM   1936  C  CB    . TYR A 1 249 ? -7.754  -28.551 16.108  1.00 51.02 ?  249 TYR A CB    1 
ATOM   1937  C  CG    . TYR A 1 249 ? -9.231  -28.307 15.823  1.00 55.79 ?  249 TYR A CG    1 
ATOM   1938  C  CD1   . TYR A 1 249 ? -10.069 -27.796 16.806  1.00 57.25 ?  249 TYR A CD1   1 
ATOM   1939  C  CD2   . TYR A 1 249 ? -9.794  -28.617 14.590  1.00 57.56 ?  249 TYR A CD2   1 
ATOM   1940  C  CE1   . TYR A 1 249 ? -11.415 -27.577 16.565  1.00 57.79 ?  249 TYR A CE1   1 
ATOM   1941  C  CE2   . TYR A 1 249 ? -11.140 -28.405 14.338  1.00 57.32 ?  249 TYR A CE2   1 
ATOM   1942  C  CZ    . TYR A 1 249 ? -11.953 -27.884 15.328  1.00 56.95 ?  249 TYR A CZ    1 
ATOM   1943  O  OH    . TYR A 1 249 ? -13.279 -27.672 15.087  1.00 63.60 ?  249 TYR A OH    1 
ATOM   1944  N  N     . ALA A 1 250 ? -4.592  -27.905 16.151  1.00 48.23 ?  250 ALA A N     1 
ATOM   1945  C  CA    . ALA A 1 250 ? -3.274  -28.306 16.611  1.00 45.18 ?  250 ALA A CA    1 
ATOM   1946  C  C     . ALA A 1 250 ? -2.657  -27.212 17.480  1.00 40.81 ?  250 ALA A C     1 
ATOM   1947  O  O     . ALA A 1 250 ? -2.095  -27.497 18.535  1.00 40.15 ?  250 ALA A O     1 
ATOM   1948  C  CB    . ALA A 1 250 ? -2.404  -28.619 15.414  1.00 47.20 ?  250 ALA A CB    1 
ATOM   1949  N  N     . ILE A 1 251 ? -2.773  -25.961 17.023  1.00 36.84 ?  251 ILE A N     1 
ATOM   1950  C  CA    . ILE A 1 251 ? -2.095  -24.842 17.658  1.00 35.54 ?  251 ILE A CA    1 
ATOM   1951  C  C     . ILE A 1 251 ? -2.940  -24.338 18.826  1.00 31.24 ?  251 ILE A C     1 
ATOM   1952  O  O     . ILE A 1 251 ? -2.409  -23.980 19.875  1.00 30.53 ?  251 ILE A O     1 
ATOM   1953  C  CB    . ILE A 1 251 ? -1.805  -23.733 16.630  1.00 35.67 ?  251 ILE A CB    1 
ATOM   1954  C  CG1   . ILE A 1 251 ? -1.060  -24.275 15.404  1.00 35.10 ?  251 ILE A CG1   1 
ATOM   1955  C  CG2   . ILE A 1 251 ? -1.058  -22.567 17.278  1.00 34.30 ?  251 ILE A CG2   1 
ATOM   1956  C  CD1   . ILE A 1 251 ? 0.268   -24.940 15.723  1.00 34.87 ?  251 ILE A CD1   1 
ATOM   1957  N  N     . LEU A 1 252 ? -4.262  -24.313 18.629  1.00 27.77 ?  252 LEU A N     1 
ATOM   1958  C  CA    . LEU A 1 252 ? -5.187  -23.918 19.677  1.00 26.74 ?  252 LEU A CA    1 
ATOM   1959  C  C     . LEU A 1 252 ? -4.930  -24.763 20.925  1.00 27.71 ?  252 LEU A C     1 
ATOM   1960  O  O     . LEU A 1 252 ? -4.917  -24.241 22.038  1.00 25.93 ?  252 LEU A O     1 
ATOM   1961  C  CB    . LEU A 1 252 ? -6.620  -24.059 19.165  1.00 23.86 ?  252 LEU A CB    1 
ATOM   1962  C  CG    . LEU A 1 252 ? -7.062  -23.040 18.109  1.00 21.08 ?  252 LEU A CG    1 
ATOM   1963  C  CD1   . LEU A 1 252 ? -8.451  -23.408 17.620  1.00 19.99 ?  252 LEU A CD1   1 
ATOM   1964  C  CD2   . LEU A 1 252 ? -7.042  -21.604 18.619  1.00 19.38 ?  252 LEU A CD2   1 
ATOM   1965  N  N     . ALA A 1 253 ? -4.710  -26.067 20.720  1.00 30.00 ?  253 ALA A N     1 
ATOM   1966  C  CA    . ALA A 1 253 ? -4.417  -26.992 21.803  1.00 29.67 ?  253 ALA A CA    1 
ATOM   1967  C  C     . ALA A 1 253 ? -3.128  -26.585 22.515  1.00 30.90 ?  253 ALA A C     1 
ATOM   1968  O  O     . ALA A 1 253 ? -3.084  -26.544 23.742  1.00 31.29 ?  253 ALA A O     1 
ATOM   1969  C  CB    . ALA A 1 253 ? -4.329  -28.403 21.265  1.00 30.05 ?  253 ALA A CB    1 
ATOM   1970  N  N     . LYS A 1 254 ? -2.078  -26.290 21.740  1.00 33.79 ?  254 LYS A N     1 
ATOM   1971  C  CA    . LYS A 1 254 ? -0.799  -25.908 22.318  1.00 39.16 ?  254 LYS A CA    1 
ATOM   1972  C  C     . LYS A 1 254 ? -0.980  -24.606 23.097  1.00 43.12 ?  254 LYS A C     1 
ATOM   1973  O  O     . LYS A 1 254 ? -0.295  -24.377 24.092  1.00 42.36 ?  254 LYS A O     1 
ATOM   1974  C  CB    . LYS A 1 254 ? 0.294   -25.813 21.245  1.00 38.07 ?  254 LYS A CB    1 
ATOM   1975  C  CG    . LYS A 1 254 ? 0.527   -27.098 20.455  1.00 41.86 ?  254 LYS A CG    1 
ATOM   1976  C  CD    . LYS A 1 254 ? 1.699   -27.065 19.480  1.00 42.98 ?  254 LYS A CD    1 
ATOM   1977  C  CE    . LYS A 1 254 ? 3.035   -27.101 20.155  1.00 47.32 ?  254 LYS A CE    1 
ATOM   1978  N  NZ    . LYS A 1 254 ? 4.132   -26.947 19.195  1.00 46.95 1  254 LYS A NZ    1 
ATOM   1979  N  N     . LEU A 1 255 ? -1.914  -23.766 22.635  1.00 40.82 ?  255 LEU A N     1 
ATOM   1980  C  CA    . LEU A 1 255 ? -2.285  -22.546 23.335  1.00 36.91 ?  255 LEU A CA    1 
ATOM   1981  C  C     . LEU A 1 255 ? -3.228  -22.891 24.486  1.00 42.46 ?  255 LEU A C     1 
ATOM   1982  O  O     . LEU A 1 255 ? -3.479  -22.059 25.355  1.00 36.82 ?  255 LEU A O     1 
ATOM   1983  C  CB    . LEU A 1 255 ? -2.940  -21.553 22.374  1.00 36.71 ?  255 LEU A CB    1 
ATOM   1984  C  CG    . LEU A 1 255 ? -2.054  -20.961 21.273  1.00 31.51 ?  255 LEU A CG    1 
ATOM   1985  C  CD1   . LEU A 1 255 ? -2.948  -20.283 20.252  1.00 32.06 ?  255 LEU A CD1   1 
ATOM   1986  C  CD2   . LEU A 1 255 ? -1.018  -19.981 21.800  1.00 29.61 ?  255 LEU A CD2   1 
ATOM   1987  N  N     . GLY A 1 256 ? -3.761  -24.118 24.465  1.00 46.59 ?  256 GLY A N     1 
ATOM   1988  C  CA    . GLY A 1 256 ? -4.604  -24.623 25.538  1.00 44.07 ?  256 GLY A CA    1 
ATOM   1989  C  C     . GLY A 1 256 ? -6.008  -24.026 25.486  1.00 43.21 ?  256 GLY A C     1 
ATOM   1990  O  O     . GLY A 1 256 ? -6.668  -23.892 26.514  1.00 49.18 ?  256 GLY A O     1 
ATOM   1991  N  N     . ILE A 1 257 ? -6.456  -23.678 24.276  1.00 39.42 ?  257 ILE A N     1 
ATOM   1992  C  CA    . ILE A 1 257 ? -7.729  -23.004 24.091  1.00 41.68 ?  257 ILE A CA    1 
ATOM   1993  C  C     . ILE A 1 257 ? -8.482  -23.662 22.939  1.00 36.80 ?  257 ILE A C     1 
ATOM   1994  O  O     . ILE A 1 257 ? -8.008  -24.628 22.347  1.00 41.75 ?  257 ILE A O     1 
ATOM   1995  C  CB    . ILE A 1 257 ? -7.519  -21.500 23.834  1.00 40.05 ?  257 ILE A CB    1 
ATOM   1996  C  CG1   . ILE A 1 257 ? -6.869  -21.248 22.469  1.00 41.07 ?  257 ILE A CG1   1 
ATOM   1997  C  CG2   . ILE A 1 257 ? -6.725  -20.859 24.972  1.00 43.92 ?  257 ILE A CG2   1 
ATOM   1998  C  CD1   . ILE A 1 257 ? -6.670  -19.781 22.132  1.00 42.59 ?  257 ILE A CD1   1 
ATOM   1999  N  N     . GLY A 1 258 ? -9.661  -23.112 22.635  1.00 41.72 ?  258 GLY A N     1 
ATOM   2000  C  CA    . GLY A 1 258 ? -10.467 -23.569 21.518  1.00 38.69 ?  258 GLY A CA    1 
ATOM   2001  C  C     . GLY A 1 258 ? -11.260 -22.416 20.910  1.00 41.54 ?  258 GLY A C     1 
ATOM   2002  O  O     . GLY A 1 258 ? -11.123 -21.269 21.333  1.00 39.66 ?  258 GLY A O     1 
ATOM   2003  N  N     . PRO A 1 259 ? -12.114 -22.690 19.900  1.00 40.11 ?  259 PRO A N     1 
ATOM   2004  C  CA    . PRO A 1 259 ? -12.928 -21.650 19.270  1.00 41.24 ?  259 PRO A CA    1 
ATOM   2005  C  C     . PRO A 1 259 ? -13.726 -20.827 20.279  1.00 49.21 ?  259 PRO A C     1 
ATOM   2006  O  O     . PRO A 1 259 ? -13.769 -19.602 20.196  1.00 52.44 ?  259 PRO A O     1 
ATOM   2007  C  CB    . PRO A 1 259 ? -13.844 -22.457 18.330  1.00 40.43 ?  259 PRO A CB    1 
ATOM   2008  C  CG    . PRO A 1 259 ? -13.051 -23.708 18.018  1.00 39.50 ?  259 PRO A CG    1 
ATOM   2009  C  CD    . PRO A 1 259 ? -12.327 -24.023 19.313  1.00 40.28 ?  259 PRO A CD    1 
ATOM   2010  N  N     . GLU A 1 260 ? -14.351 -21.526 21.232  1.00 51.20 ?  260 GLU A N     1 
ATOM   2011  C  CA    . GLU A 1 260 ? -15.294 -20.916 22.155  1.00 47.71 ?  260 GLU A CA    1 
ATOM   2012  C  C     . GLU A 1 260 ? -14.593 -19.862 23.009  1.00 51.42 ?  260 GLU A C     1 
ATOM   2013  O  O     . GLU A 1 260 ? -15.228 -18.913 23.464  1.00 53.37 ?  260 GLU A O     1 
ATOM   2014  C  CB    . GLU A 1 260 ? -15.964 -21.973 23.035  1.00 44.57 ?  260 GLU A CB    1 
ATOM   2015  C  CG    . GLU A 1 260 ? -15.015 -22.699 23.985  1.00 44.49 ?  260 GLU A CG    1 
ATOM   2016  C  CD    . GLU A 1 260 ? -14.152 -23.779 23.355  1.00 36.51 ?  260 GLU A CD    1 
ATOM   2017  O  OE1   . GLU A 1 260 ? -14.037 -23.814 22.111  1.00 26.24 ?  260 GLU A OE1   1 
ATOM   2018  O  OE2   . GLU A 1 260 ? -13.607 -24.602 24.121  1.00 33.11 -1 260 GLU A OE2   1 
ATOM   2019  N  N     . ASP A 1 261 ? -13.284 -20.034 23.224  1.00 50.38 ?  261 ASP A N     1 
ATOM   2020  C  CA    . ASP A 1 261 ? -12.528 -19.120 24.066  1.00 44.83 ?  261 ASP A CA    1 
ATOM   2021  C  C     . ASP A 1 261 ? -12.076 -17.914 23.245  1.00 42.04 ?  261 ASP A C     1 
ATOM   2022  O  O     . ASP A 1 261 ? -11.787 -16.858 23.805  1.00 47.20 ?  261 ASP A O     1 
ATOM   2023  C  CB    . ASP A 1 261 ? -11.381 -19.825 24.774  1.00 44.61 ?  261 ASP A CB    1 
ATOM   2024  C  CG    . ASP A 1 261 ? -11.793 -20.909 25.761  1.00 41.73 ?  261 ASP A CG    1 
ATOM   2025  O  OD1   . ASP A 1 261 ? -12.711 -20.650 26.567  1.00 42.15 ?  261 ASP A OD1   1 
ATOM   2026  O  OD2   . ASP A 1 261 ? -11.182 -21.998 25.725  1.00 39.59 -1 261 ASP A OD2   1 
ATOM   2027  N  N     . LEU A 1 262 ? -12.022 -18.072 21.917  1.00 41.91 ?  262 LEU A N     1 
ATOM   2028  C  CA    . LEU A 1 262 ? -11.633 -16.980 21.039  1.00 45.58 ?  262 LEU A CA    1 
ATOM   2029  C  C     . LEU A 1 262 ? -12.523 -15.774 21.329  1.00 52.93 ?  262 LEU A C     1 
ATOM   2030  O  O     . LEU A 1 262 ? -13.740 -15.842 21.173  1.00 56.14 ?  262 LEU A O     1 
ATOM   2031  C  CB    . LEU A 1 262 ? -11.715 -17.402 19.571  1.00 44.13 ?  262 LEU A CB    1 
ATOM   2032  C  CG    . LEU A 1 262 ? -10.833 -18.588 19.164  1.00 38.45 ?  262 LEU A CG    1 
ATOM   2033  C  CD1   . LEU A 1 262 ? -11.059 -19.000 17.719  1.00 33.84 ?  262 LEU A CD1   1 
ATOM   2034  C  CD2   . LEU A 1 262 ? -9.367  -18.264 19.393  1.00 41.41 ?  262 LEU A CD2   1 
ATOM   2035  N  N     . GLY A 1 263 ? -11.893 -14.675 21.760  1.00 55.10 ?  263 GLY A N     1 
ATOM   2036  C  CA    . GLY A 1 263 ? -12.605 -13.458 22.115  1.00 57.11 ?  263 GLY A CA    1 
ATOM   2037  C  C     . GLY A 1 263 ? -13.246 -12.816 20.900  1.00 57.10 ?  263 GLY A C     1 
ATOM   2038  O  O     . GLY A 1 263 ? -12.487 -12.480 19.966  1.00 55.79 ?  263 GLY A O     1 
ATOM   2039  O  OXT   . GLY A 1 263 ? -14.486 -12.666 20.924  1.00 64.31 -1 263 GLY A OXT   1 
ATOM   2040  N  N     . GLY B 2 10  ? -7.867  24.371  -19.944 1.00 38.03 ?  3   GLY B N     1 
ATOM   2041  C  CA    . GLY B 2 10  ? -9.208  24.503  -19.341 1.00 34.49 ?  3   GLY B CA    1 
ATOM   2042  C  C     . GLY B 2 10  ? -9.622  23.226  -18.613 1.00 29.63 ?  3   GLY B C     1 
ATOM   2043  O  O     . GLY B 2 10  ? -9.890  23.247  -17.414 1.00 28.71 ?  3   GLY B O     1 
ATOM   2044  N  N     . LEU B 2 11  ? -9.666  22.118  -19.361 1.00 29.89 ?  4   LEU B N     1 
ATOM   2045  C  CA    . LEU B 2 11  ? -10.101 20.834  -18.835 1.00 27.78 ?  4   LEU B CA    1 
ATOM   2046  C  C     . LEU B 2 11  ? -9.071  20.313  -17.835 1.00 26.82 ?  4   LEU B C     1 
ATOM   2047  O  O     . LEU B 2 11  ? -9.429  19.810  -16.772 1.00 27.41 ?  4   LEU B O     1 
ATOM   2048  C  CB    . LEU B 2 11  ? -10.295 19.867  -20.003 1.00 29.24 ?  4   LEU B CB    1 
ATOM   2049  C  CG    . LEU B 2 11  ? -10.947 18.521  -19.670 1.00 28.49 ?  4   LEU B CG    1 
ATOM   2050  C  CD1   . LEU B 2 11  ? -12.418 18.702  -19.340 1.00 28.32 ?  4   LEU B CD1   1 
ATOM   2051  C  CD2   . LEU B 2 11  ? -10.773 17.527  -20.806 1.00 29.15 ?  4   LEU B CD2   1 
ATOM   2052  N  N     . SER B 2 12  ? -7.790  20.448  -18.193 1.00 27.43 ?  5   SER B N     1 
ATOM   2053  C  CA    . SER B 2 12  ? -6.689  19.932  -17.394 1.00 29.43 ?  5   SER B CA    1 
ATOM   2054  C  C     . SER B 2 12  ? -6.607  20.672  -16.061 1.00 30.01 ?  5   SER B C     1 
ATOM   2055  O  O     . SER B 2 12  ? -6.462  20.054  -15.009 1.00 31.05 ?  5   SER B O     1 
ATOM   2056  C  CB    . SER B 2 12  ? -5.389  20.034  -18.152 1.00 32.99 ?  5   SER B CB    1 
ATOM   2057  O  OG    . SER B 2 12  ? -4.301  19.553  -17.375 1.00 37.47 ?  5   SER B OG    1 
ATOM   2058  N  N     . ASP B 2 13  ? -6.691  22.003  -16.131 1.00 26.63 ?  6   ASP B N     1 
ATOM   2059  C  CA    . ASP B 2 13  ? -6.632  22.854  -14.955 1.00 25.50 ?  6   ASP B CA    1 
ATOM   2060  C  C     . ASP B 2 13  ? -7.700  22.418  -13.956 1.00 24.27 ?  6   ASP B C     1 
ATOM   2061  O  O     . ASP B 2 13  ? -7.415  22.256  -12.772 1.00 27.80 ?  6   ASP B O     1 
ATOM   2062  C  CB    . ASP B 2 13  ? -6.760  24.318  -15.348 1.00 31.44 ?  6   ASP B CB    1 
ATOM   2063  C  CG    . ASP B 2 13  ? -5.576  24.889  -16.115 1.00 34.71 ?  6   ASP B CG    1 
ATOM   2064  O  OD1   . ASP B 2 13  ? -4.505  24.246  -16.106 1.00 36.35 ?  6   ASP B OD1   1 
ATOM   2065  O  OD2   . ASP B 2 13  ? -5.739  25.965  -16.729 1.00 37.53 -1 6   ASP B OD2   1 
ATOM   2066  N  N     . PHE B 2 14  ? -8.929  22.227  -14.448 1.00 22.58 ?  7   PHE B N     1 
ATOM   2067  C  CA    . PHE B 2 14  ? -10.042 21.849  -13.593 1.00 20.40 ?  7   PHE B CA    1 
ATOM   2068  C  C     . PHE B 2 14  ? -9.710  20.531  -12.894 1.00 18.54 ?  7   PHE B C     1 
ATOM   2069  O  O     . PHE B 2 14  ? -9.747  20.459  -11.669 1.00 17.44 ?  7   PHE B O     1 
ATOM   2070  C  CB    . PHE B 2 14  ? -11.343 21.803  -14.403 1.00 19.81 ?  7   PHE B CB    1 
ATOM   2071  C  CG    . PHE B 2 14  ? -12.530 21.204  -13.660 1.00 20.44 ?  7   PHE B CG    1 
ATOM   2072  C  CD1   . PHE B 2 14  ? -13.151 21.896  -12.626 1.00 22.26 ?  7   PHE B CD1   1 
ATOM   2073  C  CD2   . PHE B 2 14  ? -13.032 19.955  -14.008 1.00 21.48 ?  7   PHE B CD2   1 
ATOM   2074  C  CE1   . PHE B 2 14  ? -14.232 21.347  -11.953 1.00 22.67 ?  7   PHE B CE1   1 
ATOM   2075  C  CE2   . PHE B 2 14  ? -14.116 19.413  -13.335 1.00 22.61 ?  7   PHE B CE2   1 
ATOM   2076  C  CZ    . PHE B 2 14  ? -14.711 20.109  -12.308 1.00 22.56 ?  7   PHE B CZ    1 
ATOM   2077  N  N     . PHE B 2 15  ? -9.372  19.497  -13.674 1.00 19.73 ?  8   PHE B N     1 
ATOM   2078  C  CA    . PHE B 2 15  ? -9.137  18.173  -13.117 1.00 21.76 ?  8   PHE B CA    1 
ATOM   2079  C  C     . PHE B 2 15  ? -8.058  18.258  -12.036 1.00 19.44 ?  8   PHE B C     1 
ATOM   2080  O  O     . PHE B 2 15  ? -8.229  17.706  -10.952 1.00 19.09 ?  8   PHE B O     1 
ATOM   2081  C  CB    . PHE B 2 15  ? -8.790  17.151  -14.207 1.00 24.28 ?  8   PHE B CB    1 
ATOM   2082  C  CG    . PHE B 2 15  ? -9.932  16.750  -15.135 1.00 28.95 ?  8   PHE B CG    1 
ATOM   2083  C  CD1   . PHE B 2 15  ? -11.262 16.977  -14.791 1.00 31.65 ?  8   PHE B CD1   1 
ATOM   2084  C  CD2   . PHE B 2 15  ? -9.669  16.117  -16.346 1.00 33.10 ?  8   PHE B CD2   1 
ATOM   2085  C  CE1   . PHE B 2 15  ? -12.290 16.600  -15.644 1.00 32.84 ?  8   PHE B CE1   1 
ATOM   2086  C  CE2   . PHE B 2 15  ? -10.700 15.741  -17.192 1.00 32.66 ?  8   PHE B CE2   1 
ATOM   2087  C  CZ    . PHE B 2 15  ? -12.007 15.982  -16.840 1.00 34.44 ?  8   PHE B CZ    1 
ATOM   2088  N  N     . THR B 2 16  ? -6.951  18.953  -12.329 1.00 21.19 ?  9   THR B N     1 
ATOM   2089  C  CA    . THR B 2 16  ? -5.867  19.113  -11.369 1.00 23.75 ?  9   THR B CA    1 
ATOM   2090  C  C     . THR B 2 16  ? -6.425  19.627  -10.044 1.00 22.65 ?  9   THR B C     1 
ATOM   2091  O  O     . THR B 2 16  ? -6.132  19.072  -8.987  1.00 20.03 ?  9   THR B O     1 
ATOM   2092  C  CB    . THR B 2 16  ? -4.801  20.054  -11.932 1.00 24.31 ?  9   THR B CB    1 
ATOM   2093  O  OG1   . THR B 2 16  ? -3.996  19.235  -12.775 1.00 24.90 ?  9   THR B OG1   1 
ATOM   2094  C  CG2   . THR B 2 16  ? -3.927  20.677  -10.857 1.00 23.24 ?  9   THR B CG2   1 
ATOM   2095  N  N     . GLN B 2 17  ? -7.229  20.693  -10.116 1.00 24.35 ?  10  GLN B N     1 
ATOM   2096  C  CA    . GLN B 2 17  ? -7.760  21.341  -8.928  1.00 22.38 ?  10  GLN B CA    1 
ATOM   2097  C  C     . GLN B 2 17  ? -8.688  20.372  -8.201  1.00 18.61 ?  10  GLN B C     1 
ATOM   2098  O  O     . GLN B 2 17  ? -8.585  20.190  -6.989  1.00 16.78 ?  10  GLN B O     1 
ATOM   2099  C  CB    . GLN B 2 17  ? -8.486  22.632  -9.311  1.00 26.01 ?  10  GLN B CB    1 
ATOM   2100  C  CG    . GLN B 2 17  ? -8.949  23.461  -8.118  1.00 32.20 ?  10  GLN B CG    1 
ATOM   2101  C  CD    . GLN B 2 17  ? -9.474  24.828  -8.502  1.00 36.43 ?  10  GLN B CD    1 
ATOM   2102  O  OE1   . GLN B 2 17  ? -9.505  25.203  -9.679  1.00 40.25 ?  10  GLN B OE1   1 
ATOM   2103  N  NE2   . GLN B 2 17  ? -9.892  25.591  -7.502  1.00 40.05 ?  10  GLN B NE2   1 
ATOM   2104  N  N     . LEU B 2 18  ? -9.584  19.747  -8.970  1.00 15.24 ?  11  LEU B N     1 
ATOM   2105  C  CA    . LEU B 2 18  ? -10.609 18.877  -8.420  1.00 16.49 ?  11  LEU B CA    1 
ATOM   2106  C  C     . LEU B 2 18  ? -9.971  17.717  -7.655  1.00 15.11 ?  11  LEU B C     1 
ATOM   2107  O  O     . LEU B 2 18  ? -10.536 17.240  -6.674  1.00 13.56 ?  11  LEU B O     1 
ATOM   2108  C  CB    . LEU B 2 18  ? -11.497 18.402  -9.570  1.00 16.64 ?  11  LEU B CB    1 
ATOM   2109  C  CG    . LEU B 2 18  ? -12.650 17.468  -9.194  1.00 16.75 ?  11  LEU B CG    1 
ATOM   2110  C  CD1   . LEU B 2 18  ? -13.509 18.070  -8.096  1.00 17.83 ?  11  LEU B CD1   1 
ATOM   2111  C  CD2   . LEU B 2 18  ? -13.491 17.152  -10.418 1.00 17.20 ?  11  LEU B CD2   1 
ATOM   2112  N  N     . GLY B 2 19  ? -8.790  17.271  -8.099  1.00 16.30 ?  12  GLY B N     1 
ATOM   2113  C  CA    . GLY B 2 19  ? -8.110  16.150  -7.466  1.00 17.30 ?  12  GLY B CA    1 
ATOM   2114  C  C     . GLY B 2 19  ? -7.508  16.540  -6.117  1.00 17.78 ?  12  GLY B C     1 
ATOM   2115  O  O     . GLY B 2 19  ? -7.432  15.722  -5.200  1.00 19.96 ?  12  GLY B O     1 
ATOM   2116  N  N     . GLN B 2 20  ? -7.088  17.804  -6.013  1.00 19.69 ?  13  GLN B N     1 
ATOM   2117  C  CA    . GLN B 2 20  ? -6.350  18.299  -4.863  1.00 22.26 ?  13  GLN B CA    1 
ATOM   2118  C  C     . GLN B 2 20  ? -7.274  18.917  -3.817  1.00 21.34 ?  13  GLN B C     1 
ATOM   2119  O  O     . GLN B 2 20  ? -6.976  18.865  -2.627  1.00 20.23 ?  13  GLN B O     1 
ATOM   2120  C  CB    . GLN B 2 20  ? -5.390  19.406  -5.292  1.00 24.86 ?  13  GLN B CB    1 
ATOM   2121  C  CG    . GLN B 2 20  ? -4.276  18.932  -6.215  1.00 28.54 ?  13  GLN B CG    1 
ATOM   2122  C  CD    . GLN B 2 20  ? -3.286  20.026  -6.542  1.00 30.60 ?  13  GLN B CD    1 
ATOM   2123  O  OE1   . GLN B 2 20  ? -2.620  20.579  -5.660  1.00 30.43 ?  13  GLN B OE1   1 
ATOM   2124  N  NE2   . GLN B 2 20  ? -3.184  20.352  -7.822  1.00 34.07 ?  13  GLN B NE2   1 
ATOM   2125  N  N     . ASP B 2 21  ? -8.373  19.523  -4.278  1.00 19.01 ?  14  ASP B N     1 
ATOM   2126  C  CA    . ASP B 2 21  ? -9.188  20.389  -3.441  1.00 19.62 ?  14  ASP B CA    1 
ATOM   2127  C  C     . ASP B 2 21  ? -10.452 19.641  -3.018  1.00 15.78 ?  14  ASP B C     1 
ATOM   2128  O  O     . ASP B 2 21  ? -11.333 19.385  -3.836  1.00 18.31 ?  14  ASP B O     1 
ATOM   2129  C  CB    . ASP B 2 21  ? -9.451  21.706  -4.157  1.00 20.28 ?  14  ASP B CB    1 
ATOM   2130  C  CG    . ASP B 2 21  ? -10.163 22.783  -3.351  1.00 22.41 ?  14  ASP B CG    1 
ATOM   2131  O  OD1   . ASP B 2 21  ? -10.637 22.470  -2.240  1.00 22.56 ?  14  ASP B OD1   1 
ATOM   2132  O  OD2   . ASP B 2 21  ? -10.228 23.930  -3.841  1.00 26.89 -1 14  ASP B OD2   1 
ATOM   2133  N  N     . ALA B 2 22  ? -10.523 19.305  -1.726  1.00 13.14 ?  15  ALA B N     1 
ATOM   2134  C  CA    . ALA B 2 22  ? -11.595 18.491  -1.173  1.00 12.55 ?  15  ALA B CA    1 
ATOM   2135  C  C     . ALA B 2 22  ? -12.914 19.258  -1.193  1.00 15.33 ?  15  ALA B C     1 
ATOM   2136  O  O     . ALA B 2 22  ? -13.977 18.673  -1.389  1.00 16.49 ?  15  ALA B O     1 
ATOM   2137  C  CB    . ALA B 2 22  ? -11.229 18.067  0.231   1.00 11.70 ?  15  ALA B CB    1 
ATOM   2138  N  N     . GLN B 2 23  ? -12.831 20.570  -0.961  1.00 16.44 ?  16  GLN B N     1 
ATOM   2139  C  CA    . GLN B 2 23  ? -13.990 21.438  -1.060  1.00 20.54 ?  16  GLN B CA    1 
ATOM   2140  C  C     . GLN B 2 23  ? -14.645 21.225  -2.421  1.00 20.01 ?  16  GLN B C     1 
ATOM   2141  O  O     . GLN B 2 23  ? -15.804 20.824  -2.510  1.00 20.08 ?  16  GLN B O     1 
ATOM   2142  C  CB    . GLN B 2 23  ? -13.568 22.894  -0.867  1.00 22.33 ?  16  GLN B CB    1 
ATOM   2143  C  CG    . GLN B 2 23  ? -14.656 23.735  -0.215  1.00 29.38 ?  16  GLN B CG    1 
ATOM   2144  C  CD    . GLN B 2 23  ? -15.386 22.957  0.856   1.00 31.71 ?  16  GLN B CD    1 
ATOM   2145  O  OE1   . GLN B 2 23  ? -14.799 22.542  1.862   1.00 31.91 ?  16  GLN B OE1   1 
ATOM   2146  N  NE2   . GLN B 2 23  ? -16.670 22.720  0.633   1.00 35.41 ?  16  GLN B NE2   1 
ATOM   2147  N  N     . LEU B 2 24  ? -13.864 21.475  -3.474  1.00 22.62 ?  17  LEU B N     1 
ATOM   2148  C  CA    . LEU B 2 24  ? -14.341 21.402  -4.843  1.00 24.66 ?  17  LEU B CA    1 
ATOM   2149  C  C     . LEU B 2 24  ? -14.817 19.988  -5.163  1.00 25.47 ?  17  LEU B C     1 
ATOM   2150  O  O     . LEU B 2 24  ? -15.768 19.814  -5.921  1.00 30.58 ?  17  LEU B O     1 
ATOM   2151  C  CB    . LEU B 2 24  ? -13.227 21.844  -5.790  1.00 25.61 ?  17  LEU B CB    1 
ATOM   2152  C  CG    . LEU B 2 24  ? -13.573 21.807  -7.282  1.00 28.42 ?  17  LEU B CG    1 
ATOM   2153  C  CD1   . LEU B 2 24  ? -14.869 22.550  -7.559  1.00 31.62 ?  17  LEU B CD1   1 
ATOM   2154  C  CD2   . LEU B 2 24  ? -12.439 22.380  -8.111  1.00 29.28 ?  17  LEU B CD2   1 
ATOM   2155  N  N     . MET B 2 25  ? -14.144 18.983  -4.590  1.00 23.82 ?  18  MET B N     1 
ATOM   2156  C  CA    . MET B 2 25  ? -14.518 17.596  -4.820  1.00 24.22 ?  18  MET B CA    1 
ATOM   2157  C  C     . MET B 2 25  ? -15.914 17.341  -4.259  1.00 25.06 ?  18  MET B C     1 
ATOM   2158  O  O     . MET B 2 25  ? -16.730 16.682  -4.898  1.00 20.40 ?  18  MET B O     1 
ATOM   2159  C  CB    . MET B 2 25  ? -13.542 16.617  -4.159  1.00 22.83 ?  18  MET B CB    1 
ATOM   2160  C  CG    . MET B 2 25  ? -13.966 15.170  -4.315  1.00 24.30 ?  18  MET B CG    1 
ATOM   2161  S  SD    . MET B 2 25  ? -14.055 14.663  -6.045  1.00 27.44 ?  18  MET B SD    1 
ATOM   2162  C  CE    . MET B 2 25  ? -12.304 14.369  -6.329  1.00 26.51 ?  18  MET B CE    1 
ATOM   2163  N  N     . GLU B 2 26  ? -16.166 17.855  -3.051  1.00 30.07 ?  19  GLU B N     1 
ATOM   2164  C  CA    . GLU B 2 26  ? -17.453 17.682  -2.397  1.00 34.48 ?  19  GLU B CA    1 
ATOM   2165  C  C     . GLU B 2 26  ? -18.506 18.527  -3.110  1.00 30.04 ?  19  GLU B C     1 
ATOM   2166  O  O     . GLU B 2 26  ? -19.685 18.181  -3.106  1.00 29.37 ?  19  GLU B O     1 
ATOM   2167  C  CB    . GLU B 2 26  ? -17.348 18.018  -0.909  1.00 37.91 ?  19  GLU B CB    1 
ATOM   2168  C  CG    . GLU B 2 26  ? -16.614 16.948  -0.107  1.00 42.19 ?  19  GLU B CG    1 
ATOM   2169  C  CD    . GLU B 2 26  ? -17.258 15.578  -0.206  1.00 54.09 ?  19  GLU B CD    1 
ATOM   2170  O  OE1   . GLU B 2 26  ? -18.448 15.461  0.154   1.00 63.68 ?  19  GLU B OE1   1 
ATOM   2171  O  OE2   . GLU B 2 26  ? -16.573 14.629  -0.645  1.00 63.07 -1 19  GLU B OE2   1 
ATOM   2172  N  N     . ASP B 2 27  ? -18.071 19.632  -3.722  1.00 30.99 ?  20  ASP B N     1 
ATOM   2173  C  CA    . ASP B 2 27  ? -18.959 20.459  -4.522  1.00 33.63 ?  20  ASP B CA    1 
ATOM   2174  C  C     . ASP B 2 27  ? -19.316 19.713  -5.805  1.00 32.24 ?  20  ASP B C     1 
ATOM   2175  O  O     . ASP B 2 27  ? -20.420 19.855  -6.325  1.00 30.40 ?  20  ASP B O     1 
ATOM   2176  C  CB    . ASP B 2 27  ? -18.334 21.807  -4.844  1.00 32.09 ?  20  ASP B CB    1 
ATOM   2177  C  CG    . ASP B 2 27  ? -18.100 22.728  -3.655  1.00 32.95 ?  20  ASP B CG    1 
ATOM   2178  O  OD1   . ASP B 2 27  ? -18.760 22.522  -2.615  1.00 31.67 ?  20  ASP B OD1   1 
ATOM   2179  O  OD2   . ASP B 2 27  ? -17.245 23.631  -3.774  1.00 33.80 -1 20  ASP B OD2   1 
ATOM   2180  N  N     . TYR B 2 28  ? -18.361 18.922  -6.307  1.00 31.90 ?  21  TYR B N     1 
ATOM   2181  C  CA    . TYR B 2 28  ? -18.525 18.228  -7.574  1.00 30.54 ?  21  TYR B CA    1 
ATOM   2182  C  C     . TYR B 2 28  ? -19.448 17.028  -7.376  1.00 31.66 ?  21  TYR B C     1 
ATOM   2183  O  O     . TYR B 2 28  ? -20.272 16.727  -8.237  1.00 39.30 ?  21  TYR B O     1 
ATOM   2184  C  CB    . TYR B 2 28  ? -17.164 17.821  -8.147  1.00 27.64 ?  21  TYR B CB    1 
ATOM   2185  C  CG    . TYR B 2 28  ? -17.257 16.888  -9.348  1.00 25.60 ?  21  TYR B CG    1 
ATOM   2186  C  CD1   . TYR B 2 28  ? -17.333 17.382  -10.645 1.00 24.86 ?  21  TYR B CD1   1 
ATOM   2187  C  CD2   . TYR B 2 28  ? -17.284 15.510  -9.177  1.00 24.47 ?  21  TYR B CD2   1 
ATOM   2188  C  CE1   . TYR B 2 28  ? -17.427 16.532  -11.735 1.00 24.78 ?  21  TYR B CE1   1 
ATOM   2189  C  CE2   . TYR B 2 28  ? -17.378 14.650  -10.258 1.00 25.78 ?  21  TYR B CE2   1 
ATOM   2190  C  CZ    . TYR B 2 28  ? -17.449 15.163  -11.541 1.00 25.35 ?  21  TYR B CZ    1 
ATOM   2191  O  OH    . TYR B 2 28  ? -17.539 14.319  -12.609 1.00 31.71 ?  21  TYR B OH    1 
ATOM   2192  N  N     . LYS B 2 29  ? -19.298 16.354  -6.232  1.00 32.83 ?  22  LYS B N     1 
ATOM   2193  C  CA    . LYS B 2 29  ? -20.100 15.187  -5.899  1.00 33.32 ?  22  LYS B CA    1 
ATOM   2194  C  C     . LYS B 2 29  ? -21.579 15.562  -5.820  1.00 28.95 ?  22  LYS B C     1 
ATOM   2195  O  O     . LYS B 2 29  ? -22.439 14.781  -6.221  1.00 26.44 ?  22  LYS B O     1 
ATOM   2196  C  CB    . LYS B 2 29  ? -19.636 14.598  -4.562  1.00 35.96 ?  22  LYS B CB    1 
ATOM   2197  C  CG    . LYS B 2 29  ? -18.367 13.754  -4.606  1.00 39.22 ?  22  LYS B CG    1 
ATOM   2198  C  CD    . LYS B 2 29  ? -18.591 12.307  -5.031  1.00 42.48 ?  22  LYS B CD    1 
ATOM   2199  C  CE    . LYS B 2 29  ? -17.404 11.442  -4.735  1.00 48.28 ?  22  LYS B CE    1 
ATOM   2200  N  NZ    . LYS B 2 29  ? -17.717 10.013  -4.826  1.00 46.83 1  22  LYS B NZ    1 
ATOM   2201  N  N     . GLN B 2 30  ? -21.864 16.756  -5.289  1.00 28.52 ?  23  GLN B N     1 
ATOM   2202  C  CA    . GLN B 2 30  ? -23.234 17.180  -5.048  1.00 28.79 ?  23  GLN B CA    1 
ATOM   2203  C  C     . GLN B 2 30  ? -23.922 17.508  -6.373  1.00 24.18 ?  23  GLN B C     1 
ATOM   2204  O  O     . GLN B 2 30  ? -25.104 17.219  -6.541  1.00 20.10 ?  23  GLN B O     1 
ATOM   2205  C  CB    . GLN B 2 30  ? -23.305 18.380  -4.099  1.00 29.45 ?  23  GLN B CB    1 
ATOM   2206  C  CG    . GLN B 2 30  ? -22.974 18.066  -2.641  1.00 31.23 ?  23  GLN B CG    1 
ATOM   2207  C  CD    . GLN B 2 30  ? -24.007 17.198  -1.954  1.00 36.05 ?  23  GLN B CD    1 
ATOM   2208  O  OE1   . GLN B 2 30  ? -24.366 16.118  -2.436  1.00 46.89 ?  23  GLN B OE1   1 
ATOM   2209  N  NE2   . GLN B 2 30  ? -24.494 17.661  -0.811  1.00 31.09 ?  23  GLN B NE2   1 
ATOM   2210  N  N     . ASN B 2 31  ? -23.182 18.112  -7.311  1.00 24.17 ?  24  ASN B N     1 
ATOM   2211  C  CA    . ASN B 2 31  ? -23.776 18.604  -8.545  1.00 24.86 ?  24  ASN B CA    1 
ATOM   2212  C  C     . ASN B 2 31  ? -22.720 18.642  -9.650  1.00 24.14 ?  24  ASN B C     1 
ATOM   2213  O  O     . ASN B 2 31  ? -22.199 19.705  -9.980  1.00 26.64 ?  24  ASN B O     1 
ATOM   2214  C  CB    . ASN B 2 31  ? -24.412 19.974  -8.333  1.00 28.08 ?  24  ASN B CB    1 
ATOM   2215  C  CG    . ASN B 2 31  ? -25.446 20.297  -9.385  1.00 29.98 ?  24  ASN B CG    1 
ATOM   2216  O  OD1   . ASN B 2 31  ? -25.227 20.034  -10.573 1.00 27.32 ?  24  ASN B OD1   1 
ATOM   2217  N  ND2   . ASN B 2 31  ? -26.579 20.846  -8.972  1.00 26.99 ?  24  ASN B ND2   1 
ATOM   2218  N  N     . PRO B 2 32  ? -22.378 17.481  -10.255 1.00 19.57 ?  25  PRO B N     1 
ATOM   2219  C  CA    . PRO B 2 32  ? -21.295 17.402  -11.243 1.00 20.05 ?  25  PRO B CA    1 
ATOM   2220  C  C     . PRO B 2 32  ? -21.446 18.263  -12.496 1.00 18.44 ?  25  PRO B C     1 
ATOM   2221  O  O     . PRO B 2 32  ? -20.482 18.890  -12.932 1.00 19.16 ?  25  PRO B O     1 
ATOM   2222  C  CB    . PRO B 2 32  ? -21.268 15.898  -11.585 1.00 18.50 ?  25  PRO B CB    1 
ATOM   2223  C  CG    . PRO B 2 32  ? -21.854 15.230  -10.363 1.00 18.60 ?  25  PRO B CG    1 
ATOM   2224  C  CD    . PRO B 2 32  ? -22.971 16.168  -9.955  1.00 20.40 ?  25  PRO B CD    1 
ATOM   2225  N  N     . GLU B 2 33  ? -22.648 18.271  -13.084 1.00 17.63 ?  26  GLU B N     1 
ATOM   2226  C  CA    . GLU B 2 33  ? -22.924 19.097  -14.249 1.00 20.56 ?  26  GLU B CA    1 
ATOM   2227  C  C     . GLU B 2 33  ? -22.745 20.574  -13.903 1.00 20.19 ?  26  GLU B C     1 
ATOM   2228  O  O     . GLU B 2 33  ? -22.078 21.302  -14.635 1.00 22.78 ?  26  GLU B O     1 
ATOM   2229  C  CB    . GLU B 2 33  ? -24.333 18.885  -14.804 1.00 26.30 ?  26  GLU B CB    1 
ATOM   2230  C  CG    . GLU B 2 33  ? -24.441 17.723  -15.787 1.00 30.32 ?  26  GLU B CG    1 
ATOM   2231  C  CD    . GLU B 2 33  ? -25.709 17.754  -16.622 1.00 36.33 ?  26  GLU B CD    1 
ATOM   2232  O  OE1   . GLU B 2 33  ? -26.516 18.689  -16.431 1.00 37.81 ?  26  GLU B OE1   1 
ATOM   2233  O  OE2   . GLU B 2 33  ? -25.889 16.850  -17.465 1.00 44.38 -1 26  GLU B OE2   1 
ATOM   2234  N  N     . ALA B 2 34  ? -23.357 21.019  -12.800 1.00 19.25 ?  27  ALA B N     1 
ATOM   2235  C  CA    . ALA B 2 34  ? -23.276 22.421  -12.417 1.00 17.66 ?  27  ALA B CA    1 
ATOM   2236  C  C     . ALA B 2 34  ? -21.810 22.825  -12.295 1.00 17.64 ?  27  ALA B C     1 
ATOM   2237  O  O     . ALA B 2 34  ? -21.353 23.743  -12.972 1.00 16.42 ?  27  ALA B O     1 
ATOM   2238  C  CB    . ALA B 2 34  ? -24.027 22.670  -11.125 1.00 15.93 ?  27  ALA B CB    1 
ATOM   2239  N  N     . VAL B 2 35  ? -21.084 22.111  -11.430 1.00 19.81 ?  28  VAL B N     1 
ATOM   2240  C  CA    . VAL B 2 35  ? -19.694 22.416  -11.140 1.00 20.94 ?  28  VAL B CA    1 
ATOM   2241  C  C     . VAL B 2 35  ? -18.905 22.473  -12.447 1.00 22.13 ?  28  VAL B C     1 
ATOM   2242  O  O     . VAL B 2 35  ? -18.134 23.405  -12.666 1.00 22.79 ?  28  VAL B O     1 
ATOM   2243  C  CB    . VAL B 2 35  ? -19.110 21.381  -10.158 1.00 24.68 ?  28  VAL B CB    1 
ATOM   2244  C  CG1   . VAL B 2 35  ? -17.607 21.551  -9.971  1.00 25.52 ?  28  VAL B CG1   1 
ATOM   2245  C  CG2   . VAL B 2 35  ? -19.823 21.422  -8.810  1.00 24.79 ?  28  VAL B CG2   1 
ATOM   2246  N  N     . MET B 2 36  ? -19.118 21.481  -13.319 1.00 21.94 ?  29  MET B N     1 
ATOM   2247  C  CA    . MET B 2 36  ? -18.372 21.383  -14.564 1.00 21.15 ?  29  MET B CA    1 
ATOM   2248  C  C     . MET B 2 36  ? -18.720 22.549  -15.485 1.00 22.52 ?  29  MET B C     1 
ATOM   2249  O  O     . MET B 2 36  ? -17.825 23.186  -16.036 1.00 23.70 ?  29  MET B O     1 
ATOM   2250  C  CB    . MET B 2 36  ? -18.641 20.056  -15.282 1.00 22.07 ?  29  MET B CB    1 
ATOM   2251  C  CG    . MET B 2 36  ? -17.796 18.904  -14.770 1.00 21.57 ?  29  MET B CG    1 
ATOM   2252  S  SD    . MET B 2 36  ? -17.949 17.419  -15.783 1.00 20.64 ?  29  MET B SD    1 
ATOM   2253  C  CE    . MET B 2 36  ? -19.484 16.730  -15.150 1.00 18.87 ?  29  MET B CE    1 
ATOM   2254  N  N     . ARG B 2 37  ? -20.019 22.820  -15.661 1.00 23.50 ?  30  ARG B N     1 
ATOM   2255  C  CA    . ARG B 2 37  ? -20.443 23.939  -16.487 1.00 26.00 ?  30  ARG B CA    1 
ATOM   2256  C  C     . ARG B 2 37  ? -19.772 25.216  -15.987 1.00 23.70 ?  30  ARG B C     1 
ATOM   2257  O  O     . ARG B 2 37  ? -19.307 26.026  -16.784 1.00 21.10 ?  30  ARG B O     1 
ATOM   2258  C  CB    . ARG B 2 37  ? -21.969 24.093  -16.526 1.00 32.23 ?  30  ARG B CB    1 
ATOM   2259  C  CG    . ARG B 2 37  ? -22.638 22.990  -17.334 1.00 36.76 ?  30  ARG B CG    1 
ATOM   2260  C  CD    . ARG B 2 37  ? -24.074 23.289  -17.725 1.00 41.81 ?  30  ARG B CD    1 
ATOM   2261  N  NE    . ARG B 2 37  ? -24.367 22.636  -19.007 1.00 45.43 ?  30  ARG B NE    1 
ATOM   2262  C  CZ    . ARG B 2 37  ? -25.014 21.487  -19.162 1.00 54.45 ?  30  ARG B CZ    1 
ATOM   2263  N  NH1   . ARG B 2 37  ? -25.499 20.846  -18.113 1.00 55.02 1  30  ARG B NH1   1 
ATOM   2264  N  NH2   . ARG B 2 37  ? -25.169 20.979  -20.372 1.00 57.71 ?  30  ARG B NH2   1 
ATOM   2265  N  N     . ALA B 2 38  ? -19.712 25.377  -14.660 1.00 22.70 ?  31  ALA B N     1 
ATOM   2266  C  CA    . ALA B 2 38  ? -19.227 26.612  -14.065 1.00 22.08 ?  31  ALA B CA    1 
ATOM   2267  C  C     . ALA B 2 38  ? -17.734 26.784  -14.334 1.00 23.19 ?  31  ALA B C     1 
ATOM   2268  O  O     . ALA B 2 38  ? -17.217 27.897  -14.277 1.00 23.03 ?  31  ALA B O     1 
ATOM   2269  C  CB    . ALA B 2 38  ? -19.521 26.623  -12.582 1.00 23.91 ?  31  ALA B CB    1 
ATOM   2270  N  N     . HIS B 2 39  ? -17.051 25.671  -14.625 1.00 22.25 ?  32  HIS B N     1 
ATOM   2271  C  CA    . HIS B 2 39  ? -15.613 25.689  -14.832 1.00 21.84 ?  32  HIS B CA    1 
ATOM   2272  C  C     . HIS B 2 39  ? -15.293 25.693  -16.328 1.00 22.30 ?  32  HIS B C     1 
ATOM   2273  O  O     . HIS B 2 39  ? -14.128 25.606  -16.710 1.00 18.13 ?  32  HIS B O     1 
ATOM   2274  C  CB    . HIS B 2 39  ? -14.943 24.540  -14.068 1.00 21.12 ?  32  HIS B CB    1 
ATOM   2275  C  CG    . HIS B 2 39  ? -14.717 24.812  -12.615 1.00 19.96 ?  32  HIS B CG    1 
ATOM   2276  N  ND1   . HIS B 2 39  ? -15.662 24.582  -11.636 1.00 18.52 ?  32  HIS B ND1   1 
ATOM   2277  C  CD2   . HIS B 2 39  ? -13.638 25.293  -11.980 1.00 19.42 ?  32  HIS B CD2   1 
ATOM   2278  C  CE1   . HIS B 2 39  ? -15.159 24.917  -10.456 1.00 18.57 ?  32  HIS B CE1   1 
ATOM   2279  N  NE2   . HIS B 2 39  ? -13.931 25.350  -10.641 1.00 19.72 ?  32  HIS B NE2   1 
ATOM   2280  N  N     . GLY B 2 40  ? -16.330 25.791  -17.169 1.00 24.60 ?  33  GLY B N     1 
ATOM   2281  C  CA    . GLY B 2 40  ? -16.144 26.127  -18.573 1.00 24.12 ?  33  GLY B CA    1 
ATOM   2282  C  C     . GLY B 2 40  ? -16.177 24.907  -19.493 1.00 26.49 ?  33  GLY B C     1 
ATOM   2283  O  O     . GLY B 2 40  ? -15.973 25.039  -20.698 1.00 27.73 ?  33  GLY B O     1 
ATOM   2284  N  N     . LEU B 2 41  ? -16.442 23.727  -18.925 1.00 26.61 ?  34  LEU B N     1 
ATOM   2285  C  CA    . LEU B 2 41  ? -16.463 22.495  -19.697 1.00 27.19 ?  34  LEU B CA    1 
ATOM   2286  C  C     . LEU B 2 41  ? -17.606 22.528  -20.710 1.00 27.72 ?  34  LEU B C     1 
ATOM   2287  O  O     . LEU B 2 41  ? -18.740 22.857  -20.368 1.00 26.48 ?  34  LEU B O     1 
ATOM   2288  C  CB    . LEU B 2 41  ? -16.568 21.289  -18.764 1.00 25.30 ?  34  LEU B CB    1 
ATOM   2289  C  CG    . LEU B 2 41  ? -15.246 20.781  -18.179 1.00 27.10 ?  34  LEU B CG    1 
ATOM   2290  C  CD1   . LEU B 2 41  ? -14.497 21.872  -17.433 1.00 26.67 ?  34  LEU B CD1   1 
ATOM   2291  C  CD2   . LEU B 2 41  ? -15.475 19.586  -17.271 1.00 26.24 ?  34  LEU B CD2   1 
ATOM   2292  N  N     . THR B 2 42  ? -17.279 22.172  -21.959 1.00 29.11 ?  35  THR B N     1 
ATOM   2293  C  CA    . THR B 2 42  ? -18.248 22.087  -23.040 1.00 29.48 ?  35  THR B CA    1 
ATOM   2294  C  C     . THR B 2 42  ? -19.142 20.869  -22.820 1.00 25.41 ?  35  THR B C     1 
ATOM   2295  O  O     . THR B 2 42  ? -18.876 20.046  -21.948 1.00 22.02 ?  35  THR B O     1 
ATOM   2296  C  CB    . THR B 2 42  ? -17.518 22.000  -24.381 1.00 30.46 ?  35  THR B CB    1 
ATOM   2297  O  OG1   . THR B 2 42  ? -16.768 20.790  -24.328 1.00 34.83 ?  35  THR B OG1   1 
ATOM   2298  C  CG2   . THR B 2 42  ? -16.579 23.167  -24.626 1.00 32.95 ?  35  THR B CG2   1 
ATOM   2299  N  N     . ASP B 2 43  ? -20.192 20.765  -23.643 1.00 26.70 ?  36  ASP B N     1 
ATOM   2300  C  CA    . ASP B 2 43  ? -21.195 19.721  -23.510 1.00 30.36 ?  36  ASP B CA    1 
ATOM   2301  C  C     . ASP B 2 43  ? -20.571 18.367  -23.831 1.00 28.00 ?  36  ASP B C     1 
ATOM   2302  O  O     . ASP B 2 43  ? -20.857 17.372  -23.170 1.00 31.31 ?  36  ASP B O     1 
ATOM   2303  C  CB    . ASP B 2 43  ? -22.385 19.980  -24.420 1.00 33.36 ?  36  ASP B CB    1 
ATOM   2304  C  CG    . ASP B 2 43  ? -23.105 21.303  -24.199 1.00 35.30 ?  36  ASP B CG    1 
ATOM   2305  O  OD1   . ASP B 2 43  ? -23.581 21.529  -23.067 1.00 35.21 ?  36  ASP B OD1   1 
ATOM   2306  O  OD2   . ASP B 2 43  ? -23.187 22.093  -25.164 1.00 33.82 -1 36  ASP B OD2   1 
ATOM   2307  N  N     . GLU B 2 44  ? -19.727 18.352  -24.866 1.00 27.82 ?  37  GLU B N     1 
ATOM   2308  C  CA    . GLU B 2 44  ? -19.052 17.143  -25.306 1.00 29.39 ?  37  GLU B CA    1 
ATOM   2309  C  C     . GLU B 2 44  ? -18.134 16.640  -24.193 1.00 24.59 ?  37  GLU B C     1 
ATOM   2310  O  O     . GLU B 2 44  ? -18.055 15.439  -23.951 1.00 17.32 ?  37  GLU B O     1 
ATOM   2311  C  CB    . GLU B 2 44  ? -18.292 17.428  -26.603 1.00 31.03 ?  37  GLU B CB    1 
ATOM   2312  C  CG    . GLU B 2 44  ? -17.021 18.247  -26.395 1.00 35.55 ?  37  GLU B CG    1 
ATOM   2313  C  CD    . GLU B 2 44  ? -16.461 18.894  -27.650 1.00 39.33 ?  37  GLU B CD    1 
ATOM   2314  O  OE1   . GLU B 2 44  ? -17.004 19.941  -28.067 1.00 38.08 ?  37  GLU B OE1   1 
ATOM   2315  O  OE2   . GLU B 2 44  ? -15.492 18.346  -28.218 1.00 29.44 -1 37  GLU B OE2   1 
ATOM   2316  N  N     . GLN B 2 45  ? -17.451 17.571  -23.515 1.00 25.60 ?  38  GLN B N     1 
ATOM   2317  C  CA    . GLN B 2 45  ? -16.552 17.225  -22.425 1.00 26.52 ?  38  GLN B CA    1 
ATOM   2318  C  C     . GLN B 2 45  ? -17.356 16.678  -21.251 1.00 24.97 ?  38  GLN B C     1 
ATOM   2319  O  O     . GLN B 2 45  ? -16.942 15.720  -20.604 1.00 29.55 ?  38  GLN B O     1 
ATOM   2320  C  CB    . GLN B 2 45  ? -15.720 18.426  -21.974 1.00 29.30 ?  38  GLN B CB    1 
ATOM   2321  C  CG    . GLN B 2 45  ? -14.708 18.890  -23.015 1.00 27.99 ?  38  GLN B CG    1 
ATOM   2322  C  CD    . GLN B 2 45  ? -13.953 20.138  -22.615 1.00 27.85 ?  38  GLN B CD    1 
ATOM   2323  O  OE1   . GLN B 2 45  ? -14.301 20.827  -21.649 1.00 27.92 ?  38  GLN B OE1   1 
ATOM   2324  N  NE2   . GLN B 2 45  ? -12.910 20.448  -23.371 1.00 27.44 ?  38  GLN B NE2   1 
ATOM   2325  N  N     . ILE B 2 46  ? -18.508 17.299  -20.986 1.00 23.28 ?  39  ILE B N     1 
ATOM   2326  C  CA    . ILE B 2 46  ? -19.355 16.892  -19.878 1.00 21.34 ?  39  ILE B CA    1 
ATOM   2327  C  C     . ILE B 2 46  ? -19.978 15.533  -20.189 1.00 21.40 ?  39  ILE B C     1 
ATOM   2328  O  O     . ILE B 2 46  ? -20.076 14.678  -19.312 1.00 21.39 ?  39  ILE B O     1 
ATOM   2329  C  CB    . ILE B 2 46  ? -20.418 17.964  -19.583 1.00 18.27 ?  39  ILE B CB    1 
ATOM   2330  C  CG1   . ILE B 2 46  ? -19.761 19.262  -19.116 1.00 18.85 ?  39  ILE B CG1   1 
ATOM   2331  C  CG2   . ILE B 2 46  ? -21.452 17.450  -18.581 1.00 18.39 ?  39  ILE B CG2   1 
ATOM   2332  C  CD1   . ILE B 2 46  ? -20.720 20.274  -18.519 1.00 19.16 ?  39  ILE B CD1   1 
ATOM   2333  N  N     . ASN B 2 47  ? -20.393 15.350  -21.446 1.00 21.67 ?  40  ASN B N     1 
ATOM   2334  C  CA    . ASN B 2 47  ? -21.053 14.128  -21.877 1.00 25.69 ?  40  ASN B CA    1 
ATOM   2335  C  C     . ASN B 2 47  ? -20.102 12.947  -21.707 1.00 26.19 ?  40  ASN B C     1 
ATOM   2336  O  O     . ASN B 2 47  ? -20.502 11.871  -21.266 1.00 27.26 ?  40  ASN B O     1 
ATOM   2337  C  CB    . ASN B 2 47  ? -21.530 14.246  -23.320 1.00 27.32 ?  40  ASN B CB    1 
ATOM   2338  C  CG    . ASN B 2 47  ? -22.314 13.034  -23.763 1.00 30.80 ?  40  ASN B CG    1 
ATOM   2339  O  OD1   . ASN B 2 47  ? -23.333 12.695  -23.152 1.00 33.09 ?  40  ASN B OD1   1 
ATOM   2340  N  ND2   . ASN B 2 47  ? -21.860 12.372  -24.818 1.00 32.84 ?  40  ASN B ND2   1 
ATOM   2341  N  N     . ALA B 2 48  ? -18.838 13.173  -22.070 1.00 26.35 ?  41  ALA B N     1 
ATOM   2342  C  CA    . ALA B 2 48  ? -17.804 12.156  -21.988 1.00 28.17 ?  41  ALA B CA    1 
ATOM   2343  C  C     . ALA B 2 48  ? -17.563 11.771  -20.530 1.00 29.57 ?  41  ALA B C     1 
ATOM   2344  O  O     . ALA B 2 48  ? -17.275 10.614  -20.230 1.00 28.66 ?  41  ALA B O     1 
ATOM   2345  C  CB    . ALA B 2 48  ? -16.543 12.670  -22.646 1.00 28.16 ?  41  ALA B CB    1 
ATOM   2346  N  N     . VAL B 2 49  ? -17.685 12.757  -19.634 1.00 26.39 ?  42  VAL B N     1 
ATOM   2347  C  CA    . VAL B 2 49  ? -17.499 12.533  -18.209 1.00 25.91 ?  42  VAL B CA    1 
ATOM   2348  C  C     . VAL B 2 49  ? -18.648 11.673  -17.692 1.00 25.09 ?  42  VAL B C     1 
ATOM   2349  O  O     . VAL B 2 49  ? -18.438 10.767  -16.889 1.00 27.89 ?  42  VAL B O     1 
ATOM   2350  C  CB    . VAL B 2 49  ? -17.408 13.847  -17.410 1.00 28.48 ?  42  VAL B CB    1 
ATOM   2351  C  CG1   . VAL B 2 49  ? -17.551 13.607  -15.911 1.00 28.98 ?  42  VAL B CG1   1 
ATOM   2352  C  CG2   . VAL B 2 49  ? -16.124 14.608  -17.712 1.00 31.90 ?  42  VAL B CG2   1 
ATOM   2353  N  N     . MET B 2 50  ? -19.862 11.973  -18.160 1.00 24.33 ?  43  MET B N     1 
ATOM   2354  C  CA    . MET B 2 50  ? -21.057 11.324  -17.650 1.00 22.44 ?  43  MET B CA    1 
ATOM   2355  C  C     . MET B 2 50  ? -21.204 9.931   -18.262 1.00 20.79 ?  43  MET B C     1 
ATOM   2356  O  O     . MET B 2 50  ? -22.003 9.131   -17.781 1.00 18.69 ?  43  MET B O     1 
ATOM   2357  C  CB    . MET B 2 50  ? -22.302 12.173  -17.939 1.00 22.00 ?  43  MET B CB    1 
ATOM   2358  C  CG    . MET B 2 50  ? -22.236 13.578  -17.360 1.00 22.90 ?  43  MET B CG    1 
ATOM   2359  S  SD    . MET B 2 50  ? -21.915 13.609  -15.585 1.00 24.13 ?  43  MET B SD    1 
ATOM   2360  C  CE    . MET B 2 50  ? -23.274 12.583  -15.008 1.00 25.13 ?  43  MET B CE    1 
ATOM   2361  N  N     . THR B 2 51  ? -20.434 9.638   -19.316 1.00 23.44 ?  44  THR B N     1 
ATOM   2362  C  CA    . THR B 2 51  ? -20.498 8.326   -19.945 1.00 29.04 ?  44  THR B CA    1 
ATOM   2363  C  C     . THR B 2 51  ? -19.215 7.543   -19.665 1.00 27.93 ?  44  THR B C     1 
ATOM   2364  O  O     . THR B 2 51  ? -19.102 6.382   -20.052 1.00 30.08 ?  44  THR B O     1 
ATOM   2365  C  CB    . THR B 2 51  ? -20.762 8.466   -21.444 1.00 30.05 ?  44  THR B CB    1 
ATOM   2366  O  OG1   . THR B 2 51  ? -19.746 9.334   -21.938 1.00 34.67 ?  44  THR B OG1   1 
ATOM   2367  C  CG2   . THR B 2 51  ? -22.137 9.039   -21.738 1.00 30.28 ?  44  THR B CG2   1 
ATOM   2368  N  N     . GLY B 2 52  ? -18.253 8.187   -18.995 1.00 32.50 ?  45  GLY B N     1 
ATOM   2369  C  CA    . GLY B 2 52  ? -17.053 7.513   -18.524 1.00 31.47 ?  45  GLY B CA    1 
ATOM   2370  C  C     . GLY B 2 52  ? -16.051 7.251   -19.647 1.00 34.03 ?  45  GLY B C     1 
ATOM   2371  O  O     . GLY B 2 52  ? -15.153 6.425   -19.498 1.00 39.91 ?  45  GLY B O     1 
ATOM   2372  N  N     . ASP B 2 53  ? -16.208 7.970   -20.764 1.00 33.62 ?  46  ASP B N     1 
ATOM   2373  C  CA    . ASP B 2 53  ? -15.363 7.783   -21.933 1.00 30.51 ?  46  ASP B CA    1 
ATOM   2374  C  C     . ASP B 2 53  ? -14.046 8.531   -21.734 1.00 29.85 ?  46  ASP B C     1 
ATOM   2375  O  O     . ASP B 2 53  ? -13.839 9.607   -22.293 1.00 17.60 ?  46  ASP B O     1 
ATOM   2376  C  CB    . ASP B 2 53  ? -16.093 8.186   -23.206 1.00 32.42 ?  46  ASP B CB    1 
ATOM   2377  C  CG    . ASP B 2 53  ? -15.304 8.030   -24.499 1.00 38.58 ?  46  ASP B CG    1 
ATOM   2378  O  OD1   . ASP B 2 53  ? -14.123 7.629   -24.424 1.00 36.54 ?  46  ASP B OD1   1 
ATOM   2379  O  OD2   . ASP B 2 53  ? -15.879 8.311   -25.572 1.00 46.74 -1 46  ASP B OD2   1 
ATOM   2380  N  N     . MET B 2 54  ? -13.166 7.929   -20.925 1.00 29.72 ?  47  MET B N     1 
ATOM   2381  C  CA    . MET B 2 54  ? -11.826 8.439   -20.689 1.00 31.65 ?  47  MET B CA    1 
ATOM   2382  C  C     . MET B 2 54  ? -11.113 8.658   -22.023 1.00 34.58 ?  47  MET B C     1 
ATOM   2383  O  O     . MET B 2 54  ? -10.433 9.664   -22.210 1.00 32.56 ?  47  MET B O     1 
ATOM   2384  C  CB    . MET B 2 54  ? -11.021 7.457   -19.829 1.00 30.77 ?  47  MET B CB    1 
ATOM   2385  C  CG    . MET B 2 54  ? -11.548 7.273   -18.414 1.00 28.58 ?  47  MET B CG    1 
ATOM   2386  S  SD    . MET B 2 54  ? -11.883 8.823   -17.553 1.00 28.16 ?  47  MET B SD    1 
ATOM   2387  C  CE    . MET B 2 54  ? -13.638 8.984   -17.911 1.00 26.56 ?  47  MET B CE    1 
ATOM   2388  N  N     . GLU B 2 55  ? -11.273 7.699   -22.942 1.00 36.58 ?  48  GLU B N     1 
ATOM   2389  C  CA    . GLU B 2 55  ? -10.692 7.796   -24.273 1.00 41.34 ?  48  GLU B CA    1 
ATOM   2390  C  C     . GLU B 2 55  ? -10.913 9.195   -24.843 1.00 37.22 ?  48  GLU B C     1 
ATOM   2391  O  O     . GLU B 2 55  ? -9.953  9.889   -25.172 1.00 34.90 ?  48  GLU B O     1 
ATOM   2392  C  CB    . GLU B 2 55  ? -11.282 6.739   -25.208 1.00 46.35 ?  48  GLU B CB    1 
ATOM   2393  C  CG    . GLU B 2 55  ? -10.378 5.528   -25.414 1.00 50.03 ?  48  GLU B CG    1 
ATOM   2394  C  CD    . GLU B 2 55  ? -9.338  5.717   -26.506 1.00 55.64 ?  48  GLU B CD    1 
ATOM   2395  O  OE1   . GLU B 2 55  ? -9.317  6.804   -27.123 1.00 54.83 ?  48  GLU B OE1   1 
ATOM   2396  O  OE2   . GLU B 2 55  ? -8.554  4.773   -26.743 1.00 52.89 -1 48  GLU B OE2   1 
ATOM   2397  N  N     . LYS B 2 56  ? -12.183 9.596   -24.965 1.00 39.38 ?  49  LYS B N     1 
ATOM   2398  C  CA    . LYS B 2 56  ? -12.520 10.879  -25.558 1.00 38.15 ?  49  LYS B CA    1 
ATOM   2399  C  C     . LYS B 2 56  ? -11.878 11.996  -24.739 1.00 34.24 ?  49  LYS B C     1 
ATOM   2400  O  O     . LYS B 2 56  ? -11.155 12.827  -25.282 1.00 34.19 ?  49  LYS B O     1 
ATOM   2401  C  CB    . LYS B 2 56  ? -14.036 11.102  -25.627 1.00 40.24 ?  49  LYS B CB    1 
ATOM   2402  C  CG    . LYS B 2 56  ? -14.517 12.029  -26.741 1.00 41.32 ?  49  LYS B CG    1 
ATOM   2403  C  CD    . LYS B 2 56  ? -14.847 11.342  -28.063 1.00 42.32 ?  49  LYS B CD    1 
ATOM   2404  C  CE    . LYS B 2 56  ? -13.675 11.141  -28.968 1.00 43.30 ?  49  LYS B CE    1 
ATOM   2405  N  NZ    . LYS B 2 56  ? -14.119 10.915  -30.347 1.00 45.77 1  49  LYS B NZ    1 
ATOM   2406  N  N     . LEU B 2 57  ? -12.149 12.005  -23.429 1.00 30.90 ?  50  LEU B N     1 
ATOM   2407  C  CA    . LEU B 2 57  ? -11.689 13.080  -22.564 1.00 31.30 ?  50  LEU B CA    1 
ATOM   2408  C  C     . LEU B 2 57  ? -10.259 13.458  -22.944 1.00 35.35 ?  50  LEU B C     1 
ATOM   2409  O  O     . LEU B 2 57  ? -9.956  14.634  -23.134 1.00 32.65 ?  50  LEU B O     1 
ATOM   2410  C  CB    . LEU B 2 57  ? -11.789 12.692  -21.090 1.00 31.44 ?  50  LEU B CB    1 
ATOM   2411  C  CG    . LEU B 2 57  ? -13.190 12.748  -20.474 1.00 30.17 ?  50  LEU B CG    1 
ATOM   2412  C  CD1   . LEU B 2 57  ? -13.130 12.364  -19.006 1.00 28.66 ?  50  LEU B CD1   1 
ATOM   2413  C  CD2   . LEU B 2 57  ? -13.812 14.126  -20.649 1.00 27.81 ?  50  LEU B CD2   1 
ATOM   2414  N  N     . LYS B 2 58  ? -9.388  12.451  -23.054 1.00 35.90 ?  51  LYS B N     1 
ATOM   2415  C  CA    . LYS B 2 58  ? -7.980  12.690  -23.323 1.00 42.96 ?  51  LYS B CA    1 
ATOM   2416  C  C     . LYS B 2 58  ? -7.830  13.382  -24.676 1.00 47.07 ?  51  LYS B C     1 
ATOM   2417  O  O     . LYS B 2 58  ? -6.996  14.272  -24.833 1.00 49.91 ?  51  LYS B O     1 
ATOM   2418  C  CB    . LYS B 2 58  ? -7.206  11.371  -23.221 1.00 44.16 ?  51  LYS B CB    1 
ATOM   2419  C  CG    . LYS B 2 58  ? -7.222  10.749  -21.828 1.00 41.01 ?  51  LYS B CG    1 
ATOM   2420  C  CD    . LYS B 2 58  ? -6.396  9.477   -21.685 1.00 41.48 ?  51  LYS B CD    1 
ATOM   2421  C  CE    . LYS B 2 58  ? -6.368  8.979   -20.274 1.00 38.54 ?  51  LYS B CE    1 
ATOM   2422  N  NZ    . LYS B 2 58  ? -5.688  7.686   -20.165 1.00 39.48 1  51  LYS B NZ    1 
ATOM   2423  N  N     . THR B 2 59  ? -8.655  12.966  -25.643 1.00 52.33 ?  52  THR B N     1 
ATOM   2424  C  CA    . THR B 2 59  ? -8.694  13.579  -26.960 1.00 56.18 ?  52  THR B CA    1 
ATOM   2425  C  C     . THR B 2 59  ? -9.017  15.065  -26.820 1.00 56.19 ?  52  THR B C     1 
ATOM   2426  O  O     . THR B 2 59  ? -8.200  15.916  -27.167 1.00 59.46 ?  52  THR B O     1 
ATOM   2427  C  CB    . THR B 2 59  ? -9.725  12.847  -27.819 1.00 56.19 ?  52  THR B CB    1 
ATOM   2428  O  OG1   . THR B 2 59  ? -9.127  11.590  -28.118 1.00 61.89 ?  52  THR B OG1   1 
ATOM   2429  C  CG2   . THR B 2 59  ? -10.057 13.579  -29.107 1.00 59.50 ?  52  THR B CG2   1 
ATOM   2430  N  N     . LEU B 2 60  ? -10.218 15.363  -26.311 1.00 53.43 ?  53  LEU B N     1 
ATOM   2431  C  CA    . LEU B 2 60  ? -10.654 16.736  -26.116 1.00 50.38 ?  53  LEU B CA    1 
ATOM   2432  C  C     . LEU B 2 60  ? -9.599  17.483  -25.284 1.00 49.99 ?  53  LEU B C     1 
ATOM   2433  O  O     . LEU B 2 60  ? -8.858  18.290  -25.889 1.00 49.38 ?  53  LEU B O     1 
ATOM   2434  C  CB    . LEU B 2 60  ? -12.023 16.766  -25.435 1.00 46.25 ?  53  LEU B CB    1 
ATOM   2435  C  CG    . LEU B 2 60  ? -13.098 15.857  -26.040 1.00 38.69 ?  53  LEU B CG    1 
ATOM   2436  C  CD1   . LEU B 2 60  ? -14.407 15.954  -25.271 1.00 33.56 ?  53  LEU B CD1   1 
ATOM   2437  C  CD2   . LEU B 2 60  ? -13.310 16.185  -27.507 1.00 39.77 ?  53  LEU B CD2   1 
ATOM   2438  N  N     . SER B 2 68  ? 2.606   1.417   -19.098 1.00 36.68 ?  61  SER B N     1 
ATOM   2439  C  CA    . SER B 2 68  ? 2.439   1.356   -17.621 1.00 36.96 ?  61  SER B CA    1 
ATOM   2440  C  C     . SER B 2 68  ? 3.419   0.359   -16.999 1.00 37.94 ?  61  SER B C     1 
ATOM   2441  O  O     . SER B 2 68  ? 4.102   0.695   -16.033 1.00 42.08 ?  61  SER B O     1 
ATOM   2442  C  CB    . SER B 2 68  ? 1.012   1.029   -17.260 1.00 36.91 ?  61  SER B CB    1 
ATOM   2443  O  OG    . SER B 2 68  ? 0.789   1.182   -15.865 1.00 38.36 ?  61  SER B OG    1 
ATOM   2444  N  N     . TYR B 2 69  ? 3.490   -0.861  -17.549 1.00 35.99 ?  62  TYR B N     1 
ATOM   2445  C  CA    . TYR B 2 69  ? 4.259   -1.926  -16.919 1.00 35.82 ?  62  TYR B CA    1 
ATOM   2446  C  C     . TYR B 2 69  ? 5.680   -1.483  -16.589 1.00 32.33 ?  62  TYR B C     1 
ATOM   2447  O  O     . TYR B 2 69  ? 6.385   -0.946  -17.445 1.00 33.29 ?  62  TYR B O     1 
ATOM   2448  C  CB    . TYR B 2 69  ? 4.373   -3.208  -17.747 1.00 40.43 ?  62  TYR B CB    1 
ATOM   2449  C  CG    . TYR B 2 69  ? 3.036   -3.816  -18.145 1.00 40.25 ?  62  TYR B CG    1 
ATOM   2450  C  CD1   . TYR B 2 69  ? 2.149   -4.294  -17.189 1.00 39.95 ?  62  TYR B CD1   1 
ATOM   2451  C  CD2   . TYR B 2 69  ? 2.678   -3.931  -19.481 1.00 40.28 ?  62  TYR B CD2   1 
ATOM   2452  C  CE1   . TYR B 2 69  ? 0.932   -4.848  -17.550 1.00 41.13 ?  62  TYR B CE1   1 
ATOM   2453  C  CE2   . TYR B 2 69  ? 1.467   -4.487  -19.855 1.00 42.68 ?  62  TYR B CE2   1 
ATOM   2454  C  CZ    . TYR B 2 69  ? 0.592   -4.947  -18.887 1.00 42.87 ?  62  TYR B CZ    1 
ATOM   2455  O  OH    . TYR B 2 69  ? -0.603  -5.497  -19.251 1.00 48.55 ?  62  TYR B OH    1 
HETATM 2456  N  N     . MLE B 2 70  ? 6.110   -1.714  -15.350 1.00 29.20 ?  63  MLE B N     1 
HETATM 2457  C  CN    . MLE B 2 70  ? 5.109   -2.186  -14.425 1.00 29.12 ?  63  MLE B CN    1 
HETATM 2458  C  CA    . MLE B 2 70  ? 7.474   -1.445  -14.880 1.00 29.25 ?  63  MLE B CA    1 
HETATM 2459  C  CB    . MLE B 2 70  ? 7.280   -0.340  -13.827 1.00 29.96 ?  63  MLE B CB    1 
HETATM 2460  C  CG    . MLE B 2 70  ? 8.315   0.785   -13.786 1.00 35.58 ?  63  MLE B CG    1 
HETATM 2461  C  CD1   . MLE B 2 70  ? 7.698   2.058   -13.218 1.00 39.01 ?  63  MLE B CD1   1 
HETATM 2462  C  CD2   . MLE B 2 70  ? 9.520   0.379   -12.955 1.00 35.88 ?  63  MLE B CD2   1 
HETATM 2463  C  C     . MLE B 2 70  ? 8.226   -2.644  -14.287 1.00 28.62 ?  63  MLE B C     1 
HETATM 2464  O  O     . MLE B 2 70  ? 9.222   -2.451  -13.593 1.00 29.03 ?  63  MLE B O     1 
ATOM   2465  N  N     . VAL B 2 71  ? 7.772   -3.881  -14.572 1.00 28.52 ?  64  VAL B N     1 
ATOM   2466  C  CA    . VAL B 2 71  ? 8.406   -5.072  -14.009 1.00 29.87 ?  64  VAL B CA    1 
ATOM   2467  C  C     . VAL B 2 71  ? 7.994   -6.345  -14.761 1.00 28.29 ?  64  VAL B C     1 
ATOM   2468  O  O     . VAL B 2 71  ? 7.279   -6.279  -15.757 1.00 27.07 ?  64  VAL B O     1 
ATOM   2469  C  CB    . VAL B 2 71  ? 8.058   -5.171  -12.510 1.00 29.22 ?  64  VAL B CB    1 
ATOM   2470  C  CG1   . VAL B 2 71  ? 6.663   -5.745  -12.292 1.00 33.28 ?  64  VAL B CG1   1 
ATOM   2471  C  CG2   . VAL B 2 71  ? 9.092   -5.978  -11.734 1.00 31.25 ?  64  VAL B CG2   1 
ATOM   2472  N  N     . TRP B 2 72  ? 8.461   -7.507  -14.264 1.00 33.18 ?  65  TRP B N     1 
ATOM   2473  C  CA    . TRP B 2 72  ? 8.229   -8.819  -14.868 1.00 37.56 ?  65  TRP B CA    1 
ATOM   2474  C  C     . TRP B 2 72  ? 8.137   -9.893  -13.783 1.00 40.27 ?  65  TRP B C     1 
ATOM   2475  O  O     . TRP B 2 72  ? 7.850   -9.582  -12.628 1.00 46.04 ?  65  TRP B O     1 
ATOM   2476  C  CB    . TRP B 2 72  ? 9.381   -9.145  -15.825 1.00 39.97 ?  65  TRP B CB    1 
ATOM   2477  C  CG    . TRP B 2 72  ? 10.698  -8.836  -15.172 1.00 44.80 ?  65  TRP B CG    1 
ATOM   2478  C  CD1   . TRP B 2 72  ? 11.157  -9.337  -13.990 1.00 46.40 ?  65  TRP B CD1   1 
ATOM   2479  C  CD2   . TRP B 2 72  ? 11.665  -7.855  -15.597 1.00 47.58 ?  65  TRP B CD2   1 
ATOM   2480  N  NE1   . TRP B 2 72  ? 12.368  -8.781  -13.677 1.00 46.60 ?  65  TRP B NE1   1 
ATOM   2481  C  CE2   . TRP B 2 72  ? 12.700  -7.861  -14.637 1.00 45.49 ?  65  TRP B CE2   1 
ATOM   2482  C  CE3   . TRP B 2 72  ? 11.761  -6.993  -16.694 1.00 51.31 ?  65  TRP B CE3   1 
ATOM   2483  C  CZ2   . TRP B 2 72  ? 13.816  -7.037  -14.748 1.00 48.04 ?  65  TRP B CZ2   1 
ATOM   2484  C  CZ3   . TRP B 2 72  ? 12.862  -6.172  -16.795 1.00 52.26 ?  65  TRP B CZ3   1 
ATOM   2485  C  CH2   . TRP B 2 72  ? 13.870  -6.192  -15.833 1.00 51.59 ?  65  TRP B CH2   1 
ATOM   2486  N  N     . SER B 2 73  ? 8.398   -11.157 -14.157 1.00 43.98 ?  66  SER B N     1 
ATOM   2487  C  CA    . SER B 2 73  ? 8.488   -12.240 -13.188 1.00 46.24 ?  66  SER B CA    1 
ATOM   2488  C  C     . SER B 2 73  ? 9.807   -12.137 -12.430 1.00 51.37 ?  66  SER B C     1 
ATOM   2489  O  O     . SER B 2 73  ? 9.830   -11.861 -11.233 1.00 61.21 ?  66  SER B O     1 
ATOM   2490  C  CB    . SER B 2 73  ? 8.380   -13.601 -13.837 1.00 46.56 ?  66  SER B CB    1 
ATOM   2491  O  OG    . SER B 2 73  ? 7.518   -13.574 -14.967 1.00 47.66 ?  66  SER B OG    1 
ATOM   2492  N  N     . HIS B 2 74  ? 10.900  -12.366 -13.163 1.00 57.87 ?  67  HIS B N     1 
ATOM   2493  C  CA    . HIS B 2 74  ? 12.220  -12.526 -12.577 1.00 58.05 ?  67  HIS B CA    1 
ATOM   2494  C  C     . HIS B 2 74  ? 13.144  -11.415 -13.086 1.00 60.83 ?  67  HIS B C     1 
ATOM   2495  O  O     . HIS B 2 74  ? 13.292  -11.318 -14.325 1.00 64.07 ?  67  HIS B O     1 
ATOM   2496  C  CB    . HIS B 2 74  ? 12.758  -13.926 -12.896 1.00 55.94 ?  67  HIS B CB    1 
ATOM   2497  C  CG    . HIS B 2 74  ? 12.577  -14.320 -14.325 1.00 56.45 ?  67  HIS B CG    1 
ATOM   2498  N  ND1   . HIS B 2 74  ? 11.337  -14.576 -14.871 1.00 55.31 ?  67  HIS B ND1   1 
ATOM   2499  C  CD2   . HIS B 2 74  ? 13.457  -14.472 -15.324 1.00 57.01 ?  67  HIS B CD2   1 
ATOM   2500  C  CE1   . HIS B 2 74  ? 11.477  -14.887 -16.151 1.00 54.48 ?  67  HIS B CE1   1 
ATOM   2501  N  NE2   . HIS B 2 74  ? 12.757  -14.833 -16.447 1.00 52.74 ?  67  HIS B NE2   1 
ATOM   2502  N  N     . GLY C 1 2   ? -25.318 14.929  6.556   1.00 31.91 ?  2   GLY C N     1 
ATOM   2503  C  CA    . GLY C 1 2   ? -23.963 14.587  7.031   1.00 29.57 ?  2   GLY C CA    1 
ATOM   2504  C  C     . GLY C 1 2   ? -23.314 13.533  6.138   1.00 30.47 ?  2   GLY C C     1 
ATOM   2505  O  O     . GLY C 1 2   ? -24.003 12.797  5.435   1.00 29.39 ?  2   GLY C O     1 
ATOM   2506  N  N     . SER C 1 3   ? -21.979 13.474  6.186   1.00 26.10 ?  3   SER C N     1 
ATOM   2507  C  CA    . SER C 1 3   ? -21.207 12.588  5.330   1.00 26.82 ?  3   SER C CA    1 
ATOM   2508  C  C     . SER C 1 3   ? -20.037 12.006  6.114   1.00 23.37 ?  3   SER C C     1 
ATOM   2509  O  O     . SER C 1 3   ? -19.643 12.546  7.146   1.00 20.47 ?  3   SER C O     1 
ATOM   2510  C  CB    . SER C 1 3   ? -20.717 13.311  4.101   1.00 27.69 ?  3   SER C CB    1 
ATOM   2511  O  OG    . SER C 1 3   ? -19.840 14.373  4.450   1.00 26.87 ?  3   SER C OG    1 
ATOM   2512  N  N     . LEU C 1 4   ? -19.486 10.900  5.606   1.00 21.80 ?  4   LEU C N     1 
ATOM   2513  C  CA    . LEU C 1 4   ? -18.293 10.313  6.188   1.00 18.73 ?  4   LEU C CA    1 
ATOM   2514  C  C     . LEU C 1 4   ? -17.192 10.234  5.134   1.00 15.28 ?  4   LEU C C     1 
ATOM   2515  O  O     . LEU C 1 4   ? -17.445 9.891   3.981   1.00 11.99 ?  4   LEU C O     1 
ATOM   2516  C  CB    . LEU C 1 4   ? -18.637 8.940   6.760   1.00 23.07 ?  4   LEU C CB    1 
ATOM   2517  C  CG    . LEU C 1 4   ? -17.498 8.201   7.468   1.00 23.31 ?  4   LEU C CG    1 
ATOM   2518  C  CD1   . LEU C 1 4   ? -16.931 9.017   8.616   1.00 25.35 ?  4   LEU C CD1   1 
ATOM   2519  C  CD2   . LEU C 1 4   ? -18.000 6.855   7.951   1.00 24.85 ?  4   LEU C CD2   1 
ATOM   2520  N  N     . VAL C 1 5   ? -15.972 10.596  5.548   1.00 13.77 ?  5   VAL C N     1 
ATOM   2521  C  CA    . VAL C 1 5   ? -14.773 10.298  4.784   1.00 11.99 ?  5   VAL C CA    1 
ATOM   2522  C  C     . VAL C 1 5   ? -13.680 9.921   5.778   1.00 12.81 ?  5   VAL C C     1 
ATOM   2523  O  O     . VAL C 1 5   ? -13.269 10.729  6.608   1.00 10.71 ?  5   VAL C O     1 
ATOM   2524  C  CB    . VAL C 1 5   ? -14.273 11.409  3.842   1.00 12.45 ?  5   VAL C CB    1 
ATOM   2525  C  CG1   . VAL C 1 5   ? -13.070 10.936  3.031   1.00 11.37 ?  5   VAL C CG1   1 
ATOM   2526  C  CG2   . VAL C 1 5   ? -15.370 11.919  2.912   1.00 11.87 ?  5   VAL C CG2   1 
ATOM   2527  N  N     . CYS C 1 6   ? -13.237 8.665   5.684   1.00 12.79 ?  6   CYS C N     1 
ATOM   2528  C  CA    . CYS C 1 6   ? -12.092 8.188   6.436   1.00 12.41 ?  6   CYS C CA    1 
ATOM   2529  C  C     . CYS C 1 6   ? -10.841 8.413   5.596   1.00 11.93 ?  6   CYS C C     1 
ATOM   2530  O  O     . CYS C 1 6   ? -10.816 8.087   4.413   1.00 12.36 ?  6   CYS C O     1 
ATOM   2531  C  CB    . CYS C 1 6   ? -12.238 6.708   6.768   1.00 12.84 ?  6   CYS C CB    1 
ATOM   2532  S  SG    . CYS C 1 6   ? -13.796 6.304   7.598   1.00 14.17 ?  6   CYS C SG    1 
ATOM   2533  N  N     . VAL C 1 7   ? -9.805  8.986   6.205   1.00 13.29 ?  7   VAL C N     1 
ATOM   2534  C  CA    . VAL C 1 7   ? -8.549  9.142   5.499   1.00 13.93 ?  7   VAL C CA    1 
ATOM   2535  C  C     . VAL C 1 7   ? -7.464  8.451   6.317   1.00 13.67 ?  7   VAL C C     1 
ATOM   2536  O  O     . VAL C 1 7   ? -7.701  8.017   7.442   1.00 13.78 ?  7   VAL C O     1 
ATOM   2537  C  CB    . VAL C 1 7   ? -8.198  10.612  5.195   1.00 15.99 ?  7   VAL C CB    1 
ATOM   2538  C  CG1   . VAL C 1 7   ? -9.328  11.313  4.447   1.00 17.15 ?  7   VAL C CG1   1 
ATOM   2539  C  CG2   . VAL C 1 7   ? -7.829  11.398  6.446   1.00 17.99 ?  7   VAL C CG2   1 
ATOM   2540  N  N     . GLY C 1 8   ? -6.286  8.314   5.708   1.00 12.71 ?  8   GLY C N     1 
ATOM   2541  C  CA    . GLY C 1 8   ? -5.098  7.888   6.422   1.00 12.92 ?  8   GLY C CA    1 
ATOM   2542  C  C     . GLY C 1 8   ? -4.079  9.022   6.465   1.00 12.23 ?  8   GLY C C     1 
ATOM   2543  O  O     . GLY C 1 8   ? -4.042  9.850   5.560   1.00 10.07 ?  8   GLY C O     1 
ATOM   2544  N  N     . THR C 1 9   ? -3.263  9.054   7.525   1.00 13.59 ?  9   THR C N     1 
ATOM   2545  C  CA    . THR C 1 9   ? -2.307  10.134  7.706   1.00 17.65 ?  9   THR C CA    1 
ATOM   2546  C  C     . THR C 1 9   ? -0.900  9.659   7.353   1.00 18.59 ?  9   THR C C     1 
ATOM   2547  O  O     . THR C 1 9   ? 0.056   10.421  7.481   1.00 21.09 ?  9   THR C O     1 
ATOM   2548  C  CB    . THR C 1 9   ? -2.356  10.651  9.143   1.00 18.76 ?  9   THR C CB    1 
ATOM   2549  O  OG1   . THR C 1 9   ? -1.843  9.591   9.943   1.00 20.04 ?  9   THR C OG1   1 
ATOM   2550  C  CG2   . THR C 1 9   ? -3.755  11.038  9.587   1.00 19.93 ?  9   THR C CG2   1 
ATOM   2551  N  N     . GLY C 1 10  ? -0.769  8.403   6.914   1.00 20.42 ?  10  GLY C N     1 
ATOM   2552  C  CA    . GLY C 1 10  ? 0.546   7.823   6.697   1.00 18.19 ?  10  GLY C CA    1 
ATOM   2553  C  C     . GLY C 1 10  ? 1.174   7.423   8.029   1.00 16.26 ?  10  GLY C C     1 
ATOM   2554  O  O     . GLY C 1 10  ? 0.496   7.429   9.053   1.00 17.24 ?  10  GLY C O     1 
ATOM   2555  N  N     . LEU C 1 11  ? 2.467   7.080   8.014   1.00 17.25 ?  11  LEU C N     1 
ATOM   2556  C  CA    . LEU C 1 11  ? 3.166   6.707   9.236   1.00 17.65 ?  11  LEU C CA    1 
ATOM   2557  C  C     . LEU C 1 11  ? 3.996   7.883   9.754   1.00 13.97 ?  11  LEU C C     1 
ATOM   2558  O  O     . LEU C 1 11  ? 4.101   8.072   10.963  1.00 11.74 ?  11  LEU C O     1 
ATOM   2559  C  CB    . LEU C 1 11  ? 4.026   5.460   9.029   1.00 19.77 ?  11  LEU C CB    1 
ATOM   2560  C  CG    . LEU C 1 11  ? 3.314   4.111   9.185   1.00 22.10 ?  11  LEU C CG    1 
ATOM   2561  C  CD1   . LEU C 1 11  ? 2.742   3.970   10.588  1.00 24.42 ?  11  LEU C CD1   1 
ATOM   2562  C  CD2   . LEU C 1 11  ? 2.225   3.918   8.144   1.00 23.52 ?  11  LEU C CD2   1 
ATOM   2563  N  N     . GLN C 1 12  ? 4.585   8.666   8.842   1.00 16.01 ?  12  GLN C N     1 
ATOM   2564  C  CA    . GLN C 1 12  ? 5.460   9.767   9.221   1.00 20.46 ?  12  GLN C CA    1 
ATOM   2565  C  C     . GLN C 1 12  ? 4.647   11.035  9.470   1.00 19.17 ?  12  GLN C C     1 
ATOM   2566  O  O     . GLN C 1 12  ? 3.621   11.266  8.835   1.00 20.70 ?  12  GLN C O     1 
ATOM   2567  C  CB    . GLN C 1 12  ? 6.516   10.081  8.159   1.00 20.85 ?  12  GLN C CB    1 
ATOM   2568  C  CG    . GLN C 1 12  ? 7.837   9.335   8.325   1.00 24.10 ?  12  GLN C CG    1 
ATOM   2569  C  CD    . GLN C 1 12  ? 8.725   9.917   9.405   1.00 23.83 ?  12  GLN C CD    1 
ATOM   2570  O  OE1   . GLN C 1 12  ? 8.269   10.634  10.301  1.00 19.35 ?  12  GLN C OE1   1 
ATOM   2571  N  NE2   . GLN C 1 12  ? 10.010  9.601   9.336   1.00 26.31 ?  12  GLN C NE2   1 
ATOM   2572  N  N     . LEU C 1 13  ? 5.162   11.862  10.382  1.00 18.61 ?  13  LEU C N     1 
ATOM   2573  C  CA    . LEU C 1 13  ? 4.526   13.095  10.816  1.00 16.45 ?  13  LEU C CA    1 
ATOM   2574  C  C     . LEU C 1 13  ? 4.323   14.060  9.650   1.00 15.56 ?  13  LEU C C     1 
ATOM   2575  O  O     . LEU C 1 13  ? 5.280   14.470  8.994   1.00 14.90 ?  13  LEU C O     1 
ATOM   2576  C  CB    . LEU C 1 13  ? 5.465   13.661  11.880  1.00 15.05 ?  13  LEU C CB    1 
ATOM   2577  C  CG    . LEU C 1 13  ? 5.060   14.971  12.559  1.00 12.77 ?  13  LEU C CG    1 
ATOM   2578  C  CD1   . LEU C 1 13  ? 3.737   14.868  13.290  1.00 12.85 ?  13  LEU C CD1   1 
ATOM   2579  C  CD2   . LEU C 1 13  ? 6.175   15.351  13.516  1.00 11.92 ?  13  LEU C CD2   1 
ATOM   2580  N  N     . ALA C 1 14  ? 3.052   14.394  9.398   1.00 14.93 ?  14  ALA C N     1 
ATOM   2581  C  CA    . ALA C 1 14  ? 2.678   15.592  8.661   1.00 15.74 ?  14  ALA C CA    1 
ATOM   2582  C  C     . ALA C 1 14  ? 2.852   15.402  7.154   1.00 18.10 ?  14  ALA C C     1 
ATOM   2583  O  O     . ALA C 1 14  ? 1.960   15.752  6.383   1.00 20.10 ?  14  ALA C O     1 
ATOM   2584  C  CB    . ALA C 1 14  ? 3.477   16.774  9.176   1.00 15.73 ?  14  ALA C CB    1 
ATOM   2585  N  N     . GLY C 1 15  ? 3.993   14.836  6.741   1.00 16.56 ?  15  GLY C N     1 
ATOM   2586  C  CA    . GLY C 1 15  ? 4.415   14.877  5.349   1.00 15.05 ?  15  GLY C CA    1 
ATOM   2587  C  C     . GLY C 1 15  ? 3.984   13.655  4.536   1.00 15.19 ?  15  GLY C C     1 
ATOM   2588  O  O     . GLY C 1 15  ? 4.108   13.664  3.314   1.00 13.44 ?  15  GLY C O     1 
ATOM   2589  N  N     . GLN C 1 16  ? 3.480   12.608  5.200   1.00 14.79 ?  16  GLN C N     1 
ATOM   2590  C  CA    . GLN C 1 16  ? 3.203   11.354  4.514   1.00 14.94 ?  16  GLN C CA    1 
ATOM   2591  C  C     . GLN C 1 16  ? 1.718   11.221  4.179   1.00 14.32 ?  16  GLN C C     1 
ATOM   2592  O  O     . GLN C 1 16  ? 1.298   10.202  3.634   1.00 13.76 ?  16  GLN C O     1 
ATOM   2593  C  CB    . GLN C 1 16  ? 3.651   10.137  5.323   1.00 13.92 ?  16  GLN C CB    1 
ATOM   2594  C  CG    . GLN C 1 16  ? 3.725   8.864   4.487   1.00 16.09 ?  16  GLN C CG    1 
ATOM   2595  C  CD    . GLN C 1 16  ? 4.723   7.855   5.012   1.00 16.37 ?  16  GLN C CD    1 
ATOM   2596  O  OE1   . GLN C 1 16  ? 4.463   7.126   5.976   1.00 18.37 ?  16  GLN C OE1   1 
ATOM   2597  N  NE2   . GLN C 1 16  ? 5.874   7.791   4.360   1.00 13.23 ?  16  GLN C NE2   1 
ATOM   2598  N  N     . ILE C 1 17  ? 0.928   12.251  4.497   1.00 13.13 ?  17  ILE C N     1 
ATOM   2599  C  CA    . ILE C 1 17  ? -0.480  12.261  4.131   1.00 14.13 ?  17  ILE C CA    1 
ATOM   2600  C  C     . ILE C 1 17  ? -0.610  12.756  2.691   1.00 11.40 ?  17  ILE C C     1 
ATOM   2601  O  O     . ILE C 1 17  ? 0.171   13.594  2.248   1.00 10.47 ?  17  ILE C O     1 
ATOM   2602  C  CB    . ILE C 1 17  ? -1.301  13.119  5.112   1.00 16.38 ?  17  ILE C CB    1 
ATOM   2603  C  CG1   . ILE C 1 17  ? -2.806  12.927  4.901   1.00 18.27 ?  17  ILE C CG1   1 
ATOM   2604  C  CG2   . ILE C 1 17  ? -0.897  14.591  5.024   1.00 16.29 ?  17  ILE C CG2   1 
ATOM   2605  C  CD1   . ILE C 1 17  ? -3.676  13.695  5.880   1.00 19.23 ?  17  ILE C CD1   1 
ATOM   2606  N  N     . SER C 1 18  ? -1.598  12.221  1.963   1.00 10.99 ?  18  SER C N     1 
ATOM   2607  C  CA    . SER C 1 18  ? -1.868  12.643  0.597   1.00 11.79 ?  18  SER C CA    1 
ATOM   2608  C  C     . SER C 1 18  ? -2.418  14.067  0.602   1.00 12.59 ?  18  SER C C     1 
ATOM   2609  O  O     . SER C 1 18  ? -2.969  14.516  1.603   1.00 12.72 ?  18  SER C O     1 
ATOM   2610  C  CB    . SER C 1 18  ? -2.816  11.697  -0.096  1.00 11.15 ?  18  SER C CB    1 
ATOM   2611  O  OG    . SER C 1 18  ? -4.084  11.680  0.545   1.00 10.60 ?  18  SER C OG    1 
ATOM   2612  N  N     . VAL C 1 19  ? -2.263  14.772  -0.523  1.00 15.08 ?  19  VAL C N     1 
ATOM   2613  C  CA    . VAL C 1 19  ? -2.652  16.171  -0.601  1.00 19.42 ?  19  VAL C CA    1 
ATOM   2614  C  C     . VAL C 1 19  ? -4.164  16.271  -0.412  1.00 20.04 ?  19  VAL C C     1 
ATOM   2615  O  O     . VAL C 1 19  ? -4.634  17.068  0.397   1.00 20.56 ?  19  VAL C O     1 
ATOM   2616  C  CB    . VAL C 1 19  ? -2.193  16.848  -1.908  1.00 19.49 ?  19  VAL C CB    1 
ATOM   2617  C  CG1   . VAL C 1 19  ? -2.851  18.208  -2.109  1.00 20.71 ?  19  VAL C CG1   1 
ATOM   2618  C  CG2   . VAL C 1 19  ? -0.676  16.985  -1.960  1.00 18.56 ?  19  VAL C CG2   1 
ATOM   2619  N  N     . LEU C 1 20  ? -4.913  15.438  -1.143  1.00 21.26 ?  20  LEU C N     1 
ATOM   2620  C  CA    . LEU C 1 20  ? -6.365  15.437  -1.058  1.00 23.73 ?  20  LEU C CA    1 
ATOM   2621  C  C     . LEU C 1 20  ? -6.797  15.167  0.382   1.00 22.71 ?  20  LEU C C     1 
ATOM   2622  O  O     . LEU C 1 20  ? -7.684  15.841  0.901   1.00 22.86 ?  20  LEU C O     1 
ATOM   2623  C  CB    . LEU C 1 20  ? -6.975  14.407  -2.009  1.00 23.78 ?  20  LEU C CB    1 
ATOM   2624  C  CG    . LEU C 1 20  ? -8.505  14.318  -1.998  1.00 25.72 ?  20  LEU C CG    1 
ATOM   2625  C  CD1   . LEU C 1 20  ? -9.141  15.631  -2.427  1.00 25.40 ?  20  LEU C CD1   1 
ATOM   2626  C  CD2   . LEU C 1 20  ? -9.004  13.180  -2.873  1.00 23.71 ?  20  LEU C CD2   1 
ATOM   2627  N  N     . SER C 1 21  ? -6.160  14.175  1.016   1.00 20.35 ?  21  SER C N     1 
ATOM   2628  C  CA    . SER C 1 21  ? -6.608  13.662  2.302   1.00 17.61 ?  21  SER C CA    1 
ATOM   2629  C  C     . SER C 1 21  ? -6.442  14.718  3.387   1.00 15.66 ?  21  SER C C     1 
ATOM   2630  O  O     . SER C 1 21  ? -7.188  14.734  4.363   1.00 15.61 ?  21  SER C O     1 
ATOM   2631  C  CB    . SER C 1 21  ? -5.873  12.401  2.674   1.00 15.91 ?  21  SER C CB    1 
ATOM   2632  O  OG    . SER C 1 21  ? -6.167  11.352  1.765   1.00 15.50 ?  21  SER C OG    1 
ATOM   2633  N  N     . ARG C 1 22  ? -5.434  15.576  3.212   1.00 13.86 ?  22  ARG C N     1 
ATOM   2634  C  CA    . ARG C 1 22  ? -5.168  16.652  4.148   1.00 14.57 ?  22  ARG C CA    1 
ATOM   2635  C  C     . ARG C 1 22  ? -6.235  17.729  3.981   1.00 14.53 ?  22  ARG C C     1 
ATOM   2636  O  O     . ARG C 1 22  ? -6.708  18.303  4.959   1.00 12.73 ?  22  ARG C O     1 
ATOM   2637  C  CB    . ARG C 1 22  ? -3.763  17.204  3.891   1.00 16.78 ?  22  ARG C CB    1 
ATOM   2638  C  CG    . ARG C 1 22  ? -3.349  18.303  4.858   1.00 17.31 ?  22  ARG C CG    1 
ATOM   2639  C  CD    . ARG C 1 22  ? -2.070  18.979  4.402   1.00 20.25 ?  22  ARG C CD    1 
ATOM   2640  N  NE    . ARG C 1 22  ? -1.531  19.893  5.414   1.00 21.14 ?  22  ARG C NE    1 
ATOM   2641  C  CZ    . ARG C 1 22  ? -1.482  21.213  5.295   1.00 24.10 ?  22  ARG C CZ    1 
ATOM   2642  N  NH1   . ARG C 1 22  ? -2.030  21.808  4.249   1.00 21.85 1  22  ARG C NH1   1 
ATOM   2643  N  NH2   . ARG C 1 22  ? -0.900  21.935  6.235   1.00 27.28 ?  22  ARG C NH2   1 
ATOM   2644  N  N     . SER C 1 23  ? -6.608  17.986  2.724   1.00 15.57 ?  23  SER C N     1 
ATOM   2645  C  CA    . SER C 1 23  ? -7.606  18.988  2.398   1.00 18.47 ?  23  SER C CA    1 
ATOM   2646  C  C     . SER C 1 23  ? -8.972  18.589  2.958   1.00 18.87 ?  23  SER C C     1 
ATOM   2647  O  O     . SER C 1 23  ? -9.825  19.447  3.171   1.00 24.53 ?  23  SER C O     1 
ATOM   2648  C  CB    . SER C 1 23  ? -7.660  19.219  0.908   1.00 18.05 ?  23  SER C CB    1 
ATOM   2649  O  OG    . SER C 1 23  ? -8.668  20.160  0.568   1.00 16.65 ?  23  SER C OG    1 
ATOM   2650  N  N     . TYR C 1 24  ? -9.172  17.287  3.199   1.00 20.11 ?  24  TYR C N     1 
ATOM   2651  C  CA    . TYR C 1 24  ? -10.425 16.784  3.746   1.00 19.42 ?  24  TYR C CA    1 
ATOM   2652  C  C     . TYR C 1 24  ? -10.479 17.036  5.251   1.00 17.25 ?  24  TYR C C     1 
ATOM   2653  O  O     . TYR C 1 24  ? -11.531 17.365  5.792   1.00 17.72 ?  24  TYR C O     1 
ATOM   2654  C  CB    . TYR C 1 24  ? -10.614 15.293  3.450   1.00 20.90 ?  24  TYR C CB    1 
ATOM   2655  C  CG    . TYR C 1 24  ? -11.443 14.998  2.207   1.00 25.46 ?  24  TYR C CG    1 
ATOM   2656  C  CD1   . TYR C 1 24  ? -12.806 15.265  2.184   1.00 22.45 ?  24  TYR C CD1   1 
ATOM   2657  C  CD2   . TYR C 1 24  ? -10.875 14.431  1.073   1.00 30.34 ?  24  TYR C CD2   1 
ATOM   2658  C  CE1   . TYR C 1 24  ? -13.576 14.997  1.065   1.00 26.35 ?  24  TYR C CE1   1 
ATOM   2659  C  CE2   . TYR C 1 24  ? -11.635 14.155  -0.052  1.00 30.75 ?  24  TYR C CE2   1 
ATOM   2660  C  CZ    . TYR C 1 24  ? -12.989 14.439  -0.056  1.00 30.98 ?  24  TYR C CZ    1 
ATOM   2661  O  OH    . TYR C 1 24  ? -13.746 14.173  -1.161  1.00 31.03 ?  24  TYR C OH    1 
ATOM   2662  N  N     . ILE C 1 25  ? -9.342  16.836  5.922   1.00 17.46 ?  25  ILE C N     1 
ATOM   2663  C  CA    . ILE C 1 25  ? -9.210  17.136  7.338   1.00 20.36 ?  25  ILE C CA    1 
ATOM   2664  C  C     . ILE C 1 25  ? -9.460  18.627  7.554   1.00 21.37 ?  25  ILE C C     1 
ATOM   2665  O  O     . ILE C 1 25  ? -10.159 19.017  8.485   1.00 20.86 ?  25  ILE C O     1 
ATOM   2666  C  CB    . ILE C 1 25  ? -7.821  16.705  7.849   1.00 20.42 ?  25  ILE C CB    1 
ATOM   2667  C  CG1   . ILE C 1 25  ? -7.690  15.183  7.905   1.00 20.21 ?  25  ILE C CG1   1 
ATOM   2668  C  CG2   . ILE C 1 25  ? -7.502  17.343  9.201   1.00 19.96 ?  25  ILE C CG2   1 
ATOM   2669  C  CD1   . ILE C 1 25  ? -6.308  14.698  8.304   1.00 20.01 ?  25  ILE C CD1   1 
ATOM   2670  N  N     . GLU C 1 26  ? -8.884  19.447  6.669   1.00 22.75 ?  26  GLU C N     1 
ATOM   2671  C  CA    . GLU C 1 26  ? -8.909  20.896  6.795   1.00 25.44 ?  26  GLU C CA    1 
ATOM   2672  C  C     . GLU C 1 26  ? -10.331 21.440  6.639   1.00 24.75 ?  26  GLU C C     1 
ATOM   2673  O  O     . GLU C 1 26  ? -10.673 22.438  7.268   1.00 27.28 ?  26  GLU C O     1 
ATOM   2674  C  CB    . GLU C 1 26  ? -7.929  21.470  5.769   1.00 26.46 ?  26  GLU C CB    1 
ATOM   2675  C  CG    . GLU C 1 26  ? -7.919  22.993  5.676   1.00 29.23 ?  26  GLU C CG    1 
ATOM   2676  C  CD    . GLU C 1 26  ? -7.021  23.499  4.559   1.00 33.59 ?  26  GLU C CD    1 
ATOM   2677  O  OE1   . GLU C 1 26  ? -6.492  22.649  3.810   1.00 32.56 ?  26  GLU C OE1   1 
ATOM   2678  O  OE2   . GLU C 1 26  ? -6.843  24.730  4.438   1.00 35.76 -1 26  GLU C OE2   1 
ATOM   2679  N  N     . HIS C 1 27  ? -11.160 20.792  5.808   1.00 23.27 ?  27  HIS C N     1 
ATOM   2680  C  CA    . HIS C 1 27  ? -12.490 21.309  5.517   1.00 20.63 ?  27  HIS C CA    1 
ATOM   2681  C  C     . HIS C 1 27  ? -13.585 20.540  6.256   1.00 17.28 ?  27  HIS C C     1 
ATOM   2682  O  O     . HIS C 1 27  ? -14.762 20.858  6.099   1.00 13.02 ?  27  HIS C O     1 
ATOM   2683  C  CB    . HIS C 1 27  ? -12.763 21.336  4.009   1.00 22.64 ?  27  HIS C CB    1 
ATOM   2684  C  CG    . HIS C 1 27  ? -11.997 22.405  3.307   1.00 22.16 ?  27  HIS C CG    1 
ATOM   2685  N  ND1   . HIS C 1 27  ? -10.946 22.151  2.453   1.00 21.09 ?  27  HIS C ND1   1 
ATOM   2686  C  CD2   . HIS C 1 27  ? -12.139 23.736  3.338   1.00 22.39 ?  27  HIS C CD2   1 
ATOM   2687  C  CE1   . HIS C 1 27  ? -10.471 23.301  1.994   1.00 21.26 ?  27  HIS C CE1   1 
ATOM   2688  N  NE2   . HIS C 1 27  ? -11.180 24.277  2.520   1.00 22.99 ?  27  HIS C NE2   1 
ATOM   2689  N  N     . ALA C 1 28  ? -13.205 19.542  7.063   1.00 14.20 ?  28  ALA C N     1 
ATOM   2690  C  CA    . ALA C 1 28  ? -14.175 18.790  7.846   1.00 12.79 ?  28  ALA C CA    1 
ATOM   2691  C  C     . ALA C 1 28  ? -14.872 19.701  8.855   1.00 12.24 ?  28  ALA C C     1 
ATOM   2692  O  O     . ALA C 1 28  ? -14.320 20.718  9.267   1.00 11.97 ?  28  ALA C O     1 
ATOM   2693  C  CB    . ALA C 1 28  ? -13.503 17.634  8.556   1.00 11.92 ?  28  ALA C CB    1 
ATOM   2694  N  N     . ASP C 1 29  ? -16.082 19.292  9.260   1.00 12.91 ?  29  ASP C N     1 
ATOM   2695  C  CA    . ASP C 1 29  ? -16.799 19.902  10.369  1.00 14.93 ?  29  ASP C CA    1 
ATOM   2696  C  C     . ASP C 1 29  ? -16.230 19.374  11.682  1.00 16.04 ?  29  ASP C C     1 
ATOM   2697  O  O     . ASP C 1 29  ? -16.133 20.105  12.665  1.00 16.38 ?  29  ASP C O     1 
ATOM   2698  C  CB    . ASP C 1 29  ? -18.285 19.580  10.322  1.00 14.06 ?  29  ASP C CB    1 
ATOM   2699  C  CG    . ASP C 1 29  ? -19.091 20.289  9.243   1.00 15.30 ?  29  ASP C CG    1 
ATOM   2700  O  OD1   . ASP C 1 29  ? -18.600 21.306  8.713   1.00 15.91 ?  29  ASP C OD1   1 
ATOM   2701  O  OD2   . ASP C 1 29  ? -20.202 19.809  8.934   1.00 16.25 -1 29  ASP C OD2   1 
ATOM   2702  N  N     . ILE C 1 30  ? -15.875 18.086  11.683  1.00 17.29 ?  30  ILE C N     1 
ATOM   2703  C  CA    . ILE C 1 30  ? -15.352 17.430  12.868  1.00 17.37 ?  30  ILE C CA    1 
ATOM   2704  C  C     . ILE C 1 30  ? -14.398 16.330  12.420  1.00 17.45 ?  30  ILE C C     1 
ATOM   2705  O  O     . ILE C 1 30  ? -14.561 15.763  11.340  1.00 14.12 ?  30  ILE C O     1 
ATOM   2706  C  CB    . ILE C 1 30  ? -16.495 16.883  13.745  1.00 18.94 ?  30  ILE C CB    1 
ATOM   2707  C  CG1   . ILE C 1 30  ? -15.996 16.388  15.102  1.00 19.38 ?  30  ILE C CG1   1 
ATOM   2708  C  CG2   . ILE C 1 30  ? -17.285 15.800  13.010  1.00 17.29 ?  30  ILE C CG2   1 
ATOM   2709  C  CD1   . ILE C 1 30  ? -17.107 15.944  16.036  1.00 21.05 ?  30  ILE C CD1   1 
ATOM   2710  N  N     . VAL C 1 31  ? -13.399 16.047  13.260  1.00 17.29 ?  31  VAL C N     1 
ATOM   2711  C  CA    . VAL C 1 31  ? -12.407 15.038  12.941  1.00 18.25 ?  31  VAL C CA    1 
ATOM   2712  C  C     . VAL C 1 31  ? -12.252 14.102  14.133  1.00 19.97 ?  31  VAL C C     1 
ATOM   2713  O  O     . VAL C 1 31  ? -12.097 14.540  15.272  1.00 19.69 ?  31  VAL C O     1 
ATOM   2714  C  CB    . VAL C 1 31  ? -11.057 15.660  12.538  1.00 17.49 ?  31  VAL C CB    1 
ATOM   2715  C  CG1   . VAL C 1 31  ? -10.051 14.595  12.112  1.00 16.71 ?  31  VAL C CG1   1 
ATOM   2716  C  CG2   . VAL C 1 31  ? -11.232 16.702  11.441  1.00 14.28 ?  31  VAL C CG2   1 
ATOM   2717  N  N     . PHE C 1 32  ? -12.316 12.802  13.839  1.00 18.99 ?  32  PHE C N     1 
ATOM   2718  C  CA    . PHE C 1 32  ? -12.024 11.769  14.815  1.00 19.77 ?  32  PHE C CA    1 
ATOM   2719  C  C     . PHE C 1 32  ? -10.643 11.205  14.500  1.00 18.77 ?  32  PHE C C     1 
ATOM   2720  O  O     . PHE C 1 32  ? -10.434 10.599  13.451  1.00 18.29 ?  32  PHE C O     1 
ATOM   2721  C  CB    . PHE C 1 32  ? -13.123 10.702  14.801  1.00 20.00 ?  32  PHE C CB    1 
ATOM   2722  C  CG    . PHE C 1 32  ? -14.490 11.212  15.238  1.00 21.95 ?  32  PHE C CG    1 
ATOM   2723  C  CD1   . PHE C 1 32  ? -15.312 11.898  14.350  1.00 22.85 ?  32  PHE C CD1   1 
ATOM   2724  C  CD2   . PHE C 1 32  ? -14.954 10.998  16.532  1.00 22.80 ?  32  PHE C CD2   1 
ATOM   2725  C  CE1   . PHE C 1 32  ? -16.557 12.359  14.748  1.00 24.29 ?  32  PHE C CE1   1 
ATOM   2726  C  CE2   . PHE C 1 32  ? -16.200 11.461  16.924  1.00 22.89 ?  32  PHE C CE2   1 
ATOM   2727  C  CZ    . PHE C 1 32  ? -16.998 12.141  16.033  1.00 24.29 ?  32  PHE C CZ    1 
ATOM   2728  N  N     . SER C 1 33  ? -9.709  11.434  15.426  1.00 17.96 ?  33  SER C N     1 
ATOM   2729  C  CA    . SER C 1 33  ? -8.306  11.114  15.228  1.00 18.24 ?  33  SER C CA    1 
ATOM   2730  C  C     . SER C 1 33  ? -7.978  9.748   15.830  1.00 21.25 ?  33  SER C C     1 
ATOM   2731  O  O     . SER C 1 33  ? -8.680  9.273   16.720  1.00 24.19 ?  33  SER C O     1 
ATOM   2732  C  CB    . SER C 1 33  ? -7.443  12.198  15.826  1.00 15.06 ?  33  SER C CB    1 
ATOM   2733  O  OG    . SER C 1 33  ? -7.703  12.344  17.216  1.00 12.74 ?  33  SER C OG    1 
ATOM   2734  N  N     . LEU C 1 34  ? -6.909  9.124   15.320  1.00 25.80 ?  34  LEU C N     1 
ATOM   2735  C  CA    . LEU C 1 34  ? -6.325  7.928   15.913  1.00 29.05 ?  34  LEU C CA    1 
ATOM   2736  C  C     . LEU C 1 34  ? -4.888  7.827   15.405  1.00 28.90 ?  34  LEU C C     1 
ATOM   2737  O  O     . LEU C 1 34  ? -4.586  7.042   14.508  1.00 32.94 ?  34  LEU C O     1 
ATOM   2738  C  CB    . LEU C 1 34  ? -7.132  6.665   15.604  1.00 30.14 ?  34  LEU C CB    1 
ATOM   2739  C  CG    . LEU C 1 34  ? -6.993  5.509   16.604  1.00 34.45 ?  34  LEU C CG    1 
ATOM   2740  C  CD1   . LEU C 1 34  ? -7.101  5.985   18.044  1.00 30.83 ?  34  LEU C CD1   1 
ATOM   2741  C  CD2   . LEU C 1 34  ? -8.038  4.434   16.343  1.00 36.92 ?  34  LEU C CD2   1 
ATOM   2742  N  N     . LEU C 1 35  ? -4.018  8.655   15.991  1.00 26.11 ?  35  LEU C N     1 
ATOM   2743  C  CA    . LEU C 1 35  ? -2.681  8.903   15.478  1.00 29.83 ?  35  LEU C CA    1 
ATOM   2744  C  C     . LEU C 1 35  ? -1.645  8.268   16.404  1.00 31.19 ?  35  LEU C C     1 
ATOM   2745  O  O     . LEU C 1 35  ? -1.935  8.023   17.572  1.00 31.85 ?  35  LEU C O     1 
ATOM   2746  C  CB    . LEU C 1 35  ? -2.550  10.422  15.397  1.00 29.55 ?  35  LEU C CB    1 
ATOM   2747  C  CG    . LEU C 1 35  ? -3.640  11.126  14.580  1.00 31.63 ?  35  LEU C CG    1 
ATOM   2748  C  CD1   . LEU C 1 35  ? -3.502  12.636  14.638  1.00 28.81 ?  35  LEU C CD1   1 
ATOM   2749  C  CD2   . LEU C 1 35  ? -3.618  10.636  13.140  1.00 31.18 ?  35  LEU C CD2   1 
ATOM   2750  N  N     . PRO C 1 36  ? -0.413  7.968   15.927  1.00 31.88 ?  36  PRO C N     1 
ATOM   2751  C  CA    . PRO C 1 36  ? 0.557   7.233   16.742  1.00 33.10 ?  36  PRO C CA    1 
ATOM   2752  C  C     . PRO C 1 36  ? 1.183   8.002   17.908  1.00 34.09 ?  36  PRO C C     1 
ATOM   2753  O  O     . PRO C 1 36  ? 1.709   7.382   18.830  1.00 34.57 ?  36  PRO C O     1 
ATOM   2754  C  CB    . PRO C 1 36  ? 1.630   6.767   15.724  1.00 31.03 ?  36  PRO C CB    1 
ATOM   2755  C  CG    . PRO C 1 36  ? 1.073   7.119   14.354  1.00 31.91 ?  36  PRO C CG    1 
ATOM   2756  C  CD    . PRO C 1 36  ? 0.088   8.257   14.575  1.00 35.64 ?  36  PRO C CD    1 
ATOM   2757  N  N     . ASP C 1 37  ? 1.133   9.340   17.880  1.00 33.01 ?  37  ASP C N     1 
ATOM   2758  C  CA    . ASP C 1 37  ? 1.785   10.122  18.921  1.00 32.55 ?  37  ASP C CA    1 
ATOM   2759  C  C     . ASP C 1 37  ? 1.119   11.481  19.117  1.00 31.72 ?  37  ASP C C     1 
ATOM   2760  O  O     . ASP C 1 37  ? 0.139   11.813  18.454  1.00 33.87 ?  37  ASP C O     1 
ATOM   2761  C  CB    . ASP C 1 37  ? 3.263   10.326  18.629  1.00 34.01 ?  37  ASP C CB    1 
ATOM   2762  C  CG    . ASP C 1 37  ? 3.591   10.781  17.214  1.00 33.19 ?  37  ASP C CG    1 
ATOM   2763  O  OD1   . ASP C 1 37  ? 3.098   11.857  16.815  1.00 37.10 ?  37  ASP C OD1   1 
ATOM   2764  O  OD2   . ASP C 1 37  ? 4.337   10.054  16.525  1.00 28.77 -1 37  ASP C OD2   1 
ATOM   2765  N  N     . GLY C 1 38  ? 1.695   12.256  20.044  1.00 31.33 ?  38  GLY C N     1 
ATOM   2766  C  CA    . GLY C 1 38  ? 1.193   13.570  20.407  1.00 30.02 ?  38  GLY C CA    1 
ATOM   2767  C  C     . GLY C 1 38  ? 1.700   14.656  19.461  1.00 30.11 ?  38  GLY C C     1 
ATOM   2768  O  O     . GLY C 1 38  ? 1.192   15.776  19.479  1.00 24.29 ?  38  GLY C O     1 
ATOM   2769  N  N     . PHE C 1 39  ? 2.705   14.322  18.643  1.00 26.34 ?  39  PHE C N     1 
ATOM   2770  C  CA    . PHE C 1 39  ? 3.272   15.275  17.701  1.00 25.33 ?  39  PHE C CA    1 
ATOM   2771  C  C     . PHE C 1 39  ? 2.348   15.387  16.492  1.00 26.55 ?  39  PHE C C     1 
ATOM   2772  O  O     . PHE C 1 39  ? 2.153   16.469  15.941  1.00 30.14 ?  39  PHE C O     1 
ATOM   2773  C  CB    . PHE C 1 39  ? 4.675   14.864  17.243  1.00 24.87 ?  39  PHE C CB    1 
ATOM   2774  C  CG    . PHE C 1 39  ? 5.783   15.032  18.274  1.00 23.31 ?  39  PHE C CG    1 
ATOM   2775  C  CD1   . PHE C 1 39  ? 6.374   16.272  18.491  1.00 24.35 ?  39  PHE C CD1   1 
ATOM   2776  C  CD2   . PHE C 1 39  ? 6.250   13.944  19.002  1.00 23.68 ?  39  PHE C CD2   1 
ATOM   2777  C  CE1   . PHE C 1 39  ? 7.389   16.419  19.424  1.00 22.74 ?  39  PHE C CE1   1 
ATOM   2778  C  CE2   . PHE C 1 39  ? 7.267   14.097  19.931  1.00 23.44 ?  39  PHE C CE2   1 
ATOM   2779  C  CZ    . PHE C 1 39  ? 7.834   15.331  20.139  1.00 23.50 ?  39  PHE C CZ    1 
ATOM   2780  N  N     . SER C 1 40  ? 1.797   14.238  16.094  1.00 26.09 ?  40  SER C N     1 
ATOM   2781  C  CA    . SER C 1 40  ? 0.885   14.134  14.969  1.00 29.15 ?  40  SER C CA    1 
ATOM   2782  C  C     . SER C 1 40  ? -0.498  14.618  15.389  1.00 24.35 ?  40  SER C C     1 
ATOM   2783  O  O     . SER C 1 40  ? -1.284  15.076  14.564  1.00 28.44 ?  40  SER C O     1 
ATOM   2784  C  CB    . SER C 1 40  ? 0.831   12.711  14.463  1.00 25.35 ?  40  SER C CB    1 
ATOM   2785  O  OG    . SER C 1 40  ? -0.072  12.579  13.374  1.00 29.53 ?  40  SER C OG    1 
ATOM   2786  N  N     . GLN C 1 41  ? -0.777  14.490  16.689  1.00 24.04 ?  41  GLN C N     1 
ATOM   2787  C  CA    . GLN C 1 41  ? -2.043  14.912  17.262  1.00 25.84 ?  41  GLN C CA    1 
ATOM   2788  C  C     . GLN C 1 41  ? -2.070  16.439  17.329  1.00 24.47 ?  41  GLN C C     1 
ATOM   2789  O  O     . GLN C 1 41  ? -3.112  17.051  17.109  1.00 25.00 ?  41  GLN C O     1 
ATOM   2790  C  CB    . GLN C 1 41  ? -2.218  14.245  18.627  1.00 28.17 ?  41  GLN C CB    1 
ATOM   2791  C  CG    . GLN C 1 41  ? -3.646  14.266  19.161  1.00 33.74 ?  41  GLN C CG    1 
ATOM   2792  C  CD    . GLN C 1 41  ? -4.553  13.257  18.491  1.00 34.41 ?  41  GLN C CD    1 
ATOM   2793  O  OE1   . GLN C 1 41  ? -4.235  12.066  18.401  1.00 42.38 ?  41  GLN C OE1   1 
ATOM   2794  N  NE2   . GLN C 1 41  ? -5.700  13.723  18.018  1.00 29.27 ?  41  GLN C NE2   1 
ATOM   2795  N  N     . ARG C 1 42  ? -0.913  17.044  17.630  1.00 21.44 ?  42  ARG C N     1 
ATOM   2796  C  CA    . ARG C 1 42  ? -0.777  18.493  17.619  1.00 21.61 ?  42  ARG C CA    1 
ATOM   2797  C  C     . ARG C 1 42  ? -0.942  19.014  16.195  1.00 22.72 ?  42  ARG C C     1 
ATOM   2798  O  O     . ARG C 1 42  ? -1.808  19.844  15.930  1.00 26.72 ?  42  ARG C O     1 
ATOM   2799  C  CB    . ARG C 1 42  ? 0.581   18.968  18.147  1.00 19.52 ?  42  ARG C CB    1 
ATOM   2800  C  CG    . ARG C 1 42  ? 0.738   18.845  19.653  1.00 20.77 ?  42  ARG C CG    1 
ATOM   2801  C  CD    . ARG C 1 42  ? 2.016   19.509  20.129  1.00 23.59 ?  42  ARG C CD    1 
ATOM   2802  N  NE    . ARG C 1 42  ? 2.134   19.429  21.589  1.00 27.88 ?  42  ARG C NE    1 
ATOM   2803  C  CZ    . ARG C 1 42  ? 2.117   20.462  22.423  1.00 32.84 ?  42  ARG C CZ    1 
ATOM   2804  N  NH1   . ARG C 1 42  ? 2.027   21.696  21.959  1.00 38.82 1  42  ARG C NH1   1 
ATOM   2805  N  NH2   . ARG C 1 42  ? 2.195   20.251  23.724  1.00 33.95 ?  42  ARG C NH2   1 
ATOM   2806  N  N     . TRP C 1 43  ? -0.081  18.536  15.289  1.00 21.30 ?  43  TRP C N     1 
ATOM   2807  C  CA    . TRP C 1 43  ? -0.193  18.876  13.881  1.00 17.76 ?  43  TRP C CA    1 
ATOM   2808  C  C     . TRP C 1 43  ? -1.661  18.849  13.461  1.00 18.85 ?  43  TRP C C     1 
ATOM   2809  O  O     . TRP C 1 43  ? -2.155  19.805  12.869  1.00 16.70 ?  43  TRP C O     1 
ATOM   2810  C  CB    . TRP C 1 43  ? 0.656   17.920  13.032  1.00 14.26 ?  43  TRP C CB    1 
ATOM   2811  C  CG    . TRP C 1 43  ? 0.235   17.813  11.589  1.00 10.99 ?  43  TRP C CG    1 
ATOM   2812  C  CD1   . TRP C 1 43  ? 0.585   18.642  10.564  1.00 10.54 ?  43  TRP C CD1   1 
ATOM   2813  C  CD2   . TRP C 1 43  ? -0.593  16.783  11.006  1.00 10.47 ?  43  TRP C CD2   1 
ATOM   2814  N  NE1   . TRP C 1 43  ? 0.018   18.215  9.392   1.00 10.65 ?  43  TRP C NE1   1 
ATOM   2815  C  CE2   . TRP C 1 43  ? -0.704  17.075  9.629   1.00 10.53 ?  43  TRP C CE2   1 
ATOM   2816  C  CE3   . TRP C 1 43  ? -1.251  15.655  11.508  1.00 10.28 ?  43  TRP C CE3   1 
ATOM   2817  C  CZ2   . TRP C 1 43  ? -1.444  16.279  8.757   1.00 11.35 ?  43  TRP C CZ2   1 
ATOM   2818  C  CZ3   . TRP C 1 43  ? -1.979  14.867  10.644  1.00 10.53 ?  43  TRP C CZ3   1 
ATOM   2819  C  CH2   . TRP C 1 43  ? -2.071  15.175  9.288   1.00 10.74 ?  43  TRP C CH2   1 
ATOM   2820  N  N     . LEU C 1 44  ? -2.357  17.754  13.782  1.00 19.59 ?  44  LEU C N     1 
ATOM   2821  C  CA    . LEU C 1 44  ? -3.745  17.603  13.376  1.00 20.75 ?  44  LEU C CA    1 
ATOM   2822  C  C     . LEU C 1 44  ? -4.547  18.814  13.849  1.00 22.58 ?  44  LEU C C     1 
ATOM   2823  O  O     . LEU C 1 44  ? -5.260  19.436  13.065  1.00 18.56 ?  44  LEU C O     1 
ATOM   2824  C  CB    . LEU C 1 44  ? -4.341  16.299  13.905  1.00 21.41 ?  44  LEU C CB    1 
ATOM   2825  C  CG    . LEU C 1 44  ? -5.796  16.032  13.504  1.00 22.44 ?  44  LEU C CG    1 
ATOM   2826  C  CD1   . LEU C 1 44  ? -5.970  16.188  12.003  1.00 24.50 ?  44  LEU C CD1   1 
ATOM   2827  C  CD2   . LEU C 1 44  ? -6.265  14.659  13.948  1.00 20.67 ?  44  LEU C CD2   1 
ATOM   2828  N  N     . THR C 1 45  ? -4.407  19.143  15.138  1.00 22.00 ?  45  THR C N     1 
ATOM   2829  C  CA    . THR C 1 45  ? -5.214  20.169  15.779  1.00 25.97 ?  45  THR C CA    1 
ATOM   2830  C  C     . THR C 1 45  ? -4.981  21.525  15.112  1.00 26.31 ?  45  THR C C     1 
ATOM   2831  O  O     . THR C 1 45  ? -5.881  22.360  15.084  1.00 28.83 ?  45  THR C O     1 
ATOM   2832  C  CB    . THR C 1 45  ? -4.877  20.186  17.270  1.00 28.06 ?  45  THR C CB    1 
ATOM   2833  O  OG1   . THR C 1 45  ? -5.072  18.842  17.699  1.00 27.08 ?  45  THR C OG1   1 
ATOM   2834  C  CG2   . THR C 1 45  ? -5.760  21.128  18.069  1.00 29.14 ?  45  THR C CG2   1 
ATOM   2835  N  N     . LYS C 1 46  ? -3.773  21.740  14.577  1.00 27.93 ?  46  LYS C N     1 
ATOM   2836  C  CA    . LYS C 1 46  ? -3.448  22.975  13.880  1.00 30.01 ?  46  LYS C CA    1 
ATOM   2837  C  C     . LYS C 1 46  ? -4.091  22.969  12.493  1.00 27.60 ?  46  LYS C C     1 
ATOM   2838  O  O     . LYS C 1 46  ? -4.387  24.027  11.941  1.00 25.24 ?  46  LYS C O     1 
ATOM   2839  C  CB    . LYS C 1 46  ? -1.926  23.175  13.855  1.00 35.41 ?  46  LYS C CB    1 
ATOM   2840  C  CG    . LYS C 1 46  ? -1.314  23.377  15.240  1.00 39.36 ?  46  LYS C CG    1 
ATOM   2841  C  CD    . LYS C 1 46  ? 0.207   23.469  15.314  1.00 44.89 ?  46  LYS C CD    1 
ATOM   2842  C  CE    . LYS C 1 46  ? 0.752   24.842  15.071  1.00 49.13 ?  46  LYS C CE    1 
ATOM   2843  N  NZ    . LYS C 1 46  ? 0.685   25.235  13.661  1.00 53.47 1  46  LYS C NZ    1 
ATOM   2844  N  N     . LEU C 1 47  ? -4.312  21.770  11.939  1.00 24.06 ?  47  LEU C N     1 
ATOM   2845  C  CA    . LEU C 1 47  ? -5.048  21.617  10.692  1.00 24.59 ?  47  LEU C CA    1 
ATOM   2846  C  C     . LEU C 1 47  ? -6.518  21.970  10.902  1.00 23.35 ?  47  LEU C C     1 
ATOM   2847  O  O     . LEU C 1 47  ? -7.104  22.706  10.111  1.00 24.75 ?  47  LEU C O     1 
ATOM   2848  C  CB    . LEU C 1 47  ? -4.906  20.201  10.135  1.00 22.98 ?  47  LEU C CB    1 
ATOM   2849  C  CG    . LEU C 1 47  ? -4.065  20.081  8.862   1.00 24.31 ?  47  LEU C CG    1 
ATOM   2850  C  CD1   . LEU C 1 47  ? -3.973  18.656  8.346   1.00 22.63 ?  47  LEU C CD1   1 
ATOM   2851  C  CD2   . LEU C 1 47  ? -4.664  20.997  7.807   1.00 24.95 ?  47  LEU C CD2   1 
ATOM   2852  N  N     . ASN C 1 48  ? -7.108  21.414  11.963  1.00 21.19 ?  48  ASN C N     1 
ATOM   2853  C  CA    . ASN C 1 48  ? -8.526  21.579  12.228  1.00 20.99 ?  48  ASN C CA    1 
ATOM   2854  C  C     . ASN C 1 48  ? -8.764  21.298  13.708  1.00 21.64 ?  48  ASN C C     1 
ATOM   2855  O  O     . ASN C 1 48  ? -8.617  20.165  14.162  1.00 22.14 ?  48  ASN C O     1 
ATOM   2856  C  CB    . ASN C 1 48  ? -9.360  20.713  11.290  1.00 22.13 ?  48  ASN C CB    1 
ATOM   2857  C  CG    . ASN C 1 48  ? -10.833 20.740  11.624  1.00 22.47 ?  48  ASN C CG    1 
ATOM   2858  O  OD1   . ASN C 1 48  ? -11.221 21.197  12.706  1.00 17.50 ?  48  ASN C OD1   1 
ATOM   2859  N  ND2   . ASN C 1 48  ? -11.663 20.235  10.722  1.00 23.41 ?  48  ASN C ND2   1 
ATOM   2860  N  N     . PRO C 1 49  ? -9.131  22.329  14.501  1.00 23.52 ?  49  PRO C N     1 
ATOM   2861  C  CA    . PRO C 1 49  ? -9.181  22.202  15.958  1.00 21.86 ?  49  PRO C CA    1 
ATOM   2862  C  C     . PRO C 1 49  ? -10.347 21.375  16.496  1.00 23.31 ?  49  PRO C C     1 
ATOM   2863  O  O     . PRO C 1 49  ? -10.348 20.997  17.665  1.00 23.76 ?  49  PRO C O     1 
ATOM   2864  C  CB    . PRO C 1 49  ? -9.274  23.679  16.374  1.00 22.38 ?  49  PRO C CB    1 
ATOM   2865  C  CG    . PRO C 1 49  ? -10.116 24.291  15.281  1.00 23.73 ?  49  PRO C CG    1 
ATOM   2866  C  CD    . PRO C 1 49  ? -9.525  23.668  14.028  1.00 23.97 ?  49  PRO C CD    1 
ATOM   2867  N  N     . ASN C 1 50  ? -11.341 21.098  15.645  1.00 20.70 ?  50  ASN C N     1 
ATOM   2868  C  CA    . ASN C 1 50  ? -12.469 20.281  16.060  1.00 20.80 ?  50  ASN C CA    1 
ATOM   2869  C  C     . ASN C 1 50  ? -12.109 18.807  15.886  1.00 22.01 ?  50  ASN C C     1 
ATOM   2870  O  O     . ASN C 1 50  ? -12.422 18.210  14.859  1.00 21.41 ?  50  ASN C O     1 
ATOM   2871  C  CB    . ASN C 1 50  ? -13.743 20.635  15.301  1.00 20.40 ?  50  ASN C CB    1 
ATOM   2872  C  CG    . ASN C 1 50  ? -14.981 20.115  15.995  1.00 19.91 ?  50  ASN C CG    1 
ATOM   2873  O  OD1   . ASN C 1 50  ? -14.914 19.693  17.154  1.00 22.61 ?  50  ASN C OD1   1 
ATOM   2874  N  ND2   . ASN C 1 50  ? -16.117 20.154  15.315  1.00 19.48 ?  50  ASN C ND2   1 
ATOM   2875  N  N     . VAL C 1 51  ? -11.449 18.231  16.902  1.00 21.30 ?  51  VAL C N     1 
ATOM   2876  C  CA    . VAL C 1 51  ? -11.045 16.832  16.881  1.00 17.61 ?  51  VAL C CA    1 
ATOM   2877  C  C     . VAL C 1 51  ? -11.568 16.125  18.129  1.00 17.00 ?  51  VAL C C     1 
ATOM   2878  O  O     . VAL C 1 51  ? -11.401 16.623  19.240  1.00 18.19 ?  51  VAL C O     1 
ATOM   2879  C  CB    . VAL C 1 51  ? -9.514  16.661  16.814  1.00 18.44 ?  51  VAL C CB    1 
ATOM   2880  C  CG1   . VAL C 1 51  ? -9.112  15.189  16.857  1.00 19.06 ?  51  VAL C CG1   1 
ATOM   2881  C  CG2   . VAL C 1 51  ? -8.901  17.354  15.604  1.00 18.20 ?  51  VAL C CG2   1 
ATOM   2882  N  N     . ILE C 1 52  ? -12.166 14.942  17.935  1.00 19.29 ?  52  ILE C N     1 
ATOM   2883  C  CA    . ILE C 1 52  ? -12.385 13.997  19.021  1.00 22.54 ?  52  ILE C CA    1 
ATOM   2884  C  C     . ILE C 1 52  ? -11.440 12.810  18.849  1.00 24.59 ?  52  ILE C C     1 
ATOM   2885  O  O     . ILE C 1 52  ? -11.490 12.108  17.842  1.00 23.40 ?  52  ILE C O     1 
ATOM   2886  C  CB    . ILE C 1 52  ? -13.850 13.532  19.090  1.00 23.83 ?  52  ILE C CB    1 
ATOM   2887  C  CG1   . ILE C 1 52  ? -14.771 14.656  19.552  1.00 22.71 ?  52  ILE C CG1   1 
ATOM   2888  C  CG2   . ILE C 1 52  ? -13.982 12.295  19.981  1.00 22.19 ?  52  ILE C CG2   1 
ATOM   2889  C  CD1   . ILE C 1 52  ? -14.828 15.835  18.601  1.00 26.12 ?  52  ILE C CD1   1 
ATOM   2890  N  N     . ASN C 1 53  ? -10.604 12.586  19.869  1.00 26.20 ?  53  ASN C N     1 
ATOM   2891  C  CA    . ASN C 1 53  ? -9.573  11.559  19.850  1.00 25.38 ?  53  ASN C CA    1 
ATOM   2892  C  C     . ASN C 1 53  ? -10.158 10.207  20.268  1.00 22.23 ?  53  ASN C C     1 
ATOM   2893  O  O     . ASN C 1 53  ? -10.675 10.066  21.373  1.00 22.71 ?  53  ASN C O     1 
ATOM   2894  C  CB    . ASN C 1 53  ? -8.411  11.987  20.740  1.00 23.37 ?  53  ASN C CB    1 
ATOM   2895  C  CG    . ASN C 1 53  ? -7.166  11.168  20.502  1.00 24.44 ?  53  ASN C CG    1 
ATOM   2896  O  OD1   . ASN C 1 53  ? -7.251  10.023  20.046  1.00 24.15 ?  53  ASN C OD1   1 
ATOM   2897  N  ND2   . ASN C 1 53  ? -6.009  11.731  20.818  1.00 25.88 ?  53  ASN C ND2   1 
ATOM   2898  N  N     . LEU C 1 54  ? -10.034 9.206   19.383  1.00 22.54 ?  54  LEU C N     1 
ATOM   2899  C  CA    . LEU C 1 54  ? -10.635 7.891   19.578  1.00 22.77 ?  54  LEU C CA    1 
ATOM   2900  C  C     . LEU C 1 54  ? -9.880  7.077   20.633  1.00 23.83 ?  54  LEU C C     1 
ATOM   2901  O  O     . LEU C 1 54  ? -10.416 6.108   21.167  1.00 20.86 ?  54  LEU C O     1 
ATOM   2902  C  CB    . LEU C 1 54  ? -10.686 7.146   18.243  1.00 22.10 ?  54  LEU C CB    1 
ATOM   2903  C  CG    . LEU C 1 54  ? -11.519 7.792   17.129  1.00 24.16 ?  54  LEU C CG    1 
ATOM   2904  C  CD1   . LEU C 1 54  ? -11.628 6.852   15.935  1.00 20.01 ?  54  LEU C CD1   1 
ATOM   2905  C  CD2   . LEU C 1 54  ? -12.903 8.202   17.610  1.00 22.64 ?  54  LEU C CD2   1 
ATOM   2906  N  N     . GLN C 1 55  ? -8.632  7.464   20.918  1.00 28.92 ?  55  GLN C N     1 
ATOM   2907  C  CA    . GLN C 1 55  ? -7.791  6.804   21.908  1.00 32.26 ?  55  GLN C CA    1 
ATOM   2908  C  C     . GLN C 1 55  ? -8.531  6.613   23.234  1.00 32.88 ?  55  GLN C C     1 
ATOM   2909  O  O     . GLN C 1 55  ? -8.247  5.672   23.972  1.00 32.82 ?  55  GLN C O     1 
ATOM   2910  C  CB    . GLN C 1 55  ? -6.538  7.674   22.027  1.00 33.54 ?  55  GLN C CB    1 
ATOM   2911  C  CG    . GLN C 1 55  ? -5.807  7.595   23.364  1.00 36.76 ?  55  GLN C CG    1 
ATOM   2912  C  CD    . GLN C 1 55  ? -4.525  6.792   23.316  1.00 42.93 ?  55  GLN C CD    1 
ATOM   2913  O  OE1   . GLN C 1 55  ? -3.691  6.854   24.227  1.00 45.82 ?  55  GLN C OE1   1 
ATOM   2914  N  NE2   . GLN C 1 55  ? -4.340  6.042   22.240  1.00 48.42 ?  55  GLN C NE2   1 
ATOM   2915  N  N     . GLN C 1 56  ? -9.479  7.511   23.530  1.00 35.26 ?  56  GLN C N     1 
ATOM   2916  C  CA    . GLN C 1 56  ? -10.175 7.522   24.808  1.00 35.85 ?  56  GLN C CA    1 
ATOM   2917  C  C     . GLN C 1 56  ? -11.012 6.257   24.971  1.00 38.51 ?  56  GLN C C     1 
ATOM   2918  O  O     . GLN C 1 56  ? -11.304 5.850   26.093  1.00 41.61 ?  56  GLN C O     1 
ATOM   2919  C  CB    . GLN C 1 56  ? -11.092 8.741   24.932  1.00 34.32 ?  56  GLN C CB    1 
ATOM   2920  C  CG    . GLN C 1 56  ? -12.433 8.595   24.220  1.00 31.78 ?  56  GLN C CG    1 
ATOM   2921  C  CD    . GLN C 1 56  ? -13.203 9.895   24.148  1.00 30.47 ?  56  GLN C CD    1 
ATOM   2922  O  OE1   . GLN C 1 56  ? -14.173 10.115  24.882  1.00 30.60 ?  56  GLN C OE1   1 
ATOM   2923  N  NE2   . GLN C 1 56  ? -12.761 10.783  23.268  1.00 27.16 ?  56  GLN C NE2   1 
ATOM   2924  N  N     . PHE C 1 57  ? -11.398 5.647   23.845  1.00 39.93 ?  57  PHE C N     1 
ATOM   2925  C  CA    . PHE C 1 57  ? -12.297 4.505   23.866  1.00 41.10 ?  57  PHE C CA    1 
ATOM   2926  C  C     . PHE C 1 57  ? -11.507 3.217   24.082  1.00 38.20 ?  57  PHE C C     1 
ATOM   2927  O  O     . PHE C 1 57  ? -12.102 2.161   24.288  1.00 32.00 ?  57  PHE C O     1 
ATOM   2928  C  CB    . PHE C 1 57  ? -13.123 4.426   22.579  1.00 44.40 ?  57  PHE C CB    1 
ATOM   2929  C  CG    . PHE C 1 57  ? -14.016 5.637   22.352  1.00 46.92 ?  57  PHE C CG    1 
ATOM   2930  C  CD1   . PHE C 1 57  ? -15.253 5.739   22.977  1.00 39.92 ?  57  PHE C CD1   1 
ATOM   2931  C  CD2   . PHE C 1 57  ? -13.610 6.676   21.522  1.00 48.58 ?  57  PHE C CD2   1 
ATOM   2932  C  CE1   . PHE C 1 57  ? -16.059 6.847   22.774  1.00 40.14 ?  57  PHE C CE1   1 
ATOM   2933  C  CE2   . PHE C 1 57  ? -14.422 7.781   21.322  1.00 43.05 ?  57  PHE C CE2   1 
ATOM   2934  C  CZ    . PHE C 1 57  ? -15.643 7.863   21.947  1.00 41.22 ?  57  PHE C CZ    1 
ATOM   2935  N  N     . TYR C 1 58  ? -10.173 3.299   24.025  1.00 34.26 ?  58  TYR C N     1 
ATOM   2936  C  CA    . TYR C 1 58  ? -9.349  2.135   24.316  1.00 40.45 ?  58  TYR C CA    1 
ATOM   2937  C  C     . TYR C 1 58  ? -9.392  1.886   25.821  1.00 40.90 ?  58  TYR C C     1 
ATOM   2938  O  O     . TYR C 1 58  ? -9.646  2.804   26.598  1.00 43.10 ?  58  TYR C O     1 
ATOM   2939  C  CB    . TYR C 1 58  ? -7.880  2.244   23.893  1.00 40.48 ?  58  TYR C CB    1 
ATOM   2940  C  CG    . TYR C 1 58  ? -7.593  2.041   22.410  1.00 43.66 ?  58  TYR C CG    1 
ATOM   2941  C  CD1   . TYR C 1 58  ? -7.723  0.792   21.813  1.00 44.71 ?  58  TYR C CD1   1 
ATOM   2942  C  CD2   . TYR C 1 58  ? -7.143  3.091   21.620  1.00 42.19 ?  58  TYR C CD2   1 
ATOM   2943  C  CE1   . TYR C 1 58  ? -7.450  0.604   20.468  1.00 43.56 ?  58  TYR C CE1   1 
ATOM   2944  C  CE2   . TYR C 1 58  ? -6.862  2.914   20.276  1.00 42.49 ?  58  TYR C CE2   1 
ATOM   2945  C  CZ    . TYR C 1 58  ? -7.016  1.667   19.698  1.00 43.27 ?  58  TYR C CZ    1 
ATOM   2946  O  OH    . TYR C 1 58  ? -6.741  1.489   18.373  1.00 55.20 ?  58  TYR C OH    1 
ATOM   2947  N  N     . ALA C 1 59  ? -9.139  0.635   26.219  1.00 45.00 ?  59  ALA C N     1 
ATOM   2948  C  CA    . ALA C 1 59  ? -9.083  0.287   27.628  1.00 44.81 ?  59  ALA C CA    1 
ATOM   2949  C  C     . ALA C 1 59  ? -8.196  1.293   28.358  1.00 39.50 ?  59  ALA C C     1 
ATOM   2950  O  O     . ALA C 1 59  ? -7.108  1.620   27.892  1.00 36.29 ?  59  ALA C O     1 
ATOM   2951  C  CB    . ALA C 1 59  ? -8.582  -1.131  27.795  1.00 47.36 ?  59  ALA C CB    1 
ATOM   2952  N  N     . GLN C 1 60  ? -8.684  1.789   29.499  1.00 43.96 ?  60  GLN C N     1 
ATOM   2953  C  CA    . GLN C 1 60  ? -7.955  2.765   30.290  1.00 48.95 ?  60  GLN C CA    1 
ATOM   2954  C  C     . GLN C 1 60  ? -7.910  2.295   31.743  1.00 55.05 ?  60  GLN C C     1 
ATOM   2955  O  O     . GLN C 1 60  ? -8.940  1.945   32.314  1.00 49.23 ?  60  GLN C O     1 
ATOM   2956  C  CB    . GLN C 1 60  ? -8.628  4.138   30.212  1.00 49.32 ?  60  GLN C CB    1 
ATOM   2957  C  CG    . GLN C 1 60  ? -9.176  4.508   28.836  1.00 48.16 ?  60  GLN C CG    1 
ATOM   2958  C  CD    . GLN C 1 60  ? -8.147  5.111   27.904  1.00 46.11 ?  60  GLN C CD    1 
ATOM   2959  O  OE1   . GLN C 1 60  ? -7.054  5.512   28.319  1.00 46.41 ?  60  GLN C OE1   1 
ATOM   2960  N  NE2   . GLN C 1 60  ? -8.500  5.202   26.630  1.00 46.27 ?  60  GLN C NE2   1 
ATOM   2961  N  N     . ASN C 1 61  ? -6.707  2.280   32.330  1.00 63.58 ?  61  ASN C N     1 
ATOM   2962  C  CA    . ASN C 1 61  ? -6.539  2.045   33.756  1.00 64.95 ?  61  ASN C CA    1 
ATOM   2963  C  C     . ASN C 1 61  ? -6.618  0.554   34.078  1.00 62.28 ?  61  ASN C C     1 
ATOM   2964  O  O     . ASN C 1 61  ? -7.454  0.137   34.877  1.00 56.29 ?  61  ASN C O     1 
ATOM   2965  C  CB    . ASN C 1 61  ? -7.579  2.794   34.584  1.00 71.54 ?  61  ASN C CB    1 
ATOM   2966  C  CG    . ASN C 1 61  ? -7.339  4.285   34.607  1.00 72.76 ?  61  ASN C CG    1 
ATOM   2967  O  OD1   . ASN C 1 61  ? -6.971  4.838   35.649  1.00 75.62 ?  61  ASN C OD1   1 
ATOM   2968  N  ND2   . ASN C 1 61  ? -7.539  4.951   33.480  1.00 69.10 ?  61  ASN C ND2   1 
ATOM   2969  N  N     . GLY C 1 62  ? -5.729  -0.238  33.468  1.00 61.10 ?  62  GLY C N     1 
ATOM   2970  C  CA    . GLY C 1 62  ? -5.644  -1.664  33.743  1.00 55.10 ?  62  GLY C CA    1 
ATOM   2971  C  C     . GLY C 1 62  ? -6.988  -2.358  33.538  1.00 54.57 ?  62  GLY C C     1 
ATOM   2972  O  O     . GLY C 1 62  ? -7.205  -3.463  34.031  1.00 55.20 ?  62  GLY C O     1 
ATOM   2973  N  N     . GLU C 1 63  ? -7.876  -1.695  32.791  1.00 59.68 ?  63  GLU C N     1 
ATOM   2974  C  CA    . GLU C 1 63  ? -9.243  -2.151  32.610  1.00 53.97 ?  63  GLU C CA    1 
ATOM   2975  C  C     . GLU C 1 63  ? -9.279  -3.270  31.573  1.00 48.02 ?  63  GLU C C     1 
ATOM   2976  O  O     . GLU C 1 63  ? -8.657  -3.163  30.519  1.00 49.59 ?  63  GLU C O     1 
ATOM   2977  C  CB    . GLU C 1 63  ? -10.102 -0.965  32.168  1.00 55.50 ?  63  GLU C CB    1 
ATOM   2978  C  CG    . GLU C 1 63  ? -11.597 -1.159  32.408  1.00 61.23 ?  63  GLU C CG    1 
ATOM   2979  C  CD    . GLU C 1 63  ? -12.459 -0.028  31.876  1.00 70.85 ?  63  GLU C CD    1 
ATOM   2980  O  OE1   . GLU C 1 63  ? -11.893 0.950   31.343  1.00 77.40 ?  63  GLU C OE1   1 
ATOM   2981  O  OE2   . GLU C 1 63  ? -13.699 -0.129  31.990  1.00 73.00 -1 63  GLU C OE2   1 
ATOM   2982  N  N     . VAL C 1 64  ? -10.011 -4.343  31.893  1.00 41.31 ?  64  VAL C N     1 
ATOM   2983  C  CA    . VAL C 1 64  ? -10.263 -5.423  30.953  1.00 39.94 ?  64  VAL C CA    1 
ATOM   2984  C  C     . VAL C 1 64  ? -11.428 -5.024  30.051  1.00 43.78 ?  64  VAL C C     1 
ATOM   2985  O  O     . VAL C 1 64  ? -12.568 -4.958  30.506  1.00 48.68 ?  64  VAL C O     1 
ATOM   2986  C  CB    . VAL C 1 64  ? -10.574 -6.744  31.685  1.00 40.83 ?  64  VAL C CB    1 
ATOM   2987  C  CG1   . VAL C 1 64  ? -11.011 -7.839  30.718  1.00 40.92 ?  64  VAL C CG1   1 
ATOM   2988  C  CG2   . VAL C 1 64  ? -9.411  -7.217  32.549  1.00 39.01 ?  64  VAL C CG2   1 
ATOM   2989  N  N     . LYS C 1 65  ? -11.133 -4.762  28.772  1.00 42.86 ?  65  LYS C N     1 
ATOM   2990  C  CA    . LYS C 1 65  ? -12.166 -4.503  27.780  1.00 40.57 ?  65  LYS C CA    1 
ATOM   2991  C  C     . LYS C 1 65  ? -11.802 -5.191  26.467  1.00 33.26 ?  65  LYS C C     1 
ATOM   2992  O  O     . LYS C 1 65  ? -10.682 -5.049  25.980  1.00 29.52 ?  65  LYS C O     1 
ATOM   2993  C  CB    . LYS C 1 65  ? -12.338 -3.018  27.441  1.00 45.73 ?  65  LYS C CB    1 
ATOM   2994  C  CG    . LYS C 1 65  ? -12.385 -2.037  28.601  1.00 51.19 ?  65  LYS C CG    1 
ATOM   2995  C  CD    . LYS C 1 65  ? -13.128 -0.754  28.244  1.00 54.06 ?  65  LYS C CD    1 
ATOM   2996  C  CE    . LYS C 1 65  ? -12.848 -0.277  26.852  1.00 55.33 ?  65  LYS C CE    1 
ATOM   2997  N  NZ    . LYS C 1 65  ? -13.829 0.721   26.416  1.00 54.74 1  65  LYS C NZ    1 
ATOM   2998  N  N     . ASN C 1 66  ? -12.766 -5.916  25.892  1.00 27.61 ?  66  ASN C N     1 
ATOM   2999  C  CA    . ASN C 1 66  ? -12.602 -6.505  24.574  1.00 28.13 ?  66  ASN C CA    1 
ATOM   3000  C  C     . ASN C 1 66  ? -12.353 -5.370  23.583  1.00 31.33 ?  66  ASN C C     1 
ATOM   3001  O  O     . ASN C 1 66  ? -13.058 -4.363  23.609  1.00 35.73 ?  66  ASN C O     1 
ATOM   3002  C  CB    . ASN C 1 66  ? -13.817 -7.350  24.200  1.00 26.01 ?  66  ASN C CB    1 
ATOM   3003  C  CG    . ASN C 1 66  ? -13.530 -8.347  23.101  1.00 25.15 ?  66  ASN C CG    1 
ATOM   3004  O  OD1   . ASN C 1 66  ? -13.002 -7.980  22.045  1.00 25.67 ?  66  ASN C OD1   1 
ATOM   3005  N  ND2   . ASN C 1 66  ? -13.874 -9.607  23.326  1.00 21.31 ?  66  ASN C ND2   1 
ATOM   3006  N  N     . ARG C 1 67  ? -11.335 -5.522  22.729  1.00 34.23 ?  67  ARG C N     1 
ATOM   3007  C  CA    . ARG C 1 67  ? -11.045 -4.508  21.727  1.00 37.35 ?  67  ARG C CA    1 
ATOM   3008  C  C     . ARG C 1 67  ? -12.226 -4.375  20.768  1.00 37.25 ?  67  ARG C C     1 
ATOM   3009  O  O     . ARG C 1 67  ? -12.355 -3.364  20.082  1.00 31.97 ?  67  ARG C O     1 
ATOM   3010  C  CB    . ARG C 1 67  ? -9.738  -4.778  20.977  1.00 38.81 ?  67  ARG C CB    1 
ATOM   3011  C  CG    . ARG C 1 67  ? -8.537  -4.372  21.816  1.00 41.81 ?  67  ARG C CG    1 
ATOM   3012  C  CD    . ARG C 1 67  ? -7.346  -3.902  21.004  1.00 42.62 ?  67  ARG C CD    1 
ATOM   3013  N  NE    . ARG C 1 67  ? -6.222  -4.643  21.581  1.00 42.50 ?  67  ARG C NE    1 
ATOM   3014  C  CZ    . ARG C 1 67  ? -6.060  -5.945  21.378  1.00 44.73 ?  67  ARG C CZ    1 
ATOM   3015  N  NH1   . ARG C 1 67  ? -6.425  -6.477  20.220  1.00 46.63 1  67  ARG C NH1   1 
ATOM   3016  N  NH2   . ARG C 1 67  ? -5.460  -6.687  22.300  1.00 42.40 ?  67  ARG C NH2   1 
ATOM   3017  N  N     . ARG C 1 68  ? -13.084 -5.400  20.730  1.00 44.14 ?  68  ARG C N     1 
ATOM   3018  C  CA    . ARG C 1 68  ? -14.293 -5.350  19.926  1.00 47.17 ?  68  ARG C CA    1 
ATOM   3019  C  C     . ARG C 1 68  ? -15.205 -4.245  20.454  1.00 46.97 ?  68  ARG C C     1 
ATOM   3020  O  O     . ARG C 1 68  ? -15.711 -3.431  19.686  1.00 46.60 ?  68  ARG C O     1 
ATOM   3021  C  CB    . ARG C 1 68  ? -15.035 -6.691  19.946  1.00 48.30 ?  68  ARG C CB    1 
ATOM   3022  C  CG    . ARG C 1 68  ? -14.281 -7.850  19.310  1.00 54.20 ?  68  ARG C CG    1 
ATOM   3023  C  CD    . ARG C 1 68  ? -15.008 -9.169  19.532  1.00 56.13 ?  68  ARG C CD    1 
ATOM   3024  N  NE    . ARG C 1 68  ? -14.269 -10.342 19.051  1.00 51.35 ?  68  ARG C NE    1 
ATOM   3025  C  CZ    . ARG C 1 68  ? -14.019 -10.633 17.780  1.00 48.66 ?  68  ARG C CZ    1 
ATOM   3026  N  NH1   . ARG C 1 68  ? -14.427 -9.824  16.818  1.00 49.32 1  68  ARG C NH1   1 
ATOM   3027  N  NH2   . ARG C 1 68  ? -13.360 -11.738 17.476  1.00 39.28 ?  68  ARG C NH2   1 
ATOM   3028  N  N     . ASP C 1 69  ? -15.406 -4.239  21.777  1.00 44.04 ?  69  ASP C N     1 
ATOM   3029  C  CA    . ASP C 1 69  ? -16.267 -3.270  22.435  1.00 44.38 ?  69  ASP C CA    1 
ATOM   3030  C  C     . ASP C 1 69  ? -15.668 -1.873  22.291  1.00 43.18 ?  69  ASP C C     1 
ATOM   3031  O  O     . ASP C 1 69  ? -16.390 -0.877  22.297  1.00 41.83 ?  69  ASP C O     1 
ATOM   3032  C  CB    . ASP C 1 69  ? -16.493 -3.642  23.892  1.00 48.43 ?  69  ASP C CB    1 
ATOM   3033  C  CG    . ASP C 1 69  ? -17.329 -4.893  24.121  1.00 46.56 ?  69  ASP C CG    1 
ATOM   3034  O  OD1   . ASP C 1 69  ? -18.543 -4.846  23.832  1.00 48.98 ?  69  ASP C OD1   1 
ATOM   3035  O  OD2   . ASP C 1 69  ? -16.757 -5.906  24.578  1.00 48.30 -1 69  ASP C OD2   1 
ATOM   3036  N  N     . THR C 1 70  ? -14.339 -1.821  22.167  1.00 38.55 ?  70  THR C N     1 
ATOM   3037  C  CA    . THR C 1 70  ? -13.617 -0.578  21.959  1.00 31.85 ?  70  THR C CA    1 
ATOM   3038  C  C     . THR C 1 70  ? -14.023 0.016   20.615  1.00 33.69 ?  70  THR C C     1 
ATOM   3039  O  O     . THR C 1 70  ? -14.394 1.186   20.524  1.00 27.83 ?  70  THR C O     1 
ATOM   3040  C  CB    . THR C 1 70  ? -12.118 -0.874  22.014  1.00 30.85 ?  70  THR C CB    1 
ATOM   3041  O  OG1   . THR C 1 70  ? -11.827 -1.180  23.374  1.00 24.96 ?  70  THR C OG1   1 
ATOM   3042  C  CG2   . THR C 1 70  ? -11.264 0.293   21.549  1.00 31.03 ?  70  THR C CG2   1 
ATOM   3043  N  N     . TYR C 1 71  ? -13.952 -0.825  19.579  1.00 34.29 ?  71  TYR C N     1 
ATOM   3044  C  CA    . TYR C 1 71  ? -14.176 -0.405  18.206  1.00 34.71 ?  71  TYR C CA    1 
ATOM   3045  C  C     . TYR C 1 71  ? -15.640 -0.009  18.024  1.00 33.70 ?  71  TYR C C     1 
ATOM   3046  O  O     . TYR C 1 71  ? -15.935 0.990   17.373  1.00 38.23 ?  71  TYR C O     1 
ATOM   3047  C  CB    . TYR C 1 71  ? -13.727 -1.535  17.272  1.00 34.03 ?  71  TYR C CB    1 
ATOM   3048  C  CG    . TYR C 1 71  ? -12.256 -1.913  17.410  1.00 36.88 ?  71  TYR C CG    1 
ATOM   3049  C  CD1   . TYR C 1 71  ? -11.291 -0.951  17.682  1.00 34.13 ?  71  TYR C CD1   1 
ATOM   3050  C  CD2   . TYR C 1 71  ? -11.834 -3.231  17.278  1.00 35.50 ?  71  TYR C CD2   1 
ATOM   3051  C  CE1   . TYR C 1 71  ? -9.953  -1.285  17.811  1.00 36.70 ?  71  TYR C CE1   1 
ATOM   3052  C  CE2   . TYR C 1 71  ? -10.499 -3.579  17.406  1.00 35.20 ?  71  TYR C CE2   1 
ATOM   3053  C  CZ    . TYR C 1 71  ? -9.556  -2.604  17.674  1.00 37.54 ?  71  TYR C CZ    1 
ATOM   3054  O  OH    . TYR C 1 71  ? -8.238  -2.941  17.801  1.00 35.61 ?  71  TYR C OH    1 
ATOM   3055  N  N     . GLU C 1 72  ? -16.547 -0.798  18.610  1.00 32.55 ?  72  GLU C N     1 
ATOM   3056  C  CA    . GLU C 1 72  ? -17.971 -0.514  18.545  1.00 34.29 ?  72  GLU C CA    1 
ATOM   3057  C  C     . GLU C 1 72  ? -18.200 0.954   18.904  1.00 34.79 ?  72  GLU C C     1 
ATOM   3058  O  O     . GLU C 1 72  ? -18.778 1.705   18.122  1.00 40.03 ?  72  GLU C O     1 
ATOM   3059  C  CB    . GLU C 1 72  ? -18.715 -1.488  19.461  1.00 30.88 ?  72  GLU C CB    1 
ATOM   3060  C  CG    . GLU C 1 72  ? -20.236 -1.416  19.347  1.00 31.94 ?  72  GLU C CG    1 
ATOM   3061  C  CD    . GLU C 1 72  ? -20.783 -1.670  17.953  1.00 40.21 ?  72  GLU C CD    1 
ATOM   3062  O  OE1   . GLU C 1 72  ? -20.570 -2.780  17.418  1.00 43.37 ?  72  GLU C OE1   1 
ATOM   3063  O  OE2   . GLU C 1 72  ? -21.430 -0.753  17.403  1.00 44.10 -1 72  GLU C OE2   1 
ATOM   3064  N  N     . GLN C 1 73  ? -17.716 1.353   20.087  1.00 34.20 ?  73  GLN C N     1 
ATOM   3065  C  CA    . GLN C 1 73  ? -17.910 2.699   20.607  1.00 34.72 ?  73  GLN C CA    1 
ATOM   3066  C  C     . GLN C 1 73  ? -17.270 3.731   19.681  1.00 34.19 ?  73  GLN C C     1 
ATOM   3067  O  O     . GLN C 1 73  ? -17.769 4.848   19.558  1.00 38.99 ?  73  GLN C O     1 
ATOM   3068  C  CB    . GLN C 1 73  ? -17.297 2.843   22.000  1.00 34.01 ?  73  GLN C CB    1 
ATOM   3069  C  CG    . GLN C 1 73  ? -17.883 1.902   23.047  1.00 33.59 ?  73  GLN C CG    1 
ATOM   3070  C  CD    . GLN C 1 73  ? -17.039 1.816   24.301  1.00 31.25 ?  73  GLN C CD    1 
ATOM   3071  O  OE1   . GLN C 1 73  ? -15.907 2.311   24.354  1.00 23.89 ?  73  GLN C OE1   1 
ATOM   3072  N  NE2   . GLN C 1 73  ? -17.578 1.169   25.323  1.00 32.37 ?  73  GLN C NE2   1 
ATOM   3073  N  N     . MET C 1 74  ? -16.149 3.359   19.054  1.00 35.66 ?  74  MET C N     1 
ATOM   3074  C  CA    . MET C 1 74  ? -15.466 4.246   18.126  1.00 34.95 ?  74  MET C CA    1 
ATOM   3075  C  C     . MET C 1 74  ? -16.377 4.514   16.932  1.00 33.61 ?  74  MET C C     1 
ATOM   3076  O  O     . MET C 1 74  ? -16.597 5.662   16.551  1.00 42.21 ?  74  MET C O     1 
ATOM   3077  C  CB    . MET C 1 74  ? -14.153 3.631   17.628  1.00 37.37 ?  74  MET C CB    1 
ATOM   3078  C  CG    . MET C 1 74  ? -13.068 3.532   18.682  1.00 40.53 ?  74  MET C CG    1 
ATOM   3079  S  SD    . MET C 1 74  ? -11.649 2.565   18.126  1.00 38.92 ?  74  MET C SD    1 
ATOM   3080  C  CE    . MET C 1 74  ? -10.461 2.974   19.411  1.00 34.17 ?  74  MET C CE    1 
ATOM   3081  N  N     . VAL C 1 75  ? -16.895 3.427   16.353  1.00 36.03 ?  75  VAL C N     1 
ATOM   3082  C  CA    . VAL C 1 75  ? -17.781 3.493   15.204  1.00 35.58 ?  75  VAL C CA    1 
ATOM   3083  C  C     . VAL C 1 75  ? -18.988 4.356   15.561  1.00 34.67 ?  75  VAL C C     1 
ATOM   3084  O  O     . VAL C 1 75  ? -19.390 5.228   14.794  1.00 30.09 ?  75  VAL C O     1 
ATOM   3085  C  CB    . VAL C 1 75  ? -18.200 2.068   14.788  1.00 33.15 ?  75  VAL C CB    1 
ATOM   3086  C  CG1   . VAL C 1 75  ? -19.316 2.067   13.751  1.00 31.75 ?  75  VAL C CG1   1 
ATOM   3087  C  CG2   . VAL C 1 75  ? -17.012 1.253   14.291  1.00 34.95 ?  75  VAL C CG2   1 
ATOM   3088  N  N     . ASN C 1 76  ? -19.529 4.107   16.757  1.00 32.62 ?  76  ASN C N     1 
ATOM   3089  C  CA    . ASN C 1 76  ? -20.782 4.690   17.206  1.00 34.49 ?  76  ASN C CA    1 
ATOM   3090  C  C     . ASN C 1 76  ? -20.620 6.201   17.366  1.00 30.81 ?  76  ASN C C     1 
ATOM   3091  O  O     . ASN C 1 76  ? -21.491 6.967   16.960  1.00 31.52 ?  76  ASN C O     1 
ATOM   3092  C  CB    . ASN C 1 76  ? -21.249 3.995   18.481  1.00 38.10 ?  76  ASN C CB    1 
ATOM   3093  C  CG    . ASN C 1 76  ? -22.601 4.477   18.947  1.00 41.58 ?  76  ASN C CG    1 
ATOM   3094  O  OD1   . ASN C 1 76  ? -23.618 4.204   18.300  1.00 50.88 ?  76  ASN C OD1   1 
ATOM   3095  N  ND2   . ASN C 1 76  ? -22.635 5.177   20.071  1.00 44.69 ?  76  ASN C ND2   1 
ATOM   3096  N  N     . ALA C 1 77  ? -19.498 6.616   17.965  1.00 31.08 ?  77  ALA C N     1 
ATOM   3097  C  CA    . ALA C 1 77  ? -19.183 8.025   18.141  1.00 31.89 ?  77  ALA C CA    1 
ATOM   3098  C  C     . ALA C 1 77  ? -19.025 8.703   16.781  1.00 32.23 ?  77  ALA C C     1 
ATOM   3099  O  O     . ALA C 1 77  ? -19.479 9.828   16.591  1.00 36.86 ?  77  ALA C O     1 
ATOM   3100  C  CB    . ALA C 1 77  ? -17.931 8.175   18.981  1.00 28.22 ?  77  ALA C CB    1 
ATOM   3101  N  N     . ILE C 1 78  ? -18.368 8.009   15.845  1.00 35.77 ?  78  ILE C N     1 
ATOM   3102  C  CA    . ILE C 1 78  ? -18.183 8.522   14.496  1.00 31.87 ?  78  ILE C CA    1 
ATOM   3103  C  C     . ILE C 1 78  ? -19.554 8.723   13.854  1.00 28.50 ?  78  ILE C C     1 
ATOM   3104  O  O     . ILE C 1 78  ? -19.829 9.780   13.291  1.00 22.59 ?  78  ILE C O     1 
ATOM   3105  C  CB    . ILE C 1 78  ? -17.280 7.584   13.670  1.00 31.99 ?  78  ILE C CB    1 
ATOM   3106  C  CG1   . ILE C 1 78  ? -15.837 7.601   14.189  1.00 30.87 ?  78  ILE C CG1   1 
ATOM   3107  C  CG2   . ILE C 1 78  ? -17.345 7.929   12.181  1.00 33.11 ?  78  ILE C CG2   1 
ATOM   3108  C  CD1   . ILE C 1 78  ? -14.996 6.415   13.751  1.00 27.74 ?  78  ILE C CD1   1 
ATOM   3109  N  N     . LEU C 1 79  ? -20.416 7.706   13.965  1.00 27.16 ?  79  LEU C N     1 
ATOM   3110  C  CA    . LEU C 1 79  ? -21.732 7.738   13.346  1.00 29.59 ?  79  LEU C CA    1 
ATOM   3111  C  C     . LEU C 1 79  ? -22.573 8.869   13.937  1.00 25.55 ?  79  LEU C C     1 
ATOM   3112  O  O     . LEU C 1 79  ? -23.379 9.471   13.232  1.00 25.27 ?  79  LEU C O     1 
ATOM   3113  C  CB    . LEU C 1 79  ? -22.427 6.386   13.501  1.00 31.53 ?  79  LEU C CB    1 
ATOM   3114  C  CG    . LEU C 1 79  ? -22.293 5.424   12.316  1.00 33.72 ?  79  LEU C CG    1 
ATOM   3115  C  CD1   . LEU C 1 79  ? -22.993 5.989   11.090  1.00 37.07 ?  79  LEU C CD1   1 
ATOM   3116  C  CD2   . LEU C 1 79  ? -20.839 5.123   12.006  1.00 34.34 ?  79  LEU C CD2   1 
ATOM   3117  N  N     . ASP C 1 80  ? -22.385 9.146   15.232  1.00 23.43 ?  80  ASP C N     1 
ATOM   3118  C  CA    . ASP C 1 80  ? -23.185 10.143  15.925  1.00 23.69 ?  80  ASP C CA    1 
ATOM   3119  C  C     . ASP C 1 80  ? -23.047 11.501  15.242  1.00 19.38 ?  80  ASP C C     1 
ATOM   3120  O  O     . ASP C 1 80  ? -24.034 12.215  15.084  1.00 18.91 ?  80  ASP C O     1 
ATOM   3121  C  CB    . ASP C 1 80  ? -22.846 10.216  17.406  1.00 24.40 ?  80  ASP C CB    1 
ATOM   3122  C  CG    . ASP C 1 80  ? -23.637 9.272   18.300  1.00 23.14 ?  80  ASP C CG    1 
ATOM   3123  O  OD1   . ASP C 1 80  ? -24.461 8.507   17.758  1.00 25.37 ?  80  ASP C OD1   1 
ATOM   3124  O  OD2   . ASP C 1 80  ? -23.429 9.317   19.531  1.00 25.51 -1 80  ASP C OD2   1 
ATOM   3125  N  N     . ALA C 1 81  ? -21.820 11.855  14.848  1.00 18.79 ?  81  ALA C N     1 
ATOM   3126  C  CA    . ALA C 1 81  ? -21.571 13.142  14.222  1.00 18.19 ?  81  ALA C CA    1 
ATOM   3127  C  C     . ALA C 1 81  ? -22.167 13.158  12.815  1.00 20.04 ?  81  ALA C C     1 
ATOM   3128  O  O     . ALA C 1 81  ? -22.649 14.193  12.359  1.00 17.82 ?  81  ALA C O     1 
ATOM   3129  C  CB    . ALA C 1 81  ? -20.089 13.446  14.211  1.00 17.37 ?  81  ALA C CB    1 
ATOM   3130  N  N     . VAL C 1 82  ? -22.139 12.000  12.143  1.00 17.93 ?  82  VAL C N     1 
ATOM   3131  C  CA    . VAL C 1 82  ? -22.697 11.859  10.807  1.00 18.71 ?  82  VAL C CA    1 
ATOM   3132  C  C     . VAL C 1 82  ? -24.208 12.076  10.873  1.00 21.16 ?  82  VAL C C     1 
ATOM   3133  O  O     . VAL C 1 82  ? -24.763 12.844  10.089  1.00 21.67 ?  82  VAL C O     1 
ATOM   3134  C  CB    . VAL C 1 82  ? -22.366 10.484  10.191  1.00 20.43 ?  82  VAL C CB    1 
ATOM   3135  C  CG1   . VAL C 1 82  ? -23.068 10.268  8.854   1.00 18.70 ?  82  VAL C CG1   1 
ATOM   3136  C  CG2   . VAL C 1 82  ? -20.864 10.267  10.042  1.00 19.79 ?  82  VAL C CG2   1 
ATOM   3137  N  N     . ARG C 1 83  ? -24.859 11.386  11.818  1.00 21.91 ?  83  ARG C N     1 
ATOM   3138  C  CA    . ARG C 1 83  ? -26.309 11.386  11.933  1.00 23.28 ?  83  ARG C CA    1 
ATOM   3139  C  C     . ARG C 1 83  ? -26.808 12.754  12.395  1.00 25.61 ?  83  ARG C C     1 
ATOM   3140  O  O     . ARG C 1 83  ? -27.994 13.053  12.273  1.00 24.42 ?  83  ARG C O     1 
ATOM   3141  C  CB    . ARG C 1 83  ? -26.773 10.268  12.877  1.00 25.45 ?  83  ARG C CB    1 
ATOM   3142  C  CG    . ARG C 1 83  ? -26.681 8.872   12.277  1.00 26.04 ?  83  ARG C CG    1 
ATOM   3143  C  CD    . ARG C 1 83  ? -27.133 7.765   13.222  1.00 28.18 ?  83  ARG C CD    1 
ATOM   3144  N  NE    . ARG C 1 83  ? -26.258 7.591   14.388  1.00 27.20 ?  83  ARG C NE    1 
ATOM   3145  C  CZ    . ARG C 1 83  ? -25.708 6.442   14.768  1.00 28.60 ?  83  ARG C CZ    1 
ATOM   3146  N  NH1   . ARG C 1 83  ? -25.874 5.349   14.043  1.00 32.74 1  83  ARG C NH1   1 
ATOM   3147  N  NH2   . ARG C 1 83  ? -24.988 6.393   15.875  1.00 27.45 ?  83  ARG C NH2   1 
ATOM   3148  N  N     . ALA C 1 84  ? -25.900 13.580  12.927  1.00 25.37 ?  84  ALA C N     1 
ATOM   3149  C  CA    . ALA C 1 84  ? -26.247 14.928  13.348  1.00 26.36 ?  84  ALA C CA    1 
ATOM   3150  C  C     . ALA C 1 84  ? -26.185 15.882  12.156  1.00 24.57 ?  84  ALA C C     1 
ATOM   3151  O  O     . ALA C 1 84  ? -26.735 16.979  12.212  1.00 26.15 ?  84  ALA C O     1 
ATOM   3152  C  CB    . ALA C 1 84  ? -25.338 15.383  14.468  1.00 25.88 ?  84  ALA C CB    1 
ATOM   3153  N  N     . GLY C 1 85  ? -25.498 15.459  11.089  1.00 21.11 ?  85  GLY C N     1 
ATOM   3154  C  CA    . GLY C 1 85  ? -25.469 16.212  9.845   1.00 19.70 ?  85  GLY C CA    1 
ATOM   3155  C  C     . GLY C 1 85  ? -24.101 16.839  9.587   1.00 18.11 ?  85  GLY C C     1 
ATOM   3156  O  O     . GLY C 1 85  ? -23.941 17.623  8.653   1.00 18.00 ?  85  GLY C O     1 
ATOM   3157  N  N     . LYS C 1 86  ? -23.121 16.481  10.421  1.00 16.15 ?  86  LYS C N     1 
ATOM   3158  C  CA    . LYS C 1 86  ? -21.787 17.050  10.331  1.00 18.45 ?  86  LYS C CA    1 
ATOM   3159  C  C     . LYS C 1 86  ? -20.990 16.374  9.219   1.00 19.10 ?  86  LYS C C     1 
ATOM   3160  O  O     . LYS C 1 86  ? -20.998 15.151  9.081   1.00 15.44 ?  86  LYS C O     1 
ATOM   3161  C  CB    . LYS C 1 86  ? -21.039 16.923  11.663  1.00 23.05 ?  86  LYS C CB    1 
ATOM   3162  C  CG    . LYS C 1 86  ? -21.634 17.728  12.812  1.00 25.58 ?  86  LYS C CG    1 
ATOM   3163  C  CD    . LYS C 1 86  ? -20.637 18.021  13.929  1.00 26.95 ?  86  LYS C CD    1 
ATOM   3164  C  CE    . LYS C 1 86  ? -21.264 18.453  15.218  1.00 31.31 ?  86  LYS C CE    1 
ATOM   3165  N  NZ    . LYS C 1 86  ? -21.798 17.329  15.993  1.00 31.17 1  86  LYS C NZ    1 
ATOM   3166  N  N     . LYS C 1 87  ? -20.296 17.209  8.438   1.00 17.75 ?  87  LYS C N     1 
ATOM   3167  C  CA    . LYS C 1 87  ? -19.352 16.739  7.441   1.00 16.86 ?  87  LYS C CA    1 
ATOM   3168  C  C     . LYS C 1 87  ? -18.142 16.176  8.183   1.00 18.13 ?  87  LYS C C     1 
ATOM   3169  O  O     . LYS C 1 87  ? -17.251 16.919  8.594   1.00 14.63 ?  87  LYS C O     1 
ATOM   3170  C  CB    . LYS C 1 87  ? -19.028 17.858  6.444   1.00 15.46 ?  87  LYS C CB    1 
ATOM   3171  C  CG    . LYS C 1 87  ? -17.932 17.501  5.453   1.00 15.90 ?  87  LYS C CG    1 
ATOM   3172  C  CD    . LYS C 1 87  ? -17.717 18.489  4.314   1.00 16.06 ?  87  LYS C CD    1 
ATOM   3173  C  CE    . LYS C 1 87  ? -17.111 19.780  4.765   1.00 15.62 ?  87  LYS C CE    1 
ATOM   3174  N  NZ    . LYS C 1 87  ? -16.741 20.613  3.619   1.00 15.15 1  87  LYS C NZ    1 
ATOM   3175  N  N     . THR C 1 88  ? -18.153 14.848  8.347   1.00 19.22 ?  88  THR C N     1 
ATOM   3176  C  CA    . THR C 1 88  ? -17.298 14.150  9.294   1.00 22.19 ?  88  THR C CA    1 
ATOM   3177  C  C     . THR C 1 88  ? -16.125 13.506  8.562   1.00 24.95 ?  88  THR C C     1 
ATOM   3178  O  O     . THR C 1 88  ? -16.280 13.014  7.447   1.00 26.07 ?  88  THR C O     1 
ATOM   3179  C  CB    . THR C 1 88  ? -18.118 13.087  10.025  1.00 20.88 ?  88  THR C CB    1 
ATOM   3180  O  OG1   . THR C 1 88  ? -19.317 13.733  10.441  1.00 21.41 ?  88  THR C OG1   1 
ATOM   3181  C  CG2   . THR C 1 88  ? -17.382 12.503  11.217  1.00 22.08 ?  88  THR C CG2   1 
ATOM   3182  N  N     . VAL C 1 89  ? -14.962 13.491  9.223   1.00 25.47 ?  89  VAL C N     1 
ATOM   3183  C  CA    . VAL C 1 89  ? -13.786 12.826  8.691   1.00 25.32 ?  89  VAL C CA    1 
ATOM   3184  C  C     . VAL C 1 89  ? -13.107 12.017  9.794   1.00 26.34 ?  89  VAL C C     1 
ATOM   3185  O  O     . VAL C 1 89  ? -12.917 12.500  10.908  1.00 28.09 ?  89  VAL C O     1 
ATOM   3186  C  CB    . VAL C 1 89  ? -12.814 13.835  8.051   1.00 27.83 ?  89  VAL C CB    1 
ATOM   3187  C  CG1   . VAL C 1 89  ? -11.385 13.305  8.007   1.00 28.38 ?  89  VAL C CG1   1 
ATOM   3188  C  CG2   . VAL C 1 89  ? -13.278 14.249  6.661   1.00 28.19 ?  89  VAL C CG2   1 
ATOM   3189  N  N     . CYS C 1 90  ? -12.752 10.775  9.450   1.00 26.15 ?  90  CYS C N     1 
ATOM   3190  C  CA    . CYS C 1 90  ? -12.004 9.889   10.327  1.00 29.20 ?  90  CYS C CA    1 
ATOM   3191  C  C     . CYS C 1 90  ? -10.541 9.882   9.888   1.00 24.80 ?  90  CYS C C     1 
ATOM   3192  O  O     . CYS C 1 90  ? -10.217 9.401   8.805   1.00 32.46 ?  90  CYS C O     1 
ATOM   3193  C  CB    . CYS C 1 90  ? -12.616 8.491   10.312  1.00 28.41 ?  90  CYS C CB    1 
ATOM   3194  S  SG    . CYS C 1 90  ? -11.696 7.272   11.287  1.00 29.18 ?  90  CYS C SG    1 
ATOM   3195  N  N     . ALA C 1 91  ? -9.670  10.446  10.732  1.00 23.95 ?  91  ALA C N     1 
ATOM   3196  C  CA    . ALA C 1 91  ? -8.248  10.535  10.440  1.00 23.30 ?  91  ALA C CA    1 
ATOM   3197  C  C     . ALA C 1 91  ? -7.497  9.427   11.172  1.00 25.38 ?  91  ALA C C     1 
ATOM   3198  O  O     . ALA C 1 91  ? -7.157  9.579   12.343  1.00 27.05 ?  91  ALA C O     1 
ATOM   3199  C  CB    . ALA C 1 91  ? -7.725  11.901  10.833  1.00 21.20 ?  91  ALA C CB    1 
ATOM   3200  N  N     . LEU C 1 92  ? -7.247  8.315   10.467  1.00 24.95 ?  92  LEU C N     1 
ATOM   3201  C  CA    . LEU C 1 92  ? -6.503  7.195   11.023  1.00 26.47 ?  92  LEU C CA    1 
ATOM   3202  C  C     . LEU C 1 92  ? -5.070  7.218   10.497  1.00 25.03 ?  92  LEU C C     1 
ATOM   3203  O  O     . LEU C 1 92  ? -4.791  7.823   9.463   1.00 22.60 ?  92  LEU C O     1 
ATOM   3204  C  CB    . LEU C 1 92  ? -7.188  5.872   10.685  1.00 30.04 ?  92  LEU C CB    1 
ATOM   3205  C  CG    . LEU C 1 92  ? -8.605  5.687   11.234  1.00 30.74 ?  92  LEU C CG    1 
ATOM   3206  C  CD1   . LEU C 1 92  ? -9.074  4.262   11.010  1.00 34.98 ?  92  LEU C CD1   1 
ATOM   3207  C  CD2   . LEU C 1 92  ? -8.685  6.049   12.706  1.00 28.37 ?  92  LEU C CD2   1 
ATOM   3208  N  N     . TYR C 1 93  ? -4.176  6.532   11.220  1.00 21.08 ?  93  TYR C N     1 
ATOM   3209  C  CA    . TYR C 1 93  ? -2.766  6.494   10.871  1.00 23.08 ?  93  TYR C CA    1 
ATOM   3210  C  C     . TYR C 1 93  ? -2.559  5.454   9.773   1.00 21.60 ?  93  TYR C C     1 
ATOM   3211  O  O     . TYR C 1 93  ? -3.096  4.349   9.840   1.00 18.13 ?  93  TYR C O     1 
ATOM   3212  C  CB    . TYR C 1 93  ? -1.883  6.230   12.099  1.00 24.29 ?  93  TYR C CB    1 
ATOM   3213  C  CG    . TYR C 1 93  ? -1.709  4.776   12.520  1.00 24.42 ?  93  TYR C CG    1 
ATOM   3214  C  CD1   . TYR C 1 93  ? -0.704  3.985   11.973  1.00 27.28 ?  93  TYR C CD1   1 
ATOM   3215  C  CD2   . TYR C 1 93  ? -2.523  4.204   13.491  1.00 27.30 ?  93  TYR C CD2   1 
ATOM   3216  C  CE1   . TYR C 1 93  ? -0.531  2.665   12.359  1.00 25.77 ?  93  TYR C CE1   1 
ATOM   3217  C  CE2   . TYR C 1 93  ? -2.360  2.886   13.885  1.00 26.99 ?  93  TYR C CE2   1 
ATOM   3218  C  CZ    . TYR C 1 93  ? -1.362  2.115   13.319  1.00 23.44 ?  93  TYR C CZ    1 
ATOM   3219  O  OH    . TYR C 1 93  ? -1.205  0.819   13.714  1.00 30.17 ?  93  TYR C OH    1 
ATOM   3220  N  N     . GLY C 1 94  ? -1.780  5.843   8.757   1.00 20.16 ?  94  GLY C N     1 
ATOM   3221  C  CA    . GLY C 1 94  ? -1.451  4.974   7.639   1.00 21.48 ?  94  GLY C CA    1 
ATOM   3222  C  C     . GLY C 1 94  ? -2.571  4.944   6.603   1.00 21.08 ?  94  GLY C C     1 
ATOM   3223  O  O     . GLY C 1 94  ? -3.024  5.983   6.129   1.00 26.42 ?  94  GLY C O     1 
ATOM   3224  N  N     . HIS C 1 95  ? -2.997  3.726   6.260   1.00 18.69 ?  95  HIS C N     1 
ATOM   3225  C  CA    . HIS C 1 95  ? -4.100  3.505   5.342   1.00 19.77 ?  95  HIS C CA    1 
ATOM   3226  C  C     . HIS C 1 95  ? -5.339  3.220   6.186   1.00 18.32 ?  95  HIS C C     1 
ATOM   3227  O  O     . HIS C 1 95  ? -5.316  2.342   7.045   1.00 20.61 ?  95  HIS C O     1 
ATOM   3228  C  CB    . HIS C 1 95  ? -3.731  2.382   4.363   1.00 20.23 ?  95  HIS C CB    1 
ATOM   3229  C  CG    . HIS C 1 95  ? -4.737  2.077   3.300   1.00 18.24 ?  95  HIS C CG    1 
ATOM   3230  N  ND1   . HIS C 1 95  ? -6.068  1.809   3.537   1.00 18.06 ?  95  HIS C ND1   1 
ATOM   3231  C  CD2   . HIS C 1 95  ? -4.565  1.942   1.977   1.00 16.57 ?  95  HIS C CD2   1 
ATOM   3232  C  CE1   . HIS C 1 95  ? -6.674  1.552   2.386   1.00 16.90 ?  95  HIS C CE1   1 
ATOM   3233  N  NE2   . HIS C 1 95  ? -5.779  1.630   1.424   1.00 15.79 ?  95  HIS C NE2   1 
ATOM   3234  N  N     . PRO C 1 96  ? -6.452  3.958   5.987   1.00 17.77 ?  96  PRO C N     1 
ATOM   3235  C  CA    . PRO C 1 96  ? -7.599  3.849   6.889   1.00 17.89 ?  96  PRO C CA    1 
ATOM   3236  C  C     . PRO C 1 96  ? -8.205  2.447   6.938   1.00 16.87 ?  96  PRO C C     1 
ATOM   3237  O  O     . PRO C 1 96  ? -8.797  2.065   7.945   1.00 17.01 ?  96  PRO C O     1 
ATOM   3238  C  CB    . PRO C 1 96  ? -8.582  4.900   6.339   1.00 17.62 ?  96  PRO C CB    1 
ATOM   3239  C  CG    . PRO C 1 96  ? -8.181  5.070   4.890   1.00 15.83 ?  96  PRO C CG    1 
ATOM   3240  C  CD    . PRO C 1 96  ? -6.673  4.904   4.881   1.00 15.77 ?  96  PRO C CD    1 
ATOM   3241  N  N     . GLY C 1 97  ? -8.039  1.678   5.855   1.00 16.47 ?  97  GLY C N     1 
ATOM   3242  C  CA    . GLY C 1 97  ? -8.699  0.387   5.735   1.00 18.16 ?  97  GLY C CA    1 
ATOM   3243  C  C     . GLY C 1 97  ? -7.726  -0.789  5.804   1.00 18.86 ?  97  GLY C C     1 
ATOM   3244  O  O     . GLY C 1 97  ? -8.121  -1.928  5.566   1.00 17.26 ?  97  GLY C O     1 
ATOM   3245  N  N     . VAL C 1 98  ? -6.459  -0.517  6.137   1.00 20.83 ?  98  VAL C N     1 
ATOM   3246  C  CA    . VAL C 1 98  ? -5.445  -1.560  6.175   1.00 25.63 ?  98  VAL C CA    1 
ATOM   3247  C  C     . VAL C 1 98  ? -5.303  -2.059  7.610   1.00 28.31 ?  98  VAL C C     1 
ATOM   3248  O  O     . VAL C 1 98  ? -4.705  -1.393  8.452   1.00 29.81 ?  98  VAL C O     1 
ATOM   3249  C  CB    . VAL C 1 98  ? -4.096  -1.082  5.601   1.00 26.12 ?  98  VAL C CB    1 
ATOM   3250  C  CG1   . VAL C 1 98  ? -2.922  -1.903  6.122   1.00 27.67 ?  98  VAL C CG1   1 
ATOM   3251  C  CG2   . VAL C 1 98  ? -4.110  -1.077  4.077   1.00 25.79 ?  98  VAL C CG2   1 
ATOM   3252  N  N     . PHE C 1 99  ? -5.861  -3.246  7.872   1.00 31.67 ?  99  PHE C N     1 
ATOM   3253  C  CA    . PHE C 1 99  ? -5.915  -3.780  9.221   1.00 35.29 ?  99  PHE C CA    1 
ATOM   3254  C  C     . PHE C 1 99  ? -6.497  -2.699  10.129  1.00 34.27 ?  99  PHE C C     1 
ATOM   3255  O  O     . PHE C 1 99  ? -5.918  -2.362  11.160  1.00 31.79 ?  99  PHE C O     1 
ATOM   3256  C  CB    . PHE C 1 99  ? -4.520  -4.252  9.643   1.00 37.90 ?  99  PHE C CB    1 
ATOM   3257  C  CG    . PHE C 1 99  ? -3.971  -5.422  8.835   1.00 41.64 ?  99  PHE C CG    1 
ATOM   3258  C  CD1   . PHE C 1 99  ? -3.372  -5.216  7.596   1.00 41.13 ?  99  PHE C CD1   1 
ATOM   3259  C  CD2   . PHE C 1 99  ? -4.042  -6.722  9.322   1.00 46.03 ?  99  PHE C CD2   1 
ATOM   3260  C  CE1   . PHE C 1 99  ? -2.871  -6.282  6.865   1.00 46.63 ?  99  PHE C CE1   1 
ATOM   3261  C  CE2   . PHE C 1 99  ? -3.537  -7.784  8.586   1.00 48.29 ?  99  PHE C CE2   1 
ATOM   3262  C  CZ    . PHE C 1 99  ? -2.954  -7.562  7.361   1.00 50.49 ?  99  PHE C CZ    1 
ATOM   3263  N  N     . ALA C 1 100 ? -7.643  -2.155  9.706   1.00 34.98 ?  100 ALA C N     1 
ATOM   3264  C  CA    . ALA C 1 100 ? -8.366  -1.139  10.454  1.00 31.33 ?  100 ALA C CA    1 
ATOM   3265  C  C     . ALA C 1 100 ? -9.865  -1.398  10.332  1.00 32.27 ?  100 ALA C C     1 
ATOM   3266  O  O     . ALA C 1 100 ? -10.457 -1.144  9.286   1.00 34.41 ?  100 ALA C O     1 
ATOM   3267  C  CB    . ALA C 1 100 ? -8.003  0.238   9.941   1.00 32.50 ?  100 ALA C CB    1 
ATOM   3268  N  N     . CYS C 1 101 ? -10.470 -1.898  11.414  1.00 32.57 ?  101 CYS C N     1 
ATOM   3269  C  CA    . CYS C 1 101 ? -11.857 -2.335  11.375  1.00 35.65 ?  101 CYS C CA    1 
ATOM   3270  C  C     . CYS C 1 101 ? -12.802 -1.147  11.543  1.00 33.62 ?  101 CYS C C     1 
ATOM   3271  O  O     . CYS C 1 101 ? -13.891 -1.135  10.972  1.00 24.00 ?  101 CYS C O     1 
ATOM   3272  C  CB    . CYS C 1 101 ? -12.130 -3.401  12.431  1.00 39.83 ?  101 CYS C CB    1 
ATOM   3273  S  SG    . CYS C 1 101 ? -11.908 -2.820  14.132  1.00 45.29 ?  101 CYS C SG    1 
ATOM   3274  N  N     . VAL C 1 102 ? -12.378 -0.149  12.323  1.00 32.88 ?  102 VAL C N     1 
ATOM   3275  C  CA    . VAL C 1 102 ? -13.257 0.950   12.689  1.00 24.37 ?  102 VAL C CA    1 
ATOM   3276  C  C     . VAL C 1 102 ? -13.873 1.540   11.425  1.00 20.11 ?  102 VAL C C     1 
ATOM   3277  O  O     . VAL C 1 102 ? -15.094 1.610   11.297  1.00 13.88 ?  102 VAL C O     1 
ATOM   3278  C  CB    . VAL C 1 102 ? -12.510 2.019   13.508  1.00 28.08 ?  102 VAL C CB    1 
ATOM   3279  C  CG1   . VAL C 1 102 ? -13.293 3.324   13.606  1.00 27.15 ?  102 VAL C CG1   1 
ATOM   3280  C  CG2   . VAL C 1 102 ? -12.157 1.493   14.892  1.00 33.19 ?  102 VAL C CG2   1 
ATOM   3281  N  N     . SER C 1 103 ? -13.005 1.943   10.495  1.00 17.49 ?  103 SER C N     1 
ATOM   3282  C  CA    . SER C 1 103 ? -13.421 2.689   9.321   1.00 20.04 ?  103 SER C CA    1 
ATOM   3283  C  C     . SER C 1 103 ? -14.355 1.860   8.439   1.00 19.10 ?  103 SER C C     1 
ATOM   3284  O  O     . SER C 1 103 ? -15.394 2.361   8.020   1.00 23.02 ?  103 SER C O     1 
ATOM   3285  C  CB    . SER C 1 103 ? -12.227 3.205   8.565   1.00 19.88 ?  103 SER C CB    1 
ATOM   3286  O  OG    . SER C 1 103 ? -11.661 4.318   9.245   1.00 17.54 ?  103 SER C OG    1 
ATOM   3287  N  N     . HIS C 1 104 ? -14.001 0.598   8.160   1.00 18.07 ?  104 HIS C N     1 
ATOM   3288  C  CA    . HIS C 1 104 ? -14.842 -0.237  7.316   1.00 17.01 ?  104 HIS C CA    1 
ATOM   3289  C  C     . HIS C 1 104 ? -16.221 -0.402  7.951   1.00 16.60 ?  104 HIS C C     1 
ATOM   3290  O  O     . HIS C 1 104 ? -17.219 -0.501  7.243   1.00 17.80 ?  104 HIS C O     1 
ATOM   3291  C  CB    . HIS C 1 104 ? -14.205 -1.602  7.023   1.00 17.43 ?  104 HIS C CB    1 
ATOM   3292  C  CG    . HIS C 1 104 ? -13.108 -1.565  6.010   1.00 17.91 ?  104 HIS C CG    1 
ATOM   3293  N  ND1   . HIS C 1 104 ? -13.334 -1.538  4.651   1.00 15.29 ?  104 HIS C ND1   1 
ATOM   3294  C  CD2   . HIS C 1 104 ? -11.778 -1.547  6.163   1.00 16.66 ?  104 HIS C CD2   1 
ATOM   3295  C  CE1   . HIS C 1 104 ? -12.172 -1.500  4.015   1.00 16.43 ?  104 HIS C CE1   1 
ATOM   3296  N  NE2   . HIS C 1 104 ? -11.213 -1.508  4.915   1.00 16.49 ?  104 HIS C NE2   1 
ATOM   3297  N  N     . MET C 1 105 ? -16.267 -0.445  9.286   1.00 18.11 ?  105 MET C N     1 
ATOM   3298  C  CA    . MET C 1 105 ? -17.519 -0.638  10.000  1.00 19.75 ?  105 MET C CA    1 
ATOM   3299  C  C     . MET C 1 105 ? -18.336 0.650   9.965   1.00 20.47 ?  105 MET C C     1 
ATOM   3300  O  O     . MET C 1 105 ? -19.565 0.611   9.960   1.00 18.96 ?  105 MET C O     1 
ATOM   3301  C  CB    . MET C 1 105 ? -17.268 -1.021  11.463  1.00 22.77 ?  105 MET C CB    1 
ATOM   3302  C  CG    . MET C 1 105 ? -16.384 -2.236  11.639  1.00 24.59 ?  105 MET C CG    1 
ATOM   3303  S  SD    . MET C 1 105 ? -15.637 -2.304  13.279  1.00 33.26 ?  105 MET C SD    1 
ATOM   3304  C  CE    . MET C 1 105 ? -17.114 -2.495  14.286  1.00 38.20 ?  105 MET C CE    1 
ATOM   3305  N  N     . ALA C 1 106 ? -17.636 1.790   9.944   1.00 19.37 ?  106 ALA C N     1 
ATOM   3306  C  CA    . ALA C 1 106 ? -18.286 3.086   10.019  1.00 21.28 ?  106 ALA C CA    1 
ATOM   3307  C  C     . ALA C 1 106 ? -18.802 3.487   8.638   1.00 24.74 ?  106 ALA C C     1 
ATOM   3308  O  O     . ALA C 1 106 ? -19.850 4.121   8.534   1.00 30.61 ?  106 ALA C O     1 
ATOM   3309  C  CB    . ALA C 1 106 ? -17.338 4.116   10.596  1.00 18.87 ?  106 ALA C CB    1 
ATOM   3310  N  N     . ILE C 1 107 ? -18.070 3.108   7.583   1.00 23.49 ?  107 ILE C N     1 
ATOM   3311  C  CA    . ILE C 1 107 ? -18.536 3.336   6.224   1.00 23.10 ?  107 ILE C CA    1 
ATOM   3312  C  C     . ILE C 1 107 ? -19.784 2.490   5.973   1.00 25.69 ?  107 ILE C C     1 
ATOM   3313  O  O     . ILE C 1 107 ? -20.768 2.990   5.433   1.00 28.12 ?  107 ILE C O     1 
ATOM   3314  C  CB    . ILE C 1 107 ? -17.442 3.056   5.175   1.00 20.42 ?  107 ILE C CB    1 
ATOM   3315  C  CG1   . ILE C 1 107 ? -16.235 3.980   5.351   1.00 19.15 ?  107 ILE C CG1   1 
ATOM   3316  C  CG2   . ILE C 1 107 ? -18.021 3.151   3.762   1.00 20.52 ?  107 ILE C CG2   1 
ATOM   3317  C  CD1   . ILE C 1 107 ? -15.148 3.798   4.306   1.00 17.05 ?  107 ILE C CD1   1 
ATOM   3318  N  N     . THR C 1 108 ? -19.735 1.210   6.367   1.00 26.60 ?  108 THR C N     1 
ATOM   3319  C  CA    . THR C 1 108 ? -20.844 0.291   6.149   1.00 28.90 ?  108 THR C CA    1 
ATOM   3320  C  C     . THR C 1 108 ? -22.103 0.839   6.817   1.00 30.04 ?  108 THR C C     1 
ATOM   3321  O  O     . THR C 1 108 ? -23.132 1.013   6.168   1.00 31.27 ?  108 THR C O     1 
ATOM   3322  C  CB    . THR C 1 108 ? -20.496 -1.095  6.691   1.00 28.24 ?  108 THR C CB    1 
ATOM   3323  O  OG1   . THR C 1 108 ? -19.303 -1.487  6.021   1.00 27.70 ?  108 THR C OG1   1 
ATOM   3324  C  CG2   . THR C 1 108 ? -21.594 -2.115  6.439   1.00 27.85 ?  108 THR C CG2   1 
ATOM   3325  N  N     . ARG C 1 109 ? -22.003 1.092   8.126   1.00 33.51 ?  109 ARG C N     1 
ATOM   3326  C  CA    . ARG C 1 109 ? -23.133 1.541   8.924   1.00 31.60 ?  109 ARG C CA    1 
ATOM   3327  C  C     . ARG C 1 109 ? -23.694 2.829   8.325   1.00 28.29 ?  109 ARG C C     1 
ATOM   3328  O  O     . ARG C 1 109 ? -24.905 3.044   8.319   1.00 29.65 ?  109 ARG C O     1 
ATOM   3329  C  CB    . ARG C 1 109 ? -22.669 1.747   10.371  1.00 34.58 ?  109 ARG C CB    1 
ATOM   3330  C  CG    . ARG C 1 109 ? -23.748 1.598   11.435  1.00 41.06 ?  109 ARG C CG    1 
ATOM   3331  C  CD    . ARG C 1 109 ? -23.174 1.660   12.847  1.00 44.59 ?  109 ARG C CD    1 
ATOM   3332  N  NE    . ARG C 1 109 ? -22.252 0.560   13.155  1.00 43.71 ?  109 ARG C NE    1 
ATOM   3333  C  CZ    . ARG C 1 109 ? -22.286 -0.179  14.260  1.00 44.77 ?  109 ARG C CZ    1 
ATOM   3334  N  NH1   . ARG C 1 109 ? -23.234 0.012   15.160  1.00 41.23 1  109 ARG C NH1   1 
ATOM   3335  N  NH2   . ARG C 1 109 ? -21.368 -1.109  14.462  1.00 47.18 ?  109 ARG C NH2   1 
ATOM   3336  N  N     . ALA C 1 110 ? -22.792 3.673   7.814   1.00 26.60 ?  110 ALA C N     1 
ATOM   3337  C  CA    . ALA C 1 110 ? -23.146 4.984   7.295   1.00 26.35 ?  110 ALA C CA    1 
ATOM   3338  C  C     . ALA C 1 110 ? -23.974 4.845   6.020   1.00 30.33 ?  110 ALA C C     1 
ATOM   3339  O  O     . ALA C 1 110 ? -24.963 5.552   5.839   1.00 31.08 ?  110 ALA C O     1 
ATOM   3340  C  CB    . ALA C 1 110 ? -21.887 5.786   7.048   1.00 25.09 ?  110 ALA C CB    1 
ATOM   3341  N  N     . LYS C 1 111 ? -23.549 3.931   5.141   1.00 33.18 ?  111 LYS C N     1 
ATOM   3342  C  CA    . LYS C 1 111 ? -24.187 3.734   3.849   1.00 35.76 ?  111 LYS C CA    1 
ATOM   3343  C  C     . LYS C 1 111 ? -25.552 3.076   4.026   1.00 32.96 ?  111 LYS C C     1 
ATOM   3344  O  O     . LYS C 1 111 ? -26.469 3.328   3.249   1.00 29.11 ?  111 LYS C O     1 
ATOM   3345  C  CB    . LYS C 1 111 ? -23.334 2.845   2.939   1.00 36.89 ?  111 LYS C CB    1 
ATOM   3346  C  CG    . LYS C 1 111 ? -22.120 3.523   2.329   1.00 43.48 ?  111 LYS C CG    1 
ATOM   3347  C  CD    . LYS C 1 111 ? -21.375 2.653   1.326   1.00 44.34 ?  111 LYS C CD    1 
ATOM   3348  C  CE    . LYS C 1 111 ? -20.275 3.398   0.641   1.00 49.02 ?  111 LYS C CE    1 
ATOM   3349  N  NZ    . LYS C 1 111 ? -20.792 4.529   -0.133  1.00 54.86 1  111 LYS C NZ    1 
ATOM   3350  N  N     . ALA C 1 112 ? -25.660 2.219   5.045   1.00 32.76 ?  112 ALA C N     1 
ATOM   3351  C  CA    . ALA C 1 112 ? -26.874 1.457   5.287   1.00 32.79 ?  112 ALA C CA    1 
ATOM   3352  C  C     . ALA C 1 112 ? -27.952 2.353   5.893   1.00 32.68 ?  112 ALA C C     1 
ATOM   3353  O  O     . ALA C 1 112 ? -29.139 2.053   5.785   1.00 37.60 ?  112 ALA C O     1 
ATOM   3354  C  CB    . ALA C 1 112 ? -26.566 0.274   6.178   1.00 32.17 ?  112 ALA C CB    1 
ATOM   3355  N  N     . GLU C 1 113 ? -27.530 3.451   6.530   1.00 31.16 ?  113 GLU C N     1 
ATOM   3356  C  CA    . GLU C 1 113 ? -28.461 4.402   7.116   1.00 29.05 ?  113 GLU C CA    1 
ATOM   3357  C  C     . GLU C 1 113 ? -28.703 5.544   6.131   1.00 29.32 ?  113 GLU C C     1 
ATOM   3358  O  O     . GLU C 1 113 ? -29.413 6.498   6.442   1.00 27.22 ?  113 GLU C O     1 
ATOM   3359  C  CB    . GLU C 1 113 ? -27.949 4.884   8.473   1.00 30.39 ?  113 GLU C CB    1 
ATOM   3360  C  CG    . GLU C 1 113 ? -27.942 3.783   9.530   1.00 31.76 ?  113 GLU C CG    1 
ATOM   3361  C  CD    . GLU C 1 113 ? -27.176 4.115   10.798  1.00 35.50 ?  113 GLU C CD    1 
ATOM   3362  O  OE1   . GLU C 1 113 ? -26.808 5.294   10.981  1.00 39.73 ?  113 GLU C OE1   1 
ATOM   3363  O  OE2   . GLU C 1 113 ? -26.936 3.185   11.597  1.00 42.59 -1 113 GLU C OE2   1 
ATOM   3364  N  N     . GLY C 1 114 ? -28.099 5.430   4.943   1.00 28.66 ?  114 GLY C N     1 
ATOM   3365  C  CA    . GLY C 1 114 ? -28.413 6.306   3.826   1.00 24.95 ?  114 GLY C CA    1 
ATOM   3366  C  C     . GLY C 1 114 ? -27.508 7.534   3.777   1.00 26.65 ?  114 GLY C C     1 
ATOM   3367  O  O     . GLY C 1 114 ? -27.911 8.574   3.260   1.00 26.08 ?  114 GLY C O     1 
ATOM   3368  N  N     . PHE C 1 115 ? -26.284 7.416   4.304   1.00 21.81 ?  115 PHE C N     1 
ATOM   3369  C  CA    . PHE C 1 115 ? -25.370 8.546   4.297   1.00 21.47 ?  115 PHE C CA    1 
ATOM   3370  C  C     . PHE C 1 115 ? -24.243 8.296   3.298   1.00 21.04 ?  115 PHE C C     1 
ATOM   3371  O  O     . PHE C 1 115 ? -23.939 7.158   2.946   1.00 23.48 ?  115 PHE C O     1 
ATOM   3372  C  CB    . PHE C 1 115 ? -24.785 8.871   5.676   1.00 20.87 ?  115 PHE C CB    1 
ATOM   3373  C  CG    . PHE C 1 115 ? -25.816 9.186   6.752   1.00 20.90 ?  115 PHE C CG    1 
ATOM   3374  C  CD1   . PHE C 1 115 ? -26.577 10.349  6.697   1.00 21.86 ?  115 PHE C CD1   1 
ATOM   3375  C  CD2   . PHE C 1 115 ? -25.999 8.330   7.831   1.00 20.32 ?  115 PHE C CD2   1 
ATOM   3376  C  CE1   . PHE C 1 115 ? -27.510 10.631  7.683   1.00 20.28 ?  115 PHE C CE1   1 
ATOM   3377  C  CE2   . PHE C 1 115 ? -26.932 8.620   8.815   1.00 20.60 ?  115 PHE C CE2   1 
ATOM   3378  C  CZ    . PHE C 1 115 ? -27.684 9.768   8.739   1.00 20.26 ?  115 PHE C CZ    1 
ATOM   3379  N  N     . SER C 1 116 ? -23.643 9.404   2.854   1.00 19.34 ?  116 SER C N     1 
ATOM   3380  C  CA    . SER C 1 116 ? -22.500 9.406   1.957   1.00 21.78 ?  116 SER C CA    1 
ATOM   3381  C  C     . SER C 1 116 ? -21.228 9.023   2.713   1.00 24.31 ?  116 SER C C     1 
ATOM   3382  O  O     . SER C 1 116 ? -20.737 9.799   3.530   1.00 19.43 ?  116 SER C O     1 
ATOM   3383  C  CB    . SER C 1 116 ? -22.353 10.766  1.326   1.00 20.24 ?  116 SER C CB    1 
ATOM   3384  O  OG    . SER C 1 116 ? -21.223 10.817  0.467   1.00 23.09 ?  116 SER C OG    1 
ATOM   3385  N  N     . ALA C 1 117 ? -20.684 7.836   2.419   1.00 23.52 ?  117 ALA C N     1 
ATOM   3386  C  CA    . ALA C 1 117 ? -19.471 7.373   3.077   1.00 29.82 ?  117 ALA C CA    1 
ATOM   3387  C  C     . ALA C 1 117 ? -18.476 6.834   2.052   1.00 31.40 ?  117 ALA C C     1 
ATOM   3388  O  O     . ALA C 1 117 ? -18.858 6.115   1.131   1.00 31.76 ?  117 ALA C O     1 
ATOM   3389  C  CB    . ALA C 1 117 ? -19.814 6.320   4.106   1.00 32.19 ?  117 ALA C CB    1 
ATOM   3390  N  N     . LYS C 1 118 ? -17.193 7.177   2.230   1.00 30.76 ?  118 LYS C N     1 
ATOM   3391  C  CA    . LYS C 1 118 ? -16.151 6.661   1.358   1.00 27.48 ?  118 LYS C CA    1 
ATOM   3392  C  C     . LYS C 1 118 ? -14.842 6.501   2.129   1.00 24.14 ?  118 LYS C C     1 
ATOM   3393  O  O     . LYS C 1 118 ? -14.696 6.996   3.246   1.00 20.26 ?  118 LYS C O     1 
ATOM   3394  C  CB    . LYS C 1 118 ? -15.978 7.555   0.124   1.00 27.96 ?  118 LYS C CB    1 
ATOM   3395  C  CG    . LYS C 1 118 ? -15.249 8.873   0.339   1.00 28.95 ?  118 LYS C CG    1 
ATOM   3396  C  CD    . LYS C 1 118 ? -14.902 9.581   -0.965  1.00 32.25 ?  118 LYS C CD    1 
ATOM   3397  C  CE    . LYS C 1 118 ? -14.312 10.939  -0.747  1.00 36.87 ?  118 LYS C CE    1 
ATOM   3398  N  NZ    . LYS C 1 118 ? -14.424 11.774  -1.945  1.00 35.80 1  118 LYS C NZ    1 
ATOM   3399  N  N     . MET C 1 119 ? -13.900 5.783   1.510   1.00 27.24 ?  119 MET C N     1 
ATOM   3400  C  CA    . MET C 1 119 ? -12.583 5.563   2.081   1.00 25.50 ?  119 MET C CA    1 
ATOM   3401  C  C     . MET C 1 119 ? -11.529 6.047   1.091   1.00 19.55 ?  119 MET C C     1 
ATOM   3402  O  O     . MET C 1 119 ? -11.550 5.679   -0.081  1.00 17.43 ?  119 MET C O     1 
ATOM   3403  C  CB    . MET C 1 119 ? -12.354 4.080   2.398   1.00 28.58 ?  119 MET C CB    1 
ATOM   3404  C  CG    . MET C 1 119 ? -11.014 3.786   3.051   1.00 33.91 ?  119 MET C CG    1 
ATOM   3405  S  SD    . MET C 1 119 ? -10.855 2.076   3.603   1.00 37.10 ?  119 MET C SD    1 
ATOM   3406  C  CE    . MET C 1 119 ? -11.986 2.059   5.001   1.00 35.73 ?  119 MET C CE    1 
ATOM   3407  N  N     . GLU C 1 120 ? -10.622 6.891   1.587   1.00 19.21 ?  120 GLU C N     1 
ATOM   3408  C  CA    . GLU C 1 120 ? -9.505  7.384   0.801   1.00 18.98 ?  120 GLU C CA    1 
ATOM   3409  C  C     . GLU C 1 120 ? -8.260  6.607   1.211   1.00 19.72 ?  120 GLU C C     1 
ATOM   3410  O  O     . GLU C 1 120 ? -7.953  6.513   2.397   1.00 18.37 ?  120 GLU C O     1 
ATOM   3411  C  CB    . GLU C 1 120 ? -9.338  8.887   1.023   1.00 19.48 ?  120 GLU C CB    1 
ATOM   3412  C  CG    . GLU C 1 120 ? -10.409 9.726   0.333   1.00 19.85 ?  120 GLU C CG    1 
ATOM   3413  C  CD    . GLU C 1 120 ? -10.367 9.631   -1.181  1.00 19.43 ?  120 GLU C CD    1 
ATOM   3414  O  OE1   . GLU C 1 120 ? -9.263  9.790   -1.743  1.00 22.34 ?  120 GLU C OE1   1 
ATOM   3415  O  OE2   . GLU C 1 120 ? -11.429 9.406   -1.799  1.00 22.85 -1 120 GLU C OE2   1 
ATOM   3416  N  N     . PRO C 1 121 ? -7.516  6.003   0.258   1.00 20.96 ?  121 PRO C N     1 
ATOM   3417  C  CA    . PRO C 1 121 ? -6.357  5.184   0.613   1.00 20.01 ?  121 PRO C CA    1 
ATOM   3418  C  C     . PRO C 1 121 ? -5.193  6.035   1.114   1.00 18.56 ?  121 PRO C C     1 
ATOM   3419  O  O     . PRO C 1 121 ? -4.999  7.158   0.657   1.00 18.69 ?  121 PRO C O     1 
ATOM   3420  C  CB    . PRO C 1 121 ? -6.042  4.459   -0.705  1.00 21.45 ?  121 PRO C CB    1 
ATOM   3421  C  CG    . PRO C 1 121 ? -6.489  5.437   -1.770  1.00 21.72 ?  121 PRO C CG    1 
ATOM   3422  C  CD    . PRO C 1 121 ? -7.746  6.078   -1.195  1.00 21.40 ?  121 PRO C CD    1 
ATOM   3423  N  N     . GLY C 1 122 ? -4.433  5.482   2.066   1.00 20.26 ?  122 GLY C N     1 
ATOM   3424  C  CA    . GLY C 1 122 ? -3.267  6.149   2.624   1.00 20.31 ?  122 GLY C CA    1 
ATOM   3425  C  C     . GLY C 1 122 ? -2.031  5.255   2.544   1.00 19.90 ?  122 GLY C C     1 
ATOM   3426  O  O     . GLY C 1 122 ? -2.122  4.114   2.098   1.00 19.06 ?  122 GLY C O     1 
ATOM   3427  N  N     . ILE C 1 123 ? -0.878  5.789   2.969   1.00 20.02 ?  123 ILE C N     1 
ATOM   3428  C  CA    . ILE C 1 123 ? 0.362   5.027   3.012   1.00 19.97 ?  123 ILE C CA    1 
ATOM   3429  C  C     . ILE C 1 123 ? 0.384   4.191   4.289   1.00 21.71 ?  123 ILE C C     1 
ATOM   3430  O  O     . ILE C 1 123 ? 0.300   4.736   5.388   1.00 18.85 ?  123 ILE C O     1 
ATOM   3431  C  CB    . ILE C 1 123 ? 1.603   5.939   2.930   1.00 20.52 ?  123 ILE C CB    1 
ATOM   3432  C  CG1   . ILE C 1 123 ? 1.865   6.457   1.513   1.00 23.27 ?  123 ILE C CG1   1 
ATOM   3433  C  CG2   . ILE C 1 123 ? 2.836   5.231   3.490   1.00 19.76 ?  123 ILE C CG2   1 
ATOM   3434  C  CD1   . ILE C 1 123 ? 1.681   7.955   1.355   1.00 25.23 ?  123 ILE C CD1   1 
ATOM   3435  N  N     . SER C 1 124 ? 0.532   2.868   4.128   1.00 19.28 ?  124 SER C N     1 
ATOM   3436  C  CA    . SER C 1 124 ? 0.461   1.929   5.237   1.00 20.21 ?  124 SER C CA    1 
ATOM   3437  C  C     . SER C 1 124 ? 1.861   1.534   5.703   1.00 20.48 ?  124 SER C C     1 
ATOM   3438  O  O     . SER C 1 124 ? 2.858   1.897   5.084   1.00 21.36 ?  124 SER C O     1 
ATOM   3439  C  CB    . SER C 1 124 ? -0.325  0.701   4.855   1.00 21.97 ?  124 SER C CB    1 
ATOM   3440  O  OG    . SER C 1 124 ? 0.396   -0.090  3.921   1.00 20.83 ?  124 SER C OG    1 
ATOM   3441  N  N     . ALA C 1 125 ? 1.912   0.763   6.795   1.00 21.08 ?  125 ALA C N     1 
ATOM   3442  C  CA    . ALA C 1 125 ? 3.160   0.221   7.307   1.00 21.52 ?  125 ALA C CA    1 
ATOM   3443  C  C     . ALA C 1 125 ? 3.817   -0.653  6.241   1.00 21.38 ?  125 ALA C C     1 
ATOM   3444  O  O     . ALA C 1 125 ? 5.030   -0.603  6.048   1.00 22.81 ?  125 ALA C O     1 
ATOM   3445  C  CB    . ALA C 1 125 ? 2.900   -0.552  8.583   1.00 20.41 ?  125 ALA C CB    1 
ATOM   3446  N  N     . GLU C 1 126 ? 2.994   -1.450  5.551   1.00 20.64 ?  126 GLU C N     1 
ATOM   3447  C  CA    . GLU C 1 126 ? 3.445   -2.284  4.449   1.00 24.28 ?  126 GLU C CA    1 
ATOM   3448  C  C     . GLU C 1 126 ? 4.197   -1.440  3.422   1.00 25.54 ?  126 GLU C C     1 
ATOM   3449  O  O     . GLU C 1 126 ? 5.319   -1.769  3.045   1.00 28.40 ?  126 GLU C O     1 
ATOM   3450  C  CB    . GLU C 1 126 ? 2.224   -2.967  3.833   1.00 28.24 ?  126 GLU C CB    1 
ATOM   3451  C  CG    . GLU C 1 126 ? 2.522   -3.753  2.561   1.00 31.04 ?  126 GLU C CG    1 
ATOM   3452  C  CD    . GLU C 1 126 ? 1.348   -4.593  2.093   1.00 29.61 ?  126 GLU C CD    1 
ATOM   3453  O  OE1   . GLU C 1 126 ? 0.990   -5.553  2.808   1.00 28.79 ?  126 GLU C OE1   1 
ATOM   3454  O  OE2   . GLU C 1 126 ? 0.782   -4.280  1.025   1.00 33.55 -1 126 GLU C OE2   1 
ATOM   3455  N  N     . ALA C 1 127 ? 3.562   -0.353  2.970   1.00 22.52 ?  127 ALA C N     1 
ATOM   3456  C  CA    . ALA C 1 127 ? 4.121   0.498   1.932   1.00 21.29 ?  127 ALA C CA    1 
ATOM   3457  C  C     . ALA C 1 127 ? 5.472   1.060   2.370   1.00 17.47 ?  127 ALA C C     1 
ATOM   3458  O  O     . ALA C 1 127 ? 6.355   1.279   1.544   1.00 16.37 ?  127 ALA C O     1 
ATOM   3459  C  CB    . ALA C 1 127 ? 3.144   1.604   1.596   1.00 20.20 ?  127 ALA C CB    1 
ATOM   3460  N  N     . CYS C 1 128 ? 5.614   1.297   3.678   1.00 17.00 ?  128 CYS C N     1 
ATOM   3461  C  CA    . CYS C 1 128 ? 6.837   1.844   4.241   1.00 18.20 ?  128 CYS C CA    1 
ATOM   3462  C  C     . CYS C 1 128 ? 7.919   0.765   4.277   1.00 21.93 ?  128 CYS C C     1 
ATOM   3463  O  O     . CYS C 1 128 ? 9.103   1.064   4.134   1.00 22.97 ?  128 CYS C O     1 
ATOM   3464  C  CB    . CYS C 1 128 ? 6.581   2.417   5.631   1.00 20.63 ?  128 CYS C CB    1 
ATOM   3465  S  SG    . CYS C 1 128 ? 5.597   3.940   5.619   1.00 22.85 ?  128 CYS C SG    1 
ATOM   3466  N  N     . LEU C 1 129 ? 7.493   -0.491  4.453   1.00 21.01 ?  129 LEU C N     1 
ATOM   3467  C  CA    . LEU C 1 129 ? 8.408   -1.614  4.582   1.00 22.65 ?  129 LEU C CA    1 
ATOM   3468  C  C     . LEU C 1 129 ? 9.110   -1.873  3.250   1.00 25.83 ?  129 LEU C C     1 
ATOM   3469  O  O     . LEU C 1 129 ? 10.295  -2.198  3.233   1.00 22.30 ?  129 LEU C O     1 
ATOM   3470  C  CB    . LEU C 1 129 ? 7.672   -2.858  5.082   1.00 20.38 ?  129 LEU C CB    1 
ATOM   3471  C  CG    . LEU C 1 129 ? 8.529   -4.117  5.270   1.00 21.66 ?  129 LEU C CG    1 
ATOM   3472  C  CD1   . LEU C 1 129 ? 7.924   -5.047  6.309   1.00 20.59 ?  129 LEU C CD1   1 
ATOM   3473  C  CD2   . LEU C 1 129 ? 8.721   -4.869  3.963   1.00 21.72 ?  129 LEU C CD2   1 
ATOM   3474  N  N     . TRP C 1 130 ? 8.382   -1.733  2.136   1.00 24.98 ?  130 TRP C N     1 
ATOM   3475  C  CA    . TRP C 1 130 ? 8.974   -1.969  0.828   1.00 21.20 ?  130 TRP C CA    1 
ATOM   3476  C  C     . TRP C 1 130 ? 10.088  -0.954  0.572   1.00 19.92 ?  130 TRP C C     1 
ATOM   3477  O  O     . TRP C 1 130 ? 11.140  -1.312  0.047   1.00 20.48 ?  130 TRP C O     1 
ATOM   3478  C  CB    . TRP C 1 130 ? 7.920   -1.915  -0.288  1.00 20.82 ?  130 TRP C CB    1 
ATOM   3479  C  CG    . TRP C 1 130 ? 6.757   -2.854  -0.104  1.00 20.23 ?  130 TRP C CG    1 
ATOM   3480  C  CD1   . TRP C 1 130 ? 5.442   -2.541  -0.286  1.00 19.79 ?  130 TRP C CD1   1 
ATOM   3481  C  CD2   . TRP C 1 130 ? 6.789   -4.251  0.269   1.00 22.38 ?  130 TRP C CD2   1 
ATOM   3482  N  NE1   . TRP C 1 130 ? 4.654   -3.631  -0.036  1.00 20.70 ?  130 TRP C NE1   1 
ATOM   3483  C  CE2   . TRP C 1 130 ? 5.448   -4.694  0.302   1.00 20.87 ?  130 TRP C CE2   1 
ATOM   3484  C  CE3   . TRP C 1 130 ? 7.803   -5.164  0.582   1.00 21.02 ?  130 TRP C CE3   1 
ATOM   3485  C  CZ2   . TRP C 1 130 ? 5.102   -6.002  0.632   1.00 20.73 ?  130 TRP C CZ2   1 
ATOM   3486  C  CZ3   . TRP C 1 130 ? 7.459   -6.457  0.907   1.00 21.55 ?  130 TRP C CZ3   1 
ATOM   3487  C  CH2   . TRP C 1 130 ? 6.128   -6.869  0.931   1.00 21.19 ?  130 TRP C CH2   1 
ATOM   3488  N  N     . ALA C 1 131 ? 9.850   0.309   0.953   1.00 20.03 ?  131 ALA C N     1 
ATOM   3489  C  CA    . ALA C 1 131 ? 10.761  1.399   0.635   1.00 15.78 ?  131 ALA C CA    1 
ATOM   3490  C  C     . ALA C 1 131 ? 11.973  1.401   1.567   1.00 15.43 ?  131 ALA C C     1 
ATOM   3491  O  O     . ALA C 1 131 ? 13.080  1.711   1.135   1.00 11.84 ?  131 ALA C O     1 
ATOM   3492  C  CB    . ALA C 1 131 ? 10.023  2.721   0.689   1.00 16.31 ?  131 ALA C CB    1 
ATOM   3493  N  N     . ASP C 1 132 ? 11.755  1.073   2.846   1.00 16.23 ?  132 ASP C N     1 
ATOM   3494  C  CA    . ASP C 1 132 ? 12.816  1.093   3.842   1.00 17.15 ?  132 ASP C CA    1 
ATOM   3495  C  C     . ASP C 1 132 ? 13.773  -0.072  3.601   1.00 18.74 ?  132 ASP C C     1 
ATOM   3496  O  O     . ASP C 1 132 ? 14.989  0.092   3.667   1.00 19.62 ?  132 ASP C O     1 
ATOM   3497  C  CB    . ASP C 1 132 ? 12.255  1.050   5.256   1.00 16.35 ?  132 ASP C CB    1 
ATOM   3498  C  CG    . ASP C 1 132 ? 11.714  2.367   5.796   1.00 17.18 ?  132 ASP C CG    1 
ATOM   3499  O  OD1   . ASP C 1 132 ? 12.069  3.424   5.236   1.00 19.45 ?  132 ASP C OD1   1 
ATOM   3500  O  OD2   . ASP C 1 132 ? 10.935  2.325   6.770   1.00 21.99 -1 132 ASP C OD2   1 
ATOM   3501  N  N     . LEU C 1 133 ? 13.207  -1.252  3.330   1.00 20.04 ?  133 LEU C N     1 
ATOM   3502  C  CA    . LEU C 1 133 ? 13.995  -2.461  3.152   1.00 24.18 ?  133 LEU C CA    1 
ATOM   3503  C  C     . LEU C 1 133 ? 14.453  -2.586  1.701   1.00 25.48 ?  133 LEU C C     1 
ATOM   3504  O  O     . LEU C 1 133 ? 15.308  -3.412  1.394   1.00 25.97 ?  133 LEU C O     1 
ATOM   3505  C  CB    . LEU C 1 133 ? 13.181  -3.677  3.591   1.00 24.66 ?  133 LEU C CB    1 
ATOM   3506  C  CG    . LEU C 1 133 ? 13.198  -3.986  5.092   1.00 26.17 ?  133 LEU C CG    1 
ATOM   3507  C  CD1   . LEU C 1 133 ? 13.004  -2.736  5.933   1.00 24.41 ?  133 LEU C CD1   1 
ATOM   3508  C  CD2   . LEU C 1 133 ? 12.136  -5.019  5.419   1.00 28.30 ?  133 LEU C CD2   1 
ATOM   3509  N  N     . GLY C 1 134 ? 13.881  -1.763  0.816   1.00 28.01 ?  134 GLY C N     1 
ATOM   3510  C  CA    . GLY C 1 134 ? 14.214  -1.820  -0.598  1.00 27.39 ?  134 GLY C CA    1 
ATOM   3511  C  C     . GLY C 1 134 ? 13.856  -3.181  -1.191  1.00 27.78 ?  134 GLY C C     1 
ATOM   3512  O  O     . GLY C 1 134 ? 14.636  -3.763  -1.943  1.00 23.02 ?  134 GLY C O     1 
ATOM   3513  N  N     . ILE C 1 135 ? 12.666  -3.671  -0.827  1.00 26.27 ?  135 ILE C N     1 
ATOM   3514  C  CA    . ILE C 1 135 ? 12.126  -4.921  -1.338  1.00 23.71 ?  135 ILE C CA    1 
ATOM   3515  C  C     . ILE C 1 135 ? 10.903  -4.598  -2.190  1.00 24.13 ?  135 ILE C C     1 
ATOM   3516  O  O     . ILE C 1 135 ? 10.125  -3.709  -1.848  1.00 26.80 ?  135 ILE C O     1 
ATOM   3517  C  CB    . ILE C 1 135 ? 11.765  -5.875  -0.184  1.00 25.49 ?  135 ILE C CB    1 
ATOM   3518  C  CG1   . ILE C 1 135 ? 12.989  -6.239  0.658   1.00 25.92 ?  135 ILE C CG1   1 
ATOM   3519  C  CG2   . ILE C 1 135 ? 11.045  -7.120  -0.705  1.00 25.52 ?  135 ILE C CG2   1 
ATOM   3520  C  CD1   . ILE C 1 135 ? 12.676  -7.110  1.862   1.00 27.49 ?  135 ILE C CD1   1 
ATOM   3521  N  N     . ASP C 1 136 ? 10.743  -5.324  -3.299  1.00 19.71 ?  136 ASP C N     1 
ATOM   3522  C  CA    . ASP C 1 136 ? 9.590   -5.148  -4.166  1.00 19.20 ?  136 ASP C CA    1 
ATOM   3523  C  C     . ASP C 1 136 ? 8.665   -6.349  -3.993  1.00 20.31 ?  136 ASP C C     1 
ATOM   3524  O  O     . ASP C 1 136 ? 9.074   -7.481  -4.244  1.00 21.32 ?  136 ASP C O     1 
ATOM   3525  C  CB    . ASP C 1 136 ? 10.027  -4.940  -5.607  1.00 17.55 ?  136 ASP C CB    1 
ATOM   3526  C  CG    . ASP C 1 136 ? 8.904   -4.858  -6.630  1.00 15.65 ?  136 ASP C CG    1 
ATOM   3527  O  OD1   . ASP C 1 136 ? 7.764   -5.230  -6.281  1.00 14.58 ?  136 ASP C OD1   1 
ATOM   3528  O  OD2   . ASP C 1 136 ? 9.181   -4.416  -7.764  1.00 14.95 -1 136 ASP C OD2   1 
ATOM   3529  N  N     . PRO C 1 137 ? 7.397   -6.161  -3.562  1.00 19.20 ?  137 PRO C N     1 
ATOM   3530  C  CA    . PRO C 1 137 ? 6.523   -7.301  -3.278  1.00 18.85 ?  137 PRO C CA    1 
ATOM   3531  C  C     . PRO C 1 137 ? 6.272   -8.176  -4.504  1.00 20.53 ?  137 PRO C C     1 
ATOM   3532  O  O     . PRO C 1 137 ? 5.798   -9.303  -4.377  1.00 19.36 ?  137 PRO C O     1 
ATOM   3533  C  CB    . PRO C 1 137 ? 5.238   -6.627  -2.768  1.00 16.81 ?  137 PRO C CB    1 
ATOM   3534  C  CG    . PRO C 1 137 ? 5.261   -5.271  -3.431  1.00 17.47 ?  137 PRO C CG    1 
ATOM   3535  C  CD    . PRO C 1 137 ? 6.726   -4.866  -3.359  1.00 17.31 ?  137 PRO C CD    1 
ATOM   3536  N  N     . GLY C 1 138 ? 6.594   -7.643  -5.688  1.00 23.23 ?  138 GLY C N     1 
ATOM   3537  C  CA    . GLY C 1 138 ? 6.379   -8.361  -6.935  1.00 23.12 ?  138 GLY C CA    1 
ATOM   3538  C  C     . GLY C 1 138 ? 7.597   -9.194  -7.330  1.00 24.59 ?  138 GLY C C     1 
ATOM   3539  O  O     . GLY C 1 138 ? 7.555   -9.926  -8.317  1.00 22.15 ?  138 GLY C O     1 
ATOM   3540  N  N     . ASN C 1 139 ? 8.677   -9.082  -6.547  1.00 23.86 ?  139 ASN C N     1 
ATOM   3541  C  CA    . ASN C 1 139 ? 9.933   -9.735  -6.880  1.00 24.74 ?  139 ASN C CA    1 
ATOM   3542  C  C     . ASN C 1 139 ? 9.742   -11.249 -6.856  1.00 24.53 ?  139 ASN C C     1 
ATOM   3543  O  O     . ASN C 1 139 ? 9.997   -11.926 -7.849  1.00 27.20 ?  139 ASN C O     1 
ATOM   3544  C  CB    . ASN C 1 139 ? 11.062  -9.307  -5.950  1.00 25.65 ?  139 ASN C CB    1 
ATOM   3545  C  CG    . ASN C 1 139 ? 12.420  -9.621  -6.532  1.00 25.77 ?  139 ASN C CG    1 
ATOM   3546  O  OD1   . ASN C 1 139 ? 13.189  -10.388 -5.943  1.00 23.80 ?  139 ASN C OD1   1 
ATOM   3547  N  ND2   . ASN C 1 139 ? 12.730  -9.046  -7.684  1.00 28.88 ?  139 ASN C ND2   1 
ATOM   3548  N  N     . SER C 1 140 ? 9.301   -11.771 -5.707  1.00 25.34 ?  140 SER C N     1 
ATOM   3549  C  CA    . SER C 1 140 ? 8.990   -13.185 -5.586  1.00 27.38 ?  140 SER C CA    1 
ATOM   3550  C  C     . SER C 1 140 ? 7.609   -13.356 -4.963  1.00 22.67 ?  140 SER C C     1 
ATOM   3551  O  O     . SER C 1 140 ? 7.275   -14.432 -4.472  1.00 19.17 ?  140 SER C O     1 
ATOM   3552  C  CB    . SER C 1 140 ? 10.043  -13.917 -4.791  1.00 32.43 ?  140 SER C CB    1 
ATOM   3553  O  OG    . SER C 1 140 ? 10.047  -13.499 -3.432  1.00 30.66 ?  140 SER C OG    1 
ATOM   3554  N  N     . GLY C 1 141 ? 6.817   -12.280 -4.990  1.00 19.90 ?  141 GLY C N     1 
ATOM   3555  C  CA    . GLY C 1 141 ? 5.466   -12.311 -4.456  1.00 21.10 ?  141 GLY C CA    1 
ATOM   3556  C  C     . GLY C 1 141 ? 5.428   -11.837 -3.007  1.00 23.35 ?  141 GLY C C     1 
ATOM   3557  O  O     . GLY C 1 141 ? 6.466   -11.574 -2.402  1.00 19.65 ?  141 GLY C O     1 
ATOM   3558  N  N     . HIS C 1 142 ? 4.208   -11.750 -2.465  1.00 22.84 ?  142 HIS C N     1 
ATOM   3559  C  CA    . HIS C 1 142 ? 3.981   -11.187 -1.147  1.00 24.07 ?  142 HIS C CA    1 
ATOM   3560  C  C     . HIS C 1 142 ? 2.733   -11.807 -0.527  1.00 21.46 ?  142 HIS C C     1 
ATOM   3561  O  O     . HIS C 1 142 ? 1.713   -11.971 -1.194  1.00 21.37 ?  142 HIS C O     1 
ATOM   3562  C  CB    . HIS C 1 142 ? 3.852   -9.663  -1.242  1.00 30.62 ?  142 HIS C CB    1 
ATOM   3563  C  CG    . HIS C 1 142 ? 3.119   -9.042  -0.101  1.00 36.02 ?  142 HIS C CG    1 
ATOM   3564  N  ND1   . HIS C 1 142 ? 2.173   -8.058  -0.290  1.00 40.49 ?  142 HIS C ND1   1 
ATOM   3565  C  CD2   . HIS C 1 142 ? 3.162   -9.267  1.219   1.00 39.75 ?  142 HIS C CD2   1 
ATOM   3566  C  CE1   . HIS C 1 142 ? 1.678   -7.697  0.885   1.00 38.56 ?  142 HIS C CE1   1 
ATOM   3567  N  NE2   . HIS C 1 142 ? 2.265   -8.418  1.815   1.00 41.77 ?  142 HIS C NE2   1 
ATOM   3568  N  N     . GLN C 1 143 ? 2.843   -12.149 0.760   1.00 21.98 ?  143 GLN C N     1 
ATOM   3569  C  CA    . GLN C 1 143 ? 1.704   -12.560 1.563   1.00 20.39 ?  143 GLN C CA    1 
ATOM   3570  C  C     . GLN C 1 143 ? 1.707   -11.771 2.867   1.00 19.00 ?  143 GLN C C     1 
ATOM   3571  O  O     . GLN C 1 143 ? 2.765   -11.480 3.422   1.00 19.38 ?  143 GLN C O     1 
ATOM   3572  C  CB    . GLN C 1 143 ? 1.746   -14.050 1.896   1.00 19.60 ?  143 GLN C CB    1 
ATOM   3573  C  CG    . GLN C 1 143 ? 1.822   -14.955 0.673   1.00 22.20 ?  143 GLN C CG    1 
ATOM   3574  C  CD    . GLN C 1 143 ? 1.928   -16.420 1.032   1.00 23.39 ?  143 GLN C CD    1 
ATOM   3575  O  OE1   . GLN C 1 143 ? 2.833   -16.841 1.761   1.00 21.66 ?  143 GLN C OE1   1 
ATOM   3576  N  NE2   . GLN C 1 143 ? 0.990   -17.211 0.533   1.00 26.13 ?  143 GLN C NE2   1 
ATOM   3577  N  N     . SER C 1 144 ? 0.501   -11.441 3.339   1.00 15.53 ?  144 SER C N     1 
ATOM   3578  C  CA    . SER C 1 144 ? 0.316   -10.780 4.618   1.00 16.84 ?  144 SER C CA    1 
ATOM   3579  C  C     . SER C 1 144 ? -0.829  -11.449 5.372   1.00 15.79 ?  144 SER C C     1 
ATOM   3580  O  O     . SER C 1 144 ? -1.893  -11.694 4.810   1.00 16.80 ?  144 SER C O     1 
ATOM   3581  C  CB    . SER C 1 144 ? 0.065   -9.302  4.445   1.00 17.01 ?  144 SER C CB    1 
ATOM   3582  O  OG    . SER C 1 144 ? 1.242   -8.628  4.020   1.00 17.61 ?  144 SER C OG    1 
ATOM   3583  N  N     . PHE C 1 145 ? -0.580  -11.746 6.650   1.00 15.47 ?  145 PHE C N     1 
ATOM   3584  C  CA    . PHE C 1 145 ? -1.586  -12.306 7.535   1.00 16.27 ?  145 PHE C CA    1 
ATOM   3585  C  C     . PHE C 1 145 ? -1.409  -11.675 8.907   1.00 15.13 ?  145 PHE C C     1 
ATOM   3586  O  O     . PHE C 1 145 ? -0.327  -11.198 9.241   1.00 15.36 ?  145 PHE C O     1 
ATOM   3587  C  CB    . PHE C 1 145 ? -1.479  -13.818 7.749   1.00 19.17 ?  145 PHE C CB    1 
ATOM   3588  C  CG    . PHE C 1 145 ? -1.405  -14.643 6.474   1.00 21.58 ?  145 PHE C CG    1 
ATOM   3589  C  CD1   . PHE C 1 145 ? -0.193  -14.828 5.821   1.00 22.03 ?  145 PHE C CD1   1 
ATOM   3590  C  CD2   . PHE C 1 145 ? -2.543  -15.236 5.940   1.00 22.90 ?  145 PHE C CD2   1 
ATOM   3591  C  CE1   . PHE C 1 145 ? -0.125  -15.581 4.660   1.00 24.32 ?  145 PHE C CE1   1 
ATOM   3592  C  CE2   . PHE C 1 145 ? -2.468  -15.989 4.779   1.00 23.52 ?  145 PHE C CE2   1 
ATOM   3593  C  CZ    . PHE C 1 145 ? -1.261  -16.159 4.142   1.00 24.18 ?  145 PHE C CZ    1 
ATOM   3594  N  N     . GLU C 1 146 ? -2.474  -11.711 9.706   1.00 16.82 ?  146 GLU C N     1 
ATOM   3595  C  CA    . GLU C 1 146 ? -2.397  -11.218 11.066  1.00 19.19 ?  146 GLU C CA    1 
ATOM   3596  C  C     . GLU C 1 146 ? -1.843  -12.343 11.932  1.00 17.80 ?  146 GLU C C     1 
ATOM   3597  O  O     . GLU C 1 146 ? -2.359  -13.459 11.905  1.00 21.25 ?  146 GLU C O     1 
ATOM   3598  C  CB    . GLU C 1 146 ? -3.762  -10.693 11.510  1.00 17.57 ?  146 GLU C CB    1 
ATOM   3599  C  CG    . GLU C 1 146 ? -3.691  -9.857  12.784  1.00 18.42 ?  146 GLU C CG    1 
ATOM   3600  C  CD    . GLU C 1 146 ? -3.994  -10.605 14.068  1.00 17.67 ?  146 GLU C CD    1 
ATOM   3601  O  OE1   . GLU C 1 146 ? -4.513  -11.739 14.002  1.00 14.38 ?  146 GLU C OE1   1 
ATOM   3602  O  OE2   . GLU C 1 146 ? -3.715  -10.037 15.144  1.00 18.19 -1 146 GLU C OE2   1 
ATOM   3603  N  N     . ALA C 1 147 ? -0.776  -12.048 12.678  1.00 16.99 ?  147 ALA C N     1 
ATOM   3604  C  CA    . ALA C 1 147 ? -0.031  -13.096 13.355  1.00 19.49 ?  147 ALA C CA    1 
ATOM   3605  C  C     . ALA C 1 147 ? -0.997  -14.070 14.029  1.00 19.22 ?  147 ALA C C     1 
ATOM   3606  O  O     . ALA C 1 147 ? -0.898  -15.276 13.823  1.00 21.42 ?  147 ALA C O     1 
ATOM   3607  C  CB    . ALA C 1 147 ? 0.961   -12.499 14.331  1.00 18.58 ?  147 ALA C CB    1 
ATOM   3608  N  N     . SER C 1 148 ? -1.947  -13.544 14.812  1.00 20.28 ?  148 SER C N     1 
ATOM   3609  C  CA    . SER C 1 148 ? -2.838  -14.386 15.598  1.00 22.79 ?  148 SER C CA    1 
ATOM   3610  C  C     . SER C 1 148 ? -3.791  -15.180 14.706  1.00 22.85 ?  148 SER C C     1 
ATOM   3611  O  O     . SER C 1 148 ? -4.109  -16.326 15.018  1.00 20.18 ?  148 SER C O     1 
ATOM   3612  C  CB    . SER C 1 148 ? -3.598  -13.584 16.628  1.00 21.17 ?  148 SER C CB    1 
ATOM   3613  O  OG    . SER C 1 148 ? -2.762  -13.256 17.729  1.00 19.55 ?  148 SER C OG    1 
ATOM   3614  N  N     . GLN C 1 149 ? -4.256  -14.577 13.606  1.00 21.83 ?  149 GLN C N     1 
ATOM   3615  C  CA    . GLN C 1 149 ? -5.164  -15.269 12.704  1.00 27.25 ?  149 GLN C CA    1 
ATOM   3616  C  C     . GLN C 1 149 ? -4.431  -16.439 12.051  1.00 24.31 ?  149 GLN C C     1 
ATOM   3617  O  O     . GLN C 1 149 ? -5.030  -17.476 11.777  1.00 25.51 ?  149 GLN C O     1 
ATOM   3618  C  CB    . GLN C 1 149 ? -5.746  -14.348 11.630  1.00 29.07 ?  149 GLN C CB    1 
ATOM   3619  C  CG    . GLN C 1 149 ? -6.786  -15.029 10.746  1.00 30.03 ?  149 GLN C CG    1 
ATOM   3620  C  CD    . GLN C 1 149 ? -7.041  -14.299 9.446   1.00 31.69 ?  149 GLN C CD    1 
ATOM   3621  O  OE1   . GLN C 1 149 ? -6.734  -14.797 8.357   1.00 27.78 ?  149 GLN C OE1   1 
ATOM   3622  N  NE2   . GLN C 1 149 ? -7.598  -13.101 9.546   1.00 32.15 ?  149 GLN C NE2   1 
ATOM   3623  N  N     . PHE C 1 150 ? -3.129  -16.255 11.805  1.00 25.91 ?  150 PHE C N     1 
ATOM   3624  C  CA    . PHE C 1 150 ? -2.290  -17.285 11.213  1.00 27.27 ?  150 PHE C CA    1 
ATOM   3625  C  C     . PHE C 1 150 ? -2.085  -18.417 12.218  1.00 26.49 ?  150 PHE C C     1 
ATOM   3626  O  O     . PHE C 1 150 ? -1.831  -19.555 11.832  1.00 23.29 ?  150 PHE C O     1 
ATOM   3627  C  CB    . PHE C 1 150 ? -0.967  -16.643 10.780  1.00 28.94 ?  150 PHE C CB    1 
ATOM   3628  C  CG    . PHE C 1 150 ? 0.058   -17.589 10.166  1.00 31.27 ?  150 PHE C CG    1 
ATOM   3629  C  CD1   . PHE C 1 150 ? 0.911   -18.337 10.970  1.00 26.66 ?  150 PHE C CD1   1 
ATOM   3630  C  CD2   . PHE C 1 150 ? 0.182   -17.708 8.786   1.00 33.01 ?  150 PHE C CD2   1 
ATOM   3631  C  CE1   . PHE C 1 150 ? 1.850   -19.189 10.408  1.00 28.42 ?  150 PHE C CE1   1 
ATOM   3632  C  CE2   . PHE C 1 150 ? 1.123   -18.562 8.230   1.00 32.59 ?  150 PHE C CE2   1 
ATOM   3633  C  CZ    . PHE C 1 150 ? 1.954   -19.299 9.041   1.00 30.21 ?  150 PHE C CZ    1 
ATOM   3634  N  N     . MET C 1 151 ? -2.200  -18.088 13.509  1.00 28.84 ?  151 MET C N     1 
ATOM   3635  C  CA    . MET C 1 151 ? -1.958  -19.048 14.574  1.00 30.85 ?  151 MET C CA    1 
ATOM   3636  C  C     . MET C 1 151 ? -3.253  -19.766 14.947  1.00 34.33 ?  151 MET C C     1 
ATOM   3637  O  O     . MET C 1 151 ? -3.215  -20.849 15.526  1.00 41.81 ?  151 MET C O     1 
ATOM   3638  C  CB    . MET C 1 151 ? -1.392  -18.367 15.826  1.00 26.82 ?  151 MET C CB    1 
ATOM   3639  C  CG    . MET C 1 151 ? 0.079   -18.014 15.729  1.00 28.71 ?  151 MET C CG    1 
ATOM   3640  S  SD    . MET C 1 151 ? 0.757   -17.425 17.294  1.00 31.24 ?  151 MET C SD    1 
ATOM   3641  C  CE    . MET C 1 151 ? 0.554   -18.848 18.373  1.00 32.16 ?  151 MET C CE    1 
ATOM   3642  N  N     . PHE C 1 152 ? -4.394  -19.158 14.606  1.00 35.87 ?  152 PHE C N     1 
ATOM   3643  C  CA    . PHE C 1 152 ? -5.680  -19.636 15.089  1.00 37.34 ?  152 PHE C CA    1 
ATOM   3644  C  C     . PHE C 1 152 ? -6.369  -20.487 14.024  1.00 40.00 ?  152 PHE C C     1 
ATOM   3645  O  O     . PHE C 1 152 ? -7.084  -21.430 14.354  1.00 44.91 ?  152 PHE C O     1 
ATOM   3646  C  CB    . PHE C 1 152 ? -6.536  -18.443 15.522  1.00 36.09 ?  152 PHE C CB    1 
ATOM   3647  C  CG    . PHE C 1 152 ? -6.038  -17.740 16.778  1.00 38.14 ?  152 PHE C CG    1 
ATOM   3648  C  CD1   . PHE C 1 152 ? -5.224  -18.401 17.692  1.00 37.04 ?  152 PHE C CD1   1 
ATOM   3649  C  CD2   . PHE C 1 152 ? -6.396  -16.424 17.049  1.00 36.18 ?  152 PHE C CD2   1 
ATOM   3650  C  CE1   . PHE C 1 152 ? -4.775  -17.760 18.836  1.00 36.35 ?  152 PHE C CE1   1 
ATOM   3651  C  CE2   . PHE C 1 152 ? -5.946  -15.789 18.196  1.00 36.99 ?  152 PHE C CE2   1 
ATOM   3652  C  CZ    . PHE C 1 152 ? -5.136  -16.457 19.085  1.00 34.45 ?  152 PHE C CZ    1 
ATOM   3653  N  N     . PHE C 1 153 ? -6.154  -20.143 12.751  1.00 37.54 ?  153 PHE C N     1 
ATOM   3654  C  CA    . PHE C 1 153 ? -6.798  -20.843 11.652  1.00 36.55 ?  153 PHE C CA    1 
ATOM   3655  C  C     . PHE C 1 153 ? -5.717  -21.406 10.735  1.00 33.06 ?  153 PHE C C     1 
ATOM   3656  O  O     . PHE C 1 153 ? -4.529  -21.248 11.005  1.00 30.64 ?  153 PHE C O     1 
ATOM   3657  C  CB    . PHE C 1 153 ? -7.762  -19.883 10.947  1.00 38.06 ?  153 PHE C CB    1 
ATOM   3658  C  CG    . PHE C 1 153 ? -8.704  -19.141 11.886  1.00 36.14 ?  153 PHE C CG    1 
ATOM   3659  C  CD1   . PHE C 1 153 ? -9.864  -19.744 12.359  1.00 37.87 ?  153 PHE C CD1   1 
ATOM   3660  C  CD2   . PHE C 1 153 ? -8.430  -17.839 12.291  1.00 38.70 ?  153 PHE C CD2   1 
ATOM   3661  C  CE1   . PHE C 1 153 ? -10.719 -19.066 13.213  1.00 38.43 ?  153 PHE C CE1   1 
ATOM   3662  C  CE2   . PHE C 1 153 ? -9.289  -17.165 13.145  1.00 37.12 ?  153 PHE C CE2   1 
ATOM   3663  C  CZ    . PHE C 1 153 ? -10.431 -17.779 13.603  1.00 37.87 ?  153 PHE C CZ    1 
ATOM   3664  N  N     . ASN C 1 154 ? -6.136  -22.057 9.646   1.00 33.14 ?  154 ASN C N     1 
ATOM   3665  C  CA    . ASN C 1 154 ? -5.195  -22.750 8.783   1.00 37.60 ?  154 ASN C CA    1 
ATOM   3666  C  C     . ASN C 1 154 ? -4.818  -21.859 7.605   1.00 39.04 ?  154 ASN C C     1 
ATOM   3667  O  O     . ASN C 1 154 ? -5.621  -21.615 6.708   1.00 35.33 ?  154 ASN C O     1 
ATOM   3668  C  CB    . ASN C 1 154 ? -5.720  -24.125 8.390   1.00 40.91 ?  154 ASN C CB    1 
ATOM   3669  C  CG    . ASN C 1 154 ? -5.563  -25.106 9.528   1.00 43.05 ?  154 ASN C CG    1 
ATOM   3670  O  OD1   . ASN C 1 154 ? -4.445  -25.322 10.009  1.00 45.59 ?  154 ASN C OD1   1 
ATOM   3671  N  ND2   . ASN C 1 154 ? -6.661  -25.690 9.985   1.00 44.48 ?  154 ASN C ND2   1 
ATOM   3672  N  N     . HIS C 1 155 ? -3.569  -21.385 7.640   1.00 37.65 ?  155 HIS C N     1 
ATOM   3673  C  CA    . HIS C 1 155 ? -3.028  -20.546 6.588   1.00 38.88 ?  155 HIS C CA    1 
ATOM   3674  C  C     . HIS C 1 155 ? -1.728  -21.160 6.086   1.00 39.93 ?  155 HIS C C     1 
ATOM   3675  O  O     . HIS C 1 155 ? -0.811  -21.423 6.861   1.00 45.15 ?  155 HIS C O     1 
ATOM   3676  C  CB    . HIS C 1 155 ? -2.860  -19.104 7.077   1.00 40.23 ?  155 HIS C CB    1 
ATOM   3677  C  CG    . HIS C 1 155 ? -4.145  -18.347 7.123   1.00 39.71 ?  155 HIS C CG    1 
ATOM   3678  N  ND1   . HIS C 1 155 ? -4.691  -17.756 6.004   1.00 43.66 ?  155 HIS C ND1   1 
ATOM   3679  C  CD2   . HIS C 1 155 ? -4.996  -18.099 8.126   1.00 38.92 ?  155 HIS C CD2   1 
ATOM   3680  C  CE1   . HIS C 1 155 ? -5.830  -17.164 6.334   1.00 40.12 ?  155 HIS C CE1   1 
ATOM   3681  N  NE2   . HIS C 1 155 ? -6.034  -17.359 7.618   1.00 37.74 ?  155 HIS C NE2   1 
ATOM   3682  N  N     . VAL C 1 156 ? -1.676  -21.387 4.772   1.00 34.60 ?  156 VAL C N     1 
ATOM   3683  C  CA    . VAL C 1 156 ? -0.530  -22.014 4.143   1.00 32.92 ?  156 VAL C CA    1 
ATOM   3684  C  C     . VAL C 1 156 ? 0.262   -20.939 3.409   1.00 28.75 ?  156 VAL C C     1 
ATOM   3685  O  O     . VAL C 1 156 ? -0.216  -20.377 2.425   1.00 21.11 ?  156 VAL C O     1 
ATOM   3686  C  CB    . VAL C 1 156 ? -0.984  -23.137 3.193   1.00 34.34 ?  156 VAL C CB    1 
ATOM   3687  C  CG1   . VAL C 1 156 ? 0.195   -23.787 2.481   1.00 34.20 ?  156 VAL C CG1   1 
ATOM   3688  C  CG2   . VAL C 1 156 ? -1.822  -24.184 3.919   1.00 33.91 ?  156 VAL C CG2   1 
ATOM   3689  N  N     . PRO C 1 157 ? 1.492   -20.615 3.869   1.00 30.19 ?  157 PRO C N     1 
ATOM   3690  C  CA    . PRO C 1 157 ? 2.314   -19.602 3.213   1.00 27.75 ?  157 PRO C CA    1 
ATOM   3691  C  C     . PRO C 1 157 ? 3.087   -20.186 2.034   1.00 25.64 ?  157 PRO C C     1 
ATOM   3692  O  O     . PRO C 1 157 ? 3.363   -21.383 2.000   1.00 26.98 ?  157 PRO C O     1 
ATOM   3693  C  CB    . PRO C 1 157 ? 3.232   -19.163 4.360   1.00 27.83 ?  157 PRO C CB    1 
ATOM   3694  C  CG    . PRO C 1 157 ? 3.471   -20.444 5.133   1.00 29.01 ?  157 PRO C CG    1 
ATOM   3695  C  CD    . PRO C 1 157 ? 2.160   -21.217 5.035   1.00 30.12 ?  157 PRO C CD    1 
ATOM   3696  N  N     . ASP C 1 158 ? 3.422   -19.320 1.073   1.00 23.94 ?  158 ASP C N     1 
ATOM   3697  C  CA    . ASP C 1 158 ? 4.250   -19.692 -0.063  1.00 22.36 ?  158 ASP C CA    1 
ATOM   3698  C  C     . ASP C 1 158 ? 5.690   -19.287 0.240   1.00 22.20 ?  158 ASP C C     1 
ATOM   3699  O  O     . ASP C 1 158 ? 6.019   -18.103 0.213   1.00 20.37 ?  158 ASP C O     1 
ATOM   3700  C  CB    . ASP C 1 158 ? 3.718   -19.073 -1.347  1.00 20.14 ?  158 ASP C CB    1 
ATOM   3701  C  CG    . ASP C 1 158 ? 4.597   -19.242 -2.578  1.00 18.62 ?  158 ASP C CG    1 
ATOM   3702  O  OD1   . ASP C 1 158 ? 5.740   -19.724 -2.423  1.00 18.14 ?  158 ASP C OD1   1 
ATOM   3703  O  OD2   . ASP C 1 158 ? 4.130   -18.894 -3.685  1.00 15.19 -1 158 ASP C OD2   1 
ATOM   3704  N  N     . PRO C 1 159 ? 6.590   -20.256 0.527   1.00 20.73 ?  159 PRO C N     1 
ATOM   3705  C  CA    . PRO C 1 159 ? 7.914   -19.945 1.073   1.00 20.77 ?  159 PRO C CA    1 
ATOM   3706  C  C     . PRO C 1 159 ? 8.899   -19.347 0.071   1.00 20.75 ?  159 PRO C C     1 
ATOM   3707  O  O     . PRO C 1 159 ? 10.074  -19.166 0.384   1.00 21.08 ?  159 PRO C O     1 
ATOM   3708  C  CB    . PRO C 1 159 ? 8.383   -21.310 1.616   1.00 22.08 ?  159 PRO C CB    1 
ATOM   3709  C  CG    . PRO C 1 159 ? 7.698   -22.327 0.730   1.00 20.65 ?  159 PRO C CG    1 
ATOM   3710  C  CD    . PRO C 1 159 ? 6.369   -21.700 0.340   1.00 21.70 ?  159 PRO C CD    1 
ATOM   3711  N  N     . THR C 1 160 ? 8.399   -19.039 -1.131  1.00 17.76 ?  160 THR C N     1 
ATOM   3712  C  CA    . THR C 1 160 ? 9.154   -18.290 -2.121  1.00 17.77 ?  160 THR C CA    1 
ATOM   3713  C  C     . THR C 1 160 ? 8.865   -16.794 -1.991  1.00 18.87 ?  160 THR C C     1 
ATOM   3714  O  O     . THR C 1 160 ? 9.583   -15.981 -2.571  1.00 23.85 ?  160 THR C O     1 
ATOM   3715  C  CB    . THR C 1 160 ? 8.807   -18.807 -3.517  1.00 18.13 ?  160 THR C CB    1 
ATOM   3716  O  OG1   . THR C 1 160 ? 7.386   -18.784 -3.603  1.00 16.30 ?  160 THR C OG1   1 
ATOM   3717  C  CG2   . THR C 1 160 ? 9.304   -20.221 -3.756  1.00 18.05 ?  160 THR C CG2   1 
ATOM   3718  N  N     . THR C 1 161 ? 7.827   -16.423 -1.228  1.00 16.49 ?  161 THR C N     1 
ATOM   3719  C  CA    . THR C 1 161 ? 7.403   -15.030 -1.160  1.00 17.86 ?  161 THR C CA    1 
ATOM   3720  C  C     . THR C 1 161 ? 7.955   -14.370 0.100   1.00 18.93 ?  161 THR C C     1 
ATOM   3721  O  O     . THR C 1 161 ? 8.397   -15.050 1.023   1.00 27.01 ?  161 THR C O     1 
ATOM   3722  C  CB    . THR C 1 161 ? 5.878   -14.932 -1.187  1.00 18.18 ?  161 THR C CB    1 
ATOM   3723  O  OG1   . THR C 1 161 ? 5.426   -15.387 0.086   1.00 17.56 ?  161 THR C OG1   1 
ATOM   3724  C  CG2   . THR C 1 161 ? 5.259   -15.755 -2.301  1.00 16.78 ?  161 THR C CG2   1 
ATOM   3725  N  N     . HIS C 1 162 ? 7.921   -13.033 0.121   1.00 21.69 ?  162 HIS C N     1 
ATOM   3726  C  CA    . HIS C 1 162 ? 8.074   -12.290 1.359   1.00 19.10 ?  162 HIS C CA    1 
ATOM   3727  C  C     . HIS C 1 162 ? 6.790   -12.450 2.167   1.00 20.41 ?  162 HIS C C     1 
ATOM   3728  O  O     . HIS C 1 162 ? 5.709   -12.095 1.701   1.00 19.65 ?  162 HIS C O     1 
ATOM   3729  C  CB    . HIS C 1 162 ? 8.428   -10.823 1.085   1.00 19.07 ?  162 HIS C CB    1 
ATOM   3730  C  CG    . HIS C 1 162 ? 9.850   -10.609 0.679   1.00 19.65 ?  162 HIS C CG    1 
ATOM   3731  N  ND1   . HIS C 1 162 ? 10.254  -10.462 -0.631  1.00 20.74 ?  162 HIS C ND1   1 
ATOM   3732  C  CD2   . HIS C 1 162 ? 10.959  -10.507 1.423   1.00 18.52 ?  162 HIS C CD2   1 
ATOM   3733  C  CE1   . HIS C 1 162 ? 11.568  -10.283 -0.664  1.00 21.89 ?  162 HIS C CE1   1 
ATOM   3734  N  NE2   . HIS C 1 162 ? 12.016  -10.308 0.574   1.00 20.96 ?  162 HIS C NE2   1 
ATOM   3735  N  N     . LEU C 1 163 ? 6.924   -13.024 3.367   1.00 23.06 ?  163 LEU C N     1 
ATOM   3736  C  CA    . LEU C 1 163 ? 5.799   -13.232 4.262   1.00 21.37 ?  163 LEU C CA    1 
ATOM   3737  C  C     . LEU C 1 163 ? 5.806   -12.151 5.340   1.00 22.55 ?  163 LEU C C     1 
ATOM   3738  O  O     . LEU C 1 163 ? 6.848   -11.855 5.921   1.00 23.92 ?  163 LEU C O     1 
ATOM   3739  C  CB    . LEU C 1 163 ? 5.893   -14.631 4.870   1.00 21.43 ?  163 LEU C CB    1 
ATOM   3740  C  CG    . LEU C 1 163 ? 4.828   -14.993 5.910   1.00 20.46 ?  163 LEU C CG    1 
ATOM   3741  C  CD1   . LEU C 1 163 ? 3.438   -14.954 5.304   1.00 19.97 ?  163 LEU C CD1   1 
ATOM   3742  C  CD2   . LEU C 1 163 ? 5.106   -16.358 6.519   1.00 18.53 ?  163 LEU C CD2   1 
ATOM   3743  N  N     . LEU C 1 164 ? 4.628   -11.569 5.591   1.00 23.72 ?  164 LEU C N     1 
ATOM   3744  C  CA    . LEU C 1 164 ? 4.445   -10.613 6.672   1.00 21.95 ?  164 LEU C CA    1 
ATOM   3745  C  C     . LEU C 1 164 ? 3.446   -11.182 7.676   1.00 18.63 ?  164 LEU C C     1 
ATOM   3746  O  O     . LEU C 1 164 ? 2.467   -11.820 7.295   1.00 14.84 ?  164 LEU C O     1 
ATOM   3747  C  CB    . LEU C 1 164 ? 3.972   -9.260  6.139   1.00 22.08 ?  164 LEU C CB    1 
ATOM   3748  C  CG    . LEU C 1 164 ? 4.941   -8.503  5.225   1.00 25.26 ?  164 LEU C CG    1 
ATOM   3749  C  CD1   . LEU C 1 164 ? 4.413   -7.110  4.921   1.00 26.92 ?  164 LEU C CD1   1 
ATOM   3750  C  CD2   . LEU C 1 164 ? 6.331   -8.418  5.829   1.00 27.92 ?  164 LEU C CD2   1 
ATOM   3751  N  N     . LEU C 1 165 ? 3.724   -10.951 8.963   1.00 20.33 ?  165 LEU C N     1 
ATOM   3752  C  CA    . LEU C 1 165 ? 2.768   -11.198 10.029  1.00 18.30 ?  165 LEU C CA    1 
ATOM   3753  C  C     . LEU C 1 165 ? 2.609   -9.906  10.829  1.00 19.19 ?  165 LEU C C     1 
ATOM   3754  O  O     . LEU C 1 165 ? 3.544   -9.468  11.497  1.00 17.37 ?  165 LEU C O     1 
ATOM   3755  C  CB    . LEU C 1 165 ? 3.223   -12.353 10.921  1.00 17.88 ?  165 LEU C CB    1 
ATOM   3756  C  CG    . LEU C 1 165 ? 3.377   -13.724 10.252  1.00 15.93 ?  165 LEU C CG    1 
ATOM   3757  C  CD1   . LEU C 1 165 ? 3.752   -14.734 11.318  1.00 15.68 ?  165 LEU C CD1   1 
ATOM   3758  C  CD2   . LEU C 1 165 ? 2.138   -14.186 9.506   1.00 14.93 ?  165 LEU C CD2   1 
ATOM   3759  N  N     . TRP C 1 166 ? 1.421   -9.297  10.732  1.00 18.34 ?  166 TRP C N     1 
ATOM   3760  C  CA    . TRP C 1 166 ? 1.132   -8.039  11.403  1.00 21.70 ?  166 TRP C CA    1 
ATOM   3761  C  C     . TRP C 1 166 ? 0.692   -8.322  12.839  1.00 22.03 ?  166 TRP C C     1 
ATOM   3762  O  O     . TRP C 1 166 ? 0.249   -9.426  13.147  1.00 18.00 ?  166 TRP C O     1 
ATOM   3763  C  CB    . TRP C 1 166 ? 0.048   -7.245  10.656  1.00 22.03 ?  166 TRP C CB    1 
ATOM   3764  C  CG    . TRP C 1 166 ? 0.351   -6.912  9.217   1.00 26.01 ?  166 TRP C CG    1 
ATOM   3765  C  CD1   . TRP C 1 166 ? 0.772   -7.767  8.240   1.00 26.99 ?  166 TRP C CD1   1 
ATOM   3766  C  CD2   . TRP C 1 166 ? 0.241   -5.614  8.589   1.00 29.96 ?  166 TRP C CD2   1 
ATOM   3767  N  NE1   . TRP C 1 166 ? 0.931   -7.098  7.056   1.00 25.95 ?  166 TRP C NE1   1 
ATOM   3768  C  CE2   . TRP C 1 166 ? 0.615   -5.777  7.237   1.00 31.77 ?  166 TRP C CE2   1 
ATOM   3769  C  CE3   . TRP C 1 166 ? -0.133  -4.339  9.031   1.00 32.35 ?  166 TRP C CE3   1 
ATOM   3770  C  CZ2   . TRP C 1 166 ? 0.624   -4.717  6.333   1.00 33.60 ?  166 TRP C CZ2   1 
ATOM   3771  C  CZ3   . TRP C 1 166 ? -0.124  -3.292  8.135   1.00 33.53 ?  166 TRP C CZ3   1 
ATOM   3772  C  CH2   . TRP C 1 166 ? 0.249   -3.480  6.805   1.00 33.21 ?  166 TRP C CH2   1 
ATOM   3773  N  N     . GLN C 1 167 ? 0.809   -7.308  13.704  1.00 21.71 ?  167 GLN C N     1 
ATOM   3774  C  CA    . GLN C 1 167 ? 0.446   -7.437  15.105  1.00 21.04 ?  167 GLN C CA    1 
ATOM   3775  C  C     . GLN C 1 167 ? 1.126   -8.679  15.675  1.00 17.94 ?  167 GLN C C     1 
ATOM   3776  O  O     . GLN C 1 167 ? 0.479   -9.529  16.282  1.00 16.53 ?  167 GLN C O     1 
ATOM   3777  C  CB    . GLN C 1 167 ? -1.075  -7.488  15.268  1.00 23.08 ?  167 GLN C CB    1 
ATOM   3778  C  CG    . GLN C 1 167 ? -1.813  -6.381  14.521  1.00 24.89 ?  167 GLN C CG    1 
ATOM   3779  C  CD    . GLN C 1 167 ? -3.251  -6.205  14.960  1.00 25.28 ?  167 GLN C CD    1 
ATOM   3780  O  OE1   . GLN C 1 167 ? -3.731  -5.082  15.153  1.00 26.15 ?  167 GLN C OE1   1 
ATOM   3781  N  NE2   . GLN C 1 167 ? -3.963  -7.314  15.101  1.00 24.86 ?  167 GLN C NE2   1 
ATOM   3782  N  N     . ILE C 1 168 ? 2.443   -8.771  15.465  1.00 18.13 ?  168 ILE C N     1 
ATOM   3783  C  CA    . ILE C 1 168 ? 3.211   -9.916  15.922  1.00 16.69 ?  168 ILE C CA    1 
ATOM   3784  C  C     . ILE C 1 168 ? 3.365   -9.842  17.440  1.00 16.34 ?  168 ILE C C     1 
ATOM   3785  O  O     . ILE C 1 168 ? 3.633   -10.854 18.084  1.00 13.82 ?  168 ILE C O     1 
ATOM   3786  C  CB    . ILE C 1 168 ? 4.574   -9.996  15.208  1.00 15.83 ?  168 ILE C CB    1 
ATOM   3787  C  CG1   . ILE C 1 168 ? 5.342   -11.247 15.626  1.00 15.69 ?  168 ILE C CG1   1 
ATOM   3788  C  CG2   . ILE C 1 168 ? 5.398   -8.725  15.425  1.00 15.47 ?  168 ILE C CG2   1 
ATOM   3789  C  CD1   . ILE C 1 168 ? 4.668   -12.544 15.214  1.00 15.67 ?  168 ILE C CD1   1 
ATOM   3790  N  N     . ALA C 1 169 ? 3.165   -8.643  18.002  1.00 16.30 ?  169 ALA C N     1 
ATOM   3791  C  CA    . ALA C 1 169 ? 3.453   -8.388  19.405  1.00 17.38 ?  169 ALA C CA    1 
ATOM   3792  C  C     . ALA C 1 169 ? 2.355   -8.953  20.307  1.00 16.89 ?  169 ALA C C     1 
ATOM   3793  O  O     . ALA C 1 169 ? 2.569   -9.127  21.506  1.00 15.33 ?  169 ALA C O     1 
ATOM   3794  C  CB    . ALA C 1 169 ? 3.645   -6.903  19.626  1.00 19.25 ?  169 ALA C CB    1 
ATOM   3795  N  N     . ILE C 1 170 ? 1.181   -9.227  19.726  1.00 17.96 ?  170 ILE C N     1 
ATOM   3796  C  CA    . ILE C 1 170 ? 0.079   -9.842  20.451  1.00 18.11 ?  170 ILE C CA    1 
ATOM   3797  C  C     . ILE C 1 170 ? -0.217  -11.216 19.854  1.00 17.67 ?  170 ILE C C     1 
ATOM   3798  O  O     . ILE C 1 170 ? -1.285  -11.780 20.084  1.00 16.40 ?  170 ILE C O     1 
ATOM   3799  C  CB    . ILE C 1 170 ? -1.174  -8.946  20.438  1.00 20.07 ?  170 ILE C CB    1 
ATOM   3800  C  CG1   . ILE C 1 170 ? -1.497  -8.443  19.029  1.00 21.33 ?  170 ILE C CG1   1 
ATOM   3801  C  CG2   . ILE C 1 170 ? -1.032  -7.793  21.432  1.00 21.13 ?  170 ILE C CG2   1 
ATOM   3802  C  CD1   . ILE C 1 170 ? -2.813  -7.692  18.924  1.00 20.51 ?  170 ILE C CD1   1 
ATOM   3803  N  N     . ALA C 1 171 ? 0.740   -11.750 19.088  1.00 17.66 ?  171 ALA C N     1 
ATOM   3804  C  CA    . ALA C 1 171 ? 0.571   -13.040 18.439  1.00 16.98 ?  171 ALA C CA    1 
ATOM   3805  C  C     . ALA C 1 171 ? 0.131   -14.086 19.460  1.00 17.38 ?  171 ALA C C     1 
ATOM   3806  O  O     . ALA C 1 171 ? 0.919   -14.498 20.310  1.00 18.31 ?  171 ALA C O     1 
ATOM   3807  C  CB    . ALA C 1 171 ? 1.860   -13.451 17.762  1.00 16.63 ?  171 ALA C CB    1 
ATOM   3808  N  N     . GLY C 1 172 ? -1.134  -14.510 19.364  1.00 16.97 ?  172 GLY C N     1 
ATOM   3809  C  CA    . GLY C 1 172 ? -1.641  -15.613 20.163  1.00 19.83 ?  172 GLY C CA    1 
ATOM   3810  C  C     . GLY C 1 172 ? -2.529  -15.141 21.314  1.00 22.12 ?  172 GLY C C     1 
ATOM   3811  O  O     . GLY C 1 172 ? -3.067  -15.959 22.057  1.00 23.12 ?  172 GLY C O     1 
ATOM   3812  N  N     . GLU C 1 173 ? -2.679  -13.817 21.446  1.00 25.22 ?  173 GLU C N     1 
ATOM   3813  C  CA    . GLU C 1 173 ? -3.470  -13.210 22.507  1.00 31.57 ?  173 GLU C CA    1 
ATOM   3814  C  C     . GLU C 1 173 ? -4.951  -13.226 22.128  1.00 32.04 ?  173 GLU C C     1 
ATOM   3815  O  O     . GLU C 1 173 ? -5.437  -12.286 21.504  1.00 40.10 ?  173 GLU C O     1 
ATOM   3816  C  CB    . GLU C 1 173 ? -3.034  -11.756 22.707  1.00 31.66 ?  173 GLU C CB    1 
ATOM   3817  C  CG    . GLU C 1 173 ? -3.025  -11.295 24.162  1.00 31.89 ?  173 GLU C CG    1 
ATOM   3818  C  CD    . GLU C 1 173 ? -4.337  -11.450 24.909  1.00 36.48 ?  173 GLU C CD    1 
ATOM   3819  O  OE1   . GLU C 1 173 ? -5.327  -10.799 24.513  1.00 45.66 ?  173 GLU C OE1   1 
ATOM   3820  O  OE2   . GLU C 1 173 ? -4.366  -12.220 25.893  1.00 39.27 -1 173 GLU C OE2   1 
ATOM   3821  N  N     . HIS C 1 174 ? -5.663  -14.286 22.534  1.00 34.84 ?  174 HIS C N     1 
ATOM   3822  C  CA    . HIS C 1 174 ? -7.029  -14.533 22.087  1.00 36.45 ?  174 HIS C CA    1 
ATOM   3823  C  C     . HIS C 1 174 ? -8.037  -13.583 22.745  1.00 39.27 ?  174 HIS C C     1 
ATOM   3824  O  O     . HIS C 1 174 ? -8.938  -13.092 22.070  1.00 48.60 ?  174 HIS C O     1 
ATOM   3825  C  CB    . HIS C 1 174 ? -7.385  -16.013 22.281  1.00 34.91 ?  174 HIS C CB    1 
ATOM   3826  C  CG    . HIS C 1 174 ? -7.405  -16.455 23.705  1.00 30.12 ?  174 HIS C CG    1 
ATOM   3827  N  ND1   . HIS C 1 174 ? -6.268  -16.802 24.403  1.00 28.57 ?  174 HIS C ND1   1 
ATOM   3828  C  CD2   . HIS C 1 174 ? -8.424  -16.597 24.564  1.00 29.15 ?  174 HIS C CD2   1 
ATOM   3829  C  CE1   . HIS C 1 174 ? -6.601  -17.144 25.639  1.00 28.08 ?  174 HIS C CE1   1 
ATOM   3830  N  NE2   . HIS C 1 174 ? -7.907  -17.027 25.759  1.00 27.49 ?  174 HIS C NE2   1 
ATOM   3831  N  N     . THR C 1 175 ? -7.895  -13.323 24.054  1.00 45.47 ?  175 THR C N     1 
ATOM   3832  C  CA    . THR C 1 175 ? -8.888  -12.570 24.816  1.00 44.14 ?  175 THR C CA    1 
ATOM   3833  C  C     . THR C 1 175 ? -9.211  -11.236 24.137  1.00 46.21 ?  175 THR C C     1 
ATOM   3834  O  O     . THR C 1 175 ? -10.365 -10.812 24.137  1.00 54.16 ?  175 THR C O     1 
ATOM   3835  C  CB    . THR C 1 175 ? -8.412  -12.341 26.252  1.00 41.77 ?  175 THR C CB    1 
ATOM   3836  O  OG1   . THR C 1 175 ? -7.307  -11.447 26.150  1.00 35.26 ?  175 THR C OG1   1 
ATOM   3837  C  CG2   . THR C 1 175 ? -8.012  -13.622 26.963  1.00 44.92 ?  175 THR C CG2   1 
ATOM   3838  N  N     . LEU C 1 176 ? -8.192  -10.569 23.581  1.00 48.36 ?  176 LEU C N     1 
ATOM   3839  C  CA    . LEU C 1 176 ? -8.335  -9.226  23.029  1.00 46.86 ?  176 LEU C CA    1 
ATOM   3840  C  C     . LEU C 1 176 ? -8.478  -8.227  24.175  1.00 46.37 ?  176 LEU C C     1 
ATOM   3841  O  O     . LEU C 1 176 ? -9.343  -7.354  24.136  1.00 51.29 ?  176 LEU C O     1 
ATOM   3842  C  CB    . LEU C 1 176 ? -9.513  -9.067  22.068  1.00 47.00 ?  176 LEU C CB    1 
ATOM   3843  C  CG    . LEU C 1 176 ? -9.623  -10.073 20.919  1.00 52.78 ?  176 LEU C CG    1 
ATOM   3844  C  CD1   . LEU C 1 176 ? -10.523 -9.493  19.838  1.00 51.61 ?  176 LEU C CD1   1 
ATOM   3845  C  CD2   . LEU C 1 176 ? -8.269  -10.459 20.352  1.00 55.98 ?  176 LEU C CD2   1 
ATOM   3846  N  N     . THR C 1 177 ? -7.616  -8.360  25.186  1.00 40.18 ?  177 THR C N     1 
ATOM   3847  C  CA    . THR C 1 177 ? -7.667  -7.509  26.363  1.00 34.48 ?  177 THR C CA    1 
ATOM   3848  C  C     . THR C 1 177 ? -6.247  -7.102  26.732  1.00 32.84 ?  177 THR C C     1 
ATOM   3849  O  O     . THR C 1 177 ? -6.039  -6.149  27.480  1.00 38.15 ?  177 THR C O     1 
ATOM   3850  C  CB    . THR C 1 177 ? -8.327  -8.260  27.518  1.00 34.23 ?  177 THR C CB    1 
ATOM   3851  O  OG1   . THR C 1 177 ? -7.367  -9.233  27.923  1.00 28.78 ?  177 THR C OG1   1 
ATOM   3852  C  CG2   . THR C 1 177 ? -9.635  -8.916  27.117  1.00 32.85 ?  177 THR C CG2   1 
ATOM   3853  N  N     . GLN C 1 178 ? -5.276  -7.855  26.208  1.00 31.22 ?  178 GLN C N     1 
ATOM   3854  C  CA    . GLN C 1 178 ? -3.884  -7.654  26.565  1.00 31.43 ?  178 GLN C CA    1 
ATOM   3855  C  C     . GLN C 1 178 ? -3.197  -6.840  25.472  1.00 30.12 ?  178 GLN C C     1 
ATOM   3856  O  O     . GLN C 1 178 ? -3.555  -6.927  24.299  1.00 25.81 ?  178 GLN C O     1 
ATOM   3857  C  CB    . GLN C 1 178 ? -3.203  -8.999  26.820  1.00 28.76 ?  178 GLN C CB    1 
ATOM   3858  C  CG    . GLN C 1 178 ? -3.759  -9.752  28.025  1.00 33.86 ?  178 GLN C CG    1 
ATOM   3859  C  CD    . GLN C 1 178 ? -3.375  -9.128  29.350  1.00 36.45 ?  178 GLN C CD    1 
ATOM   3860  O  OE1   . GLN C 1 178 ? -2.562  -8.199  29.414  1.00 42.27 ?  178 GLN C OE1   1 
ATOM   3861  N  NE2   . GLN C 1 178 ? -3.951  -9.643  30.426  1.00 36.19 ?  178 GLN C NE2   1 
ATOM   3862  N  N     . PHE C 1 179 ? -2.204  -6.049  25.890  1.00 33.67 ?  179 PHE C N     1 
ATOM   3863  C  CA    . PHE C 1 179 ? -1.497  -5.147  24.999  1.00 38.72 ?  179 PHE C CA    1 
ATOM   3864  C  C     . PHE C 1 179 ? -0.309  -5.859  24.350  1.00 41.51 ?  179 PHE C C     1 
ATOM   3865  O  O     . PHE C 1 179 ? 0.234   -5.366  23.364  1.00 43.43 ?  179 PHE C O     1 
ATOM   3866  C  CB    . PHE C 1 179 ? -1.065  -3.863  25.721  1.00 45.99 ?  179 PHE C CB    1 
ATOM   3867  C  CG    . PHE C 1 179 ? -1.283  -3.758  27.227  1.00 47.43 ?  179 PHE C CG    1 
ATOM   3868  C  CD1   . PHE C 1 179 ? -1.135  -4.848  28.081  1.00 42.32 ?  179 PHE C CD1   1 
ATOM   3869  C  CD2   . PHE C 1 179 ? -1.634  -2.532  27.785  1.00 48.45 ?  179 PHE C CD2   1 
ATOM   3870  C  CE1   . PHE C 1 179 ? -1.337  -4.708  29.447  1.00 45.95 ?  179 PHE C CE1   1 
ATOM   3871  C  CE2   . PHE C 1 179 ? -1.836  -2.399  29.149  1.00 42.29 ?  179 PHE C CE2   1 
ATOM   3872  C  CZ    . PHE C 1 179 ? -1.687  -3.487  29.976  1.00 48.89 ?  179 PHE C CZ    1 
ATOM   3873  N  N     . HIS C 1 180 ? 0.087   -7.017  24.895  1.00 40.00 ?  180 HIS C N     1 
ATOM   3874  C  CA    . HIS C 1 180 ? 1.252   -7.733  24.393  1.00 34.74 ?  180 HIS C CA    1 
ATOM   3875  C  C     . HIS C 1 180 ? 1.088   -9.236  24.627  1.00 29.34 ?  180 HIS C C     1 
ATOM   3876  O  O     . HIS C 1 180 ? 0.176   -9.656  25.334  1.00 28.82 ?  180 HIS C O     1 
ATOM   3877  C  CB    . HIS C 1 180 ? 2.525   -7.176  25.040  1.00 34.91 ?  180 HIS C CB    1 
ATOM   3878  C  CG    . HIS C 1 180 ? 2.690   -7.576  26.467  1.00 42.96 ?  180 HIS C CG    1 
ATOM   3879  N  ND1   . HIS C 1 180 ? 3.469   -8.649  26.840  1.00 43.91 ?  180 HIS C ND1   1 
ATOM   3880  C  CD2   . HIS C 1 180 ? 2.193   -7.065  27.601  1.00 44.20 ?  180 HIS C CD2   1 
ATOM   3881  C  CE1   . HIS C 1 180 ? 3.436   -8.775  28.158  1.00 45.82 ?  180 HIS C CE1   1 
ATOM   3882  N  NE2   . HIS C 1 180 ? 2.666   -7.824  28.641  1.00 49.49 ?  180 HIS C NE2   1 
ATOM   3883  N  N     . THR C 1 181 ? 1.979   -10.041 24.026  1.00 30.13 ?  181 THR C N     1 
ATOM   3884  C  CA    . THR C 1 181 ? 1.901   -11.495 24.122  1.00 40.19 ?  181 THR C CA    1 
ATOM   3885  C  C     . THR C 1 181 ? 2.978   -12.028 25.067  1.00 40.32 ?  181 THR C C     1 
ATOM   3886  O  O     . THR C 1 181 ? 3.684   -11.258 25.715  1.00 44.54 ?  181 THR C O     1 
ATOM   3887  C  CB    . THR C 1 181 ? 2.034   -12.134 22.738  1.00 40.93 ?  181 THR C CB    1 
ATOM   3888  O  OG1   . THR C 1 181 ? 1.691   -13.505 22.924  1.00 44.76 ?  181 THR C OG1   1 
ATOM   3889  C  CG2   . THR C 1 181 ? 3.436   -12.028 22.166  1.00 41.49 ?  181 THR C CG2   1 
ATOM   3890  N  N     . SER C 1 182 ? 3.086   -13.363 25.125  1.00 42.04 ?  182 SER C N     1 
ATOM   3891  C  CA    . SER C 1 182 ? 4.029   -14.050 25.995  1.00 43.16 ?  182 SER C CA    1 
ATOM   3892  C  C     . SER C 1 182 ? 5.130   -14.697 25.158  1.00 41.24 ?  182 SER C C     1 
ATOM   3893  O  O     . SER C 1 182 ? 4.935   -14.952 23.972  1.00 35.91 ?  182 SER C O     1 
ATOM   3894  C  CB    . SER C 1 182 ? 3.326   -15.089 26.840  1.00 41.49 ?  182 SER C CB    1 
ATOM   3895  O  OG    . SER C 1 182 ? 3.120   -16.292 26.111  1.00 39.45 ?  182 SER C OG    1 
ATOM   3896  N  N     . SER C 1 183 ? 6.280   -14.971 25.789  1.00 41.88 ?  183 SER C N     1 
ATOM   3897  C  CA    . SER C 1 183 ? 7.369   -15.677 25.132  1.00 44.04 ?  183 SER C CA    1 
ATOM   3898  C  C     . SER C 1 183 ? 6.884   -17.033 24.625  1.00 42.51 ?  183 SER C C     1 
ATOM   3899  O  O     . SER C 1 183 ? 7.234   -17.447 23.523  1.00 42.17 ?  183 SER C O     1 
ATOM   3900  C  CB    . SER C 1 183 ? 8.553   -15.849 26.050  1.00 42.27 ?  183 SER C CB    1 
ATOM   3901  O  OG    . SER C 1 183 ? 8.186   -16.555 27.228  1.00 41.66 ?  183 SER C OG    1 
ATOM   3902  N  N     . ASP C 1 184 ? 6.082   -17.720 25.445  1.00 38.55 ?  184 ASP C N     1 
ATOM   3903  C  CA    . ASP C 1 184 ? 5.681   -19.084 25.144  1.00 42.47 ?  184 ASP C CA    1 
ATOM   3904  C  C     . ASP C 1 184 ? 4.637   -19.084 24.028  1.00 37.81 ?  184 ASP C C     1 
ATOM   3905  O  O     . ASP C 1 184 ? 4.411   -20.114 23.396  1.00 35.12 ?  184 ASP C O     1 
ATOM   3906  C  CB    . ASP C 1 184 ? 5.229   -19.830 26.390  1.00 47.68 ?  184 ASP C CB    1 
ATOM   3907  C  CG    . ASP C 1 184 ? 4.079   -19.201 27.163  1.00 53.06 ?  184 ASP C CG    1 
ATOM   3908  O  OD1   . ASP C 1 184 ? 4.272   -18.090 27.699  1.00 57.23 ?  184 ASP C OD1   1 
ATOM   3909  O  OD2   . ASP C 1 184 ? 3.001   -19.828 27.221  1.00 59.98 -1 184 ASP C OD2   1 
ATOM   3910  N  N     . ARG C 1 185 ? 4.002   -17.930 23.793  1.00 32.39 ?  185 ARG C N     1 
ATOM   3911  C  CA    . ARG C 1 185 ? 3.118   -17.776 22.648  1.00 32.02 ?  185 ARG C CA    1 
ATOM   3912  C  C     . ARG C 1 185 ? 3.954   -17.713 21.374  1.00 29.80 ?  185 ARG C C     1 
ATOM   3913  O  O     . ARG C 1 185 ? 3.664   -18.402 20.399  1.00 21.95 ?  185 ARG C O     1 
ATOM   3914  C  CB    . ARG C 1 185 ? 2.240   -16.521 22.719  1.00 29.62 ?  185 ARG C CB    1 
ATOM   3915  C  CG    . ARG C 1 185 ? 0.805   -16.778 23.156  1.00 32.70 ?  185 ARG C CG    1 
ATOM   3916  C  CD    . ARG C 1 185 ? 0.657   -17.186 24.612  1.00 35.79 ?  185 ARG C CD    1 
ATOM   3917  N  NE    . ARG C 1 185 ? -0.712  -17.649 24.869  1.00 38.10 ?  185 ARG C NE    1 
ATOM   3918  C  CZ    . ARG C 1 185 ? -1.049  -18.828 25.381  1.00 34.89 ?  185 ARG C CZ    1 
ATOM   3919  N  NH1   . ARG C 1 185 ? -0.121  -19.642 25.851  1.00 34.68 1  185 ARG C NH1   1 
ATOM   3920  N  NH2   . ARG C 1 185 ? -2.321  -19.178 25.444  1.00 33.33 ?  185 ARG C NH2   1 
ATOM   3921  N  N     . LEU C 1 186 ? 4.990   -16.870 21.409  1.00 29.72 ?  186 LEU C N     1 
ATOM   3922  C  CA    . LEU C 1 186 ? 5.834   -16.611 20.255  1.00 30.00 ?  186 LEU C CA    1 
ATOM   3923  C  C     . LEU C 1 186 ? 6.696   -17.835 19.947  1.00 33.91 ?  186 LEU C C     1 
ATOM   3924  O  O     . LEU C 1 186 ? 7.107   -18.034 18.805  1.00 34.89 ?  186 LEU C O     1 
ATOM   3925  C  CB    . LEU C 1 186 ? 6.662   -15.363 20.560  1.00 31.03 ?  186 LEU C CB    1 
ATOM   3926  C  CG    . LEU C 1 186 ? 5.901   -14.032 20.508  1.00 30.74 ?  186 LEU C CG    1 
ATOM   3927  C  CD1   . LEU C 1 186 ? 6.685   -12.900 21.150  1.00 29.70 ?  186 LEU C CD1   1 
ATOM   3928  C  CD2   . LEU C 1 186 ? 5.550   -13.676 19.071  1.00 28.23 ?  186 LEU C CD2   1 
ATOM   3929  N  N     . GLN C 1 187 ? 6.950   -18.655 20.974  1.00 32.70 ?  187 GLN C N     1 
ATOM   3930  C  CA    . GLN C 1 187 ? 7.722   -19.880 20.830  1.00 33.14 ?  187 GLN C CA    1 
ATOM   3931  C  C     . GLN C 1 187 ? 6.915   -20.923 20.060  1.00 33.15 ?  187 GLN C C     1 
ATOM   3932  O  O     . GLN C 1 187 ? 7.478   -21.727 19.320  1.00 31.79 ?  187 GLN C O     1 
ATOM   3933  C  CB    . GLN C 1 187 ? 8.107   -20.421 22.208  1.00 35.84 ?  187 GLN C CB    1 
ATOM   3934  C  CG    . GLN C 1 187 ? 8.847   -21.755 22.177  1.00 36.88 ?  187 GLN C CG    1 
ATOM   3935  C  CD    . GLN C 1 187 ? 10.108  -21.718 21.342  1.00 39.27 ?  187 GLN C CD    1 
ATOM   3936  O  OE1   . GLN C 1 187 ? 10.979  -20.860 21.523  1.00 36.52 ?  187 GLN C OE1   1 
ATOM   3937  N  NE2   . GLN C 1 187 ? 10.214  -22.653 20.409  1.00 43.95 ?  187 GLN C NE2   1 
ATOM   3938  N  N     . ILE C 1 188 ? 5.593   -20.912 20.257  1.00 32.44 ?  188 ILE C N     1 
ATOM   3939  C  CA    . ILE C 1 188 ? 4.704   -21.829 19.563  1.00 32.91 ?  188 ILE C CA    1 
ATOM   3940  C  C     . ILE C 1 188 ? 4.524   -21.343 18.128  1.00 29.69 ?  188 ILE C C     1 
ATOM   3941  O  O     . ILE C 1 188 ? 4.166   -22.120 17.245  1.00 30.00 ?  188 ILE C O     1 
ATOM   3942  C  CB    . ILE C 1 188 ? 3.367   -21.969 20.315  1.00 33.36 ?  188 ILE C CB    1 
ATOM   3943  C  CG1   . ILE C 1 188 ? 3.541   -22.801 21.588  1.00 30.58 ?  188 ILE C CG1   1 
ATOM   3944  C  CG2   . ILE C 1 188 ? 2.277   -22.546 19.411  1.00 36.15 ?  188 ILE C CG2   1 
ATOM   3945  C  CD1   . ILE C 1 188 ? 2.324   -22.823 22.494  1.00 35.66 ?  188 ILE C CD1   1 
ATOM   3946  N  N     . LEU C 1 189 ? 4.798   -20.053 17.904  1.00 28.26 ?  189 LEU C N     1 
ATOM   3947  C  CA    . LEU C 1 189 ? 4.757   -19.487 16.565  1.00 28.02 ?  189 LEU C CA    1 
ATOM   3948  C  C     . LEU C 1 189 ? 5.995   -19.942 15.797  1.00 23.19 ?  189 LEU C C     1 
ATOM   3949  O  O     . LEU C 1 189 ? 5.932   -20.167 14.591  1.00 21.37 ?  189 LEU C O     1 
ATOM   3950  C  CB    . LEU C 1 189 ? 4.658   -17.962 16.591  1.00 23.70 ?  189 LEU C CB    1 
ATOM   3951  C  CG    . LEU C 1 189 ? 4.669   -17.283 15.217  1.00 22.23 ?  189 LEU C CG    1 
ATOM   3952  C  CD1   . LEU C 1 189 ? 3.670   -17.955 14.291  1.00 22.95 ?  189 LEU C CD1   1 
ATOM   3953  C  CD2   . LEU C 1 189 ? 4.386   -15.793 15.300  1.00 20.28 ?  189 LEU C CD2   1 
ATOM   3954  N  N     . VAL C 1 190 ? 7.116   -20.070 16.513  1.00 26.56 ?  190 VAL C N     1 
ATOM   3955  C  CA    . VAL C 1 190 ? 8.380   -20.460 15.911  1.00 28.67 ?  190 VAL C CA    1 
ATOM   3956  C  C     . VAL C 1 190 ? 8.291   -21.917 15.464  1.00 30.24 ?  190 VAL C C     1 
ATOM   3957  O  O     . VAL C 1 190 ? 8.809   -22.280 14.410  1.00 30.53 ?  190 VAL C O     1 
ATOM   3958  C  CB    . VAL C 1 190 ? 9.553   -20.241 16.887  1.00 29.06 ?  190 VAL C CB    1 
ATOM   3959  C  CG1   . VAL C 1 190 ? 10.801  -21.004 16.460  1.00 30.80 ?  190 VAL C CG1   1 
ATOM   3960  C  CG2   . VAL C 1 190 ? 9.863   -18.761 17.080  1.00 25.28 ?  190 VAL C CG2   1 
ATOM   3961  N  N     . GLU C 1 191 ? 7.623   -22.742 16.277  1.00 30.86 ?  191 GLU C N     1 
ATOM   3962  C  CA    . GLU C 1 191 ? 7.518   -24.169 16.017  1.00 34.47 ?  191 GLU C CA    1 
ATOM   3963  C  C     . GLU C 1 191 ? 6.524   -24.412 14.885  1.00 34.36 ?  191 GLU C C     1 
ATOM   3964  O  O     . GLU C 1 191 ? 6.685   -25.344 14.101  1.00 34.76 ?  191 GLU C O     1 
ATOM   3965  C  CB    . GLU C 1 191 ? 7.099   -24.906 17.288  1.00 38.90 ?  191 GLU C CB    1 
ATOM   3966  C  CG    . GLU C 1 191 ? 8.177   -24.901 18.368  1.00 40.40 ?  191 GLU C CG    1 
ATOM   3967  C  CD    . GLU C 1 191 ? 7.734   -25.522 19.679  1.00 42.42 ?  191 GLU C CD    1 
ATOM   3968  O  OE1   . GLU C 1 191 ? 7.998   -24.920 20.741  1.00 42.13 ?  191 GLU C OE1   1 
ATOM   3969  O  OE2   . GLU C 1 191 ? 7.107   -26.601 19.635  1.00 45.57 -1 191 GLU C OE2   1 
ATOM   3970  N  N     . GLN C 1 192 ? 5.489   -23.567 14.827  1.00 34.06 ?  192 GLN C N     1 
ATOM   3971  C  CA    . GLN C 1 192 ? 4.526   -23.587 13.740  1.00 33.47 ?  192 GLN C CA    1 
ATOM   3972  C  C     . GLN C 1 192 ? 5.225   -23.220 12.433  1.00 35.46 ?  192 GLN C C     1 
ATOM   3973  O  O     . GLN C 1 192 ? 5.136   -23.950 11.448  1.00 37.46 ?  192 GLN C O     1 
ATOM   3974  C  CB    . GLN C 1 192 ? 3.397   -22.597 14.029  1.00 38.14 ?  192 GLN C CB    1 
ATOM   3975  C  CG    . GLN C 1 192 ? 2.291   -22.594 12.980  1.00 39.80 ?  192 GLN C CG    1 
ATOM   3976  C  CD    . GLN C 1 192 ? 1.361   -21.405 13.092  1.00 38.09 ?  192 GLN C CD    1 
ATOM   3977  O  OE1   . GLN C 1 192 ? 1.669   -20.399 13.741  1.00 36.54 ?  192 GLN C OE1   1 
ATOM   3978  N  NE2   . GLN C 1 192 ? 0.212   -21.507 12.439  1.00 38.83 ?  192 GLN C NE2   1 
ATOM   3979  N  N     . LEU C 1 193 ? 5.917   -22.076 12.440  1.00 33.32 ?  193 LEU C N     1 
ATOM   3980  C  CA    . LEU C 1 193 ? 6.602   -21.580 11.256  1.00 34.79 ?  193 LEU C CA    1 
ATOM   3981  C  C     . LEU C 1 193 ? 7.625   -22.606 10.776  1.00 34.90 ?  193 LEU C C     1 
ATOM   3982  O  O     . LEU C 1 193 ? 8.010   -22.599 9.609   1.00 34.25 ?  193 LEU C O     1 
ATOM   3983  C  CB    . LEU C 1 193 ? 7.266   -20.237 11.555  1.00 31.71 ?  193 LEU C CB    1 
ATOM   3984  C  CG    . LEU C 1 193 ? 6.342   -19.016 11.552  1.00 34.91 ?  193 LEU C CG    1 
ATOM   3985  C  CD1   . LEU C 1 193 ? 7.081   -17.781 12.037  1.00 33.18 ?  193 LEU C CD1   1 
ATOM   3986  C  CD2   . LEU C 1 193 ? 5.762   -18.790 10.165  1.00 36.77 ?  193 LEU C CD2   1 
ATOM   3987  N  N     . ASN C 1 194 ? 8.056   -23.488 11.684  1.00 37.24 ?  194 ASN C N     1 
ATOM   3988  C  CA    . ASN C 1 194 ? 9.164   -24.388 11.406  1.00 36.69 ?  194 ASN C CA    1 
ATOM   3989  C  C     . ASN C 1 194 ? 8.730   -25.472 10.422  1.00 38.88 ?  194 ASN C C     1 
ATOM   3990  O  O     . ASN C 1 194 ? 9.543   -26.298 10.013  1.00 39.29 ?  194 ASN C O     1 
ATOM   3991  C  CB    . ASN C 1 194 ? 9.729   -24.995 12.685  1.00 36.87 ?  194 ASN C CB    1 
ATOM   3992  C  CG    . ASN C 1 194 ? 11.103  -25.582 12.470  1.00 34.82 ?  194 ASN C CG    1 
ATOM   3993  O  OD1   . ASN C 1 194 ? 12.051  -24.849 12.166  1.00 35.27 ?  194 ASN C OD1   1 
ATOM   3994  N  ND2   . ASN C 1 194 ? 11.232  -26.892 12.621  1.00 32.33 ?  194 ASN C ND2   1 
ATOM   3995  N  N     . GLN C 1 195 ? 7.446   -25.468 10.048  1.00 39.93 ?  195 GLN C N     1 
ATOM   3996  C  CA    . GLN C 1 195 ? 6.958   -26.366 9.015   1.00 36.78 ?  195 GLN C CA    1 
ATOM   3997  C  C     . GLN C 1 195 ? 7.494   -25.918 7.657   1.00 37.88 ?  195 GLN C C     1 
ATOM   3998  O  O     . GLN C 1 195 ? 7.517   -26.704 6.713   1.00 38.78 ?  195 GLN C O     1 
ATOM   3999  C  CB    . GLN C 1 195 ? 5.431   -26.403 8.941   1.00 36.88 ?  195 GLN C CB    1 
ATOM   4000  C  CG    . GLN C 1 195 ? 4.740   -26.903 10.204  1.00 39.31 ?  195 GLN C CG    1 
ATOM   4001  C  CD    . GLN C 1 195 ? 3.233   -26.789 10.128  1.00 38.84 ?  195 GLN C CD    1 
ATOM   4002  O  OE1   . GLN C 1 195 ? 2.565   -27.522 9.391   1.00 37.48 ?  195 GLN C OE1   1 
ATOM   4003  N  NE2   . GLN C 1 195 ? 2.680   -25.858 10.893  1.00 39.22 ?  195 GLN C NE2   1 
ATOM   4004  N  N     . TRP C 1 196 ? 7.918   -24.651 7.562   1.00 35.19 ?  196 TRP C N     1 
ATOM   4005  C  CA    . TRP C 1 196 ? 8.286   -24.074 6.278   1.00 36.51 ?  196 TRP C CA    1 
ATOM   4006  C  C     . TRP C 1 196 ? 9.631   -23.356 6.358   1.00 34.08 ?  196 TRP C C     1 
ATOM   4007  O  O     . TRP C 1 196 ? 10.291  -23.166 5.339   1.00 33.64 ?  196 TRP C O     1 
ATOM   4008  C  CB    . TRP C 1 196 ? 7.187   -23.119 5.790   1.00 40.42 ?  196 TRP C CB    1 
ATOM   4009  C  CG    . TRP C 1 196 ? 5.809   -23.726 5.825   1.00 41.47 ?  196 TRP C CG    1 
ATOM   4010  C  CD1   . TRP C 1 196 ? 5.276   -24.595 4.919   1.00 41.76 ?  196 TRP C CD1   1 
ATOM   4011  C  CD2   . TRP C 1 196 ? 4.790   -23.512 6.826   1.00 42.29 ?  196 TRP C CD2   1 
ATOM   4012  N  NE1   . TRP C 1 196 ? 4.002   -24.938 5.283   1.00 41.53 ?  196 TRP C NE1   1 
ATOM   4013  C  CE2   . TRP C 1 196 ? 3.675   -24.291 6.446   1.00 43.74 ?  196 TRP C CE2   1 
ATOM   4014  C  CE3   . TRP C 1 196 ? 4.709   -22.745 7.994   1.00 42.32 ?  196 TRP C CE3   1 
ATOM   4015  C  CZ2   . TRP C 1 196 ? 2.500   -24.322 7.194   1.00 41.16 ?  196 TRP C CZ2   1 
ATOM   4016  C  CZ3   . TRP C 1 196 ? 3.546   -22.777 8.731   1.00 44.53 ?  196 TRP C CZ3   1 
ATOM   4017  C  CH2   . TRP C 1 196 ? 2.459   -23.556 8.336   1.00 43.33 ?  196 TRP C CH2   1 
ATOM   4018  N  N     . TYR C 1 197 ? 10.033  -22.957 7.569   1.00 29.75 ?  197 TYR C N     1 
ATOM   4019  C  CA    . TYR C 1 197 ? 11.225  -22.145 7.737   1.00 26.81 ?  197 TYR C CA    1 
ATOM   4020  C  C     . TYR C 1 197 ? 12.142  -22.784 8.775   1.00 27.33 ?  197 TYR C C     1 
ATOM   4021  O  O     . TYR C 1 197 ? 11.695  -23.172 9.852   1.00 30.60 ?  197 TYR C O     1 
ATOM   4022  C  CB    . TYR C 1 197 ? 10.817  -20.718 8.119   1.00 24.19 ?  197 TYR C CB    1 
ATOM   4023  C  CG    . TYR C 1 197 ? 9.893   -20.060 7.104   1.00 23.21 ?  197 TYR C CG    1 
ATOM   4024  C  CD1   . TYR C 1 197 ? 8.514   -20.209 7.187   1.00 23.28 ?  197 TYR C CD1   1 
ATOM   4025  C  CD2   . TYR C 1 197 ? 10.401  -19.306 6.053   1.00 20.22 ?  197 TYR C CD2   1 
ATOM   4026  C  CE1   . TYR C 1 197 ? 7.668   -19.620 6.261   1.00 22.52 ?  197 TYR C CE1   1 
ATOM   4027  C  CE2   . TYR C 1 197 ? 9.565   -18.712 5.122   1.00 19.28 ?  197 TYR C CE2   1 
ATOM   4028  C  CZ    . TYR C 1 197 ? 8.195   -18.870 5.226   1.00 19.98 ?  197 TYR C CZ    1 
ATOM   4029  O  OH    . TYR C 1 197 ? 7.369   -18.287 4.309   1.00 22.17 ?  197 TYR C OH    1 
ATOM   4030  N  N     . PRO C 1 198 ? 13.452  -22.921 8.470   1.00 28.46 ?  198 PRO C N     1 
ATOM   4031  C  CA    . PRO C 1 198 ? 14.429  -23.411 9.445   1.00 30.54 ?  198 PRO C CA    1 
ATOM   4032  C  C     . PRO C 1 198 ? 14.549  -22.481 10.650  1.00 32.26 ?  198 PRO C C     1 
ATOM   4033  O  O     . PRO C 1 198 ? 14.196  -21.306 10.567  1.00 33.11 ?  198 PRO C O     1 
ATOM   4034  C  CB    . PRO C 1 198 ? 15.737  -23.491 8.631   1.00 30.12 ?  198 PRO C CB    1 
ATOM   4035  C  CG    . PRO C 1 198 ? 15.284  -23.519 7.184   1.00 29.67 ?  198 PRO C CG    1 
ATOM   4036  C  CD    . PRO C 1 198 ? 14.048  -22.642 7.155   1.00 27.52 ?  198 PRO C CD    1 
ATOM   4037  N  N     . LEU C 1 199 ? 15.054  -23.018 11.768  1.00 31.77 ?  199 LEU C N     1 
ATOM   4038  C  CA    . LEU C 1 199 ? 15.148  -22.266 13.010  1.00 33.17 ?  199 LEU C CA    1 
ATOM   4039  C  C     . LEU C 1 199 ? 16.157  -21.130 12.855  1.00 34.06 ?  199 LEU C C     1 
ATOM   4040  O  O     . LEU C 1 199 ? 16.057  -20.116 13.542  1.00 33.86 ?  199 LEU C O     1 
ATOM   4041  C  CB    . LEU C 1 199 ? 15.517  -23.177 14.180  1.00 34.84 ?  199 LEU C CB    1 
ATOM   4042  C  CG    . LEU C 1 199 ? 14.417  -24.122 14.675  1.00 38.02 ?  199 LEU C CG    1 
ATOM   4043  C  CD1   . LEU C 1 199 ? 14.937  -24.993 15.808  1.00 37.37 ?  199 LEU C CD1   1 
ATOM   4044  C  CD2   . LEU C 1 199 ? 13.179  -23.357 15.115  1.00 37.47 ?  199 LEU C CD2   1 
ATOM   4045  N  N     . ASP C 1 200 ? 17.125  -21.305 11.948  1.00 33.36 ?  200 ASP C N     1 
ATOM   4046  C  CA    . ASP C 1 200 ? 18.183  -20.324 11.770  1.00 31.90 ?  200 ASP C CA    1 
ATOM   4047  C  C     . ASP C 1 200 ? 17.837  -19.363 10.633  1.00 26.54 ?  200 ASP C C     1 
ATOM   4048  O  O     . ASP C 1 200 ? 18.687  -18.584 10.208  1.00 23.99 ?  200 ASP C O     1 
ATOM   4049  C  CB    . ASP C 1 200 ? 19.531  -20.989 11.533  1.00 32.69 ?  200 ASP C CB    1 
ATOM   4050  C  CG    . ASP C 1 200 ? 19.684  -21.713 10.202  1.00 36.49 ?  200 ASP C CG    1 
ATOM   4051  O  OD1   . ASP C 1 200 ? 18.674  -21.829 9.477   1.00 34.64 ?  200 ASP C OD1   1 
ATOM   4052  O  OD2   . ASP C 1 200 ? 20.817  -22.141 9.895   1.00 37.47 -1 200 ASP C OD2   1 
ATOM   4053  N  N     . HIS C 1 201 ? 16.591  -19.413 10.145  1.00 25.80 ?  201 HIS C N     1 
ATOM   4054  C  CA    . HIS C 1 201 ? 16.168  -18.523 9.075   1.00 26.92 ?  201 HIS C CA    1 
ATOM   4055  C  C     . HIS C 1 201 ? 16.140  -17.089 9.592   1.00 25.62 ?  201 HIS C C     1 
ATOM   4056  O  O     . HIS C 1 201 ? 15.481  -16.794 10.587  1.00 26.08 ?  201 HIS C O     1 
ATOM   4057  C  CB    . HIS C 1 201 ? 14.805  -18.931 8.502   1.00 28.16 ?  201 HIS C CB    1 
ATOM   4058  C  CG    . HIS C 1 201 ? 14.391  -18.116 7.318   1.00 29.01 ?  201 HIS C CG    1 
ATOM   4059  N  ND1   . HIS C 1 201 ? 15.017  -18.218 6.094   1.00 29.96 ?  201 HIS C ND1   1 
ATOM   4060  C  CD2   . HIS C 1 201 ? 13.448  -17.174 7.171   1.00 30.60 ?  201 HIS C CD2   1 
ATOM   4061  C  CE1   . HIS C 1 201 ? 14.453  -17.374 5.241   1.00 30.54 ?  201 HIS C CE1   1 
ATOM   4062  N  NE2   . HIS C 1 201 ? 13.496  -16.732 5.873   1.00 31.73 ?  201 HIS C NE2   1 
ATOM   4063  N  N     . GLU C 1 202 ? 16.867  -16.205 8.902   1.00 25.73 ?  202 GLU C N     1 
ATOM   4064  C  CA    . GLU C 1 202 ? 16.906  -14.799 9.262   1.00 28.39 ?  202 GLU C CA    1 
ATOM   4065  C  C     . GLU C 1 202 ? 15.539  -14.180 8.989   1.00 27.50 ?  202 GLU C C     1 
ATOM   4066  O  O     . GLU C 1 202 ? 14.991  -14.325 7.899   1.00 26.13 ?  202 GLU C O     1 
ATOM   4067  C  CB    . GLU C 1 202 ? 17.993  -14.066 8.477   1.00 31.01 ?  202 GLU C CB    1 
ATOM   4068  C  CG    . GLU C 1 202 ? 18.108  -12.586 8.831   1.00 32.36 ?  202 GLU C CG    1 
ATOM   4069  C  CD    . GLU C 1 202 ? 19.149  -11.846 8.011   1.00 35.81 ?  202 GLU C CD    1 
ATOM   4070  O  OE1   . GLU C 1 202 ? 18.903  -11.624 6.806   1.00 34.35 ?  202 GLU C OE1   1 
ATOM   4071  O  OE2   . GLU C 1 202 ? 20.214  -11.509 8.572   1.00 36.53 -1 202 GLU C OE2   1 
ATOM   4072  N  N     . VAL C 1 203 ? 14.995  -13.502 10.003  1.00 27.64 ?  203 VAL C N     1 
ATOM   4073  C  CA    . VAL C 1 203 ? 13.766  -12.744 9.847   1.00 24.73 ?  203 VAL C CA    1 
ATOM   4074  C  C     . VAL C 1 203 ? 14.057  -11.303 10.250  1.00 25.35 ?  203 VAL C C     1 
ATOM   4075  O  O     . VAL C 1 203 ? 15.108  -11.014 10.819  1.00 23.26 ?  203 VAL C O     1 
ATOM   4076  C  CB    . VAL C 1 203 ? 12.600  -13.331 10.665  1.00 22.08 ?  203 VAL C CB    1 
ATOM   4077  C  CG1   . VAL C 1 203 ? 12.311  -14.774 10.274  1.00 23.33 ?  203 VAL C CG1   1 
ATOM   4078  C  CG2   . VAL C 1 203 ? 12.842  -13.221 12.166  1.00 23.85 ?  203 VAL C CG2   1 
ATOM   4079  N  N     . VAL C 1 204 ? 13.113  -10.407 9.949   1.00 22.66 ?  204 VAL C N     1 
ATOM   4080  C  CA    . VAL C 1 204 ? 13.302  -8.994  10.217  1.00 20.92 ?  204 VAL C CA    1 
ATOM   4081  C  C     . VAL C 1 204 ? 12.127  -8.474  11.040  1.00 21.38 ?  204 VAL C C     1 
ATOM   4082  O  O     . VAL C 1 204 ? 10.969  -8.648  10.665  1.00 19.88 ?  204 VAL C O     1 
ATOM   4083  C  CB    . VAL C 1 204 ? 13.455  -8.191  8.912   1.00 21.38 ?  204 VAL C CB    1 
ATOM   4084  C  CG1   . VAL C 1 204 ? 13.804  -6.733  9.187   1.00 19.21 ?  204 VAL C CG1   1 
ATOM   4085  C  CG2   . VAL C 1 204 ? 14.478  -8.826  7.978   1.00 21.71 ?  204 VAL C CG2   1 
ATOM   4086  N  N     . ILE C 1 205 ? 12.457  -7.835  12.166  1.00 20.29 ?  205 ILE C N     1 
ATOM   4087  C  CA    . ILE C 1 205 ? 11.494  -7.055  12.920  1.00 19.46 ?  205 ILE C CA    1 
ATOM   4088  C  C     . ILE C 1 205 ? 11.572  -5.615  12.428  1.00 18.22 ?  205 ILE C C     1 
ATOM   4089  O  O     . ILE C 1 205 ? 12.591  -4.946  12.588  1.00 17.37 ?  205 ILE C O     1 
ATOM   4090  C  CB    . ILE C 1 205 ? 11.742  -7.158  14.436  1.00 20.04 ?  205 ILE C CB    1 
ATOM   4091  C  CG1   . ILE C 1 205 ? 11.634  -8.601  14.925  1.00 18.02 ?  205 ILE C CG1   1 
ATOM   4092  C  CG2   . ILE C 1 205 ? 10.796  -6.231  15.200  1.00 20.04 ?  205 ILE C CG2   1 
ATOM   4093  C  CD1   . ILE C 1 205 ? 12.087  -8.804  16.360  1.00 19.64 ?  205 ILE C CD1   1 
ATOM   4094  N  N     . TYR C 1 206 ? 10.467  -5.165  11.826  1.00 16.55 ?  206 TYR C N     1 
ATOM   4095  C  CA    . TYR C 1 206 ? 10.390  -3.865  11.185  1.00 14.73 ?  206 TYR C CA    1 
ATOM   4096  C  C     . TYR C 1 206 ? 9.457   -2.939  11.956  1.00 15.04 ?  206 TYR C C     1 
ATOM   4097  O  O     . TYR C 1 206 ? 8.383   -3.346  12.397  1.00 14.36 ?  206 TYR C O     1 
ATOM   4098  C  CB    . TYR C 1 206 ? 9.870   -4.021  9.754   1.00 14.59 ?  206 TYR C CB    1 
ATOM   4099  C  CG    . TYR C 1 206 ? 9.604   -2.701  9.044   1.00 13.85 ?  206 TYR C CG    1 
ATOM   4100  C  CD1   . TYR C 1 206 ? 10.656  -1.872  8.676   1.00 12.76 ?  206 TYR C CD1   1 
ATOM   4101  C  CD2   . TYR C 1 206 ? 8.313   -2.292  8.724   1.00 12.66 ?  206 TYR C CD2   1 
ATOM   4102  C  CE1   . TYR C 1 206 ? 10.437  -0.670  8.026   1.00 12.10 ?  206 TYR C CE1   1 
ATOM   4103  C  CE2   . TYR C 1 206 ? 8.081   -1.092  8.071   1.00 12.96 ?  206 TYR C CE2   1 
ATOM   4104  C  CZ    . TYR C 1 206 ? 9.146   -0.281  7.719   1.00 12.57 ?  206 TYR C CZ    1 
ATOM   4105  O  OH    . TYR C 1 206 ? 8.941   0.905   7.076   1.00 16.87 ?  206 TYR C OH    1 
ATOM   4106  N  N     . GLU C 1 207 ? 9.889   -1.681  12.078  1.00 15.21 ?  207 GLU C N     1 
ATOM   4107  C  CA    . GLU C 1 207 ? 9.061   -0.608  12.597  1.00 17.28 ?  207 GLU C CA    1 
ATOM   4108  C  C     . GLU C 1 207 ? 9.335   0.654   11.787  1.00 18.71 ?  207 GLU C C     1 
ATOM   4109  O  O     . GLU C 1 207 ? 10.423  1.224   11.859  1.00 26.88 ?  207 GLU C O     1 
ATOM   4110  C  CB    . GLU C 1 207 ? 9.332   -0.378  14.084  1.00 18.47 ?  207 GLU C CB    1 
ATOM   4111  C  CG    . GLU C 1 207 ? 9.021   -1.601  14.941  1.00 19.11 ?  207 GLU C CG    1 
ATOM   4112  C  CD    . GLU C 1 207 ? 9.410   -1.479  16.402  1.00 21.05 ?  207 GLU C CD    1 
ATOM   4113  O  OE1   . GLU C 1 207 ? 9.910   -0.409  16.809  1.00 23.88 ?  207 GLU C OE1   1 
ATOM   4114  O  OE2   . GLU C 1 207 ? 9.211   -2.469  17.136  1.00 20.40 -1 207 GLU C OE2   1 
ATOM   4115  N  N     . ALA C 1 208 ? 8.335   1.061   10.999  1.00 15.49 ?  208 ALA C N     1 
ATOM   4116  C  CA    . ALA C 1 208 ? 8.379   2.311   10.259  1.00 16.28 ?  208 ALA C CA    1 
ATOM   4117  C  C     . ALA C 1 208 ? 8.494   3.481   11.230  1.00 14.23 ?  208 ALA C C     1 
ATOM   4118  O  O     . ALA C 1 208 ? 7.795   3.525   12.237  1.00 14.85 ?  208 ALA C O     1 
ATOM   4119  C  CB    . ALA C 1 208 ? 7.135   2.439   9.409   1.00 16.12 ?  208 ALA C CB    1 
ATOM   4120  N  N     . ALA C 1 209 ? 9.376   4.431   10.914  1.00 16.10 ?  209 ALA C N     1 
ATOM   4121  C  CA    . ALA C 1 209 ? 9.516   5.627   11.726  1.00 19.02 ?  209 ALA C CA    1 
ATOM   4122  C  C     . ALA C 1 209 ? 8.195   6.392   11.735  1.00 21.86 ?  209 ALA C C     1 
ATOM   4123  O  O     . ALA C 1 209 ? 7.421   6.313   10.783  1.00 21.99 ?  209 ALA C O     1 
ATOM   4124  C  CB    . ALA C 1 209 ? 10.645  6.483   11.201  1.00 18.42 ?  209 ALA C CB    1 
ATOM   4125  N  N     . ASN C 1 210 ? 7.950   7.122   12.828  1.00 21.62 ?  210 ASN C N     1 
ATOM   4126  C  CA    . ASN C 1 210 ? 6.811   8.020   12.925  1.00 22.47 ?  210 ASN C CA    1 
ATOM   4127  C  C     . ASN C 1 210 ? 7.293   9.463   12.825  1.00 21.56 ?  210 ASN C C     1 
ATOM   4128  O  O     . ASN C 1 210 ? 6.544   10.342  12.401  1.00 18.91 ?  210 ASN C O     1 
ATOM   4129  C  CB    . ASN C 1 210 ? 6.023   7.826   14.216  1.00 25.24 ?  210 ASN C CB    1 
ATOM   4130  C  CG    . ASN C 1 210 ? 5.237   6.537   14.226  1.00 25.49 ?  210 ASN C CG    1 
ATOM   4131  O  OD1   . ASN C 1 210 ? 4.594   6.194   13.228  1.00 27.95 ?  210 ASN C OD1   1 
ATOM   4132  N  ND2   . ASN C 1 210 ? 5.276   5.813   15.335  1.00 26.60 ?  210 ASN C ND2   1 
ATOM   4133  N  N     . LEU C 1 211 ? 8.548   9.697   13.226  1.00 17.63 ?  211 LEU C N     1 
ATOM   4134  C  CA    . LEU C 1 211 ? 9.096   11.042  13.255  1.00 20.18 ?  211 LEU C CA    1 
ATOM   4135  C  C     . LEU C 1 211 ? 10.184  11.188  12.195  1.00 21.02 ?  211 LEU C C     1 
ATOM   4136  O  O     . LEU C 1 211 ? 10.841  10.216  11.822  1.00 14.43 ?  211 LEU C O     1 
ATOM   4137  C  CB    . LEU C 1 211 ? 9.614   11.369  14.654  1.00 22.19 ?  211 LEU C CB    1 
ATOM   4138  C  CG    . LEU C 1 211 ? 8.560   11.367  15.766  1.00 23.55 ?  211 LEU C CG    1 
ATOM   4139  C  CD1   . LEU C 1 211 ? 9.210   11.667  17.103  1.00 25.60 ?  211 LEU C CD1   1 
ATOM   4140  C  CD2   . LEU C 1 211 ? 7.445   12.357  15.469  1.00 25.21 ?  211 LEU C CD2   1 
ATOM   4141  N  N     . PRO C 1 212 ? 10.380  12.418  11.669  1.00 20.05 ?  212 PRO C N     1 
ATOM   4142  C  CA    . PRO C 1 212 ? 11.334  12.665  10.585  1.00 21.84 ?  212 PRO C CA    1 
ATOM   4143  C  C     . PRO C 1 212 ? 12.806  12.604  10.989  1.00 23.52 ?  212 PRO C C     1 
ATOM   4144  O  O     . PRO C 1 212 ? 13.683  12.544  10.129  1.00 23.58 ?  212 PRO C O     1 
ATOM   4145  C  CB    . PRO C 1 212 ? 10.926  14.071  10.118  1.00 20.94 ?  212 PRO C CB    1 
ATOM   4146  C  CG    . PRO C 1 212 ? 10.407  14.738  11.372  1.00 22.08 ?  212 PRO C CG    1 
ATOM   4147  C  CD    . PRO C 1 212 ? 9.653   13.630  12.081  1.00 23.89 ?  212 PRO C CD    1 
ATOM   4148  N  N     . ILE C 1 213 ? 13.058  12.627  12.302  1.00 22.68 ?  213 ILE C N     1 
ATOM   4149  C  CA    . ILE C 1 213 ? 14.408  12.581  12.844  1.00 24.37 ?  213 ILE C CA    1 
ATOM   4150  C  C     . ILE C 1 213 ? 14.728  11.153  13.281  1.00 24.51 ?  213 ILE C C     1 
ATOM   4151  O  O     . ILE C 1 213 ? 15.809  10.888  13.802  1.00 24.98 ?  213 ILE C O     1 
ATOM   4152  C  CB    . ILE C 1 213 ? 14.568  13.575  14.012  1.00 25.23 ?  213 ILE C CB    1 
ATOM   4153  C  CG1   . ILE C 1 213 ? 13.493  13.388  15.090  1.00 27.67 ?  213 ILE C CG1   1 
ATOM   4154  C  CG2   . ILE C 1 213 ? 14.589  15.016  13.503  1.00 23.72 ?  213 ILE C CG2   1 
ATOM   4155  C  CD1   . ILE C 1 213 ? 13.490  12.024  15.756  1.00 26.26 ?  213 ILE C CD1   1 
ATOM   4156  N  N     . GLN C 1 214 ? 13.776  10.241  13.057  1.00 26.13 ?  214 GLN C N     1 
ATOM   4157  C  CA    . GLN C 1 214 ? 13.875  8.880   13.560  1.00 26.47 ?  214 GLN C CA    1 
ATOM   4158  C  C     . GLN C 1 214 ? 14.150  7.914   12.414  1.00 25.33 ?  214 GLN C C     1 
ATOM   4159  O  O     . GLN C 1 214 ? 13.512  7.984   11.366  1.00 26.31 ?  214 GLN C O     1 
ATOM   4160  C  CB    . GLN C 1 214 ? 12.586  8.452   14.261  1.00 27.28 ?  214 GLN C CB    1 
ATOM   4161  C  CG    . GLN C 1 214 ? 12.380  6.940   14.299  1.00 24.51 ?  214 GLN C CG    1 
ATOM   4162  C  CD    . GLN C 1 214 ? 11.023  6.536   14.832  1.00 24.24 ?  214 GLN C CD    1 
ATOM   4163  O  OE1   . GLN C 1 214 ? 9.993   7.119   14.475  1.00 20.99 ?  214 GLN C OE1   1 
ATOM   4164  N  NE2   . GLN C 1 214 ? 11.010  5.535   15.701  1.00 23.11 ?  214 GLN C NE2   1 
ATOM   4165  N  N     . ALA C 1 215 ? 15.099  7.002   12.645  1.00 25.70 ?  215 ALA C N     1 
ATOM   4166  C  CA    . ALA C 1 215 ? 15.372  5.920   11.716  1.00 24.21 ?  215 ALA C CA    1 
ATOM   4167  C  C     . ALA C 1 215 ? 14.432  4.757   12.011  1.00 23.61 ?  215 ALA C C     1 
ATOM   4168  O  O     . ALA C 1 215 ? 13.983  4.590   13.142  1.00 26.65 ?  215 ALA C O     1 
ATOM   4169  C  CB    . ALA C 1 215 ? 16.820  5.497   11.825  1.00 26.79 ?  215 ALA C CB    1 
ATOM   4170  N  N     . PRO C 1 216 ? 14.104  3.915   11.006  1.00 25.17 ?  216 PRO C N     1 
ATOM   4171  C  CA    . PRO C 1 216 ? 13.255  2.750   11.241  1.00 25.32 ?  216 PRO C CA    1 
ATOM   4172  C  C     . PRO C 1 216 ? 14.000  1.670   12.014  1.00 23.03 ?  216 PRO C C     1 
ATOM   4173  O  O     . PRO C 1 216 ? 15.229  1.640   12.029  1.00 21.64 ?  216 PRO C O     1 
ATOM   4174  C  CB    . PRO C 1 216 ? 12.905  2.304   9.817   1.00 25.27 ?  216 PRO C CB    1 
ATOM   4175  C  CG    . PRO C 1 216 ? 14.128  2.688   9.021   1.00 25.01 ?  216 PRO C CG    1 
ATOM   4176  C  CD    . PRO C 1 216 ? 14.539  4.030   9.605   1.00 26.08 ?  216 PRO C CD    1 
ATOM   4177  N  N     . ARG C 1 217 ? 13.234  0.788   12.655  1.00 23.06 ?  217 ARG C N     1 
ATOM   4178  C  CA    . ARG C 1 217 ? 13.795  -0.423  13.220  1.00 22.48 ?  217 ARG C CA    1 
ATOM   4179  C  C     . ARG C 1 217 ? 13.806  -1.496  12.138  1.00 21.88 ?  217 ARG C C     1 
ATOM   4180  O  O     . ARG C 1 217 ? 12.760  -1.866  11.611  1.00 18.67 ?  217 ARG C O     1 
ATOM   4181  C  CB    . ARG C 1 217 ? 12.990  -0.901  14.431  1.00 23.14 ?  217 ARG C CB    1 
ATOM   4182  C  CG    . ARG C 1 217 ? 13.617  -2.098  15.127  1.00 23.68 ?  217 ARG C CG    1 
ATOM   4183  C  CD    . ARG C 1 217 ? 12.701  -2.590  16.226  1.00 24.16 ?  217 ARG C CD    1 
ATOM   4184  N  NE    . ARG C 1 217 ? 13.272  -3.677  17.026  1.00 24.31 ?  217 ARG C NE    1 
ATOM   4185  C  CZ    . ARG C 1 217 ? 12.567  -4.368  17.910  1.00 25.20 ?  217 ARG C CZ    1 
ATOM   4186  N  NH1   . ARG C 1 217 ? 11.285  -4.095  18.078  1.00 22.89 1  217 ARG C NH1   1 
ATOM   4187  N  NH2   . ARG C 1 217 ? 13.137  -5.331  18.612  1.00 23.11 ?  217 ARG C NH2   1 
ATOM   4188  N  N     . ILE C 1 218 ? 15.009  -1.965  11.801  1.00 22.99 ?  218 ILE C N     1 
ATOM   4189  C  CA    . ILE C 1 218 ? 15.171  -3.071  10.876  1.00 25.87 ?  218 ILE C CA    1 
ATOM   4190  C  C     . ILE C 1 218 ? 16.128  -4.070  11.518  1.00 25.39 ?  218 ILE C C     1 
ATOM   4191  O  O     . ILE C 1 218 ? 17.331  -4.047  11.263  1.00 22.01 ?  218 ILE C O     1 
ATOM   4192  C  CB    . ILE C 1 218 ? 15.660  -2.576  9.502   1.00 28.21 ?  218 ILE C CB    1 
ATOM   4193  C  CG1   . ILE C 1 218 ? 14.822  -1.397  9.001   1.00 30.73 ?  218 ILE C CG1   1 
ATOM   4194  C  CG2   . ILE C 1 218 ? 15.688  -3.720  8.488   1.00 30.26 ?  218 ILE C CG2   1 
ATOM   4195  C  CD1   . ILE C 1 218 ? 15.389  -0.708  7.773   1.00 34.62 ?  218 ILE C CD1   1 
ATOM   4196  N  N     . GLU C 1 219 ? 15.570  -4.930  12.376  1.00 24.63 ?  219 GLU C N     1 
ATOM   4197  C  CA    . GLU C 1 219 ? 16.366  -5.816  13.205  1.00 27.29 ?  219 GLU C CA    1 
ATOM   4198  C  C     . GLU C 1 219 ? 16.311  -7.231  12.636  1.00 25.80 ?  219 GLU C C     1 
ATOM   4199  O  O     . GLU C 1 219 ? 15.246  -7.841  12.565  1.00 23.09 ?  219 GLU C O     1 
ATOM   4200  C  CB    . GLU C 1 219 ? 15.875  -5.751  14.651  1.00 28.92 ?  219 GLU C CB    1 
ATOM   4201  C  CG    . GLU C 1 219 ? 16.724  -6.575  15.614  1.00 31.82 ?  219 GLU C CG    1 
ATOM   4202  C  CD    . GLU C 1 219 ? 16.278  -6.481  17.061  1.00 33.78 ?  219 GLU C CD    1 
ATOM   4203  O  OE1   . GLU C 1 219 ? 16.339  -5.368  17.626  1.00 33.63 ?  219 GLU C OE1   1 
ATOM   4204  O  OE2   . GLU C 1 219 ? 15.863  -7.517  17.622  1.00 38.59 -1 219 GLU C OE2   1 
ATOM   4205  N  N     . ARG C 1 220 ? 17.483  -7.733  12.235  1.00 25.71 ?  220 ARG C N     1 
ATOM   4206  C  CA    . ARG C 1 220 ? 17.609  -9.059  11.654  1.00 29.05 ?  220 ARG C CA    1 
ATOM   4207  C  C     . ARG C 1 220 ? 18.082  -10.037 12.724  1.00 27.34 ?  220 ARG C C     1 
ATOM   4208  O  O     . ARG C 1 220 ? 19.008  -9.744  13.478  1.00 28.81 ?  220 ARG C O     1 
ATOM   4209  C  CB    . ARG C 1 220 ? 18.591  -9.029  10.477  1.00 31.09 ?  220 ARG C CB    1 
ATOM   4210  C  CG    . ARG C 1 220 ? 18.107  -8.189  9.305   1.00 31.34 ?  220 ARG C CG    1 
ATOM   4211  C  CD    . ARG C 1 220 ? 19.238  -7.788  8.374   1.00 30.41 ?  220 ARG C CD    1 
ATOM   4212  N  NE    . ARG C 1 220 ? 18.754  -6.925  7.292   1.00 31.86 ?  220 ARG C NE    1 
ATOM   4213  C  CZ    . ARG C 1 220 ? 18.066  -7.343  6.235   1.00 32.61 ?  220 ARG C CZ    1 
ATOM   4214  N  NH1   . ARG C 1 220 ? 17.877  -8.635  6.030   1.00 31.80 1  220 ARG C NH1   1 
ATOM   4215  N  NH2   . ARG C 1 220 ? 17.593  -6.464  5.369   1.00 32.21 ?  220 ARG C NH2   1 
ATOM   4216  N  N     . LEU C 1 221 ? 17.437  -11.205 12.766  1.00 27.88 ?  221 LEU C N     1 
ATOM   4217  C  CA    . LEU C 1 221 ? 17.727  -12.208 13.775  1.00 26.85 ?  221 LEU C CA    1 
ATOM   4218  C  C     . LEU C 1 221 ? 17.202  -13.554 13.291  1.00 28.07 ?  221 LEU C C     1 
ATOM   4219  O  O     . LEU C 1 221 ? 16.258  -13.609 12.505  1.00 31.96 ?  221 LEU C O     1 
ATOM   4220  C  CB    . LEU C 1 221 ? 17.100  -11.820 15.115  1.00 27.29 ?  221 LEU C CB    1 
ATOM   4221  C  CG    . LEU C 1 221 ? 15.584  -12.015 15.237  1.00 25.57 ?  221 LEU C CG    1 
ATOM   4222  C  CD1   . LEU C 1 221 ? 15.140  -11.931 16.689  1.00 25.65 ?  221 LEU C CD1   1 
ATOM   4223  C  CD2   . LEU C 1 221 ? 14.820  -11.006 14.398  1.00 26.07 ?  221 LEU C CD2   1 
ATOM   4224  N  N     . PRO C 1 222 ? 17.795  -14.680 13.742  1.00 27.86 ?  222 PRO C N     1 
ATOM   4225  C  CA    . PRO C 1 222 ? 17.263  -15.999 13.411  1.00 26.83 ?  222 PRO C CA    1 
ATOM   4226  C  C     . PRO C 1 222 ? 15.856  -16.129 13.984  1.00 24.88 ?  222 PRO C C     1 
ATOM   4227  O  O     . PRO C 1 222 ? 15.546  -15.548 15.022  1.00 25.28 ?  222 PRO C O     1 
ATOM   4228  C  CB    . PRO C 1 222 ? 18.264  -16.982 14.045  1.00 28.13 ?  222 PRO C CB    1 
ATOM   4229  C  CG    . PRO C 1 222 ? 18.956  -16.169 15.123  1.00 30.08 ?  222 PRO C CG    1 
ATOM   4230  C  CD    . PRO C 1 222 ? 18.989  -14.741 14.599  1.00 28.67 ?  222 PRO C CD    1 
ATOM   4231  N  N     . LEU C 1 223 ? 15.011  -16.888 13.283  1.00 22.52 ?  223 LEU C N     1 
ATOM   4232  C  CA    . LEU C 1 223 ? 13.646  -17.137 13.710  1.00 22.61 ?  223 LEU C CA    1 
ATOM   4233  C  C     . LEU C 1 223 ? 13.617  -17.631 15.155  1.00 25.11 ?  223 LEU C C     1 
ATOM   4234  O  O     . LEU C 1 223 ? 12.660  -17.369 15.881  1.00 26.91 ?  223 LEU C O     1 
ATOM   4235  C  CB    . LEU C 1 223 ? 13.055  -18.163 12.745  1.00 22.95 ?  223 LEU C CB    1 
ATOM   4236  C  CG    . LEU C 1 223 ? 11.660  -18.694 13.086  1.00 23.92 ?  223 LEU C CG    1 
ATOM   4237  C  CD1   . LEU C 1 223 ? 10.610  -17.597 13.026  1.00 25.10 ?  223 LEU C CD1   1 
ATOM   4238  C  CD2   . LEU C 1 223 ? 11.307  -19.836 12.148  1.00 23.71 ?  223 LEU C CD2   1 
ATOM   4239  N  N     . ALA C 1 224 ? 14.671  -18.342 15.570  1.00 26.23 ?  224 ALA C N     1 
ATOM   4240  C  CA    . ALA C 1 224 ? 14.654  -19.060 16.835  1.00 28.76 ?  224 ALA C CA    1 
ATOM   4241  C  C     . ALA C 1 224 ? 14.702  -18.084 18.010  1.00 26.57 ?  224 ALA C C     1 
ATOM   4242  O  O     . ALA C 1 224 ? 14.269  -18.419 19.110  1.00 25.75 ?  224 ALA C O     1 
ATOM   4243  C  CB    . ALA C 1 224 ? 15.797  -20.052 16.884  1.00 28.76 ?  224 ALA C CB    1 
ATOM   4244  N  N     . ASN C 1 225 ? 15.217  -16.875 17.760  1.00 27.70 ?  225 ASN C N     1 
ATOM   4245  C  CA    . ASN C 1 225 ? 15.413  -15.876 18.801  1.00 29.94 ?  225 ASN C CA    1 
ATOM   4246  C  C     . ASN C 1 225 ? 14.251  -14.883 18.846  1.00 34.49 ?  225 ASN C C     1 
ATOM   4247  O  O     . ASN C 1 225 ? 14.356  -13.848 19.500  1.00 43.80 ?  225 ASN C O     1 
ATOM   4248  C  CB    . ASN C 1 225 ? 16.719  -15.112 18.602  1.00 28.36 ?  225 ASN C CB    1 
ATOM   4249  C  CG    . ASN C 1 225 ? 17.937  -15.958 18.891  1.00 25.52 ?  225 ASN C CG    1 
ATOM   4250  O  OD1   . ASN C 1 225 ? 17.807  -17.101 19.341  1.00 24.24 ?  225 ASN C OD1   1 
ATOM   4251  N  ND2   . ASN C 1 225 ? 19.122  -15.414 18.652  1.00 24.65 ?  225 ASN C ND2   1 
ATOM   4252  N  N     . LEU C 1 226 ? 13.147  -15.194 18.156  1.00 33.28 ?  226 LEU C N     1 
ATOM   4253  C  CA    . LEU C 1 226 ? 12.002  -14.297 18.106  1.00 31.11 ?  226 LEU C CA    1 
ATOM   4254  C  C     . LEU C 1 226 ? 11.380  -14.170 19.497  1.00 34.42 ?  226 LEU C C     1 
ATOM   4255  O  O     . LEU C 1 226 ? 11.007  -13.073 19.908  1.00 37.57 ?  226 LEU C O     1 
ATOM   4256  C  CB    . LEU C 1 226 ? 10.975  -14.769 17.075  1.00 29.96 ?  226 LEU C CB    1 
ATOM   4257  C  CG    . LEU C 1 226 ? 9.686   -13.944 16.981  1.00 28.67 ?  226 LEU C CG    1 
ATOM   4258  C  CD1   . LEU C 1 226 ? 9.995   -12.469 16.792  1.00 30.80 ?  226 LEU C CD1   1 
ATOM   4259  C  CD2   . LEU C 1 226 ? 8.776   -14.429 15.863  1.00 28.28 ?  226 LEU C CD2   1 
ATOM   4260  N  N     . PRO C 1 227 ? 11.229  -15.279 20.259  1.00 31.96 ?  227 PRO C N     1 
ATOM   4261  C  CA    . PRO C 1 227 ? 10.580  -15.231 21.573  1.00 29.92 ?  227 PRO C CA    1 
ATOM   4262  C  C     . PRO C 1 227 ? 11.299  -14.398 22.633  1.00 26.72 ?  227 PRO C C     1 
ATOM   4263  O  O     . PRO C 1 227 ? 10.721  -14.101 23.676  1.00 23.57 ?  227 PRO C O     1 
ATOM   4264  C  CB    . PRO C 1 227 ? 10.499  -16.715 21.988  1.00 31.46 ?  227 PRO C CB    1 
ATOM   4265  C  CG    . PRO C 1 227 ? 10.667  -17.486 20.698  1.00 31.80 ?  227 PRO C CG    1 
ATOM   4266  C  CD    . PRO C 1 227 ? 11.619  -16.642 19.870  1.00 31.85 ?  227 PRO C CD    1 
ATOM   4267  N  N     . GLN C 1 228 ? 12.560  -14.034 22.371  1.00 28.23 ?  228 GLN C N     1 
ATOM   4268  C  CA    . GLN C 1 228 ? 13.326  -13.242 23.321  1.00 29.47 ?  228 GLN C CA    1 
ATOM   4269  C  C     . GLN C 1 228 ? 13.489  -11.818 22.799  1.00 29.19 ?  228 GLN C C     1 
ATOM   4270  O  O     . GLN C 1 228 ? 14.265  -11.041 23.352  1.00 28.02 ?  228 GLN C O     1 
ATOM   4271  C  CB    . GLN C 1 228 ? 14.729  -13.789 23.593  1.00 31.05 ?  228 GLN C CB    1 
ATOM   4272  C  CG    . GLN C 1 228 ? 14.769  -15.236 24.073  1.00 31.02 ?  228 GLN C CG    1 
ATOM   4273  C  CD    . GLN C 1 228 ? 15.014  -16.224 22.954  1.00 29.73 ?  228 GLN C CD    1 
ATOM   4274  O  OE1   . GLN C 1 228 ? 16.090  -16.256 22.347  1.00 30.62 ?  228 GLN C OE1   1 
ATOM   4275  N  NE2   . GLN C 1 228 ? 14.017  -17.051 22.677  1.00 29.41 ?  228 GLN C NE2   1 
ATOM   4276  N  N     . ALA C 1 229 ? 12.759  -11.487 21.730  1.00 28.22 ?  229 ALA C N     1 
ATOM   4277  C  CA    . ALA C 1 229 ? 12.910  -10.196 21.082  1.00 30.68 ?  229 ALA C CA    1 
ATOM   4278  C  C     . ALA C 1 229 ? 12.010  -9.169  21.759  1.00 30.56 ?  229 ALA C C     1 
ATOM   4279  O  O     . ALA C 1 229 ? 11.002  -9.519  22.370  1.00 30.39 ?  229 ALA C O     1 
ATOM   4280  C  CB    . ALA C 1 229 ? 12.604  -10.313 19.605  1.00 33.29 ?  229 ALA C CB    1 
ATOM   4281  N  N     . HIS C 1 230 ? 12.402  -7.897  21.644  1.00 30.95 ?  230 HIS C N     1 
ATOM   4282  C  CA    . HIS C 1 230 ? 11.617  -6.793  22.165  1.00 31.14 ?  230 HIS C CA    1 
ATOM   4283  C  C     . HIS C 1 230 ? 10.669  -6.316  21.068  1.00 27.40 ?  230 HIS C C     1 
ATOM   4284  O  O     . HIS C 1 230 ? 11.108  -5.741  20.075  1.00 29.01 ?  230 HIS C O     1 
ATOM   4285  C  CB    . HIS C 1 230 ? 12.548  -5.686  22.673  1.00 37.69 ?  230 HIS C CB    1 
ATOM   4286  C  CG    . HIS C 1 230 ? 11.845  -4.546  23.330  1.00 46.30 ?  230 HIS C CG    1 
ATOM   4287  N  ND1   . HIS C 1 230 ? 11.532  -4.542  24.672  1.00 55.35 ?  230 HIS C ND1   1 
ATOM   4288  C  CD2   . HIS C 1 230 ? 11.399  -3.381  22.841  1.00 51.31 ?  230 HIS C CD2   1 
ATOM   4289  C  CE1   . HIS C 1 230 ? 10.917  -3.408  24.973  1.00 57.57 ?  230 HIS C CE1   1 
ATOM   4290  N  NE2   . HIS C 1 230 ? 10.826  -2.687  23.876  1.00 53.88 ?  230 HIS C NE2   1 
ATOM   4291  N  N     . LEU C 1 231 ? 9.368   -6.575  21.255  1.00 24.51 ?  231 LEU C N     1 
ATOM   4292  C  CA    . LEU C 1 231 ? 8.362   -6.261  20.252  1.00 25.04 ?  231 LEU C CA    1 
ATOM   4293  C  C     . LEU C 1 231 ? 7.461   -5.135  20.758  1.00 27.97 ?  231 LEU C C     1 
ATOM   4294  O  O     . LEU C 1 231 ? 7.146   -5.068  21.945  1.00 29.41 ?  231 LEU C O     1 
ATOM   4295  C  CB    . LEU C 1 231 ? 7.550   -7.513  19.917  1.00 22.27 ?  231 LEU C CB    1 
ATOM   4296  C  CG    . LEU C 1 231 ? 8.308   -8.668  19.253  1.00 21.12 ?  231 LEU C CG    1 
ATOM   4297  C  CD1   . LEU C 1 231 ? 7.368   -9.840  19.031  1.00 20.92 ?  231 LEU C CD1   1 
ATOM   4298  C  CD2   . LEU C 1 231 ? 8.957   -8.261  17.942  1.00 20.36 ?  231 LEU C CD2   1 
ATOM   4299  N  N     . MET C 1 232 ? 7.048   -4.258  19.835  1.00 28.66 ?  232 MET C N     1 
ATOM   4300  C  CA    . MET C 1 232 ? 6.168   -3.142  20.149  1.00 31.37 ?  232 MET C CA    1 
ATOM   4301  C  C     . MET C 1 232 ? 4.874   -3.294  19.353  1.00 34.79 ?  232 MET C C     1 
ATOM   4302  O  O     . MET C 1 232 ? 4.838   -4.024  18.365  1.00 30.22 ?  232 MET C O     1 
ATOM   4303  C  CB    . MET C 1 232 ? 6.828   -1.802  19.801  1.00 33.89 ?  232 MET C CB    1 
ATOM   4304  C  CG    . MET C 1 232 ? 8.104   -1.502  20.573  1.00 36.40 ?  232 MET C CG    1 
ATOM   4305  S  SD    . MET C 1 232 ? 7.875   -1.379  22.359  1.00 44.33 ?  232 MET C SD    1 
ATOM   4306  C  CE    . MET C 1 232 ? 6.692   -0.034  22.520  1.00 50.53 ?  232 MET C CE    1 
ATOM   4307  N  N     . PRO C 1 233 ? 3.769   -2.623  19.753  1.00 36.85 ?  233 PRO C N     1 
ATOM   4308  C  CA    . PRO C 1 233 ? 2.498   -2.743  19.036  1.00 34.10 ?  233 PRO C CA    1 
ATOM   4309  C  C     . PRO C 1 233 ? 2.607   -2.384  17.556  1.00 30.03 ?  233 PRO C C     1 
ATOM   4310  O  O     . PRO C 1 233 ? 1.798   -2.833  16.746  1.00 29.29 ?  233 PRO C O     1 
ATOM   4311  C  CB    . PRO C 1 233 ? 1.576   -1.779  19.806  1.00 32.58 ?  233 PRO C CB    1 
ATOM   4312  C  CG    . PRO C 1 233 ? 2.175   -1.741  21.193  1.00 33.80 ?  233 PRO C CG    1 
ATOM   4313  C  CD    . PRO C 1 233 ? 3.673   -1.748  20.934  1.00 36.22 ?  233 PRO C CD    1 
ATOM   4314  N  N     . ILE C 1 234 ? 3.616   -1.575  17.217  1.00 25.75 ?  234 ILE C N     1 
ATOM   4315  C  CA    . ILE C 1 234 ? 3.822   -1.126  15.848  1.00 24.01 ?  234 ILE C CA    1 
ATOM   4316  C  C     . ILE C 1 234 ? 4.822   -2.033  15.131  1.00 24.83 ?  234 ILE C C     1 
ATOM   4317  O  O     . ILE C 1 234 ? 5.335   -1.663  14.078  1.00 26.84 ?  234 ILE C O     1 
ATOM   4318  C  CB    . ILE C 1 234 ? 4.297   0.339   15.812  1.00 26.81 ?  234 ILE C CB    1 
ATOM   4319  C  CG1   . ILE C 1 234 ? 5.546   0.545   16.672  1.00 26.10 ?  234 ILE C CG1   1 
ATOM   4320  C  CG2   . ILE C 1 234 ? 3.171   1.292   16.213  1.00 27.97 ?  234 ILE C CG2   1 
ATOM   4321  C  CD1   . ILE C 1 234 ? 6.379   1.752   16.278  1.00 21.65 ?  234 ILE C CD1   1 
ATOM   4322  N  N     . SER C 1 235 ? 5.101   -3.216  15.690  1.00 23.73 ?  235 SER C N     1 
ATOM   4323  C  CA    . SER C 1 235 ? 6.102   -4.099  15.111  1.00 23.14 ?  235 SER C CA    1 
ATOM   4324  C  C     . SER C 1 235 ? 5.466   -5.025  14.075  1.00 19.24 ?  235 SER C C     1 
ATOM   4325  O  O     . SER C 1 235 ? 4.457   -5.670  14.344  1.00 19.55 ?  235 SER C O     1 
ATOM   4326  C  CB    . SER C 1 235 ? 6.830   -4.884  16.179  1.00 25.57 ?  235 SER C CB    1 
ATOM   4327  O  OG    . SER C 1 235 ? 7.714   -4.049  16.916  1.00 20.89 ?  235 SER C OG    1 
ATOM   4328  N  N     . THR C 1 236 ? 6.070   -5.073  12.882  1.00 21.80 ?  236 THR C N     1 
ATOM   4329  C  CA    . THR C 1 236 ? 5.692   -6.043  11.867  1.00 21.85 ?  236 THR C CA    1 
ATOM   4330  C  C     . THR C 1 236 ? 6.851   -7.011  11.642  1.00 19.74 ?  236 THR C C     1 
ATOM   4331  O  O     . THR C 1 236 ? 8.014   -6.613  11.645  1.00 18.23 ?  236 THR C O     1 
ATOM   4332  C  CB    . THR C 1 236 ? 5.291   -5.329  10.577  1.00 22.42 ?  236 THR C CB    1 
ATOM   4333  O  OG1   . THR C 1 236 ? 4.102   -4.612  10.897  1.00 22.89 ?  236 THR C OG1   1 
ATOM   4334  C  CG2   . THR C 1 236 ? 5.023   -6.299  9.441   1.00 23.31 ?  236 THR C CG2   1 
ATOM   4335  N  N     . LEU C 1 237 ? 6.509   -8.290  11.445  1.00 20.99 ?  237 LEU C N     1 
ATOM   4336  C  CA    . LEU C 1 237 ? 7.494   -9.340  11.247  1.00 18.33 ?  237 LEU C CA    1 
ATOM   4337  C  C     . LEU C 1 237 ? 7.593   -9.676  9.761   1.00 18.87 ?  237 LEU C C     1 
ATOM   4338  O  O     . LEU C 1 237 ? 6.606   -10.067 9.141   1.00 17.46 ?  237 LEU C O     1 
ATOM   4339  C  CB    . LEU C 1 237 ? 7.120   -10.576 12.063  1.00 19.05 ?  237 LEU C CB    1 
ATOM   4340  C  CG    . LEU C 1 237 ? 8.077   -11.766 11.930  1.00 18.82 ?  237 LEU C CG    1 
ATOM   4341  C  CD1   . LEU C 1 237 ? 9.427   -11.413 12.523  1.00 19.91 ?  237 LEU C CD1   1 
ATOM   4342  C  CD2   . LEU C 1 237 ? 7.525   -13.026 12.570  1.00 18.79 ?  237 LEU C CD2   1 
ATOM   4343  N  N     . LEU C 1 238 ? 8.805   -9.522  9.214   1.00 16.37 ?  238 LEU C N     1 
ATOM   4344  C  CA    . LEU C 1 238 ? 9.108   -9.897  7.843   1.00 15.35 ?  238 LEU C CA    1 
ATOM   4345  C  C     . LEU C 1 238 ? 9.871   -11.219 7.835   1.00 17.60 ?  238 LEU C C     1 
ATOM   4346  O  O     . LEU C 1 238 ? 10.870  -11.370 8.536   1.00 16.70 ?  238 LEU C O     1 
ATOM   4347  C  CB    . LEU C 1 238 ? 9.929   -8.801  7.167   1.00 14.73 ?  238 LEU C CB    1 
ATOM   4348  C  CG    . LEU C 1 238 ? 10.462  -9.136  5.770   1.00 14.12 ?  238 LEU C CG    1 
ATOM   4349  C  CD1   . LEU C 1 238 ? 9.341   -9.168  4.747   1.00 14.09 ?  238 LEU C CD1   1 
ATOM   4350  C  CD2   . LEU C 1 238 ? 11.542  -8.158  5.351   1.00 13.66 ?  238 LEU C CD2   1 
ATOM   4351  N  N     . ILE C 1 239 ? 9.397   -12.161 7.015   1.00 18.77 ?  239 ILE C N     1 
ATOM   4352  C  CA    . ILE C 1 239 ? 10.015  -13.470 6.890   1.00 17.70 ?  239 ILE C CA    1 
ATOM   4353  C  C     . ILE C 1 239 ? 10.394  -13.688 5.428   1.00 18.15 ?  239 ILE C C     1 
ATOM   4354  O  O     . ILE C 1 239 ? 9.584   -14.181 4.646   1.00 18.97 ?  239 ILE C O     1 
ATOM   4355  C  CB    . ILE C 1 239 ? 9.062   -14.564 7.402   1.00 18.67 ?  239 ILE C CB    1 
ATOM   4356  C  CG1   . ILE C 1 239 ? 8.657   -14.307 8.854   1.00 19.60 ?  239 ILE C CG1   1 
ATOM   4357  C  CG2   . ILE C 1 239 ? 9.668   -15.956 7.211   1.00 18.79 ?  239 ILE C CG2   1 
ATOM   4358  C  CD1   . ILE C 1 239 ? 7.599   -15.257 9.385   1.00 20.39 ?  239 ILE C CD1   1 
ATOM   4359  N  N     . PRO C 1 240 ? 11.627  -13.323 5.011   1.00 16.64 ?  240 PRO C N     1 
ATOM   4360  C  CA    . PRO C 1 240 ? 12.007  -13.403 3.601   1.00 18.21 ?  240 PRO C CA    1 
ATOM   4361  C  C     . PRO C 1 240 ? 11.872  -14.828 3.076   1.00 20.85 ?  240 PRO C C     1 
ATOM   4362  O  O     . PRO C 1 240 ? 11.674  -15.764 3.848   1.00 19.25 ?  240 PRO C O     1 
ATOM   4363  C  CB    . PRO C 1 240 ? 13.460  -12.898 3.590   1.00 17.98 ?  240 PRO C CB    1 
ATOM   4364  C  CG    . PRO C 1 240 ? 13.569  -12.068 4.852   1.00 17.67 ?  240 PRO C CG    1 
ATOM   4365  C  CD    . PRO C 1 240 ? 12.715  -12.816 5.863   1.00 17.44 ?  240 PRO C CD    1 
ATOM   4366  N  N     . PRO C 1 241 ? 11.969  -15.032 1.743   1.00 21.93 ?  241 PRO C N     1 
ATOM   4367  C  CA    . PRO C 1 241 ? 11.786  -16.358 1.155   1.00 24.95 ?  241 PRO C CA    1 
ATOM   4368  C  C     . PRO C 1 241 ? 12.764  -17.366 1.748   1.00 22.74 ?  241 PRO C C     1 
ATOM   4369  O  O     . PRO C 1 241 ? 13.936  -17.057 1.948   1.00 21.53 ?  241 PRO C O     1 
ATOM   4370  C  CB    . PRO C 1 241 ? 12.027  -16.131 -0.350  1.00 25.48 ?  241 PRO C CB    1 
ATOM   4371  C  CG    . PRO C 1 241 ? 11.799  -14.648 -0.549  1.00 24.49 ?  241 PRO C CG    1 
ATOM   4372  C  CD    . PRO C 1 241 ? 12.267  -13.998 0.741   1.00 24.31 ?  241 PRO C CD    1 
ATOM   4373  N  N     . ALA C 1 242 ? 12.259  -18.571 2.029   1.00 24.16 ?  242 ALA C N     1 
ATOM   4374  C  CA    . ALA C 1 242 ? 13.094  -19.674 2.470   1.00 24.80 ?  242 ALA C CA    1 
ATOM   4375  C  C     . ALA C 1 242 ? 13.655  -20.400 1.251   1.00 29.48 ?  242 ALA C C     1 
ATOM   4376  O  O     . ALA C 1 242 ? 14.682  -21.071 1.338   1.00 25.41 ?  242 ALA C O     1 
ATOM   4377  C  CB    . ALA C 1 242 ? 12.294  -20.608 3.351   1.00 23.76 ?  242 ALA C CB    1 
ATOM   4378  N  N     . LYS C 1 243 ? 12.964  -20.247 0.114   1.00 30.64 ?  243 LYS C N     1 
ATOM   4379  C  CA    . LYS C 1 243 ? 13.341  -20.913 -1.122  1.00 33.87 ?  243 LYS C CA    1 
ATOM   4380  C  C     . LYS C 1 243 ? 13.372  -19.913 -2.275  1.00 36.01 ?  243 LYS C C     1 
ATOM   4381  O  O     . LYS C 1 243 ? 12.704  -18.882 -2.238  1.00 39.18 ?  243 LYS C O     1 
ATOM   4382  C  CB    . LYS C 1 243 ? 12.347  -22.027 -1.468  1.00 34.75 ?  243 LYS C CB    1 
ATOM   4383  C  CG    . LYS C 1 243 ? 12.299  -23.191 -0.491  1.00 35.36 ?  243 LYS C CG    1 
ATOM   4384  C  CD    . LYS C 1 243 ? 10.997  -23.982 -0.544  1.00 34.87 ?  243 LYS C CD    1 
ATOM   4385  C  CE    . LYS C 1 243 ? 10.571  -24.330 -1.934  1.00 34.71 ?  243 LYS C CE    1 
ATOM   4386  N  NZ    . LYS C 1 243 ? 9.354   -25.145 -1.921  1.00 37.98 1  243 LYS C NZ    1 
ATOM   4387  N  N     . LYS C 1 244 ? 14.150  -20.260 -3.305  1.00 34.17 ?  244 LYS C N     1 
ATOM   4388  C  CA    . LYS C 1 244 ? 14.265  -19.473 -4.521  1.00 32.14 ?  244 LYS C CA    1 
ATOM   4389  C  C     . LYS C 1 244 ? 13.219  -19.953 -5.523  1.00 27.23 ?  244 LYS C C     1 
ATOM   4390  O  O     . LYS C 1 244 ? 12.732  -21.076 -5.422  1.00 21.90 ?  244 LYS C O     1 
ATOM   4391  C  CB    . LYS C 1 244 ? 15.676  -19.656 -5.090  1.00 37.62 ?  244 LYS C CB    1 
ATOM   4392  C  CG    . LYS C 1 244 ? 16.800  -19.430 -4.087  1.00 42.96 ?  244 LYS C CG    1 
ATOM   4393  C  CD    . LYS C 1 244 ? 18.029  -20.292 -4.351  1.00 48.52 ?  244 LYS C CD    1 
ATOM   4394  C  CE    . LYS C 1 244 ? 18.936  -20.379 -3.165  1.00 49.01 ?  244 LYS C CE    1 
ATOM   4395  N  NZ    . LYS C 1 244 ? 19.944  -21.429 -3.337  1.00 50.96 1  244 LYS C NZ    1 
ATOM   4396  N  N     . LEU C 1 245 ? 12.886  -19.096 -6.494  1.00 26.66 ?  245 LEU C N     1 
ATOM   4397  C  CA    . LEU C 1 245 ? 11.868  -19.425 -7.479  1.00 28.82 ?  245 LEU C CA    1 
ATOM   4398  C  C     . LEU C 1 245 ? 12.347  -20.597 -8.333  1.00 28.41 ?  245 LEU C C     1 
ATOM   4399  O  O     . LEU C 1 245 ? 13.452  -20.568 -8.870  1.00 27.05 ?  245 LEU C O     1 
ATOM   4400  C  CB    . LEU C 1 245 ? 11.528  -18.209 -8.340  1.00 29.94 ?  245 LEU C CB    1 
ATOM   4401  C  CG    . LEU C 1 245 ? 10.873  -17.027 -7.617  1.00 30.00 ?  245 LEU C CG    1 
ATOM   4402  C  CD1   . LEU C 1 245 ? 9.823   -17.513 -6.630  1.00 31.77 ?  245 LEU C CD1   1 
ATOM   4403  C  CD2   . LEU C 1 245 ? 11.901  -16.152 -6.922  1.00 32.62 ?  245 LEU C CD2   1 
ATOM   4404  N  N     . GLU C 1 246 ? 11.497  -21.626 -8.444  1.00 30.08 ?  246 GLU C N     1 
ATOM   4405  C  CA    . GLU C 1 246 ? 11.767  -22.780 -9.289  1.00 30.23 ?  246 GLU C CA    1 
ATOM   4406  C  C     . GLU C 1 246 ? 10.756  -22.790 -10.436 1.00 30.11 ?  246 GLU C C     1 
ATOM   4407  O  O     . GLU C 1 246 ? 9.649   -22.277 -10.292 1.00 29.26 ?  246 GLU C O     1 
ATOM   4408  C  CB    . GLU C 1 246 ? 11.729  -24.067 -8.461  1.00 31.64 ?  246 GLU C CB    1 
ATOM   4409  C  CG    . GLU C 1 246 ? 12.641  -24.033 -7.237  1.00 33.49 ?  246 GLU C CG    1 
ATOM   4410  C  CD    . GLU C 1 246 ? 12.751  -25.346 -6.481  1.00 37.91 ?  246 GLU C CD    1 
ATOM   4411  O  OE1   . GLU C 1 246 ? 13.289  -26.318 -7.054  1.00 35.15 ?  246 GLU C OE1   1 
ATOM   4412  O  OE2   . GLU C 1 246 ? 12.298  -25.397 -5.318  1.00 45.93 -1 246 GLU C OE2   1 
ATOM   4413  N  N     . TYR C 1 247 ? 11.148  -23.376 -11.575 1.00 32.37 ?  247 TYR C N     1 
ATOM   4414  C  CA    . TYR C 1 247 ? 10.368  -23.285 -12.802 1.00 29.64 ?  247 TYR C CA    1 
ATOM   4415  C  C     . TYR C 1 247 ? 9.146   -24.196 -12.720 1.00 28.68 ?  247 TYR C C     1 
ATOM   4416  O  O     . TYR C 1 247 ? 9.199   -25.266 -12.116 1.00 21.50 ?  247 TYR C O     1 
ATOM   4417  C  CB    . TYR C 1 247 ? 11.207  -23.639 -14.034 1.00 28.52 ?  247 TYR C CB    1 
ATOM   4418  C  CG    . TYR C 1 247 ? 12.292  -22.630 -14.384 1.00 26.04 ?  247 TYR C CG    1 
ATOM   4419  C  CD1   . TYR C 1 247 ? 11.979  -21.429 -15.009 1.00 26.94 ?  247 TYR C CD1   1 
ATOM   4420  C  CD2   . TYR C 1 247 ? 13.631  -22.887 -14.111 1.00 27.96 ?  247 TYR C CD2   1 
ATOM   4421  C  CE1   . TYR C 1 247 ? 12.960  -20.507 -15.336 1.00 26.60 ?  247 TYR C CE1   1 
ATOM   4422  C  CE2   . TYR C 1 247 ? 14.622  -21.975 -14.435 1.00 27.34 ?  247 TYR C CE2   1 
ATOM   4423  C  CZ    . TYR C 1 247 ? 14.285  -20.781 -15.049 1.00 27.14 ?  247 TYR C CZ    1 
ATOM   4424  O  OH    . TYR C 1 247 ? 15.257  -19.877 -15.372 1.00 26.32 ?  247 TYR C OH    1 
ATOM   4425  N  N     . ASN C 1 248 ? 8.053   -23.755 -13.357 1.00 29.15 ?  248 ASN C N     1 
ATOM   4426  C  CA    . ASN C 1 248 ? 6.792   -24.479 -13.339 1.00 25.83 ?  248 ASN C CA    1 
ATOM   4427  C  C     . ASN C 1 248 ? 6.628   -25.219 -14.667 1.00 25.98 ?  248 ASN C C     1 
ATOM   4428  O  O     . ASN C 1 248 ? 5.817   -24.837 -15.508 1.00 20.29 ?  248 ASN C O     1 
ATOM   4429  C  CB    . ASN C 1 248 ? 5.634   -23.540 -13.013 1.00 26.02 ?  248 ASN C CB    1 
ATOM   4430  C  CG    . ASN C 1 248 ? 4.400   -24.290 -12.571 1.00 24.90 ?  248 ASN C CG    1 
ATOM   4431  O  OD1   . ASN C 1 248 ? 4.316   -25.509 -12.751 1.00 23.76 ?  248 ASN C OD1   1 
ATOM   4432  N  ND2   . ASN C 1 248 ? 3.437   -23.585 -11.994 1.00 21.68 ?  248 ASN C ND2   1 
ATOM   4433  N  N     . TYR C 1 249 ? 7.407   -26.296 -14.827 1.00 25.48 ?  249 TYR C N     1 
ATOM   4434  C  CA    . TYR C 1 249 ? 7.475   -27.040 -16.075 1.00 24.00 ?  249 TYR C CA    1 
ATOM   4435  C  C     . TYR C 1 249 ? 6.073   -27.435 -16.530 1.00 21.58 ?  249 TYR C C     1 
ATOM   4436  O  O     . TYR C 1 249 ? 5.798   -27.479 -17.727 1.00 22.68 ?  249 TYR C O     1 
ATOM   4437  C  CB    . TYR C 1 249 ? 8.378   -28.269 -15.923 1.00 22.91 ?  249 TYR C CB    1 
ATOM   4438  C  CG    . TYR C 1 249 ? 9.854   -27.924 -15.797 1.00 21.35 ?  249 TYR C CG    1 
ATOM   4439  C  CD1   . TYR C 1 249 ? 10.603  -27.573 -16.914 1.00 20.43 ?  249 TYR C CD1   1 
ATOM   4440  C  CD2   . TYR C 1 249 ? 10.497  -27.945 -14.566 1.00 20.78 ?  249 TYR C CD2   1 
ATOM   4441  C  CE1   . TYR C 1 249 ? 11.946  -27.252 -16.810 1.00 20.31 ?  249 TYR C CE1   1 
ATOM   4442  C  CE2   . TYR C 1 249 ? 11.840  -27.629 -14.449 1.00 19.61 ?  249 TYR C CE2   1 
ATOM   4443  C  CZ    . TYR C 1 249 ? 12.567  -27.282 -15.573 1.00 21.92 ?  249 TYR C CZ    1 
ATOM   4444  O  OH    . TYR C 1 249 ? 13.891  -26.970 -15.456 1.00 23.72 ?  249 TYR C OH    1 
ATOM   4445  N  N     . ALA C 1 250 ? 5.198   -27.729 -15.565 1.00 19.53 ?  250 ALA C N     1 
ATOM   4446  C  CA    . ALA C 1 250 ? 3.825   -28.101 -15.865 1.00 21.05 ?  250 ALA C CA    1 
ATOM   4447  C  C     . ALA C 1 250 ? 3.216   -27.114 -16.857 1.00 21.25 ?  250 ALA C C     1 
ATOM   4448  O  O     . ALA C 1 250 ? 2.768   -27.499 -17.934 1.00 24.06 ?  250 ALA C O     1 
ATOM   4449  C  CB    . ALA C 1 250 ? 3.014   -28.153 -14.589 1.00 19.38 ?  250 ALA C CB    1 
ATOM   4450  N  N     . ILE C 1 251 ? 3.205   -25.835 -16.468 1.00 24.12 ?  251 ILE C N     1 
ATOM   4451  C  CA    . ILE C 1 251 ? 2.457   -24.816 -17.184 1.00 24.42 ?  251 ILE C CA    1 
ATOM   4452  C  C     . ILE C 1 251 ? 3.257   -24.387 -18.411 1.00 24.47 ?  251 ILE C C     1 
ATOM   4453  O  O     . ILE C 1 251 ? 2.696   -24.200 -19.487 1.00 26.90 ?  251 ILE C O     1 
ATOM   4454  C  CB    . ILE C 1 251 ? 2.127   -23.636 -16.250 1.00 24.53 ?  251 ILE C CB    1 
ATOM   4455  C  CG1   . ILE C 1 251 ? 1.466   -24.113 -14.950 1.00 29.03 ?  251 ILE C CG1   1 
ATOM   4456  C  CG2   . ILE C 1 251 ? 1.275   -22.587 -16.966 1.00 25.66 ?  251 ILE C CG2   1 
ATOM   4457  C  CD1   . ILE C 1 251 ? 0.145   -24.837 -15.146 1.00 30.21 ?  251 ILE C CD1   1 
ATOM   4458  N  N     . LEU C 1 252 ? 4.575   -24.243 -18.234 1.00 25.67 ?  252 LEU C N     1 
ATOM   4459  C  CA    . LEU C 1 252 ? 5.472   -23.940 -19.337 1.00 29.19 ?  252 LEU C CA    1 
ATOM   4460  C  C     . LEU C 1 252 ? 5.189   -24.895 -20.494 1.00 30.25 ?  252 LEU C C     1 
ATOM   4461  O  O     . LEU C 1 252 ? 5.192   -24.487 -21.654 1.00 28.90 ?  252 LEU C O     1 
ATOM   4462  C  CB    . LEU C 1 252 ? 6.926   -24.034 -18.878 1.00 30.40 ?  252 LEU C CB    1 
ATOM   4463  C  CG    . LEU C 1 252 ? 7.503   -22.791 -18.192 1.00 34.81 ?  252 LEU C CG    1 
ATOM   4464  C  CD1   . LEU C 1 252 ? 6.642   -22.323 -17.032 1.00 40.86 ?  252 LEU C CD1   1 
ATOM   4465  C  CD2   . LEU C 1 252 ? 8.921   -23.067 -17.722 1.00 35.83 ?  252 LEU C CD2   1 
ATOM   4466  N  N     . ALA C 1 253 ? 4.949   -26.168 -20.163 1.00 29.70 ?  253 ALA C N     1 
ATOM   4467  C  CA    . ALA C 1 253 ? 4.632   -27.169 -21.167 1.00 32.90 ?  253 ALA C CA    1 
ATOM   4468  C  C     . ALA C 1 253 ? 3.327   -26.796 -21.865 1.00 33.95 ?  253 ALA C C     1 
ATOM   4469  O  O     . ALA C 1 253 ? 3.261   -26.792 -23.092 1.00 33.69 ?  253 ALA C O     1 
ATOM   4470  C  CB    . ALA C 1 253 ? 4.561   -28.543 -20.538 1.00 33.33 ?  253 ALA C CB    1 
ATOM   4471  N  N     . LYS C 1 254 ? 2.295   -26.471 -21.077 1.00 33.59 ?  254 LYS C N     1 
ATOM   4472  C  CA    . LYS C 1 254 ? 1.010   -26.089 -21.642 1.00 39.40 ?  254 LYS C CA    1 
ATOM   4473  C  C     . LYS C 1 254 ? 1.201   -24.874 -22.550 1.00 38.23 ?  254 LYS C C     1 
ATOM   4474  O  O     . LYS C 1 254 ? 0.599   -24.801 -23.619 1.00 37.03 ?  254 LYS C O     1 
ATOM   4475  C  CB    . LYS C 1 254 ? -0.057  -25.820 -20.572 1.00 40.89 ?  254 LYS C CB    1 
ATOM   4476  C  CG    . LYS C 1 254 ? -0.489  -27.033 -19.751 1.00 42.53 ?  254 LYS C CG    1 
ATOM   4477  C  CD    . LYS C 1 254 ? -1.838  -26.868 -19.058 1.00 45.00 ?  254 LYS C CD    1 
ATOM   4478  C  CE    . LYS C 1 254 ? -2.105  -27.914 -18.020 1.00 47.58 ?  254 LYS C CE    1 
ATOM   4479  N  NZ    . LYS C 1 254 ? -2.030  -29.275 -18.558 1.00 46.85 1  254 LYS C NZ    1 
ATOM   4480  N  N     . LEU C 1 255 ? 2.047   -23.929 -22.118 1.00 36.47 ?  255 LEU C N     1 
ATOM   4481  C  CA    . LEU C 1 255 ? 2.322   -22.724 -22.889 1.00 33.96 ?  255 LEU C CA    1 
ATOM   4482  C  C     . LEU C 1 255 ? 3.266   -23.058 -24.044 1.00 33.71 ?  255 LEU C C     1 
ATOM   4483  O  O     . LEU C 1 255 ? 3.613   -22.185 -24.837 1.00 26.31 ?  255 LEU C O     1 
ATOM   4484  C  CB    . LEU C 1 255 ? 2.914   -21.629 -22.001 1.00 34.37 ?  255 LEU C CB    1 
ATOM   4485  C  CG    . LEU C 1 255 ? 1.978   -20.986 -20.971 1.00 34.43 ?  255 LEU C CG    1 
ATOM   4486  C  CD1   . LEU C 1 255 ? 2.778   -20.212 -19.939 1.00 35.69 ?  255 LEU C CD1   1 
ATOM   4487  C  CD2   . LEU C 1 255 ? 0.965   -20.065 -21.623 1.00 37.02 ?  255 LEU C CD2   1 
ATOM   4488  N  N     . GLY C 1 256 ? 3.691   -24.324 -24.116 1.00 35.92 ?  256 GLY C N     1 
ATOM   4489  C  CA    . GLY C 1 256 ? 4.535   -24.798 -25.200 1.00 30.53 ?  256 GLY C CA    1 
ATOM   4490  C  C     . GLY C 1 256 ? 5.911   -24.135 -25.189 1.00 30.61 ?  256 GLY C C     1 
ATOM   4491  O  O     . GLY C 1 256 ? 6.495   -23.900 -26.245 1.00 29.17 ?  256 GLY C O     1 
ATOM   4492  N  N     . ILE C 1 257 ? 6.431   -23.846 -23.990 1.00 31.01 ?  257 ILE C N     1 
ATOM   4493  C  CA    . ILE C 1 257 ? 7.715   -23.175 -23.864 1.00 29.95 ?  257 ILE C CA    1 
ATOM   4494  C  C     . ILE C 1 257 ? 8.556   -23.853 -22.784 1.00 29.59 ?  257 ILE C C     1 
ATOM   4495  O  O     . ILE C 1 257 ? 8.105   -24.788 -22.127 1.00 28.66 ?  257 ILE C O     1 
ATOM   4496  C  CB    . ILE C 1 257 ? 7.522   -21.678 -23.558 1.00 31.83 ?  257 ILE C CB    1 
ATOM   4497  C  CG1   . ILE C 1 257 ? 6.821   -21.466 -22.217 1.00 31.65 ?  257 ILE C CG1   1 
ATOM   4498  C  CG2   . ILE C 1 257 ? 6.786   -20.977 -24.699 1.00 35.73 ?  257 ILE C CG2   1 
ATOM   4499  C  CD1   . ILE C 1 257 ? 6.837   -20.028 -21.732 1.00 32.45 ?  257 ILE C CD1   1 
ATOM   4500  N  N     . GLY C 1 258 ? 9.790   -23.358 -22.623 1.00 31.46 ?  258 GLY C N     1 
ATOM   4501  C  CA    . GLY C 1 258 ? 10.682  -23.788 -21.557 1.00 31.46 ?  258 GLY C CA    1 
ATOM   4502  C  C     . GLY C 1 258 ? 11.450  -22.607 -20.965 1.00 32.41 ?  258 GLY C C     1 
ATOM   4503  O  O     . GLY C 1 258 ? 11.353  -21.486 -21.461 1.00 27.60 ?  258 GLY C O     1 
ATOM   4504  N  N     . PRO C 1 259 ? 12.236  -22.826 -19.885 1.00 33.39 ?  259 PRO C N     1 
ATOM   4505  C  CA    . PRO C 1 259 ? 12.959  -21.743 -19.210 1.00 38.08 ?  259 PRO C CA    1 
ATOM   4506  C  C     . PRO C 1 259 ? 13.787  -20.865 -20.144 1.00 44.00 ?  259 PRO C C     1 
ATOM   4507  O  O     . PRO C 1 259 ? 13.823  -19.645 -19.993 1.00 42.48 ?  259 PRO C O     1 
ATOM   4508  C  CB    . PRO C 1 259 ? 13.851  -22.512 -18.216 1.00 35.26 ?  259 PRO C CB    1 
ATOM   4509  C  CG    . PRO C 1 259 ? 13.067  -23.766 -17.913 1.00 33.83 ?  259 PRO C CG    1 
ATOM   4510  C  CD    . PRO C 1 259 ? 12.448  -24.136 -19.248 1.00 34.66 ?  259 PRO C CD    1 
ATOM   4511  N  N     . GLU C 1 260 ? 14.457  -21.510 -21.103 1.00 48.64 ?  260 GLU C N     1 
ATOM   4512  C  CA    . GLU C 1 260 ? 15.343  -20.825 -22.028 1.00 54.44 ?  260 GLU C CA    1 
ATOM   4513  C  C     . GLU C 1 260 ? 14.548  -19.831 -22.872 1.00 47.72 ?  260 GLU C C     1 
ATOM   4514  O  O     . GLU C 1 260 ? 15.123  -18.912 -23.451 1.00 42.24 ?  260 GLU C O     1 
ATOM   4515  C  CB    . GLU C 1 260 ? 16.085  -21.834 -22.908 1.00 60.03 ?  260 GLU C CB    1 
ATOM   4516  C  CG    . GLU C 1 260 ? 15.173  -22.696 -23.778 1.00 66.67 ?  260 GLU C CG    1 
ATOM   4517  C  CD    . GLU C 1 260 ? 14.605  -23.926 -23.091 1.00 73.82 ?  260 GLU C CD    1 
ATOM   4518  O  OE1   . GLU C 1 260 ? 13.949  -23.770 -22.040 1.00 83.73 ?  260 GLU C OE1   1 
ATOM   4519  O  OE2   . GLU C 1 260 ? 14.815  -25.041 -23.613 1.00 74.86 -1 260 GLU C OE2   1 
ATOM   4520  N  N     . ASP C 1 261 ? 13.224  -20.015 -22.927 1.00 45.28 ?  261 ASP C N     1 
ATOM   4521  C  CA    . ASP C 1 261 ? 12.377  -19.233 -23.815 1.00 45.85 ?  261 ASP C CA    1 
ATOM   4522  C  C     . ASP C 1 261 ? 11.921  -17.942 -23.137 1.00 43.19 ?  261 ASP C C     1 
ATOM   4523  O  O     . ASP C 1 261 ? 11.448  -17.029 -23.811 1.00 44.79 ?  261 ASP C O     1 
ATOM   4524  C  CB    . ASP C 1 261 ? 11.198  -20.049 -24.322 1.00 43.71 ?  261 ASP C CB    1 
ATOM   4525  C  CG    . ASP C 1 261 ? 11.559  -21.193 -25.259 1.00 39.97 ?  261 ASP C CG    1 
ATOM   4526  O  OD1   . ASP C 1 261 ? 12.273  -20.933 -26.251 1.00 38.05 ?  261 ASP C OD1   1 
ATOM   4527  O  OD2   . ASP C 1 261 ? 11.121  -22.331 -24.992 1.00 40.86 -1 261 ASP C OD2   1 
ATOM   4528  N  N     . LEU C 1 262 ? 12.060  -17.869 -21.808 1.00 40.23 ?  262 LEU C N     1 
ATOM   4529  C  CA    . LEU C 1 262 ? 11.664  -16.685 -21.060 1.00 36.79 ?  262 LEU C CA    1 
ATOM   4530  C  C     . LEU C 1 262 ? 12.538  -15.506 -21.477 1.00 36.29 ?  262 LEU C C     1 
ATOM   4531  O  O     . LEU C 1 262 ? 13.756  -15.635 -21.575 1.00 37.65 ?  262 LEU C O     1 
ATOM   4532  C  CB    . LEU C 1 262 ? 11.776  -16.944 -19.558 1.00 38.76 ?  262 LEU C CB    1 
ATOM   4533  C  CG    . LEU C 1 262 ? 10.835  -18.005 -18.979 1.00 38.22 ?  262 LEU C CG    1 
ATOM   4534  C  CD1   . LEU C 1 262 ? 11.223  -18.335 -17.549 1.00 36.95 ?  262 LEU C CD1   1 
ATOM   4535  C  CD2   . LEU C 1 262 ? 9.389   -17.546 -19.046 1.00 39.92 ?  262 LEU C CD2   1 
ATOM   4536  N  N     . GLY C 1 263 ? 11.898  -14.355 -21.716 1.00 34.14 ?  263 GLY C N     1 
ATOM   4537  C  CA    . GLY C 1 263 ? 12.607  -13.131 -22.047 1.00 29.95 ?  263 GLY C CA    1 
ATOM   4538  C  C     . GLY C 1 263 ? 13.303  -12.555 -20.827 1.00 28.38 ?  263 GLY C C     1 
ATOM   4539  O  O     . GLY C 1 263 ? 14.260  -11.778 -21.032 1.00 25.94 ?  263 GLY C O     1 
ATOM   4540  O  OXT   . GLY C 1 263 ? 12.869  -12.900 -19.707 1.00 23.61 -1 263 GLY C OXT   1 
ATOM   4541  N  N     . LEU D 2 11  ? 9.839   22.375  19.557  1.00 27.37 ?  4   LEU D N     1 
ATOM   4542  C  CA    . LEU D 2 11  ? 10.286  21.006  19.186  1.00 29.31 ?  4   LEU D CA    1 
ATOM   4543  C  C     . LEU D 2 11  ? 9.244   20.366  18.272  1.00 26.04 ?  4   LEU D C     1 
ATOM   4544  O  O     . LEU D 2 11  ? 9.580   19.827  17.220  1.00 26.80 ?  4   LEU D O     1 
ATOM   4545  C  CB    . LEU D 2 11  ? 10.512  20.177  20.449  1.00 31.24 ?  4   LEU D CB    1 
ATOM   4546  C  CG    . LEU D 2 11  ? 11.276  18.862  20.268  1.00 35.27 ?  4   LEU D CG    1 
ATOM   4547  C  CD1   . LEU D 2 11  ? 12.484  19.016  19.358  1.00 33.92 ?  4   LEU D CD1   1 
ATOM   4548  C  CD2   . LEU D 2 11  ? 11.703  18.340  21.627  1.00 35.86 ?  4   LEU D CD2   1 
ATOM   4549  N  N     . SER D 2 12  ? 7.976   20.433  18.693  1.00 25.39 ?  5   SER D N     1 
ATOM   4550  C  CA    . SER D 2 12  ? 6.878   19.860  17.933  1.00 24.71 ?  5   SER D CA    1 
ATOM   4551  C  C     . SER D 2 12  ? 6.690   20.640  16.633  1.00 23.65 ?  5   SER D C     1 
ATOM   4552  O  O     . SER D 2 12  ? 6.134   20.120  15.669  1.00 27.01 ?  5   SER D O     1 
ATOM   4553  C  CB    . SER D 2 12  ? 5.612   19.822  18.763  1.00 22.20 ?  5   SER D CB    1 
ATOM   4554  O  OG    . SER D 2 12  ? 4.494   19.386  18.002  1.00 21.95 ?  5   SER D OG    1 
ATOM   4555  N  N     . ASP D 2 13  ? 7.187   21.884  16.615  1.00 24.17 ?  6   ASP D N     1 
ATOM   4556  C  CA    . ASP D 2 13  ? 7.066   22.763  15.463  1.00 28.24 ?  6   ASP D CA    1 
ATOM   4557  C  C     . ASP D 2 13  ? 8.132   22.430  14.423  1.00 26.60 ?  6   ASP D C     1 
ATOM   4558  O  O     . ASP D 2 13  ? 7.888   22.533  13.223  1.00 26.21 ?  6   ASP D O     1 
ATOM   4559  C  CB    . ASP D 2 13  ? 7.187   24.227  15.857  1.00 28.31 ?  6   ASP D CB    1 
ATOM   4560  C  CG    . ASP D 2 13  ? 5.983   24.817  16.576  1.00 34.70 ?  6   ASP D CG    1 
ATOM   4561  O  OD1   . ASP D 2 13  ? 5.016   24.063  16.815  1.00 39.16 ?  6   ASP D OD1   1 
ATOM   4562  O  OD2   . ASP D 2 13  ? 6.019   26.027  16.884  1.00 32.31 -1 6   ASP D OD2   1 
ATOM   4563  N  N     . PHE D 2 14  ? 9.323   22.055  14.897  1.00 25.64 ?  7   PHE D N     1 
ATOM   4564  C  CA    . PHE D 2 14  ? 10.432  21.768  14.008  1.00 25.57 ?  7   PHE D CA    1 
ATOM   4565  C  C     . PHE D 2 14  ? 10.137  20.487  13.229  1.00 23.97 ?  7   PHE D C     1 
ATOM   4566  O  O     . PHE D 2 14  ? 10.419  20.405  12.035  1.00 25.10 ?  7   PHE D O     1 
ATOM   4567  C  CB    . PHE D 2 14  ? 11.722  21.698  14.830  1.00 26.46 ?  7   PHE D CB    1 
ATOM   4568  C  CG    . PHE D 2 14  ? 12.898  21.136  14.046  1.00 28.88 ?  7   PHE D CG    1 
ATOM   4569  C  CD1   . PHE D 2 14  ? 13.559  21.913  13.102  1.00 28.34 ?  7   PHE D CD1   1 
ATOM   4570  C  CD2   . PHE D 2 14  ? 13.325  19.829  14.243  1.00 27.76 ?  7   PHE D CD2   1 
ATOM   4571  C  CE1   . PHE D 2 14  ? 14.622  21.396  12.381  1.00 27.57 ?  7   PHE D CE1   1 
ATOM   4572  C  CE2   . PHE D 2 14  ? 14.392  19.318  13.521  1.00 29.18 ?  7   PHE D CE2   1 
ATOM   4573  C  CZ    . PHE D 2 14  ? 15.036  20.101  12.592  1.00 29.55 ?  7   PHE D CZ    1 
ATOM   4574  N  N     . PHE D 2 15  ? 9.552   19.498  13.914  1.00 22.32 ?  8   PHE D N     1 
ATOM   4575  C  CA    . PHE D 2 15  ? 9.318   18.188  13.326  1.00 22.67 ?  8   PHE D CA    1 
ATOM   4576  C  C     . PHE D 2 15  ? 8.254   18.283  12.233  1.00 23.98 ?  8   PHE D C     1 
ATOM   4577  O  O     . PHE D 2 15  ? 8.356   17.604  11.214  1.00 20.27 ?  8   PHE D O     1 
ATOM   4578  C  CB    . PHE D 2 15  ? 8.914   17.161  14.387  1.00 21.14 ?  8   PHE D CB    1 
ATOM   4579  C  CG    . PHE D 2 15  ? 10.010  16.754  15.364  1.00 24.61 ?  8   PHE D CG    1 
ATOM   4580  C  CD1   . PHE D 2 15  ? 11.352  16.992  15.085  1.00 26.67 ?  8   PHE D CD1   1 
ATOM   4581  C  CD2   . PHE D 2 15  ? 9.693   16.103  16.551  1.00 26.21 ?  8   PHE D CD2   1 
ATOM   4582  C  CE1   . PHE D 2 15  ? 12.340  16.609  15.979  1.00 28.99 ?  8   PHE D CE1   1 
ATOM   4583  C  CE2   . PHE D 2 15  ? 10.685  15.722  17.440  1.00 28.10 ?  8   PHE D CE2   1 
ATOM   4584  C  CZ    . PHE D 2 15  ? 12.005  15.976  17.153  1.00 27.93 ?  8   PHE D CZ    1 
ATOM   4585  N  N     . THR D 2 16  ? 7.227   19.114  12.451  1.00 25.02 ?  9   THR D N     1 
ATOM   4586  C  CA    . THR D 2 16  ? 6.151   19.254  11.481  1.00 22.45 ?  9   THR D CA    1 
ATOM   4587  C  C     . THR D 2 16  ? 6.720   19.841  10.191  1.00 23.45 ?  9   THR D C     1 
ATOM   4588  O  O     . THR D 2 16  ? 6.478   19.319  9.104   1.00 23.76 ?  9   THR D O     1 
ATOM   4589  C  CB    . THR D 2 16  ? 5.024   20.121  12.041  1.00 23.13 ?  9   THR D CB    1 
ATOM   4590  O  OG1   . THR D 2 16  ? 4.462   19.394  13.129  1.00 21.23 ?  9   THR D OG1   1 
ATOM   4591  C  CG2   . THR D 2 16  ? 3.950   20.406  11.006  1.00 19.40 ?  9   THR D CG2   1 
ATOM   4592  N  N     . GLN D 2 17  ? 7.473   20.937  10.327  1.00 22.03 ?  10  GLN D N     1 
ATOM   4593  C  CA    . GLN D 2 17  ? 8.147   21.547  9.193   1.00 21.46 ?  10  GLN D CA    1 
ATOM   4594  C  C     . GLN D 2 17  ? 8.962   20.480  8.464   1.00 22.70 ?  10  GLN D C     1 
ATOM   4595  O  O     . GLN D 2 17  ? 8.720   20.194  7.293   1.00 24.09 ?  10  GLN D O     1 
ATOM   4596  C  CB    . GLN D 2 17  ? 9.057   22.687  9.655   1.00 22.57 ?  10  GLN D CB    1 
ATOM   4597  C  CG    . GLN D 2 17  ? 8.325   23.882  10.259  1.00 24.16 ?  10  GLN D CG    1 
ATOM   4598  C  CD    . GLN D 2 17  ? 9.266   24.905  10.860  1.00 26.04 ?  10  GLN D CD    1 
ATOM   4599  O  OE1   . GLN D 2 17  ? 10.486  24.849  10.670  1.00 28.82 ?  10  GLN D OE1   1 
ATOM   4600  N  NE2   . GLN D 2 17  ? 8.706   25.856  11.594  1.00 26.48 ?  10  GLN D NE2   1 
ATOM   4601  N  N     . LEU D 2 18  ? 9.914   19.885  9.195   1.00 19.80 ?  11  LEU D N     1 
ATOM   4602  C  CA    . LEU D 2 18  ? 10.901  18.971  8.642   1.00 17.48 ?  11  LEU D CA    1 
ATOM   4603  C  C     . LEU D 2 18  ? 10.226  17.869  7.826   1.00 17.55 ?  11  LEU D C     1 
ATOM   4604  O  O     . LEU D 2 18  ? 10.708  17.507  6.755   1.00 18.26 ?  11  LEU D O     1 
ATOM   4605  C  CB    . LEU D 2 18  ? 11.722  18.400  9.800   1.00 17.91 ?  11  LEU D CB    1 
ATOM   4606  C  CG    . LEU D 2 18  ? 12.738  17.306  9.455   1.00 17.46 ?  11  LEU D CG    1 
ATOM   4607  C  CD1   . LEU D 2 18  ? 13.724  17.766  8.396   1.00 16.43 ?  11  LEU D CD1   1 
ATOM   4608  C  CD2   . LEU D 2 18  ? 13.480  16.854  10.705  1.00 19.22 ?  11  LEU D CD2   1 
ATOM   4609  N  N     . GLY D 2 19  ? 9.114   17.339  8.344   1.00 14.67 ?  12  GLY D N     1 
ATOM   4610  C  CA    . GLY D 2 19  ? 8.452   16.192  7.742   1.00 13.79 ?  12  GLY D CA    1 
ATOM   4611  C  C     . GLY D 2 19  ? 7.652   16.570  6.496   1.00 14.06 ?  12  GLY D C     1 
ATOM   4612  O  O     . GLY D 2 19  ? 7.317   15.705  5.689   1.00 13.65 ?  12  GLY D O     1 
ATOM   4613  N  N     . GLN D 2 20  ? 7.347   17.866  6.360   1.00 14.18 ?  13  GLN D N     1 
ATOM   4614  C  CA    . GLN D 2 20  ? 6.547   18.381  5.259   1.00 16.01 ?  13  GLN D CA    1 
ATOM   4615  C  C     . GLN D 2 20  ? 7.429   19.012  4.182   1.00 18.03 ?  13  GLN D C     1 
ATOM   4616  O  O     . GLN D 2 20  ? 7.015   19.117  3.029   1.00 15.23 ?  13  GLN D O     1 
ATOM   4617  C  CB    . GLN D 2 20  ? 5.605   19.497  5.716   1.00 20.45 ?  13  GLN D CB    1 
ATOM   4618  C  CG    . GLN D 2 20  ? 4.447   19.051  6.601   1.00 21.66 ?  13  GLN D CG    1 
ATOM   4619  C  CD    . GLN D 2 20  ? 3.511   20.189  6.945   1.00 24.55 ?  13  GLN D CD    1 
ATOM   4620  O  OE1   . GLN D 2 20  ? 3.831   21.072  7.749   1.00 26.85 ?  13  GLN D OE1   1 
ATOM   4621  N  NE2   . GLN D 2 20  ? 2.338   20.184  6.328   1.00 31.54 ?  13  GLN D NE2   1 
ATOM   4622  N  N     . ASP D 2 21  ? 8.629   19.460  4.570   1.00 20.90 ?  14  ASP D N     1 
ATOM   4623  C  CA    . ASP D 2 21  ? 9.425   20.352  3.740   1.00 21.98 ?  14  ASP D CA    1 
ATOM   4624  C  C     . ASP D 2 21  ? 10.697  19.641  3.286   1.00 23.55 ?  14  ASP D C     1 
ATOM   4625  O  O     . ASP D 2 21  ? 11.598  19.405  4.089   1.00 24.64 ?  14  ASP D O     1 
ATOM   4626  C  CB    . ASP D 2 21  ? 9.739   21.640  4.488   1.00 24.46 ?  14  ASP D CB    1 
ATOM   4627  C  CG    . ASP D 2 21  ? 10.514  22.689  3.703   1.00 26.84 ?  14  ASP D CG    1 
ATOM   4628  O  OD1   . ASP D 2 21  ? 10.784  22.448  2.508   1.00 32.66 ?  14  ASP D OD1   1 
ATOM   4629  O  OD2   . ASP D 2 21  ? 10.842  23.738  4.296   1.00 28.70 -1 14  ASP D OD2   1 
ATOM   4630  N  N     . ALA D 2 22  ? 10.775  19.332  1.986   1.00 23.90 ?  15  ALA D N     1 
ATOM   4631  C  CA    . ALA D 2 22  ? 11.842  18.492  1.466   1.00 22.65 ?  15  ALA D CA    1 
ATOM   4632  C  C     . ALA D 2 22  ? 13.131  19.295  1.313   1.00 25.00 ?  15  ALA D C     1 
ATOM   4633  O  O     . ALA D 2 22  ? 14.196  18.720  1.101   1.00 21.29 ?  15  ALA D O     1 
ATOM   4634  C  CB    . ALA D 2 22  ? 11.431  17.864  0.152   1.00 21.45 ?  15  ALA D CB    1 
ATOM   4635  N  N     . GLN D 2 23  ? 13.028  20.624  1.415   1.00 25.60 ?  16  GLN D N     1 
ATOM   4636  C  CA    . GLN D 2 23  ? 14.214  21.461  1.380   1.00 28.62 ?  16  GLN D CA    1 
ATOM   4637  C  C     . GLN D 2 23  ? 14.883  21.393  2.750   1.00 26.80 ?  16  GLN D C     1 
ATOM   4638  O  O     . GLN D 2 23  ? 16.092  21.192  2.852   1.00 32.05 ?  16  GLN D O     1 
ATOM   4639  C  CB    . GLN D 2 23  ? 13.874  22.897  0.986   1.00 34.03 ?  16  GLN D CB    1 
ATOM   4640  C  CG    . GLN D 2 23  ? 15.086  23.701  0.530   1.00 39.50 ?  16  GLN D CG    1 
ATOM   4641  C  CD    . GLN D 2 23  ? 15.674  23.186  -0.765  1.00 42.32 ?  16  GLN D CD    1 
ATOM   4642  O  OE1   . GLN D 2 23  ? 15.962  21.994  -0.916  1.00 43.47 ?  16  GLN D OE1   1 
ATOM   4643  N  NE2   . GLN D 2 23  ? 15.843  24.085  -1.725  1.00 46.43 ?  16  GLN D NE2   1 
ATOM   4644  N  N     . LEU D 2 24  ? 14.066  21.549  3.796   1.00 24.70 ?  17  LEU D N     1 
ATOM   4645  C  CA    . LEU D 2 24  ? 14.523  21.456  5.171   1.00 21.89 ?  17  LEU D CA    1 
ATOM   4646  C  C     . LEU D 2 24  ? 15.026  20.040  5.451   1.00 20.96 ?  17  LEU D C     1 
ATOM   4647  O  O     . LEU D 2 24  ? 16.056  19.869  6.100   1.00 19.60 ?  17  LEU D O     1 
ATOM   4648  C  CB    . LEU D 2 24  ? 13.380  21.863  6.102   1.00 22.37 ?  17  LEU D CB    1 
ATOM   4649  C  CG    . LEU D 2 24  ? 13.693  21.884  7.602   1.00 23.70 ?  17  LEU D CG    1 
ATOM   4650  C  CD1   . LEU D 2 24  ? 14.929  22.708  7.927   1.00 24.09 ?  17  LEU D CD1   1 
ATOM   4651  C  CD2   . LEU D 2 24  ? 12.496  22.411  8.373   1.00 23.38 ?  17  LEU D CD2   1 
ATOM   4652  N  N     . MET D 2 25  ? 14.299  19.029  4.955   1.00 19.92 ?  18  MET D N     1 
ATOM   4653  C  CA    . MET D 2 25  ? 14.693  17.639  5.136   1.00 21.80 ?  18  MET D CA    1 
ATOM   4654  C  C     . MET D 2 25  ? 16.120  17.428  4.635   1.00 19.16 ?  18  MET D C     1 
ATOM   4655  O  O     . MET D 2 25  ? 16.965  16.903  5.356   1.00 16.77 ?  18  MET D O     1 
ATOM   4656  C  CB    . MET D 2 25  ? 13.780  16.675  4.369   1.00 22.68 ?  18  MET D CB    1 
ATOM   4657  C  CG    . MET D 2 25  ? 14.174  15.215  4.525   1.00 24.32 ?  18  MET D CG    1 
ATOM   4658  S  SD    . MET D 2 25  ? 14.095  14.639  6.233   1.00 28.21 ?  18  MET D SD    1 
ATOM   4659  C  CE    . MET D 2 25  ? 12.316  14.433  6.398   1.00 29.31 ?  18  MET D CE    1 
ATOM   4660  N  N     . GLU D 2 26  ? 16.366  17.827  3.384   1.00 18.99 ?  19  GLU D N     1 
ATOM   4661  C  CA    . GLU D 2 26  ? 17.652  17.610  2.742   1.00 19.00 ?  19  GLU D CA    1 
ATOM   4662  C  C     . GLU D 2 26  ? 18.741  18.396  3.468   1.00 20.77 ?  19  GLU D C     1 
ATOM   4663  O  O     . GLU D 2 26  ? 19.865  17.916  3.599   1.00 20.84 ?  19  GLU D O     1 
ATOM   4664  C  CB    . GLU D 2 26  ? 17.550  17.960  1.257   1.00 17.96 ?  19  GLU D CB    1 
ATOM   4665  C  CG    . GLU D 2 26  ? 16.753  16.931  0.462   1.00 18.93 ?  19  GLU D CG    1 
ATOM   4666  C  CD    . GLU D 2 26  ? 17.295  15.519  0.588   1.00 18.81 ?  19  GLU D CD    1 
ATOM   4667  O  OE1   . GLU D 2 26  ? 18.478  15.314  0.237   1.00 19.71 ?  19  GLU D OE1   1 
ATOM   4668  O  OE2   . GLU D 2 26  ? 16.542  14.630  1.042   1.00 16.46 -1 19  GLU D OE2   1 
ATOM   4669  N  N     . ASP D 2 27  ? 18.401  19.602  3.937   1.00 23.73 ?  20  ASP D N     1 
ATOM   4670  C  CA    . ASP D 2 27  ? 19.331  20.414  4.707   1.00 23.00 ?  20  ASP D CA    1 
ATOM   4671  C  C     . ASP D 2 27  ? 19.647  19.708  6.024   1.00 20.82 ?  20  ASP D C     1 
ATOM   4672  O  O     . ASP D 2 27  ? 20.785  19.736  6.486   1.00 17.11 ?  20  ASP D O     1 
ATOM   4673  C  CB    . ASP D 2 27  ? 18.791  21.817  4.946   1.00 27.75 ?  20  ASP D CB    1 
ATOM   4674  C  CG    . ASP D 2 27  ? 18.698  22.714  3.719   1.00 33.20 ?  20  ASP D CG    1 
ATOM   4675  O  OD1   . ASP D 2 27  ? 19.185  22.298  2.646   1.00 29.70 ?  20  ASP D OD1   1 
ATOM   4676  O  OD2   . ASP D 2 27  ? 18.135  23.822  3.846   1.00 40.60 -1 20  ASP D OD2   1 
ATOM   4677  N  N     . TYR D 2 28  ? 18.626  19.076  6.617   1.00 20.06 ?  21  TYR D N     1 
ATOM   4678  C  CA    . TYR D 2 28  ? 18.775  18.392  7.892   1.00 17.65 ?  21  TYR D CA    1 
ATOM   4679  C  C     . TYR D 2 28  ? 19.739  17.219  7.729   1.00 19.78 ?  21  TYR D C     1 
ATOM   4680  O  O     . TYR D 2 28  ? 20.629  17.022  8.554   1.00 16.01 ?  21  TYR D O     1 
ATOM   4681  C  CB    . TYR D 2 28  ? 17.413  17.940  8.434   1.00 16.13 ?  21  TYR D CB    1 
ATOM   4682  C  CG    . TYR D 2 28  ? 17.501  17.019  9.644   1.00 15.57 ?  21  TYR D CG    1 
ATOM   4683  C  CD1   . TYR D 2 28  ? 17.735  17.525  10.918  1.00 15.80 ?  21  TYR D CD1   1 
ATOM   4684  C  CD2   . TYR D 2 28  ? 17.359  15.643  9.512   1.00 15.66 ?  21  TYR D CD2   1 
ATOM   4685  C  CE1   . TYR D 2 28  ? 17.825  16.691  12.021  1.00 15.16 ?  21  TYR D CE1   1 
ATOM   4686  C  CE2   . TYR D 2 28  ? 17.448  14.798  10.607  1.00 14.72 ?  21  TYR D CE2   1 
ATOM   4687  C  CZ    . TYR D 2 28  ? 17.680  15.324  11.865  1.00 14.78 ?  21  TYR D CZ    1 
ATOM   4688  O  OH    . TYR D 2 28  ? 17.765  14.500  12.950  1.00 13.68 ?  21  TYR D OH    1 
ATOM   4689  N  N     . LYS D 2 29  ? 19.556  16.449  6.651   1.00 20.88 ?  22  LYS D N     1 
ATOM   4690  C  CA    . LYS D 2 29  ? 20.351  15.255  6.412   1.00 21.85 ?  22  LYS D CA    1 
ATOM   4691  C  C     . LYS D 2 29  ? 21.795  15.631  6.082   1.00 23.11 ?  22  LYS D C     1 
ATOM   4692  O  O     . LYS D 2 29  ? 22.702  14.825  6.277   1.00 25.93 ?  22  LYS D O     1 
ATOM   4693  C  CB    . LYS D 2 29  ? 19.623  14.394  5.372   1.00 20.01 ?  22  LYS D CB    1 
ATOM   4694  C  CG    . LYS D 2 29  ? 18.755  13.319  6.021   1.00 18.78 ?  22  LYS D CG    1 
ATOM   4695  C  CD    . LYS D 2 29  ? 17.418  13.016  5.356   1.00 17.39 ?  22  LYS D CD    1 
ATOM   4696  C  CE    . LYS D 2 29  ? 17.491  12.197  4.113   1.00 16.25 ?  22  LYS D CE    1 
ATOM   4697  N  NZ    . LYS D 2 29  ? 16.125  11.858  3.701   1.00 15.75 1  22  LYS D NZ    1 
ATOM   4698  N  N     . GLN D 2 30  ? 22.008  16.860  5.602   1.00 23.75 ?  23  GLN D N     1 
ATOM   4699  C  CA    . GLN D 2 30  ? 23.353  17.374  5.397   1.00 24.68 ?  23  GLN D CA    1 
ATOM   4700  C  C     . GLN D 2 30  ? 24.037  17.601  6.743   1.00 23.62 ?  23  GLN D C     1 
ATOM   4701  O  O     . GLN D 2 30  ? 25.196  17.230  6.920   1.00 18.71 ?  23  GLN D O     1 
ATOM   4702  C  CB    . GLN D 2 30  ? 23.331  18.669  4.586   1.00 27.20 ?  23  GLN D CB    1 
ATOM   4703  C  CG    . GLN D 2 30  ? 23.327  18.443  3.078   1.00 28.41 ?  23  GLN D CG    1 
ATOM   4704  C  CD    . GLN D 2 30  ? 24.608  17.809  2.583   1.00 30.20 ?  23  GLN D CD    1 
ATOM   4705  O  OE1   . GLN D 2 30  ? 24.931  16.662  2.914   1.00 36.36 ?  23  GLN D OE1   1 
ATOM   4706  N  NE2   . GLN D 2 30  ? 25.356  18.556  1.786   1.00 31.68 ?  23  GLN D NE2   1 
ATOM   4707  N  N     . ASN D 2 31  ? 23.316  18.221  7.683   1.00 21.32 ?  24  ASN D N     1 
ATOM   4708  C  CA    . ASN D 2 31  ? 23.902  18.564  8.968   1.00 22.12 ?  24  ASN D CA    1 
ATOM   4709  C  C     . ASN D 2 31  ? 22.824  18.540  10.048  1.00 20.19 ?  24  ASN D C     1 
ATOM   4710  O  O     . ASN D 2 31  ? 22.293  19.582  10.426  1.00 16.09 ?  24  ASN D O     1 
ATOM   4711  C  CB    . ASN D 2 31  ? 24.604  19.916  8.913   1.00 21.76 ?  24  ASN D CB    1 
ATOM   4712  C  CG    . ASN D 2 31  ? 25.704  20.026  9.940   1.00 24.81 ?  24  ASN D CG    1 
ATOM   4713  O  OD1   . ASN D 2 31  ? 25.503  19.675  11.109  1.00 30.12 ?  24  ASN D OD1   1 
ATOM   4714  N  ND2   . ASN D 2 31  ? 26.872  20.493  9.526   1.00 24.16 ?  24  ASN D ND2   1 
ATOM   4715  N  N     . PRO D 2 32  ? 22.468  17.351  10.582  1.00 19.33 ?  25  PRO D N     1 
ATOM   4716  C  CA    . PRO D 2 32  ? 21.425  17.262  11.604  1.00 21.94 ?  25  PRO D CA    1 
ATOM   4717  C  C     . PRO D 2 32  ? 21.598  18.253  12.756  1.00 22.95 ?  25  PRO D C     1 
ATOM   4718  O  O     . PRO D 2 32  ? 20.652  18.953  13.111  1.00 29.03 ?  25  PRO D O     1 
ATOM   4719  C  CB    . PRO D 2 32  ? 21.528  15.788  12.042  1.00 21.22 ?  25  PRO D CB    1 
ATOM   4720  C  CG    . PRO D 2 32  ? 21.998  15.077  10.790  1.00 20.58 ?  25  PRO D CG    1 
ATOM   4721  C  CD    . PRO D 2 32  ? 23.017  16.039  10.200  1.00 20.75 ?  25  PRO D CD    1 
ATOM   4722  N  N     . GLU D 2 33  ? 22.807  18.329  13.324  1.00 22.22 ?  26  GLU D N     1 
ATOM   4723  C  CA    . GLU D 2 33  ? 23.052  19.158  14.496  1.00 26.41 ?  26  GLU D CA    1 
ATOM   4724  C  C     . GLU D 2 33  ? 22.913  20.642  14.161  1.00 26.50 ?  26  GLU D C     1 
ATOM   4725  O  O     . GLU D 2 33  ? 22.276  21.387  14.903  1.00 25.01 ?  26  GLU D O     1 
ATOM   4726  C  CB    . GLU D 2 33  ? 24.435  18.924  15.103  1.00 29.01 ?  26  GLU D CB    1 
ATOM   4727  C  CG    . GLU D 2 33  ? 24.489  17.730  16.050  1.00 32.14 ?  26  GLU D CG    1 
ATOM   4728  C  CD    . GLU D 2 33  ? 25.677  17.754  16.994  1.00 32.24 ?  26  GLU D CD    1 
ATOM   4729  O  OE1   . GLU D 2 33  ? 26.448  18.736  16.945  1.00 31.95 ?  26  GLU D OE1   1 
ATOM   4730  O  OE2   . GLU D 2 33  ? 25.830  16.795  17.779  1.00 35.87 -1 26  GLU D OE2   1 
ATOM   4731  N  N     . ALA D 2 34  ? 23.539  21.074  13.062  1.00 26.11 ?  27  ALA D N     1 
ATOM   4732  C  CA    . ALA D 2 34  ? 23.546  22.482  12.699  1.00 27.36 ?  27  ALA D CA    1 
ATOM   4733  C  C     . ALA D 2 34  ? 22.113  22.971  12.511  1.00 28.20 ?  27  ALA D C     1 
ATOM   4734  O  O     . ALA D 2 34  ? 21.763  24.073  12.928  1.00 29.79 ?  27  ALA D O     1 
ATOM   4735  C  CB    . ALA D 2 34  ? 24.371  22.695  11.450  1.00 28.89 ?  27  ALA D CB    1 
ATOM   4736  N  N     . VAL D 2 35  ? 21.293  22.129  11.877  1.00 25.17 ?  28  VAL D N     1 
ATOM   4737  C  CA    . VAL D 2 35  ? 19.920  22.477  11.560  1.00 25.71 ?  28  VAL D CA    1 
ATOM   4738  C  C     . VAL D 2 35  ? 19.078  22.468  12.834  1.00 28.34 ?  28  VAL D C     1 
ATOM   4739  O  O     . VAL D 2 35  ? 18.196  23.306  12.997  1.00 25.49 ?  28  VAL D O     1 
ATOM   4740  C  CB    . VAL D 2 35  ? 19.365  21.524  10.485  1.00 26.15 ?  28  VAL D CB    1 
ATOM   4741  C  CG1   . VAL D 2 35  ? 17.866  21.700  10.280  1.00 26.22 ?  28  VAL D CG1   1 
ATOM   4742  C  CG2   . VAL D 2 35  ? 20.114  21.687  9.168   1.00 26.80 ?  28  VAL D CG2   1 
ATOM   4743  N  N     . MET D 2 36  ? 19.360  21.529  13.743  1.00 28.17 ?  29  MET D N     1 
ATOM   4744  C  CA    . MET D 2 36  ? 18.597  21.436  14.977  1.00 26.55 ?  29  MET D CA    1 
ATOM   4745  C  C     . MET D 2 36  ? 18.923  22.623  15.883  1.00 26.63 ?  29  MET D C     1 
ATOM   4746  O  O     . MET D 2 36  ? 18.025  23.206  16.487  1.00 23.76 ?  29  MET D O     1 
ATOM   4747  C  CB    . MET D 2 36  ? 18.854  20.102  15.683  1.00 26.47 ?  29  MET D CB    1 
ATOM   4748  C  CG    . MET D 2 36  ? 18.182  18.935  14.988  1.00 25.55 ?  29  MET D CG    1 
ATOM   4749  S  SD    . MET D 2 36  ? 18.129  17.442  15.997  1.00 25.31 ?  29  MET D SD    1 
ATOM   4750  C  CE    . MET D 2 36  ? 19.757  16.763  15.648  1.00 29.46 ?  29  MET D CE    1 
ATOM   4751  N  N     . ARG D 2 37  ? 20.210  22.979  15.960  1.00 24.02 ?  30  ARG D N     1 
ATOM   4752  C  CA    . ARG D 2 37  ? 20.652  24.113  16.756  1.00 25.07 ?  30  ARG D CA    1 
ATOM   4753  C  C     . ARG D 2 37  ? 20.068  25.406  16.187  1.00 24.61 ?  30  ARG D C     1 
ATOM   4754  O  O     . ARG D 2 37  ? 19.758  26.330  16.936  1.00 22.34 ?  30  ARG D O     1 
ATOM   4755  C  CB    . ARG D 2 37  ? 22.184  24.152  16.820  1.00 26.10 ?  30  ARG D CB    1 
ATOM   4756  C  CG    . ARG D 2 37  ? 22.788  23.072  17.709  1.00 28.56 ?  30  ARG D CG    1 
ATOM   4757  C  CD    . ARG D 2 37  ? 24.269  23.273  17.992  1.00 31.63 ?  30  ARG D CD    1 
ATOM   4758  N  NE    . ARG D 2 37  ? 24.622  22.695  19.294  1.00 39.14 ?  30  ARG D NE    1 
ATOM   4759  C  CZ    . ARG D 2 37  ? 25.338  21.593  19.494  1.00 40.90 ?  30  ARG D CZ    1 
ATOM   4760  N  NH1   . ARG D 2 37  ? 25.831  20.918  18.471  1.00 42.92 1  30  ARG D NH1   1 
ATOM   4761  N  NH2   . ARG D 2 37  ? 25.553  21.167  20.726  1.00 42.67 ?  30  ARG D NH2   1 
ATOM   4762  N  N     . ALA D 2 38  ? 19.917  25.462  14.859  1.00 23.18 ?  31  ALA D N     1 
ATOM   4763  C  CA    . ALA D 2 38  ? 19.402  26.649  14.193  1.00 20.65 ?  31  ALA D CA    1 
ATOM   4764  C  C     . ALA D 2 38  ? 17.897  26.766  14.419  1.00 21.34 ?  31  ALA D C     1 
ATOM   4765  O  O     . ALA D 2 38  ? 17.313  27.820  14.177  1.00 21.85 ?  31  ALA D O     1 
ATOM   4766  C  CB    . ALA D 2 38  ? 19.741  26.611  12.718  1.00 21.21 ?  31  ALA D CB    1 
ATOM   4767  N  N     . HIS D 2 39  ? 17.276  25.675  14.879  1.00 20.28 ?  32  HIS D N     1 
ATOM   4768  C  CA    . HIS D 2 39  ? 15.864  25.690  15.230  1.00 20.58 ?  32  HIS D CA    1 
ATOM   4769  C  C     . HIS D 2 39  ? 15.723  25.615  16.750  1.00 20.06 ?  32  HIS D C     1 
ATOM   4770  O  O     . HIS D 2 39  ? 14.654  25.298  17.266  1.00 21.11 ?  32  HIS D O     1 
ATOM   4771  C  CB    . HIS D 2 39  ? 15.106  24.601  14.461  1.00 19.14 ?  32  HIS D CB    1 
ATOM   4772  C  CG    . HIS D 2 39  ? 14.874  24.934  13.020  1.00 18.35 ?  32  HIS D CG    1 
ATOM   4773  N  ND1   . HIS D 2 39  ? 15.881  24.938  12.079  1.00 18.61 ?  32  HIS D ND1   1 
ATOM   4774  C  CD2   . HIS D 2 39  ? 13.760  25.302  12.368  1.00 18.05 ?  32  HIS D CD2   1 
ATOM   4775  C  CE1   . HIS D 2 39  ? 15.380  25.281  10.901  1.00 18.69 ?  32  HIS D CE1   1 
ATOM   4776  N  NE2   . HIS D 2 39  ? 14.092  25.504  11.052  1.00 19.25 ?  32  HIS D NE2   1 
ATOM   4777  N  N     . GLY D 2 40  ? 16.824  25.907  17.452  1.00 19.68 ?  33  GLY D N     1 
ATOM   4778  C  CA    . GLY D 2 40  ? 16.800  26.185  18.880  1.00 22.40 ?  33  GLY D CA    1 
ATOM   4779  C  C     . GLY D 2 40  ? 16.569  24.947  19.745  1.00 23.79 ?  33  GLY D C     1 
ATOM   4780  O  O     . GLY D 2 40  ? 16.203  25.081  20.910  1.00 23.79 ?  33  GLY D O     1 
ATOM   4781  N  N     . LEU D 2 41  ? 16.791  23.747  19.194  1.00 27.81 ?  34  LEU D N     1 
ATOM   4782  C  CA    . LEU D 2 41  ? 16.687  22.532  19.989  1.00 29.02 ?  34  LEU D CA    1 
ATOM   4783  C  C     . LEU D 2 41  ? 17.807  22.517  21.028  1.00 29.09 ?  34  LEU D C     1 
ATOM   4784  O  O     . LEU D 2 41  ? 18.931  22.918  20.737  1.00 28.63 ?  34  LEU D O     1 
ATOM   4785  C  CB    . LEU D 2 41  ? 16.728  21.275  19.121  1.00 30.20 ?  34  LEU D CB    1 
ATOM   4786  C  CG    . LEU D 2 41  ? 15.390  20.818  18.531  1.00 30.71 ?  34  LEU D CG    1 
ATOM   4787  C  CD1   . LEU D 2 41  ? 14.780  21.883  17.638  1.00 29.93 ?  34  LEU D CD1   1 
ATOM   4788  C  CD2   . LEU D 2 41  ? 15.564  19.513  17.772  1.00 31.81 ?  34  LEU D CD2   1 
ATOM   4789  N  N     . THR D 2 42  ? 17.485  22.040  22.237  1.00 29.05 ?  35  THR D N     1 
ATOM   4790  C  CA    . THR D 2 42  ? 18.448  21.986  23.325  1.00 32.31 ?  35  THR D CA    1 
ATOM   4791  C  C     . THR D 2 42  ? 19.410  20.824  23.105  1.00 31.41 ?  35  THR D C     1 
ATOM   4792  O  O     . THR D 2 42  ? 19.203  19.986  22.230  1.00 27.41 ?  35  THR D O     1 
ATOM   4793  C  CB    . THR D 2 42  ? 17.736  21.837  24.669  1.00 32.07 ?  35  THR D CB    1 
ATOM   4794  O  OG1   . THR D 2 42  ? 17.054  20.589  24.591  1.00 33.37 ?  35  THR D OG1   1 
ATOM   4795  C  CG2   . THR D 2 42  ? 16.767  22.969  24.952  1.00 32.87 ?  35  THR D CG2   1 
ATOM   4796  N  N     . ASP D 2 43  ? 20.447  20.781  23.947  1.00 32.20 ?  36  ASP D N     1 
ATOM   4797  C  CA    . ASP D 2 43  ? 21.497  19.782  23.853  1.00 35.96 ?  36  ASP D CA    1 
ATOM   4798  C  C     . ASP D 2 43  ? 20.941  18.401  24.198  1.00 33.17 ?  36  ASP D C     1 
ATOM   4799  O  O     . ASP D 2 43  ? 21.323  17.412  23.577  1.00 29.01 ?  36  ASP D O     1 
ATOM   4800  C  CB    . ASP D 2 43  ? 22.697  20.185  24.697  1.00 40.74 ?  36  ASP D CB    1 
ATOM   4801  C  CG    . ASP D 2 43  ? 23.393  21.462  24.247  1.00 47.20 ?  36  ASP D CG    1 
ATOM   4802  O  OD1   . ASP D 2 43  ? 23.679  21.577  23.035  1.00 49.57 ?  36  ASP D OD1   1 
ATOM   4803  O  OD2   . ASP D 2 43  ? 23.652  22.327  25.111  1.00 52.03 -1 36  ASP D OD2   1 
ATOM   4804  N  N     . GLU D 2 44  ? 20.042  18.338  25.188  1.00 31.26 ?  37  GLU D N     1 
ATOM   4805  C  CA    . GLU D 2 44  ? 19.449  17.074  25.597  1.00 33.25 ?  37  GLU D CA    1 
ATOM   4806  C  C     . GLU D 2 44  ? 18.476  16.608  24.516  1.00 30.62 ?  37  GLU D C     1 
ATOM   4807  O  O     . GLU D 2 44  ? 18.375  15.414  24.241  1.00 30.38 ?  37  GLU D O     1 
ATOM   4808  C  CB    . GLU D 2 44  ? 18.763  17.183  26.960  1.00 37.41 ?  37  GLU D CB    1 
ATOM   4809  C  CG    . GLU D 2 44  ? 17.487  18.021  26.942  1.00 45.41 ?  37  GLU D CG    1 
ATOM   4810  C  CD    . GLU D 2 44  ? 16.879  18.287  28.309  1.00 50.74 ?  37  GLU D CD    1 
ATOM   4811  O  OE1   . GLU D 2 44  ? 16.445  17.316  28.963  1.00 53.62 ?  37  GLU D OE1   1 
ATOM   4812  O  OE2   . GLU D 2 44  ? 16.840  19.467  28.720  1.00 52.23 -1 37  GLU D OE2   1 
ATOM   4813  N  N     . GLN D 2 45  ? 17.765  17.565  23.908  1.00 28.70 ?  38  GLN D N     1 
ATOM   4814  C  CA    . GLN D 2 45  ? 16.861  17.273  22.807  1.00 26.04 ?  38  GLN D CA    1 
ATOM   4815  C  C     . GLN D 2 45  ? 17.657  16.689  21.644  1.00 22.59 ?  38  GLN D C     1 
ATOM   4816  O  O     . GLN D 2 45  ? 17.287  15.658  21.087  1.00 26.08 ?  38  GLN D O     1 
ATOM   4817  C  CB    . GLN D 2 45  ? 16.087  18.524  22.386  1.00 24.26 ?  38  GLN D CB    1 
ATOM   4818  C  CG    . GLN D 2 45  ? 14.920  18.858  23.310  1.00 26.96 ?  38  GLN D CG    1 
ATOM   4819  C  CD    . GLN D 2 45  ? 14.348  20.243  23.101  1.00 29.38 ?  38  GLN D CD    1 
ATOM   4820  O  OE1   . GLN D 2 45  ? 14.864  21.052  22.321  1.00 28.30 ?  38  GLN D OE1   1 
ATOM   4821  N  NE2   . GLN D 2 45  ? 13.272  20.535  23.817  1.00 31.87 ?  38  GLN D NE2   1 
ATOM   4822  N  N     . ILE D 2 46  ? 18.755  17.362  21.289  1.00 22.86 ?  39  ILE D N     1 
ATOM   4823  C  CA    . ILE D 2 46  ? 19.614  16.916  20.205  1.00 24.08 ?  39  ILE D CA    1 
ATOM   4824  C  C     . ILE D 2 46  ? 20.214  15.561  20.577  1.00 25.51 ?  39  ILE D C     1 
ATOM   4825  O  O     . ILE D 2 46  ? 20.268  14.655  19.748  1.00 28.93 ?  39  ILE D O     1 
ATOM   4826  C  CB    . ILE D 2 46  ? 20.685  17.979  19.893  1.00 25.37 ?  39  ILE D CB    1 
ATOM   4827  C  CG1   . ILE D 2 46  ? 20.043  19.254  19.333  1.00 27.53 ?  39  ILE D CG1   1 
ATOM   4828  C  CG2   . ILE D 2 46  ? 21.760  17.428  18.956  1.00 28.37 ?  39  ILE D CG2   1 
ATOM   4829  C  CD1   . ILE D 2 46  ? 21.027  20.347  18.955  1.00 27.23 ?  39  ILE D CD1   1 
ATOM   4830  N  N     . ASN D 2 47  ? 20.644  15.428  21.836  1.00 23.11 ?  40  ASN D N     1 
ATOM   4831  C  CA    . ASN D 2 47  ? 21.212  14.182  22.324  1.00 26.81 ?  40  ASN D CA    1 
ATOM   4832  C  C     . ASN D 2 47  ? 20.177  13.065  22.220  1.00 30.34 ?  40  ASN D C     1 
ATOM   4833  O  O     . ASN D 2 47  ? 20.523  11.919  21.940  1.00 25.20 ?  40  ASN D O     1 
ATOM   4834  C  CB    . ASN D 2 47  ? 21.728  14.315  23.752  1.00 30.15 ?  40  ASN D CB    1 
ATOM   4835  C  CG    . ASN D 2 47  ? 21.974  12.968  24.388  1.00 32.91 ?  40  ASN D CG    1 
ATOM   4836  O  OD1   . ASN D 2 47  ? 22.903  12.253  23.997  1.00 35.09 ?  40  ASN D OD1   1 
ATOM   4837  N  ND2   . ASN D 2 47  ? 21.153  12.603  25.362  1.00 32.91 ?  40  ASN D ND2   1 
ATOM   4838  N  N     . ALA D 2 48  ? 18.905  13.404  22.454  1.00 30.50 ?  41  ALA D N     1 
ATOM   4839  C  CA    . ALA D 2 48  ? 17.844  12.412  22.405  1.00 33.59 ?  41  ALA D CA    1 
ATOM   4840  C  C     . ALA D 2 48  ? 17.609  11.976  20.961  1.00 34.37 ?  41  ALA D C     1 
ATOM   4841  O  O     . ALA D 2 48  ? 17.252  10.826  20.712  1.00 36.62 ?  41  ALA D O     1 
ATOM   4842  C  CB    . ALA D 2 48  ? 16.582  12.954  23.042  1.00 35.47 ?  41  ALA D CB    1 
ATOM   4843  N  N     . VAL D 2 49  ? 17.818  12.896  20.012  1.00 31.16 ?  42  VAL D N     1 
ATOM   4844  C  CA    . VAL D 2 49  ? 17.644  12.577  18.603  1.00 30.39 ?  42  VAL D CA    1 
ATOM   4845  C  C     . VAL D 2 49  ? 18.772  11.646  18.160  1.00 26.53 ?  42  VAL D C     1 
ATOM   4846  O  O     . VAL D 2 49  ? 18.520  10.623  17.529  1.00 26.23 ?  42  VAL D O     1 
ATOM   4847  C  CB    . VAL D 2 49  ? 17.578  13.823  17.699  1.00 28.61 ?  42  VAL D CB    1 
ATOM   4848  C  CG1   . VAL D 2 49  ? 17.748  13.462  16.227  1.00 27.02 ?  42  VAL D CG1   1 
ATOM   4849  C  CG2   . VAL D 2 49  ? 16.290  14.609  17.911  1.00 30.08 ?  42  VAL D CG2   1 
ATOM   4850  N  N     . MET D 2 50  ? 20.014  12.012  18.495  1.00 25.62 ?  43  MET D N     1 
ATOM   4851  C  CA    . MET D 2 50  ? 21.178  11.316  17.973  1.00 29.53 ?  43  MET D CA    1 
ATOM   4852  C  C     . MET D 2 50  ? 21.270  9.910   18.569  1.00 27.48 ?  43  MET D C     1 
ATOM   4853  O  O     . MET D 2 50  ? 21.810  9.011   17.931  1.00 24.60 ?  43  MET D O     1 
ATOM   4854  C  CB    . MET D 2 50  ? 22.464  12.108  18.242  1.00 33.00 ?  43  MET D CB    1 
ATOM   4855  C  CG    . MET D 2 50  ? 22.432  13.536  17.717  1.00 35.19 ?  43  MET D CG    1 
ATOM   4856  S  SD    . MET D 2 50  ? 21.906  13.673  15.996  1.00 41.83 ?  43  MET D SD    1 
ATOM   4857  C  CE    . MET D 2 50  ? 23.165  12.682  15.179  1.00 45.13 ?  43  MET D CE    1 
ATOM   4858  N  N     . THR D 2 51  ? 20.734  9.714   19.780  1.00 28.04 ?  44  THR D N     1 
ATOM   4859  C  CA    . THR D 2 51  ? 20.747  8.397   20.399  1.00 29.42 ?  44  THR D CA    1 
ATOM   4860  C  C     . THR D 2 51  ? 19.495  7.627   19.987  1.00 30.45 ?  44  THR D C     1 
ATOM   4861  O  O     . THR D 2 51  ? 19.326  6.469   20.362  1.00 36.16 ?  44  THR D O     1 
ATOM   4862  C  CB    . THR D 2 51  ? 20.855  8.512   21.919  1.00 31.60 ?  44  THR D CB    1 
ATOM   4863  O  OG1   . THR D 2 51  ? 19.692  9.212   22.348  1.00 32.69 ?  44  THR D OG1   1 
ATOM   4864  C  CG2   . THR D 2 51  ? 22.109  9.246   22.359  1.00 34.59 ?  44  THR D CG2   1 
ATOM   4865  N  N     . GLY D 2 52  ? 18.626  8.279   19.208  1.00 30.70 ?  45  GLY D N     1 
ATOM   4866  C  CA    . GLY D 2 52  ? 17.373  7.679   18.783  1.00 31.76 ?  45  GLY D CA    1 
ATOM   4867  C  C     . GLY D 2 52  ? 16.539  7.221   19.977  1.00 36.34 ?  45  GLY D C     1 
ATOM   4868  O  O     . GLY D 2 52  ? 16.127  6.065   20.042  1.00 36.04 ?  45  GLY D O     1 
ATOM   4869  N  N     . ASP D 2 53  ? 16.306  8.141   20.920  1.00 36.83 ?  46  ASP D N     1 
ATOM   4870  C  CA    . ASP D 2 53  ? 15.424  7.889   22.048  1.00 37.01 ?  46  ASP D CA    1 
ATOM   4871  C  C     . ASP D 2 53  ? 14.164  8.732   21.879  1.00 38.33 ?  46  ASP D C     1 
ATOM   4872  O  O     . ASP D 2 53  ? 14.179  9.937   22.120  1.00 34.10 ?  46  ASP D O     1 
ATOM   4873  C  CB    . ASP D 2 53  ? 16.117  8.163   23.374  1.00 34.84 ?  46  ASP D CB    1 
ATOM   4874  C  CG    . ASP D 2 53  ? 15.345  7.736   24.614  1.00 35.00 ?  46  ASP D CG    1 
ATOM   4875  O  OD1   . ASP D 2 53  ? 14.153  7.388   24.473  1.00 32.68 ?  46  ASP D OD1   1 
ATOM   4876  O  OD2   . ASP D 2 53  ? 15.947  7.743   25.710  1.00 39.10 -1 46  ASP D OD2   1 
ATOM   4877  N  N     . MET D 2 54  ? 13.074  8.081   21.464  1.00 38.47 ?  47  MET D N     1 
ATOM   4878  C  CA    . MET D 2 54  ? 11.856  8.784   21.099  1.00 42.76 ?  47  MET D CA    1 
ATOM   4879  C  C     . MET D 2 54  ? 11.030  9.079   22.351  1.00 46.34 ?  47  MET D C     1 
ATOM   4880  O  O     . MET D 2 54  ? 10.279  10.051  22.380  1.00 48.49 ?  47  MET D O     1 
ATOM   4881  C  CB    . MET D 2 54  ? 11.046  7.965   20.088  1.00 41.41 ?  47  MET D CB    1 
ATOM   4882  C  CG    . MET D 2 54  ? 11.783  7.676   18.787  1.00 39.59 ?  47  MET D CG    1 
ATOM   4883  S  SD    . MET D 2 54  ? 12.305  9.147   17.880  1.00 35.78 ?  47  MET D SD    1 
ATOM   4884  C  CE    . MET D 2 54  ? 14.035  9.379   18.318  1.00 37.67 ?  47  MET D CE    1 
ATOM   4885  N  N     . GLU D 2 55  ? 11.184  8.243   23.384  1.00 49.54 ?  48  GLU D N     1 
ATOM   4886  C  CA    . GLU D 2 55  ? 10.457  8.420   24.631  1.00 53.41 ?  48  GLU D CA    1 
ATOM   4887  C  C     . GLU D 2 55  ? 10.820  9.765   25.255  1.00 57.36 ?  48  GLU D C     1 
ATOM   4888  O  O     . GLU D 2 55  ? 9.943   10.583  25.523  1.00 62.10 ?  48  GLU D O     1 
ATOM   4889  C  CB    . GLU D 2 55  ? 10.762  7.311   25.638  1.00 55.55 ?  48  GLU D CB    1 
ATOM   4890  C  CG    . GLU D 2 55  ? 9.924   7.407   26.911  1.00 54.46 ?  48  GLU D CG    1 
ATOM   4891  C  CD    . GLU D 2 55  ? 8.467   7.029   26.717  1.00 48.81 ?  48  GLU D CD    1 
ATOM   4892  O  OE1   . GLU D 2 55  ? 8.206   5.870   26.331  1.00 54.00 ?  48  GLU D OE1   1 
ATOM   4893  O  OE2   . GLU D 2 55  ? 7.594   7.891   26.949  1.00 40.62 -1 48  GLU D OE2   1 
ATOM   4894  N  N     . LYS D 2 56  ? 12.120  9.979   25.489  1.00 53.50 ?  49  LYS D N     1 
ATOM   4895  C  CA    . LYS D 2 56  ? 12.585  11.173  26.177  1.00 55.77 ?  49  LYS D CA    1 
ATOM   4896  C  C     . LYS D 2 56  ? 12.187  12.409  25.375  1.00 53.14 ?  49  LYS D C     1 
ATOM   4897  O  O     . LYS D 2 56  ? 12.048  13.495  25.933  1.00 66.09 ?  49  LYS D O     1 
ATOM   4898  C  CB    . LYS D 2 56  ? 14.097  11.145  26.432  1.00 55.31 ?  49  LYS D CB    1 
ATOM   4899  C  CG    . LYS D 2 56  ? 14.584  12.205  27.417  1.00 56.74 ?  49  LYS D CG    1 
ATOM   4900  C  CD    . LYS D 2 56  ? 15.952  11.929  28.031  1.00 59.27 ?  49  LYS D CD    1 
ATOM   4901  C  CE    . LYS D 2 56  ? 16.500  13.091  28.805  1.00 60.27 ?  49  LYS D CE    1 
ATOM   4902  N  NZ    . LYS D 2 56  ? 15.661  13.463  29.948  1.00 57.01 1  49  LYS D NZ    1 
ATOM   4903  N  N     . LEU D 2 57  ? 12.005  12.232  24.062  1.00 47.44 ?  50  LEU D N     1 
ATOM   4904  C  CA    . LEU D 2 57  ? 11.544  13.311  23.204  1.00 47.46 ?  50  LEU D CA    1 
ATOM   4905  C  C     . LEU D 2 57  ? 10.058  13.560  23.450  1.00 45.88 ?  50  LEU D C     1 
ATOM   4906  O  O     . LEU D 2 57  ? 9.575   14.672  23.249  1.00 50.65 ?  50  LEU D O     1 
ATOM   4907  C  CB    . LEU D 2 57  ? 11.815  12.989  21.735  1.00 47.20 ?  50  LEU D CB    1 
ATOM   4908  C  CG    . LEU D 2 57  ? 13.178  13.425  21.188  1.00 45.17 ?  50  LEU D CG    1 
ATOM   4909  C  CD1   . LEU D 2 57  ? 13.337  12.944  19.758  1.00 45.51 ?  50  LEU D CD1   1 
ATOM   4910  C  CD2   . LEU D 2 57  ? 13.353  14.933  21.268  1.00 45.65 ?  50  LEU D CD2   1 
ATOM   4911  N  N     . LYS D 2 58  ? 9.343   12.520  23.891  1.00 44.07 ?  51  LYS D N     1 
ATOM   4912  C  CA    . LYS D 2 58  ? 7.894   12.586  23.991  1.00 45.65 ?  51  LYS D CA    1 
ATOM   4913  C  C     . LYS D 2 58  ? 7.449   12.834  25.431  1.00 46.02 ?  51  LYS D C     1 
ATOM   4914  O  O     . LYS D 2 58  ? 6.252   12.873  25.704  1.00 46.28 ?  51  LYS D O     1 
ATOM   4915  C  CB    . LYS D 2 58  ? 7.257   11.306  23.442  1.00 46.58 ?  51  LYS D CB    1 
ATOM   4916  C  CG    . LYS D 2 58  ? 7.425   11.099  21.945  1.00 46.26 ?  51  LYS D CG    1 
ATOM   4917  C  CD    . LYS D 2 58  ? 6.304   10.258  21.350  1.00 44.98 ?  51  LYS D CD    1 
ATOM   4918  C  CE    . LYS D 2 58  ? 6.668   9.613   20.055  1.00 46.44 ?  51  LYS D CE    1 
ATOM   4919  N  NZ    . LYS D 2 58  ? 5.959   8.338   19.916  1.00 49.90 1  51  LYS D NZ    1 
ATOM   4920  N  N     . THR D 2 59  ? 8.406   13.001  26.349  1.00 50.36 ?  52  THR D N     1 
ATOM   4921  C  CA    . THR D 2 59  ? 8.073   13.367  27.717  1.00 57.05 ?  52  THR D CA    1 
ATOM   4922  C  C     . THR D 2 59  ? 8.688   14.717  28.026  1.00 57.57 ?  52  THR D C     1 
ATOM   4923  O  O     . THR D 2 59  ? 9.433   15.218  27.154  1.00 59.74 ?  52  THR D O     1 
ATOM   4924  C  CB    . THR D 2 59  ? 8.548   12.293  28.695  1.00 58.90 ?  52  THR D CB    1 
ATOM   4925  O  OG1   . THR D 2 59  ? 7.905   12.603  29.928  1.00 58.34 ?  52  THR D OG1   1 
ATOM   4926  C  CG2   . THR D 2 59  ? 10.055  12.286  28.876  1.00 62.67 ?  52  THR D CG2   1 
ATOM   4927  N  N     . GLY E 1 2   ? 48.226  69.040  1.325   1.00 25.32 ?  2   GLY H N     1 
ATOM   4928  C  CA    . GLY E 1 2   ? 47.098  68.408  0.613   1.00 24.19 ?  2   GLY H CA    1 
ATOM   4929  C  C     . GLY E 1 2   ? 46.408  67.370  1.494   1.00 24.41 ?  2   GLY H C     1 
ATOM   4930  O  O     . GLY E 1 2   ? 47.065  66.625  2.219   1.00 24.40 ?  2   GLY H O     1 
ATOM   4931  N  N     . SER E 1 3   ? 45.073  67.342  1.424   1.00 20.34 ?  3   SER H N     1 
ATOM   4932  C  CA    . SER E 1 3   ? 44.278  66.488  2.291   1.00 19.67 ?  3   SER H CA    1 
ATOM   4933  C  C     . SER E 1 3   ? 43.027  66.007  1.572   1.00 16.04 ?  3   SER H C     1 
ATOM   4934  O  O     . SER E 1 3   ? 42.636  66.553  0.544   1.00 12.55 ?  3   SER H O     1 
ATOM   4935  C  CB    . SER E 1 3   ? 43.878  67.196  3.552   1.00 20.44 ?  3   SER H CB    1 
ATOM   4936  O  OG    . SER E 1 3   ? 43.027  68.295  3.257   1.00 23.41 ?  3   SER H OG    1 
ATOM   4937  N  N     . LEU E 1 4   ? 42.387  65.002  2.168   1.00 15.71 ?  4   LEU H N     1 
ATOM   4938  C  CA    . LEU E 1 4   ? 41.198  64.424  1.581   1.00 14.16 ?  4   LEU H CA    1 
ATOM   4939  C  C     . LEU E 1 4   ? 40.126  64.281  2.653   1.00 12.29 ?  4   LEU H C     1 
ATOM   4940  O  O     . LEU E 1 4   ? 40.401  63.851  3.771   1.00 9.66  ?  4   LEU H O     1 
ATOM   4941  C  CB    . LEU E 1 4   ? 41.545  63.083  0.940   1.00 16.22 ?  4   LEU H CB    1 
ATOM   4942  C  CG    . LEU E 1 4   ? 40.368  62.334  0.311   1.00 17.09 ?  4   LEU H CG    1 
ATOM   4943  C  CD1   . LEU E 1 4   ? 39.763  63.169  -0.804  1.00 16.85 ?  4   LEU H CD1   1 
ATOM   4944  C  CD2   . LEU E 1 4   ? 40.792  60.966  -0.192  1.00 17.23 ?  4   LEU H CD2   1 
ATOM   4945  N  N     . VAL E 1 5   ? 38.909  64.687  2.287   1.00 11.66 ?  5   VAL H N     1 
ATOM   4946  C  CA    . VAL E 1 5   ? 37.726  64.404  3.076   1.00 11.39 ?  5   VAL H CA    1 
ATOM   4947  C  C     . VAL E 1 5   ? 36.660  63.893  2.112   1.00 12.46 ?  5   VAL H C     1 
ATOM   4948  O  O     . VAL E 1 5   ? 36.297  64.570  1.152   1.00 12.63 ?  5   VAL H O     1 
ATOM   4949  C  CB    . VAL E 1 5   ? 37.189  65.592  3.898   1.00 12.74 ?  5   VAL H CB    1 
ATOM   4950  C  CG1   . VAL E 1 5   ? 35.972  65.177  4.717   1.00 12.31 ?  5   VAL H CG1   1 
ATOM   4951  C  CG2   . VAL E 1 5   ? 38.253  66.207  4.803   1.00 12.80 ?  5   VAL H CG2   1 
ATOM   4952  N  N     . CYS E 1 6   ? 36.188  62.673  2.375   1.00 12.75 ?  6   CYS H N     1 
ATOM   4953  C  CA    . CYS E 1 6   ? 35.123  62.070  1.595   1.00 12.31 ?  6   CYS H CA    1 
ATOM   4954  C  C     . CYS E 1 6   ? 33.812  62.234  2.353   1.00 11.34 ?  6   CYS H C     1 
ATOM   4955  O  O     . CYS E 1 6   ? 33.708  61.830  3.508   1.00 10.80 ?  6   CYS H O     1 
ATOM   4956  C  CB    . CYS E 1 6   ? 35.404  60.595  1.335   1.00 14.46 ?  6   CYS H CB    1 
ATOM   4957  S  SG    . CYS E 1 6   ? 36.873  60.308  0.314   1.00 16.42 ?  6   CYS H SG    1 
ATOM   4958  N  N     . VAL E 1 7   ? 32.820  62.846  1.700   1.00 14.49 ?  7   VAL H N     1 
ATOM   4959  C  CA    . VAL E 1 7   ? 31.545  63.096  2.349   1.00 14.09 ?  7   VAL H CA    1 
ATOM   4960  C  C     . VAL E 1 7   ? 30.429  62.470  1.519   1.00 14.72 ?  7   VAL H C     1 
ATOM   4961  O  O     . VAL E 1 7   ? 30.629  62.099  0.365   1.00 16.59 ?  7   VAL H O     1 
ATOM   4962  C  CB    . VAL E 1 7   ? 31.280  64.594  2.598   1.00 14.05 ?  7   VAL H CB    1 
ATOM   4963  C  CG1   . VAL E 1 7   ? 32.371  65.210  3.463   1.00 14.09 ?  7   VAL H CG1   1 
ATOM   4964  C  CG2   . VAL E 1 7   ? 31.107  65.387  1.307   1.00 14.56 ?  7   VAL H CG2   1 
ATOM   4965  N  N     . GLY E 1 8   ? 29.262  62.336  2.153   1.00 17.63 ?  8   GLY H N     1 
ATOM   4966  C  CA    . GLY E 1 8   ? 28.044  61.933  1.474   1.00 17.73 ?  8   GLY H CA    1 
ATOM   4967  C  C     . GLY E 1 8   ? 27.101  63.123  1.320   1.00 18.81 ?  8   GLY H C     1 
ATOM   4968  O  O     . GLY E 1 8   ? 27.141  64.056  2.120   1.00 17.82 ?  8   GLY H O     1 
ATOM   4969  N  N     . THR E 1 9   ? 26.258  63.076  0.284   1.00 17.68 ?  9   THR H N     1 
ATOM   4970  C  CA    . THR E 1 9   ? 25.317  64.149  0.013   1.00 20.47 ?  9   THR H CA    1 
ATOM   4971  C  C     . THR E 1 9   ? 23.891  63.661  0.264   1.00 19.26 ?  9   THR H C     1 
ATOM   4972  O  O     . THR E 1 9   ? 22.933  64.389  0.013   1.00 19.47 ?  9   THR H O     1 
ATOM   4973  C  CB    . THR E 1 9   ? 25.490  64.631  -1.428  1.00 20.80 ?  9   THR H CB    1 
ATOM   4974  O  OG1   . THR E 1 9   ? 25.167  63.510  -2.243  1.00 19.98 ?  9   THR H OG1   1 
ATOM   4975  C  CG2   . THR E 1 9   ? 26.901  65.103  -1.731  1.00 22.00 ?  9   THR H CG2   1 
ATOM   4976  N  N     . GLY E 1 10  ? 23.753  62.423  0.753   1.00 16.53 ?  10  GLY H N     1 
ATOM   4977  C  CA    . GLY E 1 10  ? 22.442  61.818  0.923   1.00 13.44 ?  10  GLY H CA    1 
ATOM   4978  C  C     . GLY E 1 10  ? 21.788  61.561  -0.432  1.00 12.56 ?  10  GLY H C     1 
ATOM   4979  O  O     . GLY E 1 10  ? 22.399  61.807  -1.469  1.00 11.73 ?  10  GLY H O     1 
ATOM   4980  N  N     . LEU E 1 11  ? 20.549  61.058  -0.412  1.00 13.76 ?  11  LEU H N     1 
ATOM   4981  C  CA    . LEU E 1 11  ? 19.795  60.792  -1.629  1.00 15.32 ?  11  LEU H CA    1 
ATOM   4982  C  C     . LEU E 1 11  ? 19.037  62.036  -2.088  1.00 14.48 ?  11  LEU H C     1 
ATOM   4983  O  O     . LEU E 1 11  ? 19.068  62.382  -3.267  1.00 14.13 ?  11  LEU H O     1 
ATOM   4984  C  CB    . LEU E 1 11  ? 18.842  59.625  -1.383  1.00 17.10 ?  11  LEU H CB    1 
ATOM   4985  C  CG    . LEU E 1 11  ? 19.260  58.287  -1.995  1.00 19.01 ?  11  LEU H CG    1 
ATOM   4986  C  CD1   . LEU E 1 11  ? 20.633  58.374  -2.638  1.00 20.74 ?  11  LEU H CD1   1 
ATOM   4987  C  CD2   . LEU E 1 11  ? 19.245  57.246  -0.899  1.00 19.89 ?  11  LEU H CD2   1 
ATOM   4988  N  N     . GLN E 1 12  ? 18.337  62.689  -1.156  1.00 13.53 ?  12  GLN H N     1 
ATOM   4989  C  CA    . GLN E 1 12  ? 17.463  63.797  -1.506  1.00 17.22 ?  12  GLN H CA    1 
ATOM   4990  C  C     . GLN E 1 12  ? 18.283  65.061  -1.731  1.00 18.06 ?  12  GLN H C     1 
ATOM   4991  O  O     . GLN E 1 12  ? 19.264  65.319  -1.037  1.00 18.16 ?  12  GLN H O     1 
ATOM   4992  C  CB    . GLN E 1 12  ? 16.414  64.123  -0.444  1.00 15.47 ?  12  GLN H CB    1 
ATOM   4993  C  CG    . GLN E 1 12  ? 15.105  63.356  -0.595  1.00 16.17 ?  12  GLN H CG    1 
ATOM   4994  C  CD    . GLN E 1 12  ? 14.186  63.950  -1.642  1.00 15.22 ?  12  GLN H CD    1 
ATOM   4995  O  OE1   . GLN E 1 12  ? 14.592  64.777  -2.465  1.00 13.97 ?  12  GLN H OE1   1 
ATOM   4996  N  NE2   . GLN E 1 12  ? 12.930  63.531  -1.619  1.00 15.53 ?  12  GLN H NE2   1 
ATOM   4997  N  N     . LEU E 1 13  ? 17.824  65.852  -2.701  1.00 18.32 ?  13  LEU H N     1 
ATOM   4998  C  CA    . LEU E 1 13  ? 18.461  67.102  -3.067  1.00 17.30 ?  13  LEU H CA    1 
ATOM   4999  C  C     . LEU E 1 13  ? 18.563  68.038  -1.865  1.00 16.15 ?  13  LEU H C     1 
ATOM   5000  O  O     . LEU E 1 13  ? 17.560  68.365  -1.234  1.00 18.74 ?  13  LEU H O     1 
ATOM   5001  C  CB    . LEU E 1 13  ? 17.612  67.702  -4.185  1.00 16.71 ?  13  LEU H CB    1 
ATOM   5002  C  CG    . LEU E 1 13  ? 18.065  69.062  -4.717  1.00 16.18 ?  13  LEU H CG    1 
ATOM   5003  C  CD1   . LEU E 1 13  ? 19.386  68.922  -5.448  1.00 15.83 ?  13  LEU H CD1   1 
ATOM   5004  C  CD2   . LEU E 1 13  ? 16.994  69.656  -5.613  1.00 15.61 ?  13  LEU H CD2   1 
ATOM   5005  N  N     . ALA E 1 14  ? 19.805  68.418  -1.546  1.00 14.28 ?  14  ALA H N     1 
ATOM   5006  C  CA    . ALA E 1 14  ? 20.121  69.661  -0.858  1.00 14.54 ?  14  ALA H CA    1 
ATOM   5007  C  C     . ALA E 1 14  ? 19.970  69.531  0.656   1.00 14.82 ?  14  ALA H C     1 
ATOM   5008  O  O     . ALA E 1 14  ? 20.751  70.114  1.405   1.00 14.92 ?  14  ALA H O     1 
ATOM   5009  C  CB    . ALA E 1 14  ? 19.268  70.786  -1.410  1.00 15.65 ?  14  ALA H CB    1 
ATOM   5010  N  N     . GLY E 1 15  ? 18.970  68.767  1.104   1.00 14.55 ?  15  GLY H N     1 
ATOM   5011  C  CA    . GLY E 1 15  ? 18.597  68.761  2.509   1.00 15.26 ?  15  GLY H CA    1 
ATOM   5012  C  C     . GLY E 1 15  ? 19.215  67.610  3.303   1.00 13.80 ?  15  GLY H C     1 
ATOM   5013  O  O     . GLY E 1 15  ? 19.305  67.696  4.525   1.00 14.53 ?  15  GLY H O     1 
ATOM   5014  N  N     . GLN E 1 16  ? 19.641  66.539  2.623   1.00 12.71 ?  16  GLN H N     1 
ATOM   5015  C  CA    . GLN E 1 16  ? 19.924  65.285  3.309   1.00 12.19 ?  16  GLN H CA    1 
ATOM   5016  C  C     . GLN E 1 16  ? 21.410  65.153  3.648   1.00 13.64 ?  16  GLN H C     1 
ATOM   5017  O  O     . GLN E 1 16  ? 21.823  64.152  4.232   1.00 15.08 ?  16  GLN H O     1 
ATOM   5018  C  CB    . GLN E 1 16  ? 19.436  64.097  2.480   1.00 10.76 ?  16  GLN H CB    1 
ATOM   5019  C  CG    . GLN E 1 16  ? 19.154  62.853  3.315   1.00 12.01 ?  16  GLN H CG    1 
ATOM   5020  C  CD    . GLN E 1 16  ? 18.254  61.855  2.621   1.00 12.03 ?  16  GLN H CD    1 
ATOM   5021  O  OE1   . GLN E 1 16  ? 18.514  61.430  1.490   1.00 14.00 ?  16  GLN H OE1   1 
ATOM   5022  N  NE2   . GLN E 1 16  ? 17.181  61.475  3.298   1.00 10.87 ?  16  GLN H NE2   1 
ATOM   5023  N  N     . ILE E 1 17  ? 22.208  66.165  3.293   1.00 13.96 ?  17  ILE H N     1 
ATOM   5024  C  CA    . ILE E 1 17  ? 23.624  66.180  3.630   1.00 15.77 ?  17  ILE H CA    1 
ATOM   5025  C  C     . ILE E 1 17  ? 23.790  66.707  5.055   1.00 18.12 ?  17  ILE H C     1 
ATOM   5026  O  O     . ILE E 1 17  ? 22.965  67.484  5.532   1.00 19.91 ?  17  ILE H O     1 
ATOM   5027  C  CB    . ILE E 1 17  ? 24.421  67.020  2.614   1.00 16.04 ?  17  ILE H CB    1 
ATOM   5028  C  CG1   . ILE E 1 17  ? 25.925  66.992  2.911   1.00 16.03 ?  17  ILE H CG1   1 
ATOM   5029  C  CG2   . ILE E 1 17  ? 23.883  68.451  2.546   1.00 15.54 ?  17  ILE H CG2   1 
ATOM   5030  C  CD1   . ILE E 1 17  ? 26.759  67.876  2.000   1.00 16.73 ?  17  ILE H CD1   1 
ATOM   5031  N  N     . SER E 1 18  ? 24.866  66.273  5.725   1.00 18.01 ?  18  SER H N     1 
ATOM   5032  C  CA    . SER E 1 18  ? 25.182  66.727  7.070   1.00 17.78 ?  18  SER H CA    1 
ATOM   5033  C  C     . SER E 1 18  ? 25.544  68.209  7.053   1.00 16.20 ?  18  SER H C     1 
ATOM   5034  O  O     . SER E 1 18  ? 25.978  68.735  6.032   1.00 15.10 ?  18  SER H O     1 
ATOM   5035  C  CB    . SER E 1 18  ? 26.298  65.919  7.681   1.00 18.09 ?  18  SER H CB    1 
ATOM   5036  O  OG    . SER E 1 18  ? 25.792  64.763  8.333   1.00 25.28 ?  18  SER H OG    1 
ATOM   5037  N  N     . VAL E 1 19  ? 25.372  68.863  8.205   1.00 15.36 ?  19  VAL H N     1 
ATOM   5038  C  CA    . VAL E 1 19  ? 25.718  70.266  8.352   1.00 16.88 ?  19  VAL H CA    1 
ATOM   5039  C  C     . VAL E 1 19  ? 27.230  70.423  8.200   1.00 18.24 ?  19  VAL H C     1 
ATOM   5040  O  O     . VAL E 1 19  ? 27.692  71.359  7.551   1.00 18.02 ?  19  VAL H O     1 
ATOM   5041  C  CB    . VAL E 1 19  ? 25.200  70.802  9.701   1.00 16.58 ?  19  VAL H CB    1 
ATOM   5042  C  CG1   . VAL E 1 19  ? 25.608  72.249  9.952   1.00 16.30 ?  19  VAL H CG1   1 
ATOM   5043  C  CG2   . VAL E 1 19  ? 23.687  70.655  9.808   1.00 16.86 ?  19  VAL H CG2   1 
ATOM   5044  N  N     . LEU E 1 20  ? 27.995  69.482  8.772   1.00 20.56 ?  20  LEU H N     1 
ATOM   5045  C  CA    . LEU E 1 20  ? 29.450  69.543  8.718   1.00 18.70 ?  20  LEU H CA    1 
ATOM   5046  C  C     . LEU E 1 20  ? 29.909  69.293  7.284   1.00 16.05 ?  20  LEU H C     1 
ATOM   5047  O  O     . LEU E 1 20  ? 30.749  70.020  6.761   1.00 16.49 ?  20  LEU H O     1 
ATOM   5048  C  CB    . LEU E 1 20  ? 30.096  68.549  9.686   1.00 16.44 ?  20  LEU H CB    1 
ATOM   5049  C  CG    . LEU E 1 20  ? 31.625  68.611  9.800   1.00 15.10 ?  20  LEU H CG    1 
ATOM   5050  C  CD1   . LEU E 1 20  ? 32.117  70.001  10.165  1.00 16.47 ?  20  LEU H CD1   1 
ATOM   5051  C  CD2   . LEU E 1 20  ? 32.148  67.610  10.815  1.00 13.97 ?  20  LEU H CD2   1 
ATOM   5052  N  N     . SER E 1 21  ? 29.341  68.258  6.659   1.00 17.41 ?  21  SER H N     1 
ATOM   5053  C  CA    . SER E 1 21  ? 29.753  67.834  5.331   1.00 14.58 ?  21  SER H CA    1 
ATOM   5054  C  C     . SER E 1 21  ? 29.566  68.971  4.330   1.00 13.99 ?  21  SER H C     1 
ATOM   5055  O  O     . SER E 1 21  ? 30.445  69.233  3.512   1.00 15.62 ?  21  SER H O     1 
ATOM   5056  C  CB    . SER E 1 21  ? 29.006  66.598  4.915   1.00 13.13 ?  21  SER H CB    1 
ATOM   5057  O  OG    . SER E 1 21  ? 29.279  65.534  5.816   1.00 13.08 ?  21  SER H OG    1 
ATOM   5058  N  N     . ARG E 1 22  ? 28.418  69.649  4.405   1.00 12.09 ?  22  ARG H N     1 
ATOM   5059  C  CA    . ARG E 1 22  ? 28.149  70.781  3.535   1.00 11.68 ?  22  ARG H CA    1 
ATOM   5060  C  C     . ARG E 1 22  ? 29.254  71.819  3.707   1.00 10.52 ?  22  ARG H C     1 
ATOM   5061  O  O     . ARG E 1 22  ? 29.669  72.464  2.745   1.00 9.90  ?  22  ARG H O     1 
ATOM   5062  C  CB    . ARG E 1 22  ? 26.772  71.373  3.856   1.00 12.96 ?  22  ARG H CB    1 
ATOM   5063  C  CG    . ARG E 1 22  ? 26.330  72.497  2.930   1.00 14.54 ?  22  ARG H CG    1 
ATOM   5064  C  CD    . ARG E 1 22  ? 24.983  73.072  3.350   1.00 16.66 ?  22  ARG H CD    1 
ATOM   5065  N  NE    . ARG E 1 22  ? 24.343  73.836  2.275   1.00 17.88 ?  22  ARG H NE    1 
ATOM   5066  C  CZ    . ARG E 1 22  ? 24.522  75.127  2.027   1.00 21.15 ?  22  ARG H CZ    1 
ATOM   5067  N  NH1   . ARG E 1 22  ? 25.196  75.883  2.877   1.00 21.09 1  22  ARG H NH1   1 
ATOM   5068  N  NH2   . ARG E 1 22  ? 23.986  75.664  0.945   1.00 23.04 ?  22  ARG H NH2   1 
ATOM   5069  N  N     . SER E 1 23  ? 29.724  71.964  4.949   1.00 10.66 ?  23  SER H N     1 
ATOM   5070  C  CA    . SER E 1 23  ? 30.701  72.982  5.299   1.00 11.63 ?  23  SER H CA    1 
ATOM   5071  C  C     . SER E 1 23  ? 32.067  72.619  4.721   1.00 11.39 ?  23  SER H C     1 
ATOM   5072  O  O     . SER E 1 23  ? 32.856  73.497  4.380   1.00 12.55 ?  23  SER H O     1 
ATOM   5073  C  CB    . SER E 1 23  ? 30.762  73.167  6.797   1.00 11.03 ?  23  SER H CB    1 
ATOM   5074  O  OG    . SER E 1 23  ? 31.769  74.103  7.159   1.00 11.26 ?  23  SER H OG    1 
ATOM   5075  N  N     . TYR E 1 24  ? 32.329  71.310  4.623   1.00 12.97 ?  24  TYR H N     1 
ATOM   5076  C  CA    . TYR E 1 24  ? 33.547  70.792  4.021   1.00 11.33 ?  24  TYR H CA    1 
ATOM   5077  C  C     . TYR E 1 24  ? 33.564  71.090  2.523   1.00 11.41 ?  24  TYR H C     1 
ATOM   5078  O  O     . TYR E 1 24  ? 34.586  71.510  1.985   1.00 12.53 ?  24  TYR H O     1 
ATOM   5079  C  CB    . TYR E 1 24  ? 33.669  69.287  4.277   1.00 10.58 ?  24  TYR H CB    1 
ATOM   5080  C  CG    . TYR E 1 24  ? 34.439  68.911  5.537   1.00 10.06 ?  24  TYR H CG    1 
ATOM   5081  C  CD1   . TYR E 1 24  ? 35.802  69.160  5.637   1.00 9.27  ?  24  TYR H CD1   1 
ATOM   5082  C  CD2   . TYR E 1 24  ? 33.816  68.279  6.606   1.00 10.90 ?  24  TYR H CD2   1 
ATOM   5083  C  CE1   . TYR E 1 24  ? 36.517  68.815  6.771   1.00 10.16 ?  24  TYR H CE1   1 
ATOM   5084  C  CE2   . TYR E 1 24  ? 34.521  67.925  7.745   1.00 10.54 ?  24  TYR H CE2   1 
ATOM   5085  C  CZ    . TYR E 1 24  ? 35.875  68.194  7.828   1.00 10.71 ?  24  TYR H CZ    1 
ATOM   5086  O  OH    . TYR E 1 24  ? 36.572  67.846  8.950   1.00 13.28 ?  24  TYR H OH    1 
ATOM   5087  N  N     . ILE E 1 25  ? 32.439  70.837  1.849   1.00 12.06 ?  25  ILE H N     1 
ATOM   5088  C  CA    . ILE E 1 25  ? 32.318  71.163  0.438   1.00 14.62 ?  25  ILE H CA    1 
ATOM   5089  C  C     . ILE E 1 25  ? 32.556  72.660  0.267   1.00 17.57 ?  25  ILE H C     1 
ATOM   5090  O  O     . ILE E 1 25  ? 33.350  73.085  -0.569  1.00 17.74 ?  25  ILE H O     1 
ATOM   5091  C  CB    . ILE E 1 25  ? 30.943  70.748  -0.115  1.00 14.99 ?  25  ILE H CB    1 
ATOM   5092  C  CG1   . ILE E 1 25  ? 30.814  69.234  -0.236  1.00 13.62 ?  25  ILE H CG1   1 
ATOM   5093  C  CG2   . ILE E 1 25  ? 30.664  71.440  -1.450  1.00 15.26 ?  25  ILE H CG2   1 
ATOM   5094  C  CD1   . ILE E 1 25  ? 29.409  68.765  -0.569  1.00 13.39 ?  25  ILE H CD1   1 
ATOM   5095  N  N     . GLU E 1 26  ? 31.855  73.448  1.085   1.00 22.87 ?  26  GLU H N     1 
ATOM   5096  C  CA    . GLU E 1 26  ? 31.886  74.896  0.976   1.00 25.06 ?  26  GLU H CA    1 
ATOM   5097  C  C     . GLU E 1 26  ? 33.322  75.407  1.101   1.00 25.60 ?  26  GLU H C     1 
ATOM   5098  O  O     . GLU E 1 26  ? 33.708  76.325  0.382   1.00 23.91 ?  26  GLU H O     1 
ATOM   5099  C  CB    . GLU E 1 26  ? 30.907  75.471  2.002   1.00 27.14 ?  26  GLU H CB    1 
ATOM   5100  C  CG    . GLU E 1 26  ? 31.098  76.959  2.278   1.00 33.34 ?  26  GLU H CG    1 
ATOM   5101  C  CD    . GLU E 1 26  ? 30.051  77.554  3.205   1.00 36.88 ?  26  GLU H CD    1 
ATOM   5102  O  OE1   . GLU E 1 26  ? 29.052  76.862  3.498   1.00 41.04 ?  26  GLU H OE1   1 
ATOM   5103  O  OE2   . GLU E 1 26  ? 30.242  78.708  3.644   1.00 42.12 -1 26  GLU H OE2   1 
ATOM   5104  N  N     . HIS E 1 27  ? 34.120  74.806  1.995   1.00 28.65 ?  27  HIS H N     1 
ATOM   5105  C  CA    . HIS E 1 27  ? 35.457  75.315  2.277   1.00 31.62 ?  27  HIS H CA    1 
ATOM   5106  C  C     . HIS E 1 27  ? 36.526  74.674  1.386   1.00 27.37 ?  27  HIS H C     1 
ATOM   5107  O  O     . HIS E 1 27  ? 37.670  75.122  1.390   1.00 26.03 ?  27  HIS H O     1 
ATOM   5108  C  CB    . HIS E 1 27  ? 35.792  75.185  3.769   1.00 35.32 ?  27  HIS H CB    1 
ATOM   5109  C  CG    . HIS E 1 27  ? 35.097  76.199  4.616   1.00 36.21 ?  27  HIS H CG    1 
ATOM   5110  N  ND1   . HIS E 1 27  ? 33.969  75.924  5.359   1.00 38.31 ?  27  HIS H ND1   1 
ATOM   5111  C  CD2   . HIS E 1 27  ? 35.375  77.492  4.833   1.00 33.46 ?  27  HIS H CD2   1 
ATOM   5112  C  CE1   . HIS E 1 27  ? 33.587  77.021  5.997   1.00 33.97 ?  27  HIS H CE1   1 
ATOM   5113  N  NE2   . HIS E 1 27  ? 34.427  77.986  5.691   1.00 32.18 ?  27  HIS H NE2   1 
ATOM   5114  N  N     . ALA E 1 28  ? 36.153  73.648  0.610   1.00 24.05 ?  28  ALA H N     1 
ATOM   5115  C  CA    . ALA E 1 28  ? 37.094  72.900  -0.215  1.00 24.30 ?  28  ALA H CA    1 
ATOM   5116  C  C     . ALA E 1 28  ? 37.821  73.803  -1.211  1.00 24.77 ?  28  ALA H C     1 
ATOM   5117  O  O     . ALA E 1 28  ? 37.301  74.838  -1.619  1.00 27.07 ?  28  ALA H O     1 
ATOM   5118  C  CB    . ALA E 1 28  ? 36.363  71.794  -0.947  1.00 22.36 ?  28  ALA H CB    1 
ATOM   5119  N  N     . ASP E 1 29  ? 39.029  73.371  -1.604  1.00 27.17 ?  29  ASP H N     1 
ATOM   5120  C  CA    . ASP E 1 29  ? 39.757  73.951  -2.723  1.00 30.12 ?  29  ASP H CA    1 
ATOM   5121  C  C     . ASP E 1 29  ? 39.180  73.413  -4.028  1.00 26.66 ?  29  ASP H C     1 
ATOM   5122  O  O     . ASP E 1 29  ? 39.084  74.134  -5.018  1.00 28.33 ?  29  ASP H O     1 
ATOM   5123  C  CB    . ASP E 1 29  ? 41.237  73.600  -2.687  1.00 28.59 ?  29  ASP H CB    1 
ATOM   5124  C  CG    . ASP E 1 29  ? 42.091  74.378  -1.696  1.00 33.50 ?  29  ASP H CG    1 
ATOM   5125  O  OD1   . ASP E 1 29  ? 41.644  75.457  -1.254  1.00 31.70 ?  29  ASP H OD1   1 
ATOM   5126  O  OD2   . ASP E 1 29  ? 43.194  73.890  -1.366  1.00 41.60 -1 29  ASP H OD2   1 
ATOM   5127  N  N     . ILE E 1 30  ? 38.821  72.126  -4.012  1.00 29.28 ?  30  ILE H N     1 
ATOM   5128  C  CA    . ILE E 1 30  ? 38.321  71.448  -5.195  1.00 26.74 ?  30  ILE H CA    1 
ATOM   5129  C  C     . ILE E 1 30  ? 37.407  70.315  -4.740  1.00 23.89 ?  30  ILE H C     1 
ATOM   5130  O  O     . ILE E 1 30  ? 37.642  69.714  -3.693  1.00 25.57 ?  30  ILE H O     1 
ATOM   5131  C  CB    . ILE E 1 30  ? 39.494  70.955  -6.066  1.00 29.16 ?  30  ILE H CB    1 
ATOM   5132  C  CG1   . ILE E 1 30  ? 39.030  70.472  -7.439  1.00 30.19 ?  30  ILE H CG1   1 
ATOM   5133  C  CG2   . ILE E 1 30  ? 40.313  69.888  -5.339  1.00 27.74 ?  30  ILE H CG2   1 
ATOM   5134  C  CD1   . ILE E 1 30  ? 40.148  70.379  -8.462  1.00 31.07 ?  30  ILE H CD1   1 
ATOM   5135  N  N     . VAL E 1 31  ? 36.352  70.049  -5.518  1.00 19.49 ?  31  VAL H N     1 
ATOM   5136  C  CA    . VAL E 1 31  ? 35.427  68.979  -5.189  1.00 18.69 ?  31  VAL H CA    1 
ATOM   5137  C  C     . VAL E 1 31  ? 35.298  68.039  -6.384  1.00 19.12 ?  31  VAL H C     1 
ATOM   5138  O  O     . VAL E 1 31  ? 35.178  68.474  -7.528  1.00 14.24 ?  31  VAL H O     1 
ATOM   5139  C  CB    . VAL E 1 31  ? 34.045  69.496  -4.744  1.00 18.09 ?  31  VAL H CB    1 
ATOM   5140  C  CG1   . VAL E 1 31  ? 33.171  68.369  -4.203  1.00 16.93 ?  31  VAL H CG1   1 
ATOM   5141  C  CG2   . VAL E 1 31  ? 34.173  70.610  -3.713  1.00 15.33 ?  31  VAL H CG2   1 
ATOM   5142  N  N     . PHE E 1 32  ? 35.341  66.739  -6.080  1.00 20.10 ?  32  PHE H N     1 
ATOM   5143  C  CA    . PHE E 1 32  ? 35.065  65.691  -7.046  1.00 18.87 ?  32  PHE H CA    1 
ATOM   5144  C  C     . PHE E 1 32  ? 33.699  65.094  -6.718  1.00 16.20 ?  32  PHE H C     1 
ATOM   5145  O  O     . PHE E 1 32  ? 33.495  64.553  -5.633  1.00 18.27 ?  32  PHE H O     1 
ATOM   5146  C  CB    . PHE E 1 32  ? 36.247  64.717  -7.010  1.00 18.65 ?  32  PHE H CB    1 
ATOM   5147  C  CG    . PHE E 1 32  ? 37.524  65.325  -7.574  1.00 20.47 ?  32  PHE H CG    1 
ATOM   5148  C  CD1   . PHE E 1 32  ? 38.287  66.209  -6.820  1.00 21.03 ?  32  PHE H CD1   1 
ATOM   5149  C  CD2   . PHE E 1 32  ? 37.949  65.025  -8.863  1.00 22.00 ?  32  PHE H CD2   1 
ATOM   5150  C  CE1   . PHE E 1 32  ? 39.442  66.772  -7.340  1.00 22.76 ?  32  PHE H CE1   1 
ATOM   5151  C  CE2   . PHE E 1 32  ? 39.106  65.589  -9.378  1.00 21.03 ?  32  PHE H CE2   1 
ATOM   5152  C  CZ    . PHE E 1 32  ? 39.849  66.460  -8.616  1.00 22.44 ?  32  PHE H CZ    1 
ATOM   5153  N  N     . SER E 1 33  ? 32.772  65.223  -7.672  1.00 15.23 ?  33  SER H N     1 
ATOM   5154  C  CA    . SER E 1 33  ? 31.371  64.893  -7.468  1.00 14.69 ?  33  SER H CA    1 
ATOM   5155  C  C     . SER E 1 33  ? 31.010  63.578  -8.154  1.00 16.08 ?  33  SER H C     1 
ATOM   5156  O  O     . SER E 1 33  ? 31.527  63.263  -9.225  1.00 16.50 ?  33  SER H O     1 
ATOM   5157  C  CB    . SER E 1 33  ? 30.490  66.001  -7.988  1.00 12.95 ?  33  SER H CB    1 
ATOM   5158  O  OG    . SER E 1 33  ? 30.629  66.133  -9.397  1.00 12.48 ?  33  SER H OG    1 
ATOM   5159  N  N     . LEU E 1 34  ? 30.097  62.832  -7.521  1.00 18.39 ?  34  LEU H N     1 
ATOM   5160  C  CA    . LEU E 1 34  ? 29.385  61.741  -8.166  1.00 21.25 ?  34  LEU H CA    1 
ATOM   5161  C  C     . LEU E 1 34  ? 27.944  61.751  -7.656  1.00 22.47 ?  34  LEU H C     1 
ATOM   5162  O  O     . LEU E 1 34  ? 27.641  61.164  -6.619  1.00 23.75 ?  34  LEU H O     1 
ATOM   5163  C  CB    . LEU E 1 34  ? 30.091  60.415  -7.885  1.00 22.15 ?  34  LEU H CB    1 
ATOM   5164  C  CG    . LEU E 1 34  ? 29.846  59.285  -8.892  1.00 22.07 ?  34  LEU H CG    1 
ATOM   5165  C  CD1   . LEU E 1 34  ? 30.233  59.671  -10.311 1.00 21.20 ?  34  LEU H CD1   1 
ATOM   5166  C  CD2   . LEU E 1 34  ? 30.615  58.051  -8.457  1.00 24.28 ?  34  LEU H CD2   1 
ATOM   5167  N  N     . LEU E 1 35  ? 27.065  62.437  -8.397  1.00 26.03 ?  35  LEU H N     1 
ATOM   5168  C  CA    . LEU E 1 35  ? 25.746  62.804  -7.902  1.00 26.79 ?  35  LEU H CA    1 
ATOM   5169  C  C     . LEU E 1 35  ? 24.662  62.222  -8.806  1.00 26.14 ?  35  LEU H C     1 
ATOM   5170  O  O     . LEU E 1 35  ? 24.907  61.971  -9.984  1.00 29.44 ?  35  LEU H O     1 
ATOM   5171  C  CB    . LEU E 1 35  ? 25.674  64.329  -7.844  1.00 28.74 ?  35  LEU H CB    1 
ATOM   5172  C  CG    . LEU E 1 35  ? 26.691  65.010  -6.924  1.00 30.77 ?  35  LEU H CG    1 
ATOM   5173  C  CD1   . LEU E 1 35  ? 26.581  66.516  -7.050  1.00 30.83 ?  35  LEU H CD1   1 
ATOM   5174  C  CD2   . LEU E 1 35  ? 26.513  64.575  -5.477  1.00 31.75 ?  35  LEU H CD2   1 
ATOM   5175  N  N     . PRO E 1 36  ? 23.431  61.995  -8.287  1.00 23.93 ?  36  PRO H N     1 
ATOM   5176  C  CA    . PRO E 1 36  ? 22.384  61.319  -9.057  1.00 24.68 ?  36  PRO H CA    1 
ATOM   5177  C  C     . PRO E 1 36  ? 21.891  62.018  -10.326 1.00 25.04 ?  36  PRO H C     1 
ATOM   5178  O  O     . PRO E 1 36  ? 21.405  61.348  -11.234 1.00 27.28 ?  36  PRO H O     1 
ATOM   5179  C  CB    . PRO E 1 36  ? 21.236  61.150  -8.033  1.00 23.95 ?  36  PRO H CB    1 
ATOM   5180  C  CG    . PRO E 1 36  ? 21.890  61.318  -6.680  1.00 24.12 ?  36  PRO H CG    1 
ATOM   5181  C  CD    . PRO E 1 36  ? 23.006  62.320  -6.917  1.00 25.53 ?  36  PRO H CD    1 
ATOM   5182  N  N     . ASP E 1 37  ? 22.000  63.351  -10.397 1.00 27.13 ?  37  ASP H N     1 
ATOM   5183  C  CA    . ASP E 1 37  ? 21.348  64.081  -11.474 1.00 26.60 ?  37  ASP H CA    1 
ATOM   5184  C  C     . ASP E 1 37  ? 21.910  65.495  -11.616 1.00 26.10 ?  37  ASP H C     1 
ATOM   5185  O  O     . ASP E 1 37  ? 22.870  65.865  -10.943 1.00 28.01 ?  37  ASP H O     1 
ATOM   5186  C  CB    . ASP E 1 37  ? 19.842  64.099  -11.264 1.00 26.73 ?  37  ASP H CB    1 
ATOM   5187  C  CG    . ASP E 1 37  ? 19.388  64.637  -9.915  1.00 26.10 ?  37  ASP H CG    1 
ATOM   5188  O  OD1   . ASP E 1 37  ? 19.562  65.852  -9.682  1.00 24.70 ?  37  ASP H OD1   1 
ATOM   5189  O  OD2   . ASP E 1 37  ? 18.880  63.833  -9.105  1.00 24.89 -1 37  ASP H OD2   1 
ATOM   5190  N  N     . GLY E 1 38  ? 21.282  66.271  -12.510 1.00 22.80 ?  38  GLY H N     1 
ATOM   5191  C  CA    . GLY E 1 38  ? 21.745  67.600  -12.879 1.00 21.20 ?  38  GLY H CA    1 
ATOM   5192  C  C     . GLY E 1 38  ? 21.271  68.679  -11.906 1.00 20.24 ?  38  GLY H C     1 
ATOM   5193  O  O     . GLY E 1 38  ? 21.806  69.786  -11.907 1.00 17.89 ?  38  GLY H O     1 
ATOM   5194  N  N     . PHE E 1 39  ? 20.263  68.353  -11.087 1.00 20.68 ?  39  PHE H N     1 
ATOM   5195  C  CA    . PHE E 1 39  ? 19.774  69.261  -10.060 1.00 21.92 ?  39  PHE H CA    1 
ATOM   5196  C  C     . PHE E 1 39  ? 20.725  69.230  -8.868  1.00 22.88 ?  39  PHE H C     1 
ATOM   5197  O  O     . PHE E 1 39  ? 21.051  70.267  -8.295  1.00 23.71 ?  39  PHE H O     1 
ATOM   5198  C  CB    . PHE E 1 39  ? 18.377  68.897  -9.548  1.00 21.09 ?  39  PHE H CB    1 
ATOM   5199  C  CG    . PHE E 1 39  ? 17.252  69.009  -10.567 1.00 21.83 ?  39  PHE H CG    1 
ATOM   5200  C  CD1   . PHE E 1 39  ? 16.770  70.252  -10.962 1.00 18.80 ?  39  PHE H CD1   1 
ATOM   5201  C  CD2   . PHE E 1 39  ? 16.654  67.872  -11.098 1.00 22.75 ?  39  PHE H CD2   1 
ATOM   5202  C  CE1   . PHE E 1 39  ? 15.741  70.352  -11.883 1.00 18.47 ?  39  PHE H CE1   1 
ATOM   5203  C  CE2   . PHE E 1 39  ? 15.620  67.978  -12.015 1.00 20.84 ?  39  PHE H CE2   1 
ATOM   5204  C  CZ    . PHE E 1 39  ? 15.168  69.216  -12.407 1.00 18.44 ?  39  PHE H CZ    1 
ATOM   5205  N  N     . SER E 1 40  ? 21.141  68.016  -8.494  1.00 22.69 ?  40  SER H N     1 
ATOM   5206  C  CA    . SER E 1 40  ? 22.072  67.820  -7.397  1.00 24.16 ?  40  SER H CA    1 
ATOM   5207  C  C     . SER E 1 40  ? 23.450  68.343  -7.794  1.00 22.13 ?  40  SER H C     1 
ATOM   5208  O  O     . SER E 1 40  ? 24.294  68.580  -6.935  1.00 24.09 ?  40  SER H O     1 
ATOM   5209  C  CB    . SER E 1 40  ? 22.131  66.369  -6.990  1.00 26.15 ?  40  SER H CB    1 
ATOM   5210  O  OG    . SER E 1 40  ? 22.980  66.185  -5.865  1.00 34.46 ?  40  SER H OG    1 
ATOM   5211  N  N     . GLN E 1 41  ? 23.657  68.527  -9.104  1.00 24.46 ?  41  GLN H N     1 
ATOM   5212  C  CA    . GLN E 1 41  ? 24.939  68.958  -9.638  1.00 25.18 ?  41  GLN H CA    1 
ATOM   5213  C  C     . GLN E 1 41  ? 24.986  70.484  -9.675  1.00 22.89 ?  41  GLN H C     1 
ATOM   5214  O  O     . GLN E 1 41  ? 26.051  71.080  -9.522  1.00 24.04 ?  41  GLN H O     1 
ATOM   5215  C  CB    . GLN E 1 41  ? 25.154  68.384  -11.040 1.00 24.85 ?  41  GLN H CB    1 
ATOM   5216  C  CG    . GLN E 1 41  ? 26.612  68.357  -11.488 1.00 24.78 ?  41  GLN H CG    1 
ATOM   5217  C  CD    . GLN E 1 41  ? 27.466  67.432  -10.650 1.00 27.18 ?  41  GLN H CD    1 
ATOM   5218  O  OE1   . GLN E 1 41  ? 27.021  66.361  -10.224 1.00 32.55 ?  41  GLN H OE1   1 
ATOM   5219  N  NE2   . GLN E 1 41  ? 28.700  67.842  -10.391 1.00 25.59 ?  41  GLN H NE2   1 
ATOM   5220  N  N     . ARG E 1 42  ? 23.816  71.096  -9.894  1.00 22.08 ?  42  ARG H N     1 
ATOM   5221  C  CA    . ARG E 1 42  ? 23.669  72.543  -9.889  1.00 19.51 ?  42  ARG H CA    1 
ATOM   5222  C  C     . ARG E 1 42  ? 23.819  73.071  -8.463  1.00 18.75 ?  42  ARG H C     1 
ATOM   5223  O  O     . ARG E 1 42  ? 24.495  74.071  -8.235  1.00 18.43 ?  42  ARG H O     1 
ATOM   5224  C  CB    . ARG E 1 42  ? 22.315  72.964  -10.477 1.00 20.68 ?  42  ARG H CB    1 
ATOM   5225  C  CG    . ARG E 1 42  ? 22.220  72.983  -11.997 1.00 22.89 ?  42  ARG H CG    1 
ATOM   5226  C  CD    . ARG E 1 42  ? 20.837  73.446  -12.450 1.00 22.93 ?  42  ARG H CD    1 
ATOM   5227  N  NE    . ARG E 1 42  ? 20.650  73.543  -13.903 1.00 23.19 ?  42  ARG H NE    1 
ATOM   5228  C  CZ    . ARG E 1 42  ? 19.888  72.729  -14.630 1.00 30.96 ?  42  ARG H CZ    1 
ATOM   5229  N  NH1   . ARG E 1 42  ? 19.414  71.610  -14.109 1.00 25.66 1  42  ARG H NH1   1 
ATOM   5230  N  NH2   . ARG E 1 42  ? 19.635  73.020  -15.895 1.00 33.62 ?  42  ARG H NH2   1 
ATOM   5231  N  N     . TRP E 1 43  ? 23.164  72.399  -7.510  1.00 18.03 ?  43  TRP H N     1 
ATOM   5232  C  CA    . TRP E 1 43  ? 23.295  72.728  -6.099  1.00 16.20 ?  43  TRP H CA    1 
ATOM   5233  C  C     . TRP E 1 43  ? 24.763  72.676  -5.670  1.00 17.37 ?  43  TRP H C     1 
ATOM   5234  O  O     . TRP E 1 43  ? 25.245  73.603  -5.024  1.00 13.23 ?  43  TRP H O     1 
ATOM   5235  C  CB    . TRP E 1 43  ? 22.407  71.794  -5.263  1.00 15.52 ?  43  TRP H CB    1 
ATOM   5236  C  CG    . TRP E 1 43  ? 22.807  71.637  -3.819  1.00 15.08 ?  43  TRP H CG    1 
ATOM   5237  C  CD1   . TRP E 1 43  ? 22.418  72.402  -2.760  1.00 15.85 ?  43  TRP H CD1   1 
ATOM   5238  C  CD2   . TRP E 1 43  ? 23.651  70.599  -3.273  1.00 19.81 ?  43  TRP H CD2   1 
ATOM   5239  N  NE1   . TRP E 1 43  ? 22.975  71.931  -1.601  1.00 17.20 ?  43  TRP H NE1   1 
ATOM   5240  C  CE2   . TRP E 1 43  ? 23.732  70.823  -1.882  1.00 20.90 ?  43  TRP H CE2   1 
ATOM   5241  C  CE3   . TRP E 1 43  ? 24.344  69.516  -3.823  1.00 21.20 ?  43  TRP H CE3   1 
ATOM   5242  C  CZ2   . TRP E 1 43  ? 24.479  70.003  -1.040  1.00 23.10 ?  43  TRP H CZ2   1 
ATOM   5243  C  CZ3   . TRP E 1 43  ? 25.079  68.704  -2.988  1.00 24.65 ?  43  TRP H CZ3   1 
ATOM   5244  C  CH2   . TRP E 1 43  ? 25.144  68.945  -1.617  1.00 25.04 ?  43  TRP H CH2   1 
ATOM   5245  N  N     . LEU E 1 44  ? 25.481  71.606  -6.041  1.00 20.99 ?  44  LEU H N     1 
ATOM   5246  C  CA    . LEU E 1 44  ? 26.872  71.457  -5.631  1.00 21.46 ?  44  LEU H CA    1 
ATOM   5247  C  C     . LEU E 1 44  ? 27.676  72.647  -6.150  1.00 23.28 ?  44  LEU H C     1 
ATOM   5248  O  O     . LEU E 1 44  ? 28.458  73.246  -5.413  1.00 24.51 ?  44  LEU H O     1 
ATOM   5249  C  CB    . LEU E 1 44  ? 27.481  70.135  -6.104  1.00 21.87 ?  44  LEU H CB    1 
ATOM   5250  C  CG    . LEU E 1 44  ? 28.960  69.914  -5.759  1.00 18.90 ?  44  LEU H CG    1 
ATOM   5251  C  CD1   . LEU E 1 44  ? 29.253  70.312  -4.325  1.00 18.48 ?  44  LEU H CD1   1 
ATOM   5252  C  CD2   . LEU E 1 44  ? 29.391  68.471  -5.984  1.00 17.50 ?  44  LEU H CD2   1 
ATOM   5253  N  N     . THR E 1 45  ? 27.456  72.981  -7.426  1.00 23.10 ?  45  THR H N     1 
ATOM   5254  C  CA    . THR E 1 45  ? 28.229  73.991  -8.131  1.00 25.54 ?  45  THR H CA    1 
ATOM   5255  C  C     . THR E 1 45  ? 28.022  75.364  -7.496  1.00 24.44 ?  45  THR H C     1 
ATOM   5256  O  O     . THR E 1 45  ? 28.887  76.230  -7.602  1.00 21.74 ?  45  THR H O     1 
ATOM   5257  C  CB    . THR E 1 45  ? 27.821  73.982  -9.604  1.00 28.90 ?  45  THR H CB    1 
ATOM   5258  O  OG1   . THR E 1 45  ? 28.243  72.717  -10.105 1.00 31.68 ?  45  THR H OG1   1 
ATOM   5259  C  CG2   . THR E 1 45  ? 28.473  75.093  -10.406 1.00 29.16 ?  45  THR H CG2   1 
ATOM   5260  N  N     . LYS E 1 46  ? 26.868  75.561  -6.848  1.00 26.75 ?  46  LYS H N     1 
ATOM   5261  C  CA    . LYS E 1 46  ? 26.569  76.824  -6.192  1.00 28.49 ?  46  LYS H CA    1 
ATOM   5262  C  C     . LYS E 1 46  ? 27.177  76.831  -4.793  1.00 24.21 ?  46  LYS H C     1 
ATOM   5263  O  O     . LYS E 1 46  ? 27.464  77.890  -4.242  1.00 22.21 ?  46  LYS H O     1 
ATOM   5264  C  CB    . LYS E 1 46  ? 25.059  77.078  -6.120  1.00 33.62 ?  46  LYS H CB    1 
ATOM   5265  C  CG    . LYS E 1 46  ? 24.386  77.306  -7.466  1.00 34.24 ?  46  LYS H CG    1 
ATOM   5266  C  CD    . LYS E 1 46  ? 22.932  77.747  -7.368  1.00 37.72 ?  46  LYS H CD    1 
ATOM   5267  C  CE    . LYS E 1 46  ? 22.795  79.120  -6.788  1.00 40.27 ?  46  LYS H CE    1 
ATOM   5268  N  NZ    . LYS E 1 46  ? 21.431  79.636  -6.929  1.00 41.36 1  46  LYS H NZ    1 
ATOM   5269  N  N     . LEU E 1 47  ? 27.366  75.636  -4.228  1.00 22.10 ?  47  LEU H N     1 
ATOM   5270  C  CA    . LEU E 1 47  ? 27.975  75.500  -2.918  1.00 21.77 ?  47  LEU H CA    1 
ATOM   5271  C  C     . LEU E 1 47  ? 29.473  75.779  -3.034  1.00 20.84 ?  47  LEU H C     1 
ATOM   5272  O  O     . LEU E 1 47  ? 30.057  76.426  -2.168  1.00 21.66 ?  47  LEU H O     1 
ATOM   5273  C  CB    . LEU E 1 47  ? 27.690  74.093  -2.399  1.00 24.80 ?  47  LEU H CB    1 
ATOM   5274  C  CG    . LEU E 1 47  ? 27.228  73.997  -0.943  1.00 26.63 ?  47  LEU H CG    1 
ATOM   5275  C  CD1   . LEU E 1 47  ? 27.109  72.535  -0.558  1.00 26.38 ?  47  LEU H CD1   1 
ATOM   5276  C  CD2   . LEU E 1 47  ? 28.145  74.746  0.008   1.00 27.91 ?  47  LEU H CD2   1 
ATOM   5277  N  N     . ASN E 1 48  ? 30.080  75.291  -4.123  1.00 20.93 ?  48  ASN H N     1 
ATOM   5278  C  CA    . ASN E 1 48  ? 31.492  75.509  -4.402  1.00 18.96 ?  48  ASN H CA    1 
ATOM   5279  C  C     . ASN E 1 48  ? 31.715  75.339  -5.903  1.00 22.24 ?  48  ASN H C     1 
ATOM   5280  O  O     . ASN E 1 48  ? 31.410  74.287  -6.461  1.00 22.55 ?  48  ASN H O     1 
ATOM   5281  C  CB    . ASN E 1 48  ? 32.364  74.590  -3.550  1.00 18.72 ?  48  ASN H CB    1 
ATOM   5282  C  CG    . ASN E 1 48  ? 33.842  74.880  -3.676  1.00 18.24 ?  48  ASN H CG    1 
ATOM   5283  O  OD1   . ASN E 1 48  ? 34.289  75.447  -4.680  1.00 16.99 ?  48  ASN H OD1   1 
ATOM   5284  N  ND2   . ASN E 1 48  ? 34.617  74.476  -2.680  1.00 16.89 ?  48  ASN H ND2   1 
ATOM   5285  N  N     . PRO E 1 49  ? 32.227  76.369  -6.614  1.00 29.43 ?  49  PRO H N     1 
ATOM   5286  C  CA    . PRO E 1 49  ? 32.363  76.296  -8.072  1.00 31.21 ?  49  PRO H CA    1 
ATOM   5287  C  C     . PRO E 1 49  ? 33.496  75.423  -8.611  1.00 33.49 ?  49  PRO H C     1 
ATOM   5288  O  O     . PRO E 1 49  ? 33.423  74.958  -9.747  1.00 30.87 ?  49  PRO H O     1 
ATOM   5289  C  CB    . PRO E 1 49  ? 32.551  77.777  -8.430  1.00 29.80 ?  49  PRO H CB    1 
ATOM   5290  C  CG    . PRO E 1 49  ? 33.320  78.331  -7.255  1.00 29.56 ?  49  PRO H CG    1 
ATOM   5291  C  CD    . PRO E 1 49  ? 32.665  77.662  -6.058  1.00 28.14 ?  49  PRO H CD    1 
ATOM   5292  N  N     . ASN E 1 50  ? 34.542  75.200  -7.805  1.00 32.98 ?  50  ASN H N     1 
ATOM   5293  C  CA    . ASN E 1 50  ? 35.653  74.363  -8.234  1.00 32.61 ?  50  ASN H CA    1 
ATOM   5294  C  C     . ASN E 1 50  ? 35.275  72.894  -8.058  1.00 27.91 ?  50  ASN H C     1 
ATOM   5295  O  O     . ASN E 1 50  ? 35.695  72.253  -7.098  1.00 22.30 ?  50  ASN H O     1 
ATOM   5296  C  CB    . ASN E 1 50  ? 36.948  74.689  -7.496  1.00 35.87 ?  50  ASN H CB    1 
ATOM   5297  C  CG    . ASN E 1 50  ? 38.157  74.153  -8.226  1.00 31.62 ?  50  ASN H CG    1 
ATOM   5298  O  OD1   . ASN E 1 50  ? 38.020  73.560  -9.302  1.00 37.70 ?  50  ASN H OD1   1 
ATOM   5299  N  ND2   . ASN E 1 50  ? 39.343  74.355  -7.671  1.00 28.87 ?  50  ASN H ND2   1 
ATOM   5300  N  N     . VAL E 1 51  ? 34.479  72.377  -9.002  1.00 26.96 ?  51  VAL H N     1 
ATOM   5301  C  CA    . VAL E 1 51  ? 34.024  70.997  -8.977  1.00 24.01 ?  51  VAL H CA    1 
ATOM   5302  C  C     . VAL E 1 51  ? 34.528  70.289  -10.231 1.00 23.67 ?  51  VAL H C     1 
ATOM   5303  O  O     . VAL E 1 51  ? 34.483  70.847  -11.325 1.00 26.90 ?  51  VAL H O     1 
ATOM   5304  C  CB    . VAL E 1 51  ? 32.489  70.879  -8.899  1.00 27.21 ?  51  VAL H CB    1 
ATOM   5305  C  CG1   . VAL E 1 51  ? 32.021  69.451  -9.164  1.00 25.82 ?  51  VAL H CG1   1 
ATOM   5306  C  CG2   . VAL E 1 51  ? 31.931  71.395  -7.578  1.00 24.33 ?  51  VAL H CG2   1 
ATOM   5307  N  N     . ILE E 1 52  ? 34.991  69.049  -10.052 1.00 22.05 ?  52  ILE H N     1 
ATOM   5308  C  CA    . ILE E 1 52  ? 35.259  68.151  -11.163 1.00 24.47 ?  52  ILE H CA    1 
ATOM   5309  C  C     . ILE E 1 52  ? 34.335  66.941  -11.034 1.00 21.09 ?  52  ILE H C     1 
ATOM   5310  O  O     . ILE E 1 52  ? 34.316  66.279  -9.999  1.00 22.02 ?  52  ILE H O     1 
ATOM   5311  C  CB    . ILE E 1 52  ? 36.746  67.753  -11.197 1.00 26.82 ?  52  ILE H CB    1 
ATOM   5312  C  CG1   . ILE E 1 52  ? 37.631  68.948  -11.561 1.00 24.46 ?  52  ILE H CG1   1 
ATOM   5313  C  CG2   . ILE E 1 52  ? 36.968  66.569  -12.139 1.00 27.27 ?  52  ILE H CG2   1 
ATOM   5314  C  CD1   . ILE E 1 52  ? 39.121  68.666  -11.495 1.00 29.84 ?  52  ILE H CD1   1 
ATOM   5315  N  N     . ASN E 1 53  ? 33.564  66.670  -12.093 1.00 19.94 ?  53  ASN H N     1 
ATOM   5316  C  CA    . ASN E 1 53  ? 32.526  65.651  -12.068 1.00 20.89 ?  53  ASN H CA    1 
ATOM   5317  C  C     . ASN E 1 53  ? 33.108  64.296  -12.476 1.00 19.63 ?  53  ASN H C     1 
ATOM   5318  O  O     . ASN E 1 53  ? 33.630  64.151  -13.579 1.00 19.45 ?  53  ASN H O     1 
ATOM   5319  C  CB    . ASN E 1 53  ? 31.356  66.065  -12.956 1.00 20.48 ?  53  ASN H CB    1 
ATOM   5320  C  CG    . ASN E 1 53  ? 30.163  65.151  -12.818 1.00 24.11 ?  53  ASN H CG    1 
ATOM   5321  O  OD1   . ASN E 1 53  ? 30.255  64.092  -12.186 1.00 24.15 ?  53  ASN H OD1   1 
ATOM   5322  N  ND2   . ASN E 1 53  ? 29.039  65.537  -13.404 1.00 25.93 ?  53  ASN H ND2   1 
ATOM   5323  N  N     . LEU E 1 54  ? 32.978  63.302  -11.585 1.00 19.18 ?  54  LEU H N     1 
ATOM   5324  C  CA    . LEU E 1 54  ? 33.569  61.983  -11.777 1.00 20.20 ?  54  LEU H CA    1 
ATOM   5325  C  C     . LEU E 1 54  ? 32.738  61.141  -12.746 1.00 22.07 ?  54  LEU H C     1 
ATOM   5326  O  O     . LEU E 1 54  ? 33.184  60.084  -13.189 1.00 20.30 ?  54  LEU H O     1 
ATOM   5327  C  CB    . LEU E 1 54  ? 33.710  61.272  -10.430 1.00 18.46 ?  54  LEU H CB    1 
ATOM   5328  C  CG    . LEU E 1 54  ? 34.677  61.907  -9.424  1.00 18.06 ?  54  LEU H CG    1 
ATOM   5329  C  CD1   . LEU E 1 54  ? 34.619  61.215  -8.070  1.00 15.90 ?  54  LEU H CD1   1 
ATOM   5330  C  CD2   . LEU E 1 54  ? 36.094  61.889  -9.965  1.00 17.16 ?  54  LEU H CD2   1 
ATOM   5331  N  N     . GLN E 1 55  ? 31.525  61.599  -13.066 1.00 24.25 ?  55  GLN H N     1 
ATOM   5332  C  CA    . GLN E 1 55  ? 30.645  60.862  -13.958 1.00 26.66 ?  55  GLN H CA    1 
ATOM   5333  C  C     . GLN E 1 55  ? 31.357  60.645  -15.296 1.00 25.31 ?  55  GLN H C     1 
ATOM   5334  O  O     . GLN E 1 55  ? 31.097  59.664  -15.990 1.00 20.62 ?  55  GLN H O     1 
ATOM   5335  C  CB    . GLN E 1 55  ? 29.327  61.632  -14.071 1.00 23.89 ?  55  GLN H CB    1 
ATOM   5336  C  CG    . GLN E 1 55  ? 28.117  60.798  -14.487 1.00 25.10 ?  55  GLN H CG    1 
ATOM   5337  C  CD    . GLN E 1 55  ? 27.512  59.998  -13.352 1.00 28.36 ?  55  GLN H CD    1 
ATOM   5338  O  OE1   . GLN E 1 55  ? 27.293  60.506  -12.247 1.00 33.89 ?  55  GLN H OE1   1 
ATOM   5339  N  NE2   . GLN E 1 55  ? 27.231  58.730  -13.617 1.00 25.68 ?  55  GLN H NE2   1 
ATOM   5340  N  N     . GLN E 1 56  ? 32.281  61.556  -15.634 1.00 24.77 ?  56  GLN H N     1 
ATOM   5341  C  CA    . GLN E 1 56  ? 32.914  61.579  -16.945 1.00 30.23 ?  56  GLN H CA    1 
ATOM   5342  C  C     . GLN E 1 56  ? 33.745  60.321  -17.196 1.00 33.96 ?  56  GLN H C     1 
ATOM   5343  O  O     . GLN E 1 56  ? 33.982  59.971  -18.351 1.00 29.98 ?  56  GLN H O     1 
ATOM   5344  C  CB    . GLN E 1 56  ? 33.839  62.782  -17.133 1.00 33.48 ?  56  GLN H CB    1 
ATOM   5345  C  CG    . GLN E 1 56  ? 35.048  62.795  -16.202 1.00 34.50 ?  56  GLN H CG    1 
ATOM   5346  C  CD    . GLN E 1 56  ? 36.265  63.444  -16.823 1.00 40.57 ?  56  GLN H CD    1 
ATOM   5347  O  OE1   . GLN E 1 56  ? 36.650  64.566  -16.474 1.00 47.41 ?  56  GLN H OE1   1 
ATOM   5348  N  NE2   . GLN E 1 56  ? 36.880  62.743  -17.766 1.00 40.82 ?  56  GLN H NE2   1 
ATOM   5349  N  N     . PHE E 1 57  ? 34.195  59.654  -16.124 1.00 36.95 ?  57  PHE H N     1 
ATOM   5350  C  CA    . PHE E 1 57  ? 35.131  58.544  -16.248 1.00 39.52 ?  57  PHE H CA    1 
ATOM   5351  C  C     . PHE E 1 57  ? 34.386  57.222  -16.435 1.00 38.65 ?  57  PHE H C     1 
ATOM   5352  O  O     . PHE E 1 57  ? 35.017  56.192  -16.660 1.00 37.61 ?  57  PHE H O     1 
ATOM   5353  C  CB    . PHE E 1 57  ? 36.072  58.462  -15.041 1.00 41.21 ?  57  PHE H CB    1 
ATOM   5354  C  CG    . PHE E 1 57  ? 37.079  59.602  -14.959 1.00 42.86 ?  57  PHE H CG    1 
ATOM   5355  C  CD1   . PHE E 1 57  ? 38.301  59.528  -15.617 1.00 43.63 ?  57  PHE H CD1   1 
ATOM   5356  C  CD2   . PHE E 1 57  ? 36.794  60.751  -14.229 1.00 45.98 ?  57  PHE H CD2   1 
ATOM   5357  C  CE1   . PHE E 1 57  ? 39.210  60.572  -15.544 1.00 44.15 ?  57  PHE H CE1   1 
ATOM   5358  C  CE2   . PHE E 1 57  ? 37.706  61.792  -14.160 1.00 41.42 ?  57  PHE H CE2   1 
ATOM   5359  C  CZ    . PHE E 1 57  ? 38.911  61.700  -14.816 1.00 44.80 ?  57  PHE H CZ    1 
ATOM   5360  N  N     . TYR E 1 58  ? 33.052  57.247  -16.339 1.00 35.45 ?  58  TYR H N     1 
ATOM   5361  C  CA    . TYR E 1 58  ? 32.258  56.062  -16.630 1.00 39.03 ?  58  TYR H CA    1 
ATOM   5362  C  C     . TYR E 1 58  ? 32.280  55.819  -18.137 1.00 40.12 ?  58  TYR H C     1 
ATOM   5363  O  O     . TYR E 1 58  ? 32.600  56.723  -18.906 1.00 40.47 ?  58  TYR H O     1 
ATOM   5364  C  CB    . TYR E 1 58  ? 30.800  56.159  -16.167 1.00 39.25 ?  58  TYR H CB    1 
ATOM   5365  C  CG    . TYR E 1 58  ? 30.532  55.782  -14.715 1.00 41.12 ?  58  TYR H CG    1 
ATOM   5366  C  CD1   . TYR E 1 58  ? 30.536  54.453  -14.306 1.00 39.64 ?  58  TYR H CD1   1 
ATOM   5367  C  CD2   . TYR E 1 58  ? 30.227  56.749  -13.766 1.00 40.91 ?  58  TYR H CD2   1 
ATOM   5368  C  CE1   . TYR E 1 58  ? 30.278  54.101  -12.992 1.00 39.95 ?  58  TYR H CE1   1 
ATOM   5369  C  CE2   . TYR E 1 58  ? 29.965  56.410  -12.449 1.00 39.52 ?  58  TYR H CE2   1 
ATOM   5370  C  CZ    . TYR E 1 58  ? 29.990  55.082  -12.061 1.00 37.80 ?  58  TYR H CZ    1 
ATOM   5371  O  OH    . TYR E 1 58  ? 29.733  54.735  -10.766 1.00 43.72 ?  58  TYR H OH    1 
ATOM   5372  N  N     . ALA E 1 59  ? 31.929  54.595  -18.547 1.00 42.59 ?  59  ALA H N     1 
ATOM   5373  C  CA    . ALA E 1 59  ? 31.888  54.246  -19.958 1.00 45.13 ?  59  ALA H CA    1 
ATOM   5374  C  C     . ALA E 1 59  ? 31.061  55.282  -20.715 1.00 39.98 ?  59  ALA H C     1 
ATOM   5375  O  O     . ALA E 1 59  ? 29.944  55.602  -20.315 1.00 42.28 ?  59  ALA H O     1 
ATOM   5376  C  CB    . ALA E 1 59  ? 31.332  52.849  -20.139 1.00 48.49 ?  59  ALA H CB    1 
ATOM   5377  N  N     . GLN E 1 60  ? 31.627  55.799  -21.810 1.00 42.12 ?  60  GLN H N     1 
ATOM   5378  C  CA    . GLN E 1 60  ? 30.988  56.845  -22.591 1.00 48.60 ?  60  GLN H CA    1 
ATOM   5379  C  C     . GLN E 1 60  ? 30.702  56.337  -24.005 1.00 49.08 ?  60  GLN H C     1 
ATOM   5380  O  O     . GLN E 1 60  ? 31.554  55.708  -24.628 1.00 43.64 ?  60  GLN H O     1 
ATOM   5381  C  CB    . GLN E 1 60  ? 31.901  58.072  -22.609 1.00 48.46 ?  60  GLN H CB    1 
ATOM   5382  C  CG    . GLN E 1 60  ? 32.313  58.565  -21.225 1.00 45.17 ?  60  GLN H CG    1 
ATOM   5383  C  CD    . GLN E 1 60  ? 31.196  59.264  -20.480 1.00 46.84 ?  60  GLN H CD    1 
ATOM   5384  O  OE1   . GLN E 1 60  ? 30.722  60.332  -20.882 1.00 40.65 ?  60  GLN H OE1   1 
ATOM   5385  N  NE2   . GLN E 1 60  ? 30.768  58.670  -19.376 1.00 47.44 ?  60  GLN H NE2   1 
ATOM   5386  N  N     . ASN E 1 61  ? 29.490  56.620  -24.497 1.00 53.28 ?  61  ASN H N     1 
ATOM   5387  C  CA    . ASN E 1 61  ? 29.104  56.334  -25.871 1.00 52.89 ?  61  ASN H CA    1 
ATOM   5388  C  C     . ASN E 1 61  ? 29.271  54.849  -26.187 1.00 51.15 ?  61  ASN H C     1 
ATOM   5389  O  O     . ASN E 1 61  ? 29.911  54.492  -27.173 1.00 48.39 ?  61  ASN H O     1 
ATOM   5390  C  CB    . ASN E 1 61  ? 29.894  57.178  -26.866 1.00 57.83 ?  61  ASN H CB    1 
ATOM   5391  C  CG    . ASN E 1 61  ? 29.819  58.653  -26.555 1.00 62.60 ?  61  ASN H CG    1 
ATOM   5392  O  OD1   . ASN E 1 61  ? 28.764  59.275  -26.722 1.00 68.38 ?  61  ASN H OD1   1 
ATOM   5393  N  ND2   . ASN E 1 61  ? 30.926  59.232  -26.113 1.00 61.61 ?  61  ASN H ND2   1 
ATOM   5394  N  N     . GLY E 1 62  ? 28.684  53.994  -25.343 1.00 48.98 ?  62  GLY H N     1 
ATOM   5395  C  CA    . GLY E 1 62  ? 28.524  52.581  -25.649 1.00 48.46 ?  62  GLY H CA    1 
ATOM   5396  C  C     . GLY E 1 62  ? 29.855  51.839  -25.747 1.00 46.26 ?  62  GLY H C     1 
ATOM   5397  O  O     . GLY E 1 62  ? 29.945  50.823  -26.433 1.00 49.10 ?  62  GLY H O     1 
ATOM   5398  N  N     . GLU E 1 63  ? 30.881  52.339  -25.051 1.00 45.74 ?  63  GLU H N     1 
ATOM   5399  C  CA    . GLU E 1 63  ? 32.174  51.675  -25.042 1.00 45.89 ?  63  GLU H CA    1 
ATOM   5400  C  C     . GLU E 1 63  ? 32.172  50.610  -23.950 1.00 37.71 ?  63  GLU H C     1 
ATOM   5401  O  O     . GLU E 1 63  ? 31.590  50.808  -22.886 1.00 35.86 ?  63  GLU H O     1 
ATOM   5402  C  CB    . GLU E 1 63  ? 33.334  52.643  -24.800 1.00 49.66 ?  63  GLU H CB    1 
ATOM   5403  C  CG    . GLU E 1 63  ? 33.872  52.616  -23.372 1.00 56.42 ?  63  GLU H CG    1 
ATOM   5404  C  CD    . GLU E 1 63  ? 34.977  53.625  -23.118 1.00 62.78 ?  63  GLU H CD    1 
ATOM   5405  O  OE1   . GLU E 1 63  ? 34.673  54.838  -23.119 1.00 56.80 ?  63  GLU H OE1   1 
ATOM   5406  O  OE2   . GLU E 1 63  ? 36.140  53.202  -22.934 1.00 58.57 -1 63  GLU H OE2   1 
ATOM   5407  N  N     . VAL E 1 64  ? 32.824  49.478  -24.237 1.00 29.60 ?  64  VAL H N     1 
ATOM   5408  C  CA    . VAL E 1 64  ? 33.091  48.463  -23.233 1.00 26.37 ?  64  VAL H CA    1 
ATOM   5409  C  C     . VAL E 1 64  ? 34.237  48.963  -22.362 1.00 23.48 ?  64  VAL H C     1 
ATOM   5410  O  O     . VAL E 1 64  ? 35.300  49.319  -22.867 1.00 25.04 ?  64  VAL H O     1 
ATOM   5411  C  CB    . VAL E 1 64  ? 33.430  47.093  -23.852 1.00 26.84 ?  64  VAL H CB    1 
ATOM   5412  C  CG1   . VAL E 1 64  ? 33.944  46.107  -22.809 1.00 27.00 ?  64  VAL H CG1   1 
ATOM   5413  C  CG2   . VAL E 1 64  ? 32.248  46.504  -24.612 1.00 27.68 ?  64  VAL H CG2   1 
ATOM   5414  N  N     . LYS E 1 65  ? 33.998  48.995  -21.050 1.00 23.43 ?  65  LYS H N     1 
ATOM   5415  C  CA    . LYS E 1 65  ? 35.013  49.391  -20.090 1.00 26.20 ?  65  LYS H CA    1 
ATOM   5416  C  C     . LYS E 1 65  ? 34.681  48.733  -18.756 1.00 27.50 ?  65  LYS H C     1 
ATOM   5417  O  O     . LYS E 1 65  ? 33.531  48.756  -18.323 1.00 28.12 ?  65  LYS H O     1 
ATOM   5418  C  CB    . LYS E 1 65  ? 35.051  50.921  -20.008 1.00 26.58 ?  65  LYS H CB    1 
ATOM   5419  C  CG    . LYS E 1 65  ? 35.983  51.549  -18.981 1.00 25.86 ?  65  LYS H CG    1 
ATOM   5420  C  CD    . LYS E 1 65  ? 35.917  53.072  -19.047 1.00 27.26 ?  65  LYS H CD    1 
ATOM   5421  C  CE    . LYS E 1 65  ? 36.953  53.778  -18.233 1.00 25.61 ?  65  LYS H CE    1 
ATOM   5422  N  NZ    . LYS E 1 65  ? 36.944  55.218  -18.508 1.00 23.44 1  65  LYS H NZ    1 
ATOM   5423  N  N     . ASN E 1 66  ? 35.691  48.127  -18.127 1.00 32.65 ?  66  ASN H N     1 
ATOM   5424  C  CA    . ASN E 1 66  ? 35.509  47.544  -16.810 1.00 34.20 ?  66  ASN H CA    1 
ATOM   5425  C  C     . ASN E 1 66  ? 35.275  48.688  -15.828 1.00 33.58 ?  66  ASN H C     1 
ATOM   5426  O  O     . ASN E 1 66  ? 35.963  49.704  -15.883 1.00 31.13 ?  66  ASN H O     1 
ATOM   5427  C  CB    . ASN E 1 66  ? 36.688  46.662  -16.415 1.00 35.48 ?  66  ASN H CB    1 
ATOM   5428  C  CG    . ASN E 1 66  ? 36.288  45.588  -15.431 1.00 35.25 ?  66  ASN H CG    1 
ATOM   5429  O  OD1   . ASN E 1 66  ? 35.622  45.878  -14.431 1.00 31.80 ?  66  ASN H OD1   1 
ATOM   5430  N  ND2   . ASN E 1 66  ? 36.665  44.347  -15.703 1.00 33.56 ?  66  ASN H ND2   1 
ATOM   5431  N  N     . ARG E 1 67  ? 34.283  48.521  -14.948 1.00 37.98 ?  67  ARG H N     1 
ATOM   5432  C  CA    . ARG E 1 67  ? 33.937  49.565  -13.999 1.00 42.85 ?  67  ARG H CA    1 
ATOM   5433  C  C     . ARG E 1 67  ? 35.025  49.613  -12.926 1.00 42.22 ?  67  ARG H C     1 
ATOM   5434  O  O     . ARG E 1 67  ? 35.224  50.649  -12.293 1.00 43.83 ?  67  ARG H O     1 
ATOM   5435  C  CB    . ARG E 1 67  ? 32.495  49.336  -13.522 1.00 42.01 ?  67  ARG H CB    1 
ATOM   5436  C  CG    . ARG E 1 67  ? 31.669  50.597  -13.299 1.00 43.63 ?  67  ARG H CG    1 
ATOM   5437  C  CD    . ARG E 1 67  ? 30.201  50.442  -13.701 1.00 41.94 ?  67  ARG H CD    1 
ATOM   5438  N  NE    . ARG E 1 67  ? 29.612  49.151  -13.328 1.00 38.20 ?  67  ARG H NE    1 
ATOM   5439  C  CZ    . ARG E 1 67  ? 29.172  48.246  -14.198 1.00 40.86 ?  67  ARG H CZ    1 
ATOM   5440  N  NH1   . ARG E 1 67  ? 29.244  48.481  -15.496 1.00 43.42 1  67  ARG H NH1   1 
ATOM   5441  N  NH2   . ARG E 1 67  ? 28.664  47.104  -13.768 1.00 38.27 ?  67  ARG H NH2   1 
ATOM   5442  N  N     . ARG E 1 68  ? 35.746  48.496  -12.749 1.00 43.54 ?  68  ARG H N     1 
ATOM   5443  C  CA    . ARG E 1 68  ? 36.965  48.496  -11.952 1.00 43.80 ?  68  ARG H CA    1 
ATOM   5444  C  C     . ARG E 1 68  ? 37.905  49.569  -12.499 1.00 40.82 ?  68  ARG H C     1 
ATOM   5445  O  O     . ARG E 1 68  ? 38.516  50.313  -11.736 1.00 43.91 ?  68  ARG H O     1 
ATOM   5446  C  CB    . ARG E 1 68  ? 37.723  47.160  -11.954 1.00 45.20 ?  68  ARG H CB    1 
ATOM   5447  C  CG    . ARG E 1 68  ? 37.032  45.926  -11.387 1.00 49.97 ?  68  ARG H CG    1 
ATOM   5448  C  CD    . ARG E 1 68  ? 37.965  44.715  -11.461 1.00 46.21 ?  68  ARG H CD    1 
ATOM   5449  N  NE    . ARG E 1 68  ? 37.352  43.441  -11.063 1.00 42.73 ?  68  ARG H NE    1 
ATOM   5450  C  CZ    . ARG E 1 68  ? 37.025  43.088  -9.825  1.00 43.64 ?  68  ARG H CZ    1 
ATOM   5451  N  NH1   . ARG E 1 68  ? 37.293  43.887  -8.806  1.00 43.87 1  68  ARG H NH1   1 
ATOM   5452  N  NH2   . ARG E 1 68  ? 36.441  41.923  -9.611  1.00 36.90 ?  68  ARG H NH2   1 
ATOM   5453  N  N     . ASP E 1 69  ? 38.006  49.639  -13.833 1.00 36.37 ?  69  ASP H N     1 
ATOM   5454  C  CA    . ASP E 1 69  ? 38.906  50.568  -14.501 1.00 38.51 ?  69  ASP H CA    1 
ATOM   5455  C  C     . ASP E 1 69  ? 38.385  52.000  -14.382 1.00 37.22 ?  69  ASP H C     1 
ATOM   5456  O  O     . ASP E 1 69  ? 39.164  52.949  -14.447 1.00 35.44 ?  69  ASP H O     1 
ATOM   5457  C  CB    . ASP E 1 69  ? 39.146  50.164  -15.948 1.00 39.21 ?  69  ASP H CB    1 
ATOM   5458  C  CG    . ASP E 1 69  ? 40.101  48.996  -16.153 1.00 46.95 ?  69  ASP H CG    1 
ATOM   5459  O  OD1   . ASP E 1 69  ? 41.318  49.190  -15.942 1.00 48.06 ?  69  ASP H OD1   1 
ATOM   5460  O  OD2   . ASP E 1 69  ? 39.620  47.899  -16.513 1.00 45.03 -1 69  ASP H OD2   1 
ATOM   5461  N  N     . THR E 1 70  ? 37.067  52.155  -14.221 1.00 34.71 ?  70  THR H N     1 
ATOM   5462  C  CA    . THR E 1 70  ? 36.475  53.470  -14.036 1.00 32.86 ?  70  THR H CA    1 
ATOM   5463  C  C     . THR E 1 70  ? 36.879  54.000  -12.663 1.00 33.77 ?  70  THR H C     1 
ATOM   5464  O  O     . THR E 1 70  ? 37.295  55.150  -12.532 1.00 32.63 ?  70  THR H O     1 
ATOM   5465  C  CB    . THR E 1 70  ? 34.958  53.377  -14.197 1.00 32.54 ?  70  THR H CB    1 
ATOM   5466  O  OG1   . THR E 1 70  ? 34.748  53.046  -15.567 1.00 30.41 ?  70  THR H OG1   1 
ATOM   5467  C  CG2   . THR E 1 70  ? 34.246  54.674  -13.855 1.00 32.79 ?  70  THR H CG2   1 
ATOM   5468  N  N     . TYR E 1 71  ? 36.771  53.130  -11.653 1.00 31.58 ?  71  TYR H N     1 
ATOM   5469  C  CA    . TYR E 1 71  ? 37.047  53.484  -10.270 1.00 30.68 ?  71  TYR H CA    1 
ATOM   5470  C  C     . TYR E 1 71  ? 38.506  53.927  -10.136 1.00 31.84 ?  71  TYR H C     1 
ATOM   5471  O  O     . TYR E 1 71  ? 38.780  54.991  -9.584  1.00 34.68 ?  71  TYR H O     1 
ATOM   5472  C  CB    . TYR E 1 71  ? 36.630  52.296  -9.391  1.00 28.05 ?  71  TYR H CB    1 
ATOM   5473  C  CG    . TYR E 1 71  ? 35.159  51.908  -9.519  1.00 28.79 ?  71  TYR H CG    1 
ATOM   5474  C  CD1   . TYR E 1 71  ? 34.208  52.831  -9.935  1.00 27.05 ?  71  TYR H CD1   1 
ATOM   5475  C  CD2   . TYR E 1 71  ? 34.719  50.621  -9.223  1.00 26.83 ?  71  TYR H CD2   1 
ATOM   5476  C  CE1   . TYR E 1 71  ? 32.870  52.491  -10.055 1.00 28.82 ?  71  TYR H CE1   1 
ATOM   5477  C  CE2   . TYR E 1 71  ? 33.383  50.268  -9.339  1.00 27.30 ?  71  TYR H CE2   1 
ATOM   5478  C  CZ    . TYR E 1 71  ? 32.455  51.205  -9.757  1.00 28.11 ?  71  TYR H CZ    1 
ATOM   5479  O  OH    . TYR E 1 71  ? 31.136  50.868  -9.873  1.00 23.74 ?  71  TYR H OH    1 
ATOM   5480  N  N     . GLU E 1 72  ? 39.435  53.116  -10.657 1.00 31.66 ?  72  GLU H N     1 
ATOM   5481  C  CA    . GLU E 1 72  ? 40.857  53.430  -10.613 1.00 34.57 ?  72  GLU H CA    1 
ATOM   5482  C  C     . GLU E 1 72  ? 41.117  54.871  -11.056 1.00 37.59 ?  72  GLU H C     1 
ATOM   5483  O  O     . GLU E 1 72  ? 41.908  55.577  -10.433 1.00 35.24 ?  72  GLU H O     1 
ATOM   5484  C  CB    . GLU E 1 72  ? 41.633  52.450  -11.494 1.00 34.17 ?  72  GLU H CB    1 
ATOM   5485  C  CG    . GLU E 1 72  ? 43.118  52.779  -11.624 1.00 35.11 ?  72  GLU H CG    1 
ATOM   5486  C  CD    . GLU E 1 72  ? 43.854  52.905  -10.303 1.00 42.36 ?  72  GLU H CD    1 
ATOM   5487  O  OE1   . GLU E 1 72  ? 43.608  52.068  -9.408  1.00 46.78 ?  72  GLU H OE1   1 
ATOM   5488  O  OE2   . GLU E 1 72  ? 44.691  53.826  -10.175 1.00 45.61 -1 72  GLU H OE2   1 
ATOM   5489  N  N     . GLN E 1 73  ? 40.472  55.294  -12.151 1.00 40.92 ?  73  GLN H N     1 
ATOM   5490  C  CA    . GLN E 1 73  ? 40.665  56.626  -12.715 1.00 40.34 ?  73  GLN H CA    1 
ATOM   5491  C  C     . GLN E 1 73  ? 40.109  57.690  -11.771 1.00 33.02 ?  73  GLN H C     1 
ATOM   5492  O  O     . GLN E 1 73  ? 40.752  58.715  -11.541 1.00 34.67 ?  73  GLN H O     1 
ATOM   5493  C  CB    . GLN E 1 73  ? 39.995  56.713  -14.087 1.00 43.42 ?  73  GLN H CB    1 
ATOM   5494  C  CG    . GLN E 1 73  ? 40.889  56.295  -15.249 1.00 46.33 ?  73  GLN H CG    1 
ATOM   5495  C  CD    . GLN E 1 73  ? 41.501  57.474  -15.972 1.00 46.88 ?  73  GLN H CD    1 
ATOM   5496  O  OE1   . GLN E 1 73  ? 40.836  58.168  -16.751 1.00 45.92 ?  73  GLN H OE1   1 
ATOM   5497  N  NE2   . GLN E 1 73  ? 42.781  57.710  -15.729 1.00 48.78 ?  73  GLN H NE2   1 
ATOM   5498  N  N     . MET E 1 74  ? 38.896  57.452  -11.260 1.00 30.08 ?  74  MET H N     1 
ATOM   5499  C  CA    . MET E 1 74  ? 38.323  58.288  -10.218 1.00 24.24 ?  74  MET H CA    1 
ATOM   5500  C  C     . MET E 1 74  ? 39.365  58.499  -9.121  1.00 22.48 ?  74  MET H C     1 
ATOM   5501  O  O     . MET E 1 74  ? 39.871  59.605  -8.942  1.00 27.00 ?  74  MET H O     1 
ATOM   5502  C  CB    . MET E 1 74  ? 37.061  57.643  -9.626  1.00 23.24 ?  74  MET H CB    1 
ATOM   5503  C  CG    . MET E 1 74  ? 35.799  57.867  -10.445 1.00 23.14 ?  74  MET H CG    1 
ATOM   5504  S  SD    . MET E 1 74  ? 34.413  56.816  -9.960  1.00 21.17 ?  74  MET H SD    1 
ATOM   5505  C  CE    . MET E 1 74  ? 33.318  57.149  -11.348 1.00 21.28 ?  74  MET H CE    1 
ATOM   5506  N  N     . VAL E 1 75  ? 39.676  57.417  -8.397  1.00 21.78 ?  75  VAL H N     1 
ATOM   5507  C  CA    . VAL E 1 75  ? 40.628  57.448  -7.298  1.00 19.90 ?  75  VAL H CA    1 
ATOM   5508  C  C     . VAL E 1 75  ? 41.815  58.319  -7.697  1.00 21.92 ?  75  VAL H C     1 
ATOM   5509  O  O     . VAL E 1 75  ? 42.215  59.213  -6.954  1.00 21.93 ?  75  VAL H O     1 
ATOM   5510  C  CB    . VAL E 1 75  ? 41.062  56.013  -6.927  1.00 18.89 ?  75  VAL H CB    1 
ATOM   5511  C  CG1   . VAL E 1 75  ? 42.243  55.975  -5.962  1.00 17.51 ?  75  VAL H CG1   1 
ATOM   5512  C  CG2   . VAL E 1 75  ? 39.898  55.211  -6.361  1.00 17.39 ?  75  VAL H CG2   1 
ATOM   5513  N  N     . ASN E 1 76  ? 42.340  58.071  -8.901  1.00 21.00 ?  76  ASN H N     1 
ATOM   5514  C  CA    . ASN E 1 76  ? 43.597  58.660  -9.328  1.00 22.79 ?  76  ASN H CA    1 
ATOM   5515  C  C     . ASN E 1 76  ? 43.455  60.169  -9.502  1.00 19.84 ?  76  ASN H C     1 
ATOM   5516  O  O     . ASN E 1 76  ? 44.355  60.925  -9.144  1.00 19.32 ?  76  ASN H O     1 
ATOM   5517  C  CB    . ASN E 1 76  ? 44.100  58.042  -10.626 1.00 24.35 ?  76  ASN H CB    1 
ATOM   5518  C  CG    . ASN E 1 76  ? 45.496  58.516  -10.942 1.00 24.29 ?  76  ASN H CG    1 
ATOM   5519  O  OD1   . ASN E 1 76  ? 45.708  59.209  -11.943 1.00 25.85 ?  76  ASN H OD1   1 
ATOM   5520  N  ND2   . ASN E 1 76  ? 46.450  58.180  -10.086 1.00 28.38 ?  76  ASN H ND2   1 
ATOM   5521  N  N     . ALA E 1 77  ? 42.334  60.587  -10.094 1.00 20.54 ?  77  ALA H N     1 
ATOM   5522  C  CA    . ALA E 1 77  ? 42.043  61.996  -10.294 1.00 20.96 ?  77  ALA H CA    1 
ATOM   5523  C  C     . ALA E 1 77  ? 41.969  62.712  -8.944  1.00 21.24 ?  77  ALA H C     1 
ATOM   5524  O  O     . ALA E 1 77  ? 42.537  63.789  -8.784  1.00 19.07 ?  77  ALA H O     1 
ATOM   5525  C  CB    . ALA E 1 77  ? 40.763  62.145  -11.091 1.00 20.72 ?  77  ALA H CB    1 
ATOM   5526  N  N     . ILE E 1 78  ? 41.280  62.098  -7.972  1.00 24.45 ?  78  ILE H N     1 
ATOM   5527  C  CA    . ILE E 1 78  ? 41.147  62.669  -6.638  1.00 23.12 ?  78  ILE H CA    1 
ATOM   5528  C  C     . ILE E 1 78  ? 42.535  62.884  -6.038  1.00 20.40 ?  78  ILE H C     1 
ATOM   5529  O  O     . ILE E 1 78  ? 42.841  63.970  -5.549  1.00 19.82 ?  78  ILE H O     1 
ATOM   5530  C  CB    . ILE E 1 78  ? 40.272  61.779  -5.733  1.00 22.31 ?  78  ILE H CB    1 
ATOM   5531  C  CG1   . ILE E 1 78  ? 38.821  61.726  -6.221  1.00 20.19 ?  78  ILE H CG1   1 
ATOM   5532  C  CG2   . ILE E 1 78  ? 40.352  62.239  -4.275  1.00 25.01 ?  78  ILE H CG2   1 
ATOM   5533  C  CD1   . ILE E 1 78  ? 38.057  60.491  -5.774  1.00 18.04 ?  78  ILE H CD1   1 
ATOM   5534  N  N     . LEU E 1 79  ? 43.368  61.838  -6.086  1.00 21.27 ?  79  LEU H N     1 
ATOM   5535  C  CA    . LEU E 1 79  ? 44.676  61.852  -5.448  1.00 20.08 ?  79  LEU H CA    1 
ATOM   5536  C  C     . LEU E 1 79  ? 45.572  62.897  -6.106  1.00 17.90 ?  79  LEU H C     1 
ATOM   5537  O  O     . LEU E 1 79  ? 46.396  63.517  -5.437  1.00 15.22 ?  79  LEU H O     1 
ATOM   5538  C  CB    . LEU E 1 79  ? 45.313  60.464  -5.499  1.00 19.88 ?  79  LEU H CB    1 
ATOM   5539  C  CG    . LEU E 1 79  ? 45.094  59.585  -4.263  1.00 21.06 ?  79  LEU H CG    1 
ATOM   5540  C  CD1   . LEU E 1 79  ? 45.736  60.199  -3.028  1.00 21.11 ?  79  LEU H CD1   1 
ATOM   5541  C  CD2   . LEU E 1 79  ? 43.612  59.356  -4.041  1.00 23.39 ?  79  LEU H CD2   1 
ATOM   5542  N  N     . ASP E 1 80  ? 45.417  63.071  -7.421  1.00 16.23 ?  80  ASP H N     1 
ATOM   5543  C  CA    . ASP E 1 80  ? 46.168  64.083  -8.143  1.00 17.09 ?  80  ASP H CA    1 
ATOM   5544  C  C     . ASP E 1 80  ? 45.997  65.444  -7.472  1.00 16.24 ?  80  ASP H C     1 
ATOM   5545  O  O     . ASP E 1 80  ? 46.967  66.186  -7.334  1.00 15.02 ?  80  ASP H O     1 
ATOM   5546  C  CB    . ASP E 1 80  ? 45.791  64.143  -9.615  1.00 19.15 ?  80  ASP H CB    1 
ATOM   5547  C  CG    . ASP E 1 80  ? 46.607  63.257  -10.547 1.00 21.24 ?  80  ASP H CG    1 
ATOM   5548  O  OD1   . ASP E 1 80  ? 47.314  62.359  -10.040 1.00 23.60 ?  80  ASP H OD1   1 
ATOM   5549  O  OD2   . ASP E 1 80  ? 46.547  63.492  -11.772 1.00 21.82 -1 80  ASP H OD2   1 
ATOM   5550  N  N     . ALA E 1 81  ? 44.769  65.788  -7.067  1.00 15.43 ?  81  ALA H N     1 
ATOM   5551  C  CA    . ALA E 1 81  ? 44.547  67.089  -6.454  1.00 15.55 ?  81  ALA H CA    1 
ATOM   5552  C  C     . ALA E 1 81  ? 45.204  67.118  -5.076  1.00 15.74 ?  81  ALA H C     1 
ATOM   5553  O  O     . ALA E 1 81  ? 45.816  68.117  -4.702  1.00 15.23 ?  81  ALA H O     1 
ATOM   5554  C  CB    . ALA E 1 81  ? 43.071  67.425  -6.381  1.00 13.23 ?  81  ALA H CB    1 
ATOM   5555  N  N     . VAL E 1 82  ? 45.081  66.009  -4.337  1.00 14.41 ?  82  VAL H N     1 
ATOM   5556  C  CA    . VAL E 1 82  ? 45.638  65.909  -2.998  1.00 16.08 ?  82  VAL H CA    1 
ATOM   5557  C  C     . VAL E 1 82  ? 47.148  66.129  -3.079  1.00 17.46 ?  82  VAL H C     1 
ATOM   5558  O  O     . VAL E 1 82  ? 47.698  66.936  -2.331  1.00 19.33 ?  82  VAL H O     1 
ATOM   5559  C  CB    . VAL E 1 82  ? 45.279  64.565  -2.331  1.00 17.24 ?  82  VAL H CB    1 
ATOM   5560  C  CG1   . VAL E 1 82  ? 45.966  64.374  -0.982  1.00 15.50 ?  82  VAL H CG1   1 
ATOM   5561  C  CG2   . VAL E 1 82  ? 43.772  64.404  -2.176  1.00 16.17 ?  82  VAL H CG2   1 
ATOM   5562  N  N     . ARG E 1 83  ? 47.797  65.430  -4.018  1.00 20.69 ?  83  ARG H N     1 
ATOM   5563  C  CA    . ARG E 1 83  ? 49.246  65.450  -4.164  1.00 20.37 ?  83  ARG H CA    1 
ATOM   5564  C  C     . ARG E 1 83  ? 49.733  66.851  -4.531  1.00 19.90 ?  83  ARG H C     1 
ATOM   5565  O  O     . ARG E 1 83  ? 50.810  67.267  -4.108  1.00 19.38 ?  83  ARG H O     1 
ATOM   5566  C  CB    . ARG E 1 83  ? 49.678  64.442  -5.236  1.00 22.65 ?  83  ARG H CB    1 
ATOM   5567  C  CG    . ARG E 1 83  ? 49.553  62.979  -4.834  1.00 22.90 ?  83  ARG H CG    1 
ATOM   5568  C  CD    . ARG E 1 83  ? 49.624  62.050  -6.040  1.00 22.68 ?  83  ARG H CD    1 
ATOM   5569  N  NE    . ARG E 1 83  ? 49.134  60.707  -5.711  1.00 22.24 ?  83  ARG H NE    1 
ATOM   5570  C  CZ    . ARG E 1 83  ? 48.636  59.839  -6.585  1.00 22.58 ?  83  ARG H CZ    1 
ATOM   5571  N  NH1   . ARG E 1 83  ? 48.543  60.158  -7.864  1.00 18.71 1  83  ARG H NH1   1 
ATOM   5572  N  NH2   . ARG E 1 83  ? 48.217  58.657  -6.168  1.00 24.36 ?  83  ARG H NH2   1 
ATOM   5573  N  N     . ALA E 1 84  ? 48.935  67.560  -5.337  1.00 19.86 ?  84  ALA H N     1 
ATOM   5574  C  CA    . ALA E 1 84  ? 49.259  68.912  -5.768  1.00 18.71 ?  84  ALA H CA    1 
ATOM   5575  C  C     . ALA E 1 84  ? 49.202  69.879  -4.586  1.00 19.62 ?  84  ALA H C     1 
ATOM   5576  O  O     . ALA E 1 84  ? 49.756  70.975  -4.653  1.00 23.19 ?  84  ALA H O     1 
ATOM   5577  C  CB    . ALA E 1 84  ? 48.321  69.331  -6.882  1.00 17.83 ?  84  ALA H CB    1 
ATOM   5578  N  N     . GLY E 1 85  ? 48.517  69.471  -3.511  1.00 18.61 ?  85  GLY H N     1 
ATOM   5579  C  CA    . GLY E 1 85  ? 48.505  70.228  -2.267  1.00 18.65 ?  85  GLY H CA    1 
ATOM   5580  C  C     . GLY E 1 85  ? 47.168  70.927  -2.024  1.00 17.71 ?  85  GLY H C     1 
ATOM   5581  O  O     . GLY E 1 85  ? 47.096  71.882  -1.251  1.00 19.37 ?  85  GLY H O     1 
ATOM   5582  N  N     . LYS E 1 86  ? 46.115  70.435  -2.682  1.00 15.59 ?  86  LYS H N     1 
ATOM   5583  C  CA    . LYS E 1 86  ? 44.786  71.014  -2.572  1.00 17.80 ?  86  LYS H CA    1 
ATOM   5584  C  C     . LYS E 1 86  ? 44.015  70.359  -1.430  1.00 16.55 ?  86  LYS H C     1 
ATOM   5585  O  O     . LYS E 1 86  ? 43.982  69.134  -1.315  1.00 14.24 ?  86  LYS H O     1 
ATOM   5586  C  CB    . LYS E 1 86  ? 43.982  70.792  -3.858  1.00 18.54 ?  86  LYS H CB    1 
ATOM   5587  C  CG    . LYS E 1 86  ? 44.530  71.464  -5.105  1.00 19.94 ?  86  LYS H CG    1 
ATOM   5588  C  CD    . LYS E 1 86  ? 43.826  71.008  -6.377  1.00 20.37 ?  86  LYS H CD    1 
ATOM   5589  C  CE    . LYS E 1 86  ? 44.371  71.642  -7.615  1.00 23.72 ?  86  LYS H CE    1 
ATOM   5590  N  NZ    . LYS E 1 86  ? 44.256  73.102  -7.569  1.00 25.91 1  86  LYS H NZ    1 
ATOM   5591  N  N     . LYS E 1 87  ? 43.379  71.192  -0.600  1.00 16.78 ?  87  LYS H N     1 
ATOM   5592  C  CA    . LYS E 1 87  ? 42.407  70.700  0.360   1.00 16.36 ?  87  LYS H CA    1 
ATOM   5593  C  C     . LYS E 1 87  ? 41.204  70.172  -0.416  1.00 16.41 ?  87  LYS H C     1 
ATOM   5594  O  O     . LYS E 1 87  ? 40.366  70.944  -0.880  1.00 15.08 ?  87  LYS H O     1 
ATOM   5595  C  CB    . LYS E 1 87  ? 42.006  71.776  1.372   1.00 16.29 ?  87  LYS H CB    1 
ATOM   5596  C  CG    . LYS E 1 87  ? 40.945  71.305  2.351   1.00 15.75 ?  87  LYS H CG    1 
ATOM   5597  C  CD    . LYS E 1 87  ? 40.622  72.301  3.454   1.00 16.51 ?  87  LYS H CD    1 
ATOM   5598  C  CE    . LYS E 1 87  ? 40.047  73.573  2.921   1.00 16.93 ?  87  LYS H CE    1 
ATOM   5599  N  NZ    . LYS E 1 87  ? 39.859  74.536  4.007   1.00 17.41 1  87  LYS H NZ    1 
ATOM   5600  N  N     . THR E 1 88  ? 41.145  68.841  -0.538  1.00 15.84 ?  88  THR H N     1 
ATOM   5601  C  CA    . THR E 1 88  ? 40.273  68.175  -1.491  1.00 17.00 ?  88  THR H CA    1 
ATOM   5602  C  C     . THR E 1 88  ? 39.100  67.530  -0.759  1.00 16.43 ?  88  THR H C     1 
ATOM   5603  O  O     . THR E 1 88  ? 39.268  66.954  0.313   1.00 19.33 ?  88  THR H O     1 
ATOM   5604  C  CB    . THR E 1 88  ? 41.082  67.135  -2.266  1.00 19.42 ?  88  THR H CB    1 
ATOM   5605  O  OG1   . THR E 1 88  ? 42.246  67.808  -2.735  1.00 23.38 ?  88  THR H OG1   1 
ATOM   5606  C  CG2   . THR E 1 88  ? 40.315  66.547  -3.438  1.00 21.74 ?  88  THR H CG2   1 
ATOM   5607  N  N     . VAL E 1 89  ? 37.916  67.627  -1.372  1.00 13.43 ?  89  VAL H N     1 
ATOM   5608  C  CA    . VAL E 1 89  ? 36.715  66.982  -0.872  1.00 12.86 ?  89  VAL H CA    1 
ATOM   5609  C  C     . VAL E 1 89  ? 36.148  66.106  -1.986  1.00 12.02 ?  89  VAL H C     1 
ATOM   5610  O  O     . VAL E 1 89  ? 36.134  66.501  -3.148  1.00 11.14 ?  89  VAL H O     1 
ATOM   5611  C  CB    . VAL E 1 89  ? 35.673  68.015  -0.396  1.00 13.41 ?  89  VAL H CB    1 
ATOM   5612  C  CG1   . VAL E 1 89  ? 34.313  67.380  -0.136  1.00 12.92 ?  89  VAL H CG1   1 
ATOM   5613  C  CG2   . VAL E 1 89  ? 36.142  68.788  0.831   1.00 12.81 ?  89  VAL H CG2   1 
ATOM   5614  N  N     . CYS E 1 90  ? 35.698  64.904  -1.623  1.00 12.57 ?  90  CYS H N     1 
ATOM   5615  C  CA    . CYS E 1 90  ? 34.985  64.048  -2.553  1.00 14.39 ?  90  CYS H CA    1 
ATOM   5616  C  C     . CYS E 1 90  ? 33.532  63.955  -2.091  1.00 13.21 ?  90  CYS H C     1 
ATOM   5617  O  O     . CYS E 1 90  ? 33.261  63.562  -0.959  1.00 13.39 ?  90  CYS H O     1 
ATOM   5618  C  CB    . CYS E 1 90  ? 35.702  62.709  -2.693  1.00 16.08 ?  90  CYS H CB    1 
ATOM   5619  S  SG    . CYS E 1 90  ? 34.717  61.432  -3.517  1.00 21.02 ?  90  CYS H SG    1 
ATOM   5620  N  N     . ALA E 1 91  ? 32.609  64.366  -2.968  1.00 13.96 ?  91  ALA H N     1 
ATOM   5621  C  CA    . ALA E 1 91  ? 31.191  64.390  -2.647  1.00 13.87 ?  91  ALA H CA    1 
ATOM   5622  C  C     . ALA E 1 91  ? 30.465  63.298  -3.426  1.00 15.17 ?  91  ALA H C     1 
ATOM   5623  O  O     . ALA E 1 91  ? 30.237  63.436  -4.626  1.00 14.82 ?  91  ALA H O     1 
ATOM   5624  C  CB    . ALA E 1 91  ? 30.611  65.758  -2.946  1.00 14.06 ?  91  ALA H CB    1 
ATOM   5625  N  N     . LEU E 1 92  ? 30.109  62.218  -2.719  1.00 16.57 ?  92  LEU H N     1 
ATOM   5626  C  CA    . LEU E 1 92  ? 29.365  61.109  -3.296  1.00 19.53 ?  92  LEU H CA    1 
ATOM   5627  C  C     . LEU E 1 92  ? 27.958  61.101  -2.706  1.00 21.06 ?  92  LEU H C     1 
ATOM   5628  O  O     . LEU E 1 92  ? 27.754  61.542  -1.577  1.00 19.67 ?  92  LEU H O     1 
ATOM   5629  C  CB    . LEU E 1 92  ? 30.056  59.772  -3.021  1.00 20.23 ?  92  LEU H CB    1 
ATOM   5630  C  CG    . LEU E 1 92  ? 31.534  59.656  -3.405  1.00 21.16 ?  92  LEU H CG    1 
ATOM   5631  C  CD1   . LEU E 1 92  ? 32.006  58.245  -3.106  1.00 24.37 ?  92  LEU H CD1   1 
ATOM   5632  C  CD2   . LEU E 1 92  ? 31.813  59.999  -4.856  1.00 20.81 ?  92  LEU H CD2   1 
ATOM   5633  N  N     . TYR E 1 93  ? 26.998  60.564  -3.465  1.00 22.70 ?  93  TYR H N     1 
ATOM   5634  C  CA    . TYR E 1 93  ? 25.625  60.502  -2.999  1.00 22.79 ?  93  TYR H CA    1 
ATOM   5635  C  C     . TYR E 1 93  ? 25.553  59.523  -1.828  1.00 21.74 ?  93  TYR H C     1 
ATOM   5636  O  O     . TYR E 1 93  ? 26.284  58.534  -1.781  1.00 21.27 ?  93  TYR H O     1 
ATOM   5637  C  CB    . TYR E 1 93  ? 24.694  60.222  -4.187  1.00 25.83 ?  93  TYR H CB    1 
ATOM   5638  C  CG    . TYR E 1 93  ? 24.690  58.816  -4.772  1.00 28.65 ?  93  TYR H CG    1 
ATOM   5639  C  CD1   . TYR E 1 93  ? 23.916  57.812  -4.204  1.00 30.95 ?  93  TYR H CD1   1 
ATOM   5640  C  CD2   . TYR E 1 93  ? 25.403  58.507  -5.926  1.00 34.08 ?  93  TYR H CD2   1 
ATOM   5641  C  CE1   . TYR E 1 93  ? 23.883  56.534  -4.738  1.00 30.96 ?  93  TYR H CE1   1 
ATOM   5642  C  CE2   . TYR E 1 93  ? 25.377  57.233  -6.471  1.00 32.18 ?  93  TYR H CE2   1 
ATOM   5643  C  CZ    . TYR E 1 93  ? 24.615  56.244  -5.875  1.00 30.25 ?  93  TYR H CZ    1 
ATOM   5644  O  OH    . TYR E 1 93  ? 24.578  54.985  -6.398  1.00 35.05 ?  93  TYR H OH    1 
ATOM   5645  N  N     . GLY E 1 94  ? 24.676  59.847  -0.872  1.00 19.69 ?  94  GLY H N     1 
ATOM   5646  C  CA    . GLY E 1 94  ? 24.544  59.111  0.375   1.00 18.70 ?  94  GLY H CA    1 
ATOM   5647  C  C     . GLY E 1 94  ? 25.880  58.976  1.100   1.00 19.53 ?  94  GLY H C     1 
ATOM   5648  O  O     . GLY E 1 94  ? 26.717  59.875  1.058   1.00 22.53 ?  94  GLY H O     1 
ATOM   5649  N  N     . HIS E 1 95  ? 26.047  57.831  1.770   1.00 18.26 ?  95  HIS H N     1 
ATOM   5650  C  CA    . HIS E 1 95  ? 27.253  57.511  2.514   1.00 19.86 ?  95  HIS H CA    1 
ATOM   5651  C  C     . HIS E 1 95  ? 28.383  57.216  1.530   1.00 21.74 ?  95  HIS H C     1 
ATOM   5652  O  O     . HIS E 1 95  ? 28.297  56.274  0.742   1.00 18.57 ?  95  HIS H O     1 
ATOM   5653  C  CB    . HIS E 1 95  ? 26.975  56.333  3.455   1.00 21.20 ?  95  HIS H CB    1 
ATOM   5654  C  CG    . HIS E 1 95  ? 28.005  56.131  4.515   1.00 19.25 ?  95  HIS H CG    1 
ATOM   5655  N  ND1   . HIS E 1 95  ? 29.355  56.278  4.289   1.00 19.65 ?  95  HIS H ND1   1 
ATOM   5656  C  CD2   . HIS E 1 95  ? 27.878  55.782  5.802   1.00 18.03 ?  95  HIS H CD2   1 
ATOM   5657  C  CE1   . HIS E 1 95  ? 30.013  56.029  5.412   1.00 21.50 ?  95  HIS H CE1   1 
ATOM   5658  N  NE2   . HIS E 1 95  ? 29.135  55.728  6.344   1.00 19.96 ?  95  HIS H NE2   1 
ATOM   5659  N  N     . PRO E 1 96  ? 29.483  58.001  1.554   1.00 22.78 ?  96  PRO H N     1 
ATOM   5660  C  CA    . PRO E 1 96  ? 30.544  57.865  0.554   1.00 23.65 ?  96  PRO H CA    1 
ATOM   5661  C  C     . PRO E 1 96  ? 31.215  56.493  0.556   1.00 25.71 ?  96  PRO H C     1 
ATOM   5662  O  O     . PRO E 1 96  ? 31.862  56.120  -0.420  1.00 28.74 ?  96  PRO H O     1 
ATOM   5663  C  CB    . PRO E 1 96  ? 31.524  58.994  0.926   1.00 24.05 ?  96  PRO H CB    1 
ATOM   5664  C  CG    . PRO E 1 96  ? 31.269  59.241  2.396   1.00 24.41 ?  96  PRO H CG    1 
ATOM   5665  C  CD    . PRO E 1 96  ? 29.773  59.035  2.559   1.00 23.82 ?  96  PRO H CD    1 
ATOM   5666  N  N     . GLY E 1 97  ? 31.041  55.742  1.650   1.00 26.71 ?  97  GLY H N     1 
ATOM   5667  C  CA    . GLY E 1 97  ? 31.731  54.474  1.820   1.00 28.61 ?  97  GLY H CA    1 
ATOM   5668  C  C     . GLY E 1 97  ? 30.773  53.301  2.015   1.00 27.05 ?  97  GLY H C     1 
ATOM   5669  O  O     . GLY E 1 97  ? 31.172  52.264  2.543   1.00 22.91 ?  97  GLY H O     1 
ATOM   5670  N  N     . VAL E 1 98  ? 29.517  53.460  1.582   1.00 27.17 ?  98  VAL H N     1 
ATOM   5671  C  CA    . VAL E 1 98  ? 28.557  52.367  1.630   1.00 28.43 ?  98  VAL H CA    1 
ATOM   5672  C  C     . VAL E 1 98  ? 28.293  51.886  0.204   1.00 31.50 ?  98  VAL H C     1 
ATOM   5673  O  O     . VAL E 1 98  ? 27.688  52.597  -0.596  1.00 30.23 ?  98  VAL H O     1 
ATOM   5674  C  CB    . VAL E 1 98  ? 27.245  52.740  2.347   1.00 28.34 ?  98  VAL H CB    1 
ATOM   5675  C  CG1   . VAL E 1 98  ? 26.180  51.664  2.172   1.00 32.24 ?  98  VAL H CG1   1 
ATOM   5676  C  CG2   . VAL E 1 98  ? 27.467  53.025  3.827   1.00 27.52 ?  98  VAL H CG2   1 
ATOM   5677  N  N     . PHE E 1 99  ? 28.756  50.665  -0.093  1.00 28.07 ?  99  PHE H N     1 
ATOM   5678  C  CA    . PHE E 1 99  ? 28.628  50.072  -1.416  1.00 27.18 ?  99  PHE H CA    1 
ATOM   5679  C  C     . PHE E 1 99  ? 29.253  51.007  -2.445  1.00 25.55 ?  99  PHE H C     1 
ATOM   5680  O  O     . PHE E 1 99  ? 28.726  51.176  -3.542  1.00 23.89 ?  99  PHE H O     1 
ATOM   5681  C  CB    . PHE E 1 99  ? 27.176  49.780  -1.806  1.00 26.47 ?  99  PHE H CB    1 
ATOM   5682  C  CG    . PHE E 1 99  ? 26.601  48.495  -1.225  1.00 25.97 ?  99  PHE H CG    1 
ATOM   5683  C  CD1   . PHE E 1 99  ? 26.162  48.445  0.093   1.00 24.42 ?  99  PHE H CD1   1 
ATOM   5684  C  CD2   . PHE E 1 99  ? 26.482  47.350  -2.004  1.00 25.08 ?  99  PHE H CD2   1 
ATOM   5685  C  CE1   . PHE E 1 99  ? 25.633  47.278  0.619   1.00 25.90 ?  99  PHE H CE1   1 
ATOM   5686  C  CE2   . PHE E 1 99  ? 25.951  46.185  -1.473  1.00 25.16 ?  99  PHE H CE2   1 
ATOM   5687  C  CZ    . PHE E 1 99  ? 25.529  46.151  -0.164  1.00 26.13 ?  99  PHE H CZ    1 
ATOM   5688  N  N     . ALA E 1 100 ? 30.384  51.606  -2.065  1.00 26.20 ?  100 ALA H N     1 
ATOM   5689  C  CA    . ALA E 1 100 ? 31.116  52.511  -2.933  1.00 26.91 ?  100 ALA H CA    1 
ATOM   5690  C  C     . ALA E 1 100 ? 32.599  52.426  -2.588  1.00 28.46 ?  100 ALA H C     1 
ATOM   5691  O  O     . ALA E 1 100 ? 32.986  52.633  -1.440  1.00 30.02 ?  100 ALA H O     1 
ATOM   5692  C  CB    . ALA E 1 100 ? 30.581  53.917  -2.783  1.00 28.35 ?  100 ALA H CB    1 
ATOM   5693  N  N     . CYS E 1 101 ? 33.417  52.116  -3.599  1.00 33.01 ?  101 CYS H N     1 
ATOM   5694  C  CA    . CYS E 1 101 ? 34.798  51.723  -3.375  1.00 38.27 ?  101 CYS H CA    1 
ATOM   5695  C  C     . CYS E 1 101 ? 35.749  52.872  -3.698  1.00 37.38 ?  101 CYS H C     1 
ATOM   5696  O  O     . CYS E 1 101 ? 36.946  52.780  -3.432  1.00 36.31 ?  101 CYS H O     1 
ATOM   5697  C  CB    . CYS E 1 101 ? 35.149  50.489  -4.200  1.00 40.38 ?  101 CYS H CB    1 
ATOM   5698  S  SG    . CYS E 1 101 ? 34.973  50.727  -5.988  1.00 38.46 ?  101 CYS H SG    1 
ATOM   5699  N  N     . VAL E 1 102 ? 35.210  53.953  -4.266  1.00 37.80 ?  102 VAL H N     1 
ATOM   5700  C  CA    . VAL E 1 102 ? 36.038  55.045  -4.750  1.00 33.84 ?  102 VAL H CA    1 
ATOM   5701  C  C     . VAL E 1 102 ? 36.626  55.805  -3.566  1.00 31.62 ?  102 VAL H C     1 
ATOM   5702  O  O     . VAL E 1 102 ? 37.741  56.315  -3.644  1.00 36.26 ?  102 VAL H O     1 
ATOM   5703  C  CB    . VAL E 1 102 ? 35.247  55.981  -5.680  1.00 37.23 ?  102 VAL H CB    1 
ATOM   5704  C  CG1   . VAL E 1 102 ? 35.907  57.350  -5.803  1.00 37.61 ?  102 VAL H CG1   1 
ATOM   5705  C  CG2   . VAL E 1 102 ? 35.042  55.348  -7.049  1.00 38.91 ?  102 VAL H CG2   1 
ATOM   5706  N  N     . SER E 1 103 ? 35.866  55.870  -2.471  1.00 29.82 ?  103 SER H N     1 
ATOM   5707  C  CA    . SER E 1 103 ? 36.273  56.650  -1.316  1.00 31.00 ?  103 SER H CA    1 
ATOM   5708  C  C     . SER E 1 103 ? 37.243  55.851  -0.447  1.00 28.49 ?  103 SER H C     1 
ATOM   5709  O  O     . SER E 1 103 ? 38.302  56.358  -0.086  1.00 31.71 ?  103 SER H O     1 
ATOM   5710  C  CB    . SER E 1 103 ? 35.075  57.126  -0.542  1.00 30.90 ?  103 SER H CB    1 
ATOM   5711  O  OG    . SER E 1 103 ? 34.350  58.089  -1.295  1.00 31.51 ?  103 SER H OG    1 
ATOM   5712  N  N     . HIS E 1 104 ? 36.886  54.602  -0.125  1.00 27.72 ?  104 HIS H N     1 
ATOM   5713  C  CA    . HIS E 1 104 ? 37.744  53.765  0.699   1.00 25.17 ?  104 HIS H CA    1 
ATOM   5714  C  C     . HIS E 1 104 ? 39.118  53.624  0.047   1.00 20.37 ?  104 HIS H C     1 
ATOM   5715  O  O     . HIS E 1 104 ? 40.117  53.448  0.739   1.00 17.39 ?  104 HIS H O     1 
ATOM   5716  C  CB    . HIS E 1 104 ? 37.122  52.387  0.964   1.00 25.46 ?  104 HIS H CB    1 
ATOM   5717  C  CG    . HIS E 1 104 ? 35.992  52.376  1.943   1.00 28.61 ?  104 HIS H CG    1 
ATOM   5718  N  ND1   . HIS E 1 104 ? 36.162  52.492  3.306   1.00 29.45 ?  104 HIS H ND1   1 
ATOM   5719  C  CD2   . HIS E 1 104 ? 34.673  52.251  1.747   1.00 27.78 ?  104 HIS H CD2   1 
ATOM   5720  C  CE1   . HIS E 1 104 ? 34.979  52.439  3.902   1.00 28.88 ?  104 HIS H CE1   1 
ATOM   5721  N  NE2   . HIS E 1 104 ? 34.061  52.290  2.973   1.00 27.95 ?  104 HIS H NE2   1 
ATOM   5722  N  N     . MET E 1 105 ? 39.165  53.700  -1.288  1.00 21.93 ?  105 MET H N     1 
ATOM   5723  C  CA    . MET E 1 105 ? 40.406  53.481  -2.016  1.00 21.18 ?  105 MET H CA    1 
ATOM   5724  C  C     . MET E 1 105 ? 41.246  54.755  -2.015  1.00 19.55 ?  105 MET H C     1 
ATOM   5725  O  O     . MET E 1 105 ? 42.459  54.698  -1.830  1.00 19.09 ?  105 MET H O     1 
ATOM   5726  C  CB    . MET E 1 105 ? 40.140  53.030  -3.457  1.00 23.44 ?  105 MET H CB    1 
ATOM   5727  C  CG    . MET E 1 105 ? 39.768  51.566  -3.580  1.00 25.14 ?  105 MET H CG    1 
ATOM   5728  S  SD    . MET E 1 105 ? 39.057  51.144  -5.184  1.00 31.61 ?  105 MET H SD    1 
ATOM   5729  C  CE    . MET E 1 105 ? 40.316  51.701  -6.341  1.00 32.85 ?  105 MET H CE    1 
ATOM   5730  N  N     . ALA E 1 106 ? 40.592  55.901  -2.227  1.00 17.66 ?  106 ALA H N     1 
ATOM   5731  C  CA    . ALA E 1 106 ? 41.283  57.178  -2.219  1.00 15.12 ?  106 ALA H CA    1 
ATOM   5732  C  C     . ALA E 1 106 ? 41.832  57.444  -0.821  1.00 14.51 ?  106 ALA H C     1 
ATOM   5733  O  O     . ALA E 1 106 ? 42.938  57.958  -0.671  1.00 15.46 ?  106 ALA H O     1 
ATOM   5734  C  CB    . ALA E 1 106 ? 40.356  58.284  -2.673  1.00 15.92 ?  106 ALA H CB    1 
ATOM   5735  N  N     . ILE E 1 107 ? 41.049  57.075  0.197   1.00 13.61 ?  107 ILE H N     1 
ATOM   5736  C  CA    . ILE E 1 107 ? 41.465  57.265  1.577   1.00 14.45 ?  107 ILE H CA    1 
ATOM   5737  C  C     . ILE E 1 107 ? 42.696  56.402  1.859   1.00 15.08 ?  107 ILE H C     1 
ATOM   5738  O  O     . ILE E 1 107 ? 43.681  56.900  2.399   1.00 16.12 ?  107 ILE H O     1 
ATOM   5739  C  CB    . ILE E 1 107 ? 40.311  56.987  2.559   1.00 13.28 ?  107 ILE H CB    1 
ATOM   5740  C  CG1   . ILE E 1 107 ? 39.242  58.089  2.502   1.00 12.21 ?  107 ILE H CG1   1 
ATOM   5741  C  CG2   . ILE E 1 107 ? 40.844  56.802  3.980   1.00 13.51 ?  107 ILE H CG2   1 
ATOM   5742  C  CD1   . ILE E 1 107 ? 38.150  57.957  3.549   1.00 10.62 ?  107 ILE H CD1   1 
ATOM   5743  N  N     . THR E 1 108 ? 42.636  55.117  1.480   1.00 17.94 ?  108 THR H N     1 
ATOM   5744  C  CA    . THR E 1 108 ? 43.717  54.168  1.722   1.00 18.19 ?  108 THR H CA    1 
ATOM   5745  C  C     . THR E 1 108 ? 45.002  54.637  1.041   1.00 20.34 ?  108 THR H C     1 
ATOM   5746  O  O     . THR E 1 108 ? 46.077  54.593  1.636   1.00 22.27 ?  108 THR H O     1 
ATOM   5747  C  CB    . THR E 1 108 ? 43.304  52.784  1.220   1.00 18.36 ?  108 THR H CB    1 
ATOM   5748  O  OG1   . THR E 1 108 ? 42.284  52.343  2.108   1.00 19.37 ?  108 THR H OG1   1 
ATOM   5749  C  CG2   . THR E 1 108 ? 44.448  51.784  1.227   1.00 21.80 ?  108 THR H CG2   1 
ATOM   5750  N  N     . ARG E 1 109 ? 44.878  55.068  -0.219  1.00 20.65 ?  109 ARG H N     1 
ATOM   5751  C  CA    . ARG E 1 109 ? 46.027  55.446  -1.026  1.00 21.75 ?  109 ARG H CA    1 
ATOM   5752  C  C     . ARG E 1 109 ? 46.648  56.726  -0.468  1.00 22.58 ?  109 ARG H C     1 
ATOM   5753  O  O     . ARG E 1 109 ? 47.869  56.850  -0.403  1.00 23.80 ?  109 ARG H O     1 
ATOM   5754  C  CB    . ARG E 1 109 ? 45.568  55.583  -2.483  1.00 22.90 ?  109 ARG H CB    1 
ATOM   5755  C  CG    . ARG E 1 109 ? 46.690  55.644  -3.509  1.00 24.48 ?  109 ARG H CG    1 
ATOM   5756  C  CD    . ARG E 1 109 ? 46.199  55.438  -4.938  1.00 27.53 ?  109 ARG H CD    1 
ATOM   5757  N  NE    . ARG E 1 109 ? 45.487  54.170  -5.138  1.00 28.12 ?  109 ARG H NE    1 
ATOM   5758  C  CZ    . ARG E 1 109 ? 45.104  53.705  -6.323  1.00 31.32 ?  109 ARG H CZ    1 
ATOM   5759  N  NH1   . ARG E 1 109 ? 45.375  54.391  -7.419  1.00 30.49 1  109 ARG H NH1   1 
ATOM   5760  N  NH2   . ARG E 1 109 ? 44.457  52.556  -6.411  1.00 31.89 ?  109 ARG H NH2   1 
ATOM   5761  N  N     . ALA E 1 110 ? 45.791  57.667  -0.056  1.00 22.81 ?  110 ALA H N     1 
ATOM   5762  C  CA    . ALA E 1 110 ? 46.234  58.955  0.454   1.00 22.13 ?  110 ALA H CA    1 
ATOM   5763  C  C     . ALA E 1 110 ? 47.009  58.780  1.759   1.00 21.70 ?  110 ALA H C     1 
ATOM   5764  O  O     . ALA E 1 110 ? 47.984  59.488  1.997   1.00 22.51 ?  110 ALA H O     1 
ATOM   5765  C  CB    . ALA E 1 110 ? 45.044  59.873  0.635   1.00 21.60 ?  110 ALA H CB    1 
ATOM   5766  N  N     . LYS E 1 111 ? 46.570  57.839  2.604   1.00 24.01 ?  111 LYS H N     1 
ATOM   5767  C  CA    . LYS E 1 111 ? 47.225  57.591  3.880   1.00 28.66 ?  111 LYS H CA    1 
ATOM   5768  C  C     . LYS E 1 111 ? 48.620  57.018  3.642   1.00 27.96 ?  111 LYS H C     1 
ATOM   5769  O  O     . LYS E 1 111 ? 49.574  57.401  4.315   1.00 26.36 ?  111 LYS H O     1 
ATOM   5770  C  CB    . LYS E 1 111 ? 46.425  56.635  4.773   1.00 29.25 ?  111 LYS H CB    1 
ATOM   5771  C  CG    . LYS E 1 111 ? 45.248  57.255  5.513   1.00 33.08 ?  111 LYS H CG    1 
ATOM   5772  C  CD    . LYS E 1 111 ? 44.477  56.267  6.380   1.00 34.24 ?  111 LYS H CD    1 
ATOM   5773  C  CE    . LYS E 1 111 ? 43.178  56.815  6.881   1.00 35.85 ?  111 LYS H CE    1 
ATOM   5774  N  NZ    . LYS E 1 111 ? 43.368  57.871  7.879   1.00 38.45 1  111 LYS H NZ    1 
ATOM   5775  N  N     . ALA E 1 112 ? 48.722  56.093  2.683   1.00 27.32 ?  112 ALA H N     1 
ATOM   5776  C  CA    . ALA E 1 112 ? 49.974  55.409  2.407   1.00 27.54 ?  112 ALA H CA    1 
ATOM   5777  C  C     . ALA E 1 112 ? 50.991  56.388  1.824   1.00 27.11 ?  112 ALA H C     1 
ATOM   5778  O  O     . ALA E 1 112 ? 52.193  56.136  1.871   1.00 25.55 ?  112 ALA H O     1 
ATOM   5779  C  CB    . ALA E 1 112 ? 49.728  54.238  1.481   1.00 26.55 ?  112 ALA H CB    1 
ATOM   5780  N  N     . GLU E 1 113 ? 50.496  57.508  1.284   1.00 24.70 ?  113 GLU H N     1 
ATOM   5781  C  CA    . GLU E 1 113 ? 51.354  58.519  0.687   1.00 25.13 ?  113 GLU H CA    1 
ATOM   5782  C  C     . GLU E 1 113 ? 51.533  59.690  1.653   1.00 23.31 ?  113 GLU H C     1 
ATOM   5783  O  O     . GLU E 1 113 ? 52.049  60.738  1.271   1.00 20.30 ?  113 GLU H O     1 
ATOM   5784  C  CB    . GLU E 1 113 ? 50.795  59.012  -0.648  1.00 27.67 ?  113 GLU H CB    1 
ATOM   5785  C  CG    . GLU E 1 113 ? 50.539  57.891  -1.652  1.00 26.79 ?  113 GLU H CG    1 
ATOM   5786  C  CD    . GLU E 1 113 ? 50.229  58.373  -3.058  1.00 26.97 ?  113 GLU H CD    1 
ATOM   5787  O  OE1   . GLU E 1 113 ? 50.347  59.591  -3.306  1.00 31.06 ?  113 GLU H OE1   1 
ATOM   5788  O  OE2   . GLU E 1 113 ? 49.862  57.530  -3.902  1.00 30.47 -1 113 GLU H OE2   1 
ATOM   5789  N  N     . GLY E 1 114 ? 51.089  59.502  2.901   1.00 23.33 ?  114 GLY H N     1 
ATOM   5790  C  CA    . GLY E 1 114 ? 51.402  60.425  3.981   1.00 22.09 ?  114 GLY H CA    1 
ATOM   5791  C  C     . GLY E 1 114 ? 50.495  61.654  3.992   1.00 21.18 ?  114 GLY H C     1 
ATOM   5792  O  O     . GLY E 1 114 ? 50.855  62.680  4.564   1.00 17.99 ?  114 GLY H O     1 
ATOM   5793  N  N     . PHE E 1 115 ? 49.317  61.548  3.368   1.00 22.10 ?  115 PHE H N     1 
ATOM   5794  C  CA    . PHE E 1 115 ? 48.375  62.656  3.363   1.00 20.79 ?  115 PHE H CA    1 
ATOM   5795  C  C     . PHE E 1 115 ? 47.263  62.379  4.369   1.00 19.84 ?  115 PHE H C     1 
ATOM   5796  O  O     . PHE E 1 115 ? 46.939  61.227  4.650   1.00 21.80 ?  115 PHE H O     1 
ATOM   5797  C  CB    . PHE E 1 115 ? 47.773  62.925  1.981   1.00 20.53 ?  115 PHE H CB    1 
ATOM   5798  C  CG    . PHE E 1 115 ? 48.805  63.206  0.897   1.00 19.51 ?  115 PHE H CG    1 
ATOM   5799  C  CD1   . PHE E 1 115 ? 49.641  64.313  0.978   1.00 20.47 ?  115 PHE H CD1   1 
ATOM   5800  C  CD2   . PHE E 1 115 ? 48.918  62.374  -0.209  1.00 16.51 ?  115 PHE H CD2   1 
ATOM   5801  C  CE1   . PHE E 1 115 ? 50.580  64.563  -0.010  1.00 20.50 ?  115 PHE H CE1   1 
ATOM   5802  C  CE2   . PHE E 1 115 ? 49.854  62.632  -1.197  1.00 17.99 ?  115 PHE H CE2   1 
ATOM   5803  C  CZ    . PHE E 1 115 ? 50.683  63.725  -1.095  1.00 19.11 ?  115 PHE H CZ    1 
ATOM   5804  N  N     . SER E 1 116 ? 46.699  63.464  4.905   1.00 18.23 ?  116 SER H N     1 
ATOM   5805  C  CA    . SER E 1 116 ? 45.531  63.396  5.764   1.00 19.04 ?  116 SER H CA    1 
ATOM   5806  C  C     . SER E 1 116 ? 44.308  63.044  4.925   1.00 18.63 ?  116 SER H C     1 
ATOM   5807  O  O     . SER E 1 116 ? 44.009  63.713  3.939   1.00 16.41 ?  116 SER H O     1 
ATOM   5808  C  CB    . SER E 1 116 ? 45.320  64.696  6.496   1.00 20.07 ?  116 SER H CB    1 
ATOM   5809  O  OG    . SER E 1 116 ? 44.268  64.576  7.443   1.00 24.96 ?  116 SER H OG    1 
ATOM   5810  N  N     . ALA E 1 117 ? 43.610  61.982  5.329   1.00 16.44 ?  117 ALA H N     1 
ATOM   5811  C  CA    . ALA E 1 117 ? 42.384  61.582  4.666   1.00 16.55 ?  117 ALA H CA    1 
ATOM   5812  C  C     . ALA E 1 117 ? 41.426  61.002  5.699   1.00 16.98 ?  117 ALA H C     1 
ATOM   5813  O  O     . ALA E 1 117 ? 41.842  60.275  6.599   1.00 16.24 ?  117 ALA H O     1 
ATOM   5814  C  CB    . ALA E 1 117 ? 42.692  60.591  3.566   1.00 17.07 ?  117 ALA H CB    1 
ATOM   5815  N  N     . LYS E 1 118 ? 40.143  61.348  5.572   1.00 18.59 ?  118 LYS H N     1 
ATOM   5816  C  CA    . LYS E 1 118 ? 39.124  60.776  6.433   1.00 20.03 ?  118 LYS H CA    1 
ATOM   5817  C  C     . LYS E 1 118 ? 37.780  60.747  5.709   1.00 18.48 ?  118 LYS H C     1 
ATOM   5818  O  O     . LYS E 1 118 ? 37.613  61.336  4.643   1.00 15.23 ?  118 LYS H O     1 
ATOM   5819  C  CB    . LYS E 1 118 ? 39.090  61.483  7.795   1.00 27.28 ?  118 LYS H CB    1 
ATOM   5820  C  CG    . LYS E 1 118 ? 39.898  62.775  7.920   1.00 34.08 ?  118 LYS H CG    1 
ATOM   5821  C  CD    . LYS E 1 118 ? 39.894  63.373  9.325   1.00 40.51 ?  118 LYS H CD    1 
ATOM   5822  C  CE    . LYS E 1 118 ? 40.746  62.645  10.325  1.00 43.39 ?  118 LYS H CE    1 
ATOM   5823  N  NZ    . LYS E 1 118 ? 42.131  63.125  10.340  1.00 43.58 1  118 LYS H NZ    1 
ATOM   5824  N  N     . MET E 1 119 ? 36.836  60.015  6.309   1.00 18.25 ?  119 MET H N     1 
ATOM   5825  C  CA    . MET E 1 119 ? 35.515  59.818  5.742   1.00 21.50 ?  119 MET H CA    1 
ATOM   5826  C  C     . MET E 1 119 ? 34.471  60.348  6.718   1.00 19.70 ?  119 MET H C     1 
ATOM   5827  O  O     . MET E 1 119 ? 34.518  60.042  7.907   1.00 19.71 ?  119 MET H O     1 
ATOM   5828  C  CB    . MET E 1 119 ? 35.244  58.332  5.485   1.00 24.88 ?  119 MET H CB    1 
ATOM   5829  C  CG    . MET E 1 119 ? 33.900  58.060  4.837   1.00 27.25 ?  119 MET H CG    1 
ATOM   5830  S  SD    . MET E 1 119 ? 33.636  56.317  4.459   1.00 28.78 ?  119 MET H SD    1 
ATOM   5831  C  CE    . MET E 1 119 ? 34.741  56.139  3.052   1.00 26.85 ?  119 MET H CE    1 
ATOM   5832  N  N     . GLU E 1 120 ? 33.535  61.148  6.199   1.00 20.23 ?  120 GLU H N     1 
ATOM   5833  C  CA    . GLU E 1 120 ? 32.426  61.644  6.995   1.00 17.33 ?  120 GLU H CA    1 
ATOM   5834  C  C     . GLU E 1 120 ? 31.177  60.844  6.642   1.00 13.63 ?  120 GLU H C     1 
ATOM   5835  O  O     . GLU E 1 120 ? 30.758  60.826  5.488   1.00 12.83 ?  120 GLU H O     1 
ATOM   5836  C  CB    . GLU E 1 120 ? 32.219  63.141  6.761   1.00 18.96 ?  120 GLU H CB    1 
ATOM   5837  C  CG    . GLU E 1 120 ? 33.306  63.998  7.402   1.00 19.67 ?  120 GLU H CG    1 
ATOM   5838  C  CD    . GLU E 1 120 ? 33.362  63.861  8.912   1.00 19.48 ?  120 GLU H CD    1 
ATOM   5839  O  OE1   . GLU E 1 120 ? 32.408  63.287  9.482   1.00 23.53 ?  120 GLU H OE1   1 
ATOM   5840  O  OE2   . GLU E 1 120 ? 34.359  64.309  9.516   1.00 19.36 -1 120 GLU H OE2   1 
ATOM   5841  N  N     . PRO E 1 121 ? 30.547  60.147  7.614   1.00 12.54 ?  121 PRO H N     1 
ATOM   5842  C  CA    . PRO E 1 121 ? 29.378  59.325  7.311   1.00 13.55 ?  121 PRO H CA    1 
ATOM   5843  C  C     . PRO E 1 121 ? 28.245  60.185  6.760   1.00 14.77 ?  121 PRO H C     1 
ATOM   5844  O  O     . PRO E 1 121 ? 28.155  61.375  7.054   1.00 16.65 ?  121 PRO H O     1 
ATOM   5845  C  CB    . PRO E 1 121 ? 29.033  58.661  8.652   1.00 13.18 ?  121 PRO H CB    1 
ATOM   5846  C  CG    . PRO E 1 121 ? 29.636  59.589  9.685   1.00 12.83 ?  121 PRO H CG    1 
ATOM   5847  C  CD    . PRO E 1 121 ? 30.909  60.116  9.040   1.00 12.07 ?  121 PRO H CD    1 
ATOM   5848  N  N     . GLY E 1 122 ? 27.401  59.555  5.940   1.00 15.07 ?  122 GLY H N     1 
ATOM   5849  C  CA    . GLY E 1 122 ? 26.283  60.225  5.302   1.00 16.25 ?  122 GLY H CA    1 
ATOM   5850  C  C     . GLY E 1 122 ? 25.029  59.366  5.409   1.00 15.38 ?  122 GLY H C     1 
ATOM   5851  O  O     . GLY E 1 122 ? 25.049  58.324  6.060   1.00 15.68 ?  122 GLY H O     1 
ATOM   5852  N  N     . ILE E 1 123 ? 23.947  59.812  4.765   1.00 14.94 ?  123 ILE H N     1 
ATOM   5853  C  CA    . ILE E 1 123 ? 22.687  59.090  4.796   1.00 15.10 ?  123 ILE H CA    1 
ATOM   5854  C  C     . ILE E 1 123 ? 22.595  58.228  3.540   1.00 16.44 ?  123 ILE H C     1 
ATOM   5855  O  O     . ILE E 1 123 ? 22.751  58.729  2.429   1.00 17.25 ?  123 ILE H O     1 
ATOM   5856  C  CB    . ILE E 1 123 ? 21.499  60.064  4.920   1.00 13.63 ?  123 ILE H CB    1 
ATOM   5857  C  CG1   . ILE E 1 123 ? 21.510  60.812  6.255   1.00 14.16 ?  123 ILE H CG1   1 
ATOM   5858  C  CG2   . ILE E 1 123 ? 20.175  59.334  4.702   1.00 13.00 ?  123 ILE H CG2   1 
ATOM   5859  C  CD1   . ILE E 1 123 ? 20.429  61.871  6.380   1.00 14.52 ?  123 ILE H CD1   1 
ATOM   5860  N  N     . SER E 1 124 ? 22.332  56.930  3.730   1.00 17.29 ?  124 SER H N     1 
ATOM   5861  C  CA    . SER E 1 124 ? 22.401  55.965  2.645   1.00 17.69 ?  124 SER H CA    1 
ATOM   5862  C  C     . SER E 1 124 ? 21.002  55.525  2.222   1.00 18.92 ?  124 SER H C     1 
ATOM   5863  O  O     . SER E 1 124 ? 20.015  55.842  2.884   1.00 18.28 ?  124 SER H O     1 
ATOM   5864  C  CB    . SER E 1 124 ? 23.234  54.774  3.038   1.00 16.45 ?  124 SER H CB    1 
ATOM   5865  O  OG    . SER E 1 124 ? 22.548  53.969  3.987   1.00 16.70 ?  124 SER H OG    1 
ATOM   5866  N  N     . ALA E 1 125 ? 20.945  54.766  1.122   1.00 18.96 ?  125 ALA H N     1 
ATOM   5867  C  CA    . ALA E 1 125 ? 19.690  54.274  0.576   1.00 18.98 ?  125 ALA H CA    1 
ATOM   5868  C  C     . ALA E 1 125 ? 19.041  53.307  1.561   1.00 17.70 ?  125 ALA H C     1 
ATOM   5869  O  O     . ALA E 1 125 ? 17.825  53.130  1.557   1.00 18.92 ?  125 ALA H O     1 
ATOM   5870  C  CB    . ALA E 1 125 ? 19.932  53.616  -0.766  1.00 16.79 ?  125 ALA H CB    1 
ATOM   5871  N  N     . GLU E 1 126 ? 19.877  52.685  2.397   1.00 17.24 ?  126 GLU H N     1 
ATOM   5872  C  CA    . GLU E 1 126 ? 19.429  51.749  3.414   1.00 17.09 ?  126 GLU H CA    1 
ATOM   5873  C  C     . GLU E 1 126 ? 18.772  52.516  4.557   1.00 16.05 ?  126 GLU H C     1 
ATOM   5874  O  O     . GLU E 1 126 ? 17.726  52.118  5.065   1.00 16.30 ?  126 GLU H O     1 
ATOM   5875  C  CB    . GLU E 1 126 ? 20.641  50.982  3.940   1.00 20.54 ?  126 GLU H CB    1 
ATOM   5876  C  CG    . GLU E 1 126 ? 20.276  49.843  4.886   1.00 22.77 ?  126 GLU H CG    1 
ATOM   5877  C  CD    . GLU E 1 126 ? 21.467  49.203  5.574   1.00 25.02 ?  126 GLU H CD    1 
ATOM   5878  O  OE1   . GLU E 1 126 ? 22.469  48.910  4.890   1.00 28.16 ?  126 GLU H OE1   1 
ATOM   5879  O  OE2   . GLU E 1 126 ? 21.381  48.981  6.798   1.00 30.98 -1 126 GLU H OE2   1 
ATOM   5880  N  N     . ALA E 1 127 ? 19.425  53.608  4.965   1.00 14.83 ?  127 ALA H N     1 
ATOM   5881  C  CA    . ALA E 1 127 ? 18.872  54.520  5.951   1.00 15.83 ?  127 ALA H CA    1 
ATOM   5882  C  C     . ALA E 1 127 ? 17.506  55.010  5.476   1.00 14.04 ?  127 ALA H C     1 
ATOM   5883  O  O     . ALA E 1 127 ? 16.550  55.057  6.245   1.00 14.38 ?  127 ALA H O     1 
ATOM   5884  C  CB    . ALA E 1 127 ? 19.833  55.668  6.175   1.00 14.68 ?  127 ALA H CB    1 
ATOM   5885  N  N     . CYS E 1 128 ? 17.434  55.358  4.189   1.00 13.85 ?  128 CYS H N     1 
ATOM   5886  C  CA    . CYS E 1 128 ? 16.219  55.873  3.581   1.00 12.33 ?  128 CYS H CA    1 
ATOM   5887  C  C     . CYS E 1 128 ? 15.117  54.814  3.614   1.00 13.63 ?  128 CYS H C     1 
ATOM   5888  O  O     . CYS E 1 128 ? 13.960  55.143  3.869   1.00 10.92 ?  128 CYS H O     1 
ATOM   5889  C  CB    . CYS E 1 128 ? 16.502  56.360  2.165   1.00 13.43 ?  128 CYS H CB    1 
ATOM   5890  S  SG    . CYS E 1 128 ? 17.375  57.948  2.106   1.00 17.25 ?  128 CYS H SG    1 
ATOM   5891  N  N     . LEU E 1 129 ? 15.491  53.548  3.373   1.00 13.81 ?  129 LEU H N     1 
ATOM   5892  C  CA    . LEU E 1 129 ? 14.535  52.458  3.228   1.00 15.19 ?  129 LEU H CA    1 
ATOM   5893  C  C     . LEU E 1 129 ? 13.774  52.249  4.536   1.00 16.65 ?  129 LEU H C     1 
ATOM   5894  O  O     . LEU E 1 129 ? 12.545  52.228  4.547   1.00 18.15 ?  129 LEU H O     1 
ATOM   5895  C  CB    . LEU E 1 129 ? 15.265  51.191  2.775   1.00 17.03 ?  129 LEU H CB    1 
ATOM   5896  C  CG    . LEU E 1 129 ? 14.411  49.930  2.591   1.00 16.09 ?  129 LEU H CG    1 
ATOM   5897  C  CD1   . LEU E 1 129 ? 15.008  49.015  1.532   1.00 16.22 ?  129 LEU H CD1   1 
ATOM   5898  C  CD2   . LEU E 1 129 ? 14.262  49.167  3.896   1.00 16.84 ?  129 LEU H CD2   1 
ATOM   5899  N  N     . TRP E 1 130 ? 14.516  52.094  5.636   1.00 16.78 ?  130 TRP H N     1 
ATOM   5900  C  CA    . TRP E 1 130 ? 13.927  51.895  6.950   1.00 18.85 ?  130 TRP H CA    1 
ATOM   5901  C  C     . TRP E 1 130 ? 12.807  52.908  7.187   1.00 21.42 ?  130 TRP H C     1 
ATOM   5902  O  O     . TRP E 1 130 ? 11.735  52.549  7.671   1.00 23.86 ?  130 TRP H O     1 
ATOM   5903  C  CB    . TRP E 1 130 ? 15.008  52.011  8.035   1.00 18.76 ?  130 TRP H CB    1 
ATOM   5904  C  CG    . TRP E 1 130 ? 16.180  51.082  7.851   1.00 21.15 ?  130 TRP H CG    1 
ATOM   5905  C  CD1   . TRP E 1 130 ? 17.497  51.402  8.002   1.00 20.37 ?  130 TRP H CD1   1 
ATOM   5906  C  CD2   . TRP E 1 130 ? 16.147  49.679  7.504   1.00 22.36 ?  130 TRP H CD2   1 
ATOM   5907  N  NE1   . TRP E 1 130 ? 18.285  50.309  7.763   1.00 21.82 ?  130 TRP H NE1   1 
ATOM   5908  C  CE2   . TRP E 1 130 ? 17.488  49.237  7.458   1.00 22.84 ?  130 TRP H CE2   1 
ATOM   5909  C  CE3   . TRP E 1 130 ? 15.128  48.761  7.227   1.00 21.30 ?  130 TRP H CE3   1 
ATOM   5910  C  CZ2   . TRP E 1 130 ? 17.829  47.923  7.148   1.00 23.47 ?  130 TRP H CZ2   1 
ATOM   5911  C  CZ3   . TRP E 1 130 ? 15.468  47.461  6.921   1.00 23.76 ?  130 TRP H CZ3   1 
ATOM   5912  C  CH2   . TRP E 1 130 ? 16.799  47.050  6.884   1.00 23.76 ?  130 TRP H CH2   1 
ATOM   5913  N  N     . ALA E 1 131 ? 13.075  54.173  6.839   1.00 20.66 ?  131 ALA H N     1 
ATOM   5914  C  CA    . ALA E 1 131 ? 12.160  55.273  7.103   1.00 20.55 ?  131 ALA H CA    1 
ATOM   5915  C  C     . ALA E 1 131 ? 10.946  55.216  6.174   1.00 21.86 ?  131 ALA H C     1 
ATOM   5916  O  O     . ALA E 1 131 ? 9.819   55.416  6.619   1.00 22.94 ?  131 ALA H O     1 
ATOM   5917  C  CB    . ALA E 1 131 ? 12.896  56.589  6.968   1.00 18.91 ?  131 ALA H CB    1 
ATOM   5918  N  N     . ASP E 1 132 ? 11.183  54.950  4.884   1.00 22.13 ?  132 ASP H N     1 
ATOM   5919  C  CA    . ASP E 1 132 ? 10.128  54.998  3.883   1.00 19.81 ?  132 ASP H CA    1 
ATOM   5920  C  C     . ASP E 1 132 ? 9.180   53.814  4.053   1.00 19.47 ?  132 ASP H C     1 
ATOM   5921  O  O     . ASP E 1 132 ? 7.991   53.925  3.759   1.00 21.28 ?  132 ASP H O     1 
ATOM   5922  C  CB    . ASP E 1 132 ? 10.701  55.055  2.477   1.00 18.37 ?  132 ASP H CB    1 
ATOM   5923  C  CG    . ASP E 1 132 ? 11.431  56.345  2.135   1.00 18.70 ?  132 ASP H CG    1 
ATOM   5924  O  OD1   . ASP E 1 132 ? 11.469  57.242  3.004   1.00 27.88 ?  132 ASP H OD1   1 
ATOM   5925  O  OD2   . ASP E 1 132 ? 11.946  56.447  1.005   1.00 17.72 -1 132 ASP H OD2   1 
ATOM   5926  N  N     . LEU E 1 133 ? 9.712   52.681  4.522   1.00 19.24 ?  133 LEU H N     1 
ATOM   5927  C  CA    . LEU E 1 133 ? 8.913   51.477  4.679   1.00 19.91 ?  133 LEU H CA    1 
ATOM   5928  C  C     . LEU E 1 133 ? 8.530   51.289  6.143   1.00 20.64 ?  133 LEU H C     1 
ATOM   5929  O  O     . LEU E 1 133 ? 7.922   50.282  6.500   1.00 21.38 ?  133 LEU H O     1 
ATOM   5930  C  CB    . LEU E 1 133 ? 9.667   50.261  4.144   1.00 21.00 ?  133 LEU H CB    1 
ATOM   5931  C  CG    . LEU E 1 133 ? 9.650   50.085  2.622   1.00 22.19 ?  133 LEU H CG    1 
ATOM   5932  C  CD1   . LEU E 1 133 ? 10.401  51.210  1.932   1.00 23.23 ?  133 LEU H CD1   1 
ATOM   5933  C  CD2   . LEU E 1 133 ? 10.219  48.734  2.223   1.00 24.94 ?  133 LEU H CD2   1 
ATOM   5934  N  N     . GLY E 1 134 ? 8.888   52.263  6.984   1.00 19.86 ?  134 GLY H N     1 
ATOM   5935  C  CA    . GLY E 1 134 ? 8.582   52.189  8.402   1.00 19.61 ?  134 GLY H CA    1 
ATOM   5936  C  C     . GLY E 1 134 ? 9.008   50.844  8.986   1.00 21.23 ?  134 GLY H C     1 
ATOM   5937  O  O     . GLY E 1 134 ? 8.243   50.206  9.707   1.00 21.40 ?  134 GLY H O     1 
ATOM   5938  N  N     . ILE E 1 135 ? 10.237  50.428  8.657   1.00 22.00 ?  135 ILE H N     1 
ATOM   5939  C  CA    . ILE E 1 135 ? 10.808  49.194  9.172   1.00 23.40 ?  135 ILE H CA    1 
ATOM   5940  C  C     . ILE E 1 135 ? 12.035  49.525  10.016  1.00 24.86 ?  135 ILE H C     1 
ATOM   5941  O  O     . ILE E 1 135 ? 12.895  50.300  9.603   1.00 25.38 ?  135 ILE H O     1 
ATOM   5942  C  CB    . ILE E 1 135 ? 11.172  48.224  8.032   1.00 24.14 ?  135 ILE H CB    1 
ATOM   5943  C  CG1   . ILE E 1 135 ? 9.976   47.936  7.128   1.00 23.93 ?  135 ILE H CG1   1 
ATOM   5944  C  CG2   . ILE E 1 135 ? 11.783  46.936  8.587   1.00 25.40 ?  135 ILE H CG2   1 
ATOM   5945  C  CD1   . ILE E 1 135 ? 10.312  47.093  5.912   1.00 23.50 ?  135 ILE H CD1   1 
ATOM   5946  N  N     . ASP E 1 136 ? 12.098  48.910  11.199  1.00 28.73 ?  136 ASP H N     1 
ATOM   5947  C  CA    . ASP E 1 136 ? 13.239  49.029  12.090  1.00 30.59 ?  136 ASP H CA    1 
ATOM   5948  C  C     . ASP E 1 136 ? 14.141  47.814  11.883  1.00 29.72 ?  136 ASP H C     1 
ATOM   5949  O  O     . ASP E 1 136 ? 13.750  46.692  12.196  1.00 23.41 ?  136 ASP H O     1 
ATOM   5950  C  CB    . ASP E 1 136 ? 12.762  49.170  13.527  1.00 33.79 ?  136 ASP H CB    1 
ATOM   5951  C  CG    . ASP E 1 136 ? 13.849  49.272  14.587  1.00 33.75 ?  136 ASP H CG    1 
ATOM   5952  O  OD1   . ASP E 1 136 ? 15.040  49.233  14.212  1.00 32.83 ?  136 ASP H OD1   1 
ATOM   5953  O  OD2   . ASP E 1 136 ? 13.492  49.388  15.780  1.00 34.91 -1 136 ASP H OD2   1 
ATOM   5954  N  N     . PRO E 1 137 ? 15.371  47.987  11.343  1.00 28.73 ?  137 PRO H N     1 
ATOM   5955  C  CA    . PRO E 1 137 ? 16.244  46.850  11.049  1.00 25.91 ?  137 PRO H CA    1 
ATOM   5956  C  C     . PRO E 1 137 ? 16.407  45.927  12.254  1.00 28.20 ?  137 PRO H C     1 
ATOM   5957  O  O     . PRO E 1 137 ? 16.618  44.725  12.101  1.00 28.76 ?  137 PRO H O     1 
ATOM   5958  C  CB    . PRO E 1 137 ? 17.579  47.495  10.621  1.00 25.83 ?  137 PRO H CB    1 
ATOM   5959  C  CG    . PRO E 1 137 ? 17.470  48.943  11.063  1.00 26.14 ?  137 PRO H CG    1 
ATOM   5960  C  CD    . PRO E 1 137 ? 15.990  49.278  11.006  1.00 25.48 ?  137 PRO H CD    1 
ATOM   5961  N  N     . GLY E 1 138 ? 16.297  46.508  13.452  1.00 23.49 ?  138 GLY H N     1 
ATOM   5962  C  CA    . GLY E 1 138 ? 16.490  45.769  14.687  1.00 23.56 ?  138 GLY H CA    1 
ATOM   5963  C  C     . GLY E 1 138 ? 15.289  44.889  15.024  1.00 24.22 ?  138 GLY H C     1 
ATOM   5964  O  O     . GLY E 1 138 ? 15.386  44.020  15.888  1.00 21.73 ?  138 GLY H O     1 
ATOM   5965  N  N     . ASN E 1 139 ? 14.162  45.112  14.338  1.00 24.94 ?  139 ASN H N     1 
ATOM   5966  C  CA    . ASN E 1 139 ? 12.935  44.401  14.659  1.00 27.22 ?  139 ASN H CA    1 
ATOM   5967  C  C     . ASN E 1 139 ? 13.211  42.900  14.644  1.00 27.06 ?  139 ASN H C     1 
ATOM   5968  O  O     . ASN E 1 139 ? 13.006  42.221  15.647  1.00 27.38 ?  139 ASN H O     1 
ATOM   5969  C  CB    . ASN E 1 139 ? 11.780  44.765  13.732  1.00 28.79 ?  139 ASN H CB    1 
ATOM   5970  C  CG    . ASN E 1 139 ? 10.470  44.200  14.230  1.00 28.73 ?  139 ASN H CG    1 
ATOM   5971  O  OD1   . ASN E 1 139 ? 10.143  44.342  15.413  1.00 32.52 ?  139 ASN H OD1   1 
ATOM   5972  N  ND2   . ASN E 1 139 ? 9.715   43.548  13.358  1.00 31.07 ?  139 ASN H ND2   1 
ATOM   5973  N  N     . SER E 1 140 ? 13.678  42.391  13.498  1.00 25.41 ?  140 SER H N     1 
ATOM   5974  C  CA    . SER E 1 140 ? 14.025  40.984  13.385  1.00 23.03 ?  140 SER H CA    1 
ATOM   5975  C  C     . SER E 1 140 ? 15.450  40.813  12.856  1.00 21.14 ?  140 SER H C     1 
ATOM   5976  O  O     . SER E 1 140 ? 15.892  39.687  12.640  1.00 24.94 ?  140 SER H O     1 
ATOM   5977  C  CB    . SER E 1 140 ? 13.031  40.241  12.525  1.00 21.31 ?  140 SER H CB    1 
ATOM   5978  O  OG    . SER E 1 140 ? 12.920  40.828  11.236  1.00 18.61 ?  140 SER H OG    1 
ATOM   5979  N  N     . GLY E 1 141 ? 16.167  41.927  12.657  1.00 19.51 ?  141 GLY H N     1 
ATOM   5980  C  CA    . GLY E 1 141 ? 17.538  41.879  12.169  1.00 19.71 ?  141 GLY H CA    1 
ATOM   5981  C  C     . GLY E 1 141 ? 17.632  42.298  10.702  1.00 20.01 ?  141 GLY H C     1 
ATOM   5982  O  O     . GLY E 1 141 ? 16.631  42.272  9.987   1.00 19.06 ?  141 GLY H O     1 
ATOM   5983  N  N     . HIS E 1 142 ? 18.848  42.672  10.272  1.00 20.54 ?  142 HIS H N     1 
ATOM   5984  C  CA    . HIS E 1 142 ? 19.106  43.160  8.922   1.00 22.28 ?  142 HIS H CA    1 
ATOM   5985  C  C     . HIS E 1 142 ? 20.243  42.384  8.256   1.00 22.18 ?  142 HIS H C     1 
ATOM   5986  O  O     . HIS E 1 142 ? 21.254  42.095  8.891   1.00 20.59 ?  142 HIS H O     1 
ATOM   5987  C  CB    . HIS E 1 142 ? 19.535  44.634  8.919   1.00 22.84 ?  142 HIS H CB    1 
ATOM   5988  C  CG    . HIS E 1 142 ? 19.873  45.101  7.541   1.00 26.69 ?  142 HIS H CG    1 
ATOM   5989  N  ND1   . HIS E 1 142 ? 20.935  45.897  7.161   1.00 28.86 ?  142 HIS H ND1   1 
ATOM   5990  C  CD2   . HIS E 1 142 ? 19.227  44.787  6.414   1.00 29.39 ?  142 HIS H CD2   1 
ATOM   5991  C  CE1   . HIS E 1 142 ? 20.902  46.066  5.844   1.00 31.92 ?  142 HIS H CE1   1 
ATOM   5992  N  NE2   . HIS E 1 142 ? 19.871  45.400  5.372   1.00 32.56 ?  142 HIS H NE2   1 
ATOM   5993  N  N     . GLN E 1 143 ? 20.081  42.095  6.957   1.00 24.27 ?  143 GLN H N     1 
ATOM   5994  C  CA    . GLN E 1 143 ? 21.129  41.499  6.140   1.00 25.76 ?  143 GLN H CA    1 
ATOM   5995  C  C     . GLN E 1 143 ? 21.215  42.224  4.797   1.00 19.94 ?  143 GLN H C     1 
ATOM   5996  O  O     . GLN E 1 143 ? 20.195  42.443  4.148   1.00 20.64 ?  143 GLN H O     1 
ATOM   5997  C  CB    . GLN E 1 143 ? 20.850  40.029  5.822   1.00 27.77 ?  143 GLN H CB    1 
ATOM   5998  C  CG    . GLN E 1 143 ? 20.830  39.096  7.028   1.00 30.18 ?  143 GLN H CG    1 
ATOM   5999  C  CD    . GLN E 1 143 ? 20.589  37.655  6.635   1.00 32.46 ?  143 GLN H CD    1 
ATOM   6000  O  OE1   . GLN E 1 143 ? 21.346  36.747  6.998   1.00 39.81 ?  143 GLN H OE1   1 
ATOM   6001  N  NE2   . GLN E 1 143 ? 19.526  37.433  5.876   1.00 35.28 ?  143 GLN H NE2   1 
ATOM   6002  N  N     . SER E 1 144 ? 22.441  42.559  4.374   1.00 16.51 ?  144 SER H N     1 
ATOM   6003  C  CA    . SER E 1 144 ? 22.671  43.210  3.091   1.00 17.27 ?  144 SER H CA    1 
ATOM   6004  C  C     . SER E 1 144 ? 23.745  42.474  2.292   1.00 16.53 ?  144 SER H C     1 
ATOM   6005  O  O     . SER E 1 144 ? 24.746  42.031  2.848   1.00 20.32 ?  144 SER H O     1 
ATOM   6006  C  CB    . SER E 1 144 ? 23.052  44.662  3.267   1.00 16.46 ?  144 SER H CB    1 
ATOM   6007  O  OG    . SER E 1 144 ? 21.907  45.478  3.475   1.00 19.34 ?  144 SER H OG    1 
ATOM   6008  N  N     . PHE E 1 145 ? 23.527  42.378  0.974   1.00 14.66 ?  145 PHE H N     1 
ATOM   6009  C  CA    . PHE E 1 145 ? 24.518  41.843  0.056   1.00 14.59 ?  145 PHE H CA    1 
ATOM   6010  C  C     . PHE E 1 145 ? 24.320  42.466  -1.323  1.00 15.52 ?  145 PHE H C     1 
ATOM   6011  O  O     . PHE E 1 145 ? 23.192  42.622  -1.784  1.00 14.12 ?  145 PHE H O     1 
ATOM   6012  C  CB    . PHE E 1 145 ? 24.432  40.327  -0.155  1.00 14.70 ?  145 PHE H CB    1 
ATOM   6013  C  CG    . PHE E 1 145 ? 24.368  39.446  1.086   1.00 15.56 ?  145 PHE H CG    1 
ATOM   6014  C  CD1   . PHE E 1 145 ? 25.526  39.044  1.744   1.00 14.65 ?  145 PHE H CD1   1 
ATOM   6015  C  CD2   . PHE E 1 145 ? 23.147  38.974  1.555   1.00 14.14 ?  145 PHE H CD2   1 
ATOM   6016  C  CE1   . PHE E 1 145 ? 25.457  38.220  2.857   1.00 15.79 ?  145 PHE H CE1   1 
ATOM   6017  C  CE2   . PHE E 1 145 ? 23.085  38.154  2.670   1.00 13.83 ?  145 PHE H CE2   1 
ATOM   6018  C  CZ    . PHE E 1 145 ? 24.238  37.778  3.317   1.00 15.30 ?  145 PHE H CZ    1 
ATOM   6019  N  N     . GLU E 1 146 ? 25.435  42.798  -1.980  1.00 17.31 ?  146 GLU H N     1 
ATOM   6020  C  CA    . GLU E 1 146 ? 25.432  43.096  -3.401  1.00 17.55 ?  146 GLU H CA    1 
ATOM   6021  C  C     . GLU E 1 146 ? 24.858  41.879  -4.126  1.00 18.60 ?  146 GLU H C     1 
ATOM   6022  O  O     . GLU E 1 146 ? 25.224  40.746  -3.818  1.00 21.90 ?  146 GLU H O     1 
ATOM   6023  C  CB    . GLU E 1 146 ? 26.865  43.451  -3.801  1.00 18.89 ?  146 GLU H CB    1 
ATOM   6024  C  CG    . GLU E 1 146 ? 26.964  44.386  -5.003  1.00 19.16 ?  146 GLU H CG    1 
ATOM   6025  C  CD    . GLU E 1 146 ? 26.752  43.730  -6.353  1.00 21.54 ?  146 GLU H CD    1 
ATOM   6026  O  OE1   . GLU E 1 146 ? 26.757  42.481  -6.429  1.00 23.12 ?  146 GLU H OE1   1 
ATOM   6027  O  OE2   . GLU E 1 146 ? 26.579  44.483  -7.333  1.00 20.72 -1 146 GLU H OE2   1 
ATOM   6028  N  N     . ALA E 1 147 ? 23.943  42.121  -5.072  1.00 16.49 ?  147 ALA H N     1 
ATOM   6029  C  CA    . ALA E 1 147 ? 23.124  41.067  -5.652  1.00 18.35 ?  147 ALA H CA    1 
ATOM   6030  C  C     . ALA E 1 147 ? 23.979  40.025  -6.374  1.00 19.62 ?  147 ALA H C     1 
ATOM   6031  O  O     . ALA E 1 147 ? 23.670  38.835  -6.335  1.00 18.42 ?  147 ALA H O     1 
ATOM   6032  C  CB    . ALA E 1 147 ? 22.100  41.673  -6.587  1.00 18.04 ?  147 ALA H CB    1 
ATOM   6033  N  N     . SER E 1 148 ? 25.045  40.482  -7.039  1.00 21.95 ?  148 SER H N     1 
ATOM   6034  C  CA    . SER E 1 148 ? 25.853  39.624  -7.892  1.00 24.34 ?  148 SER H CA    1 
ATOM   6035  C  C     . SER E 1 148 ? 26.793  38.768  -7.048  1.00 24.41 ?  148 SER H C     1 
ATOM   6036  O  O     . SER E 1 148 ? 27.042  37.608  -7.372  1.00 23.66 ?  148 SER H O     1 
ATOM   6037  C  CB    . SER E 1 148 ? 26.620  40.433  -8.908  1.00 25.96 ?  148 SER H CB    1 
ATOM   6038  O  OG    . SER E 1 148 ? 25.745  41.009  -9.868  1.00 27.92 ?  148 SER H OG    1 
ATOM   6039  N  N     . GLN E 1 149 ? 27.316  39.358  -5.969  1.00 23.54 ?  149 GLN H N     1 
ATOM   6040  C  CA    . GLN E 1 149 ? 28.207  38.653  -5.065  1.00 23.72 ?  149 GLN H CA    1 
ATOM   6041  C  C     . GLN E 1 149 ? 27.415  37.573  -4.336  1.00 21.89 ?  149 GLN H C     1 
ATOM   6042  O  O     . GLN E 1 149 ? 27.975  36.574  -3.892  1.00 27.62 ?  149 GLN H O     1 
ATOM   6043  C  CB    . GLN E 1 149 ? 28.835  39.614  -4.057  1.00 25.40 ?  149 GLN H CB    1 
ATOM   6044  C  CG    . GLN E 1 149 ? 29.773  38.934  -3.066  1.00 25.35 ?  149 GLN H CG    1 
ATOM   6045  C  CD    . GLN E 1 149 ? 30.064  39.782  -1.848  1.00 23.35 ?  149 GLN H CD    1 
ATOM   6046  O  OE1   . GLN E 1 149 ? 29.499  39.575  -0.769  1.00 22.76 ?  149 GLN H OE1   1 
ATOM   6047  N  NE2   . GLN E 1 149 ? 30.937  40.765  -2.016  1.00 24.57 ?  149 GLN H NE2   1 
ATOM   6048  N  N     . PHE E 1 150 ? 26.104  37.800  -4.218  1.00 17.37 ?  150 PHE H N     1 
ATOM   6049  C  CA    . PHE E 1 150 ? 25.204  36.837  -3.612  1.00 16.40 ?  150 PHE H CA    1 
ATOM   6050  C  C     . PHE E 1 150 ? 25.042  35.638  -4.541  1.00 18.30 ?  150 PHE H C     1 
ATOM   6051  O  O     . PHE E 1 150 ? 24.804  34.520  -4.089  1.00 15.95 ?  150 PHE H O     1 
ATOM   6052  C  CB    . PHE E 1 150 ? 23.842  37.478  -3.336  1.00 15.42 ?  150 PHE H CB    1 
ATOM   6053  C  CG    . PHE E 1 150 ? 22.887  36.537  -2.616  1.00 14.47 ?  150 PHE H CG    1 
ATOM   6054  C  CD1   . PHE E 1 150 ? 22.175  35.572  -3.319  1.00 11.83 ?  150 PHE H CD1   1 
ATOM   6055  C  CD2   . PHE E 1 150 ? 22.729  36.602  -1.237  1.00 14.04 ?  150 PHE H CD2   1 
ATOM   6056  C  CE1   . PHE E 1 150 ? 21.317  34.708  -2.660  1.00 12.75 ?  150 PHE H CE1   1 
ATOM   6057  C  CE2   . PHE E 1 150 ? 21.869  35.734  -0.584  1.00 13.36 ?  150 PHE H CE2   1 
ATOM   6058  C  CZ    . PHE E 1 150 ? 21.165  34.792  -1.296  1.00 13.42 ?  150 PHE H CZ    1 
ATOM   6059  N  N     . MET E 1 151 ? 25.159  35.893  -5.848  1.00 19.37 ?  151 MET H N     1 
ATOM   6060  C  CA    . MET E 1 151 ? 24.974  34.860  -6.852  1.00 19.93 ?  151 MET H CA    1 
ATOM   6061  C  C     . MET E 1 151 ? 26.296  34.139  -7.098  1.00 19.02 ?  151 MET H C     1 
ATOM   6062  O  O     . MET E 1 151 ? 26.317  32.923  -7.268  1.00 20.41 ?  151 MET H O     1 
ATOM   6063  C  CB    . MET E 1 151 ? 24.457  35.452  -8.169  1.00 18.84 ?  151 MET H CB    1 
ATOM   6064  C  CG    . MET E 1 151 ? 23.026  35.943  -8.096  1.00 18.30 ?  151 MET H CG    1 
ATOM   6065  S  SD    . MET E 1 151 ? 22.371  36.506  -9.680  1.00 20.33 ?  151 MET H SD    1 
ATOM   6066  C  CE    . MET E 1 151 ? 22.091  34.956  -10.549 1.00 19.92 ?  151 MET H CE    1 
ATOM   6067  N  N     . PHE E 1 152 ? 27.392  34.904  -7.094  1.00 20.72 ?  152 PHE H N     1 
ATOM   6068  C  CA    . PHE E 1 152 ? 28.688  34.403  -7.522  1.00 20.76 ?  152 PHE H CA    1 
ATOM   6069  C  C     . PHE E 1 152 ? 29.382  33.661  -6.384  1.00 23.80 ?  152 PHE H C     1 
ATOM   6070  O  O     . PHE E 1 152 ? 30.181  32.759  -6.630  1.00 25.98 ?  152 PHE H O     1 
ATOM   6071  C  CB    . PHE E 1 152 ? 29.555  35.564  -8.015  1.00 19.99 ?  152 PHE H CB    1 
ATOM   6072  C  CG    . PHE E 1 152 ? 28.982  36.292  -9.222  1.00 19.23 ?  152 PHE H CG    1 
ATOM   6073  C  CD1   . PHE E 1 152 ? 28.030  35.683  -10.032 1.00 18.94 ?  152 PHE H CD1   1 
ATOM   6074  C  CD2   . PHE E 1 152 ? 29.406  37.574  -9.552  1.00 18.44 ?  152 PHE H CD2   1 
ATOM   6075  C  CE1   . PHE E 1 152 ? 27.511  36.344  -11.134 1.00 21.13 ?  152 PHE H CE1   1 
ATOM   6076  C  CE2   . PHE E 1 152 ? 28.884  38.229  -10.656 1.00 19.87 ?  152 PHE H CE2   1 
ATOM   6077  C  CZ    . PHE E 1 152 ? 27.938  37.613  -11.443 1.00 19.51 ?  152 PHE H CZ    1 
ATOM   6078  N  N     . PHE E 1 153 ? 29.082  34.054  -5.143  1.00 23.09 ?  153 PHE H N     1 
ATOM   6079  C  CA    . PHE E 1 153 ? 29.787  33.515  -3.994  1.00 22.69 ?  153 PHE H CA    1 
ATOM   6080  C  C     . PHE E 1 153 ? 28.788  32.863  -3.043  1.00 23.85 ?  153 PHE H C     1 
ATOM   6081  O  O     . PHE E 1 153 ? 27.578  32.962  -3.231  1.00 24.34 ?  153 PHE H O     1 
ATOM   6082  C  CB    . PHE E 1 153 ? 30.610  34.626  -3.333  1.00 24.18 ?  153 PHE H CB    1 
ATOM   6083  C  CG    . PHE E 1 153 ? 31.707  35.217  -4.210  1.00 23.81 ?  153 PHE H CG    1 
ATOM   6084  C  CD1   . PHE E 1 153 ? 32.934  34.576  -4.345  1.00 25.57 ?  153 PHE H CD1   1 
ATOM   6085  C  CD2   . PHE E 1 153 ? 31.516  36.418  -4.886  1.00 26.70 ?  153 PHE H CD2   1 
ATOM   6086  C  CE1   . PHE E 1 153 ? 33.933  35.117  -5.141  1.00 24.07 ?  153 PHE H CE1   1 
ATOM   6087  C  CE2   . PHE E 1 153 ? 32.518  36.953  -5.680  1.00 23.38 ?  153 PHE H CE2   1 
ATOM   6088  C  CZ    . PHE E 1 153 ? 33.724  36.303  -5.804  1.00 25.68 ?  153 PHE H CZ    1 
ATOM   6089  N  N     . ASN E 1 154 ? 29.325  32.193  -2.018  1.00 29.28 ?  154 ASN H N     1 
ATOM   6090  C  CA    . ASN E 1 154 ? 28.522  31.403  -1.102  1.00 29.74 ?  154 ASN H CA    1 
ATOM   6091  C  C     . ASN E 1 154 ? 28.015  32.302  0.022   1.00 34.01 ?  154 ASN H C     1 
ATOM   6092  O  O     . ASN E 1 154 ? 28.768  32.674  0.921   1.00 29.69 ?  154 ASN H O     1 
ATOM   6093  C  CB    . ASN E 1 154 ? 29.297  30.207  -0.559  1.00 31.70 ?  154 ASN H CB    1 
ATOM   6094  C  CG    . ASN E 1 154 ? 29.728  29.246  -1.644  1.00 31.66 ?  154 ASN H CG    1 
ATOM   6095  O  OD1   . ASN E 1 154 ? 28.896  28.774  -2.427  1.00 29.20 ?  154 ASN H OD1   1 
ATOM   6096  N  ND2   . ASN E 1 154 ? 31.014  28.934  -1.702  1.00 34.50 ?  154 ASN H ND2   1 
ATOM   6097  N  N     . HIS E 1 155 ? 26.727  32.649  -0.056  1.00 29.28 ?  155 HIS H N     1 
ATOM   6098  C  CA    . HIS E 1 155 ? 26.052  33.374  1.005   1.00 29.20 ?  155 HIS H CA    1 
ATOM   6099  C  C     . HIS E 1 155 ? 24.775  32.627  1.373   1.00 30.90 ?  155 HIS H C     1 
ATOM   6100  O  O     . HIS E 1 155 ? 24.055  32.147  0.500   1.00 31.15 ?  155 HIS H O     1 
ATOM   6101  C  CB    . HIS E 1 155 ? 25.764  34.823  0.595   1.00 24.32 ?  155 HIS H CB    1 
ATOM   6102  C  CG    . HIS E 1 155 ? 26.988  35.668  0.510   1.00 20.66 ?  155 HIS H CG    1 
ATOM   6103  N  ND1   . HIS E 1 155 ? 27.737  35.987  1.622   1.00 19.90 ?  155 HIS H ND1   1 
ATOM   6104  C  CD2   . HIS E 1 155 ? 27.613  36.228  -0.533  1.00 18.29 ?  155 HIS H CD2   1 
ATOM   6105  C  CE1   . HIS E 1 155 ? 28.769  36.732  1.253   1.00 19.47 ?  155 HIS H CE1   1 
ATOM   6106  N  NE2   . HIS E 1 155 ? 28.711  36.894  -0.052  1.00 18.08 ?  155 HIS H NE2   1 
ATOM   6107  N  N     . VAL E 1 156 ? 24.522  32.529  2.680   1.00 33.83 ?  156 VAL H N     1 
ATOM   6108  C  CA    . VAL E 1 156 ? 23.307  31.920  3.190   1.00 36.09 ?  156 VAL H CA    1 
ATOM   6109  C  C     . VAL E 1 156 ? 22.574  32.963  4.028   1.00 37.25 ?  156 VAL H C     1 
ATOM   6110  O  O     . VAL E 1 156 ? 23.056  33.364  5.085   1.00 31.97 ?  156 VAL H O     1 
ATOM   6111  C  CB    . VAL E 1 156 ? 23.630  30.653  4.004   1.00 46.20 ?  156 VAL H CB    1 
ATOM   6112  C  CG1   . VAL E 1 156 ? 22.389  30.060  4.661   1.00 47.92 ?  156 VAL H CG1   1 
ATOM   6113  C  CG2   . VAL E 1 156 ? 24.341  29.604  3.155   1.00 48.81 ?  156 VAL H CG2   1 
ATOM   6114  N  N     . PRO E 1 157 ? 21.398  33.451  3.572   1.00 35.22 ?  157 PRO H N     1 
ATOM   6115  C  CA    . PRO E 1 157 ? 20.648  34.463  4.315   1.00 32.29 ?  157 PRO H CA    1 
ATOM   6116  C  C     . PRO E 1 157 ? 19.855  33.857  5.470   1.00 31.35 ?  157 PRO H C     1 
ATOM   6117  O  O     . PRO E 1 157 ? 19.443  32.701  5.405   1.00 30.91 ?  157 PRO H O     1 
ATOM   6118  C  CB    . PRO E 1 157 ? 19.738  35.042  3.221   1.00 31.43 ?  157 PRO H CB    1 
ATOM   6119  C  CG    . PRO E 1 157 ? 19.433  33.846  2.345   1.00 33.98 ?  157 PRO H CG    1 
ATOM   6120  C  CD    . PRO E 1 157 ? 20.732  33.053  2.321   1.00 34.41 ?  157 PRO H CD    1 
ATOM   6121  N  N     . ASP E 1 158 ? 19.665  34.651  6.528   1.00 27.36 ?  158 ASP H N     1 
ATOM   6122  C  CA    . ASP E 1 158 ? 18.762  34.293  7.609   1.00 27.91 ?  158 ASP H CA    1 
ATOM   6123  C  C     . ASP E 1 158 ? 17.354  34.739  7.227   1.00 29.18 ?  158 ASP H C     1 
ATOM   6124  O  O     . ASP E 1 158 ? 17.084  35.934  7.134   1.00 27.94 ?  158 ASP H O     1 
ATOM   6125  C  CB    . ASP E 1 158 ? 19.198  34.909  8.929   1.00 25.20 ?  158 ASP H CB    1 
ATOM   6126  C  CG    . ASP E 1 158 ? 18.336  34.556  10.132  1.00 22.77 ?  158 ASP H CG    1 
ATOM   6127  O  OD1   . ASP E 1 158 ? 17.342  33.822  9.948   1.00 22.18 ?  158 ASP H OD1   1 
ATOM   6128  O  OD2   . ASP E 1 158 ? 18.667  35.013  11.245  1.00 17.80 -1 158 ASP H OD2   1 
ATOM   6129  N  N     . PRO E 1 159 ? 16.412  33.796  7.002   1.00 30.45 ?  159 PRO H N     1 
ATOM   6130  C  CA    . PRO E 1 159 ? 15.097  34.146  6.463   1.00 33.40 ?  159 PRO H CA    1 
ATOM   6131  C  C     . PRO E 1 159 ? 14.132  34.809  7.446   1.00 35.69 ?  159 PRO H C     1 
ATOM   6132  O  O     . PRO E 1 159 ? 12.995  35.101  7.085   1.00 37.88 ?  159 PRO H O     1 
ATOM   6133  C  CB    . PRO E 1 159 ? 14.571  32.788  5.959   1.00 33.42 ?  159 PRO H CB    1 
ATOM   6134  C  CG    . PRO E 1 159 ? 15.234  31.762  6.856   1.00 32.12 ?  159 PRO H CG    1 
ATOM   6135  C  CD    . PRO E 1 159 ? 16.577  32.355  7.245   1.00 30.68 ?  159 PRO H CD    1 
ATOM   6136  N  N     . THR E 1 160 ? 14.589  35.052  8.682   1.00 31.05 ?  160 THR H N     1 
ATOM   6137  C  CA    . THR E 1 160 ? 13.770  35.729  9.677   1.00 28.41 ?  160 THR H CA    1 
ATOM   6138  C  C     . THR E 1 160 ? 14.076  37.224  9.660   1.00 27.09 ?  160 THR H C     1 
ATOM   6139  O  O     . THR E 1 160 ? 13.357  38.010  10.273  1.00 28.65 ?  160 THR H O     1 
ATOM   6140  C  CB    . THR E 1 160 ? 14.010  35.161  11.076  1.00 31.01 ?  160 THR H CB    1 
ATOM   6141  O  OG1   . THR E 1 160 ? 15.332  35.550  11.432  1.00 27.55 ?  160 THR H OG1   1 
ATOM   6142  C  CG2   . THR E 1 160 ? 13.861  33.652  11.139  1.00 30.58 ?  160 THR H CG2   1 
ATOM   6143  N  N     . THR E 1 161 ? 15.155  37.606  8.971   1.00 21.90 ?  161 THR H N     1 
ATOM   6144  C  CA    . THR E 1 161 ? 15.597  38.989  8.974   1.00 21.74 ?  161 THR H CA    1 
ATOM   6145  C  C     . THR E 1 161 ? 15.049  39.694  7.739   1.00 21.44 ?  161 THR H C     1 
ATOM   6146  O  O     . THR E 1 161 ? 14.398  39.077  6.899   1.00 21.34 ?  161 THR H O     1 
ATOM   6147  C  CB    . THR E 1 161 ? 17.122  39.053  9.020   1.00 21.21 ?  161 THR H CB    1 
ATOM   6148  O  OG1   . THR E 1 161 ? 17.571  38.541  7.769   1.00 26.45 ?  161 THR H OG1   1 
ATOM   6149  C  CG2   . THR E 1 161 ? 17.696  38.243  10.168  1.00 20.59 ?  161 THR H CG2   1 
ATOM   6150  N  N     . HIS E 1 162 ? 15.313  41.001  7.665   1.00 20.64 ?  162 HIS H N     1 
ATOM   6151  C  CA    . HIS E 1 162 ? 15.083  41.770  6.455   1.00 20.66 ?  162 HIS H CA    1 
ATOM   6152  C  C     . HIS E 1 162 ? 16.319  41.665  5.570   1.00 19.98 ?  162 HIS H C     1 
ATOM   6153  O  O     . HIS E 1 162 ? 17.412  42.074  5.958   1.00 17.94 ?  162 HIS H O     1 
ATOM   6154  C  CB    . HIS E 1 162 ? 14.706  43.217  6.788   1.00 23.05 ?  162 HIS H CB    1 
ATOM   6155  C  CG    . HIS E 1 162 ? 13.261  43.368  7.119   1.00 23.48 ?  162 HIS H CG    1 
ATOM   6156  N  ND1   . HIS E 1 162 ? 12.302  43.499  6.138   1.00 23.47 ?  162 HIS H ND1   1 
ATOM   6157  C  CD2   . HIS E 1 162 ? 12.603  43.374  8.286   1.00 22.76 ?  162 HIS H CD2   1 
ATOM   6158  C  CE1   . HIS E 1 162 ? 11.109  43.595  6.704   1.00 22.86 ?  162 HIS H CE1   1 
ATOM   6159  N  NE2   . HIS E 1 162 ? 11.267  43.522  8.009   1.00 23.71 ?  162 HIS H NE2   1 
ATOM   6160  N  N     . LEU E 1 163 ? 16.122  41.098  4.378   1.00 19.80 ?  163 LEU H N     1 
ATOM   6161  C  CA    . LEU E 1 163 ? 17.207  40.874  3.442   1.00 19.21 ?  163 LEU H CA    1 
ATOM   6162  C  C     . LEU E 1 163 ? 17.147  41.909  2.323   1.00 18.23 ?  163 LEU H C     1 
ATOM   6163  O  O     . LEU E 1 163 ? 16.117  42.069  1.669   1.00 18.93 ?  163 LEU H O     1 
ATOM   6164  C  CB    . LEU E 1 163 ? 17.107  39.453  2.893   1.00 18.94 ?  163 LEU H CB    1 
ATOM   6165  C  CG    . LEU E 1 163 ? 18.048  39.127  1.729   1.00 18.75 ?  163 LEU H CG    1 
ATOM   6166  C  CD1   . LEU E 1 163 ? 19.487  39.376  2.135   1.00 18.36 ?  163 LEU H CD1   1 
ATOM   6167  C  CD2   . LEU E 1 163 ? 17.861  37.698  1.250   1.00 18.18 ?  163 LEU H CD2   1 
ATOM   6168  N  N     . LEU E 1 164 ? 18.277  42.592  2.113   1.00 17.09 ?  164 LEU H N     1 
ATOM   6169  C  CA    . LEU E 1 164 ? 18.443  43.516  1.003   1.00 17.45 ?  164 LEU H CA    1 
ATOM   6170  C  C     . LEU E 1 164 ? 19.451  42.949  0.009   1.00 16.23 ?  164 LEU H C     1 
ATOM   6171  O  O     . LEU E 1 164 ? 20.478  42.402  0.404   1.00 14.30 ?  164 LEU H O     1 
ATOM   6172  C  CB    . LEU E 1 164 ? 18.916  44.873  1.521   1.00 18.26 ?  164 LEU H CB    1 
ATOM   6173  C  CG    . LEU E 1 164 ? 17.974  45.588  2.492   1.00 20.10 ?  164 LEU H CG    1 
ATOM   6174  C  CD1   . LEU E 1 164 ? 18.495  46.971  2.831   1.00 20.00 ?  164 LEU H CD1   1 
ATOM   6175  C  CD2   . LEU E 1 164 ? 16.581  45.663  1.899   1.00 22.08 ?  164 LEU H CD2   1 
ATOM   6176  N  N     . LEU E 1 165 ? 19.140  43.105  -1.282  1.00 16.41 ?  165 LEU H N     1 
ATOM   6177  C  CA    . LEU E 1 165 ? 20.088  42.856  -2.354  1.00 15.44 ?  165 LEU H CA    1 
ATOM   6178  C  C     . LEU E 1 165 ? 20.263  44.149  -3.144  1.00 15.40 ?  165 LEU H C     1 
ATOM   6179  O  O     . LEU E 1 165 ? 19.343  44.580  -3.834  1.00 16.10 ?  165 LEU H O     1 
ATOM   6180  C  CB    . LEU E 1 165 ? 19.594  41.726  -3.256  1.00 14.93 ?  165 LEU H CB    1 
ATOM   6181  C  CG    . LEU E 1 165 ? 19.358  40.372  -2.581  1.00 12.94 ?  165 LEU H CG    1 
ATOM   6182  C  CD1   . LEU E 1 165 ? 19.131  39.316  -3.648  1.00 12.75 ?  165 LEU H CD1   1 
ATOM   6183  C  CD2   . LEU E 1 165 ? 20.504  39.984  -1.664  1.00 12.18 ?  165 LEU H CD2   1 
ATOM   6184  N  N     . TRP E 1 166 ? 21.443  44.767  -3.020  1.00 17.09 ?  166 TRP H N     1 
ATOM   6185  C  CA    . TRP E 1 166 ? 21.732  46.008  -3.720  1.00 18.45 ?  166 TRP H CA    1 
ATOM   6186  C  C     . TRP E 1 166 ? 22.148  45.686  -5.154  1.00 19.25 ?  166 TRP H C     1 
ATOM   6187  O  O     . TRP E 1 166 ? 22.552  44.562  -5.447  1.00 14.97 ?  166 TRP H O     1 
ATOM   6188  C  CB    . TRP E 1 166 ? 22.823  46.815  -2.997  1.00 17.86 ?  166 TRP H CB    1 
ATOM   6189  C  CG    . TRP E 1 166 ? 22.511  47.179  -1.567  1.00 19.25 ?  166 TRP H CG    1 
ATOM   6190  C  CD1   . TRP E 1 166 ? 21.986  46.362  -0.608  1.00 17.66 ?  166 TRP H CD1   1 
ATOM   6191  C  CD2   . TRP E 1 166 ? 22.710  48.464  -0.931  1.00 18.03 ?  166 TRP H CD2   1 
ATOM   6192  N  NE1   . TRP E 1 166 ? 21.844  47.041  0.573   1.00 17.31 ?  166 TRP H NE1   1 
ATOM   6193  C  CE2   . TRP E 1 166 ? 22.277  48.331  0.407   1.00 19.39 ?  166 TRP H CE2   1 
ATOM   6194  C  CE3   . TRP E 1 166 ? 23.203  49.704  -1.355  1.00 18.92 ?  166 TRP H CE3   1 
ATOM   6195  C  CZ2   . TRP E 1 166 ? 22.327  49.388  1.314   1.00 20.07 ?  166 TRP H CZ2   1 
ATOM   6196  C  CZ3   . TRP E 1 166 ? 23.254  50.746  -0.455  1.00 18.46 ?  166 TRP H CZ3   1 
ATOM   6197  C  CH2   . TRP E 1 166 ? 22.820  50.590  0.860   1.00 19.33 ?  166 TRP H CH2   1 
ATOM   6198  N  N     . GLN E 1 167 ? 22.034  46.681  -6.041  1.00 19.03 ?  167 GLN H N     1 
ATOM   6199  C  CA    . GLN E 1 167 ? 22.482  46.555  -7.419  1.00 19.12 ?  167 GLN H CA    1 
ATOM   6200  C  C     . GLN E 1 167 ? 21.807  45.348  -8.066  1.00 20.04 ?  167 GLN H C     1 
ATOM   6201  O  O     . GLN E 1 167 ? 22.440  44.584  -8.792  1.00 18.94 ?  167 GLN H O     1 
ATOM   6202  C  CB    . GLN E 1 167 ? 24.012  46.521  -7.437  1.00 20.99 ?  167 GLN H CB    1 
ATOM   6203  C  CG    . GLN E 1 167 ? 24.632  47.806  -6.895  1.00 21.90 ?  167 GLN H CG    1 
ATOM   6204  C  CD    . GLN E 1 167 ? 26.138  47.885  -7.013  1.00 23.11 ?  167 GLN H CD    1 
ATOM   6205  O  OE1   . GLN E 1 167 ? 26.737  48.947  -6.806  1.00 21.04 ?  167 GLN H OE1   1 
ATOM   6206  N  NE2   . GLN E 1 167 ? 26.772  46.772  -7.353  1.00 24.84 ?  167 GLN H NE2   1 
ATOM   6207  N  N     . ILE E 1 168 ? 20.501  45.213  -7.812  1.00 22.16 ?  168 ILE H N     1 
ATOM   6208  C  CA    . ILE E 1 168 ? 19.713  44.104  -8.325  1.00 22.33 ?  168 ILE H CA    1 
ATOM   6209  C  C     . ILE E 1 168 ? 19.562  44.238  -9.839  1.00 22.97 ?  168 ILE H C     1 
ATOM   6210  O  O     . ILE E 1 168 ? 19.264  43.259  -10.519 1.00 19.75 ?  168 ILE H O     1 
ATOM   6211  C  CB    . ILE E 1 168 ? 18.342  44.044  -7.624  1.00 22.68 ?  168 ILE H CB    1 
ATOM   6212  C  CG1   . ILE E 1 168 ? 17.544  42.813  -8.046  1.00 21.42 ?  168 ILE H CG1   1 
ATOM   6213  C  CG2   . ILE E 1 168 ? 17.549  45.331  -7.855  1.00 23.75 ?  168 ILE H CG2   1 
ATOM   6214  C  CD1   . ILE E 1 168 ? 18.181  41.493  -7.645  1.00 23.40 ?  168 ILE H CD1   1 
ATOM   6215  N  N     . ALA E 1 169 ? 19.772  45.454  -10.359 1.00 25.34 ?  169 ALA H N     1 
ATOM   6216  C  CA    . ALA E 1 169 ? 19.547  45.730  -11.769 1.00 27.52 ?  169 ALA H CA    1 
ATOM   6217  C  C     . ALA E 1 169 ? 20.667  45.136  -12.622 1.00 27.82 ?  169 ALA H C     1 
ATOM   6218  O  O     . ALA E 1 169 ? 20.527  45.041  -13.840 1.00 30.26 ?  169 ALA H O     1 
ATOM   6219  C  CB    . ALA E 1 169 ? 19.412  47.221  -11.995 1.00 27.62 ?  169 ALA H CB    1 
ATOM   6220  N  N     . ILE E 1 170 ? 21.776  44.742  -11.982 1.00 25.01 ?  170 ILE H N     1 
ATOM   6221  C  CA    . ILE E 1 170 ? 22.887  44.125  -12.693 1.00 23.01 ?  170 ILE H CA    1 
ATOM   6222  C  C     . ILE E 1 170 ? 23.211  42.767  -12.075 1.00 22.49 ?  170 ILE H C     1 
ATOM   6223  O  O     . ILE E 1 170 ? 24.315  42.253  -12.246 1.00 19.04 ?  170 ILE H O     1 
ATOM   6224  C  CB    . ILE E 1 170 ? 24.130  45.035  -12.714 1.00 20.00 ?  170 ILE H CB    1 
ATOM   6225  C  CG1   . ILE E 1 170 ? 24.510  45.530  -11.320 1.00 21.07 ?  170 ILE H CG1   1 
ATOM   6226  C  CG2   . ILE E 1 170 ? 23.936  46.194  -13.691 1.00 21.16 ?  170 ILE H CG2   1 
ATOM   6227  C  CD1   . ILE E 1 170 ? 25.805  46.322  -11.283 1.00 21.15 ?  170 ILE H CD1   1 
ATOM   6228  N  N     . ALA E 1 171 ? 22.236  42.190  -11.367 1.00 20.74 ?  171 ALA H N     1 
ATOM   6229  C  CA    . ALA E 1 171 ? 22.426  40.918  -10.689 1.00 21.92 ?  171 ALA H CA    1 
ATOM   6230  C  C     . ALA E 1 171 ? 22.793  39.833  -11.699 1.00 26.80 ?  171 ALA H C     1 
ATOM   6231  O  O     . ALA E 1 171 ? 21.983  39.469  -12.550 1.00 26.33 ?  171 ALA H O     1 
ATOM   6232  C  CB    . ALA E 1 171 ? 21.172  40.558  -9.925  1.00 23.54 ?  171 ALA H CB    1 
ATOM   6233  N  N     . GLY E 1 172 ? 24.024  39.320  -11.587 1.00 25.96 ?  172 GLY H N     1 
ATOM   6234  C  CA    . GLY E 1 172 ? 24.493  38.232  -12.430 1.00 28.32 ?  172 GLY H CA    1 
ATOM   6235  C  C     . GLY E 1 172 ? 25.229  38.765  -13.656 1.00 28.25 ?  172 GLY H C     1 
ATOM   6236  O  O     . GLY E 1 172 ? 25.410  38.053  -14.641 1.00 31.87 ?  172 GLY H O     1 
ATOM   6237  N  N     . GLU E 1 173 ? 25.650  40.031  -13.558 1.00 26.60 ?  173 GLU H N     1 
ATOM   6238  C  CA    . GLU E 1 173 ? 26.301  40.758  -14.635 1.00 27.83 ?  173 GLU H CA    1 
ATOM   6239  C  C     . GLU E 1 173 ? 27.811  40.741  -14.411 1.00 26.65 ?  173 GLU H C     1 
ATOM   6240  O  O     . GLU E 1 173 ? 28.384  41.723  -13.947 1.00 28.60 ?  173 GLU H O     1 
ATOM   6241  C  CB    . GLU E 1 173 ? 25.759  42.188  -14.624 1.00 31.00 ?  173 GLU H CB    1 
ATOM   6242  C  CG    . GLU E 1 173 ? 26.501  43.151  -15.546 1.00 32.93 ?  173 GLU H CG    1 
ATOM   6243  C  CD    . GLU E 1 173 ? 26.536  42.717  -16.997 1.00 36.98 ?  173 GLU H CD    1 
ATOM   6244  O  OE1   . GLU E 1 173 ? 27.610  42.840  -17.624 1.00 46.26 ?  173 GLU H OE1   1 
ATOM   6245  O  OE2   . GLU E 1 173 ? 25.495  42.239  -17.495 1.00 42.93 -1 173 GLU H OE2   1 
ATOM   6246  N  N     . HIS E 1 174 ? 28.441  39.620  -14.779 1.00 26.15 ?  174 HIS H N     1 
ATOM   6247  C  CA    . HIS E 1 174 ? 29.769  39.269  -14.302 1.00 22.64 ?  174 HIS H CA    1 
ATOM   6248  C  C     . HIS E 1 174 ? 30.861  40.064  -15.017 1.00 23.26 ?  174 HIS H C     1 
ATOM   6249  O  O     . HIS E 1 174 ? 31.992  40.114  -14.539 1.00 22.07 ?  174 HIS H O     1 
ATOM   6250  C  CB    . HIS E 1 174 ? 30.029  37.775  -14.521 1.00 23.92 ?  174 HIS H CB    1 
ATOM   6251  C  CG    . HIS E 1 174 ? 30.027  37.415  -15.969 1.00 20.78 ?  174 HIS H CG    1 
ATOM   6252  N  ND1   . HIS E 1 174 ? 28.950  36.833  -16.602 1.00 21.16 ?  174 HIS H ND1   1 
ATOM   6253  C  CD2   . HIS E 1 174 ? 30.962  37.586  -16.912 1.00 20.90 ?  174 HIS H CD2   1 
ATOM   6254  C  CE1   . HIS E 1 174 ? 29.242  36.655  -17.882 1.00 21.39 ?  174 HIS H CE1   1 
ATOM   6255  N  NE2   . HIS E 1 174 ? 30.458  37.108  -18.094 1.00 19.60 ?  174 HIS H NE2   1 
ATOM   6256  N  N     . THR E 1 175 ? 30.531  40.664  -16.167 1.00 26.23 ?  175 THR H N     1 
ATOM   6257  C  CA    . THR E 1 175 ? 31.530  41.323  -16.997 1.00 32.67 ?  175 THR H CA    1 
ATOM   6258  C  C     . THR E 1 175 ? 31.927  42.658  -16.372 1.00 31.11 ?  175 THR H C     1 
ATOM   6259  O  O     . THR E 1 175 ? 33.061  43.105  -16.526 1.00 30.20 ?  175 THR H O     1 
ATOM   6260  C  CB    . THR E 1 175 ? 31.000  41.537  -18.415 1.00 36.61 ?  175 THR H CB    1 
ATOM   6261  O  OG1   . THR E 1 175 ? 30.003  42.547  -18.289 1.00 32.68 ?  175 THR H OG1   1 
ATOM   6262  C  CG2   . THR E 1 175 ? 30.421  40.278  -19.034 1.00 37.02 ?  175 THR H CG2   1 
ATOM   6263  N  N     . LEU E 1 176 ? 30.974  43.295  -15.685 1.00 34.91 ?  176 LEU H N     1 
ATOM   6264  C  CA    . LEU E 1 176 ? 31.159  44.641  -15.165 1.00 39.37 ?  176 LEU H CA    1 
ATOM   6265  C  C     . LEU E 1 176 ? 31.406  45.604  -16.325 1.00 37.53 ?  176 LEU H C     1 
ATOM   6266  O  O     . LEU E 1 176 ? 32.241  46.499  -16.221 1.00 34.21 ?  176 LEU H O     1 
ATOM   6267  C  CB    . LEU E 1 176 ? 32.313  44.695  -14.164 1.00 41.94 ?  176 LEU H CB    1 
ATOM   6268  C  CG    . LEU E 1 176 ? 32.315  43.636  -13.057 1.00 51.01 ?  176 LEU H CG    1 
ATOM   6269  C  CD1   . LEU E 1 176 ? 33.542  43.828  -12.181 1.00 53.95 ?  176 LEU H CD1   1 
ATOM   6270  C  CD2   . LEU E 1 176 ? 31.046  43.670  -12.223 1.00 55.76 ?  176 LEU H CD2   1 
ATOM   6271  N  N     . THR E 1 177 ? 30.681  45.403  -17.433 1.00 37.65 ?  177 THR H N     1 
ATOM   6272  C  CA    . THR E 1 177 ? 30.733  46.319  -18.562 1.00 37.77 ?  177 THR H CA    1 
ATOM   6273  C  C     . THR E 1 177 ? 29.318  46.777  -18.911 1.00 40.84 ?  177 THR H C     1 
ATOM   6274  O  O     . THR E 1 177 ? 29.144  47.771  -19.612 1.00 47.74 ?  177 THR H O     1 
ATOM   6275  C  CB    . THR E 1 177 ? 31.401  45.649  -19.764 1.00 36.47 ?  177 THR H CB    1 
ATOM   6276  O  OG1   . THR E 1 177 ? 30.487  44.637  -20.173 1.00 34.83 ?  177 THR H OG1   1 
ATOM   6277  C  CG2   . THR E 1 177 ? 32.756  45.044  -19.438 1.00 37.41 ?  177 THR H CG2   1 
ATOM   6278  N  N     . GLN E 1 178 ? 28.310  46.040  -18.424 1.00 41.35 ?  178 GLN H N     1 
ATOM   6279  C  CA    . GLN E 1 178 ? 26.922  46.318  -18.762 1.00 42.41 ?  178 GLN H CA    1 
ATOM   6280  C  C     . GLN E 1 178 ? 26.267  47.134  -17.649 1.00 45.91 ?  178 GLN H C     1 
ATOM   6281  O  O     . GLN E 1 178 ? 26.698  47.087  -16.498 1.00 39.25 ?  178 GLN H O     1 
ATOM   6282  C  CB    . GLN E 1 178 ? 26.120  45.035  -18.990 1.00 38.38 ?  178 GLN H CB    1 
ATOM   6283  C  CG    . GLN E 1 178 ? 26.602  44.186  -20.162 1.00 40.59 ?  178 GLN H CG    1 
ATOM   6284  C  CD    . GLN E 1 178 ? 26.291  44.793  -21.513 1.00 41.32 ?  178 GLN H CD    1 
ATOM   6285  O  OE1   . GLN E 1 178 ? 25.687  45.867  -21.615 1.00 42.42 ?  178 GLN H OE1   1 
ATOM   6286  N  NE2   . GLN E 1 178 ? 26.697  44.104  -22.570 1.00 35.13 ?  178 GLN H NE2   1 
ATOM   6287  N  N     . PHE E 1 179 ? 25.209  47.869  -18.013 1.00 49.95 ?  179 PHE H N     1 
ATOM   6288  C  CA    . PHE E 1 179 ? 24.527  48.763  -17.091 1.00 51.82 ?  179 PHE H CA    1 
ATOM   6289  C  C     . PHE E 1 179 ? 23.358  48.040  -16.423 1.00 48.67 ?  179 PHE H C     1 
ATOM   6290  O  O     . PHE E 1 179 ? 22.848  48.502  -15.404 1.00 48.93 ?  179 PHE H O     1 
ATOM   6291  C  CB    . PHE E 1 179 ? 24.042  50.015  -17.829 1.00 60.81 ?  179 PHE H CB    1 
ATOM   6292  C  CG    . PHE E 1 179 ? 25.133  50.899  -18.421 1.00 65.64 ?  179 PHE H CG    1 
ATOM   6293  C  CD1   . PHE E 1 179 ? 26.304  51.165  -17.719 1.00 66.59 ?  179 PHE H CD1   1 
ATOM   6294  C  CD2   . PHE E 1 179 ? 24.982  51.464  -19.683 1.00 67.36 ?  179 PHE H CD2   1 
ATOM   6295  C  CE1   . PHE E 1 179 ? 27.290  51.974  -18.264 1.00 66.72 ?  179 PHE H CE1   1 
ATOM   6296  C  CE2   . PHE E 1 179 ? 25.972  52.270  -20.224 1.00 67.17 ?  179 PHE H CE2   1 
ATOM   6297  C  CZ    . PHE E 1 179 ? 27.122  52.523  -19.514 1.00 67.15 ?  179 PHE H CZ    1 
ATOM   6298  N  N     . HIS E 1 180 ? 22.933  46.912  -17.005 1.00 45.60 ?  180 HIS H N     1 
ATOM   6299  C  CA    . HIS E 1 180 ? 21.811  46.148  -16.477 1.00 41.97 ?  180 HIS H CA    1 
ATOM   6300  C  C     . HIS E 1 180 ? 22.011  44.669  -16.808 1.00 36.16 ?  180 HIS H C     1 
ATOM   6301  O  O     . HIS E 1 180 ? 22.952  44.315  -17.515 1.00 30.17 ?  180 HIS H O     1 
ATOM   6302  C  CB    . HIS E 1 180 ? 20.486  46.710  -17.007 1.00 42.86 ?  180 HIS H CB    1 
ATOM   6303  C  CG    . HIS E 1 180 ? 20.296  46.550  -18.479 1.00 43.32 ?  180 HIS H CG    1 
ATOM   6304  N  ND1   . HIS E 1 180 ? 19.737  45.419  -19.033 1.00 35.82 ?  180 HIS H ND1   1 
ATOM   6305  C  CD2   . HIS E 1 180 ? 20.580  47.364  -19.504 1.00 39.92 ?  180 HIS H CD2   1 
ATOM   6306  C  CE1   . HIS E 1 180 ? 19.693  45.554  -20.350 1.00 36.15 ?  180 HIS H CE1   1 
ATOM   6307  N  NE2   . HIS E 1 180 ? 20.199  46.729  -20.658 1.00 40.70 ?  180 HIS H NE2   1 
ATOM   6308  N  N     . THR E 1 181 ? 21.128  43.809  -16.284 1.00 36.51 ?  181 THR H N     1 
ATOM   6309  C  CA    . THR E 1 181 ? 21.233  42.376  -16.522 1.00 36.59 ?  181 THR H CA    1 
ATOM   6310  C  C     . THR E 1 181 ? 20.091  41.928  -17.432 1.00 33.86 ?  181 THR H C     1 
ATOM   6311  O  O     . THR E 1 181 ? 19.459  42.747  -18.095 1.00 31.81 ?  181 THR H O     1 
ATOM   6312  C  CB    . THR E 1 181 ? 21.236  41.609  -15.198 1.00 35.75 ?  181 THR H CB    1 
ATOM   6313  O  OG1   . THR E 1 181 ? 21.570  40.267  -15.543 1.00 36.92 ?  181 THR H OG1   1 
ATOM   6314  C  CG2   . THR E 1 181 ? 19.897  41.646  -14.484 1.00 32.06 ?  181 THR H CG2   1 
ATOM   6315  N  N     . SER E 1 182 ? 19.851  40.613  -17.460 1.00 36.79 ?  182 SER H N     1 
ATOM   6316  C  CA    . SER E 1 182 ? 18.806  40.027  -18.283 1.00 36.18 ?  182 SER H CA    1 
ATOM   6317  C  C     . SER E 1 182 ? 17.781  39.327  -17.394 1.00 34.63 ?  182 SER H C     1 
ATOM   6318  O  O     . SER E 1 182 ? 18.023  39.119  -16.208 1.00 28.93 ?  182 SER H O     1 
ATOM   6319  C  CB    . SER E 1 182 ? 19.387  39.074  -19.298 1.00 36.47 ?  182 SER H CB    1 
ATOM   6320  O  OG    . SER E 1 182 ? 20.077  38.008  -18.660 1.00 40.83 ?  182 SER H OG    1 
ATOM   6321  N  N     . SER E 1 183 ? 16.640  38.961  -17.989 1.00 41.15 ?  183 SER H N     1 
ATOM   6322  C  CA    . SER E 1 183 ? 15.556  38.321  -17.262 1.00 43.22 ?  183 SER H CA    1 
ATOM   6323  C  C     . SER E 1 183 ? 15.962  36.903  -16.872 1.00 40.74 ?  183 SER H C     1 
ATOM   6324  O  O     . SER E 1 183 ? 15.557  36.399  -15.827 1.00 40.93 ?  183 SER H O     1 
ATOM   6325  C  CB    . SER E 1 183 ? 14.286  38.311  -18.073 1.00 41.49 ?  183 SER H CB    1 
ATOM   6326  O  OG    . SER E 1 183 ? 14.326  37.294  -19.064 1.00 43.36 ?  183 SER H OG    1 
ATOM   6327  N  N     . ASP E 1 184 ? 16.759  36.270  -17.739 1.00 40.24 ?  184 ASP H N     1 
ATOM   6328  C  CA    . ASP E 1 184 ? 17.260  34.928  -17.499 1.00 38.44 ?  184 ASP H CA    1 
ATOM   6329  C  C     . ASP E 1 184 ? 18.098  34.925  -16.223 1.00 32.66 ?  184 ASP H C     1 
ATOM   6330  O  O     . ASP E 1 184 ? 17.973  34.019  -15.401 1.00 31.64 ?  184 ASP H O     1 
ATOM   6331  C  CB    . ASP E 1 184 ? 18.026  34.414  -18.708 1.00 41.55 ?  184 ASP H CB    1 
ATOM   6332  C  CG    . ASP E 1 184 ? 19.152  35.316  -19.193 1.00 45.07 ?  184 ASP H CG    1 
ATOM   6333  O  OD1   . ASP E 1 184 ? 20.215  35.334  -18.536 1.00 53.30 ?  184 ASP H OD1   1 
ATOM   6334  O  OD2   . ASP E 1 184 ? 18.949  36.010  -20.213 1.00 43.52 -1 184 ASP H OD2   1 
ATOM   6335  N  N     . ARG E 1 185 ? 18.953  35.944  -16.070 1.00 28.66 ?  185 ARG H N     1 
ATOM   6336  C  CA    . ARG E 1 185 ? 19.776  36.087  -14.879 1.00 32.69 ?  185 ARG H CA    1 
ATOM   6337  C  C     . ARG E 1 185 ? 18.880  36.183  -13.647 1.00 31.15 ?  185 ARG H C     1 
ATOM   6338  O  O     . ARG E 1 185 ? 19.135  35.531  -12.637 1.00 28.16 ?  185 ARG H O     1 
ATOM   6339  C  CB    . ARG E 1 185 ? 20.677  37.328  -14.928 1.00 36.04 ?  185 ARG H CB    1 
ATOM   6340  C  CG    . ARG E 1 185 ? 22.156  37.072  -15.183 1.00 37.89 ?  185 ARG H CG    1 
ATOM   6341  C  CD    . ARG E 1 185 ? 22.514  36.625  -16.591 1.00 41.87 ?  185 ARG H CD    1 
ATOM   6342  N  NE    . ARG E 1 185 ? 23.954  36.347  -16.654 1.00 44.29 ?  185 ARG H NE    1 
ATOM   6343  C  CZ    . ARG E 1 185 ? 24.618  35.858  -17.694 1.00 45.46 ?  185 ARG H CZ    1 
ATOM   6344  N  NH1   . ARG E 1 185 ? 23.990  35.591  -18.825 1.00 44.41 1  185 ARG H NH1   1 
ATOM   6345  N  NH2   . ARG E 1 185 ? 25.917  35.640  -17.593 1.00 47.97 ?  185 ARG H NH2   1 
ATOM   6346  N  N     . LEU E 1 186 ? 17.832  37.006  -13.752 1.00 28.57 ?  186 LEU H N     1 
ATOM   6347  C  CA    . LEU E 1 186 ? 16.962  37.299  -12.626 1.00 26.43 ?  186 LEU H CA    1 
ATOM   6348  C  C     . LEU E 1 186 ? 16.131  36.064  -12.282 1.00 28.32 ?  186 LEU H C     1 
ATOM   6349  O  O     . LEU E 1 186 ? 15.765  35.859  -11.126 1.00 28.20 ?  186 LEU H O     1 
ATOM   6350  C  CB    . LEU E 1 186 ? 16.102  38.513  -12.976 1.00 25.74 ?  186 LEU H CB    1 
ATOM   6351  C  CG    . LEU E 1 186 ? 16.812  39.871  -12.928 1.00 26.63 ?  186 LEU H CG    1 
ATOM   6352  C  CD1   . LEU E 1 186 ? 15.974  40.943  -13.602 1.00 26.51 ?  186 LEU H CD1   1 
ATOM   6353  C  CD2   . LEU E 1 186 ? 17.134  40.283  -11.499 1.00 26.71 ?  186 LEU H CD2   1 
ATOM   6354  N  N     . GLN E 1 187 ? 15.853  35.242  -13.300 1.00 25.20 ?  187 GLN H N     1 
ATOM   6355  C  CA    . GLN E 1 187 ? 15.167  33.972  -13.118 1.00 22.38 ?  187 GLN H CA    1 
ATOM   6356  C  C     . GLN E 1 187 ? 16.046  33.006  -12.326 1.00 21.33 ?  187 GLN H C     1 
ATOM   6357  O  O     . GLN E 1 187 ? 15.539  32.206  -11.544 1.00 18.67 ?  187 GLN H O     1 
ATOM   6358  C  CB    . GLN E 1 187 ? 14.816  33.354  -14.472 1.00 21.91 ?  187 GLN H CB    1 
ATOM   6359  C  CG    . GLN E 1 187 ? 14.048  32.039  -14.383 1.00 22.73 ?  187 GLN H CG    1 
ATOM   6360  C  CD    . GLN E 1 187 ? 12.776  32.147  -13.571 1.00 22.37 ?  187 GLN H CD    1 
ATOM   6361  O  OE1   . GLN E 1 187 ? 12.072  33.162  -13.614 1.00 22.42 ?  187 GLN H OE1   1 
ATOM   6362  N  NE2   . GLN E 1 187 ? 12.479  31.105  -12.806 1.00 20.90 ?  187 GLN H NE2   1 
ATOM   6363  N  N     . ILE E 1 188 ? 17.362  33.073  -12.554 1.00 21.60 ?  188 ILE H N     1 
ATOM   6364  C  CA    . ILE E 1 188 ? 18.306  32.200  -11.873 1.00 23.73 ?  188 ILE H CA    1 
ATOM   6365  C  C     . ILE E 1 188 ? 18.395  32.616  -10.407 1.00 21.19 ?  188 ILE H C     1 
ATOM   6366  O  O     . ILE E 1 188 ? 18.529  31.772  -9.522  1.00 19.04 ?  188 ILE H O     1 
ATOM   6367  C  CB    . ILE E 1 188 ? 19.677  32.224  -12.575 1.00 26.99 ?  188 ILE H CB    1 
ATOM   6368  C  CG1   . ILE E 1 188 ? 19.641  31.413  -13.873 1.00 30.12 ?  188 ILE H CG1   1 
ATOM   6369  C  CG2   . ILE E 1 188 ? 20.788  31.741  -11.640 1.00 26.50 ?  188 ILE H CG2   1 
ATOM   6370  C  CD1   . ILE E 1 188 ? 20.885  31.551  -14.732 1.00 33.46 ?  188 ILE H CD1   1 
ATOM   6371  N  N     . LEU E 1 189 ? 18.309  33.927  -10.170 1.00 19.06 ?  189 LEU H N     1 
ATOM   6372  C  CA    . LEU E 1 189 ? 18.315  34.473  -8.825  1.00 18.53 ?  189 LEU H CA    1 
ATOM   6373  C  C     . LEU E 1 189 ? 17.091  33.968  -8.066  1.00 19.30 ?  189 LEU H C     1 
ATOM   6374  O  O     . LEU E 1 189 ? 17.194  33.543  -6.918  1.00 20.54 ?  189 LEU H O     1 
ATOM   6375  C  CB    . LEU E 1 189 ? 18.337  35.997  -8.921  1.00 17.94 ?  189 LEU H CB    1 
ATOM   6376  C  CG    . LEU E 1 189 ? 18.225  36.745  -7.591  1.00 17.16 ?  189 LEU H CG    1 
ATOM   6377  C  CD1   . LEU E 1 189 ? 19.261  36.215  -6.616  1.00 16.32 ?  189 LEU H CD1   1 
ATOM   6378  C  CD2   . LEU E 1 189 ? 18.380  38.241  -7.796  1.00 15.98 ?  189 LEU H CD2   1 
ATOM   6379  N  N     . VAL E 1 190 ? 15.933  34.020  -8.731  1.00 20.09 ?  190 VAL H N     1 
ATOM   6380  C  CA    . VAL E 1 190 ? 14.687  33.545  -8.155  1.00 22.20 ?  190 VAL H CA    1 
ATOM   6381  C  C     . VAL E 1 190 ? 14.860  32.096  -7.711  1.00 22.82 ?  190 VAL H C     1 
ATOM   6382  O  O     . VAL E 1 190 ? 14.481  31.736  -6.599  1.00 19.86 ?  190 VAL H O     1 
ATOM   6383  C  CB    . VAL E 1 190 ? 13.517  33.673  -9.149  1.00 23.89 ?  190 VAL H CB    1 
ATOM   6384  C  CG1   . VAL E 1 190 ? 12.301  32.871  -8.699  1.00 24.70 ?  190 VAL H CG1   1 
ATOM   6385  C  CG2   . VAL E 1 190 ? 13.147  35.128  -9.406  1.00 22.59 ?  190 VAL H CG2   1 
ATOM   6386  N  N     . GLU E 1 191 ? 15.423  31.266  -8.594  1.00 21.43 ?  191 GLU H N     1 
ATOM   6387  C  CA    . GLU E 1 191 ? 15.511  29.838  -8.335  1.00 24.50 ?  191 GLU H CA    1 
ATOM   6388  C  C     . GLU E 1 191 ? 16.450  29.600  -7.155  1.00 22.31 ?  191 GLU H C     1 
ATOM   6389  O  O     . GLU E 1 191 ? 16.205  28.728  -6.326  1.00 25.09 ?  191 GLU H O     1 
ATOM   6390  C  CB    . GLU E 1 191 ? 15.931  29.090  -9.599  1.00 27.92 ?  191 GLU H CB    1 
ATOM   6391  C  CG    . GLU E 1 191 ? 14.869  29.142  -10.693 1.00 30.46 ?  191 GLU H CG    1 
ATOM   6392  C  CD    . GLU E 1 191 ? 15.301  28.525  -12.009 1.00 35.39 ?  191 GLU H CD    1 
ATOM   6393  O  OE1   . GLU E 1 191 ? 15.397  29.277  -13.001 1.00 39.09 ?  191 GLU H OE1   1 
ATOM   6394  O  OE2   . GLU E 1 191 ? 15.538  27.298  -12.044 1.00 37.28 -1 191 GLU H OE2   1 
ATOM   6395  N  N     . GLN E 1 192 ? 17.515  30.403  -7.092  1.00 22.04 ?  192 GLN H N     1 
ATOM   6396  C  CA    . GLN E 1 192 ? 18.446  30.385  -5.977  1.00 18.94 ?  192 GLN H CA    1 
ATOM   6397  C  C     . GLN E 1 192 ? 17.731  30.775  -4.687  1.00 22.56 ?  192 GLN H C     1 
ATOM   6398  O  O     . GLN E 1 192 ? 17.819  30.068  -3.685  1.00 26.06 ?  192 GLN H O     1 
ATOM   6399  C  CB    . GLN E 1 192 ? 19.569  31.377  -6.268  1.00 17.96 ?  192 GLN H CB    1 
ATOM   6400  C  CG    . GLN E 1 192 ? 20.641  31.440  -5.188  1.00 17.09 ?  192 GLN H CG    1 
ATOM   6401  C  CD    . GLN E 1 192 ? 21.725  32.442  -5.514  1.00 16.93 ?  192 GLN H CD    1 
ATOM   6402  O  OE1   . GLN E 1 192 ? 21.599  33.237  -6.452  1.00 15.69 ?  192 GLN H OE1   1 
ATOM   6403  N  NE2   . GLN E 1 192 ? 22.797  32.419  -4.735  1.00 15.12 ?  192 GLN H NE2   1 
ATOM   6404  N  N     . LEU E 1 193 ? 17.038  31.919  -4.722  1.00 22.54 ?  193 LEU H N     1 
ATOM   6405  C  CA    . LEU E 1 193 ? 16.380  32.455  -3.541  1.00 21.37 ?  193 LEU H CA    1 
ATOM   6406  C  C     . LEU E 1 193 ? 15.316  31.471  -3.063  1.00 21.31 ?  193 LEU H C     1 
ATOM   6407  O  O     . LEU E 1 193 ? 14.919  31.497  -1.900  1.00 17.47 ?  193 LEU H O     1 
ATOM   6408  C  CB    . LEU E 1 193 ? 15.779  33.828  -3.842  1.00 24.57 ?  193 LEU H CB    1 
ATOM   6409  C  CG    . LEU E 1 193 ? 16.758  35.007  -3.878  1.00 26.96 ?  193 LEU H CG    1 
ATOM   6410  C  CD1   . LEU E 1 193 ? 16.054  36.251  -4.387  1.00 27.02 ?  193 LEU H CD1   1 
ATOM   6411  C  CD2   . LEU E 1 193 ? 17.379  35.277  -2.517  1.00 28.82 ?  193 LEU H CD2   1 
ATOM   6412  N  N     . ASN E 1 194 ? 14.874  30.595  -3.973  1.00 26.29 ?  194 ASN H N     1 
ATOM   6413  C  CA    . ASN E 1 194 ? 13.807  29.650  -3.686  1.00 28.74 ?  194 ASN H CA    1 
ATOM   6414  C  C     . ASN E 1 194 ? 14.265  28.630  -2.644  1.00 29.23 ?  194 ASN H C     1 
ATOM   6415  O  O     . ASN E 1 194 ? 13.434  27.943  -2.054  1.00 28.11 ?  194 ASN H O     1 
ATOM   6416  C  CB    . ASN E 1 194 ? 13.317  28.954  -4.952  1.00 32.27 ?  194 ASN H CB    1 
ATOM   6417  C  CG    . ASN E 1 194 ? 11.992  28.256  -4.749  1.00 35.34 ?  194 ASN H CG    1 
ATOM   6418  O  OD1   . ASN E 1 194 ? 11.335  28.453  -3.721  1.00 45.15 ?  194 ASN H OD1   1 
ATOM   6419  N  ND2   . ASN E 1 194 ? 11.577  27.452  -5.716  1.00 37.94 ?  194 ASN H ND2   1 
ATOM   6420  N  N     . GLN E 1 195 ? 15.581  28.527  -2.418  1.00 27.67 ?  195 GLN H N     1 
ATOM   6421  C  CA    . GLN E 1 195 ? 16.090  27.637  -1.385  1.00 29.20 ?  195 GLN H CA    1 
ATOM   6422  C  C     . GLN E 1 195 ? 15.450  28.016  -0.051  1.00 34.31 ?  195 GLN H C     1 
ATOM   6423  O  O     . GLN E 1 195 ? 15.209  27.153  0.791   1.00 34.04 ?  195 GLN H O     1 
ATOM   6424  C  CB    . GLN E 1 195 ? 17.614  27.685  -1.250  1.00 26.66 ?  195 GLN H CB    1 
ATOM   6425  C  CG    . GLN E 1 195 ? 18.373  27.296  -2.514  1.00 27.50 ?  195 GLN H CG    1 
ATOM   6426  C  CD    . GLN E 1 195 ? 19.864  27.535  -2.411  1.00 28.04 ?  195 GLN H CD    1 
ATOM   6427  O  OE1   . GLN E 1 195 ? 20.589  26.818  -1.712  1.00 27.43 ?  195 GLN H OE1   1 
ATOM   6428  N  NE2   . GLN E 1 195 ? 20.338  28.549  -3.120  1.00 28.70 ?  195 GLN H NE2   1 
ATOM   6429  N  N     . TRP E 1 196 ? 15.168  29.315  0.114   1.00 32.77 ?  196 TRP H N     1 
ATOM   6430  C  CA    . TRP E 1 196 ? 14.731  29.868  1.386   1.00 30.46 ?  196 TRP H CA    1 
ATOM   6431  C  C     . TRP E 1 196 ? 13.327  30.463  1.268   1.00 29.96 ?  196 TRP H C     1 
ATOM   6432  O  O     . TRP E 1 196 ? 12.507  30.296  2.168   1.00 27.29 ?  196 TRP H O     1 
ATOM   6433  C  CB    . TRP E 1 196 ? 15.738  30.922  1.870   1.00 30.57 ?  196 TRP H CB    1 
ATOM   6434  C  CG    . TRP E 1 196 ? 17.156  30.421  1.960   1.00 28.29 ?  196 TRP H CG    1 
ATOM   6435  C  CD1   . TRP E 1 196 ? 17.719  29.746  3.003   1.00 26.06 ?  196 TRP H CD1   1 
ATOM   6436  C  CD2   . TRP E 1 196 ? 18.197  30.564  0.967   1.00 26.43 ?  196 TRP H CD2   1 
ATOM   6437  N  NE1   . TRP E 1 196 ? 19.029  29.454  2.731   1.00 26.79 ?  196 TRP H NE1   1 
ATOM   6438  C  CE2   . TRP E 1 196 ? 19.352  29.942  1.492   1.00 27.79 ?  196 TRP H CE2   1 
ATOM   6439  C  CE3   . TRP E 1 196 ? 18.268  31.148  -0.302  1.00 24.95 ?  196 TRP H CE3   1 
ATOM   6440  C  CZ2   . TRP E 1 196 ? 20.554  29.892  0.791   1.00 28.32 ?  196 TRP H CZ2   1 
ATOM   6441  C  CZ3   . TRP E 1 196 ? 19.458  31.098  -0.994  1.00 28.19 ?  196 TRP H CZ3   1 
ATOM   6442  C  CH2   . TRP E 1 196 ? 20.584  30.478  -0.453  1.00 27.44 ?  196 TRP H CH2   1 
ATOM   6443  N  N     . TYR E 1 197 ? 13.058  31.152  0.152   1.00 28.49 ?  197 TYR H N     1 
ATOM   6444  C  CA    . TYR E 1 197 ? 11.837  31.928  -0.008  1.00 28.53 ?  197 TYR H CA    1 
ATOM   6445  C  C     . TYR E 1 197 ? 10.943  31.302  -1.079  1.00 29.95 ?  197 TYR H C     1 
ATOM   6446  O  O     . TYR E 1 197 ? 11.402  31.032  -2.186  1.00 33.95 ?  197 TYR H O     1 
ATOM   6447  C  CB    . TYR E 1 197 ? 12.220  33.364  -0.383  1.00 28.25 ?  197 TYR H CB    1 
ATOM   6448  C  CG    . TYR E 1 197 ? 13.199  34.040  0.569   1.00 30.32 ?  197 TYR H CG    1 
ATOM   6449  C  CD1   . TYR E 1 197 ? 12.747  34.762  1.666   1.00 30.50 ?  197 TYR H CD1   1 
ATOM   6450  C  CD2   . TYR E 1 197 ? 14.573  33.965  0.366   1.00 29.57 ?  197 TYR H CD2   1 
ATOM   6451  C  CE1   . TYR E 1 197 ? 13.628  35.381  2.537   1.00 27.77 ?  197 TYR H CE1   1 
ATOM   6452  C  CE2   . TYR E 1 197 ? 15.464  34.580  1.230   1.00 29.07 ?  197 TYR H CE2   1 
ATOM   6453  C  CZ    . TYR E 1 197 ? 14.990  35.291  2.318   1.00 25.54 ?  197 TYR H CZ    1 
ATOM   6454  O  OH    . TYR E 1 197 ? 15.856  35.903  3.177   1.00 27.25 ?  197 TYR H OH    1 
ATOM   6455  N  N     . PRO E 1 198 ? 9.642   31.056  -0.792  1.00 30.12 ?  198 PRO H N     1 
ATOM   6456  C  CA    . PRO E 1 198 ? 8.704   30.584  -1.815  1.00 31.57 ?  198 PRO H CA    1 
ATOM   6457  C  C     . PRO E 1 198 ? 8.542   31.573  -2.970  1.00 33.82 ?  198 PRO H C     1 
ATOM   6458  O  O     . PRO E 1 198 ? 8.975   32.719  -2.874  1.00 31.77 ?  198 PRO H O     1 
ATOM   6459  C  CB    . PRO E 1 198 ? 7.383   30.341  -1.052  1.00 31.64 ?  198 PRO H CB    1 
ATOM   6460  C  CG    . PRO E 1 198 ? 7.537   31.091  0.259   1.00 31.96 ?  198 PRO H CG    1 
ATOM   6461  C  CD    . PRO E 1 198 ? 9.026   31.175  0.539   1.00 29.44 ?  198 PRO H CD    1 
ATOM   6462  N  N     . LEU E 1 199 ? 7.912   31.114  -4.061  1.00 35.06 ?  199 LEU H N     1 
ATOM   6463  C  CA    . LEU E 1 199 ? 7.866   31.863  -5.310  1.00 36.32 ?  199 LEU H CA    1 
ATOM   6464  C  C     . LEU E 1 199 ? 6.840   32.988  -5.197  1.00 35.79 ?  199 LEU H C     1 
ATOM   6465  O  O     . LEU E 1 199 ? 6.948   34.004  -5.879  1.00 34.88 ?  199 LEU H O     1 
ATOM   6466  C  CB    . LEU E 1 199 ? 7.541   30.939  -6.486  1.00 37.97 ?  199 LEU H CB    1 
ATOM   6467  C  CG    . LEU E 1 199 ? 8.585   29.871  -6.831  1.00 41.10 ?  199 LEU H CG    1 
ATOM   6468  C  CD1   . LEU E 1 199 ? 8.091   28.989  -7.967  1.00 40.98 ?  199 LEU H CD1   1 
ATOM   6469  C  CD2   . LEU E 1 199 ? 9.930   30.480  -7.191  1.00 41.65 ?  199 LEU H CD2   1 
ATOM   6470  N  N     . ASP E 1 200 ? 5.846   32.787  -4.327  1.00 37.27 ?  200 ASP H N     1 
ATOM   6471  C  CA    . ASP E 1 200 ? 4.759   33.735  -4.157  1.00 35.97 ?  200 ASP H CA    1 
ATOM   6472  C  C     . ASP E 1 200 ? 5.102   34.722  -3.041  1.00 35.55 ?  200 ASP H C     1 
ATOM   6473  O  O     . ASP E 1 200 ? 4.279   35.563  -2.683  1.00 35.43 ?  200 ASP H O     1 
ATOM   6474  C  CB    . ASP E 1 200 ? 3.450   33.009  -3.888  1.00 35.52 ?  200 ASP H CB    1 
ATOM   6475  C  CG    . ASP E 1 200 ? 3.404   32.214  -2.591  1.00 36.47 ?  200 ASP H CG    1 
ATOM   6476  O  OD1   . ASP E 1 200 ? 4.446   32.149  -1.906  1.00 34.26 ?  200 ASP H OD1   1 
ATOM   6477  O  OD2   . ASP E 1 200 ? 2.323   31.674  -2.270  1.00 32.64 -1 200 ASP H OD2   1 
ATOM   6478  N  N     . HIS E 1 201 ? 6.322   34.616  -2.500  1.00 33.07 ?  201 HIS H N     1 
ATOM   6479  C  CA    . HIS E 1 201 ? 6.751   35.458  -1.393  1.00 31.67 ?  201 HIS H CA    1 
ATOM   6480  C  C     . HIS E 1 201 ? 6.836   36.909  -1.853  1.00 28.89 ?  201 HIS H C     1 
ATOM   6481  O  O     . HIS E 1 201 ? 7.581   37.230  -2.777  1.00 24.93 ?  201 HIS H O     1 
ATOM   6482  C  CB    . HIS E 1 201 ? 8.098   34.991  -0.826  1.00 34.12 ?  201 HIS H CB    1 
ATOM   6483  C  CG    . HIS E 1 201 ? 8.585   35.797  0.337   1.00 31.24 ?  201 HIS H CG    1 
ATOM   6484  N  ND1   . HIS E 1 201 ? 8.167   35.566  1.630   1.00 28.90 ?  201 HIS H ND1   1 
ATOM   6485  C  CD2   . HIS E 1 201 ? 9.445   36.823  0.407   1.00 29.71 ?  201 HIS H CD2   1 
ATOM   6486  C  CE1   . HIS E 1 201 ? 8.761   36.426  2.444   1.00 29.11 ?  201 HIS H CE1   1 
ATOM   6487  N  NE2   . HIS E 1 201 ? 9.544   37.198  1.722   1.00 29.83 ?  201 HIS H NE2   1 
ATOM   6488  N  N     . GLU E 1 202 ? 6.069   37.777  -1.187  1.00 28.31 ?  202 GLU H N     1 
ATOM   6489  C  CA    . GLU E 1 202 ? 6.044   39.190  -1.520  1.00 25.00 ?  202 GLU H CA    1 
ATOM   6490  C  C     . GLU E 1 202 ? 7.424   39.789  -1.275  1.00 22.66 ?  202 GLU H C     1 
ATOM   6491  O  O     . GLU E 1 202 ? 7.958   39.699  -0.172  1.00 21.54 ?  202 GLU H O     1 
ATOM   6492  C  CB    . GLU E 1 202 ? 5.015   39.949  -0.682  1.00 28.96 ?  202 GLU H CB    1 
ATOM   6493  C  CG    . GLU E 1 202 ? 4.904   41.423  -1.060  1.00 32.20 ?  202 GLU H CG    1 
ATOM   6494  C  CD    . GLU E 1 202 ? 3.864   42.195  -0.270  1.00 35.55 ?  202 GLU H CD    1 
ATOM   6495  O  OE1   . GLU E 1 202 ? 4.047   42.354  0.955   1.00 38.41 ?  202 GLU H OE1   1 
ATOM   6496  O  OE2   . GLU E 1 202 ? 2.866   42.630  -0.882  1.00 33.04 -1 202 GLU H OE2   1 
ATOM   6497  N  N     . VAL E 1 203 ? 7.991   40.397  -2.319  1.00 21.44 ?  203 VAL H N     1 
ATOM   6498  C  CA    . VAL E 1 203 ? 9.207   41.175  -2.176  1.00 19.51 ?  203 VAL H CA    1 
ATOM   6499  C  C     . VAL E 1 203 ? 8.883   42.622  -2.533  1.00 17.94 ?  203 VAL H C     1 
ATOM   6500  O  O     . VAL E 1 203 ? 7.768   42.930  -2.948  1.00 15.41 ?  203 VAL H O     1 
ATOM   6501  C  CB    . VAL E 1 203 ? 10.366  40.622  -3.026  1.00 20.77 ?  203 VAL H CB    1 
ATOM   6502  C  CG1   . VAL E 1 203 ? 10.756  39.217  -2.584  1.00 22.06 ?  203 VAL H CG1   1 
ATOM   6503  C  CG2   . VAL E 1 203 ? 10.047  40.650  -4.516  1.00 20.30 ?  203 VAL H CG2   1 
ATOM   6504  N  N     . VAL E 1 204 ? 9.874   43.499  -2.361  1.00 17.55 ?  204 VAL H N     1 
ATOM   6505  C  CA    . VAL E 1 204 ? 9.673   44.927  -2.520  1.00 16.20 ?  204 VAL H CA    1 
ATOM   6506  C  C     . VAL E 1 204 ? 10.807  45.501  -3.358  1.00 15.35 ?  204 VAL H C     1 
ATOM   6507  O  O     . VAL E 1 204 ? 11.975  45.349  -3.010  1.00 15.17 ?  204 VAL H O     1 
ATOM   6508  C  CB    . VAL E 1 204 ? 9.616   45.621  -1.147  1.00 15.33 ?  204 VAL H CB    1 
ATOM   6509  C  CG1   . VAL E 1 204 ? 9.488   47.136  -1.279  1.00 14.95 ?  204 VAL H CG1   1 
ATOM   6510  C  CG2   . VAL E 1 204 ? 8.508   45.049  -0.274  1.00 15.45 ?  204 VAL H CG2   1 
ATOM   6511  N  N     . ILE E 1 205 ? 10.443  46.172  -4.455  1.00 15.37 ?  205 ILE H N     1 
ATOM   6512  C  CA    . ILE E 1 205 ? 11.391  46.999  -5.178  1.00 15.47 ?  205 ILE H CA    1 
ATOM   6513  C  C     . ILE E 1 205 ? 11.292  48.415  -4.622  1.00 17.77 ?  205 ILE H C     1 
ATOM   6514  O  O     . ILE E 1 205 ? 10.264  49.076  -4.754  1.00 15.88 ?  205 ILE H O     1 
ATOM   6515  C  CB    . ILE E 1 205 ? 11.148  46.962  -6.697  1.00 15.32 ?  205 ILE H CB    1 
ATOM   6516  C  CG1   . ILE E 1 205 ? 11.225  45.539  -7.245  1.00 16.66 ?  205 ILE H CG1   1 
ATOM   6517  C  CG2   . ILE E 1 205 ? 12.121  47.898  -7.415  1.00 15.46 ?  205 ILE H CG2   1 
ATOM   6518  C  CD1   . ILE E 1 205 ? 10.732  45.399  -8.673  1.00 18.86 ?  205 ILE H CD1   1 
ATOM   6519  N  N     . TYR E 1 206 ? 12.383  48.853  -3.991  1.00 18.18 ?  206 TYR H N     1 
ATOM   6520  C  CA    . TYR E 1 206 ? 12.448  50.162  -3.372  1.00 18.52 ?  206 TYR H CA    1 
ATOM   6521  C  C     . TYR E 1 206 ? 13.377  51.055  -4.188  1.00 20.25 ?  206 TYR H C     1 
ATOM   6522  O  O     . TYR E 1 206 ? 14.378  50.592  -4.733  1.00 19.91 ?  206 TYR H O     1 
ATOM   6523  C  CB    . TYR E 1 206 ? 12.908  50.005  -1.919  1.00 20.04 ?  206 TYR H CB    1 
ATOM   6524  C  CG    . TYR E 1 206 ? 13.240  51.313  -1.213  1.00 18.73 ?  206 TYR H CG    1 
ATOM   6525  C  CD1   . TYR E 1 206 ? 12.241  52.110  -0.666  1.00 17.75 ?  206 TYR H CD1   1 
ATOM   6526  C  CD2   . TYR E 1 206 ? 14.554  51.747  -1.088  1.00 18.59 ?  206 TYR H CD2   1 
ATOM   6527  C  CE1   . TYR E 1 206 ? 12.538  53.300  -0.022  1.00 15.59 ?  206 TYR H CE1   1 
ATOM   6528  C  CE2   . TYR E 1 206 ? 14.864  52.935  -0.447  1.00 18.82 ?  206 TYR H CE2   1 
ATOM   6529  C  CZ    . TYR E 1 206 ? 13.853  53.713  0.088   1.00 17.69 ?  206 TYR H CZ    1 
ATOM   6530  O  OH    . TYR E 1 206 ? 14.160  54.883  0.721   1.00 22.35 ?  206 TYR H OH    1 
ATOM   6531  N  N     . GLU E 1 207 ? 12.999  52.334  -4.278  1.00 17.72 ?  207 GLU H N     1 
ATOM   6532  C  CA    . GLU E 1 207 ? 13.865  53.378  -4.796  1.00 20.74 ?  207 GLU H CA    1 
ATOM   6533  C  C     . GLU E 1 207 ? 13.595  54.655  -4.005  1.00 23.10 ?  207 GLU H C     1 
ATOM   6534  O  O     . GLU E 1 207 ? 12.500  55.209  -4.077  1.00 30.78 ?  207 GLU H O     1 
ATOM   6535  C  CB    . GLU E 1 207 ? 13.612  53.640  -6.281  1.00 21.97 ?  207 GLU H CB    1 
ATOM   6536  C  CG    . GLU E 1 207 ? 13.549  52.375  -7.131  1.00 20.03 ?  207 GLU H CG    1 
ATOM   6537  C  CD    . GLU E 1 207 ? 13.240  52.638  -8.594  1.00 21.76 ?  207 GLU H CD    1 
ATOM   6538  O  OE1   . GLU E 1 207 ? 13.008  53.814  -8.944  1.00 18.60 ?  207 GLU H OE1   1 
ATOM   6539  O  OE2   . GLU E 1 207 ? 13.238  51.670  -9.387  1.00 19.78 -1 207 GLU H OE2   1 
ATOM   6540  N  N     . ALA E 1 208 ? 14.595  55.104  -3.237  1.00 22.04 ?  208 ALA H N     1 
ATOM   6541  C  CA    . ALA E 1 208 ? 14.499  56.356  -2.506  1.00 22.16 ?  208 ALA H CA    1 
ATOM   6542  C  C     . ALA E 1 208 ? 14.392  57.512  -3.496  1.00 17.86 ?  208 ALA H C     1 
ATOM   6543  O  O     . ALA E 1 208 ? 15.033  57.491  -4.543  1.00 21.14 ?  208 ALA H O     1 
ATOM   6544  C  CB    . ALA E 1 208 ? 15.702  56.520  -1.602  1.00 22.36 ?  208 ALA H CB    1 
ATOM   6545  N  N     . ALA E 1 209 ? 13.583  58.520  -3.159  1.00 17.66 ?  209 ALA H N     1 
ATOM   6546  C  CA    . ALA E 1 209 ? 13.430  59.683  -4.019  1.00 16.28 ?  209 ALA H CA    1 
ATOM   6547  C  C     . ALA E 1 209 ? 14.714  60.508  -3.999  1.00 13.79 ?  209 ALA H C     1 
ATOM   6548  O  O     . ALA E 1 209 ? 15.414  60.549  -2.990  1.00 12.59 ?  209 ALA H O     1 
ATOM   6549  C  CB    . ALA E 1 209 ? 12.235  60.501  -3.583  1.00 16.60 ?  209 ALA H CB    1 
ATOM   6550  N  N     . ASN E 1 210 ? 15.016  61.155  -5.130  1.00 12.67 ?  210 ASN H N     1 
ATOM   6551  C  CA    . ASN E 1 210 ? 16.183  62.014  -5.242  1.00 11.99 ?  210 ASN H CA    1 
ATOM   6552  C  C     . ASN E 1 210 ? 15.748  63.477  -5.219  1.00 13.62 ?  210 ASN H C     1 
ATOM   6553  O  O     . ASN E 1 210 ? 16.564  64.371  -4.999  1.00 12.47 ?  210 ASN H O     1 
ATOM   6554  C  CB    . ASN E 1 210 ? 16.995  61.706  -6.497  1.00 12.44 ?  210 ASN H CB    1 
ATOM   6555  C  CG    . ASN E 1 210 ? 17.691  60.368  -6.415  1.00 12.25 ?  210 ASN H CG    1 
ATOM   6556  O  OD1   . ASN E 1 210 ? 18.364  60.077  -5.420  1.00 11.04 ?  210 ASN H OD1   1 
ATOM   6557  N  ND2   . ASN E 1 210 ? 17.545  59.541  -7.439  1.00 12.20 ?  210 ASN H ND2   1 
ATOM   6558  N  N     . LEU E 1 211 ? 14.451  63.712  -5.444  1.00 14.44 ?  211 LEU H N     1 
ATOM   6559  C  CA    . LEU E 1 211 ? 13.935  65.066  -5.528  1.00 15.37 ?  211 LEU H CA    1 
ATOM   6560  C  C     . LEU E 1 211 ? 12.852  65.279  -4.474  1.00 16.22 ?  211 LEU H C     1 
ATOM   6561  O  O     . LEU E 1 211 ? 12.159  64.345  -4.071  1.00 12.23 ?  211 LEU H O     1 
ATOM   6562  C  CB    . LEU E 1 211 ? 13.419  65.338  -6.939  1.00 17.36 ?  211 LEU H CB    1 
ATOM   6563  C  CG    . LEU E 1 211 ? 14.489  65.428  -8.032  1.00 19.41 ?  211 LEU H CG    1 
ATOM   6564  C  CD1   . LEU E 1 211 ? 13.835  65.785  -9.352  1.00 20.63 ?  211 LEU H CD1   1 
ATOM   6565  C  CD2   . LEU E 1 211 ? 15.578  66.430  -7.679  1.00 21.45 ?  211 LEU H CD2   1 
ATOM   6566  N  N     . PRO E 1 212 ? 12.707  66.531  -3.987  1.00 17.78 ?  212 PRO H N     1 
ATOM   6567  C  CA    . PRO E 1 212 ? 11.726  66.861  -2.952  1.00 17.60 ?  212 PRO H CA    1 
ATOM   6568  C  C     . PRO E 1 212 ? 10.268  66.611  -3.343  1.00 20.13 ?  212 PRO H C     1 
ATOM   6569  O  O     . PRO E 1 212 ? 9.441   66.328  -2.478  1.00 18.69 ?  212 PRO H O     1 
ATOM   6570  C  CB    . PRO E 1 212 ? 12.005  68.351  -2.641  1.00 15.95 ?  212 PRO H CB    1 
ATOM   6571  C  CG    . PRO E 1 212 ? 12.806  68.868  -3.820  1.00 17.27 ?  212 PRO H CG    1 
ATOM   6572  C  CD    . PRO E 1 212 ? 13.543  67.674  -4.383  1.00 18.58 ?  212 PRO H CD    1 
ATOM   6573  N  N     . ILE E 1 213 ? 9.962   66.701  -4.644  1.00 22.21 ?  213 ILE H N     1 
ATOM   6574  C  CA    . ILE E 1 213 ? 8.593   66.572  -5.122  1.00 24.82 ?  213 ILE H CA    1 
ATOM   6575  C  C     . ILE E 1 213 ? 8.337   65.139  -5.580  1.00 25.64 ?  213 ILE H C     1 
ATOM   6576  O  O     . ILE E 1 213 ? 7.325   64.863  -6.222  1.00 23.93 ?  213 ILE H O     1 
ATOM   6577  C  CB    . ILE E 1 213 ? 8.293   67.566  -6.262  1.00 26.06 ?  213 ILE H CB    1 
ATOM   6578  C  CG1   . ILE E 1 213 ? 8.906   67.123  -7.599  1.00 27.98 ?  213 ILE H CG1   1 
ATOM   6579  C  CG2   . ILE E 1 213 ? 8.715   68.985  -5.880  1.00 30.24 ?  213 ILE H CG2   1 
ATOM   6580  C  CD1   . ILE E 1 213 ? 10.405  67.333  -7.711  1.00 27.89 ?  213 ILE H CD1   1 
ATOM   6581  N  N     . GLN E 1 214 ? 9.256   64.231  -5.241  1.00 24.93 ?  214 GLN H N     1 
ATOM   6582  C  CA    . GLN E 1 214 ? 9.222   62.882  -5.779  1.00 25.69 ?  214 GLN H CA    1 
ATOM   6583  C  C     . GLN E 1 214 ? 8.865   61.900  -4.670  1.00 24.57 ?  214 GLN H C     1 
ATOM   6584  O  O     . GLN E 1 214 ? 9.458   61.928  -3.594  1.00 31.24 ?  214 GLN H O     1 
ATOM   6585  C  CB    . GLN E 1 214 ? 10.569  62.510  -6.401  1.00 27.19 ?  214 GLN H CB    1 
ATOM   6586  C  CG    . GLN E 1 214 ? 10.635  61.073  -6.910  1.00 27.84 ?  214 GLN H CG    1 
ATOM   6587  C  CD    . GLN E 1 214 ? 12.031  60.626  -7.287  1.00 27.26 ?  214 GLN H CD    1 
ATOM   6588  O  OE1   . GLN E 1 214 ? 13.012  61.365  -7.148  1.00 25.76 ?  214 GLN H OE1   1 
ATOM   6589  N  NE2   . GLN E 1 214 ? 12.131  59.394  -7.766  1.00 27.78 ?  214 GLN H NE2   1 
ATOM   6590  N  N     . ALA E 1 215 ? 7.885   61.039  -4.951  1.00 23.57 ?  215 ALA H N     1 
ATOM   6591  C  CA    . ALA E 1 215 ? 7.537   59.956  -4.049  1.00 26.11 ?  215 ALA H CA    1 
ATOM   6592  C  C     . ALA E 1 215 ? 8.474   58.781  -4.303  1.00 23.93 ?  215 ALA H C     1 
ATOM   6593  O  O     . ALA E 1 215 ? 8.902   58.562  -5.434  1.00 23.35 ?  215 ALA H O     1 
ATOM   6594  C  CB    . ALA E 1 215 ? 6.090   59.563  -4.247  1.00 28.26 ?  215 ALA H CB    1 
ATOM   6595  N  N     . PRO E 1 216 ? 8.825   57.988  -3.266  1.00 24.97 ?  216 PRO H N     1 
ATOM   6596  C  CA    . PRO E 1 216 ? 9.677   56.817  -3.460  1.00 26.58 ?  216 PRO H CA    1 
ATOM   6597  C  C     . PRO E 1 216 ? 8.908   55.700  -4.157  1.00 24.13 ?  216 PRO H C     1 
ATOM   6598  O  O     . PRO E 1 216 ? 7.681   55.655  -4.098  1.00 27.16 ?  216 PRO H O     1 
ATOM   6599  C  CB    . PRO E 1 216 ? 10.060  56.457  -2.021  1.00 25.68 ?  216 PRO H CB    1 
ATOM   6600  C  CG    . PRO E 1 216 ? 8.830   56.841  -1.234  1.00 25.84 ?  216 PRO H CG    1 
ATOM   6601  C  CD    . PRO E 1 216 ? 8.404   58.159  -1.865  1.00 26.59 ?  216 PRO H CD    1 
ATOM   6602  N  N     . ARG E 1 217 ? 9.649   54.809  -4.818  1.00 23.02 ?  217 ARG H N     1 
ATOM   6603  C  CA    . ARG E 1 217 ? 9.072   53.608  -5.393  1.00 21.59 ?  217 ARG H CA    1 
ATOM   6604  C  C     . ARG E 1 217 ? 9.086   52.509  -4.336  1.00 20.49 ?  217 ARG H C     1 
ATOM   6605  O  O     . ARG E 1 217 ? 10.134  52.190  -3.782  1.00 17.65 ?  217 ARG H O     1 
ATOM   6606  C  CB    . ARG E 1 217 ? 9.861   53.163  -6.629  1.00 21.74 ?  217 ARG H CB    1 
ATOM   6607  C  CG    . ARG E 1 217 ? 9.258   51.970  -7.356  1.00 21.12 ?  217 ARG H CG    1 
ATOM   6608  C  CD    . ARG E 1 217 ? 10.171  51.476  -8.467  1.00 23.36 ?  217 ARG H CD    1 
ATOM   6609  N  NE    . ARG E 1 217 ? 9.624   50.322  -9.189  1.00 23.65 ?  217 ARG H NE    1 
ATOM   6610  C  CZ    . ARG E 1 217 ? 10.278  49.648  -10.129 1.00 26.08 ?  217 ARG H CZ    1 
ATOM   6611  N  NH1   . ARG E 1 217 ? 11.521  49.976  -10.437 1.00 25.93 1  217 ARG H NH1   1 
ATOM   6612  N  NH2   . ARG E 1 217 ? 9.690   48.642  -10.751 1.00 23.27 ?  217 ARG H NH2   1 
ATOM   6613  N  N     . ILE E 1 218 ? 7.906   51.950  -4.058  1.00 24.23 ?  218 ILE H N     1 
ATOM   6614  C  CA    . ILE E 1 218 ? 7.773   50.851  -3.116  1.00 26.53 ?  218 ILE H CA    1 
ATOM   6615  C  C     . ILE E 1 218 ? 6.861   49.798  -3.737  1.00 30.88 ?  218 ILE H C     1 
ATOM   6616  O  O     . ILE E 1 218 ? 5.716   49.638  -3.319  1.00 34.84 ?  218 ILE H O     1 
ATOM   6617  C  CB    . ILE E 1 218 ? 7.229   51.345  -1.763  1.00 27.33 ?  218 ILE H CB    1 
ATOM   6618  C  CG1   . ILE E 1 218 ? 8.111   52.438  -1.164  1.00 28.50 ?  218 ILE H CG1   1 
ATOM   6619  C  CG2   . ILE E 1 218 ? 7.038   50.178  -0.793  1.00 26.90 ?  218 ILE H CG2   1 
ATOM   6620  C  CD1   . ILE E 1 218 ? 7.606   52.975  0.163   1.00 31.10 ?  218 ILE H CD1   1 
ATOM   6621  N  N     . GLU E 1 219 ? 7.386   49.083  -4.737  1.00 28.41 ?  219 GLU H N     1 
ATOM   6622  C  CA    . GLU E 1 219 ? 6.577   48.183  -5.540  1.00 25.45 ?  219 GLU H CA    1 
ATOM   6623  C  C     . GLU E 1 219 ? 6.641   46.769  -4.971  1.00 23.23 ?  219 GLU H C     1 
ATOM   6624  O  O     . GLU E 1 219 ? 7.711   46.168  -4.894  1.00 24.10 ?  219 GLU H O     1 
ATOM   6625  C  CB    . GLU E 1 219 ? 7.041   48.212  -6.995  1.00 25.85 ?  219 GLU H CB    1 
ATOM   6626  C  CG    . GLU E 1 219 ? 6.231   47.289  -7.899  1.00 25.09 ?  219 GLU H CG    1 
ATOM   6627  C  CD    . GLU E 1 219 ? 6.595   47.407  -9.366  1.00 26.87 ?  219 GLU H CD    1 
ATOM   6628  O  OE1   . GLU E 1 219 ? 7.422   48.284  -9.693  1.00 27.78 ?  219 GLU H OE1   1 
ATOM   6629  O  OE2   . GLU E 1 219 ? 6.058   46.624  -10.179 1.00 27.75 -1 219 GLU H OE2   1 
ATOM   6630  N  N     . ARG E 1 220 ? 5.468   46.248  -4.599  1.00 21.39 ?  220 ARG H N     1 
ATOM   6631  C  CA    . ARG E 1 220 ? 5.341   44.924  -4.015  1.00 22.50 ?  220 ARG H CA    1 
ATOM   6632  C  C     . ARG E 1 220 ? 4.901   43.925  -5.082  1.00 22.17 ?  220 ARG H C     1 
ATOM   6633  O  O     . ARG E 1 220 ? 4.007   44.212  -5.875  1.00 24.21 ?  220 ARG H O     1 
ATOM   6634  C  CB    . ARG E 1 220 ? 4.322   44.974  -2.871  1.00 24.15 ?  220 ARG H CB    1 
ATOM   6635  C  CG    . ARG E 1 220 ? 4.821   45.691  -1.626  1.00 27.57 ?  220 ARG H CG    1 
ATOM   6636  C  CD    . ARG E 1 220 ? 3.675   46.058  -0.699  1.00 29.28 ?  220 ARG H CD    1 
ATOM   6637  N  NE    . ARG E 1 220 ? 4.117   46.993  0.340   1.00 33.78 ?  220 ARG H NE    1 
ATOM   6638  C  CZ    . ARG E 1 220 ? 4.810   46.661  1.422   1.00 35.56 ?  220 ARG H CZ    1 
ATOM   6639  N  NH1   . ARG E 1 220 ? 5.014   45.389  1.722   1.00 34.00 1  220 ARG H NH1   1 
ATOM   6640  N  NH2   . ARG E 1 220 ? 5.267   47.607  2.222   1.00 32.39 ?  220 ARG H NH2   1 
ATOM   6641  N  N     . LEU E 1 221 ? 5.533   42.745  -5.079  1.00 20.54 ?  221 LEU H N     1 
ATOM   6642  C  CA    . LEU E 1 221 ? 5.237   41.708  -6.055  1.00 20.82 ?  221 LEU H CA    1 
ATOM   6643  C  C     . LEU E 1 221 ? 5.732   40.363  -5.535  1.00 22.78 ?  221 LEU H C     1 
ATOM   6644  O  O     . LEU E 1 221 ? 6.694   40.302  -4.771  1.00 21.95 ?  221 LEU H O     1 
ATOM   6645  C  CB    . LEU E 1 221 ? 5.872   42.015  -7.411  1.00 24.03 ?  221 LEU H CB    1 
ATOM   6646  C  CG    . LEU E 1 221 ? 7.404   41.978  -7.473  1.00 22.76 ?  221 LEU H CG    1 
ATOM   6647  C  CD1   . LEU E 1 221 ? 7.894   41.908  -8.911  1.00 24.95 ?  221 LEU H CD1   1 
ATOM   6648  C  CD2   . LEU E 1 221 ? 8.014   43.181  -6.774  1.00 23.33 ?  221 LEU H CD2   1 
ATOM   6649  N  N     . PRO E 1 222 ? 5.103   39.244  -5.960  1.00 26.01 ?  222 PRO H N     1 
ATOM   6650  C  CA    . PRO E 1 222 ? 5.634   37.913  -5.676  1.00 25.29 ?  222 PRO H CA    1 
ATOM   6651  C  C     . PRO E 1 222 ? 7.036   37.798  -6.266  1.00 22.34 ?  222 PRO H C     1 
ATOM   6652  O  O     . PRO E 1 222 ? 7.335   38.409  -7.288  1.00 22.03 ?  222 PRO H O     1 
ATOM   6653  C  CB    . PRO E 1 222 ? 4.626   36.951  -6.332  1.00 25.93 ?  222 PRO H CB    1 
ATOM   6654  C  CG    . PRO E 1 222 ? 3.899   37.805  -7.351  1.00 26.97 ?  222 PRO H CG    1 
ATOM   6655  C  CD    . PRO E 1 222 ? 3.870   39.206  -6.761  1.00 26.77 ?  222 PRO H CD    1 
ATOM   6656  N  N     . LEU E 1 223 ? 7.886   37.010  -5.602  1.00 22.19 ?  223 LEU H N     1 
ATOM   6657  C  CA    . LEU E 1 223 ? 9.276   36.848  -5.994  1.00 21.15 ?  223 LEU H CA    1 
ATOM   6658  C  C     . LEU E 1 223 ? 9.374   36.388  -7.448  1.00 20.83 ?  223 LEU H C     1 
ATOM   6659  O  O     . LEU E 1 223 ? 10.246  36.840  -8.187  1.00 20.86 ?  223 LEU H O     1 
ATOM   6660  C  CB    . LEU E 1 223 ? 9.905   35.843  -5.030  1.00 21.16 ?  223 LEU H CB    1 
ATOM   6661  C  CG    . LEU E 1 223 ? 11.305  35.330  -5.379  1.00 21.57 ?  223 LEU H CG    1 
ATOM   6662  C  CD1   . LEU E 1 223 ? 12.360  36.423  -5.373  1.00 21.95 ?  223 LEU H CD1   1 
ATOM   6663  C  CD2   . LEU E 1 223 ? 11.662  34.230  -4.396  1.00 22.36 ?  223 LEU H CD2   1 
ATOM   6664  N  N     . ALA E 1 224 ? 8.473   35.486  -7.848  1.00 21.90 ?  224 ALA H N     1 
ATOM   6665  C  CA    . ALA E 1 224 ? 8.528   34.874  -9.166  1.00 26.11 ?  224 ALA H CA    1 
ATOM   6666  C  C     . ALA E 1 224 ? 8.475   35.932  -10.269 1.00 26.35 ?  224 ALA H C     1 
ATOM   6667  O  O     . ALA E 1 224 ? 9.001   35.710  -11.356 1.00 25.53 ?  224 ALA H O     1 
ATOM   6668  C  CB    . ALA E 1 224 ? 7.407   33.866  -9.309  1.00 26.13 ?  224 ALA H CB    1 
ATOM   6669  N  N     . ASN E 1 225 ? 7.850   37.082  -9.987  1.00 26.59 ?  225 ASN H N     1 
ATOM   6670  C  CA    . ASN E 1 225 ? 7.590   38.083  -11.013 1.00 25.38 ?  225 ASN H CA    1 
ATOM   6671  C  C     . ASN E 1 225 ? 8.786   39.018  -11.193 1.00 23.44 ?  225 ASN H C     1 
ATOM   6672  O  O     . ASN E 1 225 ? 8.776   39.863  -12.085 1.00 23.18 ?  225 ASN H O     1 
ATOM   6673  C  CB    . ASN E 1 225 ? 6.329   38.888  -10.713 1.00 26.80 ?  225 ASN H CB    1 
ATOM   6674  C  CG    . ASN E 1 225 ? 5.068   38.077  -10.899 1.00 27.42 ?  225 ASN H CG    1 
ATOM   6675  O  OD1   . ASN E 1 225 ? 5.137   36.876  -11.180 1.00 29.15 ?  225 ASN H OD1   1 
ATOM   6676  N  ND2   . ASN E 1 225 ? 3.913   38.710  -10.746 1.00 28.90 ?  225 ASN H ND2   1 
ATOM   6677  N  N     . LEU E 1 226 ? 9.817   38.860  -10.357 1.00 22.92 ?  226 LEU H N     1 
ATOM   6678  C  CA    . LEU E 1 226 ? 10.947  39.778  -10.346 1.00 22.59 ?  226 LEU H CA    1 
ATOM   6679  C  C     . LEU E 1 226 ? 11.548  39.909  -11.745 1.00 25.34 ?  226 LEU H C     1 
ATOM   6680  O  O     . LEU E 1 226 ? 11.846  41.017  -12.189 1.00 25.07 ?  226 LEU H O     1 
ATOM   6681  C  CB    . LEU E 1 226 ? 11.988  39.305  -9.333  1.00 23.13 ?  226 LEU H CB    1 
ATOM   6682  C  CG    . LEU E 1 226 ? 13.331  40.042  -9.354  1.00 22.77 ?  226 LEU H CG    1 
ATOM   6683  C  CD1   . LEU E 1 226 ? 13.175  41.501  -8.952  1.00 22.84 ?  226 LEU H CD1   1 
ATOM   6684  C  CD2   . LEU E 1 226 ? 14.336  39.336  -8.458  1.00 22.87 ?  226 LEU H CD2   1 
ATOM   6685  N  N     . PRO E 1 227 ? 11.763  38.791  -12.476 1.00 24.59 ?  227 PRO H N     1 
ATOM   6686  C  CA    . PRO E 1 227 ? 12.437  38.832  -13.778 1.00 25.56 ?  227 PRO H CA    1 
ATOM   6687  C  C     . PRO E 1 227 ? 11.728  39.678  -14.833 1.00 24.70 ?  227 PRO H C     1 
ATOM   6688  O  O     . PRO E 1 227 ? 12.353  40.133  -15.788 1.00 22.51 ?  227 PRO H O     1 
ATOM   6689  C  CB    . PRO E 1 227 ? 12.496  37.345  -14.183 1.00 24.66 ?  227 PRO H CB    1 
ATOM   6690  C  CG    . PRO E 1 227 ? 12.380  36.596  -12.876 1.00 25.15 ?  227 PRO H CG    1 
ATOM   6691  C  CD    . PRO E 1 227 ? 11.398  37.425  -12.072 1.00 26.17 ?  227 PRO H CD    1 
ATOM   6692  N  N     . GLN E 1 228 ? 10.417  39.873  -14.660 1.00 28.32 ?  228 GLN H N     1 
ATOM   6693  C  CA    . GLN E 1 228 ? 9.641   40.679  -15.587 1.00 32.97 ?  228 GLN H CA    1 
ATOM   6694  C  C     . GLN E 1 228 ? 9.660   42.140  -15.144 1.00 32.33 ?  228 GLN H C     1 
ATOM   6695  O  O     . GLN E 1 228 ? 9.360   43.032  -15.936 1.00 31.64 ?  228 GLN H O     1 
ATOM   6696  C  CB    . GLN E 1 228 ? 8.206   40.161  -15.706 1.00 35.28 ?  228 GLN H CB    1 
ATOM   6697  C  CG    . GLN E 1 228 ? 8.074   38.858  -16.488 1.00 37.70 ?  228 GLN H CG    1 
ATOM   6698  C  CD    . GLN E 1 228 ? 8.536   37.642  -15.716 1.00 40.54 ?  228 GLN H CD    1 
ATOM   6699  O  OE1   . GLN E 1 228 ? 7.976   37.290  -14.671 1.00 44.13 ?  228 GLN H OE1   1 
ATOM   6700  N  NE2   . GLN E 1 228 ? 9.560   36.977  -16.230 1.00 39.23 ?  228 GLN H NE2   1 
ATOM   6701  N  N     . ALA E 1 229 ? 10.027  42.377  -13.880 1.00 30.91 ?  229 ALA H N     1 
ATOM   6702  C  CA    . ALA E 1 229 ? 9.942   43.703  -13.289 1.00 32.17 ?  229 ALA H CA    1 
ATOM   6703  C  C     . ALA E 1 229 ? 10.830  44.690  -14.042 1.00 32.31 ?  229 ALA H C     1 
ATOM   6704  O  O     . ALA E 1 229 ? 11.810  44.305  -14.676 1.00 33.62 ?  229 ALA H O     1 
ATOM   6705  C  CB    . ALA E 1 229 ? 10.316  43.649  -11.823 1.00 31.35 ?  229 ALA H CB    1 
ATOM   6706  N  N     . HIS E 1 230 ? 10.454  45.970  -13.955 1.00 32.63 ?  230 HIS H N     1 
ATOM   6707  C  CA    . HIS E 1 230 ? 11.261  47.072  -14.448 1.00 31.31 ?  230 HIS H CA    1 
ATOM   6708  C  C     . HIS E 1 230 ? 12.179  47.529  -13.315 1.00 30.11 ?  230 HIS H C     1 
ATOM   6709  O  O     . HIS E 1 230 ? 11.702  47.954  -12.264 1.00 32.71 ?  230 HIS H O     1 
ATOM   6710  C  CB    . HIS E 1 230 ? 10.341  48.176  -14.987 1.00 37.16 ?  230 HIS H CB    1 
ATOM   6711  C  CG    . HIS E 1 230 ? 11.034  49.354  -15.590 1.00 41.87 ?  230 HIS H CG    1 
ATOM   6712  N  ND1   . HIS E 1 230 ? 11.699  49.295  -16.796 1.00 47.83 ?  230 HIS H ND1   1 
ATOM   6713  C  CD2   . HIS E 1 230 ? 11.163  50.616  -15.158 1.00 44.23 ?  230 HIS H CD2   1 
ATOM   6714  C  CE1   . HIS E 1 230 ? 12.207  50.487  -17.073 1.00 48.84 ?  230 HIS H CE1   1 
ATOM   6715  N  NE2   . HIS E 1 230 ? 11.892  51.306  -16.094 1.00 43.40 ?  230 HIS H NE2   1 
ATOM   6716  N  N     . LEU E 1 231 ? 13.495  47.412  -13.532 1.00 28.33 ?  231 LEU H N     1 
ATOM   6717  C  CA    . LEU E 1 231 ? 14.486  47.753  -12.522 1.00 25.33 ?  231 LEU H CA    1 
ATOM   6718  C  C     . LEU E 1 231 ? 15.394  48.857  -13.064 1.00 23.33 ?  231 LEU H C     1 
ATOM   6719  O  O     . LEU E 1 231 ? 15.607  48.955  -14.270 1.00 23.35 ?  231 LEU H O     1 
ATOM   6720  C  CB    . LEU E 1 231 ? 15.298  46.520  -12.119 1.00 24.37 ?  231 LEU H CB    1 
ATOM   6721  C  CG    . LEU E 1 231 ? 14.532  45.368  -11.457 1.00 23.71 ?  231 LEU H CG    1 
ATOM   6722  C  CD1   . LEU E 1 231 ? 15.409  44.128  -11.370 1.00 24.35 ?  231 LEU H CD1   1 
ATOM   6723  C  CD2   . LEU E 1 231 ? 14.029  45.740  -10.074 1.00 22.56 ?  231 LEU H CD2   1 
ATOM   6724  N  N     . MET E 1 232 ? 15.932  49.673  -12.149 1.00 18.80 ?  232 MET H N     1 
ATOM   6725  C  CA    . MET E 1 232 ? 16.788  50.797  -12.496 1.00 18.72 ?  232 MET H CA    1 
ATOM   6726  C  C     . MET E 1 232 ? 18.077  50.716  -11.680 1.00 18.16 ?  232 MET H C     1 
ATOM   6727  O  O     . MET E 1 232 ? 18.112  50.046  -10.650 1.00 16.33 ?  232 MET H O     1 
ATOM   6728  C  CB    . MET E 1 232 ? 16.070  52.119  -12.199 1.00 22.19 ?  232 MET H CB    1 
ATOM   6729  C  CG    . MET E 1 232 ? 14.744  52.282  -12.922 1.00 21.93 ?  232 MET H CG    1 
ATOM   6730  S  SD    . MET E 1 232 ? 14.942  52.491  -14.703 1.00 24.28 ?  232 MET H SD    1 
ATOM   6731  C  CE    . MET E 1 232 ? 16.202  53.772  -14.749 1.00 24.70 ?  232 MET H CE    1 
ATOM   6732  N  N     . PRO E 1 233 ? 19.177  51.385  -12.100 1.00 17.99 ?  233 PRO H N     1 
ATOM   6733  C  CA    . PRO E 1 233 ? 20.446  51.298  -11.372 1.00 18.50 ?  233 PRO H CA    1 
ATOM   6734  C  C     . PRO E 1 233 ? 20.340  51.670  -9.895  1.00 18.58 ?  233 PRO H C     1 
ATOM   6735  O  O     . PRO E 1 233 ? 21.187  51.276  -9.095  1.00 17.64 ?  233 PRO H O     1 
ATOM   6736  C  CB    . PRO E 1 233 ? 21.377  52.253  -12.140 1.00 16.72 ?  233 PRO H CB    1 
ATOM   6737  C  CG    . PRO E 1 233 ? 20.779  52.317  -13.528 1.00 18.14 ?  233 PRO H CG    1 
ATOM   6738  C  CD    . PRO E 1 233 ? 19.275  52.218  -13.309 1.00 18.97 ?  233 PRO H CD    1 
ATOM   6739  N  N     . ILE E 1 234 ? 19.295  52.424  -9.535  1.00 18.58 ?  234 ILE H N     1 
ATOM   6740  C  CA    . ILE E 1 234 ? 19.145  52.896  -8.168  1.00 19.36 ?  234 ILE H CA    1 
ATOM   6741  C  C     . ILE E 1 234 ? 18.319  51.898  -7.362  1.00 18.60 ?  234 ILE H C     1 
ATOM   6742  O  O     . ILE E 1 234 ? 18.161  52.066  -6.156  1.00 18.58 ?  234 ILE H O     1 
ATOM   6743  C  CB    . ILE E 1 234 ? 18.528  54.308  -8.116  1.00 23.11 ?  234 ILE H CB    1 
ATOM   6744  C  CG1   . ILE E 1 234 ? 17.173  54.374  -8.830  1.00 24.75 ?  234 ILE H CG1   1 
ATOM   6745  C  CG2   . ILE E 1 234 ? 19.508  55.347  -8.659  1.00 25.44 ?  234 ILE H CG2   1 
ATOM   6746  C  CD1   . ILE E 1 234 ? 16.603  55.775  -8.958  1.00 25.24 ?  234 ILE H CD1   1 
ATOM   6747  N  N     . SER E 1 235 ? 17.816  50.851  -8.026  1.00 18.44 ?  235 SER H N     1 
ATOM   6748  C  CA    . SER E 1 235 ? 16.837  49.966  -7.418  1.00 17.69 ?  235 SER H CA    1 
ATOM   6749  C  C     . SER E 1 235 ? 17.496  49.041  -6.401  1.00 18.57 ?  235 SER H C     1 
ATOM   6750  O  O     . SER E 1 235 ? 18.553  48.467  -6.655  1.00 21.98 ?  235 SER H O     1 
ATOM   6751  C  CB    . SER E 1 235 ? 16.089  49.175  -8.460  1.00 19.43 ?  235 SER H CB    1 
ATOM   6752  O  OG    . SER E 1 235 ? 15.342  50.031  -9.312  1.00 17.24 ?  235 SER H OG    1 
ATOM   6753  N  N     . THR E 1 236 ? 16.840  48.911  -5.244  1.00 20.54 ?  236 THR H N     1 
ATOM   6754  C  CA    . THR E 1 236 ? 17.218  47.946  -4.229  1.00 19.00 ?  236 THR H CA    1 
ATOM   6755  C  C     . THR E 1 236 ? 16.054  46.983  -4.022  1.00 18.54 ?  236 THR H C     1 
ATOM   6756  O  O     . THR E 1 236 ? 14.898  47.401  -3.984  1.00 19.75 ?  236 THR H O     1 
ATOM   6757  C  CB    . THR E 1 236 ? 17.582  48.666  -2.932  1.00 19.53 ?  236 THR H CB    1 
ATOM   6758  O  OG1   . THR E 1 236 ? 18.773  49.393  -3.215  1.00 18.51 ?  236 THR H OG1   1 
ATOM   6759  C  CG2   . THR E 1 236 ? 17.822  47.699  -1.787  1.00 20.31 ?  236 THR H CG2   1 
ATOM   6760  N  N     . LEU E 1 237 ? 16.378  45.694  -3.893  1.00 16.86 ?  237 LEU H N     1 
ATOM   6761  C  CA    . LEU E 1 237 ? 15.384  44.666  -3.641  1.00 15.60 ?  237 LEU H CA    1 
ATOM   6762  C  C     . LEU E 1 237 ? 15.352  44.341  -2.149  1.00 16.77 ?  237 LEU H C     1 
ATOM   6763  O  O     . LEU E 1 237 ? 16.377  43.992  -1.568  1.00 14.09 ?  237 LEU H O     1 
ATOM   6764  C  CB    . LEU E 1 237 ? 15.701  43.417  -4.460  1.00 13.91 ?  237 LEU H CB    1 
ATOM   6765  C  CG    . LEU E 1 237 ? 14.734  42.247  -4.255  1.00 14.17 ?  237 LEU H CG    1 
ATOM   6766  C  CD1   . LEU E 1 237 ? 13.366  42.635  -4.785  1.00 13.61 ?  237 LEU H CD1   1 
ATOM   6767  C  CD2   . LEU E 1 237 ? 15.220  40.955  -4.890  1.00 16.12 ?  237 LEU H CD2   1 
ATOM   6768  N  N     . LEU E 1 238 ? 14.162  44.452  -1.547  1.00 19.81 ?  238 LEU H N     1 
ATOM   6769  C  CA    . LEU E 1 238 ? 13.953  44.062  -0.161  1.00 21.47 ?  238 LEU H CA    1 
ATOM   6770  C  C     . LEU E 1 238 ? 13.210  42.732  -0.126  1.00 23.09 ?  238 LEU H C     1 
ATOM   6771  O  O     . LEU E 1 238 ? 12.151  42.589  -0.735  1.00 24.47 ?  238 LEU H O     1 
ATOM   6772  C  CB    . LEU E 1 238 ? 13.175  45.122  0.616   1.00 22.77 ?  238 LEU H CB    1 
ATOM   6773  C  CG    . LEU E 1 238 ? 12.716  44.720  2.023   1.00 22.60 ?  238 LEU H CG    1 
ATOM   6774  C  CD1   . LEU E 1 238 ? 13.834  44.758  3.054   1.00 23.15 ?  238 LEU H CD1   1 
ATOM   6775  C  CD2   . LEU E 1 238 ? 11.569  45.612  2.457   1.00 24.03 ?  238 LEU H CD2   1 
ATOM   6776  N  N     . ILE E 1 239 ? 13.771  41.770  0.610   1.00 22.94 ?  239 ILE H N     1 
ATOM   6777  C  CA    . ILE E 1 239 ? 13.112  40.494  0.817   1.00 24.70 ?  239 ILE H CA    1 
ATOM   6778  C  C     . ILE E 1 239 ? 12.717  40.372  2.287   1.00 24.98 ?  239 ILE H C     1 
ATOM   6779  O  O     . ILE E 1 239 ? 13.545  40.050  3.136   1.00 29.85 ?  239 ILE H O     1 
ATOM   6780  C  CB    . ILE E 1 239 ? 14.018  39.342  0.346   1.00 24.02 ?  239 ILE H CB    1 
ATOM   6781  C  CG1   . ILE E 1 239 ? 14.485  39.573  -1.096  1.00 25.39 ?  239 ILE H CG1   1 
ATOM   6782  C  CG2   . ILE E 1 239 ? 13.316  37.995  0.517   1.00 23.10 ?  239 ILE H CG2   1 
ATOM   6783  C  CD1   . ILE E 1 239 ? 15.452  38.528  -1.622  1.00 26.41 ?  239 ILE H CD1   1 
ATOM   6784  N  N     . PRO E 1 240 ? 11.437  40.653  2.628   1.00 28.16 ?  240 PRO H N     1 
ATOM   6785  C  CA    . PRO E 1 240 ? 10.948  40.521  4.003   1.00 24.09 ?  240 PRO H CA    1 
ATOM   6786  C  C     . PRO E 1 240 ? 11.018  39.091  4.532   1.00 23.11 ?  240 PRO H C     1 
ATOM   6787  O  O     . PRO E 1 240 ? 11.005  38.135  3.759   1.00 19.94 ?  240 PRO H O     1 
ATOM   6788  C  CB    . PRO E 1 240 ? 9.492   41.027  3.916   1.00 24.31 ?  240 PRO H CB    1 
ATOM   6789  C  CG    . PRO E 1 240 ? 9.451   41.858  2.652   1.00 24.69 ?  240 PRO H CG    1 
ATOM   6790  C  CD    . PRO E 1 240 ? 10.406  41.153  1.706   1.00 27.62 ?  240 PRO H CD    1 
ATOM   6791  N  N     . PRO E 1 241 ? 11.091  38.910  5.871   1.00 24.71 ?  241 PRO H N     1 
ATOM   6792  C  CA    . PRO E 1 241 ? 11.152  37.578  6.475   1.00 27.40 ?  241 PRO H CA    1 
ATOM   6793  C  C     . PRO E 1 241 ? 10.194  36.569  5.850   1.00 29.31 ?  241 PRO H C     1 
ATOM   6794  O  O     . PRO E 1 241 ? 9.048   36.897  5.551   1.00 30.89 ?  241 PRO H O     1 
ATOM   6795  C  CB    . PRO E 1 241 ? 10.797  37.867  7.943   1.00 25.72 ?  241 PRO H CB    1 
ATOM   6796  C  CG    . PRO E 1 241 ? 11.333  39.259  8.187   1.00 27.20 ?  241 PRO H CG    1 
ATOM   6797  C  CD    . PRO E 1 241 ? 11.142  39.991  6.868   1.00 26.93 ?  241 PRO H CD    1 
ATOM   6798  N  N     . ALA E 1 242 ? 10.681  35.337  5.670   1.00 32.82 ?  242 ALA H N     1 
ATOM   6799  C  CA    . ALA E 1 242 ? 9.850   34.241  5.200   1.00 36.42 ?  242 ALA H CA    1 
ATOM   6800  C  C     . ALA E 1 242 ? 9.334   33.434  6.390   1.00 40.30 ?  242 ALA H C     1 
ATOM   6801  O  O     . ALA E 1 242 ? 8.371   32.681  6.260   1.00 37.03 ?  242 ALA H O     1 
ATOM   6802  C  CB    . ALA E 1 242 ? 10.633  33.373  4.238   1.00 38.61 ?  242 ALA H CB    1 
ATOM   6803  N  N     . LYS E 1 243 ? 9.983   33.603  7.549   1.00 48.43 ?  243 LYS H N     1 
ATOM   6804  C  CA    . LYS E 1 243 ? 9.627   32.872  8.757   1.00 52.33 ?  243 LYS H CA    1 
ATOM   6805  C  C     . LYS E 1 243 ? 9.519   33.832  9.938   1.00 53.56 ?  243 LYS H C     1 
ATOM   6806  O  O     . LYS E 1 243 ? 10.148  34.888  9.946   1.00 46.62 ?  243 LYS H O     1 
ATOM   6807  C  CB    . LYS E 1 243 ? 10.685  31.812  9.087   1.00 56.00 ?  243 LYS H CB    1 
ATOM   6808  C  CG    . LYS E 1 243 ? 10.610  30.518  8.290   1.00 63.16 ?  243 LYS H CG    1 
ATOM   6809  C  CD    . LYS E 1 243 ? 11.902  29.709  8.310   1.00 67.99 ?  243 LYS H CD    1 
ATOM   6810  C  CE    . LYS E 1 243 ? 12.506  29.583  9.674   1.00 67.69 ?  243 LYS H CE    1 
ATOM   6811  N  NZ    . LYS E 1 243 ? 13.718  28.761  9.651   1.00 63.38 1  243 LYS H NZ    1 
ATOM   6812  N  N     . LYS E 1 244 ? 8.719   33.443  10.939  1.00 56.48 ?  244 LYS H N     1 
ATOM   6813  C  CA    . LYS E 1 244 ? 8.632   34.181  12.190  1.00 58.20 ?  244 LYS H CA    1 
ATOM   6814  C  C     . LYS E 1 244 ? 9.713   33.676  13.142  1.00 52.81 ?  244 LYS H C     1 
ATOM   6815  O  O     . LYS E 1 244 ? 10.163  32.538  13.031  1.00 52.30 ?  244 LYS H O     1 
ATOM   6816  C  CB    . LYS E 1 244 ? 7.253   34.055  12.850  1.00 61.97 ?  244 LYS H CB    1 
ATOM   6817  C  CG    . LYS E 1 244 ? 6.101   34.708  12.097  1.00 69.21 ?  244 LYS H CG    1 
ATOM   6818  C  CD    . LYS E 1 244 ? 4.934   35.117  12.990  1.00 73.53 ?  244 LYS H CD    1 
ATOM   6819  C  CE    . LYS E 1 244 ? 4.190   33.965  13.587  1.00 75.03 ?  244 LYS H CE    1 
ATOM   6820  N  NZ    . LYS E 1 244 ? 3.321   33.310  12.607  1.00 75.60 1  244 LYS H NZ    1 
ATOM   6821  N  N     . LEU E 1 245 ? 10.114  34.541  14.080  1.00 50.26 ?  245 LEU H N     1 
ATOM   6822  C  CA    . LEU E 1 245 ? 11.198  34.244  15.002  1.00 55.01 ?  245 LEU H CA    1 
ATOM   6823  C  C     . LEU E 1 245 ? 10.819  33.050  15.875  1.00 58.41 ?  245 LEU H C     1 
ATOM   6824  O  O     . LEU E 1 245 ? 9.804   33.078  16.567  1.00 59.33 ?  245 LEU H O     1 
ATOM   6825  C  CB    . LEU E 1 245 ? 11.503  35.478  15.850  1.00 51.79 ?  245 LEU H CB    1 
ATOM   6826  C  CG    . LEU E 1 245 ? 12.023  36.704  15.093  1.00 50.23 ?  245 LEU H CG    1 
ATOM   6827  C  CD1   . LEU E 1 245 ? 11.994  37.929  15.990  1.00 49.69 ?  245 LEU H CD1   1 
ATOM   6828  C  CD2   . LEU E 1 245 ? 13.425  36.468  14.558  1.00 52.90 ?  245 LEU H CD2   1 
ATOM   6829  N  N     . GLU E 1 246 ? 11.657  32.008  15.833  1.00 59.47 ?  246 GLU H N     1 
ATOM   6830  C  CA    . GLU E 1 246 ? 11.442  30.804  16.618  1.00 59.86 ?  246 GLU H CA    1 
ATOM   6831  C  C     . GLU E 1 246 ? 12.401  30.802  17.807  1.00 60.86 ?  246 GLU H C     1 
ATOM   6832  O  O     . GLU E 1 246 ? 13.542  31.247  17.695  1.00 56.65 ?  246 GLU H O     1 
ATOM   6833  C  CB    . GLU E 1 246 ? 11.594  29.574  15.722  1.00 62.99 ?  246 GLU H CB    1 
ATOM   6834  C  CG    . GLU E 1 246 ? 10.582  29.542  14.580  1.00 61.82 ?  246 GLU H CG    1 
ATOM   6835  C  CD    . GLU E 1 246 ? 10.522  28.233  13.813  1.00 57.59 ?  246 GLU H CD    1 
ATOM   6836  O  OE1   . GLU E 1 246 ? 11.428  27.978  12.992  1.00 55.75 ?  246 GLU H OE1   1 
ATOM   6837  O  OE2   . GLU E 1 246 ? 9.568   27.462  14.049  1.00 56.53 -1 246 GLU H OE2   1 
ATOM   6838  N  N     . TYR E 1 247 ? 11.918  30.288  18.944  1.00 60.07 ?  247 TYR H N     1 
ATOM   6839  C  CA    . TYR E 1 247 ? 12.609  30.422  20.217  1.00 57.02 ?  247 TYR H CA    1 
ATOM   6840  C  C     . TYR E 1 247 ? 13.847  29.533  20.243  1.00 49.95 ?  247 TYR H C     1 
ATOM   6841  O  O     . TYR E 1 247 ? 13.814  28.387  19.800  1.00 45.67 ?  247 TYR H O     1 
ATOM   6842  C  CB    . TYR E 1 247 ? 11.717  30.074  21.411  1.00 57.70 ?  247 TYR H CB    1 
ATOM   6843  C  CG    . TYR E 1 247 ? 10.677  31.136  21.737  1.00 59.95 ?  247 TYR H CG    1 
ATOM   6844  C  CD1   . TYR E 1 247 ? 11.034  32.310  22.387  1.00 57.53 ?  247 TYR H CD1   1 
ATOM   6845  C  CD2   . TYR E 1 247 ? 9.340   30.958  21.404  1.00 61.75 ?  247 TYR H CD2   1 
ATOM   6846  C  CE1   . TYR E 1 247 ? 10.095  33.282  22.688  1.00 61.42 ?  247 TYR H CE1   1 
ATOM   6847  C  CE2   . TYR E 1 247 ? 8.391   31.921  21.701  1.00 64.66 ?  247 TYR H CE2   1 
ATOM   6848  C  CZ    . TYR E 1 247 ? 8.770   33.086  22.344  1.00 65.53 ?  247 TYR H CZ    1 
ATOM   6849  O  OH    . TYR E 1 247 ? 7.840   34.040  22.641  1.00 74.75 ?  247 TYR H OH    1 
ATOM   6850  N  N     . ASN E 1 248 ? 14.924  30.091  20.803  1.00 46.92 ?  248 ASN H N     1 
ATOM   6851  C  CA    . ASN E 1 248 ? 16.200  29.407  20.903  1.00 41.83 ?  248 ASN H CA    1 
ATOM   6852  C  C     . ASN E 1 248 ? 16.314  28.773  22.287  1.00 41.83 ?  248 ASN H C     1 
ATOM   6853  O  O     . ASN E 1 248 ? 16.827  29.390  23.219  1.00 36.48 ?  248 ASN H O     1 
ATOM   6854  C  CB    . ASN E 1 248 ? 17.343  30.368  20.598  1.00 37.94 ?  248 ASN H CB    1 
ATOM   6855  C  CG    . ASN E 1 248 ? 18.651  29.646  20.388  1.00 31.12 ?  248 ASN H CG    1 
ATOM   6856  O  OD1   . ASN E 1 248 ? 18.762  28.456  20.702  1.00 29.34 ?  248 ASN H OD1   1 
ATOM   6857  N  ND2   . ASN E 1 248 ? 19.646  30.343  19.860  1.00 28.88 ?  248 ASN H ND2   1 
ATOM   6858  N  N     . TYR E 1 249 ? 15.835  27.530  22.403  1.00 43.22 ?  249 TYR H N     1 
ATOM   6859  C  CA    . TYR E 1 249 ? 15.684  26.875  23.693  1.00 46.48 ?  249 TYR H CA    1 
ATOM   6860  C  C     . TYR E 1 249 ? 17.048  26.598  24.316  1.00 42.82 ?  249 TYR H C     1 
ATOM   6861  O  O     . TYR E 1 249 ? 17.213  26.713  25.528  1.00 39.29 ?  249 TYR H O     1 
ATOM   6862  C  CB    . TYR E 1 249 ? 14.884  25.577  23.551  1.00 51.16 ?  249 TYR H CB    1 
ATOM   6863  C  CG    . TYR E 1 249 ? 13.410  25.817  23.262  1.00 59.59 ?  249 TYR H CG    1 
ATOM   6864  C  CD1   . TYR E 1 249 ? 12.553  26.250  24.265  1.00 61.89 ?  249 TYR H CD1   1 
ATOM   6865  C  CD2   . TYR E 1 249 ? 12.881  25.621  21.993  1.00 61.73 ?  249 TYR H CD2   1 
ATOM   6866  C  CE1   . TYR E 1 249 ? 11.211  26.481  24.015  1.00 65.43 ?  249 TYR H CE1   1 
ATOM   6867  C  CE2   . TYR E 1 249 ? 11.539  25.845  21.731  1.00 64.87 ?  249 TYR H CE2   1 
ATOM   6868  C  CZ    . TYR E 1 249 ? 10.703  26.276  22.745  1.00 63.69 ?  249 TYR H CZ    1 
ATOM   6869  O  OH    . TYR E 1 249 ? 9.380   26.500  22.496  1.00 68.02 ?  249 TYR H OH    1 
ATOM   6870  N  N     . ALA E 1 250 ? 18.014  26.221  23.475  1.00 42.76 ?  250 ALA H N     1 
ATOM   6871  C  CA    . ALA E 1 250 ? 19.327  25.822  23.950  1.00 36.07 ?  250 ALA H CA    1 
ATOM   6872  C  C     . ALA E 1 250 ? 19.910  26.912  24.844  1.00 31.51 ?  250 ALA H C     1 
ATOM   6873  O  O     . ALA E 1 250 ? 20.422  26.631  25.926  1.00 34.41 ?  250 ALA H O     1 
ATOM   6874  C  CB    . ALA E 1 250 ? 20.229  25.536  22.770  1.00 36.60 ?  250 ALA H CB    1 
ATOM   6875  N  N     . ILE E 1 251 ? 19.809  28.158  24.374  1.00 28.91 ?  251 ILE H N     1 
ATOM   6876  C  CA    . ILE E 1 251 ? 20.496  29.283  24.986  1.00 29.11 ?  251 ILE H CA    1 
ATOM   6877  C  C     . ILE E 1 251 ? 19.659  29.828  26.142  1.00 26.39 ?  251 ILE H C     1 
ATOM   6878  O  O     . ILE E 1 251 ? 20.203  30.360  27.107  1.00 27.98 ?  251 ILE H O     1 
ATOM   6879  C  CB    . ILE E 1 251 ? 20.795  30.361  23.928  1.00 29.95 ?  251 ILE H CB    1 
ATOM   6880  C  CG1   . ILE E 1 251 ? 21.544  29.779  22.722  1.00 31.69 ?  251 ILE H CG1   1 
ATOM   6881  C  CG2   . ILE E 1 251 ? 21.543  31.543  24.545  1.00 31.47 ?  251 ILE H CG2   1 
ATOM   6882  C  CD1   . ILE E 1 251 ? 22.864  29.111  23.069  1.00 29.87 ?  251 ILE H CD1   1 
ATOM   6883  N  N     . LEU E 1 252 ? 18.333  29.696  26.035  1.00 24.13 ?  252 LEU H N     1 
ATOM   6884  C  CA    . LEU E 1 252 ? 17.440  30.083  27.116  1.00 24.04 ?  252 LEU H CA    1 
ATOM   6885  C  C     . LEU E 1 252 ? 17.707  29.187  28.323  1.00 25.26 ?  252 LEU H C     1 
ATOM   6886  O  O     . LEU E 1 252 ? 17.726  29.659  29.458  1.00 25.79 ?  252 LEU H O     1 
ATOM   6887  C  CB    . LEU E 1 252 ? 15.981  30.006  26.667  1.00 22.56 ?  252 LEU H CB    1 
ATOM   6888  C  CG    . LEU E 1 252 ? 15.539  31.038  25.624  1.00 22.10 ?  252 LEU H CG    1 
ATOM   6889  C  CD1   . LEU E 1 252 ? 14.144  30.708  25.127  1.00 20.70 ?  252 LEU H CD1   1 
ATOM   6890  C  CD2   . LEU E 1 252 ? 15.585  32.462  26.160  1.00 21.76 ?  252 LEU H CD2   1 
ATOM   6891  N  N     . ALA E 1 253 ? 17.919  27.892  28.058  1.00 27.24 ?  253 ALA H N     1 
ATOM   6892  C  CA    . ALA E 1 253 ? 18.233  26.925  29.097  1.00 26.69 ?  253 ALA H CA    1 
ATOM   6893  C  C     . ALA E 1 253 ? 19.528  27.317  29.805  1.00 29.51 ?  253 ALA H C     1 
ATOM   6894  O  O     . ALA E 1 253 ? 19.592  27.293  31.032  1.00 31.72 ?  253 ALA H O     1 
ATOM   6895  C  CB    . ALA E 1 253 ? 18.322  25.536  28.503  1.00 27.56 ?  253 ALA H CB    1 
ATOM   6896  N  N     . LYS E 1 254 ? 20.556  27.679  29.028  1.00 30.67 ?  254 LYS H N     1 
ATOM   6897  C  CA    . LYS E 1 254 ? 21.836  28.066  29.602  1.00 36.29 ?  254 LYS H CA    1 
ATOM   6898  C  C     . LYS E 1 254 ? 21.650  29.350  30.412  1.00 40.14 ?  254 LYS H C     1 
ATOM   6899  O  O     . LYS E 1 254 ? 22.282  29.522  31.452  1.00 39.05 ?  254 LYS H O     1 
ATOM   6900  C  CB    . LYS E 1 254 ? 22.932  28.180  28.533  1.00 41.81 ?  254 LYS H CB    1 
ATOM   6901  C  CG    . LYS E 1 254 ? 23.258  26.877  27.801  1.00 49.20 ?  254 LYS H CG    1 
ATOM   6902  C  CD    . LYS E 1 254 ? 24.438  26.937  26.836  1.00 53.00 ?  254 LYS H CD    1 
ATOM   6903  C  CE    . LYS E 1 254 ? 25.772  26.893  27.515  1.00 54.74 ?  254 LYS H CE    1 
ATOM   6904  N  NZ    . LYS E 1 254 ? 26.875  26.980  26.554  1.00 55.19 1  254 LYS H NZ    1 
ATOM   6905  N  N     . LEU E 1 255 ? 20.771  30.242  29.934  1.00 34.90 ?  255 LEU H N     1 
ATOM   6906  C  CA    . LEU E 1 255 ? 20.430  31.455  30.662  1.00 33.58 ?  255 LEU H CA    1 
ATOM   6907  C  C     . LEU E 1 255 ? 19.470  31.110  31.799  1.00 36.71 ?  255 LEU H C     1 
ATOM   6908  O  O     . LEU E 1 255 ? 19.139  31.967  32.615  1.00 27.87 ?  255 LEU H O     1 
ATOM   6909  C  CB    . LEU E 1 255 ? 19.817  32.503  29.732  1.00 30.87 ?  255 LEU H CB    1 
ATOM   6910  C  CG    . LEU E 1 255 ? 20.743  33.100  28.668  1.00 27.75 ?  255 LEU H CG    1 
ATOM   6911  C  CD1   . LEU E 1 255 ? 19.920  33.771  27.583  1.00 29.32 ?  255 LEU H CD1   1 
ATOM   6912  C  CD2   . LEU E 1 255 ? 21.728  34.089  29.266  1.00 27.01 ?  255 LEU H CD2   1 
ATOM   6913  N  N     . GLY E 1 256 ? 19.014  29.851  31.828  1.00 39.04 ?  256 GLY H N     1 
ATOM   6914  C  CA    . GLY E 1 256 ? 18.174  29.348  32.903  1.00 37.08 ?  256 GLY H CA    1 
ATOM   6915  C  C     . GLY E 1 256 ? 16.776  29.962  32.877  1.00 37.04 ?  256 GLY H C     1 
ATOM   6916  O  O     . GLY E 1 256 ? 16.142  30.109  33.920  1.00 37.71 ?  256 GLY H O     1 
ATOM   6917  N  N     . ILE E 1 257 ? 16.299  30.303  31.674  1.00 38.08 ?  257 ILE H N     1 
ATOM   6918  C  CA    . ILE E 1 257 ? 15.016  30.968  31.512  1.00 35.89 ?  257 ILE H CA    1 
ATOM   6919  C  C     . ILE E 1 257 ? 14.217  30.273  30.411  1.00 38.11 ?  257 ILE H C     1 
ATOM   6920  O  O     . ILE E 1 257 ? 14.655  29.271  29.852  1.00 37.35 ?  257 ILE H O     1 
ATOM   6921  C  CB    . ILE E 1 257 ? 15.215  32.465  31.206  1.00 37.02 ?  257 ILE H CB    1 
ATOM   6922  C  CG1   . ILE E 1 257 ? 15.877  32.682  29.843  1.00 33.85 ?  257 ILE H CG1   1 
ATOM   6923  C  CG2   . ILE E 1 257 ? 15.996  33.152  32.328  1.00 39.36 ?  257 ILE H CG2   1 
ATOM   6924  C  CD1   . ILE E 1 257 ? 16.007  34.140  29.439  1.00 33.86 ?  257 ILE H CD1   1 
ATOM   6925  N  N     . GLY E 1 258 ? 13.032  30.824  30.119  1.00 41.94 ?  258 GLY H N     1 
ATOM   6926  C  CA    . GLY E 1 258 ? 12.202  30.365  29.017  1.00 43.16 ?  258 GLY H CA    1 
ATOM   6927  C  C     . GLY E 1 258 ? 11.377  31.515  28.445  1.00 41.66 ?  258 GLY H C     1 
ATOM   6928  O  O     . GLY E 1 258 ? 11.453  32.638  28.939  1.00 42.69 ?  258 GLY H O     1 
ATOM   6929  N  N     . PRO E 1 259 ? 10.560  31.276  27.393  1.00 38.19 ?  259 PRO H N     1 
ATOM   6930  C  CA    . PRO E 1 259 ? 9.805   32.353  26.748  1.00 37.70 ?  259 PRO H CA    1 
ATOM   6931  C  C     . PRO E 1 259 ? 9.011   33.192  27.745  1.00 40.74 ?  259 PRO H C     1 
ATOM   6932  O  O     . PRO E 1 259 ? 8.998   34.419  27.671  1.00 36.06 ?  259 PRO H O     1 
ATOM   6933  C  CB    . PRO E 1 259 ? 8.889   31.591  25.772  1.00 35.83 ?  259 PRO H CB    1 
ATOM   6934  C  CG    . PRO E 1 259 ? 9.652   30.323  25.463  1.00 35.16 ?  259 PRO H CG    1 
ATOM   6935  C  CD    . PRO E 1 259 ? 10.320  29.961  26.778  1.00 36.67 ?  259 PRO H CD    1 
ATOM   6936  N  N     . GLU E 1 260 ? 8.356   32.499  28.682  1.00 43.78 ?  260 GLU H N     1 
ATOM   6937  C  CA    . GLU E 1 260 ? 7.438   33.116  29.624  1.00 46.15 ?  260 GLU H CA    1 
ATOM   6938  C  C     . GLU E 1 260 ? 8.164   34.135  30.501  1.00 47.07 ?  260 GLU H C     1 
ATOM   6939  O  O     . GLU E 1 260 ? 7.529   35.013  31.081  1.00 43.84 ?  260 GLU H O     1 
ATOM   6940  C  CB    . GLU E 1 260 ? 6.780   32.040  30.489  1.00 44.26 ?  260 GLU H CB    1 
ATOM   6941  C  CG    . GLU E 1 260 ? 7.771   31.264  31.353  1.00 45.68 ?  260 GLU H CG    1 
ATOM   6942  C  CD    . GLU E 1 260 ? 8.441   30.083  30.674  1.00 40.10 ?  260 GLU H CD    1 
ATOM   6943  O  OE1   . GLU E 1 260 ? 8.796   30.194  29.481  1.00 33.51 ?  260 GLU H OE1   1 
ATOM   6944  O  OE2   . GLU E 1 260 ? 8.627   29.053  31.356  1.00 38.62 -1 260 GLU H OE2   1 
ATOM   6945  N  N     . ASP E 1 261 ? 9.492   34.009  30.600  1.00 47.47 ?  261 ASP H N     1 
ATOM   6946  C  CA    . ASP E 1 261 ? 10.277  34.882  31.458  1.00 46.02 ?  261 ASP H CA    1 
ATOM   6947  C  C     . ASP E 1 261 ? 10.756  36.101  30.671  1.00 47.16 ?  261 ASP H C     1 
ATOM   6948  O  O     . ASP E 1 261 ? 11.113  37.116  31.264  1.00 46.21 ?  261 ASP H O     1 
ATOM   6949  C  CB    . ASP E 1 261 ? 11.430  34.139  32.117  1.00 46.49 ?  261 ASP H CB    1 
ATOM   6950  C  CG    . ASP E 1 261 ? 11.026  33.064  33.117  1.00 42.97 ?  261 ASP H CG    1 
ATOM   6951  O  OD1   . ASP E 1 261 ? 10.241  33.383  34.034  1.00 40.55 ?  261 ASP H OD1   1 
ATOM   6952  O  OD2   . ASP E 1 261 ? 11.506  31.919  32.975  1.00 44.17 -1 261 ASP H OD2   1 
ATOM   6953  N  N     . LEU E 1 262 ? 10.763  35.996  29.338  1.00 46.09 ?  262 LEU H N     1 
ATOM   6954  C  CA    . LEU E 1 262 ? 11.151  37.116  28.497  1.00 44.93 ?  262 LEU H CA    1 
ATOM   6955  C  C     . LEU E 1 262 ? 10.275  38.315  28.855  1.00 48.75 ?  262 LEU H C     1 
ATOM   6956  O  O     . LEU E 1 262 ? 9.051   38.211  28.885  1.00 48.49 ?  262 LEU H O     1 
ATOM   6957  C  CB    . LEU E 1 262 ? 11.046  36.754  27.015  1.00 45.83 ?  262 LEU H CB    1 
ATOM   6958  C  CG    . LEU E 1 262 ? 11.937  35.597  26.546  1.00 43.06 ?  262 LEU H CG    1 
ATOM   6959  C  CD1   . LEU E 1 262 ? 11.690  35.246  25.088  1.00 41.50 ?  262 LEU H CD1   1 
ATOM   6960  C  CD2   . LEU E 1 262 ? 13.406  35.918  26.765  1.00 43.06 ?  262 LEU H CD2   1 
ATOM   6961  N  N     . GLY E 1 263 ? 10.927  39.448  29.140  1.00 48.18 ?  263 GLY H N     1 
ATOM   6962  C  CA    . GLY E 1 263 ? 10.240  40.656  29.567  1.00 50.26 ?  263 GLY H CA    1 
ATOM   6963  C  C     . GLY E 1 263 ? 9.620   41.387  28.391  1.00 50.70 ?  263 GLY H C     1 
ATOM   6964  O  O     . GLY E 1 263 ? 10.010  41.062  27.250  1.00 54.22 ?  263 GLY H O     1 
ATOM   6965  O  OXT   . GLY E 1 263 ? 8.767   42.261  28.652  1.00 51.29 -1 263 GLY H OXT   1 
ATOM   6966  N  N     . GLY F 3 10  ? 14.999  78.452  -12.436 1.00 37.78 ?  3   GLY I N     1 
ATOM   6967  C  CA    . GLY F 3 10  ? 13.616  78.598  -11.941 1.00 33.78 ?  3   GLY I CA    1 
ATOM   6968  C  C     . GLY F 3 10  ? 13.132  77.315  -11.271 1.00 30.61 ?  3   GLY I C     1 
ATOM   6969  O  O     . GLY F 3 10  ? 12.734  77.328  -10.109 1.00 26.35 ?  3   GLY I O     1 
ATOM   6970  N  N     . LEU F 3 11  ? 13.178  76.210  -12.024 1.00 29.75 ?  4   LEU I N     1 
ATOM   6971  C  CA    . LEU F 3 11  ? 12.768  74.913  -11.513 1.00 29.45 ?  4   LEU I CA    1 
ATOM   6972  C  C     . LEU F 3 11  ? 13.790  74.423  -10.487 1.00 26.11 ?  4   LEU I C     1 
ATOM   6973  O  O     . LEU F 3 11  ? 13.414  73.982  -9.403  1.00 26.90 ?  4   LEU I O     1 
ATOM   6974  C  CB    . LEU F 3 11  ? 12.601  73.924  -12.667 1.00 30.16 ?  4   LEU I CB    1 
ATOM   6975  C  CG    . LEU F 3 11  ? 11.891  72.607  -12.331 1.00 32.26 ?  4   LEU I CG    1 
ATOM   6976  C  CD1   . LEU F 3 11  ? 10.436  72.835  -11.956 1.00 30.81 ?  4   LEU I CD1   1 
ATOM   6977  C  CD2   . LEU F 3 11  ? 11.989  71.619  -13.481 1.00 32.86 ?  4   LEU I CD2   1 
ATOM   6978  N  N     . SER F 3 12  ? 15.080  74.514  -10.833 1.00 25.31 ?  5   SER I N     1 
ATOM   6979  C  CA    . SER F 3 12  ? 16.147  73.986  -9.993  1.00 24.97 ?  5   SER I CA    1 
ATOM   6980  C  C     . SER F 3 12  ? 16.218  74.759  -8.678  1.00 25.04 ?  5   SER I C     1 
ATOM   6981  O  O     . SER F 3 12  ? 16.409  74.170  -7.617  1.00 24.36 ?  5   SER I O     1 
ATOM   6982  C  CB    . SER F 3 12  ? 17.479  74.009  -10.714 1.00 27.89 ?  5   SER I CB    1 
ATOM   6983  O  OG    . SER F 3 12  ? 18.520  73.482  -9.901  1.00 27.50 ?  5   SER I OG    1 
ATOM   6984  N  N     . ASP F 3 13  ? 16.054  76.083  -8.765  1.00 24.01 ?  6   ASP I N     1 
ATOM   6985  C  CA    . ASP F 3 13  ? 16.157  76.960  -7.610  1.00 24.89 ?  6   ASP I CA    1 
ATOM   6986  C  C     . ASP F 3 13  ? 15.109  76.572  -6.570  1.00 24.22 ?  6   ASP I C     1 
ATOM   6987  O  O     . ASP F 3 13  ? 15.376  76.607  -5.371  1.00 28.00 ?  6   ASP I O     1 
ATOM   6988  C  CB    . ASP F 3 13  ? 16.037  78.416  -8.030  1.00 30.23 ?  6   ASP I CB    1 
ATOM   6989  C  CG    . ASP F 3 13  ? 17.248  78.981  -8.758  1.00 34.27 ?  6   ASP I CG    1 
ATOM   6990  O  OD1   . ASP F 3 13  ? 18.318  78.338  -8.700  1.00 40.42 ?  6   ASP I OD1   1 
ATOM   6991  O  OD2   . ASP F 3 13  ? 17.107  80.049  -9.391  1.00 35.98 -1 6   ASP I OD2   1 
ATOM   6992  N  N     . PHE F 3 14  ? 13.918  76.201  -7.050  1.00 21.58 ?  7   PHE I N     1 
ATOM   6993  C  CA    . PHE F 3 14  ? 12.804  75.860  -6.184  1.00 20.34 ?  7   PHE I CA    1 
ATOM   6994  C  C     . PHE F 3 14  ? 13.094  74.542  -5.466  1.00 18.24 ?  7   PHE I C     1 
ATOM   6995  O  O     . PHE F 3 14  ? 12.995  74.469  -4.243  1.00 16.42 ?  7   PHE I O     1 
ATOM   6996  C  CB    . PHE F 3 14  ? 11.531  75.839  -7.035  1.00 18.87 ?  7   PHE I CB    1 
ATOM   6997  C  CG    . PHE F 3 14  ? 10.333  75.226  -6.325  1.00 18.95 ?  7   PHE I CG    1 
ATOM   6998  C  CD1   . PHE F 3 14  ? 9.694   75.907  -5.296  1.00 21.01 ?  7   PHE I CD1   1 
ATOM   6999  C  CD2   . PHE F 3 14  ? 9.852   73.974  -6.688  1.00 19.84 ?  7   PHE I CD2   1 
ATOM   7000  C  CE1   . PHE F 3 14  ? 8.607   75.347  -4.646  1.00 20.97 ?  7   PHE I CE1   1 
ATOM   7001  C  CE2   . PHE F 3 14  ? 8.762   73.420  -6.036  1.00 20.61 ?  7   PHE I CE2   1 
ATOM   7002  C  CZ    . PHE F 3 14  ? 8.144   74.107  -5.017  1.00 21.90 ?  7   PHE I CZ    1 
ATOM   7003  N  N     . PHE F 3 15  ? 13.456  73.505  -6.230  1.00 20.62 ?  8   PHE I N     1 
ATOM   7004  C  CA    . PHE F 3 15  ? 13.714  72.191  -5.660  1.00 21.47 ?  8   PHE I CA    1 
ATOM   7005  C  C     . PHE F 3 15  ? 14.781  72.301  -4.568  1.00 20.13 ?  8   PHE I C     1 
ATOM   7006  O  O     . PHE F 3 15  ? 14.616  71.743  -3.486  1.00 19.90 ?  8   PHE I O     1 
ATOM   7007  C  CB    . PHE F 3 15  ? 14.104  71.183  -6.747  1.00 23.48 ?  8   PHE I CB    1 
ATOM   7008  C  CG    . PHE F 3 15  ? 12.984  70.788  -7.704  1.00 26.20 ?  8   PHE I CG    1 
ATOM   7009  C  CD1   . PHE F 3 15  ? 11.648  70.986  -7.372  1.00 29.45 ?  8   PHE I CD1   1 
ATOM   7010  C  CD2   . PHE F 3 15  ? 13.274  70.199  -8.930  1.00 27.93 ?  8   PHE I CD2   1 
ATOM   7011  C  CE1   . PHE F 3 15  ? 10.637  70.621  -8.249  1.00 32.23 ?  8   PHE I CE1   1 
ATOM   7012  C  CE2   . PHE F 3 15  ? 12.260  69.834  -9.801  1.00 31.41 ?  8   PHE I CE2   1 
ATOM   7013  C  CZ    . PHE F 3 15  ? 10.945  70.045  -9.459  1.00 32.73 ?  8   PHE I CZ    1 
ATOM   7014  N  N     . THR F 3 16  ? 15.873  73.021  -4.854  1.00 22.94 ?  9   THR I N     1 
ATOM   7015  C  CA    . THR F 3 16  ? 16.953  73.199  -3.893  1.00 24.20 ?  9   THR I CA    1 
ATOM   7016  C  C     . THR F 3 16  ? 16.400  73.736  -2.574  1.00 25.63 ?  9   THR I C     1 
ATOM   7017  O  O     . THR F 3 16  ? 16.735  73.230  -1.504  1.00 22.69 ?  9   THR I O     1 
ATOM   7018  C  CB    . THR F 3 16  ? 18.011  74.131  -4.483  1.00 27.46 ?  9   THR I CB    1 
ATOM   7019  O  OG1   . THR F 3 16  ? 18.705  73.337  -5.440  1.00 24.34 ?  9   THR I OG1   1 
ATOM   7020  C  CG2   . THR F 3 16  ? 18.991  74.653  -3.447  1.00 27.82 ?  9   THR I CG2   1 
ATOM   7021  N  N     . GLN F 3 17  ? 15.559  74.772  -2.662  1.00 24.29 ?  10  GLN I N     1 
ATOM   7022  C  CA    . GLN F 3 17  ? 15.015  75.431  -1.487  1.00 21.82 ?  10  GLN I CA    1 
ATOM   7023  C  C     . GLN F 3 17  ? 14.085  74.467  -0.756  1.00 19.72 ?  10  GLN I C     1 
ATOM   7024  O  O     . GLN F 3 17  ? 14.195  74.277  0.454   1.00 23.00 ?  10  GLN I O     1 
ATOM   7025  C  CB    . GLN F 3 17  ? 14.293  76.711  -1.914  1.00 26.22 ?  10  GLN I CB    1 
ATOM   7026  C  CG    . GLN F 3 17  ? 13.851  77.593  -0.750  1.00 30.87 ?  10  GLN I CG    1 
ATOM   7027  C  CD    . GLN F 3 17  ? 13.348  78.954  -1.181  1.00 35.13 ?  10  GLN I CD    1 
ATOM   7028  O  OE1   . GLN F 3 17  ? 13.301  79.282  -2.372  1.00 38.89 ?  10  GLN I OE1   1 
ATOM   7029  N  NE2   . GLN F 3 17  ? 12.968  79.766  -0.205  1.00 37.39 ?  10  GLN I NE2   1 
ATOM   7030  N  N     . LEU F 3 18  ? 13.184  73.850  -1.526  1.00 16.59 ?  11  LEU I N     1 
ATOM   7031  C  CA    . LEU F 3 18  ? 12.171  72.953  -0.999  1.00 16.96 ?  11  LEU I CA    1 
ATOM   7032  C  C     . LEU F 3 18  ? 12.810  71.796  -0.235  1.00 16.86 ?  11  LEU I C     1 
ATOM   7033  O  O     . LEU F 3 18  ? 12.241  71.304  0.738   1.00 16.27 ?  11  LEU I O     1 
ATOM   7034  C  CB    . LEU F 3 18  ? 11.341  72.458  -2.182  1.00 16.54 ?  11  LEU I CB    1 
ATOM   7035  C  CG    . LEU F 3 18  ? 10.198  71.499  -1.843  1.00 15.99 ?  11  LEU I CG    1 
ATOM   7036  C  CD1   . LEU F 3 18  ? 9.372   72.020  -0.683  1.00 15.97 ?  11  LEU I CD1   1 
ATOM   7037  C  CD2   . LEU F 3 18  ? 9.335   71.286  -3.071  1.00 17.04 ?  11  LEU I CD2   1 
ATOM   7038  N  N     . GLY F 3 19  ? 13.987  71.356  -0.692  1.00 17.31 ?  12  GLY I N     1 
ATOM   7039  C  CA    . GLY F 3 19  ? 14.689  70.252  -0.057  1.00 18.41 ?  12  GLY I CA    1 
ATOM   7040  C  C     . GLY F 3 19  ? 15.251  70.649  1.307   1.00 17.09 ?  12  GLY I C     1 
ATOM   7041  O  O     . GLY F 3 19  ? 15.176  69.881  2.263   1.00 24.31 ?  12  GLY I O     1 
ATOM   7042  N  N     . GLN F 3 20  ? 15.808  71.862  1.379   1.00 17.78 ?  13  GLN I N     1 
ATOM   7043  C  CA    . GLN F 3 20  ? 16.531  72.324  2.554   1.00 20.08 ?  13  GLN I CA    1 
ATOM   7044  C  C     . GLN F 3 20  ? 15.602  72.957  3.589   1.00 22.91 ?  13  GLN I C     1 
ATOM   7045  O  O     . GLN F 3 20  ? 15.913  72.944  4.778   1.00 27.37 ?  13  GLN I O     1 
ATOM   7046  C  CB    . GLN F 3 20  ? 17.556  73.390  2.167   1.00 22.11 ?  13  GLN I CB    1 
ATOM   7047  C  CG    . GLN F 3 20  ? 18.627  72.907  1.195   1.00 24.29 ?  13  GLN I CG    1 
ATOM   7048  C  CD    . GLN F 3 20  ? 19.626  73.988  0.846   1.00 27.46 ?  13  GLN I CD    1 
ATOM   7049  O  OE1   . GLN F 3 20  ? 20.302  74.546  1.717   1.00 29.72 ?  13  GLN I OE1   1 
ATOM   7050  N  NE2   . GLN F 3 20  ? 19.723  74.297  -0.438  1.00 35.45 ?  13  GLN I NE2   1 
ATOM   7051  N  N     . ASP F 3 21  ? 14.481  73.532  3.134   1.00 22.65 ?  14  ASP I N     1 
ATOM   7052  C  CA    . ASP F 3 21  ? 13.651  74.384  3.975   1.00 20.15 ?  14  ASP I CA    1 
ATOM   7053  C  C     . ASP F 3 21  ? 12.382  73.632  4.375   1.00 17.64 ?  14  ASP I C     1 
ATOM   7054  O  O     . ASP F 3 21  ? 11.535  73.338  3.533   1.00 17.98 ?  14  ASP I O     1 
ATOM   7055  C  CB    . ASP F 3 21  ? 13.388  75.716  3.283   1.00 21.00 ?  14  ASP I CB    1 
ATOM   7056  C  CG    . ASP F 3 21  ? 12.614  76.757  4.080   1.00 21.65 ?  14  ASP I CG    1 
ATOM   7057  O  OD1   . ASP F 3 21  ? 12.086  76.407  5.155   1.00 20.95 ?  14  ASP I OD1   1 
ATOM   7058  O  OD2   . ASP F 3 21  ? 12.551  77.918  3.619   1.00 24.95 -1 14  ASP I OD2   1 
ATOM   7059  N  N     . ALA F 3 22  ? 12.260  73.348  5.677   1.00 15.70 ?  15  ALA I N     1 
ATOM   7060  C  CA    . ALA F 3 22  ? 11.178  72.536  6.216   1.00 14.92 ?  15  ALA I CA    1 
ATOM   7061  C  C     . ALA F 3 22  ? 9.867   73.316  6.204   1.00 18.20 ?  15  ALA I C     1 
ATOM   7062  O  O     . ALA F 3 22  ? 8.790   72.738  6.067   1.00 17.58 ?  15  ALA I O     1 
ATOM   7063  C  CB    . ALA F 3 22  ? 11.529  72.090  7.618   1.00 14.47 ?  15  ALA I CB    1 
ATOM   7064  N  N     . GLN F 3 23  ? 9.978   74.635  6.376   1.00 20.24 ?  16  GLN I N     1 
ATOM   7065  C  CA    . GLN F 3 23  ? 8.823   75.514  6.354   1.00 24.27 ?  16  GLN I CA    1 
ATOM   7066  C  C     . GLN F 3 23  ? 8.145   75.375  4.993   1.00 21.33 ?  16  GLN I C     1 
ATOM   7067  O  O     . GLN F 3 23  ? 6.952   75.088  4.909   1.00 19.40 ?  16  GLN I O     1 
ATOM   7068  C  CB    . GLN F 3 23  ? 9.310   76.926  6.680   1.00 28.64 ?  16  GLN I CB    1 
ATOM   7069  C  CG    . GLN F 3 23  ? 8.218   77.864  7.182   1.00 35.13 ?  16  GLN I CG    1 
ATOM   7070  C  CD    . GLN F 3 23  ? 7.299   77.206  8.187   1.00 38.47 ?  16  GLN I CD    1 
ATOM   7071  O  OE1   . GLN F 3 23  ? 7.743   76.554  9.138   1.00 36.28 ?  16  GLN I OE1   1 
ATOM   7072  N  NE2   . GLN F 3 23  ? 6.001   77.353  7.969   1.00 39.60 ?  16  GLN I NE2   1 
ATOM   7073  N  N     . LEU F 3 24  ? 8.945   75.543  3.934   1.00 21.09 ?  17  LEU I N     1 
ATOM   7074  C  CA    . LEU F 3 24  ? 8.481   75.447  2.559   1.00 22.61 ?  17  LEU I CA    1 
ATOM   7075  C  C     . LEU F 3 24  ? 8.009   74.026  2.250   1.00 24.77 ?  17  LEU I C     1 
ATOM   7076  O  O     . LEU F 3 24  ? 7.054   73.847  1.497   1.00 27.22 ?  17  LEU I O     1 
ATOM   7077  C  CB    . LEU F 3 24  ? 9.613   75.889  1.630   1.00 24.47 ?  17  LEU I CB    1 
ATOM   7078  C  CG    . LEU F 3 24  ? 9.321   75.831  0.126   1.00 29.57 ?  17  LEU I CG    1 
ATOM   7079  C  CD1   . LEU F 3 24  ? 8.045   76.576  -0.228  1.00 28.84 ?  17  LEU I CD1   1 
ATOM   7080  C  CD2   . LEU F 3 24  ? 10.490  76.386  -0.671  1.00 32.76 ?  17  LEU I CD2   1 
ATOM   7081  N  N     . MET F 3 25  ? 8.677   73.018  2.827   1.00 24.47 ?  18  MET I N     1 
ATOM   7082  C  CA    . MET F 3 25  ? 8.317   71.627  2.586   1.00 26.34 ?  18  MET I CA    1 
ATOM   7083  C  C     . MET F 3 25  ? 6.930   71.338  3.153   1.00 25.32 ?  18  MET I C     1 
ATOM   7084  O  O     . MET F 3 25  ? 6.126   70.658  2.519   1.00 18.30 ?  18  MET I O     1 
ATOM   7085  C  CB    . MET F 3 25  ? 9.307   70.652  3.231   1.00 26.51 ?  18  MET I CB    1 
ATOM   7086  C  CG    . MET F 3 25  ? 8.880   69.200  3.112   1.00 26.88 ?  18  MET I CG    1 
ATOM   7087  S  SD    . MET F 3 25  ? 8.747   68.653  1.398   1.00 28.13 ?  18  MET I SD    1 
ATOM   7088  C  CE    . MET F 3 25  ? 10.501  68.449  1.057   1.00 24.36 ?  18  MET I CE    1 
ATOM   7089  N  N     . GLU F 3 26  ? 6.673   71.840  4.365   1.00 30.44 ?  19  GLU I N     1 
ATOM   7090  C  CA    . GLU F 3 26  ? 5.381   71.674  5.009   1.00 32.90 ?  19  GLU I CA    1 
ATOM   7091  C  C     . GLU F 3 26  ? 4.326   72.499  4.275   1.00 31.06 ?  19  GLU I C     1 
ATOM   7092  O  O     . GLU F 3 26  ? 3.159   72.115  4.227   1.00 31.77 ?  19  GLU I O     1 
ATOM   7093  C  CB    . GLU F 3 26  ? 5.471   72.058  6.486   1.00 37.10 ?  19  GLU I CB    1 
ATOM   7094  C  CG    . GLU F 3 26  ? 6.238   71.040  7.325   1.00 44.26 ?  19  GLU I CG    1 
ATOM   7095  C  CD    . GLU F 3 26  ? 5.622   69.653  7.306   1.00 52.00 ?  19  GLU I CD    1 
ATOM   7096  O  OE1   . GLU F 3 26  ? 4.423   69.539  7.637   1.00 56.20 ?  19  GLU I OE1   1 
ATOM   7097  O  OE2   . GLU F 3 26  ? 6.337   68.688  6.961   1.00 67.50 -1 19  GLU I OE2   1 
ATOM   7098  N  N     . ASP F 3 27  ? 4.744   73.636  3.708   1.00 31.26 ?  20  ASP I N     1 
ATOM   7099  C  CA    . ASP F 3 27  ? 3.849   74.464  2.915   1.00 30.04 ?  20  ASP I CA    1 
ATOM   7100  C  C     . ASP F 3 27  ? 3.472   73.705  1.648   1.00 29.26 ?  20  ASP I C     1 
ATOM   7101  O  O     . ASP F 3 27  ? 2.310   73.687  1.248   1.00 27.64 ?  20  ASP I O     1 
ATOM   7102  C  CB    . ASP F 3 27  ? 4.473   75.809  2.573   1.00 29.16 ?  20  ASP I CB    1 
ATOM   7103  C  CG    . ASP F 3 27  ? 4.608   76.798  3.722   1.00 27.73 ?  20  ASP I CG    1 
ATOM   7104  O  OD1   . ASP F 3 27  ? 4.026   76.538  4.795   1.00 26.18 ?  20  ASP I OD1   1 
ATOM   7105  O  OD2   . ASP F 3 27  ? 5.303   77.819  3.535   1.00 31.95 -1 20  ASP I OD2   1 
ATOM   7106  N  N     . TYR F 3 28  ? 4.478   73.077  1.030   1.00 33.80 ?  21  TYR I N     1 
ATOM   7107  C  CA    . TYR F 3 28  ? 4.291   72.322  -0.197  1.00 27.49 ?  21  TYR I CA    1 
ATOM   7108  C  C     . TYR F 3 28  ? 3.343   71.154  0.063   1.00 28.50 ?  21  TYR I C     1 
ATOM   7109  O  O     . TYR F 3 28  ? 2.439   70.897  -0.729  1.00 26.13 ?  21  TYR I O     1 
ATOM   7110  C  CB    . TYR F 3 28  ? 5.646   71.847  -0.733  1.00 26.01 ?  21  TYR I CB    1 
ATOM   7111  C  CG    . TYR F 3 28  ? 5.532   70.936  -1.948  1.00 22.54 ?  21  TYR I CG    1 
ATOM   7112  C  CD1   . TYR F 3 28  ? 5.406   71.459  -3.228  1.00 20.76 ?  21  TYR I CD1   1 
ATOM   7113  C  CD2   . TYR F 3 28  ? 5.532   69.553  -1.809  1.00 22.80 ?  21  TYR I CD2   1 
ATOM   7114  C  CE1   . TYR F 3 28  ? 5.289   70.635  -4.336  1.00 21.41 ?  21  TYR I CE1   1 
ATOM   7115  C  CE2   . TYR F 3 28  ? 5.418   68.718  -2.909  1.00 20.99 ?  21  TYR I CE2   1 
ATOM   7116  C  CZ    . TYR F 3 28  ? 5.297   69.262  -4.175  1.00 21.00 ?  21  TYR I CZ    1 
ATOM   7117  O  OH    . TYR F 3 28  ? 5.185   68.447  -5.264  1.00 25.06 ?  21  TYR I OH    1 
ATOM   7118  N  N     . LYS F 3 29  ? 3.564   70.456  1.182   1.00 30.96 ?  22  LYS I N     1 
ATOM   7119  C  CA    . LYS F 3 29  ? 2.788   69.278  1.538   1.00 32.67 ?  22  LYS I CA    1 
ATOM   7120  C  C     . LYS F 3 29  ? 1.305   69.637  1.632   1.00 28.71 ?  22  LYS I C     1 
ATOM   7121  O  O     . LYS F 3 29  ? 0.448   68.844  1.250   1.00 29.16 ?  22  LYS I O     1 
ATOM   7122  C  CB    . LYS F 3 29  ? 3.299   68.682  2.857   1.00 33.63 ?  22  LYS I CB    1 
ATOM   7123  C  CG    . LYS F 3 29  ? 4.596   67.873  2.787   1.00 34.09 ?  22  LYS I CG    1 
ATOM   7124  C  CD    . LYS F 3 29  ? 4.450   66.428  2.320   1.00 34.01 ?  22  LYS I CD    1 
ATOM   7125  C  CE    . LYS F 3 29  ? 5.645   65.591  2.681   1.00 39.06 ?  22  LYS I CE    1 
ATOM   7126  N  NZ    . LYS F 3 29  ? 5.519   64.194  2.252   1.00 38.44 1  22  LYS I NZ    1 
ATOM   7127  N  N     . GLN F 3 30  ? 1.015   70.837  2.147   1.00 29.06 ?  23  GLN I N     1 
ATOM   7128  C  CA    . GLN F 3 30  ? -0.355  71.282  2.344   1.00 27.34 ?  23  GLN I CA    1 
ATOM   7129  C  C     . GLN F 3 30  ? -1.017  71.556  0.995   1.00 22.18 ?  23  GLN I C     1 
ATOM   7130  O  O     . GLN F 3 30  ? -2.139  71.114  0.758   1.00 17.43 ?  23  GLN I O     1 
ATOM   7131  C  CB    . GLN F 3 30  ? -0.406  72.522  3.237   1.00 31.23 ?  23  GLN I CB    1 
ATOM   7132  C  CG    . GLN F 3 30  ? -0.110  72.238  4.706   1.00 38.09 ?  23  GLN I CG    1 
ATOM   7133  C  CD    . GLN F 3 30  ? -1.110  71.298  5.342   1.00 50.26 ?  23  GLN I CD    1 
ATOM   7134  O  OE1   . GLN F 3 30  ? -1.278  70.149  4.917   1.00 49.24 ?  23  GLN I OE1   1 
ATOM   7135  N  NE2   . GLN F 3 30  ? -1.788  71.781  6.373   1.00 58.38 ?  23  GLN I NE2   1 
ATOM   7136  N  N     . ASN F 3 31  ? -0.320  72.289  0.119   1.00 20.56 ?  24  ASN I N     1 
ATOM   7137  C  CA    . ASN F 3 31  ? -0.905  72.705  -1.146  1.00 21.24 ?  24  ASN I CA    1 
ATOM   7138  C  C     . ASN F 3 31  ? 0.171   72.731  -2.228  1.00 19.42 ?  24  ASN I C     1 
ATOM   7139  O  O     . ASN F 3 31  ? 0.714   73.784  -2.557  1.00 21.20 ?  24  ASN I O     1 
ATOM   7140  C  CB    . ASN F 3 31  ? -1.613  74.049  -1.022  1.00 20.76 ?  24  ASN I CB    1 
ATOM   7141  C  CG    . ASN F 3 31  ? -2.599  74.269  -2.144  1.00 23.33 ?  24  ASN I CG    1 
ATOM   7142  O  OD1   . ASN F 3 31  ? -2.281  74.014  -3.310  1.00 27.76 ?  24  ASN I OD1   1 
ATOM   7143  N  ND2   . ASN F 3 31  ? -3.801  74.721  -1.815  1.00 24.26 ?  24  ASN I ND2   1 
ATOM   7144  N  N     . PRO F 3 32  ? 0.489   71.559  -2.819  1.00 17.02 ?  25  PRO I N     1 
ATOM   7145  C  CA    . PRO F 3 32  ? 1.570   71.440  -3.802  1.00 17.70 ?  25  PRO I CA    1 
ATOM   7146  C  C     . PRO F 3 32  ? 1.415   72.302  -5.053  1.00 17.75 ?  25  PRO I C     1 
ATOM   7147  O  O     . PRO F 3 32  ? 2.375   72.927  -5.498  1.00 19.65 ?  25  PRO I O     1 
ATOM   7148  C  CB    . PRO F 3 32  ? 1.551   69.937  -4.143  1.00 16.82 ?  25  PRO I CB    1 
ATOM   7149  C  CG    . PRO F 3 32  ? 0.903   69.285  -2.944  1.00 16.51 ?  25  PRO I CG    1 
ATOM   7150  C  CD    . PRO F 3 32  ? -0.162  70.274  -2.523  1.00 17.48 ?  25  PRO I CD    1 
ATOM   7151  N  N     . GLU F 3 33  ? 0.208   72.308  -5.629  1.00 18.16 ?  26  GLU I N     1 
ATOM   7152  C  CA    . GLU F 3 33  ? -0.066  73.106  -6.814  1.00 21.48 ?  26  GLU I CA    1 
ATOM   7153  C  C     . GLU F 3 33  ? 0.099   74.589  -6.495  1.00 18.90 ?  26  GLU I C     1 
ATOM   7154  O  O     . GLU F 3 33  ? 0.719   75.322  -7.262  1.00 22.23 ?  26  GLU I O     1 
ATOM   7155  C  CB    . GLU F 3 33  ? -1.468  72.874  -7.375  1.00 26.15 ?  26  GLU I CB    1 
ATOM   7156  C  CG    . GLU F 3 33  ? -1.544  71.742  -8.395  1.00 30.23 ?  26  GLU I CG    1 
ATOM   7157  C  CD    . GLU F 3 33  ? -2.821  71.769  -9.214  1.00 35.54 ?  26  GLU I CD    1 
ATOM   7158  O  OE1   . GLU F 3 33  ? -3.645  72.678  -8.978  1.00 35.52 ?  26  GLU I OE1   1 
ATOM   7159  O  OE2   . GLU F 3 33  ? -2.994  70.890  -10.085 1.00 40.96 -1 26  GLU I OE2   1 
ATOM   7160  N  N     . ALA F 3 34  ? -0.475  75.029  -5.369  1.00 20.32 ?  27  ALA I N     1 
ATOM   7161  C  CA    . ALA F 3 34  ? -0.412  76.430  -4.985  1.00 18.07 ?  27  ALA I CA    1 
ATOM   7162  C  C     . ALA F 3 34  ? 1.048   76.856  -4.861  1.00 16.14 ?  27  ALA I C     1 
ATOM   7163  O  O     . ALA F 3 34  ? 1.501   77.754  -5.565  1.00 16.23 ?  27  ALA I O     1 
ATOM   7164  C  CB    . ALA F 3 34  ? -1.173  76.662  -3.696  1.00 17.97 ?  27  ALA I CB    1 
ATOM   7165  N  N     . VAL F 3 35  ? 1.775   76.184  -3.964  1.00 18.37 ?  28  VAL I N     1 
ATOM   7166  C  CA    . VAL F 3 35  ? 3.183   76.459  -3.730  1.00 18.62 ?  28  VAL I CA    1 
ATOM   7167  C  C     . VAL F 3 35  ? 3.931   76.521  -5.060  1.00 19.11 ?  28  VAL I C     1 
ATOM   7168  O  O     . VAL F 3 35  ? 4.708   77.444  -5.292  1.00 20.91 ?  28  VAL I O     1 
ATOM   7169  C  CB    . VAL F 3 35  ? 3.781   75.396  -2.788  1.00 20.88 ?  28  VAL I CB    1 
ATOM   7170  C  CG1   . VAL F 3 35  ? 5.291   75.541  -2.651  1.00 20.89 ?  28  VAL I CG1   1 
ATOM   7171  C  CG2   . VAL F 3 35  ? 3.112   75.422  -1.418  1.00 22.70 ?  28  VAL I CG2   1 
ATOM   7172  N  N     . MET F 3 36  ? 3.693   75.539  -5.936  1.00 18.26 ?  29  MET I N     1 
ATOM   7173  C  CA    . MET F 3 36  ? 4.434   75.448  -7.183  1.00 18.22 ?  29  MET I CA    1 
ATOM   7174  C  C     . MET F 3 36  ? 4.088   76.627  -8.090  1.00 18.75 ?  29  MET I C     1 
ATOM   7175  O  O     . MET F 3 36  ? 4.986   77.267  -8.633  1.00 19.18 ?  29  MET I O     1 
ATOM   7176  C  CB    . MET F 3 36  ? 4.169   74.122  -7.903  1.00 17.28 ?  29  MET I CB    1 
ATOM   7177  C  CG    . MET F 3 36  ? 4.979   72.970  -7.344  1.00 17.59 ?  29  MET I CG    1 
ATOM   7178  S  SD    . MET F 3 36  ? 4.869   71.482  -8.355  1.00 15.22 ?  29  MET I SD    1 
ATOM   7179  C  CE    . MET F 3 36  ? 3.339   70.775  -7.730  1.00 13.23 ?  29  MET I CE    1 
ATOM   7180  N  N     . ARG F 3 37  ? 2.791   76.912  -8.251  1.00 19.16 ?  30  ARG I N     1 
ATOM   7181  C  CA    . ARG F 3 37  ? 2.373   78.052  -9.053  1.00 22.40 ?  30  ARG I CA    1 
ATOM   7182  C  C     . ARG F 3 37  ? 3.042   79.318  -8.522  1.00 19.09 ?  30  ARG I C     1 
ATOM   7183  O  O     . ARG F 3 37  ? 3.513   80.142  -9.301  1.00 20.32 ?  30  ARG I O     1 
ATOM   7184  C  CB    . ARG F 3 37  ? 0.848   78.203  -9.109  1.00 27.80 ?  30  ARG I CB    1 
ATOM   7185  C  CG    . ARG F 3 37  ? 0.203   77.096  -9.929  1.00 33.31 ?  30  ARG I CG    1 
ATOM   7186  C  CD    . ARG F 3 37  ? -1.234  77.369  -10.332 1.00 38.32 ?  30  ARG I CD    1 
ATOM   7187  N  NE    . ARG F 3 37  ? -1.498  76.726  -11.624 1.00 43.77 ?  30  ARG I NE    1 
ATOM   7188  C  CZ    . ARG F 3 37  ? -2.171  75.596  -11.812 1.00 52.97 ?  30  ARG I CZ    1 
ATOM   7189  N  NH1   . ARG F 3 37  ? -2.712  74.959  -10.789 1.00 55.10 1  30  ARG I NH1   1 
ATOM   7190  N  NH2   . ARG F 3 37  ? -2.294  75.104  -13.032 1.00 56.40 ?  30  ARG I NH2   1 
ATOM   7191  N  N     . ALA F 3 38  ? 3.098   79.453  -7.192  1.00 19.02 ?  31  ALA I N     1 
ATOM   7192  C  CA    . ALA F 3 38  ? 3.610   80.662  -6.565  1.00 18.38 ?  31  ALA I CA    1 
ATOM   7193  C  C     . ALA F 3 38  ? 5.087   80.856  -6.901  1.00 18.93 ?  31  ALA I C     1 
ATOM   7194  O  O     . ALA F 3 38  ? 5.587   81.979  -6.877  1.00 18.94 ?  31  ALA I O     1 
ATOM   7195  C  CB    . ALA F 3 38  ? 3.397   80.597  -5.069  1.00 19.40 ?  31  ALA I CB    1 
ATOM   7196  N  N     . HIS F 3 39  ? 5.772   79.749  -7.208  1.00 18.70 ?  32  HIS I N     1 
ATOM   7197  C  CA    . HIS F 3 39  ? 7.204   79.765  -7.460  1.00 18.40 ?  32  HIS I CA    1 
ATOM   7198  C  C     . HIS F 3 39  ? 7.476   79.760  -8.965  1.00 19.39 ?  32  HIS I C     1 
ATOM   7199  O  O     . HIS F 3 39  ? 8.630   79.700  -9.385  1.00 15.81 ?  32  HIS I O     1 
ATOM   7200  C  CB    . HIS F 3 39  ? 7.892   78.602  -6.731  1.00 18.91 ?  32  HIS I CB    1 
ATOM   7201  C  CG    . HIS F 3 39  ? 8.137   78.822  -5.271  1.00 16.93 ?  32  HIS I CG    1 
ATOM   7202  N  ND1   . HIS F 3 39  ? 7.202   78.567  -4.290  1.00 15.54 ?  32  HIS I ND1   1 
ATOM   7203  C  CD2   . HIS F 3 39  ? 9.233   79.261  -4.631  1.00 15.63 ?  32  HIS I CD2   1 
ATOM   7204  C  CE1   . HIS F 3 39  ? 7.724   78.850  -3.103  1.00 15.69 ?  32  HIS I CE1   1 
ATOM   7205  N  NE2   . HIS F 3 39  ? 8.958   79.271  -3.288  1.00 15.73 ?  32  HIS I NE2   1 
ATOM   7206  N  N     . GLY F 3 40  ? 6.409   79.814  -9.772  1.00 19.90 ?  33  GLY I N     1 
ATOM   7207  C  CA    . GLY F 3 40  ? 6.530   80.150  -11.183 1.00 20.97 ?  33  GLY I CA    1 
ATOM   7208  C  C     . GLY F 3 40  ? 6.541   78.925  -12.095 1.00 23.15 ?  33  GLY I C     1 
ATOM   7209  O  O     . GLY F 3 40  ? 6.781   79.051  -13.294 1.00 24.68 ?  33  GLY I O     1 
ATOM   7210  N  N     . LEU F 3 41  ? 6.273   77.745  -11.527 1.00 22.82 ?  34  LEU I N     1 
ATOM   7211  C  CA    . LEU F 3 41  ? 6.308   76.504  -12.287 1.00 23.86 ?  34  LEU I CA    1 
ATOM   7212  C  C     . LEU F 3 41  ? 5.159   76.473  -13.291 1.00 23.22 ?  34  LEU I C     1 
ATOM   7213  O  O     . LEU F 3 41  ? 4.004   76.690  -12.930 1.00 20.94 ?  34  LEU I O     1 
ATOM   7214  C  CB    . LEU F 3 41  ? 6.266   75.300  -11.347 1.00 22.15 ?  34  LEU I CB    1 
ATOM   7215  C  CG    . LEU F 3 41  ? 7.621   74.852  -10.789 1.00 23.42 ?  34  LEU I CG    1 
ATOM   7216  C  CD1   . LEU F 3 41  ? 8.281   75.971  -10.006 1.00 22.36 ?  34  LEU I CD1   1 
ATOM   7217  C  CD2   . LEU F 3 41  ? 7.493   73.605  -9.931  1.00 24.09 ?  34  LEU I CD2   1 
ATOM   7218  N  N     . THR F 3 42  ? 5.504   76.182  -14.551 1.00 23.04 ?  35  THR I N     1 
ATOM   7219  C  CA    . THR F 3 42  ? 4.539   76.113  -15.636 1.00 25.05 ?  35  THR I CA    1 
ATOM   7220  C  C     . THR F 3 42  ? 3.596   74.935  -15.405 1.00 21.86 ?  35  THR I C     1 
ATOM   7221  O  O     . THR F 3 42  ? 3.786   74.152  -14.477 1.00 18.07 ?  35  THR I O     1 
ATOM   7222  C  CB    . THR F 3 42  ? 5.269   75.971  -16.972 1.00 24.54 ?  35  THR I CB    1 
ATOM   7223  O  OG1   . THR F 3 42  ? 5.959   74.729  -16.881 1.00 30.10 ?  35  THR I OG1   1 
ATOM   7224  C  CG2   . THR F 3 42  ? 6.255   77.093  -17.239 1.00 25.02 ?  35  THR I CG2   1 
ATOM   7225  N  N     . ASP F 3 43  ? 2.594   74.818  -16.284 1.00 21.53 ?  36  ASP I N     1 
ATOM   7226  C  CA    . ASP F 3 43  ? 1.569   73.793  -16.180 1.00 24.47 ?  36  ASP I CA    1 
ATOM   7227  C  C     . ASP F 3 43  ? 2.152   72.430  -16.535 1.00 22.56 ?  36  ASP I C     1 
ATOM   7228  O  O     . ASP F 3 43  ? 1.744   71.417  -15.973 1.00 20.94 ?  36  ASP I O     1 
ATOM   7229  C  CB    . ASP F 3 43  ? 0.385   74.091  -17.087 1.00 27.15 ?  36  ASP I CB    1 
ATOM   7230  C  CG    . ASP F 3 43  ? -0.372  75.374  -16.777 1.00 31.86 ?  36  ASP I CG    1 
ATOM   7231  O  OD1   . ASP F 3 43  ? -0.766  75.554  -15.605 1.00 33.92 ?  36  ASP I OD1   1 
ATOM   7232  O  OD2   . ASP F 3 43  ? -0.569  76.177  -17.713 1.00 30.35 -1 36  ASP I OD2   1 
ATOM   7233  N  N     . GLU F 3 44  ? 3.086   72.419  -17.490 1.00 24.32 ?  37  GLU I N     1 
ATOM   7234  C  CA    . GLU F 3 44  ? 3.752   71.195  -17.900 1.00 27.00 ?  37  GLU I CA    1 
ATOM   7235  C  C     . GLU F 3 44  ? 4.665   70.725  -16.769 1.00 25.91 ?  37  GLU I C     1 
ATOM   7236  O  O     . GLU F 3 44  ? 4.761   69.528  -16.506 1.00 19.24 ?  37  GLU I O     1 
ATOM   7237  C  CB    . GLU F 3 44  ? 4.496   71.410  -19.220 1.00 26.73 ?  37  GLU I CB    1 
ATOM   7238  C  CG    . GLU F 3 44  ? 5.765   72.248  -19.085 1.00 33.02 ?  37  GLU I CG    1 
ATOM   7239  C  CD    . GLU F 3 44  ? 6.346   72.756  -20.394 1.00 36.05 ?  37  GLU I CD    1 
ATOM   7240  O  OE1   . GLU F 3 44  ? 5.759   73.688  -20.985 1.00 44.13 ?  37  GLU I OE1   1 
ATOM   7241  O  OE2   . GLU F 3 44  ? 7.387   72.219  -20.826 1.00 32.44 -1 37  GLU I OE2   1 
ATOM   7242  N  N     . GLN F 3 45  ? 5.325   71.673  -16.095 1.00 25.69 ?  38  GLN I N     1 
ATOM   7243  C  CA    . GLN F 3 45  ? 6.237   71.334  -15.014 1.00 24.73 ?  38  GLN I CA    1 
ATOM   7244  C  C     . GLN F 3 45  ? 5.442   70.777  -13.837 1.00 21.94 ?  38  GLN I C     1 
ATOM   7245  O  O     . GLN F 3 45  ? 5.872   69.829  -13.184 1.00 28.72 ?  38  GLN I O     1 
ATOM   7246  C  CB    . GLN F 3 45  ? 7.085   72.534  -14.595 1.00 26.45 ?  38  GLN I CB    1 
ATOM   7247  C  CG    . GLN F 3 45  ? 8.150   72.907  -15.620 1.00 27.75 ?  38  GLN I CG    1 
ATOM   7248  C  CD    . GLN F 3 45  ? 8.863   74.202  -15.300 1.00 26.60 ?  38  GLN I CD    1 
ATOM   7249  O  OE1   . GLN F 3 45  ? 8.550   74.888  -14.321 1.00 30.49 ?  38  GLN I OE1   1 
ATOM   7250  N  NE2   . GLN F 3 45  ? 9.830   74.553  -16.135 1.00 25.53 ?  38  GLN I NE2   1 
ATOM   7251  N  N     . ILE F 3 46  ? 4.274   71.370  -13.585 1.00 20.61 ?  39  ILE I N     1 
ATOM   7252  C  CA    . ILE F 3 46  ? 3.435   70.957  -12.473 1.00 19.13 ?  39  ILE I CA    1 
ATOM   7253  C  C     . ILE F 3 46  ? 2.809   69.600  -12.782 1.00 18.58 ?  39  ILE I C     1 
ATOM   7254  O  O     . ILE F 3 46  ? 2.688   68.755  -11.899 1.00 19.21 ?  39  ILE I O     1 
ATOM   7255  C  CB    . ILE F 3 46  ? 2.371   72.025  -12.170 1.00 15.69 ?  39  ILE I CB    1 
ATOM   7256  C  CG1   . ILE F 3 46  ? 3.025   73.317  -11.686 1.00 15.79 ?  39  ILE I CG1   1 
ATOM   7257  C  CG2   . ILE F 3 46  ? 1.334   71.500  -11.179 1.00 16.01 ?  39  ILE I CG2   1 
ATOM   7258  C  CD1   . ILE F 3 46  ? 2.067   74.292  -11.027 1.00 15.78 ?  39  ILE I CD1   1 
ATOM   7259  N  N     . ASN F 3 47  ? 2.408   69.412  -14.042 1.00 17.85 ?  40  ASN I N     1 
ATOM   7260  C  CA    . ASN F 3 47  ? 1.770   68.181  -14.476 1.00 22.64 ?  40  ASN I CA    1 
ATOM   7261  C  C     . ASN F 3 47  ? 2.736   67.019  -14.276 1.00 22.89 ?  40  ASN I C     1 
ATOM   7262  O  O     . ASN F 3 47  ? 2.384   65.992  -13.699 1.00 21.74 ?  40  ASN I O     1 
ATOM   7263  C  CB    . ASN F 3 47  ? 1.331   68.281  -15.932 1.00 23.41 ?  40  ASN I CB    1 
ATOM   7264  C  CG    . ASN F 3 47  ? 0.643   67.024  -16.407 1.00 26.19 ?  40  ASN I CG    1 
ATOM   7265  O  OD1   . ASN F 3 47  ? -0.396  66.640  -15.859 1.00 28.24 ?  40  ASN I OD1   1 
ATOM   7266  N  ND2   . ASN F 3 47  ? 1.203   66.374  -17.417 1.00 30.12 ?  40  ASN I ND2   1 
ATOM   7267  N  N     . ALA F 3 48  ? 3.959   67.209  -14.776 1.00 22.15 ?  41  ALA I N     1 
ATOM   7268  C  CA    . ALA F 3 48  ? 5.027   66.236  -14.635 1.00 25.01 ?  41  ALA I CA    1 
ATOM   7269  C  C     . ALA F 3 48  ? 5.196   65.854  -13.166 1.00 27.09 ?  41  ALA I C     1 
ATOM   7270  O  O     . ALA F 3 48  ? 5.340   64.675  -12.846 1.00 31.04 ?  41  ALA I O     1 
ATOM   7271  C  CB    . ALA F 3 48  ? 6.303   66.802  -15.219 1.00 24.54 ?  41  ALA I CB    1 
ATOM   7272  N  N     . VAL F 3 49  ? 5.171   66.854  -12.277 1.00 24.75 ?  42  VAL I N     1 
ATOM   7273  C  CA    . VAL F 3 49  ? 5.351   66.608  -10.854 1.00 24.85 ?  42  VAL I CA    1 
ATOM   7274  C  C     . VAL F 3 49  ? 4.202   65.734  -10.356 1.00 25.15 ?  42  VAL I C     1 
ATOM   7275  O  O     . VAL F 3 49  ? 4.423   64.784  -9.609  1.00 29.22 ?  42  VAL I O     1 
ATOM   7276  C  CB    . VAL F 3 49  ? 5.458   67.889  -10.003 1.00 26.05 ?  42  VAL I CB    1 
ATOM   7277  C  CG1   . VAL F 3 49  ? 5.286   67.592  -8.516  1.00 25.88 ?  42  VAL I CG1   1 
ATOM   7278  C  CG2   . VAL F 3 49  ? 6.767   68.629  -10.248 1.00 26.57 ?  42  VAL I CG2   1 
ATOM   7279  N  N     . MET F 3 50  ? 2.975   66.064  -10.775 1.00 24.15 ?  43  MET I N     1 
ATOM   7280  C  CA    . MET F 3 50  ? 1.790   65.424  -10.228 1.00 21.03 ?  43  MET I CA    1 
ATOM   7281  C  C     . MET F 3 50  ? 1.638   64.008  -10.784 1.00 19.01 ?  43  MET I C     1 
ATOM   7282  O  O     . MET F 3 50  ? 0.913   63.200  -10.209 1.00 17.16 ?  43  MET I O     1 
ATOM   7283  C  CB    . MET F 3 50  ? 0.528   66.246  -10.521 1.00 18.83 ?  43  MET I CB    1 
ATOM   7284  C  CG    . MET F 3 50  ? 0.535   67.645  -9.915  1.00 20.93 ?  43  MET I CG    1 
ATOM   7285  S  SD    . MET F 3 50  ? 0.883   67.698  -8.145  1.00 19.74 ?  43  MET I SD    1 
ATOM   7286  C  CE    . MET F 3 50  ? -0.488  66.721  -7.513  1.00 23.55 ?  43  MET I CE    1 
ATOM   7287  N  N     . THR F 3 51  ? 2.318   63.707  -11.897 1.00 21.77 ?  44  THR I N     1 
ATOM   7288  C  CA    . THR F 3 51  ? 2.254   62.378  -12.488 1.00 22.35 ?  44  THR I CA    1 
ATOM   7289  C  C     . THR F 3 51  ? 3.501   61.588  -12.100 1.00 21.99 ?  44  THR I C     1 
ATOM   7290  O  O     . THR F 3 51  ? 3.560   60.375  -12.298 1.00 23.86 ?  44  THR I O     1 
ATOM   7291  C  CB    . THR F 3 51  ? 2.104   62.477  -14.005 1.00 23.56 ?  44  THR I CB    1 
ATOM   7292  O  OG1   . THR F 3 51  ? 3.186   63.294  -14.438 1.00 25.20 ?  44  THR I OG1   1 
ATOM   7293  C  CG2   . THR F 3 51  ? 0.775   63.082  -14.421 1.00 26.29 ?  44  THR I CG2   1 
ATOM   7294  N  N     . GLY F 3 52  ? 4.495   62.293  -11.554 1.00 23.98 ?  45  GLY I N     1 
ATOM   7295  C  CA    . GLY F 3 52  ? 5.730   61.672  -11.107 1.00 26.75 ?  45  GLY I CA    1 
ATOM   7296  C  C     . GLY F 3 52  ? 6.605   61.251  -12.286 1.00 31.93 ?  45  GLY I C     1 
ATOM   7297  O  O     . GLY F 3 52  ? 7.278   60.225  -12.224 1.00 36.71 ?  45  GLY I O     1 
ATOM   7298  N  N     . ASP F 3 53  ? 6.582   62.052  -13.356 1.00 31.49 ?  46  ASP I N     1 
ATOM   7299  C  CA    . ASP F 3 53  ? 7.430   61.811  -14.512 1.00 32.12 ?  46  ASP I CA    1 
ATOM   7300  C  C     . ASP F 3 53  ? 8.746   62.562  -14.329 1.00 31.11 ?  46  ASP I C     1 
ATOM   7301  O  O     . ASP F 3 53  ? 8.903   63.681  -14.813 1.00 20.81 ?  46  ASP I O     1 
ATOM   7302  C  CB    . ASP F 3 53  ? 6.729   62.188  -15.808 1.00 34.27 ?  46  ASP I CB    1 
ATOM   7303  C  CG    . ASP F 3 53  ? 7.547   61.973  -17.074 1.00 37.01 ?  46  ASP I CG    1 
ATOM   7304  O  OD1   . ASP F 3 53  ? 8.697   61.501  -16.954 1.00 36.90 ?  46  ASP I OD1   1 
ATOM   7305  O  OD2   . ASP F 3 53  ? 7.028   62.282  -18.168 1.00 40.52 -1 46  ASP I OD2   1 
ATOM   7306  N  N     . MET F 3 54  ? 9.685   61.922  -13.622 1.00 32.77 ?  47  MET I N     1 
ATOM   7307  C  CA    . MET F 3 54  ? 10.994  62.495  -13.354 1.00 33.70 ?  47  MET I CA    1 
ATOM   7308  C  C     . MET F 3 54  ? 11.745  62.720  -14.667 1.00 37.06 ?  47  MET I C     1 
ATOM   7309  O  O     . MET F 3 54  ? 12.523  63.664  -14.783 1.00 37.77 ?  47  MET I O     1 
ATOM   7310  C  CB    . MET F 3 54  ? 11.820  61.579  -12.441 1.00 31.43 ?  47  MET I CB    1 
ATOM   7311  C  CG    . MET F 3 54  ? 11.278  61.420  -11.026 1.00 28.83 ?  47  MET I CG    1 
ATOM   7312  S  SD    . MET F 3 54  ? 10.886  62.972  -10.192 1.00 30.31 ?  47  MET I SD    1 
ATOM   7313  C  CE    . MET F 3 54  ? 9.122   63.078  -10.520 1.00 28.70 ?  47  MET I CE    1 
ATOM   7314  N  N     . GLU F 3 55  ? 11.508  61.842  -15.650 1.00 43.46 ?  48  GLU I N     1 
ATOM   7315  C  CA    . GLU F 3 55  ? 12.182  61.915  -16.938 1.00 45.61 ?  48  GLU I CA    1 
ATOM   7316  C  C     . GLU F 3 55  ? 11.976  63.288  -17.573 1.00 43.39 ?  48  GLU I C     1 
ATOM   7317  O  O     . GLU F 3 55  ? 12.925  63.886  -18.077 1.00 41.11 ?  48  GLU I O     1 
ATOM   7318  C  CB    . GLU F 3 55  ? 11.684  60.832  -17.897 1.00 49.13 ?  48  GLU I CB    1 
ATOM   7319  C  CG    . GLU F 3 55  ? 12.547  59.573  -17.920 1.00 47.88 ?  48  GLU I CG    1 
ATOM   7320  C  CD    . GLU F 3 55  ? 13.882  59.731  -18.627 1.00 51.80 ?  48  GLU I CD    1 
ATOM   7321  O  OE1   . GLU F 3 55  ? 14.203  60.860  -19.059 1.00 47.46 ?  48  GLU I OE1   1 
ATOM   7322  O  OE2   . GLU F 3 55  ? 14.600  58.716  -18.751 1.00 52.34 -1 48  GLU I OE2   1 
ATOM   7323  N  N     . LYS F 3 56  ? 10.730  63.774  -17.554 1.00 45.99 ?  49  LYS I N     1 
ATOM   7324  C  CA    . LYS F 3 56  ? 10.378  65.004  -18.246 1.00 44.70 ?  49  LYS I CA    1 
ATOM   7325  C  C     . LYS F 3 56  ? 10.856  66.208  -17.435 1.00 41.79 ?  49  LYS I C     1 
ATOM   7326  O  O     . LYS F 3 56  ? 11.298  67.202  -18.007 1.00 43.26 ?  49  LYS I O     1 
ATOM   7327  C  CB    . LYS F 3 56  ? 8.871   65.088  -18.522 1.00 50.72 ?  49  LYS I CB    1 
ATOM   7328  C  CG    . LYS F 3 56  ? 8.505   65.989  -19.699 1.00 56.97 ?  49  LYS I CG    1 
ATOM   7329  C  CD    . LYS F 3 56  ? 7.020   66.261  -19.909 1.00 64.05 ?  49  LYS I CD    1 
ATOM   7330  C  CE    . LYS F 3 56  ? 6.237   65.065  -20.352 1.00 70.02 ?  49  LYS I CE    1 
ATOM   7331  N  NZ    . LYS F 3 56  ? 4.903   65.447  -20.826 1.00 72.21 1  49  LYS I NZ    1 
ATOM   7332  N  N     . LEU F 3 57  ? 10.762  66.115  -16.103 1.00 39.47 ?  50  LEU I N     1 
ATOM   7333  C  CA    . LEU F 3 57  ? 11.199  67.195  -15.231 1.00 39.75 ?  50  LEU I CA    1 
ATOM   7334  C  C     . LEU F 3 57  ? 12.624  67.593  -15.605 1.00 42.10 ?  50  LEU I C     1 
ATOM   7335  O  O     . LEU F 3 57  ? 12.904  68.766  -15.847 1.00 39.14 ?  50  LEU I O     1 
ATOM   7336  C  CB    . LEU F 3 57  ? 11.114  66.798  -13.757 1.00 40.43 ?  50  LEU I CB    1 
ATOM   7337  C  CG    . LEU F 3 57  ? 9.736   66.922  -13.100 1.00 38.46 ?  50  LEU I CG    1 
ATOM   7338  C  CD1   . LEU F 3 57  ? 9.796   66.434  -11.662 1.00 35.08 ?  50  LEU I CD1   1 
ATOM   7339  C  CD2   . LEU F 3 57  ? 9.225   68.353  -13.160 1.00 39.91 ?  50  LEU I CD2   1 
ATOM   7340  N  N     . LYS F 3 58  ? 13.515  66.598  -15.645 1.00 45.26 ?  51  LYS I N     1 
ATOM   7341  C  CA    . LYS F 3 58  ? 14.917  66.834  -15.940 1.00 52.67 ?  51  LYS I CA    1 
ATOM   7342  C  C     . LYS F 3 58  ? 15.034  67.509  -17.304 1.00 57.49 ?  51  LYS I C     1 
ATOM   7343  O  O     . LYS F 3 58  ? 15.806  68.451  -17.469 1.00 58.72 ?  51  LYS I O     1 
ATOM   7344  C  CB    . LYS F 3 58  ? 15.695  65.515  -15.856 1.00 54.86 ?  51  LYS I CB    1 
ATOM   7345  C  CG    . LYS F 3 58  ? 15.632  64.839  -14.491 1.00 53.61 ?  51  LYS I CG    1 
ATOM   7346  C  CD    . LYS F 3 58  ? 16.460  63.566  -14.368 1.00 54.13 ?  51  LYS I CD    1 
ATOM   7347  C  CE    . LYS F 3 58  ? 16.442  63.020  -12.975 1.00 53.19 ?  51  LYS I CE    1 
ATOM   7348  N  NZ    . LYS F 3 58  ? 17.183  61.761  -12.872 1.00 55.58 1  51  LYS I NZ    1 
ATOM   7349  N  N     . THR F 3 59  ? 14.250  67.020  -18.271 1.00 56.66 ?  52  THR I N     1 
ATOM   7350  C  CA    . THR F 3 59  ? 14.203  67.607  -19.600 1.00 57.22 ?  52  THR I CA    1 
ATOM   7351  C  C     . THR F 3 59  ? 13.859  69.090  -19.485 1.00 58.76 ?  52  THR I C     1 
ATOM   7352  O  O     . THR F 3 59  ? 14.658  69.945  -19.860 1.00 61.87 ?  52  THR I O     1 
ATOM   7353  C  CB    . THR F 3 59  ? 13.186  66.855  -20.458 1.00 57.61 ?  52  THR I CB    1 
ATOM   7354  O  OG1   . THR F 3 59  ? 13.845  65.652  -20.841 1.00 58.49 ?  52  THR I OG1   1 
ATOM   7355  C  CG2   . THR F 3 59  ? 12.768  67.629  -21.695 1.00 57.45 ?  52  THR I CG2   1 
ATOM   7356  N  N     . LEU F 3 60  ? 12.663  69.378  -18.961 1.00 54.62 ?  53  LEU I N     1 
ATOM   7357  C  CA    . LEU F 3 60  ? 12.172  70.743  -18.860 1.00 52.44 ?  53  LEU I CA    1 
ATOM   7358  C  C     . LEU F 3 60  ? 13.216  71.603  -18.127 1.00 55.05 ?  53  LEU I C     1 
ATOM   7359  O  O     . LEU F 3 60  ? 13.229  72.827  -18.384 1.00 58.47 ?  53  LEU I O     1 
ATOM   7360  C  CB    . LEU F 3 60  ? 10.823  70.771  -18.142 1.00 54.07 ?  53  LEU I CB    1 
ATOM   7361  C  CG    . LEU F 3 60  ? 9.733   69.858  -18.715 1.00 49.16 ?  53  LEU I CG    1 
ATOM   7362  C  CD1   . LEU F 3 60  ? 8.449   69.979  -17.912 1.00 44.30 ?  53  LEU I CD1   1 
ATOM   7363  C  CD2   . LEU F 3 60  ? 9.477   70.157  -20.182 1.00 50.29 ?  53  LEU I CD2   1 
ATOM   7364  N  N     . LEU F 3 70  ? 29.373  52.308  -8.535  1.00 36.10 ?  63  LEU I N     1 
ATOM   7365  C  CA    . LEU F 3 70  ? 30.417  52.632  -7.525  1.00 31.94 ?  63  LEU I CA    1 
ATOM   7366  C  C     . LEU F 3 70  ? 30.987  51.366  -6.879  1.00 30.71 ?  63  LEU I C     1 
ATOM   7367  O  O     . LEU F 3 70  ? 32.016  51.447  -6.214  1.00 26.41 ?  63  LEU I O     1 
ATOM   7368  C  CB    . LEU F 3 70  ? 29.853  53.592  -6.476  1.00 30.33 ?  63  LEU I CB    1 
ATOM   7369  C  CG    . LEU F 3 70  ? 30.181  55.076  -6.667  1.00 31.42 ?  63  LEU I CG    1 
ATOM   7370  C  CD1   . LEU F 3 70  ? 29.125  55.953  -6.014  1.00 25.46 ?  63  LEU I CD1   1 
ATOM   7371  C  CD2   . LEU F 3 70  ? 31.557  55.387  -6.095  1.00 31.08 ?  63  LEU I CD2   1 
ATOM   7372  N  N     . VAL F 3 71  ? 30.347  50.199  -7.058  1.00 28.60 ?  64  VAL I N     1 
ATOM   7373  C  CA    . VAL F 3 71  ? 30.852  48.998  -6.404  1.00 26.90 ?  64  VAL I CA    1 
ATOM   7374  C  C     . VAL F 3 71  ? 30.562  47.747  -7.235  1.00 26.88 ?  64  VAL I C     1 
ATOM   7375  O  O     . VAL F 3 71  ? 29.639  47.710  -8.045  1.00 20.26 ?  64  VAL I O     1 
ATOM   7376  C  CB    . VAL F 3 71  ? 30.301  48.849  -4.971  1.00 27.02 ?  64  VAL I CB    1 
ATOM   7377  C  CG1   . VAL F 3 71  ? 29.114  47.894  -4.902  1.00 30.21 ?  64  VAL I CG1   1 
ATOM   7378  C  CG2   . VAL F 3 71  ? 31.382  48.394  -3.997  1.00 28.32 ?  64  VAL I CG2   1 
ATOM   7379  N  N     . TRP F 3 72  ? 31.395  46.727  -6.997  1.00 31.83 ?  65  TRP I N     1 
ATOM   7380  C  CA    . TRP F 3 72  ? 31.275  45.392  -7.561  1.00 37.40 ?  65  TRP I CA    1 
ATOM   7381  C  C     . TRP F 3 72  ? 31.139  44.410  -6.398  1.00 38.12 ?  65  TRP I C     1 
ATOM   7382  O  O     . TRP F 3 72  ? 31.123  44.839  -5.247  1.00 39.20 ?  65  TRP I O     1 
ATOM   7383  C  CB    . TRP F 3 72  ? 32.507  45.099  -8.431  1.00 42.74 ?  65  TRP I CB    1 
ATOM   7384  C  CG    . TRP F 3 72  ? 33.058  43.707  -8.275  1.00 49.81 ?  65  TRP I CG    1 
ATOM   7385  C  CD1   . TRP F 3 72  ? 32.847  42.636  -9.093  1.00 51.19 ?  65  TRP I CD1   1 
ATOM   7386  C  CD2   . TRP F 3 72  ? 33.915  43.237  -7.211  1.00 53.50 ?  65  TRP I CD2   1 
ATOM   7387  N  NE1   . TRP F 3 72  ? 33.513  41.538  -8.619  1.00 51.55 ?  65  TRP I NE1   1 
ATOM   7388  C  CE2   . TRP F 3 72  ? 34.174  41.873  -7.467  1.00 51.70 ?  65  TRP I CE2   1 
ATOM   7389  C  CE3   . TRP F 3 72  ? 34.483  43.829  -6.077  1.00 55.97 ?  65  TRP I CE3   1 
ATOM   7390  C  CZ2   . TRP F 3 72  ? 34.976  41.100  -6.629  1.00 48.50 ?  65  TRP I CZ2   1 
ATOM   7391  C  CZ3   . TRP F 3 72  ? 35.273  43.062  -5.250  1.00 53.18 ?  65  TRP I CZ3   1 
ATOM   7392  C  CH2   . TRP F 3 72  ? 35.515  41.716  -5.524  1.00 47.47 ?  65  TRP I CH2   1 
ATOM   7393  N  N     . SER F 3 73  ? 31.032  43.105  -6.677  1.00 41.85 ?  66  SER I N     1 
ATOM   7394  C  CA    . SER F 3 73  ? 31.025  42.120  -5.605  1.00 38.53 ?  66  SER I CA    1 
ATOM   7395  C  C     . SER F 3 73  ? 30.897  40.702  -6.183  1.00 40.44 ?  66  SER I C     1 
ATOM   7396  O  O     . SER F 3 73  ? 31.622  39.816  -5.678  1.00 32.48 ?  66  SER I O     1 
ATOM   7397  C  CB    . SER F 3 73  ? 29.933  42.404  -4.597  1.00 38.18 ?  66  SER I CB    1 
ATOM   7398  O  OG    . SER F 3 73  ? 30.301  43.460  -3.720  1.00 43.26 ?  66  SER I OG    1 
ATOM   7399  N  N     . GLY G 1 2   ? -2.410  69.204  14.034  1.00 27.80 ?  2   GLY J N     1 
ATOM   7400  C  CA    . GLY G 1 2   ? -1.103  68.723  14.522  1.00 27.87 ?  2   GLY J CA    1 
ATOM   7401  C  C     . GLY G 1 2   ? -0.525  67.659  13.593  1.00 29.72 ?  2   GLY J C     1 
ATOM   7402  O  O     . GLY G 1 2   ? -1.265  66.976  12.888  1.00 29.96 ?  2   GLY J O     1 
ATOM   7403  N  N     . SER G 1 3   ? 0.806   67.534  13.610  1.00 26.47 ?  3   SER J N     1 
ATOM   7404  C  CA    . SER G 1 3   ? 1.514   66.594  12.758  1.00 26.81 ?  3   SER J CA    1 
ATOM   7405  C  C     . SER G 1 3   ? 2.741   66.064  13.494  1.00 26.33 ?  3   SER J C     1 
ATOM   7406  O  O     . SER G 1 3   ? 3.148   66.626  14.508  1.00 25.32 ?  3   SER J O     1 
ATOM   7407  C  CB    . SER G 1 3   ? 1.899   67.236  11.449  1.00 25.44 ?  3   SER J CB    1 
ATOM   7408  O  OG    . SER G 1 3   ? 2.709   68.384  11.665  1.00 24.91 ?  3   SER J OG    1 
ATOM   7409  N  N     . LEU G 1 4   ? 3.326   64.982  12.969  1.00 24.83 ?  4   LEU J N     1 
ATOM   7410  C  CA    . LEU G 1 4   ? 4.510   64.393  13.569  1.00 23.39 ?  4   LEU J CA    1 
ATOM   7411  C  C     . LEU G 1 4   ? 5.610   64.237  12.523  1.00 19.21 ?  4   LEU J C     1 
ATOM   7412  O  O     . LEU G 1 4   ? 5.376   63.724  11.432  1.00 16.42 ?  4   LEU J O     1 
ATOM   7413  C  CB    . LEU G 1 4   ? 4.146   63.046  14.189  1.00 25.98 ?  4   LEU J CB    1 
ATOM   7414  C  CG    . LEU G 1 4   ? 5.297   62.273  14.837  1.00 28.00 ?  4   LEU J CG    1 
ATOM   7415  C  CD1   . LEU G 1 4   ? 5.916   63.044  15.990  1.00 30.24 ?  4   LEU J CD1   1 
ATOM   7416  C  CD2   . LEU G 1 4   ? 4.789   60.921  15.294  1.00 29.51 ?  4   LEU J CD2   1 
ATOM   7417  N  N     . VAL G 1 5   ? 6.815   64.690  12.883  1.00 19.87 ?  5   VAL J N     1 
ATOM   7418  C  CA    . VAL G 1 5   ? 8.012   64.365  12.130  1.00 17.29 ?  5   VAL J CA    1 
ATOM   7419  C  C     . VAL G 1 5   ? 9.100   63.949  13.115  1.00 15.07 ?  5   VAL J C     1 
ATOM   7420  O  O     . VAL G 1 5   ? 9.516   64.732  13.966  1.00 14.00 ?  5   VAL J O     1 
ATOM   7421  C  CB    . VAL G 1 5   ? 8.487   65.519  11.228  1.00 17.21 ?  5   VAL J CB    1 
ATOM   7422  C  CG1   . VAL G 1 5   ? 9.781   65.170  10.501  1.00 15.98 ?  5   VAL J CG1   1 
ATOM   7423  C  CG2   . VAL G 1 5   ? 7.407   65.929  10.234  1.00 16.70 ?  5   VAL J CG2   1 
ATOM   7424  N  N     . CYS G 1 6   ? 9.535   62.691  12.989  1.00 16.17 ?  6   CYS J N     1 
ATOM   7425  C  CA    . CYS G 1 6   ? 10.679  62.185  13.724  1.00 14.89 ?  6   CYS J CA    1 
ATOM   7426  C  C     . CYS G 1 6   ? 11.939  62.405  12.892  1.00 14.57 ?  6   CYS J C     1 
ATOM   7427  O  O     . CYS G 1 6   ? 11.967  62.074  11.709  1.00 15.58 ?  6   CYS J O     1 
ATOM   7428  C  CB    . CYS G 1 6   ? 10.515  60.703  14.036  1.00 15.13 ?  6   CYS J CB    1 
ATOM   7429  S  SG    . CYS G 1 6   ? 9.045   60.327  15.025  1.00 15.90 ?  6   CYS J SG    1 
ATOM   7430  N  N     . VAL G 1 7   ? 12.975  62.969  13.517  1.00 15.95 ?  7   VAL J N     1 
ATOM   7431  C  CA    . VAL G 1 7   ? 14.240  63.180  12.836  1.00 15.94 ?  7   VAL J CA    1 
ATOM   7432  C  C     . VAL G 1 7   ? 15.348  62.541  13.667  1.00 17.25 ?  7   VAL J C     1 
ATOM   7433  O  O     . VAL G 1 7   ? 15.108  62.065  14.775  1.00 18.83 ?  7   VAL J O     1 
ATOM   7434  C  CB    . VAL G 1 7   ? 14.518  64.673  12.565  1.00 17.04 ?  7   VAL J CB    1 
ATOM   7435  C  CG1   . VAL G 1 7   ? 13.355  65.334  11.833  1.00 15.57 ?  7   VAL J CG1   1 
ATOM   7436  C  CG2   . VAL G 1 7   ? 14.852  65.447  13.835  1.00 16.49 ?  7   VAL J CG2   1 
ATOM   7437  N  N     . GLY G 1 8   ? 16.557  62.511  13.100  1.00 16.57 ?  8   GLY J N     1 
ATOM   7438  C  CA    . GLY G 1 8   ? 17.740  62.086  13.826  1.00 14.91 ?  8   GLY J CA    1 
ATOM   7439  C  C     . GLY G 1 8   ? 18.774  63.207  13.875  1.00 13.47 ?  8   GLY J C     1 
ATOM   7440  O  O     . GLY G 1 8   ? 18.796  64.072  13.004  1.00 12.84 ?  8   GLY J O     1 
ATOM   7441  N  N     . THR G 1 9   ? 19.628  63.179  14.902  1.00 15.68 ?  9   THR J N     1 
ATOM   7442  C  CA    . THR G 1 9   ? 20.627  64.217  15.093  1.00 17.04 ?  9   THR J CA    1 
ATOM   7443  C  C     . THR G 1 9   ? 22.022  63.650  14.837  1.00 16.92 ?  9   THR J C     1 
ATOM   7444  O  O     . THR G 1 9   ? 23.017  64.322  15.096  1.00 19.59 ?  9   THR J O     1 
ATOM   7445  C  CB    . THR G 1 9   ? 20.512  64.777  16.509  1.00 17.53 ?  9   THR J CB    1 
ATOM   7446  O  OG1   . THR G 1 9   ? 20.983  63.739  17.362  1.00 17.39 ?  9   THR J OG1   1 
ATOM   7447  C  CG2   . THR G 1 9   ? 19.088  65.160  16.870  1.00 17.03 ?  9   THR J CG2   1 
ATOM   7448  N  N     . GLY G 1 10  ? 22.088  62.414  14.331  1.00 16.48 ?  10  GLY J N     1 
ATOM   7449  C  CA    . GLY G 1 10  ? 23.366  61.757  14.114  1.00 15.86 ?  10  GLY J CA    1 
ATOM   7450  C  C     . GLY G 1 10  ? 24.001  61.366  15.446  1.00 15.93 ?  10  GLY J C     1 
ATOM   7451  O  O     . GLY G 1 10  ? 23.317  61.308  16.464  1.00 15.41 ?  10  GLY J O     1 
ATOM   7452  N  N     . LEU G 1 11  ? 25.312  61.107  15.429  1.00 17.80 ?  11  LEU J N     1 
ATOM   7453  C  CA    . LEU G 1 11  ? 26.039  60.760  16.640  1.00 17.99 ?  11  LEU J CA    1 
ATOM   7454  C  C     . LEU G 1 11  ? 26.817  61.972  17.149  1.00 16.50 ?  11  LEU J C     1 
ATOM   7455  O  O     . LEU G 1 11  ? 26.833  62.237  18.349  1.00 17.48 ?  11  LEU J O     1 
ATOM   7456  C  CB    . LEU G 1 11  ? 26.964  59.572  16.380  1.00 19.24 ?  11  LEU J CB    1 
ATOM   7457  C  CG    . LEU G 1 11  ? 26.322  58.183  16.469  1.00 19.57 ?  11  LEU J CG    1 
ATOM   7458  C  CD1   . LEU G 1 11  ? 25.786  57.963  17.873  1.00 21.64 ?  11  LEU J CD1   1 
ATOM   7459  C  CD2   . LEU G 1 11  ? 25.225  57.977  15.440  1.00 22.21 ?  11  LEU J CD2   1 
ATOM   7460  N  N     . GLN G 1 12  ? 27.462  62.698  16.230  1.00 18.45 ?  12  GLN J N     1 
ATOM   7461  C  CA    . GLN G 1 12  ? 28.324  63.813  16.593  1.00 21.28 ?  12  GLN J CA    1 
ATOM   7462  C  C     . GLN G 1 12  ? 27.483  65.056  16.880  1.00 22.03 ?  12  GLN J C     1 
ATOM   7463  O  O     . GLN G 1 12  ? 26.450  65.282  16.255  1.00 23.05 ?  12  GLN J O     1 
ATOM   7464  C  CB    . GLN G 1 12  ? 29.359  64.094  15.501  1.00 22.11 ?  12  GLN J CB    1 
ATOM   7465  C  CG    . GLN G 1 12  ? 30.632  63.255  15.598  1.00 21.45 ?  12  GLN J CG    1 
ATOM   7466  C  CD    . GLN G 1 12  ? 31.581  63.720  16.682  1.00 22.22 ?  12  GLN J CD    1 
ATOM   7467  O  OE1   . GLN G 1 12  ? 31.243  64.561  17.523  1.00 19.61 ?  12  GLN J OE1   1 
ATOM   7468  N  NE2   . GLN G 1 12  ? 32.788  63.173  16.673  1.00 22.22 ?  12  GLN J NE2   1 
ATOM   7469  N  N     . LEU G 1 13  ? 27.967  65.855  17.837  1.00 21.46 ?  13  LEU J N     1 
ATOM   7470  C  CA    . LEU G 1 13  ? 27.336  67.095  18.261  1.00 18.48 ?  13  LEU J CA    1 
ATOM   7471  C  C     . LEU G 1 13  ? 27.153  68.056  17.087  1.00 19.05 ?  13  LEU J C     1 
ATOM   7472  O  O     . LEU G 1 13  ? 28.121  68.467  16.450  1.00 16.67 ?  13  LEU J O     1 
ATOM   7473  C  CB    . LEU G 1 13  ? 28.248  67.677  19.342  1.00 18.38 ?  13  LEU J CB    1 
ATOM   7474  C  CG    . LEU G 1 13  ? 27.876  69.046  19.921  1.00 17.60 ?  13  LEU J CG    1 
ATOM   7475  C  CD1   . LEU G 1 13  ? 26.506  69.076  20.577  1.00 17.67 ?  13  LEU J CD1   1 
ATOM   7476  C  CD2   . LEU G 1 13  ? 28.949  69.441  20.922  1.00 16.29 ?  13  LEU J CD2   1 
ATOM   7477  N  N     . ALA G 1 14  ? 25.888  68.394  16.810  1.00 18.52 ?  14  ALA J N     1 
ATOM   7478  C  CA    . ALA G 1 14  ? 25.532  69.583  16.050  1.00 18.75 ?  14  ALA J CA    1 
ATOM   7479  C  C     . ALA G 1 14  ? 25.741  69.393  14.546  1.00 19.15 ?  14  ALA J C     1 
ATOM   7480  O  O     . ALA G 1 14  ? 24.868  69.744  13.756  1.00 22.42 ?  14  ALA J O     1 
ATOM   7481  C  CB    . ALA G 1 14  ? 26.314  70.770  16.574  1.00 20.81 ?  14  ALA J CB    1 
ATOM   7482  N  N     . GLY G 1 15  ? 26.895  68.847  14.147  1.00 16.16 ?  15  GLY J N     1 
ATOM   7483  C  CA    . GLY G 1 15  ? 27.313  68.898  12.754  1.00 14.42 ?  15  GLY J CA    1 
ATOM   7484  C  C     . GLY G 1 15  ? 26.817  67.714  11.923  1.00 13.74 ?  15  GLY J C     1 
ATOM   7485  O  O     . GLY G 1 15  ? 26.931  67.740  10.699  1.00 11.72 ?  15  GLY J O     1 
ATOM   7486  N  N     . GLN G 1 16  ? 26.264  66.685  12.577  1.00 13.28 ?  16  GLN J N     1 
ATOM   7487  C  CA    . GLN G 1 16  ? 25.978  65.432  11.894  1.00 14.23 ?  16  GLN J CA    1 
ATOM   7488  C  C     . GLN G 1 16  ? 24.486  65.299  11.587  1.00 13.80 ?  16  GLN J C     1 
ATOM   7489  O  O     . GLN G 1 16  ? 24.071  64.317  10.974  1.00 12.90 ?  16  GLN J O     1 
ATOM   7490  C  CB    . GLN G 1 16  ? 26.489  64.239  12.702  1.00 14.93 ?  16  GLN J CB    1 
ATOM   7491  C  CG    . GLN G 1 16  ? 26.657  62.967  11.876  1.00 16.67 ?  16  GLN J CG    1 
ATOM   7492  C  CD    . GLN G 1 16  ? 27.660  62.001  12.468  1.00 18.77 ?  16  GLN J CD    1 
ATOM   7493  O  OE1   . GLN G 1 16  ? 27.379  61.288  13.438  1.00 19.49 ?  16  GLN J OE1   1 
ATOM   7494  N  NE2   . GLN G 1 16  ? 28.843  61.958  11.872  1.00 17.57 ?  16  GLN J NE2   1 
ATOM   7495  N  N     . ILE G 1 17  ? 23.679  66.285  11.994  1.00 13.54 ?  17  ILE J N     1 
ATOM   7496  C  CA    . ILE G 1 17  ? 22.279  66.304  11.596  1.00 14.39 ?  17  ILE J CA    1 
ATOM   7497  C  C     . ILE G 1 17  ? 22.197  66.813  10.160  1.00 11.40 ?  17  ILE J C     1 
ATOM   7498  O  O     . ILE G 1 17  ? 22.950  67.702  9.772   1.00 12.49 ?  17  ILE J O     1 
ATOM   7499  C  CB    . ILE G 1 17  ? 21.422  67.156  12.551  1.00 15.32 ?  17  ILE J CB    1 
ATOM   7500  C  CG1   . ILE G 1 17  ? 19.926  66.980  12.262  1.00 15.73 ?  17  ILE J CG1   1 
ATOM   7501  C  CG2   . ILE G 1 17  ? 21.843  68.626  12.495  1.00 14.79 ?  17  ILE J CG2   1 
ATOM   7502  C  CD1   . ILE G 1 17  ? 19.008  67.683  13.246  1.00 15.71 ?  17  ILE J CD1   1 
ATOM   7503  N  N     . SER G 1 18  ? 21.285  66.228  9.377   1.00 10.70 ?  18  SER J N     1 
ATOM   7504  C  CA    . SER G 1 18  ? 21.030  66.666  8.014   1.00 11.32 ?  18  SER J CA    1 
ATOM   7505  C  C     . SER G 1 18  ? 20.428  68.071  8.027   1.00 13.32 ?  18  SER J C     1 
ATOM   7506  O  O     . SER G 1 18  ? 19.859  68.493  9.031   1.00 12.08 ?  18  SER J O     1 
ATOM   7507  C  CB    . SER G 1 18  ? 20.130  65.695  7.295   1.00 11.03 ?  18  SER J CB    1 
ATOM   7508  O  OG    . SER G 1 18  ? 18.840  65.661  7.889   1.00 10.17 ?  18  SER J OG    1 
ATOM   7509  N  N     . VAL G 1 19  ? 20.552  68.784  6.902   1.00 15.09 ?  19  VAL J N     1 
ATOM   7510  C  CA    . VAL G 1 19  ? 20.176  70.188  6.838   1.00 19.77 ?  19  VAL J CA    1 
ATOM   7511  C  C     . VAL G 1 19  ? 18.665  70.306  7.031   1.00 20.98 ?  19  VAL J C     1 
ATOM   7512  O  O     . VAL G 1 19  ? 18.204  71.100  7.848   1.00 24.63 ?  19  VAL J O     1 
ATOM   7513  C  CB    . VAL G 1 19  ? 20.644  70.849  5.526   1.00 20.90 ?  19  VAL J CB    1 
ATOM   7514  C  CG1   . VAL G 1 19  ? 20.022  72.224  5.318   1.00 23.88 ?  19  VAL J CG1   1 
ATOM   7515  C  CG2   . VAL G 1 19  ? 22.165  70.943  5.456   1.00 20.85 ?  19  VAL J CG2   1 
ATOM   7516  N  N     . LEU G 1 20  ? 17.906  69.498  6.284   1.00 22.91 ?  20  LEU J N     1 
ATOM   7517  C  CA    . LEU G 1 20  ? 16.455  69.492  6.379   1.00 21.93 ?  20  LEU J CA    1 
ATOM   7518  C  C     . LEU G 1 20  ? 16.025  69.202  7.816   1.00 22.06 ?  20  LEU J C     1 
ATOM   7519  O  O     . LEU G 1 20  ? 15.115  69.846  8.333   1.00 21.57 ?  20  LEU J O     1 
ATOM   7520  C  CB    . LEU G 1 20  ? 15.875  68.462  5.410   1.00 24.11 ?  20  LEU J CB    1 
ATOM   7521  C  CG    . LEU G 1 20  ? 14.345  68.376  5.362   1.00 27.52 ?  20  LEU J CG    1 
ATOM   7522  C  CD1   . LEU G 1 20  ? 13.755  69.686  4.869   1.00 29.23 ?  20  LEU J CD1   1 
ATOM   7523  C  CD2   . LEU G 1 20  ? 13.863  67.219  4.501   1.00 25.49 ?  20  LEU J CD2   1 
ATOM   7524  N  N     . SER G 1 21  ? 16.688  68.228  8.452   1.00 20.29 ?  21  SER J N     1 
ATOM   7525  C  CA    . SER G 1 21  ? 16.254  67.716  9.743   1.00 17.66 ?  21  SER J CA    1 
ATOM   7526  C  C     . SER G 1 21  ? 16.409  68.787  10.815  1.00 15.20 ?  21  SER J C     1 
ATOM   7527  O  O     . SER G 1 21  ? 15.652  68.822  11.784  1.00 16.10 ?  21  SER J O     1 
ATOM   7528  C  CB    . SER G 1 21  ? 17.012  66.470  10.126  1.00 17.19 ?  21  SER J CB    1 
ATOM   7529  O  OG    . SER G 1 21  ? 16.623  65.367  9.321   1.00 18.56 ?  21  SER J OG    1 
ATOM   7530  N  N     . ARG G 1 22  ? 17.412  69.646  10.628  1.00 12.97 ?  22  ARG J N     1 
ATOM   7531  C  CA    . ARG G 1 22  ? 17.684  70.728  11.553  1.00 14.61 ?  22  ARG J CA    1 
ATOM   7532  C  C     . ARG G 1 22  ? 16.602  71.796  11.403  1.00 15.78 ?  22  ARG J C     1 
ATOM   7533  O  O     . ARG G 1 22  ? 16.076  72.300  12.393  1.00 12.87 ?  22  ARG J O     1 
ATOM   7534  C  CB    . ARG G 1 22  ? 19.088  71.261  11.254  1.00 16.53 ?  22  ARG J CB    1 
ATOM   7535  C  CG    . ARG G 1 22  ? 19.572  72.303  12.250  1.00 17.61 ?  22  ARG J CG    1 
ATOM   7536  C  CD    . ARG G 1 22  ? 20.817  73.018  11.759  1.00 18.80 ?  22  ARG J CD    1 
ATOM   7537  N  NE    . ARG G 1 22  ? 21.396  73.857  12.813  1.00 19.42 ?  22  ARG J NE    1 
ATOM   7538  C  CZ    . ARG G 1 22  ? 21.318  75.181  12.864  1.00 19.82 ?  22  ARG J CZ    1 
ATOM   7539  N  NH1   . ARG G 1 22  ? 20.630  75.844  11.951  1.00 18.05 1  22  ARG J NH1   1 
ATOM   7540  N  NH2   . ARG G 1 22  ? 21.917  75.838  13.841  1.00 21.37 ?  22  ARG J NH2   1 
ATOM   7541  N  N     . SER G 1 23  ? 16.274  72.118  10.148  1.00 16.97 ?  23  SER J N     1 
ATOM   7542  C  CA    . SER G 1 23  ? 15.259  73.112  9.840   1.00 18.76 ?  23  SER J CA    1 
ATOM   7543  C  C     . SER G 1 23  ? 13.898  72.683  10.389  1.00 20.10 ?  23  SER J C     1 
ATOM   7544  O  O     . SER G 1 23  ? 13.057  73.531  10.673  1.00 26.00 ?  23  SER J O     1 
ATOM   7545  C  CB    . SER G 1 23  ? 15.200  73.381  8.357   1.00 17.08 ?  23  SER J CB    1 
ATOM   7546  O  OG    . SER G 1 23  ? 14.058  74.157  8.024   1.00 15.09 ?  23  SER J OG    1 
ATOM   7547  N  N     . TYR G 1 24  ? 13.687  71.370  10.547  1.00 22.82 ?  24  TYR J N     1 
ATOM   7548  C  CA    . TYR G 1 24  ? 12.444  70.864  11.112  1.00 23.11 ?  24  TYR J CA    1 
ATOM   7549  C  C     . TYR G 1 24  ? 12.417  71.138  12.614  1.00 22.01 ?  24  TYR J C     1 
ATOM   7550  O  O     . TYR G 1 24  ? 11.394  71.554  13.153  1.00 24.81 ?  24  TYR J O     1 
ATOM   7551  C  CB    . TYR G 1 24  ? 12.226  69.367  10.864  1.00 23.89 ?  24  TYR J CB    1 
ATOM   7552  C  CG    . TYR G 1 24  ? 11.411  69.024  9.623   1.00 28.25 ?  24  TYR J CG    1 
ATOM   7553  C  CD1   . TYR G 1 24  ? 10.035  69.220  9.593   1.00 26.32 ?  24  TYR J CD1   1 
ATOM   7554  C  CD2   . TYR G 1 24  ? 12.010  68.471  8.498   1.00 29.36 ?  24  TYR J CD2   1 
ATOM   7555  C  CE1   . TYR G 1 24  ? 9.285   68.900  8.474   1.00 27.45 ?  24  TYR J CE1   1 
ATOM   7556  C  CE2   . TYR G 1 24  ? 11.270  68.145  7.374   1.00 31.39 ?  24  TYR J CE2   1 
ATOM   7557  C  CZ    . TYR G 1 24  ? 9.904   68.360  7.361   1.00 28.57 ?  24  TYR J CZ    1 
ATOM   7558  O  OH    . TYR G 1 24  ? 9.171   68.038  6.256   1.00 28.40 ?  24  TYR J OH    1 
ATOM   7559  N  N     . ILE G 1 25  ? 13.547  70.883  13.282  1.00 20.66 ?  25  ILE J N     1 
ATOM   7560  C  CA    . ILE G 1 25  ? 13.679  71.140  14.706  1.00 19.50 ?  25  ILE J CA    1 
ATOM   7561  C  C     . ILE G 1 25  ? 13.430  72.625  14.961  1.00 20.97 ?  25  ILE J C     1 
ATOM   7562  O  O     . ILE G 1 25  ? 12.718  72.994  15.892  1.00 20.95 ?  25  ILE J O     1 
ATOM   7563  C  CB    . ILE G 1 25  ? 15.063  70.686  15.208  1.00 18.93 ?  25  ILE J CB    1 
ATOM   7564  C  CG1   . ILE G 1 25  ? 15.171  69.160  15.252  1.00 18.17 ?  25  ILE J CG1   1 
ATOM   7565  C  CG2   . ILE G 1 25  ? 15.396  71.309  16.564  1.00 18.60 ?  25  ILE J CG2   1 
ATOM   7566  C  CD1   . ILE G 1 25  ? 16.541  68.645  15.653  1.00 17.22 ?  25  ILE J CD1   1 
ATOM   7567  N  N     . GLU G 1 26  ? 14.016  73.459  14.096  1.00 21.96 ?  26  GLU J N     1 
ATOM   7568  C  CA    . GLU G 1 26  ? 13.975  74.908  14.215  1.00 24.80 ?  26  GLU J CA    1 
ATOM   7569  C  C     . GLU G 1 26  ? 12.539  75.432  14.155  1.00 22.30 ?  26  GLU J C     1 
ATOM   7570  O  O     . GLU G 1 26  ? 12.175  76.313  14.930  1.00 24.03 ?  26  GLU J O     1 
ATOM   7571  C  CB    . GLU G 1 26  ? 14.855  75.473  13.098  1.00 26.74 ?  26  GLU J CB    1 
ATOM   7572  C  CG    . GLU G 1 26  ? 14.946  76.995  13.067  1.00 29.48 ?  26  GLU J CG    1 
ATOM   7573  C  CD    . GLU G 1 26  ? 15.812  77.513  11.931  1.00 36.40 ?  26  GLU J CD    1 
ATOM   7574  O  OE1   . GLU G 1 26  ? 16.330  76.678  11.157  1.00 33.89 ?  26  GLU J OE1   1 
ATOM   7575  O  OE2   . GLU G 1 26  ? 15.970  78.747  11.817  1.00 40.73 -1 26  GLU J OE2   1 
ATOM   7576  N  N     . HIS G 1 27  ? 11.729  74.893  13.234  1.00 22.39 ?  27  HIS J N     1 
ATOM   7577  C  CA    . HIS G 1 27  ? 10.407  75.437  12.956  1.00 20.94 ?  27  HIS J CA    1 
ATOM   7578  C  C     . HIS G 1 27  ? 9.301   74.675  13.684  1.00 19.01 ?  27  HIS J C     1 
ATOM   7579  O  O     . HIS G 1 27  ? 8.124   74.903  13.415  1.00 16.51 ?  27  HIS J O     1 
ATOM   7580  C  CB    . HIS G 1 27  ? 10.113  75.428  11.451  1.00 24.36 ?  27  HIS J CB    1 
ATOM   7581  C  CG    . HIS G 1 27  ? 10.866  76.468  10.694  1.00 25.72 ?  27  HIS J CG    1 
ATOM   7582  N  ND1   . HIS G 1 27  ? 11.958  76.195  9.899   1.00 26.71 ?  27  HIS J ND1   1 
ATOM   7583  C  CD2   . HIS G 1 27  ? 10.668  77.789  10.612  1.00 24.75 ?  27  HIS J CD2   1 
ATOM   7584  C  CE1   . HIS G 1 27  ? 12.401  77.325  9.366   1.00 28.13 ?  27  HIS J CE1   1 
ATOM   7585  N  NE2   . HIS G 1 27  ? 11.633  78.306  9.787   1.00 27.90 ?  27  HIS J NE2   1 
ATOM   7586  N  N     . ALA G 1 28  ? 9.675   73.776  14.602  1.00 17.95 ?  28  ALA J N     1 
ATOM   7587  C  CA    . ALA G 1 28  ? 8.701   72.975  15.327  1.00 16.16 ?  28  ALA J CA    1 
ATOM   7588  C  C     . ALA G 1 28  ? 7.983   73.819  16.377  1.00 14.75 ?  28  ALA J C     1 
ATOM   7589  O  O     . ALA G 1 28  ? 8.548   74.773  16.904  1.00 12.81 ?  28  ALA J O     1 
ATOM   7590  C  CB    . ALA G 1 28  ? 9.380   71.790  15.978  1.00 16.26 ?  28  ALA J CB    1 
ATOM   7591  N  N     . ASP G 1 29  ? 6.742   73.427  16.690  1.00 15.32 ?  29  ASP J N     1 
ATOM   7592  C  CA    . ASP G 1 29  ? 6.007   73.990  17.811  1.00 16.32 ?  29  ASP J CA    1 
ATOM   7593  C  C     . ASP G 1 29  ? 6.618   73.470  19.108  1.00 17.47 ?  29  ASP J C     1 
ATOM   7594  O  O     . ASP G 1 29  ? 6.759   74.211  20.078  1.00 18.10 ?  29  ASP J O     1 
ATOM   7595  C  CB    . ASP G 1 29  ? 4.533   73.618  17.768  1.00 17.36 ?  29  ASP J CB    1 
ATOM   7596  C  CG    . ASP G 1 29  ? 3.693   74.336  16.722  1.00 15.84 ?  29  ASP J CG    1 
ATOM   7597  O  OD1   . ASP G 1 29  ? 4.175   75.347  16.173  1.00 16.30 ?  29  ASP J OD1   1 
ATOM   7598  O  OD2   . ASP G 1 29  ? 2.569   73.865  16.454  1.00 15.57 -1 29  ASP J OD2   1 
ATOM   7599  N  N     . ILE G 1 30  ? 6.971   72.181  19.100  1.00 16.50 ?  30  ILE J N     1 
ATOM   7600  C  CA    . ILE G 1 30  ? 7.482   71.509  20.282  1.00 17.26 ?  30  ILE J CA    1 
ATOM   7601  C  C     . ILE G 1 30  ? 8.407   70.381  19.839  1.00 17.15 ?  30  ILE J C     1 
ATOM   7602  O  O     . ILE G 1 30  ? 8.215   69.798  18.773  1.00 14.31 ?  30  ILE J O     1 
ATOM   7603  C  CB    . ILE G 1 30  ? 6.323   70.985  21.149  1.00 17.38 ?  30  ILE J CB    1 
ATOM   7604  C  CG1   . ILE G 1 30  ? 6.817   70.412  22.474  1.00 17.28 ?  30  ILE J CG1   1 
ATOM   7605  C  CG2   . ILE G 1 30  ? 5.482   69.968  20.376  1.00 16.92 ?  30  ILE J CG2   1 
ATOM   7606  C  CD1   . ILE G 1 30  ? 5.702   70.083  23.451  1.00 18.59 ?  30  ILE J CD1   1 
ATOM   7607  N  N     . VAL G 1 31  ? 9.401   70.077  20.681  1.00 17.51 ?  31  VAL J N     1 
ATOM   7608  C  CA    . VAL G 1 31  ? 10.396  69.068  20.360  1.00 19.90 ?  31  VAL J CA    1 
ATOM   7609  C  C     . VAL G 1 31  ? 10.517  68.091  21.524  1.00 19.76 ?  31  VAL J C     1 
ATOM   7610  O  O     . VAL G 1 31  ? 10.660  68.496  22.676  1.00 20.07 ?  31  VAL J O     1 
ATOM   7611  C  CB    . VAL G 1 31  ? 11.758  69.713  20.043  1.00 19.19 ?  31  VAL J CB    1 
ATOM   7612  C  CG1   . VAL G 1 31  ? 12.813  68.670  19.689  1.00 20.00 ?  31  VAL J CG1   1 
ATOM   7613  C  CG2   . VAL G 1 31  ? 11.637  70.757  18.942  1.00 18.10 ?  31  VAL J CG2   1 
ATOM   7614  N  N     . PHE G 1 32  ? 10.459  66.798  21.197  1.00 19.85 ?  32  PHE J N     1 
ATOM   7615  C  CA    . PHE G 1 32  ? 10.762  65.746  22.149  1.00 20.43 ?  32  PHE J CA    1 
ATOM   7616  C  C     . PHE G 1 32  ? 12.131  65.171  21.807  1.00 21.02 ?  32  PHE J C     1 
ATOM   7617  O  O     . PHE G 1 32  ? 12.319  64.582  20.745  1.00 20.47 ?  32  PHE J O     1 
ATOM   7618  C  CB    . PHE G 1 32  ? 9.660   64.685  22.130  1.00 20.94 ?  32  PHE J CB    1 
ATOM   7619  C  CG    . PHE G 1 32  ? 8.308   65.227  22.569  1.00 22.65 ?  32  PHE J CG    1 
ATOM   7620  C  CD1   . PHE G 1 32  ? 7.476   65.879  21.665  1.00 22.24 ?  32  PHE J CD1   1 
ATOM   7621  C  CD2   . PHE G 1 32  ? 7.883   65.101  23.886  1.00 22.55 ?  32  PHE J CD2   1 
ATOM   7622  C  CE1   . PHE G 1 32  ? 6.248   66.378  22.068  1.00 23.56 ?  32  PHE J CE1   1 
ATOM   7623  C  CE2   . PHE G 1 32  ? 6.653   65.601  24.283  1.00 23.18 ?  32  PHE J CE2   1 
ATOM   7624  C  CZ    . PHE G 1 32  ? 5.839   66.239  23.375  1.00 24.22 ?  32  PHE J CZ    1 
ATOM   7625  N  N     . SER G 1 33  ? 13.074  65.357  22.732  1.00 21.29 ?  33  SER J N     1 
ATOM   7626  C  CA    . SER G 1 33  ? 14.468  65.040  22.488  1.00 21.70 ?  33  SER J CA    1 
ATOM   7627  C  C     . SER G 1 33  ? 14.829  63.710  23.141  1.00 23.80 ?  33  SER J C     1 
ATOM   7628  O  O     . SER G 1 33  ? 14.146  63.247  24.052  1.00 23.27 ?  33  SER J O     1 
ATOM   7629  C  CB    . SER G 1 33  ? 15.359  66.148  22.989  1.00 20.16 ?  33  SER J CB    1 
ATOM   7630  O  OG    . SER G 1 33  ? 15.189  66.342  24.386  1.00 18.82 ?  33  SER J OG    1 
ATOM   7631  N  N     . LEU G 1 34  ? 15.912  63.109  22.640  1.00 26.42 ?  34  LEU J N     1 
ATOM   7632  C  CA    . LEU G 1 34  ? 16.555  61.974  23.279  1.00 28.11 ?  34  LEU J CA    1 
ATOM   7633  C  C     . LEU G 1 34  ? 17.972  61.888  22.720  1.00 27.60 ?  34  LEU J C     1 
ATOM   7634  O  O     . LEU G 1 34  ? 18.221  61.213  21.723  1.00 30.07 ?  34  LEU J O     1 
ATOM   7635  C  CB    . LEU G 1 34  ? 15.769  60.681  23.064  1.00 29.00 ?  34  LEU J CB    1 
ATOM   7636  C  CG    . LEU G 1 34  ? 16.097  59.536  24.028  1.00 33.81 ?  34  LEU J CG    1 
ATOM   7637  C  CD1   . LEU G 1 34  ? 15.701  59.898  25.452  1.00 35.47 ?  34  LEU J CD1   1 
ATOM   7638  C  CD2   . LEU G 1 34  ? 15.421  58.246  23.598  1.00 35.97 ?  34  LEU J CD2   1 
ATOM   7639  N  N     . LEU G 1 35  ? 18.880  62.615  23.376  1.00 27.41 ?  35  LEU J N     1 
ATOM   7640  C  CA    . LEU G 1 35  ? 20.212  62.874  22.858  1.00 27.77 ?  35  LEU J CA    1 
ATOM   7641  C  C     . LEU G 1 35  ? 21.248  62.209  23.760  1.00 27.22 ?  35  LEU J C     1 
ATOM   7642  O  O     . LEU G 1 35  ? 20.944  61.851  24.895  1.00 23.43 ?  35  LEU J O     1 
ATOM   7643  C  CB    . LEU G 1 35  ? 20.373  64.393  22.805  1.00 27.10 ?  35  LEU J CB    1 
ATOM   7644  C  CG    . LEU G 1 35  ? 19.277  65.149  22.044  1.00 28.72 ?  35  LEU J CG    1 
ATOM   7645  C  CD1   . LEU G 1 35  ? 19.528  66.646  22.071  1.00 28.68 ?  35  LEU J CD1   1 
ATOM   7646  C  CD2   . LEU G 1 35  ? 19.155  64.656  20.611  1.00 27.19 ?  35  LEU J CD2   1 
ATOM   7647  N  N     . PRO G 1 36  ? 22.498  62.005  23.283  1.00 29.23 ?  36  PRO J N     1 
ATOM   7648  C  CA    . PRO G 1 36  ? 23.513  61.291  24.064  1.00 28.20 ?  36  PRO J CA    1 
ATOM   7649  C  C     . PRO G 1 36  ? 24.004  61.967  25.344  1.00 29.49 ?  36  PRO J C     1 
ATOM   7650  O  O     . PRO G 1 36  ? 24.497  61.288  26.242  1.00 28.76 ?  36  PRO J O     1 
ATOM   7651  C  CB    . PRO G 1 36  ? 24.662  61.123  23.042  1.00 29.00 ?  36  PRO J CB    1 
ATOM   7652  C  CG    . PRO G 1 36  ? 24.002  61.297  21.692  1.00 29.52 ?  36  PRO J CG    1 
ATOM   7653  C  CD    . PRO G 1 36  ? 22.971  62.380  21.941  1.00 29.95 ?  36  PRO J CD    1 
ATOM   7654  N  N     . ASP G 1 37  ? 23.876  63.297  25.427  1.00 29.08 ?  37  ASP J N     1 
ATOM   7655  C  CA    . ASP G 1 37  ? 24.533  64.046  26.488  1.00 28.33 ?  37  ASP J CA    1 
ATOM   7656  C  C     . ASP G 1 37  ? 23.964  65.458  26.600  1.00 28.26 ?  37  ASP J C     1 
ATOM   7657  O  O     . ASP G 1 37  ? 23.030  65.823  25.889  1.00 30.69 ?  37  ASP J O     1 
ATOM   7658  C  CB    . ASP G 1 37  ? 26.034  64.108  26.252  1.00 28.78 ?  37  ASP J CB    1 
ATOM   7659  C  CG    . ASP G 1 37  ? 26.450  64.691  24.910  1.00 27.92 ?  37  ASP J CG    1 
ATOM   7660  O  OD1   . ASP G 1 37  ? 26.135  65.874  24.663  1.00 30.06 ?  37  ASP J OD1   1 
ATOM   7661  O  OD2   . ASP G 1 37  ? 27.077  63.956  24.119  1.00 24.24 -1 37  ASP J OD2   1 
ATOM   7662  N  N     . GLY G 1 38  ? 24.566  66.246  27.500  1.00 28.88 ?  38  GLY J N     1 
ATOM   7663  C  CA    . GLY G 1 38  ? 24.097  67.583  27.826  1.00 28.11 ?  38  GLY J CA    1 
ATOM   7664  C  C     . GLY G 1 38  ? 24.568  68.630  26.818  1.00 26.91 ?  38  GLY J C     1 
ATOM   7665  O  O     . GLY G 1 38  ? 23.938  69.675  26.676  1.00 25.88 ?  38  GLY J O     1 
ATOM   7666  N  N     . PHE G 1 39  ? 25.684  68.354  26.134  1.00 25.89 ?  39  PHE J N     1 
ATOM   7667  C  CA    . PHE G 1 39  ? 26.206  69.265  25.128  1.00 24.96 ?  39  PHE J CA    1 
ATOM   7668  C  C     . PHE G 1 39  ? 25.244  69.308  23.946  1.00 25.63 ?  39  PHE J C     1 
ATOM   7669  O  O     . PHE G 1 39  ? 24.994  70.364  23.369  1.00 28.93 ?  39  PHE J O     1 
ATOM   7670  C  CB    . PHE G 1 39  ? 27.602  68.835  24.670  1.00 25.80 ?  39  PHE J CB    1 
ATOM   7671  C  CG    . PHE G 1 39  ? 28.669  69.013  25.740  1.00 25.89 ?  39  PHE J CG    1 
ATOM   7672  C  CD1   . PHE G 1 39  ? 29.133  70.281  26.069  1.00 26.01 ?  39  PHE J CD1   1 
ATOM   7673  C  CD2   . PHE G 1 39  ? 29.200  67.919  26.413  1.00 25.91 ?  39  PHE J CD2   1 
ATOM   7674  C  CE1   . PHE G 1 39  ? 30.099  70.449  27.048  1.00 24.73 ?  39  PHE J CE1   1 
ATOM   7675  C  CE2   . PHE G 1 39  ? 30.168  68.094  27.389  1.00 26.56 ?  39  PHE J CE2   1 
ATOM   7676  C  CZ    . PHE G 1 39  ? 30.614  69.356  27.703  1.00 25.79 ?  39  PHE J CZ    1 
ATOM   7677  N  N     . SER G 1 40  ? 24.724  68.129  23.602  1.00 25.65 ?  40  SER J N     1 
ATOM   7678  C  CA    . SER G 1 40  ? 23.786  67.972  22.506  1.00 25.23 ?  40  SER J CA    1 
ATOM   7679  C  C     . SER G 1 40  ? 22.431  68.536  22.917  1.00 22.25 ?  40  SER J C     1 
ATOM   7680  O  O     . SER G 1 40  ? 21.678  69.039  22.086  1.00 20.35 ?  40  SER J O     1 
ATOM   7681  C  CB    . SER G 1 40  ? 23.677  66.521  22.110  1.00 24.51 ?  40  SER J CB    1 
ATOM   7682  O  OG    . SER G 1 40  ? 22.642  66.327  21.156  1.00 28.03 ?  40  SER J OG    1 
ATOM   7683  N  N     . GLN G 1 41  ? 22.140  68.436  24.217  1.00 21.52 ?  41  GLN J N     1 
ATOM   7684  C  CA    . GLN G 1 41  ? 20.881  68.904  24.767  1.00 23.19 ?  41  GLN J CA    1 
ATOM   7685  C  C     . GLN G 1 41  ? 20.853  70.430  24.727  1.00 23.26 ?  41  GLN J C     1 
ATOM   7686  O  O     . GLN G 1 41  ? 19.830  71.023  24.393  1.00 23.15 ?  41  GLN J O     1 
ATOM   7687  C  CB    . GLN G 1 41  ? 20.695  68.368  26.187  1.00 25.61 ?  41  GLN J CB    1 
ATOM   7688  C  CG    . GLN G 1 41  ? 19.261  68.453  26.698  1.00 25.55 ?  41  GLN J CG    1 
ATOM   7689  C  CD    . GLN G 1 41  ? 18.317  67.511  25.982  1.00 26.32 ?  41  GLN J CD    1 
ATOM   7690  O  OE1   . GLN G 1 41  ? 18.508  66.290  25.972  1.00 31.33 ?  41  GLN J OE1   1 
ATOM   7691  N  NE2   . GLN G 1 41  ? 17.282  68.072  25.374  1.00 25.90 ?  41  GLN J NE2   1 
ATOM   7692  N  N     . ARG G 1 42  ? 21.986  71.057  25.064  1.00 22.53 ?  42  ARG J N     1 
ATOM   7693  C  CA    . ARG G 1 42  ? 22.100  72.506  25.034  1.00 25.64 ?  42  ARG J CA    1 
ATOM   7694  C  C     . ARG G 1 42  ? 21.952  73.011  23.603  1.00 25.61 ?  42  ARG J C     1 
ATOM   7695  O  O     . ARG G 1 42  ? 21.188  73.938  23.345  1.00 26.80 ?  42  ARG J O     1 
ATOM   7696  C  CB    . ARG G 1 42  ? 23.444  72.995  25.583  1.00 26.49 ?  42  ARG J CB    1 
ATOM   7697  C  CG    . ARG G 1 42  ? 23.557  72.907  27.096  1.00 29.36 ?  42  ARG J CG    1 
ATOM   7698  C  CD    . ARG G 1 42  ? 24.904  73.416  27.577  1.00 34.96 ?  42  ARG J CD    1 
ATOM   7699  N  NE    . ARG G 1 42  ? 25.025  73.307  29.034  1.00 37.95 ?  42  ARG J NE    1 
ATOM   7700  C  CZ    . ARG G 1 42  ? 25.143  74.332  29.868  1.00 48.99 ?  42  ARG J CZ    1 
ATOM   7701  N  NH1   . ARG G 1 42  ? 25.172  75.570  29.405  1.00 48.70 1  42  ARG J NH1   1 
ATOM   7702  N  NH2   . ARG G 1 42  ? 25.233  74.111  31.167  1.00 49.08 ?  42  ARG J NH2   1 
ATOM   7703  N  N     . TRP G 1 43  ? 22.713  72.409  22.683  1.00 24.54 ?  43  TRP J N     1 
ATOM   7704  C  CA    . TRP G 1 43  ? 22.638  72.774  21.279  1.00 22.11 ?  43  TRP J CA    1 
ATOM   7705  C  C     . TRP G 1 43  ? 21.180  72.795  20.830  1.00 21.33 ?  43  TRP J C     1 
ATOM   7706  O  O     . TRP G 1 43  ? 20.739  73.747  20.191  1.00 21.46 ?  43  TRP J O     1 
ATOM   7707  C  CB    . TRP G 1 43  ? 23.473  71.808  20.425  1.00 20.19 ?  43  TRP J CB    1 
ATOM   7708  C  CG    . TRP G 1 43  ? 23.075  71.752  18.973  1.00 18.56 ?  43  TRP J CG    1 
ATOM   7709  C  CD1   . TRP G 1 43  ? 23.467  72.592  17.972  1.00 20.18 ?  43  TRP J CD1   1 
ATOM   7710  C  CD2   . TRP G 1 43  ? 22.220  70.765  18.354  1.00 17.51 ?  43  TRP J CD2   1 
ATOM   7711  N  NE1   . TRP G 1 43  ? 22.905  72.211  16.781  1.00 19.51 ?  43  TRP J NE1   1 
ATOM   7712  C  CE2   . TRP G 1 43  ? 22.140  71.092  16.982  1.00 18.08 ?  43  TRP J CE2   1 
ATOM   7713  C  CE3   . TRP G 1 43  ? 21.517  69.650  18.823  1.00 16.44 ?  43  TRP J CE3   1 
ATOM   7714  C  CZ2   . TRP G 1 43  ? 21.387  70.340  16.083  1.00 18.16 ?  43  TRP J CZ2   1 
ATOM   7715  C  CZ3   . TRP G 1 43  ? 20.777  68.906  17.931  1.00 16.49 ?  43  TRP J CZ3   1 
ATOM   7716  C  CH2   . TRP G 1 43  ? 20.715  69.247  16.580  1.00 17.39 ?  43  TRP J CH2   1 
ATOM   7717  N  N     . LEU G 1 44  ? 20.436  71.742  21.184  1.00 21.30 ?  44  LEU J N     1 
ATOM   7718  C  CA    . LEU G 1 44  ? 19.059  71.603  20.741  1.00 23.21 ?  44  LEU J CA    1 
ATOM   7719  C  C     . LEU G 1 44  ? 18.234  72.778  21.261  1.00 25.37 ?  44  LEU J C     1 
ATOM   7720  O  O     . LEU G 1 44  ? 17.446  73.365  20.523  1.00 25.84 ?  44  LEU J O     1 
ATOM   7721  C  CB    . LEU G 1 44  ? 18.479  70.268  21.206  1.00 21.53 ?  44  LEU J CB    1 
ATOM   7722  C  CG    . LEU G 1 44  ? 17.007  70.031  20.856  1.00 22.19 ?  44  LEU J CG    1 
ATOM   7723  C  CD1   . LEU G 1 44  ? 16.770  70.183  19.363  1.00 24.27 ?  44  LEU J CD1   1 
ATOM   7724  C  CD2   . LEU G 1 44  ? 16.539  68.670  21.333  1.00 21.29 ?  44  LEU J CD2   1 
ATOM   7725  N  N     . THR G 1 45  ? 18.435  73.110  22.539  1.00 27.08 ?  45  THR J N     1 
ATOM   7726  C  CA    . THR G 1 45  ? 17.633  74.111  23.223  1.00 30.46 ?  45  THR J CA    1 
ATOM   7727  C  C     . THR G 1 45  ? 17.901  75.492  22.625  1.00 30.52 ?  45  THR J C     1 
ATOM   7728  O  O     . THR G 1 45  ? 17.037  76.365  22.677  1.00 32.98 ?  45  THR J O     1 
ATOM   7729  C  CB    . THR G 1 45  ? 17.944  74.041  24.718  1.00 31.62 ?  45  THR J CB    1 
ATOM   7730  O  OG1   . THR G 1 45  ? 17.521  72.741  25.120  1.00 29.39 ?  45  THR J OG1   1 
ATOM   7731  C  CG2   . THR G 1 45  ? 17.217  75.099  25.528  1.00 30.57 ?  45  THR J CG2   1 
ATOM   7732  N  N     . LYS G 1 46  ? 19.099  75.679  22.056  1.00 31.27 ?  46  LYS J N     1 
ATOM   7733  C  CA    . LYS G 1 46  ? 19.437  76.892  21.326  1.00 30.08 ?  46  LYS J CA    1 
ATOM   7734  C  C     . LYS G 1 46  ? 18.683  76.930  19.997  1.00 28.13 ?  46  LYS J C     1 
ATOM   7735  O  O     . LYS G 1 46  ? 18.239  77.991  19.565  1.00 26.98 ?  46  LYS J O     1 
ATOM   7736  C  CB    . LYS G 1 46  ? 20.951  76.996  21.102  1.00 35.36 ?  46  LYS J CB    1 
ATOM   7737  C  CG    . LYS G 1 46  ? 21.721  77.776  22.163  1.00 39.29 ?  46  LYS J CG    1 
ATOM   7738  C  CD    . LYS G 1 46  ? 23.236  77.688  22.018  1.00 43.41 ?  46  LYS J CD    1 
ATOM   7739  C  CE    . LYS G 1 46  ? 23.955  78.892  22.544  1.00 47.32 ?  46  LYS J CE    1 
ATOM   7740  N  NZ    . LYS G 1 46  ? 23.839  80.028  21.625  1.00 51.39 1  46  LYS J NZ    1 
ATOM   7741  N  N     . LEU G 1 47  ? 18.552  75.765  19.350  1.00 26.07 ?  47  LEU J N     1 
ATOM   7742  C  CA    . LEU G 1 47  ? 17.809  75.651  18.104  1.00 25.27 ?  47  LEU J CA    1 
ATOM   7743  C  C     . LEU G 1 47  ? 16.336  75.977  18.336  1.00 23.70 ?  47  LEU J C     1 
ATOM   7744  O  O     . LEU G 1 47  ? 15.727  76.699  17.551  1.00 24.25 ?  47  LEU J O     1 
ATOM   7745  C  CB    . LEU G 1 47  ? 17.966  74.256  17.498  1.00 23.07 ?  47  LEU J CB    1 
ATOM   7746  C  CG    . LEU G 1 47  ? 18.852  74.163  16.253  1.00 22.92 ?  47  LEU J CG    1 
ATOM   7747  C  CD1   . LEU G 1 47  ? 18.963  72.732  15.751  1.00 21.75 ?  47  LEU J CD1   1 
ATOM   7748  C  CD2   . LEU G 1 47  ? 18.299  75.073  15.168  1.00 23.06 ?  47  LEU J CD2   1 
ATOM   7749  N  N     . ASN G 1 48  ? 15.769  75.421  19.411  1.00 22.65 ?  48  ASN J N     1 
ATOM   7750  C  CA    . ASN G 1 48  ? 14.347  75.558  19.681  1.00 21.03 ?  48  ASN J CA    1 
ATOM   7751  C  C     . ASN G 1 48  ? 14.103  75.306  21.166  1.00 22.91 ?  48  ASN J C     1 
ATOM   7752  O  O     . ASN G 1 48  ? 14.263  74.188  21.651  1.00 21.34 ?  48  ASN J O     1 
ATOM   7753  C  CB    . ASN G 1 48  ? 13.530  74.656  18.763  1.00 22.33 ?  48  ASN J CB    1 
ATOM   7754  C  CG    . ASN G 1 48  ? 12.049  74.728  19.049  1.00 23.26 ?  48  ASN J CG    1 
ATOM   7755  O  OD1   . ASN G 1 48  ? 11.644  75.167  20.132  1.00 21.91 ?  48  ASN J OD1   1 
ATOM   7756  N  ND2   . ASN G 1 48  ? 11.232  74.287  18.105  1.00 22.88 ?  48  ASN J ND2   1 
ATOM   7757  N  N     . PRO G 1 49  ? 13.705  76.350  21.928  1.00 25.11 ?  49  PRO J N     1 
ATOM   7758  C  CA    . PRO G 1 49  ? 13.624  76.255  23.387  1.00 23.87 ?  49  PRO J CA    1 
ATOM   7759  C  C     . PRO G 1 49  ? 12.484  75.394  23.928  1.00 23.83 ?  49  PRO J C     1 
ATOM   7760  O  O     . PRO G 1 49  ? 12.517  74.984  25.086  1.00 23.45 ?  49  PRO J O     1 
ATOM   7761  C  CB    . PRO G 1 49  ? 13.481  77.735  23.791  1.00 24.44 ?  49  PRO J CB    1 
ATOM   7762  C  CG    . PRO G 1 49  ? 12.737  78.360  22.634  1.00 25.22 ?  49  PRO J CG    1 
ATOM   7763  C  CD    . PRO G 1 49  ? 13.322  77.675  21.413  1.00 25.45 ?  49  PRO J CD    1 
ATOM   7764  N  N     . ASN G 1 50  ? 11.479  75.118  23.089  1.00 22.94 ?  50  ASN J N     1 
ATOM   7765  C  CA    . ASN G 1 50  ? 10.347  74.307  23.508  1.00 21.27 ?  50  ASN J CA    1 
ATOM   7766  C  C     . ASN G 1 50  ? 10.686  72.830  23.310  1.00 21.75 ?  50  ASN J C     1 
ATOM   7767  O  O     . ASN G 1 50  ? 10.342  72.245  22.285  1.00 19.78 ?  50  ASN J O     1 
ATOM   7768  C  CB    . ASN G 1 50  ? 9.073   74.698  22.766  1.00 21.14 ?  50  ASN J CB    1 
ATOM   7769  C  CG    . ASN G 1 50  ? 7.827   74.243  23.489  1.00 21.93 ?  50  ASN J CG    1 
ATOM   7770  O  OD1   . ASN G 1 50  ? 7.889   73.885  24.670  1.00 24.30 ?  50  ASN J OD1   1 
ATOM   7771  N  ND2   . ASN G 1 50  ? 6.688   74.271  22.812  1.00 22.80 ?  50  ASN J ND2   1 
ATOM   7772  N  N     . VAL G 1 51  ? 11.361  72.238  24.304  1.00 21.71 ?  51  VAL J N     1 
ATOM   7773  C  CA    . VAL G 1 51  ? 11.779  70.843  24.251  1.00 22.01 ?  51  VAL J CA    1 
ATOM   7774  C  C     . VAL G 1 51  ? 11.274  70.115  25.496  1.00 20.74 ?  51  VAL J C     1 
ATOM   7775  O  O     . VAL G 1 51  ? 11.371  70.640  26.603  1.00 21.02 ?  51  VAL J O     1 
ATOM   7776  C  CB    . VAL G 1 51  ? 13.314  70.723  24.150  1.00 23.70 ?  51  VAL J CB    1 
ATOM   7777  C  CG1   . VAL G 1 51  ? 13.781  69.274  24.224  1.00 25.30 ?  51  VAL J CG1   1 
ATOM   7778  C  CG2   . VAL G 1 51  ? 13.868  71.401  22.903  1.00 25.26 ?  51  VAL J CG2   1 
ATOM   7779  N  N     . ILE G 1 52  ? 10.740  68.902  25.303  1.00 21.50 ?  52  ILE J N     1 
ATOM   7780  C  CA    . ILE G 1 52  ? 10.476  67.987  26.405  1.00 23.22 ?  52  ILE J CA    1 
ATOM   7781  C  C     . ILE G 1 52  ? 11.410  66.785  26.266  1.00 22.49 ?  52  ILE J C     1 
ATOM   7782  O  O     . ILE G 1 52  ? 11.384  66.082  25.258  1.00 20.61 ?  52  ILE J O     1 
ATOM   7783  C  CB    . ILE G 1 52  ? 8.995   67.559  26.459  1.00 24.49 ?  52  ILE J CB    1 
ATOM   7784  C  CG1   . ILE G 1 52  ? 8.083   68.669  27.004  1.00 24.25 ?  52  ILE J CG1   1 
ATOM   7785  C  CG2   . ILE G 1 52  ? 8.837   66.278  27.278  1.00 23.38 ?  52  ILE J CG2   1 
ATOM   7786  C  CD1   . ILE G 1 52  ? 7.990   69.904  26.127  1.00 23.54 ?  52  ILE J CD1   1 
ATOM   7787  N  N     . ASN G 1 53  ? 12.227  66.559  27.301  1.00 21.72 ?  53  ASN J N     1 
ATOM   7788  C  CA    . ASN G 1 53  ? 13.297  65.573  27.268  1.00 20.42 ?  53  ASN J CA    1 
ATOM   7789  C  C     . ASN G 1 53  ? 12.730  64.198  27.622  1.00 19.52 ?  53  ASN J C     1 
ATOM   7790  O  O     . ASN G 1 53  ? 12.302  63.971  28.751  1.00 18.78 ?  53  ASN J O     1 
ATOM   7791  C  CB    . ASN G 1 53  ? 14.436  66.017  28.182  1.00 19.02 ?  53  ASN J CB    1 
ATOM   7792  C  CG    . ASN G 1 53  ? 15.693  65.200  28.005  1.00 18.81 ?  53  ASN J CG    1 
ATOM   7793  O  OD1   . ASN G 1 53  ? 15.630  64.031  27.607  1.00 18.61 ?  53  ASN J OD1   1 
ATOM   7794  N  ND2   . ASN G 1 53  ? 16.838  65.788  28.321  1.00 18.08 ?  53  ASN J ND2   1 
ATOM   7795  N  N     . LEU G 1 54  ? 12.740  63.282  26.647  1.00 21.06 ?  54  LEU J N     1 
ATOM   7796  C  CA    . LEU G 1 54  ? 12.161  61.959  26.825  1.00 21.53 ?  54  LEU J CA    1 
ATOM   7797  C  C     . LEU G 1 54  ? 12.939  61.179  27.885  1.00 22.92 ?  54  LEU J C     1 
ATOM   7798  O  O     . LEU G 1 54  ? 12.395  60.276  28.515  1.00 25.78 ?  54  LEU J O     1 
ATOM   7799  C  CB    . LEU G 1 54  ? 12.141  61.223  25.486  1.00 22.86 ?  54  LEU J CB    1 
ATOM   7800  C  CG    . LEU G 1 54  ? 11.286  61.856  24.383  1.00 26.32 ?  54  LEU J CG    1 
ATOM   7801  C  CD1   . LEU G 1 54  ? 11.429  61.083  23.082  1.00 24.48 ?  54  LEU J CD1   1 
ATOM   7802  C  CD2   . LEU G 1 54  ? 9.826   61.942  24.799  1.00 27.49 ?  54  LEU J CD2   1 
ATOM   7803  N  N     . GLN G 1 55  ? 14.213  61.540  28.075  1.00 27.66 ?  55  GLN J N     1 
ATOM   7804  C  CA    . GLN G 1 55  ? 15.095  60.860  29.013  1.00 32.34 ?  55  GLN J CA    1 
ATOM   7805  C  C     . GLN G 1 55  ? 14.405  60.678  30.365  1.00 31.66 ?  55  GLN J C     1 
ATOM   7806  O  O     . GLN G 1 55  ? 14.771  59.790  31.131  1.00 32.96 ?  55  GLN J O     1 
ATOM   7807  C  CB    . GLN G 1 55  ? 16.394  61.658  29.150  1.00 38.61 ?  55  GLN J CB    1 
ATOM   7808  C  CG    . GLN G 1 55  ? 17.526  60.921  29.861  1.00 44.39 ?  55  GLN J CG    1 
ATOM   7809  C  CD    . GLN G 1 55  ? 18.097  59.771  29.058  1.00 50.40 ?  55  GLN J CD    1 
ATOM   7810  O  OE1   . GLN G 1 55  ? 18.104  58.617  29.502  1.00 55.28 ?  55  GLN J OE1   1 
ATOM   7811  N  NE2   . GLN G 1 55  ? 18.594  60.076  27.868  1.00 50.06 ?  55  GLN J NE2   1 
ATOM   7812  N  N     . GLN G 1 56  ? 13.403  61.518  30.653  1.00 32.51 ?  56  GLN J N     1 
ATOM   7813  C  CA    . GLN G 1 56  ? 12.764  61.533  31.961  1.00 32.89 ?  56  GLN J CA    1 
ATOM   7814  C  C     . GLN G 1 56  ? 11.922  60.275  32.169  1.00 32.24 ?  56  GLN J C     1 
ATOM   7815  O  O     . GLN G 1 56  ? 11.645  59.905  33.307  1.00 31.60 ?  56  GLN J O     1 
ATOM   7816  C  CB    . GLN G 1 56  ? 11.869  62.760  32.140  1.00 31.33 ?  56  GLN J CB    1 
ATOM   7817  C  CG    . GLN G 1 56  ? 10.533  62.662  31.412  1.00 30.85 ?  56  GLN J CG    1 
ATOM   7818  C  CD    . GLN G 1 56  ? 9.742   63.953  31.435  1.00 28.41 ?  56  GLN J CD    1 
ATOM   7819  O  OE1   . GLN G 1 56  ? 8.672   64.046  32.046  1.00 29.41 ?  56  GLN J OE1   1 
ATOM   7820  N  NE2   . GLN G 1 56  ? 10.265  64.967  30.761  1.00 27.67 ?  56  GLN J NE2   1 
ATOM   7821  N  N     . PHE G 1 57  ? 11.510  59.623  31.075  1.00 32.33 ?  57  PHE J N     1 
ATOM   7822  C  CA    . PHE G 1 57  ? 10.603  58.490  31.178  1.00 33.65 ?  57  PHE J CA    1 
ATOM   7823  C  C     . PHE G 1 57  ? 11.398  57.208  31.420  1.00 31.25 ?  57  PHE J C     1 
ATOM   7824  O  O     . PHE G 1 57  ? 10.813  56.166  31.706  1.00 24.33 ?  57  PHE J O     1 
ATOM   7825  C  CB    . PHE G 1 57  ? 9.700   58.387  29.944  1.00 33.36 ?  57  PHE J CB    1 
ATOM   7826  C  CG    . PHE G 1 57  ? 8.783   59.591  29.775  1.00 36.14 ?  57  PHE J CG    1 
ATOM   7827  C  CD1   . PHE G 1 57  ? 7.619   59.713  30.526  1.00 33.27 ?  57  PHE J CD1   1 
ATOM   7828  C  CD2   . PHE G 1 57  ? 9.101   60.609  28.884  1.00 40.88 ?  57  PHE J CD2   1 
ATOM   7829  C  CE1   . PHE G 1 57  ? 6.796   60.819  30.382  1.00 31.59 ?  57  PHE J CE1   1 
ATOM   7830  C  CE2   . PHE G 1 57  ? 8.272   61.711  28.742  1.00 37.57 ?  57  PHE J CE2   1 
ATOM   7831  C  CZ    . PHE G 1 57  ? 7.123   61.813  29.489  1.00 34.45 ?  57  PHE J CZ    1 
ATOM   7832  N  N     . TYR G 1 58  ? 12.728  57.291  31.306  1.00 32.01 ?  58  TYR J N     1 
ATOM   7833  C  CA    . TYR G 1 58  ? 13.586  56.157  31.613  1.00 37.85 ?  58  TYR J CA    1 
ATOM   7834  C  C     . TYR G 1 58  ? 13.581  55.931  33.123  1.00 39.52 ?  58  TYR J C     1 
ATOM   7835  O  O     . TYR G 1 58  ? 13.240  56.828  33.891  1.00 44.20 ?  58  TYR J O     1 
ATOM   7836  C  CB    . TYR G 1 58  ? 15.040  56.317  31.151  1.00 36.99 ?  58  TYR J CB    1 
ATOM   7837  C  CG    . TYR G 1 58  ? 15.314  56.063  29.673  1.00 38.72 ?  58  TYR J CG    1 
ATOM   7838  C  CD1   . TYR G 1 58  ? 15.236  54.784  29.132  1.00 37.59 ?  58  TYR J CD1   1 
ATOM   7839  C  CD2   . TYR G 1 58  ? 15.708  57.096  28.831  1.00 37.05 ?  58  TYR J CD2   1 
ATOM   7840  C  CE1   . TYR G 1 58  ? 15.501  54.549  27.793  1.00 38.66 ?  58  TYR J CE1   1 
ATOM   7841  C  CE2   . TYR G 1 58  ? 15.979  56.873  27.492  1.00 40.17 ?  58  TYR J CE2   1 
ATOM   7842  C  CZ    . TYR G 1 58  ? 15.876  55.596  26.971  1.00 40.88 ?  58  TYR J CZ    1 
ATOM   7843  O  OH    . TYR G 1 58  ? 16.143  55.374  25.651  1.00 53.60 ?  58  TYR J OH    1 
ATOM   7844  N  N     . ALA G 1 59  ? 13.967  54.717  33.526  1.00 45.16 ?  59  ALA J N     1 
ATOM   7845  C  CA    . ALA G 1 59  ? 14.122  54.367  34.928  1.00 44.71 ?  59  ALA J CA    1 
ATOM   7846  C  C     . ALA G 1 59  ? 14.875  55.473  35.663  1.00 40.58 ?  59  ALA J C     1 
ATOM   7847  O  O     . ALA G 1 59  ? 15.924  55.920  35.206  1.00 34.82 ?  59  ALA J O     1 
ATOM   7848  C  CB    . ALA G 1 59  ? 14.853  53.046  35.035  1.00 48.65 ?  59  ALA J CB    1 
ATOM   7849  N  N     . GLN G 1 60  ? 14.332  55.908  36.806  1.00 44.51 ?  60  GLN J N     1 
ATOM   7850  C  CA    . GLN G 1 60  ? 14.995  56.904  37.632  1.00 49.22 ?  60  GLN J CA    1 
ATOM   7851  C  C     . GLN G 1 60  ? 15.093  56.393  39.068  1.00 56.61 ?  60  GLN J C     1 
ATOM   7852  O  O     . GLN G 1 60  ? 14.083  56.065  39.686  1.00 55.12 ?  60  GLN J O     1 
ATOM   7853  C  CB    . GLN G 1 60  ? 14.248  58.239  37.630  1.00 49.91 ?  60  GLN J CB    1 
ATOM   7854  C  CG    . GLN G 1 60  ? 13.697  58.656  36.269  1.00 52.14 ?  60  GLN J CG    1 
ATOM   7855  C  CD    . GLN G 1 60  ? 14.740  59.236  35.339  1.00 45.58 ?  60  GLN J CD    1 
ATOM   7856  O  OE1   . GLN G 1 60  ? 15.811  59.682  35.765  1.00 40.44 ?  60  GLN J OE1   1 
ATOM   7857  N  NE2   . GLN G 1 60  ? 14.421  59.259  34.053  1.00 44.04 ?  60  GLN J NE2   1 
ATOM   7858  N  N     . ASN G 1 61  ? 16.326  56.328  39.583  1.00 63.06 ?  61  ASN J N     1 
ATOM   7859  C  CA    . ASN G 1 61  ? 16.578  56.103  40.998  1.00 62.51 ?  61  ASN J CA    1 
ATOM   7860  C  C     . ASN G 1 61  ? 16.308  54.646  41.367  1.00 53.42 ?  61  ASN J C     1 
ATOM   7861  O  O     . ASN G 1 61  ? 15.447  54.364  42.198  1.00 49.19 ?  61  ASN J O     1 
ATOM   7862  C  CB    . ASN G 1 61  ? 15.753  57.041  41.874  1.00 66.03 ?  61  ASN J CB    1 
ATOM   7863  C  CG    . ASN G 1 61  ? 15.741  58.458  41.353  1.00 72.14 ?  61  ASN J CG    1 
ATOM   7864  O  OD1   . ASN G 1 61  ? 16.791  58.996  40.985  1.00 75.61 ?  61  ASN J OD1   1 
ATOM   7865  N  ND2   . ASN G 1 61  ? 14.568  59.073  41.301  1.00 73.94 ?  61  ASN J ND2   1 
ATOM   7866  N  N     . GLY G 1 62  ? 17.055  53.729  40.743  1.00 50.44 ?  62  GLY J N     1 
ATOM   7867  C  CA    . GLY G 1 62  ? 17.108  52.339  41.172  1.00 46.34 ?  62  GLY J CA    1 
ATOM   7868  C  C     . GLY G 1 62  ? 15.769  51.622  41.011  1.00 46.01 ?  62  GLY J C     1 
ATOM   7869  O  O     . GLY G 1 62  ? 15.563  50.553  41.582  1.00 45.13 ?  62  GLY J O     1 
ATOM   7870  N  N     . GLU G 1 63  ? 14.872  52.215  40.216  1.00 46.79 ?  63  GLU J N     1 
ATOM   7871  C  CA    . GLU G 1 63  ? 13.528  51.695  40.025  1.00 41.30 ?  63  GLU J CA    1 
ATOM   7872  C  C     . GLU G 1 63  ? 13.531  50.556  39.008  1.00 41.37 ?  63  GLU J C     1 
ATOM   7873  O  O     . GLU G 1 63  ? 14.273  50.593  38.029  1.00 46.42 ?  63  GLU J O     1 
ATOM   7874  C  CB    . GLU G 1 63  ? 12.625  52.838  39.563  1.00 46.69 ?  63  GLU J CB    1 
ATOM   7875  C  CG    . GLU G 1 63  ? 11.390  52.377  38.794  1.00 53.61 ?  63  GLU J CG    1 
ATOM   7876  C  CD    . GLU G 1 63  ? 10.541  53.522  38.273  1.00 60.15 ?  63  GLU J CD    1 
ATOM   7877  O  OE1   . GLU G 1 63  ? 10.992  54.683  38.378  1.00 65.30 ?  63  GLU J OE1   1 
ATOM   7878  O  OE2   . GLU G 1 63  ? 9.427   53.257  37.773  1.00 59.53 -1 63  GLU J OE2   1 
ATOM   7879  N  N     . VAL G 1 64  ? 12.681  49.551  39.257  1.00 34.77 ?  64  VAL J N     1 
ATOM   7880  C  CA    . VAL G 1 64  ? 12.470  48.455  38.326  1.00 37.23 ?  64  VAL J CA    1 
ATOM   7881  C  C     . VAL G 1 64  ? 11.310  48.821  37.403  1.00 36.53 ?  64  VAL J C     1 
ATOM   7882  O  O     . VAL G 1 64  ? 10.156  48.861  37.824  1.00 28.93 ?  64  VAL J O     1 
ATOM   7883  C  CB    . VAL G 1 64  ? 12.211  47.114  39.041  1.00 39.86 ?  64  VAL J CB    1 
ATOM   7884  C  CG1   . VAL G 1 64  ? 11.785  46.020  38.067  1.00 36.58 ?  64  VAL J CG1   1 
ATOM   7885  C  CG2   . VAL G 1 64  ? 13.418  46.662  39.854  1.00 38.54 ?  64  VAL J CG2   1 
ATOM   7886  N  N     . LYS G 1 65  ? 11.650  49.079  36.137  1.00 37.49 ?  65  LYS J N     1 
ATOM   7887  C  CA    . LYS G 1 65  ? 10.698  49.497  35.122  1.00 35.61 ?  65  LYS J CA    1 
ATOM   7888  C  C     . LYS G 1 65  ? 11.047  48.817  33.802  1.00 28.34 ?  65  LYS J C     1 
ATOM   7889  O  O     . LYS G 1 65  ? 12.146  48.993  33.279  1.00 22.86 ?  65  LYS J O     1 
ATOM   7890  C  CB    . LYS G 1 65  ? 10.748  51.020  34.946  1.00 43.06 ?  65  LYS J CB    1 
ATOM   7891  C  CG    . LYS G 1 65  ? 10.523  51.516  33.519  1.00 48.91 ?  65  LYS J CG    1 
ATOM   7892  C  CD    . LYS G 1 65  ? 9.086   51.870  33.156  1.00 55.45 ?  65  LYS J CD    1 
ATOM   7893  C  CE    . LYS G 1 65  ? 8.802   53.334  33.309  1.00 60.09 ?  65  LYS J CE    1 
ATOM   7894  N  NZ    . LYS G 1 65  ? 9.268   53.869  34.590  1.00 61.77 1  65  LYS J NZ    1 
ATOM   7895  N  N     . ASN G 1 66  ? 10.094  48.040  33.281  1.00 24.21 ?  66  ASN J N     1 
ATOM   7896  C  CA    . ASN G 1 66  ? 10.213  47.434  31.967  1.00 29.02 ?  66  ASN J CA    1 
ATOM   7897  C  C     . ASN G 1 66  ? 10.430  48.545  30.941  1.00 27.56 ?  66  ASN J C     1 
ATOM   7898  O  O     . ASN G 1 66  ? 9.720   49.547  30.959  1.00 31.94 ?  66  ASN J O     1 
ATOM   7899  C  CB    . ASN G 1 66  ? 8.979   46.594  31.656  1.00 26.49 ?  66  ASN J CB    1 
ATOM   7900  C  CG    . ASN G 1 66  ? 9.204   45.642  30.508  1.00 25.13 ?  66  ASN J CG    1 
ATOM   7901  O  OD1   . ASN G 1 66  ? 9.612   46.062  29.420  1.00 26.56 ?  66  ASN J OD1   1 
ATOM   7902  N  ND2   . ASN G 1 66  ? 8.949   44.361  30.730  1.00 24.73 ?  66  ASN J ND2   1 
ATOM   7903  N  N     . ARG G 1 67  ? 11.419  48.370  30.057  1.00 29.85 ?  67  ARG J N     1 
ATOM   7904  C  CA    . ARG G 1 67  ? 11.727  49.387  29.063  1.00 33.28 ?  67  ARG J CA    1 
ATOM   7905  C  C     . ARG G 1 67  ? 10.530  49.573  28.128  1.00 30.02 ?  67  ARG J C     1 
ATOM   7906  O  O     . ARG G 1 67  ? 10.368  50.639  27.539  1.00 27.42 ?  67  ARG J O     1 
ATOM   7907  C  CB    . ARG G 1 67  ? 13.029  49.094  28.305  1.00 33.65 ?  67  ARG J CB    1 
ATOM   7908  C  CG    . ARG G 1 67  ? 14.291  49.393  29.104  1.00 39.41 ?  67  ARG J CG    1 
ATOM   7909  C  CD    . ARG G 1 67  ? 15.471  49.791  28.223  1.00 40.69 ?  67  ARG J CD    1 
ATOM   7910  N  NE    . ARG G 1 67  ? 15.791  48.785  27.204  1.00 46.21 ?  67  ARG J NE    1 
ATOM   7911  C  CZ    . ARG G 1 67  ? 16.367  47.613  27.440  1.00 46.87 ?  67  ARG J CZ    1 
ATOM   7912  N  NH1   . ARG G 1 67  ? 16.765  47.302  28.662  1.00 47.61 1  67  ARG J NH1   1 
ATOM   7913  N  NH2   . ARG G 1 67  ? 16.558  46.763  26.447  1.00 44.84 ?  67  ARG J NH2   1 
ATOM   7914  N  N     . ARG G 1 68  ? 9.688   48.539  28.007  1.00 32.50 ?  68  ARG J N     1 
ATOM   7915  C  CA    . ARG G 1 68  ? 8.489   48.624  27.187  1.00 36.30 ?  68  ARG J CA    1 
ATOM   7916  C  C     . ARG G 1 68  ? 7.591   49.744  27.705  1.00 38.38 ?  68  ARG J C     1 
ATOM   7917  O  O     . ARG G 1 68  ? 6.991   50.480  26.925  1.00 35.59 ?  68  ARG J O     1 
ATOM   7918  C  CB    . ARG G 1 68  ? 7.708   47.306  27.188  1.00 38.32 ?  68  ARG J CB    1 
ATOM   7919  C  CG    . ARG G 1 68  ? 8.479   46.136  26.595  1.00 42.76 ?  68  ARG J CG    1 
ATOM   7920  C  CD    . ARG G 1 68  ? 7.610   44.906  26.404  1.00 45.70 ?  68  ARG J CD    1 
ATOM   7921  N  NE    . ARG G 1 68  ? 8.413   43.746  26.001  1.00 46.27 ?  68  ARG J NE    1 
ATOM   7922  C  CZ    . ARG G 1 68  ? 8.457   43.237  24.776  1.00 49.21 ?  68  ARG J CZ    1 
ATOM   7923  N  NH1   . ARG G 1 68  ? 7.784   43.809  23.793  1.00 51.36 1  68  ARG J NH1   1 
ATOM   7924  N  NH2   . ARG G 1 68  ? 9.189   42.164  24.537  1.00 50.58 ?  68  ARG J NH2   1 
ATOM   7925  N  N     . ASP G 1 69  ? 7.509   49.851  29.035  1.00 41.39 ?  69  ASP J N     1 
ATOM   7926  C  CA    . ASP G 1 69  ? 6.640   50.813  29.691  1.00 40.43 ?  69  ASP J CA    1 
ATOM   7927  C  C     . ASP G 1 69  ? 7.235   52.214  29.568  1.00 37.12 ?  69  ASP J C     1 
ATOM   7928  O  O     . ASP G 1 69  ? 6.511   53.206  29.621  1.00 35.48 ?  69  ASP J O     1 
ATOM   7929  C  CB    . ASP G 1 69  ? 6.378   50.408  31.133  1.00 42.66 ?  69  ASP J CB    1 
ATOM   7930  C  CG    . ASP G 1 69  ? 5.537   49.152  31.306  1.00 45.16 ?  69  ASP J CG    1 
ATOM   7931  O  OD1   . ASP G 1 69  ? 4.420   49.117  30.749  1.00 51.46 ?  69  ASP J OD1   1 
ATOM   7932  O  OD2   . ASP G 1 69  ? 6.004   48.221  31.997  1.00 43.49 -1 69  ASP J OD2   1 
ATOM   7933  N  N     . THR G 1 70  ? 8.560   52.279  29.402  1.00 30.09 ?  70  THR J N     1 
ATOM   7934  C  CA    . THR G 1 70  ? 9.260   53.539  29.219  1.00 28.57 ?  70  THR J CA    1 
ATOM   7935  C  C     . THR G 1 70  ? 8.947   54.089  27.830  1.00 30.35 ?  70  THR J C     1 
ATOM   7936  O  O     . THR G 1 70  ? 8.716   55.286  27.667  1.00 32.62 ?  70  THR J O     1 
ATOM   7937  C  CB    . THR G 1 70  ? 10.757  53.305  29.425  1.00 27.94 ?  70  THR J CB    1 
ATOM   7938  O  OG1   . THR G 1 70  ? 10.907  53.174  30.835  1.00 28.95 ?  70  THR J OG1   1 
ATOM   7939  C  CG2   . THR G 1 70  ? 11.622  54.442  28.911  1.00 26.97 ?  70  THR J CG2   1 
ATOM   7940  N  N     . TYR G 1 71  ? 8.933   53.191  26.839  1.00 29.15 ?  71  TYR J N     1 
ATOM   7941  C  CA    . TYR G 1 71  ? 8.703   53.560  25.452  1.00 28.99 ?  71  TYR J CA    1 
ATOM   7942  C  C     . TYR G 1 71  ? 7.237   53.950  25.269  1.00 32.18 ?  71  TYR J C     1 
ATOM   7943  O  O     . TYR G 1 71  ? 6.932   54.896  24.547  1.00 30.56 ?  71  TYR J O     1 
ATOM   7944  C  CB    . TYR G 1 71  ? 9.133   52.398  24.550  1.00 28.40 ?  71  TYR J CB    1 
ATOM   7945  C  CG    . TYR G 1 71  ? 10.583  51.966  24.729  1.00 27.11 ?  71  TYR J CG    1 
ATOM   7946  C  CD1   . TYR G 1 71  ? 11.593  52.900  24.926  1.00 26.95 ?  71  TYR J CD1   1 
ATOM   7947  C  CD2   . TYR G 1 71  ? 10.940  50.622  24.716  1.00 26.25 ?  71  TYR J CD2   1 
ATOM   7948  C  CE1   . TYR G 1 71  ? 12.912  52.514  25.095  1.00 28.03 ?  71  TYR J CE1   1 
ATOM   7949  C  CE2   . TYR G 1 71  ? 12.256  50.223  24.887  1.00 27.99 ?  71  TYR J CE2   1 
ATOM   7950  C  CZ    . TYR G 1 71  ? 13.245  51.171  25.076  1.00 29.07 ?  71  TYR J CZ    1 
ATOM   7951  O  OH    . TYR G 1 71  ? 14.544  50.787  25.245  1.00 33.45 ?  71  TYR J OH    1 
ATOM   7952  N  N     . GLU G 1 72  ? 6.341   53.214  25.936  1.00 31.95 ?  72  GLU J N     1 
ATOM   7953  C  CA    . GLU G 1 72  ? 4.914   53.487  25.872  1.00 32.54 ?  72  GLU J CA    1 
ATOM   7954  C  C     . GLU G 1 72  ? 4.668   54.945  26.255  1.00 31.29 ?  72  GLU J C     1 
ATOM   7955  O  O     . GLU G 1 72  ? 4.002   55.678  25.527  1.00 36.65 ?  72  GLU J O     1 
ATOM   7956  C  CB    . GLU G 1 72  ? 4.159   52.512  26.778  1.00 31.96 ?  72  GLU J CB    1 
ATOM   7957  C  CG    . GLU G 1 72  ? 2.642   52.680  26.753  1.00 34.64 ?  72  GLU J CG    1 
ATOM   7958  C  CD    . GLU G 1 72  ? 1.989   52.395  25.412  1.00 39.12 ?  72  GLU J CD    1 
ATOM   7959  O  OE1   . GLU G 1 72  ? 2.258   51.317  24.840  1.00 42.76 ?  72  GLU J OE1   1 
ATOM   7960  O  OE2   . GLU G 1 72  ? 1.199   53.243  24.947  1.00 43.37 -1 72  GLU J OE2   1 
ATOM   7961  N  N     . GLN G 1 73  ? 5.229   55.355  27.400  1.00 31.04 ?  73  GLN J N     1 
ATOM   7962  C  CA    . GLN G 1 73  ? 5.036   56.693  27.937  1.00 29.93 ?  73  GLN J CA    1 
ATOM   7963  C  C     . GLN G 1 73  ? 5.656   57.732  27.003  1.00 30.37 ?  73  GLN J C     1 
ATOM   7964  O  O     . GLN G 1 73  ? 5.115   58.825  26.847  1.00 33.80 ?  73  GLN J O     1 
ATOM   7965  C  CB    . GLN G 1 73  ? 5.643   56.817  29.336  1.00 29.13 ?  73  GLN J CB    1 
ATOM   7966  C  CG    . GLN G 1 73  ? 4.982   55.932  30.390  1.00 27.24 ?  73  GLN J CG    1 
ATOM   7967  C  CD    . GLN G 1 73  ? 5.772   55.846  31.679  1.00 25.68 ?  73  GLN J CD    1 
ATOM   7968  O  OE1   . GLN G 1 73  ? 6.880   56.381  31.797  1.00 22.14 ?  73  GLN J OE1   1 
ATOM   7969  N  NE2   . GLN G 1 73  ? 5.211   55.157  32.662  1.00 25.24 ?  73  GLN J NE2   1 
ATOM   7970  N  N     . MET G 1 74  ? 6.801   57.393  26.401  1.00 33.36 ?  74  MET J N     1 
ATOM   7971  C  CA    . MET G 1 74  ? 7.440   58.272  25.435  1.00 33.08 ?  74  MET J CA    1 
ATOM   7972  C  C     . MET G 1 74  ? 6.490   58.509  24.264  1.00 31.00 ?  74  MET J C     1 
ATOM   7973  O  O     . MET G 1 74  ? 6.230   59.651  23.891  1.00 32.26 ?  74  MET J O     1 
ATOM   7974  C  CB    . MET G 1 74  ? 8.750   57.677  24.905  1.00 37.58 ?  74  MET J CB    1 
ATOM   7975  C  CG    . MET G 1 74  ? 9.848   57.555  25.944  1.00 40.27 ?  74  MET J CG    1 
ATOM   7976  S  SD    . MET G 1 74  ? 11.365  56.850  25.269  1.00 45.86 ?  74  MET J SD    1 
ATOM   7977  C  CE    . MET G 1 74  ? 12.490  57.150  26.639  1.00 42.73 ?  74  MET J CE    1 
ATOM   7978  N  N     . VAL G 1 75  ? 5.978   57.414  23.692  1.00 30.86 ?  75  VAL J N     1 
ATOM   7979  C  CA    . VAL G 1 75  ? 5.104   57.481  22.531  1.00 30.24 ?  75  VAL J CA    1 
ATOM   7980  C  C     . VAL G 1 75  ? 3.899   58.355  22.869  1.00 29.89 ?  75  VAL J C     1 
ATOM   7981  O  O     . VAL G 1 75  ? 3.484   59.193  22.071  1.00 29.31 ?  75  VAL J O     1 
ATOM   7982  C  CB    . VAL G 1 75  ? 4.659   56.073  22.087  1.00 28.89 ?  75  VAL J CB    1 
ATOM   7983  C  CG1   . VAL G 1 75  ? 3.597   56.131  20.996  1.00 27.91 ?  75  VAL J CG1   1 
ATOM   7984  C  CG2   . VAL G 1 75  ? 5.835   55.213  21.640  1.00 30.35 ?  75  VAL J CG2   1 
ATOM   7985  N  N     . ASN G 1 76  ? 3.361   58.145  24.073  1.00 31.72 ?  76  ASN J N     1 
ATOM   7986  C  CA    . ASN G 1 76  ? 2.100   58.728  24.500  1.00 34.23 ?  76  ASN J CA    1 
ATOM   7987  C  C     . ASN G 1 76  ? 2.263   60.230  24.727  1.00 33.98 ?  76  ASN J C     1 
ATOM   7988  O  O     . ASN G 1 76  ? 1.375   61.009  24.386  1.00 33.23 ?  76  ASN J O     1 
ATOM   7989  C  CB    . ASN G 1 76  ? 1.579   58.020  25.745  1.00 40.45 ?  76  ASN J CB    1 
ATOM   7990  C  CG    . ASN G 1 76  ? 0.179   58.452  26.110  1.00 41.88 ?  76  ASN J CG    1 
ATOM   7991  O  OD1   . ASN G 1 76  ? -0.779  58.115  25.406  1.00 46.77 ?  76  ASN J OD1   1 
ATOM   7992  N  ND2   . ASN G 1 76  ? 0.039   59.184  27.205  1.00 46.22 ?  76  ASN J ND2   1 
ATOM   7993  N  N     . ALA G 1 77  ? 3.395   60.626  25.319  1.00 31.53 ?  77  ALA J N     1 
ATOM   7994  C  CA    . ALA G 1 77  ? 3.703   62.034  25.508  1.00 29.29 ?  77  ALA J CA    1 
ATOM   7995  C  C     . ALA G 1 77  ? 3.830   62.718  24.150  1.00 28.79 ?  77  ALA J C     1 
ATOM   7996  O  O     . ALA G 1 77  ? 3.386   63.852  23.982  1.00 27.79 ?  77  ALA J O     1 
ATOM   7997  C  CB    . ALA G 1 77  ? 4.967   62.196  26.326  1.00 27.24 ?  77  ALA J CB    1 
ATOM   7998  N  N     . ILE G 1 78  ? 4.442   62.022  23.185  1.00 26.88 ?  78  ILE J N     1 
ATOM   7999  C  CA    . ILE G 1 78  ? 4.612   62.571  21.849  1.00 28.83 ?  78  ILE J CA    1 
ATOM   8000  C  C     . ILE G 1 78  ? 3.232   62.782  21.227  1.00 26.21 ?  78  ILE J C     1 
ATOM   8001  O  O     . ILE G 1 78  ? 2.945   63.853  20.697  1.00 22.93 ?  78  ILE J O     1 
ATOM   8002  C  CB    . ILE G 1 78  ? 5.503   61.669  20.973  1.00 27.09 ?  78  ILE J CB    1 
ATOM   8003  C  CG1   . ILE G 1 78  ? 6.943   61.618  21.491  1.00 25.96 ?  78  ILE J CG1   1 
ATOM   8004  C  CG2   . ILE G 1 78  ? 5.454   62.115  19.510  1.00 26.88 ?  78  ILE J CG2   1 
ATOM   8005  C  CD1   . ILE G 1 78  ? 7.783   60.511  20.878  1.00 25.49 ?  78  ILE J CD1   1 
ATOM   8006  N  N     . LEU G 1 79  ? 2.380   61.755  21.310  1.00 25.39 ?  79  LEU J N     1 
ATOM   8007  C  CA    . LEU G 1 79  ? 1.072   61.792  20.674  1.00 27.95 ?  79  LEU J CA    1 
ATOM   8008  C  C     . LEU G 1 79  ? 0.207   62.882  21.308  1.00 26.68 ?  79  LEU J C     1 
ATOM   8009  O  O     . LEU G 1 79  ? -0.616  63.488  20.626  1.00 25.32 ?  79  LEU J O     1 
ATOM   8010  C  CB    . LEU G 1 79  ? 0.399   60.422  20.744  1.00 30.40 ?  79  LEU J CB    1 
ATOM   8011  C  CG    . LEU G 1 79  ? 0.664   59.480  19.564  1.00 32.08 ?  79  LEU J CG    1 
ATOM   8012  C  CD1   . LEU G 1 79  ? 0.002   59.998  18.296  1.00 35.61 ?  79  LEU J CD1   1 
ATOM   8013  C  CD2   . LEU G 1 79  ? 2.150   59.277  19.336  1.00 33.88 ?  79  LEU J CD2   1 
ATOM   8014  N  N     . ASP G 1 80  ? 0.400   63.128  22.610  1.00 25.46 ?  80  ASP J N     1 
ATOM   8015  C  CA    . ASP G 1 80  ? -0.392  64.112  23.332  1.00 24.09 ?  80  ASP J CA    1 
ATOM   8016  C  C     . ASP G 1 80  ? -0.236  65.489  22.692  1.00 22.28 ?  80  ASP J C     1 
ATOM   8017  O  O     . ASP G 1 80  ? -1.210  66.227  22.564  1.00 20.51 ?  80  ASP J O     1 
ATOM   8018  C  CB    . ASP G 1 80  ? -0.041  64.153  24.812  1.00 26.11 ?  80  ASP J CB    1 
ATOM   8019  C  CG    . ASP G 1 80  ? -0.776  63.153  25.694  1.00 25.68 ?  80  ASP J CG    1 
ATOM   8020  O  OD1   . ASP G 1 80  ? -1.583  62.370  25.151  1.00 25.35 ?  80  ASP J OD1   1 
ATOM   8021  O  OD2   . ASP G 1 80  ? -0.541  63.173  26.921  1.00 28.29 -1 80  ASP J OD2   1 
ATOM   8022  N  N     . ALA G 1 81  ? 0.996   65.835  22.302  1.00 20.62 ?  81  ALA J N     1 
ATOM   8023  C  CA    . ALA G 1 81  ? 1.266   67.131  21.703  1.00 18.29 ?  81  ALA J CA    1 
ATOM   8024  C  C     . ALA G 1 81  ? 0.671   67.192  20.296  1.00 18.72 ?  81  ALA J C     1 
ATOM   8025  O  O     . ALA G 1 81  ? 0.190   68.240  19.872  1.00 15.09 ?  81  ALA J O     1 
ATOM   8026  C  CB    . ALA G 1 81  ? 2.755   67.398  21.700  1.00 18.08 ?  81  ALA J CB    1 
ATOM   8027  N  N     . VAL G 1 82  ? 0.708   66.056  19.587  1.00 19.35 ?  82  VAL J N     1 
ATOM   8028  C  CA    . VAL G 1 82  ? 0.151   65.941  18.246  1.00 20.03 ?  82  VAL J CA    1 
ATOM   8029  C  C     . VAL G 1 82  ? -1.361  66.143  18.314  1.00 21.46 ?  82  VAL J C     1 
ATOM   8030  O  O     . VAL G 1 82  ? -1.920  66.927  17.550  1.00 19.93 ?  82  VAL J O     1 
ATOM   8031  C  CB    . VAL G 1 82  ? 0.489   64.585  17.591  1.00 22.21 ?  82  VAL J CB    1 
ATOM   8032  C  CG1   . VAL G 1 82  ? -0.239  64.391  16.264  1.00 19.91 ?  82  VAL J CG1   1 
ATOM   8033  C  CG2   . VAL G 1 82  ? 1.988   64.390  17.397  1.00 21.98 ?  82  VAL J CG2   1 
ATOM   8034  N  N     . ARG G 1 83  ? -2.011  65.417  19.232  1.00 23.77 ?  83  ARG J N     1 
ATOM   8035  C  CA    . ARG G 1 83  ? -3.462  65.407  19.343  1.00 24.66 ?  83  ARG J CA    1 
ATOM   8036  C  C     . ARG G 1 83  ? -3.969  66.770  19.813  1.00 28.23 ?  83  ARG J C     1 
ATOM   8037  O  O     . ARG G 1 83  ? -5.145  67.086  19.646  1.00 25.80 ?  83  ARG J O     1 
ATOM   8038  C  CB    . ARG G 1 83  ? -3.920  64.288  20.288  1.00 26.34 ?  83  ARG J CB    1 
ATOM   8039  C  CG    . ARG G 1 83  ? -3.790  62.886  19.707  1.00 27.79 ?  83  ARG J CG    1 
ATOM   8040  C  CD    . ARG G 1 83  ? -4.327  61.790  20.623  1.00 29.40 ?  83  ARG J CD    1 
ATOM   8041  N  NE    . ARG G 1 83  ? -3.504  61.575  21.819  1.00 29.96 ?  83  ARG J NE    1 
ATOM   8042  C  CZ    . ARG G 1 83  ? -2.976  60.413  22.193  1.00 32.87 ?  83  ARG J CZ    1 
ATOM   8043  N  NH1   . ARG G 1 83  ? -3.150  59.329  21.457  1.00 31.70 1  83  ARG J NH1   1 
ATOM   8044  N  NH2   . ARG G 1 83  ? -2.273  60.343  23.309  1.00 33.46 ?  83  ARG J NH2   1 
ATOM   8045  N  N     . ALA G 1 84  ? -3.073  67.565  20.407  1.00 27.45 ?  84  ALA J N     1 
ATOM   8046  C  CA    . ALA G 1 84  ? -3.412  68.901  20.872  1.00 28.02 ?  84  ALA J CA    1 
ATOM   8047  C  C     . ALA G 1 84  ? -3.385  69.886  19.706  1.00 26.91 ?  84  ALA J C     1 
ATOM   8048  O  O     . ALA G 1 84  ? -3.991  70.953  19.780  1.00 28.01 ?  84  ALA J O     1 
ATOM   8049  C  CB    . ALA G 1 84  ? -2.466  69.320  21.977  1.00 28.67 ?  84  ALA J CB    1 
ATOM   8050  N  N     . GLY G 1 85  ? -2.670  69.522  18.634  1.00 22.57 ?  85  GLY J N     1 
ATOM   8051  C  CA    . GLY G 1 85  ? -2.671  70.300  17.405  1.00 21.75 ?  85  GLY J CA    1 
ATOM   8052  C  C     . GLY G 1 85  ? -1.300  70.900  17.105  1.00 21.40 ?  85  GLY J C     1 
ATOM   8053  O  O     . GLY G 1 85  ? -1.158  71.702  16.184  1.00 18.90 ?  85  GLY J O     1 
ATOM   8054  N  N     . LYS G 1 86  ? -0.294  70.496  17.889  1.00 21.28 ?  86  LYS J N     1 
ATOM   8055  C  CA    . LYS G 1 86  ? 1.043   71.054  17.776  1.00 22.08 ?  86  LYS J CA    1 
ATOM   8056  C  C     . LYS G 1 86  ? 1.792   70.394  16.622  1.00 21.38 ?  86  LYS J C     1 
ATOM   8057  O  O     . LYS G 1 86  ? 1.720   69.181  16.440  1.00 17.41 ?  86  LYS J O     1 
ATOM   8058  C  CB    . LYS G 1 86  ? 1.834   70.859  19.075  1.00 24.27 ?  86  LYS J CB    1 
ATOM   8059  C  CG    . LYS G 1 86  ? 1.270   71.569  20.299  1.00 26.44 ?  86  LYS J CG    1 
ATOM   8060  C  CD    . LYS G 1 86  ? 2.258   71.646  21.457  1.00 30.05 ?  86  LYS J CD    1 
ATOM   8061  C  CE    . LYS G 1 86  ? 1.697   72.278  22.692  1.00 32.08 ?  86  LYS J CE    1 
ATOM   8062  N  NZ    . LYS G 1 86  ? 0.850   71.355  23.452  1.00 32.82 1  86  LYS J NZ    1 
ATOM   8063  N  N     . LYS G 1 87  ? 2.502   71.221  15.845  1.00 20.88 ?  87  LYS J N     1 
ATOM   8064  C  CA    . LYS G 1 87  ? 3.476   70.735  14.883  1.00 20.25 ?  87  LYS J CA    1 
ATOM   8065  C  C     . LYS G 1 87  ? 4.651   70.156  15.668  1.00 19.94 ?  87  LYS J C     1 
ATOM   8066  O  O     . LYS G 1 87  ? 5.504   70.895  16.156  1.00 18.94 ?  87  LYS J O     1 
ATOM   8067  C  CB    . LYS G 1 87  ? 3.875   71.858  13.916  1.00 19.44 ?  87  LYS J CB    1 
ATOM   8068  C  CG    . LYS G 1 87  ? 4.900   71.465  12.856  1.00 20.79 ?  87  LYS J CG    1 
ATOM   8069  C  CD    . LYS G 1 87  ? 5.109   72.466  11.725  1.00 20.88 ?  87  LYS J CD    1 
ATOM   8070  C  CE    . LYS G 1 87  ? 5.669   73.779  12.169  1.00 22.92 ?  87  LYS J CE    1 
ATOM   8071  N  NZ    . LYS G 1 87  ? 5.907   74.658  11.021  1.00 23.67 1  87  LYS J NZ    1 
ATOM   8072  N  N     . THR G 1 88  ? 4.668   68.824  15.791  1.00 21.81 ?  88  THR J N     1 
ATOM   8073  C  CA    . THR G 1 88  ? 5.541   68.133  16.728  1.00 21.15 ?  88  THR J CA    1 
ATOM   8074  C  C     . THR G 1 88  ? 6.720   67.517  15.981  1.00 22.72 ?  88  THR J C     1 
ATOM   8075  O  O     . THR G 1 88  ? 6.565   67.019  14.869  1.00 25.13 ?  88  THR J O     1 
ATOM   8076  C  CB    . THR G 1 88  ? 4.736   67.064  17.466  1.00 20.16 ?  88  THR J CB    1 
ATOM   8077  O  OG1   . THR G 1 88  ? 3.516   67.690  17.850  1.00 17.81 ?  88  THR J OG1   1 
ATOM   8078  C  CG2   . THR G 1 88  ? 5.466   66.524  18.682  1.00 19.99 ?  88  THR J CG2   1 
ATOM   8079  N  N     . VAL G 1 89  ? 7.896   67.548  16.619  1.00 23.69 ?  89  VAL J N     1 
ATOM   8080  C  CA    . VAL G 1 89  ? 9.098   66.947  16.064  1.00 24.64 ?  89  VAL J CA    1 
ATOM   8081  C  C     . VAL G 1 89  ? 9.780   66.113  17.148  1.00 23.74 ?  89  VAL J C     1 
ATOM   8082  O  O     . VAL G 1 89  ? 10.016  66.594  18.254  1.00 23.41 ?  89  VAL J O     1 
ATOM   8083  C  CB    . VAL G 1 89  ? 10.026  68.035  15.485  1.00 23.69 ?  89  VAL J CB    1 
ATOM   8084  C  CG1   . VAL G 1 89  ? 11.437  67.525  15.213  1.00 25.07 ?  89  VAL J CG1   1 
ATOM   8085  C  CG2   . VAL G 1 89  ? 9.436   68.653  14.223  1.00 24.91 ?  89  VAL J CG2   1 
ATOM   8086  N  N     . CYS G 1 90  ? 10.062  64.846  16.817  1.00 23.32 ?  90  CYS J N     1 
ATOM   8087  C  CA    . CYS G 1 90  ? 10.781  63.941  17.700  1.00 23.85 ?  90  CYS J CA    1 
ATOM   8088  C  C     . CYS G 1 90  ? 12.234  63.843  17.240  1.00 23.00 ?  90  CYS J C     1 
ATOM   8089  O  O     . CYS G 1 90  ? 12.516  63.303  16.172  1.00 30.47 ?  90  CYS J O     1 
ATOM   8090  C  CB    . CYS G 1 90  ? 10.116  62.567  17.738  1.00 24.76 ?  90  CYS J CB    1 
ATOM   8091  S  SG    . CYS G 1 90  ? 11.011  61.336  18.723  1.00 26.52 ?  90  CYS J SG    1 
ATOM   8092  N  N     . ALA G 1 91  ? 13.141  64.387  18.058  1.00 19.94 ?  91  ALA J N     1 
ATOM   8093  C  CA    . ALA G 1 91  ? 14.560  64.428  17.747  1.00 19.21 ?  91  ALA J CA    1 
ATOM   8094  C  C     . ALA G 1 91  ? 15.301  63.353  18.539  1.00 21.06 ?  91  ALA J C     1 
ATOM   8095  O  O     . ALA G 1 91  ? 15.606  63.546  19.714  1.00 22.17 ?  91  ALA J O     1 
ATOM   8096  C  CB    . ALA G 1 91  ? 15.103  65.809  18.047  1.00 19.28 ?  91  ALA J CB    1 
ATOM   8097  N  N     . LEU G 1 92  ? 15.578  62.220  17.881  1.00 22.86 ?  92  LEU J N     1 
ATOM   8098  C  CA    . LEU G 1 92  ? 16.357  61.144  18.471  1.00 24.12 ?  92  LEU J CA    1 
ATOM   8099  C  C     . LEU G 1 92  ? 17.785  61.218  17.938  1.00 23.11 ?  92  LEU J C     1 
ATOM   8100  O  O     . LEU G 1 92  ? 18.030  61.831  16.901  1.00 22.93 ?  92  LEU J O     1 
ATOM   8101  C  CB    . LEU G 1 92  ? 15.728  59.786  18.160  1.00 26.01 ?  92  LEU J CB    1 
ATOM   8102  C  CG    . LEU G 1 92  ? 14.274  59.594  18.602  1.00 27.68 ?  92  LEU J CG    1 
ATOM   8103  C  CD1   . LEU G 1 92  ? 13.808  58.194  18.249  1.00 28.44 ?  92  LEU J CD1   1 
ATOM   8104  C  CD2   . LEU G 1 92  ? 14.090  59.859  20.086  1.00 27.73 ?  92  LEU J CD2   1 
ATOM   8105  N  N     . TYR G 1 93  ? 18.718  60.580  18.655  1.00 18.11 ?  93  TYR J N     1 
ATOM   8106  C  CA    . TYR G 1 93  ? 20.112  60.563  18.244  1.00 20.10 ?  93  TYR J CA    1 
ATOM   8107  C  C     . TYR G 1 93  ? 20.276  59.518  17.145  1.00 18.97 ?  93  TYR J C     1 
ATOM   8108  O  O     . TYR G 1 93  ? 19.585  58.501  17.133  1.00 19.31 ?  93  TYR J O     1 
ATOM   8109  C  CB    . TYR G 1 93  ? 21.071  60.308  19.414  1.00 20.14 ?  93  TYR J CB    1 
ATOM   8110  C  CG    . TYR G 1 93  ? 21.143  58.870  19.913  1.00 19.29 ?  93  TYR J CG    1 
ATOM   8111  C  CD1   . TYR G 1 93  ? 22.031  57.959  19.354  1.00 21.40 ?  93  TYR J CD1   1 
ATOM   8112  C  CD2   . TYR G 1 93  ? 20.339  58.433  20.958  1.00 20.59 ?  93  TYR J CD2   1 
ATOM   8113  C  CE1   . TYR G 1 93  ? 22.107  56.653  19.808  1.00 20.58 ?  93  TYR J CE1   1 
ATOM   8114  C  CE2   . TYR G 1 93  ? 20.403  57.129  21.420  1.00 20.49 ?  93  TYR J CE2   1 
ATOM   8115  C  CZ    . TYR G 1 93  ? 21.290  56.237  20.845  1.00 20.12 ?  93  TYR J CZ    1 
ATOM   8116  O  OH    . TYR G 1 93  ? 21.353  54.954  21.304  1.00 26.35 ?  93  TYR J OH    1 
ATOM   8117  N  N     . GLY G 1 94  ? 21.200  59.800  16.221  1.00 17.04 ?  94  GLY J N     1 
ATOM   8118  C  CA    . GLY G 1 94  ? 21.423  58.957  15.061  1.00 17.90 ?  94  GLY J CA    1 
ATOM   8119  C  C     . GLY G 1 94  ? 20.198  58.923  14.153  1.00 17.60 ?  94  GLY J C     1 
ATOM   8120  O  O     . GLY G 1 94  ? 19.579  59.952  13.885  1.00 18.56 ?  94  GLY J O     1 
ATOM   8121  N  N     . HIS G 1 95  ? 19.867  57.716  13.690  1.00 15.14 ?  95  HIS J N     1 
ATOM   8122  C  CA    . HIS G 1 95  ? 18.743  57.494  12.798  1.00 15.58 ?  95  HIS J CA    1 
ATOM   8123  C  C     . HIS G 1 95  ? 17.515  57.190  13.654  1.00 15.36 ?  95  HIS J C     1 
ATOM   8124  O  O     . HIS G 1 95  ? 17.551  56.308  14.509  1.00 17.68 ?  95  HIS J O     1 
ATOM   8125  C  CB    . HIS G 1 95  ? 19.118  56.402  11.788  1.00 13.93 ?  95  HIS J CB    1 
ATOM   8126  C  CG    . HIS G 1 95  ? 18.090  56.114  10.748  1.00 12.55 ?  95  HIS J CG    1 
ATOM   8127  N  ND1   . HIS G 1 95  ? 16.756  55.925  11.030  1.00 12.14 ?  95  HIS J ND1   1 
ATOM   8128  C  CD2   . HIS G 1 95  ? 18.220  55.940  9.426   1.00 11.59 ?  95  HIS J CD2   1 
ATOM   8129  C  CE1   . HIS G 1 95  ? 16.106  55.666  9.903   1.00 11.98 ?  95  HIS J CE1   1 
ATOM   8130  N  NE2   . HIS G 1 95  ? 16.976  55.672  8.917   1.00 11.34 ?  95  HIS J NE2   1 
ATOM   8131  N  N     . PRO G 1 96  ? 16.397  57.928  13.472  1.00 14.72 ?  96  PRO J N     1 
ATOM   8132  C  CA    . PRO G 1 96  ? 15.241  57.790  14.362  1.00 15.45 ?  96  PRO J CA    1 
ATOM   8133  C  C     . PRO G 1 96  ? 14.551  56.427  14.340  1.00 14.61 ?  96  PRO J C     1 
ATOM   8134  O  O     . PRO G 1 96  ? 13.814  56.099  15.267  1.00 15.14 ?  96  PRO J O     1 
ATOM   8135  C  CB    . PRO G 1 96  ? 14.305  58.920  13.887  1.00 14.91 ?  96  PRO J CB    1 
ATOM   8136  C  CG    . PRO G 1 96  ? 14.702  59.160  12.446  1.00 13.99 ?  96  PRO J CG    1 
ATOM   8137  C  CD    . PRO G 1 96  ? 16.201  58.937  12.418  1.00 13.96 ?  96  PRO J CD    1 
ATOM   8138  N  N     . GLY G 1 97  ? 14.797  55.637  13.288  1.00 14.20 ?  97  GLY J N     1 
ATOM   8139  C  CA    . GLY G 1 97  ? 14.103  54.371  13.111  1.00 16.16 ?  97  GLY J CA    1 
ATOM   8140  C  C     . GLY G 1 97  ? 15.039  53.168  13.225  1.00 18.11 ?  97  GLY J C     1 
ATOM   8141  O  O     . GLY G 1 97  ? 14.605  52.030  13.067  1.00 18.08 ?  97  GLY J O     1 
ATOM   8142  N  N     . VAL G 1 98  ? 16.319  53.428  13.508  1.00 19.41 ?  98  VAL J N     1 
ATOM   8143  C  CA    . VAL G 1 98  ? 17.318  52.374  13.569  1.00 23.43 ?  98  VAL J CA    1 
ATOM   8144  C  C     . VAL G 1 98  ? 17.462  51.922  15.018  1.00 24.81 ?  98  VAL J C     1 
ATOM   8145  O  O     . VAL G 1 98  ? 17.950  52.669  15.863  1.00 21.36 ?  98  VAL J O     1 
ATOM   8146  C  CB    . VAL G 1 98  ? 18.660  52.840  12.969  1.00 23.47 ?  98  VAL J CB    1 
ATOM   8147  C  CG1   . VAL G 1 98  ? 19.829  51.964  13.404  1.00 24.28 ?  98  VAL J CG1   1 
ATOM   8148  C  CG2   . VAL G 1 98  ? 18.590  52.923  11.449  1.00 21.73 ?  98  VAL J CG2   1 
ATOM   8149  N  N     . PHE G 1 99  ? 17.013  50.693  15.293  1.00 29.38 ?  99  PHE J N     1 
ATOM   8150  C  CA    . PHE G 1 99  ? 16.969  50.193  16.655  1.00 31.94 ?  99  PHE J CA    1 
ATOM   8151  C  C     . PHE G 1 99  ? 16.384  51.288  17.544  1.00 33.55 ?  99  PHE J C     1 
ATOM   8152  O  O     . PHE G 1 99  ? 16.978  51.672  18.549  1.00 30.84 ?  99  PHE J O     1 
ATOM   8153  C  CB    . PHE G 1 99  ? 18.378  49.736  17.048  1.00 33.74 ?  99  PHE J CB    1 
ATOM   8154  C  CG    . PHE G 1 99  ? 18.833  48.441  16.387  1.00 35.55 ?  99  PHE J CG    1 
ATOM   8155  C  CD1   . PHE G 1 99  ? 19.313  48.428  15.081  1.00 35.61 ?  99  PHE J CD1   1 
ATOM   8156  C  CD2   . PHE G 1 99  ? 18.792  47.237  17.082  1.00 38.13 ?  99  PHE J CD2   1 
ATOM   8157  C  CE1   . PHE G 1 99  ? 19.728  47.245  14.490  1.00 37.60 ?  99  PHE J CE1   1 
ATOM   8158  C  CE2   . PHE G 1 99  ? 19.210  46.058  16.486  1.00 40.14 ?  99  PHE J CE2   1 
ATOM   8159  C  CZ    . PHE G 1 99  ? 19.677  46.064  15.192  1.00 37.59 ?  99  PHE J CZ    1 
ATOM   8160  N  N     . ALA G 1 100 ? 15.217  51.796  17.131  1.00 33.35 ?  100 ALA J N     1 
ATOM   8161  C  CA    . ALA G 1 100 ? 14.461  52.772  17.900  1.00 31.20 ?  100 ALA J CA    1 
ATOM   8162  C  C     . ALA G 1 100 ? 12.971  52.576  17.631  1.00 36.66 ?  100 ALA J C     1 
ATOM   8163  O  O     . ALA G 1 100 ? 12.476  52.926  16.562  1.00 40.84 ?  100 ALA J O     1 
ATOM   8164  C  CB    . ALA G 1 100 ? 14.907  54.176  17.554  1.00 29.19 ?  100 ALA J CB    1 
ATOM   8165  N  N     . CYS G 1 101 ? 12.269  52.013  18.620  1.00 35.57 ?  101 CYS J N     1 
ATOM   8166  C  CA    . CYS G 1 101 ? 10.874  51.633  18.461  1.00 36.98 ?  101 CYS J CA    1 
ATOM   8167  C  C     . CYS G 1 101 ? 9.950   52.820  18.727  1.00 33.52 ?  101 CYS J C     1 
ATOM   8168  O  O     . CYS G 1 101 ? 8.830   52.857  18.223  1.00 30.09 ?  101 CYS J O     1 
ATOM   8169  C  CB    . CYS G 1 101 ? 10.515  50.476  19.385  1.00 37.09 ?  101 CYS J CB    1 
ATOM   8170  S  SG    . CYS G 1 101 ? 10.618  50.897  21.144  1.00 40.44 ?  101 CYS J SG    1 
ATOM   8171  N  N     . VAL G 1 102 ? 10.420  53.786  19.523  1.00 31.96 ?  102 VAL J N     1 
ATOM   8172  C  CA    . VAL G 1 102 ? 9.595   54.918  19.916  1.00 25.71 ?  102 VAL J CA    1 
ATOM   8173  C  C     . VAL G 1 102 ? 8.990   55.562  18.671  1.00 24.25 ?  102 VAL J C     1 
ATOM   8174  O  O     . VAL G 1 102 ? 7.771   55.671  18.559  1.00 21.86 ?  102 VAL J O     1 
ATOM   8175  C  CB    . VAL G 1 102 ? 10.389  55.947  20.744  1.00 25.54 ?  102 VAL J CB    1 
ATOM   8176  C  CG1   . VAL G 1 102 ? 9.651   57.277  20.862  1.00 26.13 ?  102 VAL J CG1   1 
ATOM   8177  C  CG2   . VAL G 1 102 ? 10.743  55.395  22.118  1.00 24.91 ?  102 VAL J CG2   1 
ATOM   8178  N  N     . SER G 1 103 ? 9.854   55.986  17.743  1.00 21.53 ?  103 SER J N     1 
ATOM   8179  C  CA    . SER G 1 103 ? 9.415   56.715  16.565  1.00 25.28 ?  103 SER J CA    1 
ATOM   8180  C  C     . SER G 1 103 ? 8.436   55.881  15.740  1.00 24.29 ?  103 SER J C     1 
ATOM   8181  O  O     . SER G 1 103 ? 7.379   56.379  15.361  1.00 26.55 ?  103 SER J O     1 
ATOM   8182  C  CB    . SER G 1 103 ? 10.585  57.180  15.733  1.00 27.24 ?  103 SER J CB    1 
ATOM   8183  O  OG    . SER G 1 103 ? 11.146  58.370  16.272  1.00 29.28 ?  103 SER J OG    1 
ATOM   8184  N  N     . HIS G 1 104 ? 8.789   54.622  15.453  1.00 21.35 ?  104 HIS J N     1 
ATOM   8185  C  CA    . HIS G 1 104 ? 7.944   53.784  14.617  1.00 22.42 ?  104 HIS J CA    1 
ATOM   8186  C  C     . HIS G 1 104 ? 6.557   53.677  15.250  1.00 23.31 ?  104 HIS J C     1 
ATOM   8187  O  O     . HIS G 1 104 ? 5.548   53.721  14.551  1.00 24.50 ?  104 HIS J O     1 
ATOM   8188  C  CB    . HIS G 1 104 ? 8.596   52.422  14.341  1.00 20.95 ?  104 HIS J CB    1 
ATOM   8189  C  CG    . HIS G 1 104 ? 9.691   52.465  13.321  1.00 18.88 ?  104 HIS J CG    1 
ATOM   8190  N  ND1   . HIS G 1 104 ? 9.452   52.528  11.965  1.00 15.31 ?  104 HIS J ND1   1 
ATOM   8191  C  CD2   . HIS G 1 104 ? 11.023  52.466  13.460  1.00 16.47 ?  104 HIS J CD2   1 
ATOM   8192  C  CE1   . HIS G 1 104 ? 10.608  52.564  11.317  1.00 16.89 ?  104 HIS J CE1   1 
ATOM   8193  N  NE2   . HIS G 1 104 ? 11.575  52.526  12.206  1.00 16.83 ?  104 HIS J NE2   1 
ATOM   8194  N  N     . MET G 1 105 ? 6.522   53.552  16.581  1.00 25.11 ?  105 MET J N     1 
ATOM   8195  C  CA    . MET G 1 105 ? 5.275   53.396  17.312  1.00 26.13 ?  105 MET J CA    1 
ATOM   8196  C  C     . MET G 1 105 ? 4.474   54.694  17.266  1.00 25.52 ?  105 MET J C     1 
ATOM   8197  O  O     . MET G 1 105 ? 3.249   54.665  17.154  1.00 24.52 ?  105 MET J O     1 
ATOM   8198  C  CB    . MET G 1 105 ? 5.532   53.027  18.777  1.00 29.10 ?  105 MET J CB    1 
ATOM   8199  C  CG    . MET G 1 105 ? 6.259   51.711  18.966  1.00 32.05 ?  105 MET J CG    1 
ATOM   8200  S  SD    . MET G 1 105 ? 6.895   51.502  20.641  1.00 34.70 ?  105 MET J SD    1 
ATOM   8201  C  CE    . MET G 1 105 ? 5.373   51.126  21.522  1.00 36.95 ?  105 MET J CE    1 
ATOM   8202  N  N     . ALA G 1 106 ? 5.172   55.831  17.365  1.00 22.13 ?  106 ALA J N     1 
ATOM   8203  C  CA    . ALA G 1 106 ? 4.505   57.121  17.407  1.00 24.83 ?  106 ALA J CA    1 
ATOM   8204  C  C     . ALA G 1 106 ? 3.954   57.467  16.025  1.00 27.80 ?  106 ALA J C     1 
ATOM   8205  O  O     . ALA G 1 106 ? 2.858   58.011  15.918  1.00 28.43 ?  106 ALA J O     1 
ATOM   8206  C  CB    . ALA G 1 106 ? 5.445   58.190  17.924  1.00 22.68 ?  106 ALA J CB    1 
ATOM   8207  N  N     . ILE G 1 107 ? 4.715   57.144  14.972  1.00 27.15 ?  107 ILE J N     1 
ATOM   8208  C  CA    . ILE G 1 107 ? 4.261   57.388  13.611  1.00 25.28 ?  107 ILE J CA    1 
ATOM   8209  C  C     . ILE G 1 107 ? 3.042   56.511  13.333  1.00 26.92 ?  107 ILE J C     1 
ATOM   8210  O  O     . ILE G 1 107 ? 2.024   56.997  12.845  1.00 25.34 ?  107 ILE J O     1 
ATOM   8211  C  CB    . ILE G 1 107 ? 5.382   57.156  12.580  1.00 24.37 ?  107 ILE J CB    1 
ATOM   8212  C  CG1   . ILE G 1 107 ? 6.548   58.130  12.783  1.00 22.77 ?  107 ILE J CG1   1 
ATOM   8213  C  CG2   . ILE G 1 107 ? 4.826   57.234  11.157  1.00 25.54 ?  107 ILE J CG2   1 
ATOM   8214  C  CD1   . ILE G 1 107 ? 7.680   57.971  11.783  1.00 20.96 ?  107 ILE J CD1   1 
ATOM   8215  N  N     . THR G 1 108 ? 3.155   55.217  13.653  1.00 27.27 ?  108 THR J N     1 
ATOM   8216  C  CA    . THR G 1 108 ? 2.072   54.271  13.434  1.00 29.67 ?  108 THR J CA    1 
ATOM   8217  C  C     . THR G 1 108 ? 0.797   54.797  14.089  1.00 30.43 ?  108 THR J C     1 
ATOM   8218  O  O     . THR G 1 108 ? -0.239  54.918  13.439  1.00 29.37 ?  108 THR J O     1 
ATOM   8219  C  CB    . THR G 1 108 ? 2.453   52.902  13.997  1.00 31.20 ?  108 THR J CB    1 
ATOM   8220  O  OG1   . THR G 1 108 ? 3.633   52.506  13.305  1.00 29.89 ?  108 THR J OG1   1 
ATOM   8221  C  CG2   . THR G 1 108 ? 1.362   51.864  13.797  1.00 32.44 ?  108 THR J CG2   1 
ATOM   8222  N  N     . ARG G 1 109 ? 0.891   55.102  15.387  1.00 34.09 ?  109 ARG J N     1 
ATOM   8223  C  CA    . ARG G 1 109 ? -0.267  55.476  16.181  1.00 33.89 ?  109 ARG J CA    1 
ATOM   8224  C  C     . ARG G 1 109 ? -0.879  56.761  15.629  1.00 30.79 ?  109 ARG J C     1 
ATOM   8225  O  O     . ARG G 1 109 ? -2.099  56.918  15.616  1.00 28.29 ?  109 ARG J O     1 
ATOM   8226  C  CB    . ARG G 1 109 ? 0.147   55.631  17.648  1.00 38.27 ?  109 ARG J CB    1 
ATOM   8227  C  CG    . ARG G 1 109 ? -1.022  55.676  18.621  1.00 42.46 ?  109 ARG J CG    1 
ATOM   8228  C  CD    . ARG G 1 109 ? -0.565  55.608  20.069  1.00 46.06 ?  109 ARG J CD    1 
ATOM   8229  N  NE    . ARG G 1 109 ? 0.223   54.397  20.325  1.00 46.04 ?  109 ARG J NE    1 
ATOM   8230  C  CZ    . ARG G 1 109 ? 0.624   53.986  21.521  1.00 51.80 ?  109 ARG J CZ    1 
ATOM   8231  N  NH1   . ARG G 1 109 ? 0.290   54.665  22.604  1.00 51.92 1  109 ARG J NH1   1 
ATOM   8232  N  NH2   . ARG G 1 109 ? 1.351   52.888  21.628  1.00 57.04 ?  109 ARG J NH2   1 
ATOM   8233  N  N     . ALA G 1 110 ? -0.013  57.673  15.174  1.00 28.07 ?  110 ALA J N     1 
ATOM   8234  C  CA    . ALA G 1 110 ? -0.434  58.963  14.655  1.00 28.13 ?  110 ALA J CA    1 
ATOM   8235  C  C     . ALA G 1 110 ? -1.275  58.773  13.395  1.00 32.50 ?  110 ALA J C     1 
ATOM   8236  O  O     . ALA G 1 110 ? -2.328  59.388  13.247  1.00 34.77 ?  110 ALA J O     1 
ATOM   8237  C  CB    . ALA G 1 110 ? 0.780   59.824  14.381  1.00 27.84 ?  110 ALA J CB    1 
ATOM   8238  N  N     . LYS G 1 111 ? -0.787  57.916  12.491  1.00 34.50 ?  111 LYS J N     1 
ATOM   8239  C  CA    . LYS G 1 111 ? -1.444  57.667  11.219  1.00 38.05 ?  111 LYS J CA    1 
ATOM   8240  C  C     . LYS G 1 111 ? -2.845  57.109  11.454  1.00 36.97 ?  111 LYS J C     1 
ATOM   8241  O  O     . LYS G 1 111 ? -3.793  57.502  10.778  1.00 36.55 ?  111 LYS J O     1 
ATOM   8242  C  CB    . LYS G 1 111 ? -0.626  56.687  10.370  1.00 39.87 ?  111 LYS J CB    1 
ATOM   8243  C  CG    . LYS G 1 111 ? 0.472   57.314  9.522   1.00 43.74 ?  111 LYS J CG    1 
ATOM   8244  C  CD    . LYS G 1 111 ? 1.442   56.296  8.934   1.00 46.35 ?  111 LYS J CD    1 
ATOM   8245  C  CE    . LYS G 1 111 ? 2.101   56.782  7.684   1.00 46.02 ?  111 LYS J CE    1 
ATOM   8246  N  NZ    . LYS G 1 111 ? 2.652   58.130  7.842   1.00 48.97 1  111 LYS J NZ    1 
ATOM   8247  N  N     . ALA G 1 112 ? -2.957  56.187  12.414  1.00 33.02 ?  112 ALA J N     1 
ATOM   8248  C  CA    . ALA G 1 112 ? -4.212  55.505  12.682  1.00 32.42 ?  112 ALA J CA    1 
ATOM   8249  C  C     . ALA G 1 112 ? -5.245  56.482  13.242  1.00 31.86 ?  112 ALA J C     1 
ATOM   8250  O  O     . ALA G 1 112 ? -6.441  56.301  13.029  1.00 35.26 ?  112 ALA J O     1 
ATOM   8251  C  CB    . ALA G 1 112 ? -3.977  54.340  13.619  1.00 33.27 ?  112 ALA J CB    1 
ATOM   8252  N  N     . GLU G 1 113 ? -4.783  57.517  13.954  1.00 29.03 ?  113 GLU J N     1 
ATOM   8253  C  CA    . GLU G 1 113 ? -5.688  58.501  14.531  1.00 29.62 ?  113 GLU J CA    1 
ATOM   8254  C  C     . GLU G 1 113 ? -5.941  59.627  13.529  1.00 28.07 ?  113 GLU J C     1 
ATOM   8255  O  O     . GLU G 1 113 ? -6.704  60.549  13.811  1.00 28.77 ?  113 GLU J O     1 
ATOM   8256  C  CB    . GLU G 1 113 ? -5.163  59.012  15.874  1.00 32.04 ?  113 GLU J CB    1 
ATOM   8257  C  CG    . GLU G 1 113 ? -5.185  57.938  16.958  1.00 34.21 ?  113 GLU J CG    1 
ATOM   8258  C  CD    . GLU G 1 113 ? -4.573  58.332  18.290  1.00 38.58 ?  113 GLU J CD    1 
ATOM   8259  O  OE1   . GLU G 1 113 ? -4.155  59.500  18.436  1.00 42.30 ?  113 GLU J OE1   1 
ATOM   8260  O  OE2   . GLU G 1 113 ? -4.513  57.461  19.183  1.00 43.44 -1 113 GLU J OE2   1 
ATOM   8261  N  N     . GLY G 1 114 ? -5.298  59.542  12.359  1.00 26.24 ?  114 GLY J N     1 
ATOM   8262  C  CA    . GLY G 1 114 ? -5.593  60.436  11.251  1.00 24.74 ?  114 GLY J CA    1 
ATOM   8263  C  C     . GLY G 1 114 ? -4.681  61.661  11.217  1.00 23.30 ?  114 GLY J C     1 
ATOM   8264  O  O     . GLY G 1 114 ? -5.071  62.702  10.692  1.00 24.59 ?  114 GLY J O     1 
ATOM   8265  N  N     . PHE G 1 115 ? -3.465  61.539  11.760  1.00 19.65 ?  115 PHE J N     1 
ATOM   8266  C  CA    . PHE G 1 115 ? -2.530  62.653  11.739  1.00 20.23 ?  115 PHE J CA    1 
ATOM   8267  C  C     . PHE G 1 115 ? -1.433  62.392  10.710  1.00 21.08 ?  115 PHE J C     1 
ATOM   8268  O  O     . PHE G 1 115 ? -1.144  61.249  10.364  1.00 24.98 ?  115 PHE J O     1 
ATOM   8269  C  CB    . PHE G 1 115 ? -1.929  62.928  13.121  1.00 19.05 ?  115 PHE J CB    1 
ATOM   8270  C  CG    . PHE G 1 115 ? -2.974  63.287  14.167  1.00 20.62 ?  115 PHE J CG    1 
ATOM   8271  C  CD1   . PHE G 1 115 ? -3.700  64.469  14.071  1.00 22.13 ?  115 PHE J CD1   1 
ATOM   8272  C  CD2   . PHE G 1 115 ? -3.226  62.444  15.242  1.00 20.65 ?  115 PHE J CD2   1 
ATOM   8273  C  CE1   . PHE G 1 115 ? -4.656  64.791  15.021  1.00 21.31 ?  115 PHE J CE1   1 
ATOM   8274  C  CE2   . PHE G 1 115 ? -4.181  62.773  16.190  1.00 21.63 ?  115 PHE J CE2   1 
ATOM   8275  C  CZ    . PHE G 1 115 ? -4.893  63.944  16.078  1.00 21.03 ?  115 PHE J CZ    1 
ATOM   8276  N  N     . SER G 1 116 ? -0.845  63.491  10.228  1.00 20.41 ?  116 SER J N     1 
ATOM   8277  C  CA    . SER G 1 116 ? 0.303   63.463  9.338   1.00 22.25 ?  116 SER J CA    1 
ATOM   8278  C  C     . SER G 1 116 ? 1.558   63.063  10.110  1.00 23.19 ?  116 SER J C     1 
ATOM   8279  O  O     . SER G 1 116 ? 1.984   63.780  11.014  1.00 18.46 ?  116 SER J O     1 
ATOM   8280  C  CB    . SER G 1 116 ? 0.483   64.809  8.684   1.00 22.63 ?  116 SER J CB    1 
ATOM   8281  O  OG    . SER G 1 116 ? 1.632   64.827  7.848   1.00 24.17 ?  116 SER J OG    1 
ATOM   8282  N  N     . ALA G 1 117 ? 2.156   61.925  9.737   1.00 24.29 ?  117 ALA J N     1 
ATOM   8283  C  CA    . ALA G 1 117 ? 3.350   61.432  10.406  1.00 27.55 ?  117 ALA J CA    1 
ATOM   8284  C  C     . ALA G 1 117 ? 4.338   60.873  9.386   1.00 26.69 ?  117 ALA J C     1 
ATOM   8285  O  O     . ALA G 1 117 ? 3.956   60.115  8.498   1.00 22.96 ?  117 ALA J O     1 
ATOM   8286  C  CB    . ALA G 1 117 ? 2.971   60.380  11.424  1.00 28.51 ?  117 ALA J CB    1 
ATOM   8287  N  N     . LYS G 1 118 ? 5.615   61.245  9.531   1.00 27.08 ?  118 LYS J N     1 
ATOM   8288  C  CA    . LYS G 1 118 ? 6.656   60.710  8.671   1.00 27.75 ?  118 LYS J CA    1 
ATOM   8289  C  C     . LYS G 1 118 ? 7.949   60.540  9.463   1.00 26.64 ?  118 LYS J C     1 
ATOM   8290  O  O     . LYS G 1 118 ? 8.069   61.016  10.590  1.00 27.28 ?  118 LYS J O     1 
ATOM   8291  C  CB    . LYS G 1 118 ? 6.856   61.600  7.439   1.00 29.51 ?  118 LYS J CB    1 
ATOM   8292  C  CG    . LYS G 1 118 ? 7.457   62.974  7.689   1.00 29.45 ?  118 LYS J CG    1 
ATOM   8293  C  CD    . LYS G 1 118 ? 7.722   63.732  6.394   1.00 36.45 ?  118 LYS J CD    1 
ATOM   8294  C  CE    . LYS G 1 118 ? 8.408   65.045  6.595   1.00 39.33 ?  118 LYS J CE    1 
ATOM   8295  N  NZ    . LYS G 1 118 ? 8.296   65.884  5.399   1.00 36.52 1  118 LYS J NZ    1 
ATOM   8296  N  N     . MET G 1 119 ? 8.903   59.829  8.854   1.00 31.51 ?  119 MET J N     1 
ATOM   8297  C  CA    . MET G 1 119 ? 10.224  59.650  9.428   1.00 27.82 ?  119 MET J CA    1 
ATOM   8298  C  C     . MET G 1 119 ? 11.260  60.150  8.427   1.00 25.20 ?  119 MET J C     1 
ATOM   8299  O  O     . MET G 1 119 ? 11.229  59.788  7.253   1.00 24.24 ?  119 MET J O     1 
ATOM   8300  C  CB    . MET G 1 119 ? 10.495  58.179  9.771   1.00 28.18 ?  119 MET J CB    1 
ATOM   8301  C  CG    . MET G 1 119 ? 11.855  57.933  10.409  1.00 31.38 ?  119 MET J CG    1 
ATOM   8302  S  SD    . MET G 1 119 ? 12.136  56.213  10.876  1.00 34.17 ?  119 MET J SD    1 
ATOM   8303  C  CE    . MET G 1 119 ? 10.984  56.001  12.240  1.00 31.57 ?  119 MET J CE    1 
ATOM   8304  N  N     . GLU G 1 120 ? 12.156  61.009  8.918   1.00 23.10 ?  120 GLU J N     1 
ATOM   8305  C  CA    . GLU G 1 120 ? 13.312  61.447  8.159   1.00 22.58 ?  120 GLU J CA    1 
ATOM   8306  C  C     . GLU G 1 120 ? 14.504  60.597  8.579   1.00 23.83 ?  120 GLU J C     1 
ATOM   8307  O  O     . GLU G 1 120 ? 14.747  60.411  9.770   1.00 23.81 ?  120 GLU J O     1 
ATOM   8308  C  CB    . GLU G 1 120 ? 13.588  62.929  8.412   1.00 21.58 ?  120 GLU J CB    1 
ATOM   8309  C  CG    . GLU G 1 120 ? 12.599  63.856  7.714   1.00 22.53 ?  120 GLU J CG    1 
ATOM   8310  C  CD    . GLU G 1 120 ? 12.650  63.739  6.202   1.00 23.05 ?  120 GLU J CD    1 
ATOM   8311  O  OE1   . GLU G 1 120 ? 13.775  63.698  5.658   1.00 23.91 ?  120 GLU J OE1   1 
ATOM   8312  O  OE2   . GLU G 1 120 ? 11.574  63.697  5.570   1.00 29.15 -1 120 GLU J OE2   1 
ATOM   8313  N  N     . PRO G 1 121 ? 15.279  60.046  7.621   1.00 20.56 ?  121 PRO J N     1 
ATOM   8314  C  CA    . PRO G 1 121 ? 16.441  59.232  7.969   1.00 20.56 ?  121 PRO J CA    1 
ATOM   8315  C  C     . PRO G 1 121 ? 17.570  60.105  8.505   1.00 17.72 ?  121 PRO J C     1 
ATOM   8316  O  O     . PRO G 1 121 ? 17.714  61.258  8.107   1.00 17.63 ?  121 PRO J O     1 
ATOM   8317  C  CB    . PRO G 1 121 ? 16.790  58.554  6.638   1.00 21.35 ?  121 PRO J CB    1 
ATOM   8318  C  CG    . PRO G 1 121 ? 16.354  59.564  5.598   1.00 21.47 ?  121 PRO J CG    1 
ATOM   8319  C  CD    . PRO G 1 121 ? 15.089  60.190  6.169   1.00 20.17 ?  121 PRO J CD    1 
ATOM   8320  N  N     . GLY G 1 122 ? 18.357  59.536  9.421   1.00 17.99 ?  122 GLY J N     1 
ATOM   8321  C  CA    . GLY G 1 122 ? 19.533  60.201  9.956   1.00 14.98 ?  122 GLY J CA    1 
ATOM   8322  C  C     . GLY G 1 122 ? 20.739  59.269  9.922   1.00 15.35 ?  122 GLY J C     1 
ATOM   8323  O  O     . GLY G 1 122 ? 20.630  58.120  9.500   1.00 13.75 ?  122 GLY J O     1 
ATOM   8324  N  N     . ILE G 1 123 ? 21.883  59.783  10.383  1.00 14.62 ?  123 ILE J N     1 
ATOM   8325  C  CA    . ILE G 1 123 ? 23.147  59.068  10.343  1.00 16.63 ?  123 ILE J CA    1 
ATOM   8326  C  C     . ILE G 1 123 ? 23.273  58.215  11.606  1.00 18.42 ?  123 ILE J C     1 
ATOM   8327  O  O     . ILE G 1 123 ? 23.359  58.754  12.707  1.00 18.77 ?  123 ILE J O     1 
ATOM   8328  C  CB    . ILE G 1 123 ? 24.298  60.082  10.194  1.00 18.42 ?  123 ILE J CB    1 
ATOM   8329  C  CG1   . ILE G 1 123 ? 24.304  60.726  8.801   1.00 19.20 ?  123 ILE J CG1   1 
ATOM   8330  C  CG2   . ILE G 1 123 ? 25.649  59.449  10.530  1.00 19.03 ?  123 ILE J CG2   1 
ATOM   8331  C  CD1   . ILE G 1 123 ? 25.121  62.002  8.705   1.00 19.15 ?  123 ILE J CD1   1 
ATOM   8332  N  N     . SER G 1 124 ? 23.285  56.885  11.434  1.00 16.00 ?  124 SER J N     1 
ATOM   8333  C  CA    . SER G 1 124 ? 23.227  55.953  12.552  1.00 18.40 ?  124 SER J CA    1 
ATOM   8334  C  C     . SER G 1 124 ? 24.631  55.566  13.016  1.00 19.44 ?  124 SER J C     1 
ATOM   8335  O  O     . SER G 1 124 ? 25.624  55.923  12.387  1.00 21.70 ?  124 SER J O     1 
ATOM   8336  C  CB    . SER G 1 124 ? 22.433  54.719  12.194  1.00 20.17 ?  124 SER J CB    1 
ATOM   8337  O  OG    . SER G 1 124 ? 23.149  53.891  11.287  1.00 19.06 ?  124 SER J OG    1 
ATOM   8338  N  N     . ALA G 1 125 ? 24.694  54.820  14.125  1.00 20.07 ?  125 ALA J N     1 
ATOM   8339  C  CA    . ALA G 1 125 ? 25.947  54.271  14.619  1.00 20.48 ?  125 ALA J CA    1 
ATOM   8340  C  C     . ALA G 1 125 ? 26.579  53.389  13.545  1.00 21.48 ?  125 ALA J C     1 
ATOM   8341  O  O     . ALA G 1 125 ? 27.796  53.386  13.371  1.00 18.98 ?  125 ALA J O     1 
ATOM   8342  C  CB    . ALA G 1 125 ? 25.708  53.498  15.899  1.00 18.94 ?  125 ALA J CB    1 
ATOM   8343  N  N     . GLU G 1 126 ? 25.732  52.642  12.828  1.00 21.92 ?  126 GLU J N     1 
ATOM   8344  C  CA    . GLU G 1 126 ? 26.181  51.774  11.752  1.00 25.49 ?  126 GLU J CA    1 
ATOM   8345  C  C     . GLU G 1 126 ? 26.929  52.597  10.707  1.00 25.77 ?  126 GLU J C     1 
ATOM   8346  O  O     . GLU G 1 126 ? 28.030  52.240  10.293  1.00 26.95 ?  126 GLU J O     1 
ATOM   8347  C  CB    . GLU G 1 126 ? 24.971  51.064  11.144  1.00 28.58 ?  126 GLU J CB    1 
ATOM   8348  C  CG    . GLU G 1 126 ? 25.265  50.346  9.831   1.00 31.64 ?  126 GLU J CG    1 
ATOM   8349  C  CD    . GLU G 1 126 ? 24.120  49.461  9.371   1.00 33.24 ?  126 GLU J CD    1 
ATOM   8350  O  OE1   . GLU G 1 126 ? 23.798  48.498  10.097  1.00 34.75 ?  126 GLU J OE1   1 
ATOM   8351  O  OE2   . GLU G 1 126 ? 23.544  49.738  8.298   1.00 37.46 -1 126 GLU J OE2   1 
ATOM   8352  N  N     . ALA G 1 127 ? 26.309  53.705  10.290  1.00 22.59 ?  127 ALA J N     1 
ATOM   8353  C  CA    . ALA G 1 127 ? 26.873  54.570  9.269   1.00 21.00 ?  127 ALA J CA    1 
ATOM   8354  C  C     . ALA G 1 127 ? 28.209  55.138  9.741   1.00 18.06 ?  127 ALA J C     1 
ATOM   8355  O  O     . ALA G 1 127 ? 29.087  55.412  8.926   1.00 17.21 ?  127 ALA J O     1 
ATOM   8356  C  CB    . ALA G 1 127 ? 25.884  55.664  8.926   1.00 18.48 ?  127 ALA J CB    1 
ATOM   8357  N  N     . CYS G 1 128 ? 28.355  55.308  11.060  1.00 17.52 ?  128 CYS J N     1 
ATOM   8358  C  CA    . CYS G 1 128 ? 29.575  55.851  11.636  1.00 19.01 ?  128 CYS J CA    1 
ATOM   8359  C  C     . CYS G 1 128 ? 30.665  54.782  11.687  1.00 21.92 ?  128 CYS J C     1 
ATOM   8360  O  O     . CYS G 1 128 ? 31.851  55.098  11.610  1.00 23.23 ?  128 CYS J O     1 
ATOM   8361  C  CB    . CYS G 1 128 ? 29.335  56.412  13.035  1.00 21.32 ?  128 CYS J CB    1 
ATOM   8362  S  SG    . CYS G 1 128 ? 28.402  57.966  13.056  1.00 16.27 ?  128 CYS J SG    1 
ATOM   8363  N  N     . LEU G 1 129 ? 30.254  53.516  11.818  1.00 20.46 ?  129 LEU J N     1 
ATOM   8364  C  CA    . LEU G 1 129 ? 31.193  52.419  11.994  1.00 20.54 ?  129 LEU J CA    1 
ATOM   8365  C  C     . LEU G 1 129 ? 31.933  52.151  10.685  1.00 24.28 ?  129 LEU J C     1 
ATOM   8366  O  O     . LEU G 1 129 ? 33.133  51.886  10.696  1.00 24.02 ?  129 LEU J O     1 
ATOM   8367  C  CB    . LEU G 1 129 ? 30.460  51.176  12.496  1.00 18.95 ?  129 LEU J CB    1 
ATOM   8368  C  CG    . LEU G 1 129 ? 31.321  49.922  12.689  1.00 17.80 ?  129 LEU J CG    1 
ATOM   8369  C  CD1   . LEU G 1 129 ? 30.721  49.015  13.746  1.00 16.10 ?  129 LEU J CD1   1 
ATOM   8370  C  CD2   . LEU G 1 129 ? 31.483  49.167  11.382  1.00 17.41 ?  129 LEU J CD2   1 
ATOM   8371  N  N     . TRP G 1 130 ? 31.211  52.221  9.561   1.00 23.23 ?  130 TRP J N     1 
ATOM   8372  C  CA    . TRP G 1 130 ? 31.805  51.983  8.256   1.00 22.68 ?  130 TRP J CA    1 
ATOM   8373  C  C     . TRP G 1 130 ? 32.917  52.997  7.996   1.00 21.69 ?  130 TRP J C     1 
ATOM   8374  O  O     . TRP G 1 130 ? 33.988  52.638  7.513   1.00 22.75 ?  130 TRP J O     1 
ATOM   8375  C  CB    . TRP G 1 130 ? 30.739  52.051  7.153   1.00 23.55 ?  130 TRP J CB    1 
ATOM   8376  C  CG    . TRP G 1 130 ? 29.566  51.125  7.348   1.00 22.77 ?  130 TRP J CG    1 
ATOM   8377  C  CD1   . TRP G 1 130 ? 28.256  51.449  7.150   1.00 21.25 ?  130 TRP J CD1   1 
ATOM   8378  C  CD2   . TRP G 1 130 ? 29.579  49.735  7.750   1.00 22.64 ?  130 TRP J CD2   1 
ATOM   8379  N  NE1   . TRP G 1 130 ? 27.453  50.373  7.413   1.00 22.46 ?  130 TRP J NE1   1 
ATOM   8380  C  CE2   . TRP G 1 130 ? 28.233  49.308  7.780   1.00 20.56 ?  130 TRP J CE2   1 
ATOM   8381  C  CE3   . TRP G 1 130 ? 30.580  48.817  8.089   1.00 23.39 ?  130 TRP J CE3   1 
ATOM   8382  C  CZ2   . TRP G 1 130 ? 27.870  48.011  8.133   1.00 21.75 ?  130 TRP J CZ2   1 
ATOM   8383  C  CZ3   . TRP G 1 130 ? 30.218  47.533  8.437   1.00 23.60 ?  130 TRP J CZ3   1 
ATOM   8384  C  CH2   . TRP G 1 130 ? 28.881  47.137  8.456   1.00 21.31 ?  130 TRP J CH2   1 
ATOM   8385  N  N     . ALA G 1 131 ? 32.645  54.266  8.322   1.00 23.49 ?  131 ALA J N     1 
ATOM   8386  C  CA    . ALA G 1 131 ? 33.537  55.368  7.999   1.00 17.75 ?  131 ALA J CA    1 
ATOM   8387  C  C     . ALA G 1 131 ? 34.756  55.376  8.921   1.00 16.20 ?  131 ALA J C     1 
ATOM   8388  O  O     . ALA G 1 131 ? 35.853  55.723  8.492   1.00 14.53 ?  131 ALA J O     1 
ATOM   8389  C  CB    . ALA G 1 131 ? 32.781  56.676  8.086   1.00 17.86 ?  131 ALA J CB    1 
ATOM   8390  N  N     . ASP G 1 132 ? 34.545  55.020  10.192  1.00 17.42 ?  132 ASP J N     1 
ATOM   8391  C  CA    . ASP G 1 132 ? 35.605  55.032  11.188  1.00 18.06 ?  132 ASP J CA    1 
ATOM   8392  C  C     . ASP G 1 132 ? 36.548  53.855  10.961  1.00 20.26 ?  132 ASP J C     1 
ATOM   8393  O  O     . ASP G 1 132 ? 37.764  54.000  11.064  1.00 20.78 ?  132 ASP J O     1 
ATOM   8394  C  CB    . ASP G 1 132 ? 35.042  54.976  12.600  1.00 18.03 ?  132 ASP J CB    1 
ATOM   8395  C  CG    . ASP G 1 132 ? 34.492  56.285  13.146  1.00 17.60 ?  132 ASP J CG    1 
ATOM   8396  O  OD1   . ASP G 1 132 ? 34.829  57.344  12.580  1.00 19.80 ?  132 ASP J OD1   1 
ATOM   8397  O  OD2   . ASP G 1 132 ? 33.723  56.231  14.128  1.00 21.40 -1 132 ASP J OD2   1 
ATOM   8398  N  N     . LEU G 1 133 ? 35.967  52.686  10.667  1.00 21.25 ?  133 LEU J N     1 
ATOM   8399  C  CA    . LEU G 1 133 ? 36.738  51.464  10.517  1.00 27.35 ?  133 LEU J CA    1 
ATOM   8400  C  C     . LEU G 1 133 ? 37.246  51.344  9.082   1.00 27.82 ?  133 LEU J C     1 
ATOM   8401  O  O     . LEU G 1 133 ? 38.083  50.494  8.791   1.00 28.32 ?  133 LEU J O     1 
ATOM   8402  C  CB    . LEU G 1 133 ? 35.917  50.236  10.908  1.00 27.23 ?  133 LEU J CB    1 
ATOM   8403  C  CG    . LEU G 1 133 ? 35.403  50.184  12.350  1.00 27.34 ?  133 LEU J CG    1 
ATOM   8404  C  CD1   . LEU G 1 133 ? 35.834  48.863  12.960  1.00 29.88 ?  133 LEU J CD1   1 
ATOM   8405  C  CD2   . LEU G 1 133 ? 35.849  51.348  13.215  1.00 25.99 ?  133 LEU J CD2   1 
ATOM   8406  N  N     . GLY G 1 134 ? 36.724  52.192  8.189   1.00 31.72 ?  134 GLY J N     1 
ATOM   8407  C  CA    . GLY G 1 134 ? 37.118  52.165  6.789   1.00 27.42 ?  134 GLY J CA    1 
ATOM   8408  C  C     . GLY G 1 134 ? 36.671  50.872  6.113   1.00 27.78 ?  134 GLY J C     1 
ATOM   8409  O  O     . GLY G 1 134 ? 37.379  50.329  5.267   1.00 20.18 ?  134 GLY J O     1 
ATOM   8410  N  N     . ILE G 1 135 ? 35.479  50.402  6.502   1.00 28.60 ?  135 ILE J N     1 
ATOM   8411  C  CA    . ILE G 1 135 ? 34.900  49.170  5.992   1.00 26.31 ?  135 ILE J CA    1 
ATOM   8412  C  C     . ILE G 1 135 ? 33.676  49.509  5.146   1.00 29.60 ?  135 ILE J C     1 
ATOM   8413  O  O     . ILE G 1 135 ? 32.861  50.343  5.535   1.00 29.83 ?  135 ILE J O     1 
ATOM   8414  C  CB    . ILE G 1 135 ? 34.513  48.235  7.153   1.00 28.22 ?  135 ILE J CB    1 
ATOM   8415  C  CG1   . ILE G 1 135 ? 35.720  47.872  8.020   1.00 31.37 ?  135 ILE J CG1   1 
ATOM   8416  C  CG2   . ILE G 1 135 ? 33.786  46.995  6.632   1.00 30.84 ?  135 ILE J CG2   1 
ATOM   8417  C  CD1   . ILE G 1 135 ? 35.376  47.043  9.245   1.00 32.27 ?  135 ILE J CD1   1 
ATOM   8418  N  N     . ASP G 1 136 ? 33.551  48.844  3.993   1.00 24.89 ?  136 ASP J N     1 
ATOM   8419  C  CA    . ASP G 1 136 ? 32.370  48.978  3.157   1.00 23.51 ?  136 ASP J CA    1 
ATOM   8420  C  C     . ASP G 1 136 ? 31.474  47.761  3.378   1.00 26.92 ?  136 ASP J C     1 
ATOM   8421  O  O     . ASP G 1 136 ? 31.900  46.629  3.160   1.00 29.05 ?  136 ASP J O     1 
ATOM   8422  C  CB    . ASP G 1 136 ? 32.759  49.174  1.701   1.00 21.70 ?  136 ASP J CB    1 
ATOM   8423  C  CG    . ASP G 1 136 ? 31.608  49.186  0.706   1.00 18.88 ?  136 ASP J CG    1 
ATOM   8424  O  OD1   . ASP G 1 136 ? 30.480  48.833  1.108   1.00 17.91 ?  136 ASP J OD1   1 
ATOM   8425  O  OD2   . ASP G 1 136 ? 31.852  49.558  -0.462  1.00 17.19 -1 136 ASP J OD2   1 
ATOM   8426  N  N     . PRO G 1 137 ? 30.210  47.947  3.823   1.00 25.35 ?  137 PRO J N     1 
ATOM   8427  C  CA    . PRO G 1 137 ? 29.326  46.813  4.103   1.00 23.40 ?  137 PRO J CA    1 
ATOM   8428  C  C     . PRO G 1 137 ? 29.004  45.982  2.863   1.00 24.69 ?  137 PRO J C     1 
ATOM   8429  O  O     . PRO G 1 137 ? 28.421  44.904  2.971   1.00 23.47 ?  137 PRO J O     1 
ATOM   8430  C  CB    . PRO G 1 137 ? 28.078  47.491  4.699   1.00 21.26 ?  137 PRO J CB    1 
ATOM   8431  C  CG    . PRO G 1 137 ? 28.096  48.875  4.097   1.00 21.13 ?  137 PRO J CG    1 
ATOM   8432  C  CD    . PRO G 1 137 ? 29.568  49.247  4.078   1.00 21.40 ?  137 PRO J CD    1 
ATOM   8433  N  N     . GLY G 1 138 ? 29.392  46.493  1.690   1.00 26.20 ?  138 GLY J N     1 
ATOM   8434  C  CA    . GLY G 1 138 ? 29.183  45.787  0.436   1.00 28.40 ?  138 GLY J CA    1 
ATOM   8435  C  C     . GLY G 1 138 ? 30.388  44.927  0.059   1.00 26.09 ?  138 GLY J C     1 
ATOM   8436  O  O     . GLY G 1 138 ? 30.353  44.214  -0.942  1.00 27.08 ?  138 GLY J O     1 
ATOM   8437  N  N     . ASN G 1 139 ? 31.447  44.992  0.873   1.00 25.84 ?  139 ASN J N     1 
ATOM   8438  C  CA    . ASN G 1 139 ? 32.694  44.313  0.562   1.00 27.87 ?  139 ASN J CA    1 
ATOM   8439  C  C     . ASN G 1 139 ? 32.460  42.804  0.578   1.00 26.44 ?  139 ASN J C     1 
ATOM   8440  O  O     . ASN G 1 139 ? 32.622  42.136  -0.440  1.00 23.55 ?  139 ASN J O     1 
ATOM   8441  C  CB    . ASN G 1 139 ? 33.813  44.739  1.505   1.00 30.41 ?  139 ASN J CB    1 
ATOM   8442  C  CG    . ASN G 1 139 ? 35.180  44.426  0.945   1.00 29.82 ?  139 ASN J CG    1 
ATOM   8443  O  OD1   . ASN G 1 139 ? 35.956  43.694  1.568   1.00 28.70 ?  139 ASN J OD1   1 
ATOM   8444  N  ND2   . ASN G 1 139 ? 35.495  44.971  -0.222  1.00 32.11 ?  139 ASN J ND2   1 
ATOM   8445  N  N     . SER G 1 140 ? 32.079  42.275  1.745   1.00 30.40 ?  140 SER J N     1 
ATOM   8446  C  CA    . SER G 1 140 ? 31.673  40.884  1.848   1.00 32.95 ?  140 SER J CA    1 
ATOM   8447  C  C     . SER G 1 140 ? 30.282  40.795  2.472   1.00 28.48 ?  140 SER J C     1 
ATOM   8448  O  O     . SER G 1 140 ? 29.877  39.733  2.939   1.00 25.83 ?  140 SER J O     1 
ATOM   8449  C  CB    . SER G 1 140 ? 32.681  40.067  2.617   1.00 33.89 ?  140 SER J CB    1 
ATOM   8450  O  OG    . SER G 1 140 ? 32.915  40.618  3.905   1.00 36.24 ?  140 SER J OG    1 
ATOM   8451  N  N     . GLY G 1 141 ? 29.559  41.921  2.473   1.00 24.54 ?  141 GLY J N     1 
ATOM   8452  C  CA    . GLY G 1 141 ? 28.173  41.942  2.913   1.00 27.17 ?  141 GLY J CA    1 
ATOM   8453  C  C     . GLY G 1 141 ? 28.050  42.310  4.390   1.00 25.24 ?  141 GLY J C     1 
ATOM   8454  O  O     . GLY G 1 141 ? 29.044  42.337  5.112   1.00 24.42 ?  141 GLY J O     1 
ATOM   8455  N  N     . HIS G 1 142 ? 26.814  42.580  4.827   1.00 28.65 ?  142 HIS J N     1 
ATOM   8456  C  CA    . HIS G 1 142 ? 26.564  43.098  6.162   1.00 27.29 ?  142 HIS J CA    1 
ATOM   8457  C  C     . HIS G 1 142 ? 25.412  42.355  6.831   1.00 23.99 ?  142 HIS J C     1 
ATOM   8458  O  O     . HIS G 1 142 ? 24.443  41.975  6.179   1.00 21.18 ?  142 HIS J O     1 
ATOM   8459  C  CB    . HIS G 1 142 ? 26.233  44.594  6.118   1.00 32.07 ?  142 HIS J CB    1 
ATOM   8460  C  CG    . HIS G 1 142 ? 25.749  45.118  7.430   1.00 39.71 ?  142 HIS J CG    1 
ATOM   8461  N  ND1   . HIS G 1 142 ? 24.627  45.905  7.571   1.00 41.90 ?  142 HIS J ND1   1 
ATOM   8462  C  CD2   . HIS G 1 142 ? 26.223  44.925  8.667   1.00 43.20 ?  142 HIS J CD2   1 
ATOM   8463  C  CE1   . HIS G 1 142 ? 24.451  46.189  8.854   1.00 41.47 ?  142 HIS J CE1   1 
ATOM   8464  N  NE2   . HIS G 1 142 ? 25.412  45.606  9.537   1.00 45.98 ?  142 HIS J NE2   1 
ATOM   8465  N  N     . GLN G 1 143 ? 25.539  42.180  8.151   1.00 25.82 ?  143 GLN J N     1 
ATOM   8466  C  CA    . GLN G 1 143 ? 24.495  41.609  8.985   1.00 22.36 ?  143 GLN J CA    1 
ATOM   8467  C  C     . GLN G 1 143 ? 24.427  42.370  10.306  1.00 19.34 ?  143 GLN J C     1 
ATOM   8468  O  O     . GLN G 1 143 ? 25.457  42.705  10.889  1.00 16.53 ?  143 GLN J O     1 
ATOM   8469  C  CB    . GLN G 1 143 ? 24.771  40.141  9.305   1.00 25.03 ?  143 GLN J CB    1 
ATOM   8470  C  CG    . GLN G 1 143 ? 24.582  39.193  8.128   1.00 29.71 ?  143 GLN J CG    1 
ATOM   8471  C  CD    . GLN G 1 143 ? 24.713  37.741  8.531   1.00 30.42 ?  143 GLN J CD    1 
ATOM   8472  O  OE1   . GLN G 1 143 ? 25.696  37.335  9.161   1.00 30.41 ?  143 GLN J OE1   1 
ATOM   8473  N  NE2   . GLN G 1 143 ? 23.707  36.947  8.194   1.00 32.94 ?  143 GLN J NE2   1 
ATOM   8474  N  N     . SER G 1 144 ? 23.202  42.616  10.779  1.00 16.06 ?  144 SER J N     1 
ATOM   8475  C  CA    . SER G 1 144 ? 22.987  43.303  12.042  1.00 16.15 ?  144 SER J CA    1 
ATOM   8476  C  C     . SER G 1 144 ? 21.868  42.622  12.822  1.00 15.13 ?  144 SER J C     1 
ATOM   8477  O  O     . SER G 1 144 ? 20.802  42.348  12.277  1.00 14.19 ?  144 SER J O     1 
ATOM   8478  C  CB    . SER G 1 144 ? 22.687  44.765  11.830  1.00 14.04 ?  144 SER J CB    1 
ATOM   8479  O  OG    . SER G 1 144 ? 23.883  45.513  11.668  1.00 16.07 ?  144 SER J OG    1 
ATOM   8480  N  N     . PHE G 1 145 ? 22.129  42.356  14.105  1.00 16.07 ?  145 PHE J N     1 
ATOM   8481  C  CA    . PHE G 1 145 ? 21.110  41.824  14.992  1.00 16.49 ?  145 PHE J CA    1 
ATOM   8482  C  C     . PHE G 1 145 ? 21.274  42.439  16.373  1.00 16.52 ?  145 PHE J C     1 
ATOM   8483  O  O     . PHE G 1 145 ? 22.343  42.928  16.730  1.00 17.19 ?  145 PHE J O     1 
ATOM   8484  C  CB    . PHE G 1 145 ? 21.161  40.317  15.253  1.00 19.01 ?  145 PHE J CB    1 
ATOM   8485  C  CG    . PHE G 1 145 ? 21.288  39.438  14.020  1.00 23.46 ?  145 PHE J CG    1 
ATOM   8486  C  CD1   . PHE G 1 145 ? 22.528  39.226  13.431  1.00 25.29 ?  145 PHE J CD1   1 
ATOM   8487  C  CD2   . PHE G 1 145 ? 20.179  38.802  13.475  1.00 25.97 ?  145 PHE J CD2   1 
ATOM   8488  C  CE1   . PHE G 1 145 ? 22.651  38.417  12.314  1.00 27.63 ?  145 PHE J CE1   1 
ATOM   8489  C  CE2   . PHE G 1 145 ? 20.308  37.992  12.359  1.00 27.62 ?  145 PHE J CE2   1 
ATOM   8490  C  CZ    . PHE G 1 145 ? 21.543  37.802  11.782  1.00 28.38 ?  145 PHE J CZ    1 
ATOM   8491  N  N     . GLU G 1 146 ? 20.198  42.358  17.155  1.00 16.69 ?  146 GLU J N     1 
ATOM   8492  C  CA    . GLU G 1 146 ? 20.230  42.826  18.525  1.00 18.07 ?  146 GLU J CA    1 
ATOM   8493  C  C     . GLU G 1 146 ? 20.759  41.694  19.397  1.00 16.30 ?  146 GLU J C     1 
ATOM   8494  O  O     . GLU G 1 146 ? 20.208  40.596  19.406  1.00 19.01 ?  146 GLU J O     1 
ATOM   8495  C  CB    . GLU G 1 146 ? 18.850  43.345  18.925  1.00 16.19 ?  146 GLU J CB    1 
ATOM   8496  C  CG    . GLU G 1 146 ? 18.886  44.198  20.188  1.00 15.89 ?  146 GLU J CG    1 
ATOM   8497  C  CD    . GLU G 1 146 ? 18.642  43.444  21.482  1.00 15.24 ?  146 GLU J CD    1 
ATOM   8498  O  OE1   . GLU G 1 146 ? 18.195  42.279  21.427  1.00 14.56 ?  146 GLU J OE1   1 
ATOM   8499  O  OE2   . GLU G 1 146 ? 18.905  44.034  22.551  1.00 14.46 -1 146 GLU J OE2   1 
ATOM   8500  N  N     . ALA G 1 147 ? 21.846  41.979  20.117  1.00 17.98 ?  147 ALA J N     1 
ATOM   8501  C  CA    . ALA G 1 147 ? 22.584  40.950  20.825  1.00 19.59 ?  147 ALA J CA    1 
ATOM   8502  C  C     . ALA G 1 147 ? 21.620  39.993  21.526  1.00 19.18 ?  147 ALA J C     1 
ATOM   8503  O  O     . ALA G 1 147 ? 21.717  38.781  21.347  1.00 22.80 ?  147 ALA J O     1 
ATOM   8504  C  CB    . ALA G 1 147 ? 23.564  41.588  21.785  1.00 19.32 ?  147 ALA J CB    1 
ATOM   8505  N  N     . SER G 1 148 ? 20.679  40.536  22.308  1.00 19.38 ?  148 SER J N     1 
ATOM   8506  C  CA    . SER G 1 148 ? 19.777  39.706  23.093  1.00 20.01 ?  148 SER J CA    1 
ATOM   8507  C  C     . SER G 1 148 ? 18.858  38.885  22.188  1.00 21.41 ?  148 SER J C     1 
ATOM   8508  O  O     . SER G 1 148 ? 18.592  37.720  22.477  1.00 19.11 ?  148 SER J O     1 
ATOM   8509  C  CB    . SER G 1 148 ? 18.986  40.526  24.085  1.00 21.40 ?  148 SER J CB    1 
ATOM   8510  O  OG    . SER G 1 148 ? 19.811  40.964  25.157  1.00 20.24 ?  148 SER J OG    1 
ATOM   8511  N  N     . GLN G 1 149 ? 18.372  39.492  21.098  1.00 21.58 ?  149 GLN J N     1 
ATOM   8512  C  CA    . GLN G 1 149 ? 17.497  38.790  20.170  1.00 23.19 ?  149 GLN J CA    1 
ATOM   8513  C  C     . GLN G 1 149 ? 18.249  37.610  19.554  1.00 21.93 ?  149 GLN J C     1 
ATOM   8514  O  O     . GLN G 1 149 ? 17.668  36.548  19.342  1.00 20.35 ?  149 GLN J O     1 
ATOM   8515  C  CB    . GLN G 1 149 ? 16.948  39.702  19.070  1.00 22.94 ?  149 GLN J CB    1 
ATOM   8516  C  CG    . GLN G 1 149 ? 15.864  39.050  18.216  1.00 22.35 ?  149 GLN J CG    1 
ATOM   8517  C  CD    . GLN G 1 149 ? 15.481  39.865  16.999  1.00 25.52 ?  149 GLN J CD    1 
ATOM   8518  O  OE1   . GLN G 1 149 ? 15.688  39.449  15.853  1.00 26.36 ?  149 GLN J OE1   1 
ATOM   8519  N  NE2   . GLN G 1 149 ? 14.918  41.041  17.235  1.00 26.33 ?  149 GLN J NE2   1 
ATOM   8520  N  N     . PHE G 1 150 ? 19.542  37.811  19.270  1.00 24.26 ?  150 PHE J N     1 
ATOM   8521  C  CA    . PHE G 1 150 ? 20.373  36.798  18.636  1.00 25.04 ?  150 PHE J CA    1 
ATOM   8522  C  C     . PHE G 1 150 ? 20.553  35.621  19.592  1.00 25.21 ?  150 PHE J C     1 
ATOM   8523  O  O     . PHE G 1 150 ? 20.818  34.500  19.166  1.00 24.49 ?  150 PHE J O     1 
ATOM   8524  C  CB    . PHE G 1 150 ? 21.715  37.420  18.232  1.00 27.09 ?  150 PHE J CB    1 
ATOM   8525  C  CG    . PHE G 1 150 ? 22.696  36.470  17.556  1.00 29.41 ?  150 PHE J CG    1 
ATOM   8526  C  CD1   . PHE G 1 150 ? 23.560  35.681  18.309  1.00 30.32 ?  150 PHE J CD1   1 
ATOM   8527  C  CD2   . PHE G 1 150 ? 22.759  36.374  16.170  1.00 32.15 ?  150 PHE J CD2   1 
ATOM   8528  C  CE1   . PHE G 1 150 ? 24.452  34.817  17.692  1.00 30.50 ?  150 PHE J CE1   1 
ATOM   8529  C  CE2   . PHE G 1 150 ? 23.654  35.508  15.559  1.00 33.94 ?  150 PHE J CE2   1 
ATOM   8530  C  CZ    . PHE G 1 150 ? 24.497  34.733  16.320  1.00 30.98 ?  150 PHE J CZ    1 
ATOM   8531  N  N     . MET G 1 151 ? 20.402  35.898  20.891  1.00 26.10 ?  151 MET J N     1 
ATOM   8532  C  CA    . MET G 1 151 ? 20.605  34.901  21.928  1.00 30.43 ?  151 MET J CA    1 
ATOM   8533  C  C     . MET G 1 151 ? 19.289  34.192  22.239  1.00 34.48 ?  151 MET J C     1 
ATOM   8534  O  O     . MET G 1 151 ? 19.287  33.021  22.613  1.00 35.06 ?  151 MET J O     1 
ATOM   8535  C  CB    . MET G 1 151 ? 21.139  35.545  23.213  1.00 29.47 ?  151 MET J CB    1 
ATOM   8536  C  CG    . MET G 1 151 ? 22.604  35.931  23.155  1.00 28.83 ?  151 MET J CG    1 
ATOM   8537  S  SD    . MET G 1 151 ? 23.198  36.575  24.732  1.00 29.40 ?  151 MET J SD    1 
ATOM   8538  C  CE    . MET G 1 151 ? 23.108  35.097  25.752  1.00 34.85 ?  151 MET J CE    1 
ATOM   8539  N  N     . PHE G 1 152 ? 18.174  34.914  22.075  1.00 36.73 ?  152 PHE J N     1 
ATOM   8540  C  CA    . PHE G 1 152 ? 16.879  34.442  22.538  1.00 37.48 ?  152 PHE J CA    1 
ATOM   8541  C  C     . PHE G 1 152 ? 16.123  33.739  21.415  1.00 39.72 ?  152 PHE J C     1 
ATOM   8542  O  O     . PHE G 1 152 ? 15.153  33.030  21.672  1.00 37.65 ?  152 PHE J O     1 
ATOM   8543  C  CB    . PHE G 1 152 ? 16.038  35.605  23.072  1.00 37.77 ?  152 PHE J CB    1 
ATOM   8544  C  CG    . PHE G 1 152 ? 16.627  36.306  24.289  1.00 39.38 ?  152 PHE J CG    1 
ATOM   8545  C  CD1   . PHE G 1 152 ? 17.509  35.647  25.138  1.00 38.31 ?  152 PHE J CD1   1 
ATOM   8546  C  CD2   . PHE G 1 152 ? 16.287  37.621  24.584  1.00 38.01 ?  152 PHE J CD2   1 
ATOM   8547  C  CE1   . PHE G 1 152 ? 18.039  36.291  26.246  1.00 37.18 ?  152 PHE J CE1   1 
ATOM   8548  C  CE2   . PHE G 1 152 ? 16.820  38.259  25.692  1.00 35.91 ?  152 PHE J CE2   1 
ATOM   8549  C  CZ    . PHE G 1 152 ? 17.693  37.593  26.520  1.00 36.08 ?  152 PHE J CZ    1 
ATOM   8550  N  N     . PHE G 1 153 ? 16.559  33.952  20.172  1.00 41.25 ?  153 PHE J N     1 
ATOM   8551  C  CA    . PHE G 1 153 ? 15.893  33.344  19.034  1.00 40.93 ?  153 PHE J CA    1 
ATOM   8552  C  C     . PHE G 1 153 ? 16.945  32.695  18.143  1.00 37.42 ?  153 PHE J C     1 
ATOM   8553  O  O     . PHE G 1 153 ? 18.132  32.710  18.460  1.00 34.73 ?  153 PHE J O     1 
ATOM   8554  C  CB    . PHE G 1 153 ? 15.046  34.392  18.306  1.00 41.64 ?  153 PHE J CB    1 
ATOM   8555  C  CG    . PHE G 1 153 ? 13.974  35.026  19.182  1.00 40.73 ?  153 PHE J CG    1 
ATOM   8556  C  CD1   . PHE G 1 153 ? 12.774  34.369  19.429  1.00 41.96 ?  153 PHE J CD1   1 
ATOM   8557  C  CD2   . PHE G 1 153 ? 14.169  36.276  19.759  1.00 43.30 ?  153 PHE J CD2   1 
ATOM   8558  C  CE1   . PHE G 1 153 ? 11.801  34.945  20.230  1.00 40.89 ?  153 PHE J CE1   1 
ATOM   8559  C  CE2   . PHE G 1 153 ? 13.191  36.849  20.557  1.00 43.93 ?  153 PHE J CE2   1 
ATOM   8560  C  CZ    . PHE G 1 153 ? 12.011  36.183  20.791  1.00 42.95 ?  153 PHE J CZ    1 
ATOM   8561  N  N     . ASN G 1 154 ? 16.488  32.121  17.029  1.00 37.16 ?  154 ASN J N     1 
ATOM   8562  C  CA    . ASN G 1 154 ? 17.372  31.394  16.139  1.00 40.30 ?  154 ASN J CA    1 
ATOM   8563  C  C     . ASN G 1 154 ? 17.765  32.302  14.981  1.00 36.42 ?  154 ASN J C     1 
ATOM   8564  O  O     . ASN G 1 154 ? 16.954  32.611  14.110  1.00 34.05 ?  154 ASN J O     1 
ATOM   8565  C  CB    . ASN G 1 154 ? 16.753  30.067  15.723  1.00 45.42 ?  154 ASN J CB    1 
ATOM   8566  C  CG    . ASN G 1 154 ? 16.612  29.145  16.910  1.00 53.19 ?  154 ASN J CG    1 
ATOM   8567  O  OD1   . ASN G 1 154 ? 17.613  28.795  17.547  1.00 60.36 ?  154 ASN J OD1   1 
ATOM   8568  N  ND2   . ASN G 1 154 ? 15.388  28.761  17.238  1.00 52.17 ?  154 ASN J ND2   1 
ATOM   8569  N  N     . HIS G 1 155 ? 19.028  32.728  15.013  1.00 34.32 ?  155 HIS J N     1 
ATOM   8570  C  CA    . HIS G 1 155 ? 19.601  33.558  13.972  1.00 33.03 ?  155 HIS J CA    1 
ATOM   8571  C  C     . HIS G 1 155 ? 20.920  32.936  13.535  1.00 32.43 ?  155 HIS J C     1 
ATOM   8572  O  O     . HIS G 1 155 ? 21.817  32.724  14.348  1.00 34.48 ?  155 HIS J O     1 
ATOM   8573  C  CB    . HIS G 1 155 ? 19.775  35.001  14.457  1.00 33.17 ?  155 HIS J CB    1 
ATOM   8574  C  CG    . HIS G 1 155 ? 18.496  35.764  14.543  1.00 32.16 ?  155 HIS J CG    1 
ATOM   8575  N  ND1   . HIS G 1 155 ? 17.937  36.391  13.450  1.00 33.74 ?  155 HIS J ND1   1 
ATOM   8576  C  CD2   . HIS G 1 155 ? 17.668  35.999  15.568  1.00 30.83 ?  155 HIS J CD2   1 
ATOM   8577  C  CE1   . HIS G 1 155 ? 16.811  36.986  13.816  1.00 33.03 ?  155 HIS J CE1   1 
ATOM   8578  N  NE2   . HIS G 1 155 ? 16.630  36.762  15.100  1.00 32.30 ?  155 HIS J NE2   1 
ATOM   8579  N  N     . VAL G 1 156 ? 21.004  32.637  12.238  1.00 28.99 ?  156 VAL J N     1 
ATOM   8580  C  CA    . VAL G 1 156 ? 22.185  32.027  11.660  1.00 29.55 ?  156 VAL J CA    1 
ATOM   8581  C  C     . VAL G 1 156 ? 22.951  33.107  10.908  1.00 26.59 ?  156 VAL J C     1 
ATOM   8582  O  O     . VAL G 1 156 ? 22.484  33.605  9.886   1.00 24.41 ?  156 VAL J O     1 
ATOM   8583  C  CB    . VAL G 1 156 ? 21.815  30.858  10.728  1.00 30.44 ?  156 VAL J CB    1 
ATOM   8584  C  CG1   . VAL G 1 156 ? 23.056  30.192  10.149  1.00 33.10 ?  156 VAL J CG1   1 
ATOM   8585  C  CG2   . VAL G 1 156 ? 20.931  29.834  11.429  1.00 28.43 ?  156 VAL J CG2   1 
ATOM   8586  N  N     . PRO G 1 157 ? 24.142  33.510  11.402  1.00 27.93 ?  157 PRO J N     1 
ATOM   8587  C  CA    . PRO G 1 157 ? 24.954  34.510  10.714  1.00 25.78 ?  157 PRO J CA    1 
ATOM   8588  C  C     . PRO G 1 157 ? 25.712  33.886  9.546   1.00 24.04 ?  157 PRO J C     1 
ATOM   8589  O  O     . PRO G 1 157 ? 26.024  32.698  9.567   1.00 23.69 ?  157 PRO J O     1 
ATOM   8590  C  CB    . PRO G 1 157 ? 25.881  34.990  11.840  1.00 24.56 ?  157 PRO J CB    1 
ATOM   8591  C  CG    . PRO G 1 157 ? 26.106  33.745  12.671  1.00 26.32 ?  157 PRO J CG    1 
ATOM   8592  C  CD    . PRO G 1 157 ? 24.771  33.013  12.636  1.00 28.20 ?  157 PRO J CD    1 
ATOM   8593  N  N     . ASP G 1 158 ? 25.980  34.704  8.524   1.00 23.03 ?  158 ASP J N     1 
ATOM   8594  C  CA    . ASP G 1 158 ? 26.857  34.321  7.431   1.00 20.71 ?  158 ASP J CA    1 
ATOM   8595  C  C     . ASP G 1 158 ? 28.280  34.726  7.801   1.00 20.04 ?  158 ASP J C     1 
ATOM   8596  O  O     . ASP G 1 158 ? 28.592  35.913  7.830   1.00 17.93 ?  158 ASP J O     1 
ATOM   8597  C  CB    . ASP G 1 158 ? 26.410  34.957  6.123   1.00 18.90 ?  158 ASP J CB    1 
ATOM   8598  C  CG    . ASP G 1 158 ? 27.344  34.746  4.939   1.00 16.44 ?  158 ASP J CG    1 
ATOM   8599  O  OD1   . ASP G 1 158 ? 28.470  34.255  5.159   1.00 18.33 ?  158 ASP J OD1   1 
ATOM   8600  O  OD2   . ASP G 1 158 ? 26.935  35.060  3.803   1.00 15.43 -1 158 ASP J OD2   1 
ATOM   8601  N  N     . PRO G 1 159 ? 29.182  33.765  8.112   1.00 21.33 ?  159 PRO J N     1 
ATOM   8602  C  CA    . PRO G 1 159 ? 30.526  34.102  8.592   1.00 21.56 ?  159 PRO J CA    1 
ATOM   8603  C  C     . PRO G 1 159 ? 31.498  34.672  7.558   1.00 20.90 ?  159 PRO J C     1 
ATOM   8604  O  O     . PRO G 1 159 ? 32.670  34.876  7.865   1.00 18.88 ?  159 PRO J O     1 
ATOM   8605  C  CB    . PRO G 1 159 ? 31.017  32.762  9.180   1.00 22.94 ?  159 PRO J CB    1 
ATOM   8606  C  CG    . PRO G 1 159 ? 30.289  31.705  8.378   1.00 23.09 ?  159 PRO J CG    1 
ATOM   8607  C  CD    . PRO G 1 159 ? 28.934  32.315  8.060   1.00 23.00 ?  159 PRO J CD    1 
ATOM   8608  N  N     . THR G 1 160 ? 31.002  34.944  6.343   1.00 20.14 ?  160 THR J N     1 
ATOM   8609  C  CA    . THR G 1 160 ? 31.766  35.684  5.350   1.00 20.44 ?  160 THR J CA    1 
ATOM   8610  C  C     . THR G 1 160 ? 31.492  37.185  5.467   1.00 21.03 ?  160 THR J C     1 
ATOM   8611  O  O     . THR G 1 160 ? 32.171  37.977  4.817   1.00 24.54 ?  160 THR J O     1 
ATOM   8612  C  CB    . THR G 1 160 ? 31.430  35.185  3.943   1.00 20.27 ?  160 THR J CB    1 
ATOM   8613  O  OG1   . THR G 1 160 ? 30.011  35.243  3.846   1.00 16.33 ?  160 THR J OG1   1 
ATOM   8614  C  CG2   . THR G 1 160 ? 31.908  33.767  3.683   1.00 20.89 ?  160 THR J CG2   1 
ATOM   8615  N  N     . THR G 1 161 ? 30.508  37.587  6.285   1.00 18.31 ?  161 THR J N     1 
ATOM   8616  C  CA    . THR G 1 161 ? 30.075  38.980  6.300   1.00 19.61 ?  161 THR J CA    1 
ATOM   8617  C  C     . THR G 1 161 ? 30.525  39.665  7.588   1.00 18.77 ?  161 THR J C     1 
ATOM   8618  O  O     . THR G 1 161 ? 30.757  39.006  8.597   1.00 24.68 ?  161 THR J O     1 
ATOM   8619  C  CB    . THR G 1 161 ? 28.556  39.067  6.160   1.00 17.74 ?  161 THR J CB    1 
ATOM   8620  O  OG1   . THR G 1 161 ? 28.028  38.691  7.428   1.00 20.60 ?  161 THR J OG1   1 
ATOM   8621  C  CG2   . THR G 1 161 ? 28.015  38.164  5.067   1.00 18.60 ?  161 THR J CG2   1 
ATOM   8622  N  N     . HIS G 1 162 ? 30.626  40.999  7.547   1.00 20.32 ?  162 HIS J N     1 
ATOM   8623  C  CA    . HIS G 1 162 ? 30.747  41.772  8.772   1.00 17.75 ?  162 HIS J CA    1 
ATOM   8624  C  C     . HIS G 1 162 ? 29.452  41.617  9.564   1.00 19.16 ?  162 HIS J C     1 
ATOM   8625  O  O     . HIS G 1 162 ? 28.387  42.029  9.108   1.00 20.05 ?  162 HIS J O     1 
ATOM   8626  C  CB    . HIS G 1 162 ? 31.082  43.240  8.486   1.00 17.38 ?  162 HIS J CB    1 
ATOM   8627  C  CG    . HIS G 1 162 ? 32.509  43.470  8.115   1.00 16.21 ?  162 HIS J CG    1 
ATOM   8628  N  ND1   . HIS G 1 162 ? 32.940  43.623  6.815   1.00 16.10 ?  162 HIS J ND1   1 
ATOM   8629  C  CD2   . HIS G 1 162 ? 33.600  43.579  8.884   1.00 15.74 ?  162 HIS J CD2   1 
ATOM   8630  C  CE1   . HIS G 1 162 ? 34.252  43.814  6.811   1.00 17.72 ?  162 HIS J CE1   1 
ATOM   8631  N  NE2   . HIS G 1 162 ? 34.674  43.789  8.057   1.00 16.55 ?  162 HIS J NE2   1 
ATOM   8632  N  N     . LEU G 1 163 ? 29.558  40.993  10.742  1.00 21.58 ?  163 LEU J N     1 
ATOM   8633  C  CA    . LEU G 1 163 ? 28.423  40.811  11.632  1.00 20.48 ?  163 LEU J CA    1 
ATOM   8634  C  C     . LEU G 1 163 ? 28.434  41.907  12.695  1.00 20.74 ?  163 LEU J C     1 
ATOM   8635  O  O     . LEU G 1 163 ? 29.492  42.271  13.203  1.00 21.92 ?  163 LEU J O     1 
ATOM   8636  C  CB    . LEU G 1 163 ? 28.491  39.416  12.256  1.00 19.90 ?  163 LEU J CB    1 
ATOM   8637  C  CG    . LEU G 1 163 ? 27.492  39.128  13.383  1.00 19.52 ?  163 LEU J CG    1 
ATOM   8638  C  CD1   . LEU G 1 163 ? 26.062  39.231  12.890  1.00 21.29 ?  163 LEU J CD1   1 
ATOM   8639  C  CD2   . LEU G 1 163 ? 27.731  37.762  14.005  1.00 18.35 ?  163 LEU J CD2   1 
ATOM   8640  N  N     . LEU G 1 164 ? 27.245  42.432  13.021  1.00 22.94 ?  164 LEU J N     1 
ATOM   8641  C  CA    . LEU G 1 164 ? 27.094  43.393  14.105  1.00 21.91 ?  164 LEU J CA    1 
ATOM   8642  C  C     . LEU G 1 164 ? 26.093  42.858  15.128  1.00 19.38 ?  164 LEU J C     1 
ATOM   8643  O  O     . LEU G 1 164 ? 25.067  42.286  14.763  1.00 17.22 ?  164 LEU J O     1 
ATOM   8644  C  CB    . LEU G 1 164 ? 26.652  44.761  13.582  1.00 22.23 ?  164 LEU J CB    1 
ATOM   8645  C  CG    . LEU G 1 164 ? 27.652  45.508  12.693  1.00 23.69 ?  164 LEU J CG    1 
ATOM   8646  C  CD1   . LEU G 1 164 ? 27.140  46.893  12.327  1.00 24.64 ?  164 LEU J CD1   1 
ATOM   8647  C  CD2   . LEU G 1 164 ? 29.004  45.612  13.370  1.00 25.79 ?  164 LEU J CD2   1 
ATOM   8648  N  N     . LEU G 1 165 ? 26.413  43.055  16.413  1.00 19.02 ?  165 LEU J N     1 
ATOM   8649  C  CA    . LEU G 1 165 ? 25.476  42.825  17.502  1.00 16.74 ?  165 LEU J CA    1 
ATOM   8650  C  C     . LEU G 1 165 ? 25.307  44.130  18.279  1.00 18.36 ?  165 LEU J C     1 
ATOM   8651  O  O     . LEU G 1 165 ? 26.220  44.555  18.986  1.00 15.57 ?  165 LEU J O     1 
ATOM   8652  C  CB    . LEU G 1 165 ? 25.956  41.704  18.425  1.00 17.10 ?  165 LEU J CB    1 
ATOM   8653  C  CG    . LEU G 1 165 ? 26.119  40.312  17.804  1.00 16.69 ?  165 LEU J CG    1 
ATOM   8654  C  CD1   . LEU G 1 165 ? 26.526  39.332  18.890  1.00 17.64 ?  165 LEU J CD1   1 
ATOM   8655  C  CD2   . LEU G 1 165 ? 24.871  39.819  17.096  1.00 16.28 ?  165 LEU J CD2   1 
ATOM   8656  N  N     . TRP G 1 166 ? 24.132  44.760  18.143  1.00 17.01 ?  166 TRP J N     1 
ATOM   8657  C  CA    . TRP G 1 166 ? 23.857  46.023  18.812  1.00 17.56 ?  166 TRP J CA    1 
ATOM   8658  C  C     . TRP G 1 166 ? 23.395  45.754  20.243  1.00 17.38 ?  166 TRP J C     1 
ATOM   8659  O  O     . TRP G 1 166 ? 22.887  44.676  20.547  1.00 12.14 ?  166 TRP J O     1 
ATOM   8660  C  CB    . TRP G 1 166 ? 22.795  46.843  18.062  1.00 19.44 ?  166 TRP J CB    1 
ATOM   8661  C  CG    . TRP G 1 166 ? 23.064  47.129  16.606  1.00 21.86 ?  166 TRP J CG    1 
ATOM   8662  C  CD1   . TRP G 1 166 ? 23.395  46.246  15.619  1.00 22.36 ?  166 TRP J CD1   1 
ATOM   8663  C  CD2   . TRP G 1 166 ? 22.989  48.425  15.970  1.00 27.07 ?  166 TRP J CD2   1 
ATOM   8664  N  NE1   . TRP G 1 166 ? 23.536  46.899  14.422  1.00 21.51 ?  166 TRP J NE1   1 
ATOM   8665  C  CE2   . TRP G 1 166 ? 23.293  48.235  14.605  1.00 27.08 ?  166 TRP J CE2   1 
ATOM   8666  C  CE3   . TRP G 1 166 ? 22.700  49.718  16.421  1.00 30.60 ?  166 TRP J CE3   1 
ATOM   8667  C  CZ2   . TRP G 1 166 ? 23.315  49.291  13.695  1.00 29.59 ?  166 TRP J CZ2   1 
ATOM   8668  C  CZ3   . TRP G 1 166 ? 22.720  50.759  15.520  1.00 30.55 ?  166 TRP J CZ3   1 
ATOM   8669  C  CH2   . TRP G 1 166 ? 23.022  50.546  14.176  1.00 30.94 ?  166 TRP J CH2   1 
ATOM   8670  N  N     . GLN G 1 167 ? 23.567  46.757  21.112  1.00 15.94 ?  167 GLN J N     1 
ATOM   8671  C  CA    . GLN G 1 167 ? 23.162  46.666  22.505  1.00 15.29 ?  167 GLN J CA    1 
ATOM   8672  C  C     . GLN G 1 167 ? 23.844  45.463  23.154  1.00 14.57 ?  167 GLN J C     1 
ATOM   8673  O  O     . GLN G 1 167 ? 23.216  44.721  23.905  1.00 13.46 ?  167 GLN J O     1 
ATOM   8674  C  CB    . GLN G 1 167 ? 21.641  46.561  22.639  1.00 16.82 ?  167 GLN J CB    1 
ATOM   8675  C  CG    . GLN G 1 167 ? 20.870  47.675  21.937  1.00 17.64 ?  167 GLN J CG    1 
ATOM   8676  C  CD    . GLN G 1 167 ? 19.448  47.828  22.434  1.00 19.38 ?  167 GLN J CD    1 
ATOM   8677  O  OE1   . GLN G 1 167 ? 18.958  48.941  22.652  1.00 21.98 ?  167 GLN J OE1   1 
ATOM   8678  N  NE2   . GLN G 1 167 ? 18.760  46.707  22.601  1.00 19.75 ?  167 GLN J NE2   1 
ATOM   8679  N  N     . ILE G 1 168 ? 25.138  45.289  22.865  1.00 16.17 ?  168 ILE J N     1 
ATOM   8680  C  CA    . ILE G 1 168 ? 25.892  44.146  23.354  1.00 15.47 ?  168 ILE J CA    1 
ATOM   8681  C  C     . ILE G 1 168 ? 25.997  44.222  24.877  1.00 14.55 ?  168 ILE J C     1 
ATOM   8682  O  O     . ILE G 1 168 ? 26.160  43.201  25.542  1.00 12.22 ?  168 ILE J O     1 
ATOM   8683  C  CB    . ILE G 1 168 ? 27.278  44.077  22.683  1.00 16.95 ?  168 ILE J CB    1 
ATOM   8684  C  CG1   . ILE G 1 168 ? 28.044  42.811  23.082  1.00 15.74 ?  168 ILE J CG1   1 
ATOM   8685  C  CG2   . ILE G 1 168 ? 28.092  45.341  22.964  1.00 16.41 ?  168 ILE J CG2   1 
ATOM   8686  C  CD1   . ILE G 1 168 ? 27.403  41.522  22.600  1.00 15.91 ?  168 ILE J CD1   1 
ATOM   8687  N  N     . ALA G 1 169 ? 25.884  45.438  25.423  1.00 14.19 ?  169 ALA J N     1 
ATOM   8688  C  CA    . ALA G 1 169 ? 26.119  45.666  26.840  1.00 14.14 ?  169 ALA J CA    1 
ATOM   8689  C  C     . ALA G 1 169 ? 24.979  45.093  27.680  1.00 15.92 ?  169 ALA J C     1 
ATOM   8690  O  O     . ALA G 1 169 ? 25.124  44.933  28.889  1.00 17.79 ?  169 ALA J O     1 
ATOM   8691  C  CB    . ALA G 1 169 ? 26.310  47.143  27.104  1.00 14.38 ?  169 ALA J CB    1 
ATOM   8692  N  N     . ILE G 1 170 ? 23.843  44.792  27.040  1.00 16.36 ?  170 ILE J N     1 
ATOM   8693  C  CA    . ILE G 1 170 ? 22.722  44.186  27.742  1.00 16.29 ?  170 ILE J CA    1 
ATOM   8694  C  C     . ILE G 1 170 ? 22.411  42.823  27.127  1.00 16.47 ?  170 ILE J C     1 
ATOM   8695  O  O     . ILE G 1 170 ? 21.329  42.279  27.339  1.00 14.50 ?  170 ILE J O     1 
ATOM   8696  C  CB    . ILE G 1 170 ? 21.487  45.108  27.738  1.00 17.53 ?  170 ILE J CB    1 
ATOM   8697  C  CG1   . ILE G 1 170 ? 21.162  45.622  26.338  1.00 19.31 ?  170 ILE J CG1   1 
ATOM   8698  C  CG2   . ILE G 1 170 ? 21.656  46.259  28.731  1.00 19.42 ?  170 ILE J CG2   1 
ATOM   8699  C  CD1   . ILE G 1 170 ? 19.874  46.421  26.258  1.00 18.32 ?  170 ILE J CD1   1 
ATOM   8700  N  N     . ALA G 1 171 ? 23.372  42.272  26.378  1.00 14.55 ?  171 ALA J N     1 
ATOM   8701  C  CA    . ALA G 1 171 ? 23.226  40.944  25.805  1.00 14.75 ?  171 ALA J CA    1 
ATOM   8702  C  C     . ALA G 1 171 ? 22.805  39.956  26.889  1.00 15.85 ?  171 ALA J C     1 
ATOM   8703  O  O     . ALA G 1 171 ? 23.580  39.660  27.795  1.00 21.11 ?  171 ALA J O     1 
ATOM   8704  C  CB    . ALA G 1 171 ? 24.523  40.517  25.154  1.00 15.04 ?  171 ALA J CB    1 
ATOM   8705  N  N     . GLY G 1 172 ? 21.570  39.455  26.785  1.00 15.72 ?  172 GLY J N     1 
ATOM   8706  C  CA    . GLY G 1 172 ? 21.095  38.386  27.647  1.00 15.66 ?  172 GLY J CA    1 
ATOM   8707  C  C     . GLY G 1 172 ? 20.245  38.910  28.803  1.00 19.64 ?  172 GLY J C     1 
ATOM   8708  O  O     . GLY G 1 172 ? 19.757  38.130  29.618  1.00 19.20 ?  172 GLY J O     1 
ATOM   8709  N  N     . GLU G 1 173 ? 20.065  40.233  28.859  1.00 22.03 ?  173 GLU J N     1 
ATOM   8710  C  CA    . GLU G 1 173 ? 19.373  40.868  29.969  1.00 25.49 ?  173 GLU J CA    1 
ATOM   8711  C  C     . GLU G 1 173 ? 17.873  40.853  29.678  1.00 27.04 ?  173 GLU J C     1 
ATOM   8712  O  O     . GLU G 1 173 ? 17.327  41.804  29.122  1.00 33.83 ?  173 GLU J O     1 
ATOM   8713  C  CB    . GLU G 1 173 ? 19.958  42.264  30.182  1.00 27.32 ?  173 GLU J CB    1 
ATOM   8714  C  CG    . GLU G 1 173 ? 19.726  42.812  31.587  1.00 30.82 ?  173 GLU J CG    1 
ATOM   8715  C  CD    . GLU G 1 173 ? 18.267  43.047  31.933  1.00 34.49 ?  173 GLU J CD    1 
ATOM   8716  O  OE1   . GLU G 1 173 ? 17.700  44.054  31.458  1.00 37.08 ?  173 GLU J OE1   1 
ATOM   8717  O  OE2   . GLU G 1 173 ? 17.691  42.211  32.661  1.00 36.54 -1 173 GLU J OE2   1 
ATOM   8718  N  N     . HIS G 1 174 ? 17.224  39.759  30.092  1.00 29.38 ?  174 HIS J N     1 
ATOM   8719  C  CA    . HIS G 1 174 ? 15.927  39.355  29.572  1.00 29.83 ?  174 HIS J CA    1 
ATOM   8720  C  C     . HIS G 1 174 ? 14.790  40.164  30.195  1.00 34.71 ?  174 HIS J C     1 
ATOM   8721  O  O     . HIS G 1 174 ? 13.713  40.259  29.609  1.00 38.97 ?  174 HIS J O     1 
ATOM   8722  C  CB    . HIS G 1 174 ? 15.717  37.854  29.806  1.00 29.85 ?  174 HIS J CB    1 
ATOM   8723  C  CG    . HIS G 1 174 ? 15.637  37.475  31.248  1.00 27.35 ?  174 HIS J CG    1 
ATOM   8724  N  ND1   . HIS G 1 174 ? 16.751  37.296  32.040  1.00 28.02 ?  174 HIS J ND1   1 
ATOM   8725  C  CD2   . HIS G 1 174 ? 14.581  37.253  32.041  1.00 25.61 ?  174 HIS J CD2   1 
ATOM   8726  C  CE1   . HIS G 1 174 ? 16.368  36.970  33.267  1.00 25.78 ?  174 HIS J CE1   1 
ATOM   8727  N  NE2   . HIS G 1 174 ? 15.054  36.937  33.290  1.00 25.21 ?  174 HIS J NE2   1 
ATOM   8728  N  N     . THR G 1 175 ? 15.025  40.737  31.381  1.00 32.86 ?  175 THR J N     1 
ATOM   8729  C  CA    . THR G 1 175 ? 13.968  41.410  32.122  1.00 34.35 ?  175 THR J CA    1 
ATOM   8730  C  C     . THR G 1 175 ? 13.699  42.783  31.510  1.00 37.91 ?  175 THR J C     1 
ATOM   8731  O  O     . THR G 1 175 ? 12.609  43.329  31.665  1.00 39.90 ?  175 THR J O     1 
ATOM   8732  C  CB    . THR G 1 175 ? 14.340  41.526  33.601  1.00 33.38 ?  175 THR J CB    1 
ATOM   8733  O  OG1   . THR G 1 175 ? 15.279  42.594  33.689  1.00 21.92 ?  175 THR J OG1   1 
ATOM   8734  C  CG2   . THR G 1 175 ? 14.909  40.236  34.167  1.00 33.21 ?  175 THR J CG2   1 
ATOM   8735  N  N     . LEU G 1 176 ? 14.704  43.338  30.824  1.00 41.30 ?  176 LEU J N     1 
ATOM   8736  C  CA    . LEU G 1 176 ? 14.594  44.648  30.201  1.00 39.42 ?  176 LEU J CA    1 
ATOM   8737  C  C     . LEU G 1 176 ? 14.467  45.719  31.284  1.00 40.68 ?  176 LEU J C     1 
ATOM   8738  O  O     . LEU G 1 176 ? 13.972  46.813  31.020  1.00 38.81 ?  176 LEU J O     1 
ATOM   8739  C  CB    . LEU G 1 176 ? 13.410  44.700  29.234  1.00 41.47 ?  176 LEU J CB    1 
ATOM   8740  C  CG    . LEU G 1 176 ? 13.335  43.587  28.183  1.00 50.16 ?  176 LEU J CG    1 
ATOM   8741  C  CD1   . LEU G 1 176 ? 12.200  43.858  27.208  1.00 50.72 ?  176 LEU J CD1   1 
ATOM   8742  C  CD2   . LEU G 1 176 ? 14.647  43.412  27.434  1.00 53.07 ?  176 LEU J CD2   1 
ATOM   8743  N  N     . THR G 1 177 ? 14.924  45.400  32.501  1.00 35.12 ?  177 THR J N     1 
ATOM   8744  C  CA    . THR G 1 177 ? 14.840  46.331  33.615  1.00 28.66 ?  177 THR J CA    1 
ATOM   8745  C  C     . THR G 1 177 ? 16.235  46.830  33.984  1.00 29.45 ?  177 THR J C     1 
ATOM   8746  O  O     . THR G 1 177 ? 16.363  47.818  34.703  1.00 26.77 ?  177 THR J O     1 
ATOM   8747  C  CB    . THR G 1 177 ? 14.161  45.673  34.817  1.00 28.31 ?  177 THR J CB    1 
ATOM   8748  O  OG1   . THR G 1 177 ? 15.036  44.630  35.234  1.00 29.23 ?  177 THR J OG1   1 
ATOM   8749  C  CG2   . THR G 1 177 ? 12.787  45.120  34.486  1.00 27.50 ?  177 THR J CG2   1 
ATOM   8750  N  N     . GLN G 1 178 ? 17.274  46.142  33.497  1.00 26.40 ?  178 GLN J N     1 
ATOM   8751  C  CA    . GLN G 1 178 ? 18.643  46.477  33.857  1.00 25.69 ?  178 GLN J CA    1 
ATOM   8752  C  C     . GLN G 1 178 ? 19.317  47.186  32.685  1.00 25.31 ?  178 GLN J C     1 
ATOM   8753  O  O     . GLN G 1 178 ? 18.857  47.086  31.551  1.00 21.27 ?  178 GLN J O     1 
ATOM   8754  C  CB    . GLN G 1 178 ? 19.433  45.223  34.234  1.00 27.85 ?  178 GLN J CB    1 
ATOM   8755  C  CG    . GLN G 1 178 ? 18.791  44.373  35.326  1.00 31.02 ?  178 GLN J CG    1 
ATOM   8756  C  CD    . GLN G 1 178 ? 19.128  44.839  36.726  1.00 33.36 ?  178 GLN J CD    1 
ATOM   8757  O  OE1   . GLN G 1 178 ? 19.594  45.964  36.938  1.00 33.97 ?  178 GLN J OE1   1 
ATOM   8758  N  NE2   . GLN G 1 178 ? 18.890  43.971  37.700  1.00 31.35 ?  178 GLN J NE2   1 
ATOM   8759  N  N     . PHE G 1 179 ? 20.423  47.885  32.971  1.00 29.76 ?  179 PHE J N     1 
ATOM   8760  C  CA    . PHE G 1 179 ? 21.099  48.687  31.962  1.00 33.08 ?  179 PHE J CA    1 
ATOM   8761  C  C     . PHE G 1 179 ? 22.418  48.042  31.540  1.00 31.26 ?  179 PHE J C     1 
ATOM   8762  O  O     . PHE G 1 179 ? 23.102  48.565  30.663  1.00 31.00 ?  179 PHE J O     1 
ATOM   8763  C  CB    . PHE G 1 179 ? 21.283  50.125  32.455  1.00 33.54 ?  179 PHE J CB    1 
ATOM   8764  C  CG    . PHE G 1 179 ? 20.064  50.974  32.127  1.00 43.72 ?  179 PHE J CG    1 
ATOM   8765  C  CD1   . PHE G 1 179 ? 19.835  51.398  30.823  1.00 42.96 ?  179 PHE J CD1   1 
ATOM   8766  C  CD2   . PHE G 1 179 ? 19.131  51.308  33.102  1.00 50.07 ?  179 PHE J CD2   1 
ATOM   8767  C  CE1   . PHE G 1 179 ? 18.716  52.151  30.508  1.00 44.55 ?  179 PHE J CE1   1 
ATOM   8768  C  CE2   . PHE G 1 179 ? 18.014  52.064  32.782  1.00 48.54 ?  179 PHE J CE2   1 
ATOM   8769  C  CZ    . PHE G 1 179 ? 17.809  52.484  31.487  1.00 49.07 ?  179 PHE J CZ    1 
ATOM   8770  N  N     . HIS G 1 180 ? 22.767  46.906  32.150  1.00 31.12 ?  180 HIS J N     1 
ATOM   8771  C  CA    . HIS G 1 180 ? 23.949  46.171  31.733  1.00 30.20 ?  180 HIS J CA    1 
ATOM   8772  C  C     . HIS G 1 180 ? 23.752  44.684  32.013  1.00 29.90 ?  180 HIS J C     1 
ATOM   8773  O  O     . HIS G 1 180 ? 22.903  44.305  32.816  1.00 25.21 ?  180 HIS J O     1 
ATOM   8774  C  CB    . HIS G 1 180 ? 25.212  46.733  32.396  1.00 31.30 ?  180 HIS J CB    1 
ATOM   8775  C  CG    . HIS G 1 180 ? 25.339  46.432  33.853  1.00 35.31 ?  180 HIS J CG    1 
ATOM   8776  N  ND1   . HIS G 1 180 ? 25.757  45.207  34.325  1.00 33.81 ?  180 HIS J ND1   1 
ATOM   8777  C  CD2   . HIS G 1 180 ? 25.106  47.187  34.935  1.00 41.27 ?  180 HIS J CD2   1 
ATOM   8778  C  CE1   . HIS G 1 180 ? 25.775  45.233  35.649  1.00 41.23 ?  180 HIS J CE1   1 
ATOM   8779  N  NE2   . HIS G 1 180 ? 25.384  46.426  36.042  1.00 45.27 ?  180 HIS J NE2   1 
ATOM   8780  N  N     . THR G 1 181 ? 24.548  43.853  31.330  1.00 29.81 ?  181 THR J N     1 
ATOM   8781  C  CA    . THR G 1 181 ? 24.480  42.410  31.498  1.00 36.62 ?  181 THR J CA    1 
ATOM   8782  C  C     . THR G 1 181 ? 25.609  41.970  32.428  1.00 34.02 ?  181 THR J C     1 
ATOM   8783  O  O     . THR G 1 181 ? 26.259  42.806  33.051  1.00 39.58 ?  181 THR J O     1 
ATOM   8784  C  CB    . THR G 1 181 ? 24.555  41.730  30.131  1.00 39.29 ?  181 THR J CB    1 
ATOM   8785  O  OG1   . THR G 1 181 ? 24.255  40.359  30.373  1.00 43.23 ?  181 THR J OG1   1 
ATOM   8786  C  CG2   . THR G 1 181 ? 25.918  41.865  29.477  1.00 40.28 ?  181 THR J CG2   1 
ATOM   8787  N  N     . SER G 1 182 ? 25.832  40.654  32.519  1.00 38.56 ?  182 SER J N     1 
ATOM   8788  C  CA    . SER G 1 182 ? 26.875  40.111  33.375  1.00 39.34 ?  182 SER J CA    1 
ATOM   8789  C  C     . SER G 1 182 ? 27.892  39.331  32.544  1.00 38.60 ?  182 SER J C     1 
ATOM   8790  O  O     . SER G 1 182 ? 27.635  38.996  31.391  1.00 34.41 ?  182 SER J O     1 
ATOM   8791  C  CB    . SER G 1 182 ? 26.292  39.252  34.471  1.00 40.11 ?  182 SER J CB    1 
ATOM   8792  O  OG    . SER G 1 182 ? 25.716  38.064  33.943  1.00 43.47 ?  182 SER J OG    1 
ATOM   8793  N  N     . SER G 1 183 ? 29.044  39.044  33.164  1.00 43.59 ?  183 SER J N     1 
ATOM   8794  C  CA    . SER G 1 183 ? 30.166  38.383  32.514  1.00 40.65 ?  183 SER J CA    1 
ATOM   8795  C  C     . SER G 1 183 ? 29.777  36.985  32.037  1.00 39.71 ?  183 SER J C     1 
ATOM   8796  O  O     . SER G 1 183 ? 30.284  36.510  31.023  1.00 39.94 ?  183 SER J O     1 
ATOM   8797  C  CB    . SER G 1 183 ? 31.355  38.319  33.441  1.00 40.42 ?  183 SER J CB    1 
ATOM   8798  O  OG    . SER G 1 183 ? 31.009  37.702  34.674  1.00 40.23 ?  183 SER J OG    1 
ATOM   8799  N  N     . ASP G 1 184 ? 28.888  36.329  32.788  1.00 39.20 ?  184 ASP J N     1 
ATOM   8800  C  CA    . ASP G 1 184 ? 28.477  34.968  32.483  1.00 39.50 ?  184 ASP J CA    1 
ATOM   8801  C  C     . ASP G 1 184 ? 27.486  34.971  31.322  1.00 36.11 ?  184 ASP J C     1 
ATOM   8802  O  O     . ASP G 1 184 ? 27.379  33.985  30.596  1.00 32.95 ?  184 ASP J O     1 
ATOM   8803  C  CB    . ASP G 1 184 ? 27.874  34.284  33.699  1.00 43.58 ?  184 ASP J CB    1 
ATOM   8804  C  CG    . ASP G 1 184 ? 26.826  35.100  34.442  1.00 52.68 ?  184 ASP J CG    1 
ATOM   8805  O  OD1   . ASP G 1 184 ? 27.225  35.971  35.244  1.00 49.12 ?  184 ASP J OD1   1 
ATOM   8806  O  OD2   . ASP G 1 184 ? 25.622  34.874  34.191  1.00 61.48 -1 184 ASP J OD2   1 
ATOM   8807  N  N     . ARG G 1 185 ? 26.749  36.076  31.170  1.00 31.74 ?  185 ARG J N     1 
ATOM   8808  C  CA    . ARG G 1 185 ? 25.848  36.236  30.040  1.00 30.14 ?  185 ARG J CA    1 
ATOM   8809  C  C     . ARG G 1 185 ? 26.665  36.319  28.755  1.00 27.44 ?  185 ARG J C     1 
ATOM   8810  O  O     . ARG G 1 185 ? 26.374  35.629  27.781  1.00 23.91 ?  185 ARG J O     1 
ATOM   8811  C  CB    . ARG G 1 185 ? 24.954  37.474  30.163  1.00 31.67 ?  185 ARG J CB    1 
ATOM   8812  C  CG    . ARG G 1 185 ? 23.519  37.173  30.571  1.00 35.64 ?  185 ARG J CG    1 
ATOM   8813  C  CD    . ARG G 1 185 ? 23.364  36.764  32.026  1.00 38.30 ?  185 ARG J CD    1 
ATOM   8814  N  NE    . ARG G 1 185 ? 21.985  36.350  32.308  1.00 41.44 ?  185 ARG J NE    1 
ATOM   8815  C  CZ    . ARG G 1 185 ? 21.617  35.181  32.821  1.00 40.84 ?  185 ARG J CZ    1 
ATOM   8816  N  NH1   . ARG G 1 185 ? 22.528  34.302  33.199  1.00 41.34 1  185 ARG J NH1   1 
ATOM   8817  N  NH2   . ARG G 1 185 ? 20.334  34.902  32.971  1.00 37.72 ?  185 ARG J NH2   1 
ATOM   8818  N  N     . LEU G 1 186 ? 27.685  37.181  28.774  1.00 28.22 ?  186 LEU J N     1 
ATOM   8819  C  CA    . LEU G 1 186 ? 28.549  37.394  27.626  1.00 29.19 ?  186 LEU J CA    1 
ATOM   8820  C  C     . LEU G 1 186 ? 29.343  36.125  27.312  1.00 34.36 ?  186 LEU J C     1 
ATOM   8821  O  O     . LEU G 1 186 ? 29.665  35.868  26.154  1.00 34.01 ?  186 LEU J O     1 
ATOM   8822  C  CB    . LEU G 1 186 ? 29.439  38.593  27.944  1.00 29.77 ?  186 LEU J CB    1 
ATOM   8823  C  CG    . LEU G 1 186 ? 28.728  39.951  27.929  1.00 28.59 ?  186 LEU J CG    1 
ATOM   8824  C  CD1   . LEU G 1 186 ? 29.523  41.048  28.617  1.00 26.87 ?  186 LEU J CD1   1 
ATOM   8825  C  CD2   . LEU G 1 186 ? 28.419  40.336  26.490  1.00 26.30 ?  186 LEU J CD2   1 
ATOM   8826  N  N     . GLN G 1 187 ? 29.637  35.331  28.349  1.00 33.57 ?  187 GLN J N     1 
ATOM   8827  C  CA    . GLN G 1 187 ? 30.388  34.092  28.201  1.00 33.95 ?  187 GLN J CA    1 
ATOM   8828  C  C     . GLN G 1 187 ? 29.556  33.063  27.436  1.00 35.16 ?  187 GLN J C     1 
ATOM   8829  O  O     . GLN G 1 187 ? 30.098  32.244  26.697  1.00 29.56 ?  187 GLN J O     1 
ATOM   8830  C  CB    . GLN G 1 187 ? 30.780  33.556  29.579  1.00 35.28 ?  187 GLN J CB    1 
ATOM   8831  C  CG    . GLN G 1 187 ? 31.514  32.219  29.555  1.00 34.71 ?  187 GLN J CG    1 
ATOM   8832  C  CD    . GLN G 1 187 ? 32.796  32.256  28.753  1.00 33.28 ?  187 GLN J CD    1 
ATOM   8833  O  OE1   . GLN G 1 187 ? 33.678  33.090  28.985  1.00 34.80 ?  187 GLN J OE1   1 
ATOM   8834  N  NE2   . GLN G 1 187 ? 32.909  31.350  27.793  1.00 36.35 ?  187 GLN J NE2   1 
ATOM   8835  N  N     . ILE G 1 188 ? 28.235  33.110  27.633  1.00 35.42 ?  188 ILE J N     1 
ATOM   8836  C  CA    . ILE G 1 188 ? 27.324  32.200  26.960  1.00 35.29 ?  188 ILE J CA    1 
ATOM   8837  C  C     . ILE G 1 188 ? 27.129  32.667  25.519  1.00 31.56 ?  188 ILE J C     1 
ATOM   8838  O  O     . ILE G 1 188 ? 26.787  31.870  24.647  1.00 30.83 ?  188 ILE J O     1 
ATOM   8839  C  CB    . ILE G 1 188 ? 25.996  32.092  27.732  1.00 36.75 ?  188 ILE J CB    1 
ATOM   8840  C  CG1   . ILE G 1 188 ? 26.186  31.320  29.039  1.00 38.76 ?  188 ILE J CG1   1 
ATOM   8841  C  CG2   . ILE G 1 188 ? 24.899  31.471  26.865  1.00 38.62 ?  188 ILE J CG2   1 
ATOM   8842  C  CD1   . ILE G 1 188 ? 24.965  31.301  29.940  1.00 42.82 ?  188 ILE J CD1   1 
ATOM   8843  N  N     . LEU G 1 189 ? 27.365  33.962  25.283  1.00 29.55 ?  189 LEU J N     1 
ATOM   8844  C  CA    . LEU G 1 189 ? 27.316  34.521  23.940  1.00 29.01 ?  189 LEU J CA    1 
ATOM   8845  C  C     . LEU G 1 189 ? 28.544  34.062  23.158  1.00 24.02 ?  189 LEU J C     1 
ATOM   8846  O  O     . LEU G 1 189 ? 28.461  33.833  21.954  1.00 25.98 ?  189 LEU J O     1 
ATOM   8847  C  CB    . LEU G 1 189 ? 27.225  36.047  23.969  1.00 23.42 ?  189 LEU J CB    1 
ATOM   8848  C  CG    . LEU G 1 189 ? 27.325  36.738  22.604  1.00 21.13 ?  189 LEU J CG    1 
ATOM   8849  C  CD1   . LEU G 1 189 ? 26.275  36.190  21.652  1.00 20.66 ?  189 LEU J CD1   1 
ATOM   8850  C  CD2   . LEU G 1 189 ? 27.202  38.247  22.715  1.00 19.66 ?  189 LEU J CD2   1 
ATOM   8851  N  N     . VAL G 1 190 ? 29.680  33.940  23.854  1.00 27.10 ?  190 VAL J N     1 
ATOM   8852  C  CA    . VAL G 1 190 ? 30.935  33.545  23.232  1.00 30.15 ?  190 VAL J CA    1 
ATOM   8853  C  C     . VAL G 1 190 ? 30.831  32.094  22.771  1.00 28.69 ?  190 VAL J C     1 
ATOM   8854  O  O     . VAL G 1 190 ? 31.283  31.748  21.682  1.00 34.15 ?  190 VAL J O     1 
ATOM   8855  C  CB    . VAL G 1 190 ? 32.125  33.738  24.193  1.00 31.92 ?  190 VAL J CB    1 
ATOM   8856  C  CG1   . VAL G 1 190 ? 33.362  32.973  23.736  1.00 35.87 ?  190 VAL J CG1   1 
ATOM   8857  C  CG2   . VAL G 1 190 ? 32.452  35.211  24.403  1.00 32.33 ?  190 VAL J CG2   1 
ATOM   8858  N  N     . GLU G 1 191 ? 30.233  31.253  23.618  1.00 27.67 ?  191 GLU J N     1 
ATOM   8859  C  CA    . GLU G 1 191 ? 30.141  29.827  23.354  1.00 31.55 ?  191 GLU J CA    1 
ATOM   8860  C  C     . GLU G 1 191 ? 29.109  29.582  22.259  1.00 33.21 ?  191 GLU J C     1 
ATOM   8861  O  O     . GLU G 1 191 ? 29.232  28.639  21.479  1.00 32.70 ?  191 GLU J O     1 
ATOM   8862  C  CB    . GLU G 1 191 ? 29.788  29.097  24.649  1.00 33.99 ?  191 GLU J CB    1 
ATOM   8863  C  CG    . GLU G 1 191 ? 30.915  29.126  25.676  1.00 32.93 ?  191 GLU J CG    1 
ATOM   8864  C  CD    . GLU G 1 191 ? 30.488  28.700  27.069  1.00 36.20 ?  191 GLU J CD    1 
ATOM   8865  O  OE1   . GLU G 1 191 ? 30.918  29.349  28.046  1.00 35.91 ?  191 GLU J OE1   1 
ATOM   8866  O  OE2   . GLU G 1 191 ? 29.706  27.731  27.175  1.00 37.78 -1 191 GLU J OE2   1 
ATOM   8867  N  N     . GLN G 1 192 ? 28.089  30.444  22.219  1.00 32.89 ?  192 GLN J N     1 
ATOM   8868  C  CA    . GLN G 1 192 ? 27.098  30.414  21.159  1.00 34.66 ?  192 GLN J CA    1 
ATOM   8869  C  C     . GLN G 1 192 ? 27.758  30.800  19.838  1.00 32.68 ?  192 GLN J C     1 
ATOM   8870  O  O     . GLN G 1 192 ? 27.553  30.141  18.821  1.00 33.19 ?  192 GLN J O     1 
ATOM   8871  C  CB    . GLN G 1 192 ? 25.953  31.377  21.467  1.00 37.60 ?  192 GLN J CB    1 
ATOM   8872  C  CG    . GLN G 1 192 ? 24.882  31.415  20.383  1.00 39.10 ?  192 GLN J CG    1 
ATOM   8873  C  CD    . GLN G 1 192 ? 23.913  32.566  20.538  1.00 40.69 ?  192 GLN J CD    1 
ATOM   8874  O  OE1   . GLN G 1 192 ? 24.122  33.485  21.338  1.00 37.12 ?  192 GLN J OE1   1 
ATOM   8875  N  NE2   . GLN G 1 192 ? 22.842  32.529  19.758  1.00 42.97 ?  192 GLN J NE2   1 
ATOM   8876  N  N     . LEU G 1 193 ? 28.546  31.880  19.873  1.00 29.45 ?  193 LEU J N     1 
ATOM   8877  C  CA    . LEU G 1 193 ? 29.212  32.395  18.687  1.00 28.79 ?  193 LEU J CA    1 
ATOM   8878  C  C     . LEU G 1 193 ? 30.243  31.391  18.181  1.00 26.88 ?  193 LEU J C     1 
ATOM   8879  O  O     . LEU G 1 193 ? 30.595  31.404  17.004  1.00 26.06 ?  193 LEU J O     1 
ATOM   8880  C  CB    . LEU G 1 193 ? 29.863  33.741  19.003  1.00 25.68 ?  193 LEU J CB    1 
ATOM   8881  C  CG    . LEU G 1 193 ? 28.938  34.959  18.954  1.00 26.35 ?  193 LEU J CG    1 
ATOM   8882  C  CD1   . LEU G 1 193 ? 29.677  36.220  19.366  1.00 25.01 ?  193 LEU J CD1   1 
ATOM   8883  C  CD2   . LEU G 1 193 ? 28.345  35.102  17.562  1.00 24.99 ?  193 LEU J CD2   1 
ATOM   8884  N  N     . ASN G 1 194 ? 30.718  30.525  19.082  1.00 28.03 ?  194 ASN J N     1 
ATOM   8885  C  CA    . ASN G 1 194 ? 31.813  29.617  18.782  1.00 28.40 ?  194 ASN J CA    1 
ATOM   8886  C  C     . ASN G 1 194 ? 31.350  28.550  17.792  1.00 29.70 ?  194 ASN J C     1 
ATOM   8887  O  O     . ASN G 1 194 ? 32.129  27.679  17.411  1.00 29.78 ?  194 ASN J O     1 
ATOM   8888  C  CB    . ASN G 1 194 ? 32.382  28.995  20.053  1.00 27.53 ?  194 ASN J CB    1 
ATOM   8889  C  CG    . ASN G 1 194 ? 33.755  28.402  19.835  1.00 26.93 ?  194 ASN J CG    1 
ATOM   8890  O  OD1   . ASN G 1 194 ? 34.700  29.129  19.511  1.00 27.29 ?  194 ASN J OD1   1 
ATOM   8891  N  ND2   . ASN G 1 194 ? 33.887  27.096  20.013  1.00 25.30 ?  194 ASN J ND2   1 
ATOM   8892  N  N     . GLN G 1 195 ? 30.078  28.619  17.383  1.00 34.00 ?  195 GLN J N     1 
ATOM   8893  C  CA    . GLN G 1 195 ? 29.568  27.746  16.339  1.00 33.09 ?  195 GLN J CA    1 
ATOM   8894  C  C     . GLN G 1 195 ? 30.036  28.250  14.975  1.00 31.74 ?  195 GLN J C     1 
ATOM   8895  O  O     . GLN G 1 195 ? 29.919  27.535  13.982  1.00 28.89 ?  195 GLN J O     1 
ATOM   8896  C  CB    . GLN G 1 195 ? 28.039  27.668  16.311  1.00 35.40 ?  195 GLN J CB    1 
ATOM   8897  C  CG    . GLN G 1 195 ? 27.394  27.156  17.594  1.00 36.96 ?  195 GLN J CG    1 
ATOM   8898  C  CD    . GLN G 1 195 ? 25.883  27.259  17.566  1.00 39.18 ?  195 GLN J CD    1 
ATOM   8899  O  OE1   . GLN G 1 195 ? 25.192  26.458  16.926  1.00 40.76 ?  195 GLN J OE1   1 
ATOM   8900  N  NE2   . GLN G 1 195 ? 25.354  28.252  18.266  1.00 40.24 ?  195 GLN J NE2   1 
ATOM   8901  N  N     . TRP G 1 196 ? 30.553  29.486  14.924  1.00 27.63 ?  196 TRP J N     1 
ATOM   8902  C  CA    . TRP G 1 196 ? 30.930  30.089  13.653  1.00 28.74 ?  196 TRP J CA    1 
ATOM   8903  C  C     . TRP G 1 196 ? 32.288  30.784  13.738  1.00 25.63 ?  196 TRP J C     1 
ATOM   8904  O  O     . TRP G 1 196 ? 32.954  30.957  12.719  1.00 24.95 ?  196 TRP J O     1 
ATOM   8905  C  CB    . TRP G 1 196 ? 29.850  31.074  13.183  1.00 30.51 ?  196 TRP J CB    1 
ATOM   8906  C  CG    . TRP G 1 196 ? 28.468  30.478  13.144  1.00 30.25 ?  196 TRP J CG    1 
ATOM   8907  C  CD1   . TRP G 1 196 ? 27.928  29.708  12.156  1.00 30.41 ?  196 TRP J CD1   1 
ATOM   8908  C  CD2   . TRP G 1 196 ? 27.448  30.606  14.157  1.00 29.70 ?  196 TRP J CD2   1 
ATOM   8909  N  NE1   . TRP G 1 196 ? 26.648  29.347  12.481  1.00 28.95 ?  196 TRP J NE1   1 
ATOM   8910  C  CE2   . TRP G 1 196 ? 26.325  29.882  13.701  1.00 29.77 ?  196 TRP J CE2   1 
ATOM   8911  C  CE3   . TRP G 1 196 ? 27.376  31.256  15.394  1.00 28.52 ?  196 TRP J CE3   1 
ATOM   8912  C  CZ2   . TRP G 1 196 ? 25.149  29.793  14.442  1.00 27.50 ?  196 TRP J CZ2   1 
ATOM   8913  C  CZ3   . TRP G 1 196 ? 26.212  31.167  16.124  1.00 29.54 ?  196 TRP J CZ3   1 
ATOM   8914  C  CH2   . TRP G 1 196 ? 25.117  30.444  15.654  1.00 28.22 ?  196 TRP J CH2   1 
ATOM   8915  N  N     . TYR G 1 197 ? 32.691  31.194  14.945  1.00 24.75 ?  197 TYR J N     1 
ATOM   8916  C  CA    . TYR G 1 197 ? 33.905  31.977  15.115  1.00 25.07 ?  197 TYR J CA    1 
ATOM   8917  C  C     . TYR G 1 197 ? 34.801  31.308  16.152  1.00 25.10 ?  197 TYR J C     1 
ATOM   8918  O  O     . TYR G 1 197 ? 34.328  30.896  17.208  1.00 25.96 ?  197 TYR J O     1 
ATOM   8919  C  CB    . TYR G 1 197 ? 33.545  33.411  15.519  1.00 22.35 ?  197 TYR J CB    1 
ATOM   8920  C  CG    . TYR G 1 197 ? 32.583  34.076  14.546  1.00 22.14 ?  197 TYR J CG    1 
ATOM   8921  C  CD1   . TYR G 1 197 ? 33.050  34.790  13.450  1.00 20.64 ?  197 TYR J CD1   1 
ATOM   8922  C  CD2   . TYR G 1 197 ? 31.209  33.959  14.706  1.00 22.37 ?  197 TYR J CD2   1 
ATOM   8923  C  CE1   . TYR G 1 197 ? 32.178  35.381  12.551  1.00 18.98 ?  197 TYR J CE1   1 
ATOM   8924  C  CE2   . TYR G 1 197 ? 30.326  34.545  13.815  1.00 22.75 ?  197 TYR J CE2   1 
ATOM   8925  C  CZ    . TYR G 1 197 ? 30.813  35.257  12.734  1.00 20.35 ?  197 TYR J CZ    1 
ATOM   8926  O  OH    . TYR G 1 197 ? 29.943  35.835  11.856  1.00 22.96 ?  197 TYR J OH    1 
ATOM   8927  N  N     . PRO G 1 198 ? 36.119  31.174  15.881  1.00 28.12 ?  198 PRO J N     1 
ATOM   8928  C  CA    . PRO G 1 198 ? 37.051  30.633  16.872  1.00 29.49 ?  198 PRO J CA    1 
ATOM   8929  C  C     . PRO G 1 198 ? 37.169  31.558  18.081  1.00 30.15 ?  198 PRO J C     1 
ATOM   8930  O  O     . PRO G 1 198 ? 36.804  32.729  18.010  1.00 30.72 ?  198 PRO J O     1 
ATOM   8931  C  CB    . PRO G 1 198 ? 38.377  30.493  16.096  1.00 30.59 ?  198 PRO J CB    1 
ATOM   8932  C  CG    . PRO G 1 198 ? 37.976  30.570  14.634  1.00 31.70 ?  198 PRO J CG    1 
ATOM   8933  C  CD    . PRO G 1 198 ? 36.773  31.497  14.603  1.00 29.15 ?  198 PRO J CD    1 
ATOM   8934  N  N     . LEU G 1 199 ? 37.686  31.014  19.189  1.00 29.59 ?  199 LEU J N     1 
ATOM   8935  C  CA    . LEU G 1 199 ? 37.789  31.746  20.441  1.00 30.64 ?  199 LEU J CA    1 
ATOM   8936  C  C     . LEU G 1 199 ? 38.798  32.884  20.302  1.00 34.81 ?  199 LEU J C     1 
ATOM   8937  O  O     . LEU G 1 199 ? 38.689  33.894  20.993  1.00 36.13 ?  199 LEU J O     1 
ATOM   8938  C  CB    . LEU G 1 199 ? 38.175  30.802  21.579  1.00 32.01 ?  199 LEU J CB    1 
ATOM   8939  C  CG    . LEU G 1 199 ? 37.092  29.828  22.054  1.00 35.15 ?  199 LEU J CG    1 
ATOM   8940  C  CD1   . LEU G 1 199 ? 37.637  28.936  23.158  1.00 35.80 ?  199 LEU J CD1   1 
ATOM   8941  C  CD2   . LEU G 1 199 ? 35.847  30.559  22.528  1.00 36.51 ?  199 LEU J CD2   1 
ATOM   8942  N  N     . ASP G 1 200 ? 39.781  32.711  19.410  1.00 33.71 ?  200 ASP J N     1 
ATOM   8943  C  CA    . ASP G 1 200 ? 40.835  33.699  19.239  1.00 31.86 ?  200 ASP J CA    1 
ATOM   8944  C  C     . ASP G 1 200 ? 40.504  34.643  18.083  1.00 26.59 ?  200 ASP J C     1 
ATOM   8945  O  O     . ASP G 1 200 ? 41.362  35.412  17.655  1.00 24.93 ?  200 ASP J O     1 
ATOM   8946  C  CB    . ASP G 1 200 ? 42.190  33.041  19.026  1.00 33.01 ?  200 ASP J CB    1 
ATOM   8947  C  CG    . ASP G 1 200 ? 42.334  32.248  17.735  1.00 35.00 ?  200 ASP J CG    1 
ATOM   8948  O  OD1   . ASP G 1 200 ? 41.319  32.098  17.023  1.00 34.26 ?  200 ASP J OD1   1 
ATOM   8949  O  OD2   . ASP G 1 200 ? 43.463  31.799  17.445  1.00 41.56 -1 200 ASP J OD2   1 
ATOM   8950  N  N     . HIS G 1 201 ? 39.264  34.588  17.584  1.00 26.16 ?  201 HIS J N     1 
ATOM   8951  C  CA    . HIS G 1 201 ? 38.852  35.453  16.488  1.00 26.93 ?  201 HIS J CA    1 
ATOM   8952  C  C     . HIS G 1 201 ? 38.829  36.898  16.978  1.00 25.66 ?  201 HIS J C     1 
ATOM   8953  O  O     . HIS G 1 201 ? 38.217  37.202  18.000  1.00 26.77 ?  201 HIS J O     1 
ATOM   8954  C  CB    . HIS G 1 201 ? 37.500  35.010  15.913  1.00 29.27 ?  201 HIS J CB    1 
ATOM   8955  C  CG    . HIS G 1 201 ? 37.049  35.791  14.719  1.00 31.50 ?  201 HIS J CG    1 
ATOM   8956  N  ND1   . HIS G 1 201 ? 37.577  35.611  13.459  1.00 32.18 ?  201 HIS J ND1   1 
ATOM   8957  C  CD2   . HIS G 1 201 ? 36.125  36.754  14.597  1.00 32.66 ?  201 HIS J CD2   1 
ATOM   8958  C  CE1   . HIS G 1 201 ? 36.983  36.441  12.612  1.00 32.81 ?  201 HIS J CE1   1 
ATOM   8959  N  NE2   . HIS G 1 201 ? 36.096  37.144  13.282  1.00 31.07 ?  201 HIS J NE2   1 
ATOM   8960  N  N     . GLU G 1 202 ? 39.511  37.778  16.240  1.00 25.52 ?  202 GLU J N     1 
ATOM   8961  C  CA    . GLU G 1 202 ? 39.565  39.186  16.593  1.00 26.00 ?  202 GLU J CA    1 
ATOM   8962  C  C     . GLU G 1 202 ? 38.176  39.787  16.393  1.00 28.02 ?  202 GLU J C     1 
ATOM   8963  O  O     . GLU G 1 202 ? 37.545  39.578  15.359  1.00 24.10 ?  202 GLU J O     1 
ATOM   8964  C  CB    . GLU G 1 202 ? 40.639  39.899  15.769  1.00 26.54 ?  202 GLU J CB    1 
ATOM   8965  C  CG    . GLU G 1 202 ? 40.916  41.327  16.232  1.00 29.11 ?  202 GLU J CG    1 
ATOM   8966  C  CD    . GLU G 1 202 ? 41.950  42.069  15.403  1.00 29.54 ?  202 GLU J CD    1 
ATOM   8967  O  OE1   . GLU G 1 202 ? 41.668  42.343  14.218  1.00 31.42 ?  202 GLU J OE1   1 
ATOM   8968  O  OE2   . GLU G 1 202 ? 43.038  42.369  15.939  1.00 30.40 -1 202 GLU J OE2   1 
ATOM   8969  N  N     . VAL G 1 203 ? 37.696  40.504  17.413  1.00 27.79 ?  203 VAL J N     1 
ATOM   8970  C  CA    . VAL G 1 203 ? 36.454  41.253  17.309  1.00 27.00 ?  203 VAL J CA    1 
ATOM   8971  C  C     . VAL G 1 203 ? 36.737  42.678  17.773  1.00 26.60 ?  203 VAL J C     1 
ATOM   8972  O  O     . VAL G 1 203 ? 37.748  42.935  18.423  1.00 24.86 ?  203 VAL J O     1 
ATOM   8973  C  CB    . VAL G 1 203 ? 35.282  40.629  18.092  1.00 24.41 ?  203 VAL J CB    1 
ATOM   8974  C  CG1   . VAL G 1 203 ? 34.979  39.210  17.628  1.00 23.47 ?  203 VAL J CG1   1 
ATOM   8975  C  CG2   . VAL G 1 203 ? 35.509  40.660  19.599  1.00 24.82 ?  203 VAL J CG2   1 
ATOM   8976  N  N     . VAL G 1 204 ? 35.832  43.598  17.425  1.00 23.95 ?  204 VAL J N     1 
ATOM   8977  C  CA    . VAL G 1 204 ? 36.055  45.014  17.660  1.00 23.92 ?  204 VAL J CA    1 
ATOM   8978  C  C     . VAL G 1 204 ? 34.900  45.582  18.480  1.00 23.49 ?  204 VAL J C     1 
ATOM   8979  O  O     . VAL G 1 204 ? 33.740  45.459  18.092  1.00 25.66 ?  204 VAL J O     1 
ATOM   8980  C  CB    . VAL G 1 204 ? 36.207  45.760  16.320  1.00 22.56 ?  204 VAL J CB    1 
ATOM   8981  C  CG1   . VAL G 1 204 ? 36.493  47.242  16.525  1.00 20.61 ?  204 VAL J CG1   1 
ATOM   8982  C  CG2   . VAL G 1 204 ? 37.271  45.119  15.437  1.00 21.41 ?  204 VAL J CG2   1 
ATOM   8983  N  N     . ILE G 1 205 ? 35.235  46.201  19.618  1.00 23.48 ?  205 ILE J N     1 
ATOM   8984  C  CA    . ILE G 1 205 ? 34.265  46.964  20.384  1.00 19.92 ?  205 ILE J CA    1 
ATOM   8985  C  C     . ILE G 1 205 ? 34.319  48.408  19.900  1.00 18.16 ?  205 ILE J C     1 
ATOM   8986  O  O     . ILE G 1 205 ? 35.330  49.091  20.060  1.00 16.29 ?  205 ILE J O     1 
ATOM   8987  C  CB    . ILE G 1 205 ? 34.508  46.859  21.901  1.00 19.14 ?  205 ILE J CB    1 
ATOM   8988  C  CG1   . ILE G 1 205 ? 34.304  45.435  22.410  1.00 17.44 ?  205 ILE J CG1   1 
ATOM   8989  C  CG2   . ILE G 1 205 ? 33.623  47.848  22.660  1.00 19.86 ?  205 ILE J CG2   1 
ATOM   8990  C  CD1   . ILE G 1 205 ? 34.789  45.218  23.831  1.00 17.44 ?  205 ILE J CD1   1 
ATOM   8991  N  N     . TYR G 1 206 ? 33.208  48.849  19.304  1.00 16.51 ?  206 TYR J N     1 
ATOM   8992  C  CA    . TYR G 1 206 ? 33.151  50.125  18.616  1.00 16.54 ?  206 TYR J CA    1 
ATOM   8993  C  C     . TYR G 1 206 ? 32.215  51.081  19.348  1.00 17.44 ?  206 TYR J C     1 
ATOM   8994  O  O     . TYR G 1 206 ? 31.109  50.709  19.735  1.00 16.97 ?  206 TYR J O     1 
ATOM   8995  C  CB    . TYR G 1 206 ? 32.676  49.938  17.173  1.00 16.06 ?  206 TYR J CB    1 
ATOM   8996  C  CG    . TYR G 1 206 ? 32.434  51.261  16.461  1.00 15.82 ?  206 TYR J CG    1 
ATOM   8997  C  CD1   . TYR G 1 206 ? 33.501  52.068  16.089  1.00 15.46 ?  206 TYR J CD1   1 
ATOM   8998  C  CD2   . TYR G 1 206 ? 31.150  51.707  16.170  1.00 14.56 ?  206 TYR J CD2   1 
ATOM   8999  C  CE1   . TYR G 1 206 ? 33.302  53.280  15.451  1.00 14.52 ?  206 TYR J CE1   1 
ATOM   9000  C  CE2   . TYR G 1 206 ? 30.937  52.916  15.527  1.00 14.29 ?  206 TYR J CE2   1 
ATOM   9001  C  CZ    . TYR G 1 206 ? 32.016  53.704  15.167  1.00 14.07 ?  206 TYR J CZ    1 
ATOM   9002  O  OH    . TYR G 1 206 ? 31.825  54.897  14.532  1.00 14.30 ?  206 TYR J OH    1 
ATOM   9003  N  N     . GLU G 1 207 ? 32.685  52.322  19.507  1.00 17.58 ?  207 GLU J N     1 
ATOM   9004  C  CA    . GLU G 1 207 ? 31.877  53.410  20.029  1.00 18.92 ?  207 GLU J CA    1 
ATOM   9005  C  C     . GLU G 1 207 ? 32.166  54.671  19.221  1.00 19.86 ?  207 GLU J C     1 
ATOM   9006  O  O     . GLU G 1 207 ? 33.263  55.223  19.284  1.00 25.43 ?  207 GLU J O     1 
ATOM   9007  C  CB    . GLU G 1 207 ? 32.138  53.631  21.519  1.00 19.12 ?  207 GLU J CB    1 
ATOM   9008  C  CG    . GLU G 1 207 ? 31.719  52.440  22.376  1.00 19.02 ?  207 GLU J CG    1 
ATOM   9009  C  CD    . GLU G 1 207 ? 32.115  52.517  23.840  1.00 19.97 ?  207 GLU J CD    1 
ATOM   9010  O  OE1   . GLU G 1 207 ? 32.682  53.547  24.260  1.00 21.96 ?  207 GLU J OE1   1 
ATOM   9011  O  OE2   . GLU G 1 207 ? 31.860  51.531  24.561  1.00 19.75 -1 207 GLU J OE2   1 
ATOM   9012  N  N     . ALA G 1 208 ? 31.162  55.095  18.450  1.00 18.70 ?  208 ALA J N     1 
ATOM   9013  C  CA    . ALA G 1 208 ? 31.224  56.321  17.674  1.00 19.03 ?  208 ALA J CA    1 
ATOM   9014  C  C     . ALA G 1 208 ? 31.292  57.520  18.615  1.00 17.36 ?  208 ALA J C     1 
ATOM   9015  O  O     . ALA G 1 208 ? 30.519  57.610  19.565  1.00 17.17 ?  208 ALA J O     1 
ATOM   9016  C  CB    . ALA G 1 208 ? 30.014  56.402  16.771  1.00 19.56 ?  208 ALA J CB    1 
ATOM   9017  N  N     . ALA G 1 209 ? 32.219  58.441  18.340  1.00 19.01 ?  209 ALA J N     1 
ATOM   9018  C  CA    . ALA G 1 209 ? 32.357  59.634  19.157  1.00 19.81 ?  209 ALA J CA    1 
ATOM   9019  C  C     . ALA G 1 209 ? 31.057  60.432  19.107  1.00 23.81 ?  209 ALA J C     1 
ATOM   9020  O  O     . ALA G 1 209 ? 30.349  60.406  18.103  1.00 25.23 ?  209 ALA J O     1 
ATOM   9021  C  CB    . ALA G 1 209 ? 33.535  60.458  18.687  1.00 20.28 ?  209 ALA J CB    1 
ATOM   9022  N  N     . ASN G 1 210 ? 30.753  61.127  20.209  1.00 24.66 ?  210 ASN J N     1 
ATOM   9023  C  CA    . ASN G 1 210 ? 29.617  62.032  20.269  1.00 24.89 ?  210 ASN J CA    1 
ATOM   9024  C  C     . ASN G 1 210 ? 30.101  63.478  20.178  1.00 24.98 ?  210 ASN J C     1 
ATOM   9025  O  O     . ASN G 1 210 ? 29.356  64.354  19.741  1.00 22.55 ?  210 ASN J O     1 
ATOM   9026  C  CB    . ASN G 1 210 ? 28.791  61.835  21.536  1.00 27.65 ?  210 ASN J CB    1 
ATOM   9027  C  CG    . ASN G 1 210 ? 28.079  60.503  21.559  1.00 28.79 ?  210 ASN J CG    1 
ATOM   9028  O  OD1   . ASN G 1 210 ? 27.326  60.183  20.633  1.00 30.79 ?  210 ASN J OD1   1 
ATOM   9029  N  ND2   . ASN G 1 210 ? 28.300  59.718  22.603  1.00 32.06 ?  210 ASN J ND2   1 
ATOM   9030  N  N     . LEU G 1 211 ? 31.347  63.721  20.601  1.00 21.45 ?  211 LEU J N     1 
ATOM   9031  C  CA    . LEU G 1 211 ? 31.891  65.070  20.639  1.00 22.92 ?  211 LEU J CA    1 
ATOM   9032  C  C     . LEU G 1 211 ? 33.002  65.221  19.602  1.00 20.66 ?  211 LEU J C     1 
ATOM   9033  O  O     . LEU G 1 211 ? 33.704  64.262  19.286  1.00 14.89 ?  211 LEU J O     1 
ATOM   9034  C  CB    . LEU G 1 211 ? 32.393  65.398  22.044  1.00 22.86 ?  211 LEU J CB    1 
ATOM   9035  C  CG    . LEU G 1 211 ? 31.340  65.379  23.156  1.00 25.16 ?  211 LEU J CG    1 
ATOM   9036  C  CD1   . LEU G 1 211 ? 31.986  65.676  24.497  1.00 26.67 ?  211 LEU J CD1   1 
ATOM   9037  C  CD2   . LEU G 1 211 ? 30.212  66.360  22.873  1.00 27.60 ?  211 LEU J CD2   1 
ATOM   9038  N  N     . PRO G 1 212 ? 33.197  66.446  19.060  1.00 19.62 ?  212 PRO J N     1 
ATOM   9039  C  CA    . PRO G 1 212 ? 34.168  66.687  17.988  1.00 20.66 ?  212 PRO J CA    1 
ATOM   9040  C  C     . PRO G 1 212 ? 35.640  66.675  18.394  1.00 21.40 ?  212 PRO J C     1 
ATOM   9041  O  O     . PRO G 1 212 ? 36.518  66.737  17.534  1.00 21.13 ?  212 PRO J O     1 
ATOM   9042  C  CB    . PRO G 1 212 ? 33.733  68.076  17.492  1.00 21.16 ?  212 PRO J CB    1 
ATOM   9043  C  CG    . PRO G 1 212 ? 33.232  68.761  18.741  1.00 22.04 ?  212 PRO J CG    1 
ATOM   9044  C  CD    . PRO G 1 212 ? 32.465  67.662  19.452  1.00 22.40 ?  212 PRO J CD    1 
ATOM   9045  N  N     . ILE G 1 213 ? 35.897  66.611  19.705  1.00 18.53 ?  213 ILE J N     1 
ATOM   9046  C  CA    . ILE G 1 213 ? 37.253  66.564  20.229  1.00 21.34 ?  213 ILE J CA    1 
ATOM   9047  C  C     . ILE G 1 213 ? 37.564  65.140  20.682  1.00 22.92 ?  213 ILE J C     1 
ATOM   9048  O  O     . ILE G 1 213 ? 38.648  64.871  21.193  1.00 26.67 ?  213 ILE J O     1 
ATOM   9049  C  CB    . ILE G 1 213 ? 37.441  67.584  21.370  1.00 23.55 ?  213 ILE J CB    1 
ATOM   9050  C  CG1   . ILE G 1 213 ? 36.445  67.373  22.516  1.00 24.25 ?  213 ILE J CG1   1 
ATOM   9051  C  CG2   . ILE G 1 213 ? 37.362  69.014  20.834  1.00 23.03 ?  213 ILE J CG2   1 
ATOM   9052  C  CD1   . ILE G 1 213 ? 36.429  65.969  23.092  1.00 23.39 ?  213 ILE J CD1   1 
ATOM   9053  N  N     . GLN G 1 214 ? 36.601  64.235  20.471  1.00 22.46 ?  214 GLN J N     1 
ATOM   9054  C  CA    . GLN G 1 214 ? 36.697  62.864  20.945  1.00 24.58 ?  214 GLN J CA    1 
ATOM   9055  C  C     . GLN G 1 214 ? 36.977  61.920  19.778  1.00 25.61 ?  214 GLN J C     1 
ATOM   9056  O  O     . GLN G 1 214 ? 36.361  62.030  18.720  1.00 27.41 ?  214 GLN J O     1 
ATOM   9057  C  CB    . GLN G 1 214 ? 35.399  62.461  21.647  1.00 24.94 ?  214 GLN J CB    1 
ATOM   9058  C  CG    . GLN G 1 214 ? 35.221  60.954  21.805  1.00 24.84 ?  214 GLN J CG    1 
ATOM   9059  C  CD    . GLN G 1 214 ? 33.853  60.561  22.320  1.00 23.31 ?  214 GLN J CD    1 
ATOM   9060  O  OE1   . GLN G 1 214 ? 32.841  61.196  22.006  1.00 23.52 ?  214 GLN J OE1   1 
ATOM   9061  N  NE2   . GLN G 1 214 ? 33.811  59.510  23.126  1.00 20.67 ?  214 GLN J NE2   1 
ATOM   9062  N  N     . ALA G 1 215 ? 37.914  60.991  19.993  1.00 26.67 ?  215 ALA J N     1 
ATOM   9063  C  CA    . ALA G 1 215 ? 38.173  59.911  19.055  1.00 26.13 ?  215 ALA J CA    1 
ATOM   9064  C  C     . ALA G 1 215 ? 37.211  58.762  19.334  1.00 24.22 ?  215 ALA J C     1 
ATOM   9065  O  O     . ALA G 1 215 ? 36.720  58.617  20.450  1.00 25.43 ?  215 ALA J O     1 
ATOM   9066  C  CB    . ALA G 1 215 ? 39.610  59.451  19.170  1.00 27.09 ?  215 ALA J CB    1 
ATOM   9067  N  N     . PRO G 1 216 ? 36.914  57.907  18.330  1.00 24.71 ?  216 PRO J N     1 
ATOM   9068  C  CA    . PRO G 1 216 ? 36.065  56.740  18.553  1.00 25.00 ?  216 PRO J CA    1 
ATOM   9069  C  C     . PRO G 1 216 ? 36.794  55.658  19.338  1.00 23.53 ?  216 PRO J C     1 
ATOM   9070  O  O     . PRO G 1 216 ? 38.022  55.621  19.372  1.00 22.38 ?  216 PRO J O     1 
ATOM   9071  C  CB    . PRO G 1 216 ? 35.722  56.289  17.127  1.00 25.77 ?  216 PRO J CB    1 
ATOM   9072  C  CG    . PRO G 1 216 ? 36.928  56.708  16.316  1.00 26.33 ?  216 PRO J CG    1 
ATOM   9073  C  CD    . PRO G 1 216 ? 37.371  58.025  16.936  1.00 26.18 ?  216 PRO J CD    1 
ATOM   9074  N  N     . ARG G 1 217 ? 36.014  54.781  19.970  1.00 23.94 ?  217 ARG J N     1 
ATOM   9075  C  CA    . ARG G 1 217 ? 36.559  53.572  20.552  1.00 23.25 ?  217 ARG J CA    1 
ATOM   9076  C  C     . ARG G 1 217 ? 36.565  52.480  19.487  1.00 22.08 ?  217 ARG J C     1 
ATOM   9077  O  O     . ARG G 1 217 ? 35.515  52.085  18.986  1.00 18.94 ?  217 ARG J O     1 
ATOM   9078  C  CB    . ARG G 1 217 ? 35.747  53.136  21.774  1.00 24.07 ?  217 ARG J CB    1 
ATOM   9079  C  CG    . ARG G 1 217 ? 36.354  51.936  22.482  1.00 24.81 ?  217 ARG J CG    1 
ATOM   9080  C  CD    . ARG G 1 217 ? 35.462  51.487  23.615  1.00 26.03 ?  217 ARG J CD    1 
ATOM   9081  N  NE    . ARG G 1 217 ? 36.071  50.414  24.406  1.00 27.40 ?  217 ARG J NE    1 
ATOM   9082  C  CZ    . ARG G 1 217 ? 35.419  49.707  25.317  1.00 25.83 ?  217 ARG J CZ    1 
ATOM   9083  N  NH1   . ARG G 1 217 ? 34.148  49.968  25.567  1.00 23.08 1  217 ARG J NH1   1 
ATOM   9084  N  NH2   . ARG G 1 217 ? 36.039  48.740  25.969  1.00 24.14 ?  217 ARG J NH2   1 
ATOM   9085  N  N     . ILE G 1 218 ? 37.771  52.027  19.136  1.00 22.09 ?  218 ILE J N     1 
ATOM   9086  C  CA    . ILE G 1 218 ? 37.951  50.888  18.253  1.00 22.84 ?  218 ILE J CA    1 
ATOM   9087  C  C     . ILE G 1 218 ? 38.887  49.908  18.955  1.00 23.81 ?  218 ILE J C     1 
ATOM   9088  O  O     . ILE G 1 218 ? 40.097  49.922  18.738  1.00 24.03 ?  218 ILE J O     1 
ATOM   9089  C  CB    . ILE G 1 218 ? 38.481  51.333  16.876  1.00 24.27 ?  218 ILE J CB    1 
ATOM   9090  C  CG1   . ILE G 1 218 ? 37.650  52.486  16.299  1.00 24.63 ?  218 ILE J CG1   1 
ATOM   9091  C  CG2   . ILE G 1 218 ? 38.554  50.151  15.908  1.00 24.16 ?  218 ILE J CG2   1 
ATOM   9092  C  CD1   . ILE G 1 218 ? 38.196  53.061  15.005  1.00 24.28 ?  218 ILE J CD1   1 
ATOM   9093  N  N     . GLU G 1 219 ? 38.300  49.072  19.817  1.00 23.35 ?  219 GLU J N     1 
ATOM   9094  C  CA    . GLU G 1 219 ? 39.053  48.173  20.673  1.00 26.21 ?  219 GLU J CA    1 
ATOM   9095  C  C     . GLU G 1 219 ? 39.009  46.761  20.092  1.00 24.86 ?  219 GLU J C     1 
ATOM   9096  O  O     . GLU G 1 219 ? 37.960  46.119  20.082  1.00 19.96 ?  219 GLU J O     1 
ATOM   9097  C  CB    . GLU G 1 219 ? 38.467  48.259  22.083  1.00 27.91 ?  219 GLU J CB    1 
ATOM   9098  C  CG    . GLU G 1 219 ? 39.245  47.465  23.127  1.00 31.34 ?  219 GLU J CG    1 
ATOM   9099  C  CD    . GLU G 1 219 ? 38.761  47.697  24.548  1.00 30.71 ?  219 GLU J CD    1 
ATOM   9100  O  OE1   . GLU G 1 219 ? 38.651  48.877  24.941  1.00 31.47 ?  219 GLU J OE1   1 
ATOM   9101  O  OE2   . GLU G 1 219 ? 38.500  46.707  25.263  1.00 31.75 -1 219 GLU J OE2   1 
ATOM   9102  N  N     . ARG G 1 220 ? 40.167  46.299  19.605  1.00 23.88 ?  220 ARG J N     1 
ATOM   9103  C  CA    . ARG G 1 220 ? 40.304  44.976  19.017  1.00 26.70 ?  220 ARG J CA    1 
ATOM   9104  C  C     . ARG G 1 220 ? 40.748  43.994  20.097  1.00 26.38 ?  220 ARG J C     1 
ATOM   9105  O  O     . ARG G 1 220 ? 41.646  44.294  20.881  1.00 25.41 ?  220 ARG J O     1 
ATOM   9106  C  CB    . ARG G 1 220 ? 41.307  45.021  17.856  1.00 29.25 ?  220 ARG J CB    1 
ATOM   9107  C  CG    . ARG G 1 220 ? 40.827  45.818  16.651  1.00 30.53 ?  220 ARG J CG    1 
ATOM   9108  C  CD    . ARG G 1 220 ? 41.962  46.315  15.767  1.00 30.89 ?  220 ARG J CD    1 
ATOM   9109  N  NE    . ARG G 1 220 ? 41.460  47.222  14.729  1.00 31.22 ?  220 ARG J NE    1 
ATOM   9110  C  CZ    . ARG G 1 220 ? 40.719  46.848  13.694  1.00 31.39 ?  220 ARG J CZ    1 
ATOM   9111  N  NH1   . ARG G 1 220 ? 40.506  45.565  13.462  1.00 31.72 1  220 ARG J NH1   1 
ATOM   9112  N  NH2   . ARG G 1 220 ? 40.216  47.758  12.879  1.00 28.83 ?  220 ARG J NH2   1 
ATOM   9113  N  N     . LEU G 1 221 ? 40.112  42.817  20.124  1.00 26.84 ?  221 LEU J N     1 
ATOM   9114  C  CA    . LEU G 1 221 ? 40.389  41.822  21.147  1.00 24.94 ?  221 LEU J CA    1 
ATOM   9115  C  C     . LEU G 1 221 ? 39.858  40.467  20.693  1.00 25.12 ?  221 LEU J C     1 
ATOM   9116  O  O     . LEU G 1 221 ? 38.938  40.396  19.881  1.00 26.08 ?  221 LEU J O     1 
ATOM   9117  C  CB    . LEU G 1 221 ? 39.751  42.231  22.474  1.00 26.46 ?  221 LEU J CB    1 
ATOM   9118  C  CG    . LEU G 1 221 ? 38.237  42.021  22.581  1.00 25.10 ?  221 LEU J CG    1 
ATOM   9119  C  CD1   . LEU G 1 221 ? 37.794  42.012  24.033  1.00 25.99 ?  221 LEU J CD1   1 
ATOM   9120  C  CD2   . LEU G 1 221 ? 37.466  43.073  21.803  1.00 24.27 ?  221 LEU J CD2   1 
ATOM   9121  N  N     . PRO G 1 222 ? 40.414  39.351  21.214  1.00 24.26 ?  222 PRO J N     1 
ATOM   9122  C  CA    . PRO G 1 222 ? 39.891  38.022  20.901  1.00 24.51 ?  222 PRO J CA    1 
ATOM   9123  C  C     . PRO G 1 222 ? 38.475  37.862  21.442  1.00 23.49 ?  222 PRO J C     1 
ATOM   9124  O  O     . PRO G 1 222 ? 38.142  38.395  22.498  1.00 22.35 ?  222 PRO J O     1 
ATOM   9125  C  CB    . PRO G 1 222 ? 40.894  37.064  21.570  1.00 26.46 ?  222 PRO J CB    1 
ATOM   9126  C  CG    . PRO G 1 222 ? 41.525  37.892  22.670  1.00 27.12 ?  222 PRO J CG    1 
ATOM   9127  C  CD    . PRO G 1 222 ? 41.567  39.312  22.127  1.00 25.43 ?  222 PRO J CD    1 
ATOM   9128  N  N     . LEU G 1 223 ? 37.649  37.123  20.697  1.00 24.01 ?  223 LEU J N     1 
ATOM   9129  C  CA    . LEU G 1 223 ? 36.283  36.841  21.102  1.00 23.54 ?  223 LEU J CA    1 
ATOM   9130  C  C     . LEU G 1 223 ? 36.260  36.330  22.540  1.00 25.49 ?  223 LEU J C     1 
ATOM   9131  O  O     . LEU G 1 223 ? 35.290  36.547  23.264  1.00 27.12 ?  223 LEU J O     1 
ATOM   9132  C  CB    . LEU G 1 223 ? 35.695  35.819  20.130  1.00 24.15 ?  223 LEU J CB    1 
ATOM   9133  C  CG    . LEU G 1 223 ? 34.313  35.265  20.490  1.00 24.89 ?  223 LEU J CG    1 
ATOM   9134  C  CD1   . LEU G 1 223 ? 33.269  36.367  20.525  1.00 25.27 ?  223 LEU J CD1   1 
ATOM   9135  C  CD2   . LEU G 1 223 ? 33.909  34.169  19.518  1.00 24.89 ?  223 LEU J CD2   1 
ATOM   9136  N  N     . ALA G 1 224 ? 37.340  35.656  22.950  1.00 26.64 ?  224 ALA J N     1 
ATOM   9137  C  CA    . ALA G 1 224 ? 37.363  34.954  24.222  1.00 26.99 ?  224 ALA J CA    1 
ATOM   9138  C  C     . ALA G 1 224 ? 37.339  35.948  25.382  1.00 24.54 ?  224 ALA J C     1 
ATOM   9139  O  O     . ALA G 1 224 ? 36.852  35.628  26.464  1.00 22.65 ?  224 ALA J O     1 
ATOM   9140  C  CB    . ALA G 1 224 ? 38.575  34.046  24.290  1.00 27.02 ?  224 ALA J CB    1 
ATOM   9141  N  N     . ASN G 1 225 ? 37.856  37.157  25.138  1.00 25.51 ?  225 ASN J N     1 
ATOM   9142  C  CA    . ASN G 1 225 ? 38.076  38.141  26.187  1.00 27.95 ?  225 ASN J CA    1 
ATOM   9143  C  C     . ASN G 1 225 ? 36.895  39.103  26.299  1.00 33.25 ?  225 ASN J C     1 
ATOM   9144  O  O     . ASN G 1 225 ? 36.954  40.067  27.059  1.00 40.80 ?  225 ASN J O     1 
ATOM   9145  C  CB    . ASN G 1 225 ? 39.363  38.924  25.949  1.00 26.12 ?  225 ASN J CB    1 
ATOM   9146  C  CG    . ASN G 1 225 ? 40.595  38.101  26.238  1.00 24.24 ?  225 ASN J CG    1 
ATOM   9147  O  OD1   . ASN G 1 225 ? 40.492  36.897  26.498  1.00 24.07 ?  225 ASN J OD1   1 
ATOM   9148  N  ND2   . ASN G 1 225 ? 41.763  38.726  26.200  1.00 26.08 ?  225 ASN J ND2   1 
ATOM   9149  N  N     . LEU G 1 226 ? 35.822  38.839  25.547  1.00 32.39 ?  226 LEU J N     1 
ATOM   9150  C  CA    . LEU G 1 226 ? 34.684  39.743  25.503  1.00 31.91 ?  226 LEU J CA    1 
ATOM   9151  C  C     . LEU G 1 226 ? 34.038  39.834  26.885  1.00 32.32 ?  226 LEU J C     1 
ATOM   9152  O  O     . LEU G 1 226 ? 33.649  40.915  27.318  1.00 26.84 ?  226 LEU J O     1 
ATOM   9153  C  CB    . LEU G 1 226 ? 33.685  39.283  24.442  1.00 31.13 ?  226 LEU J CB    1 
ATOM   9154  C  CG    . LEU G 1 226 ? 32.375  40.074  24.366  1.00 32.37 ?  226 LEU J CG    1 
ATOM   9155  C  CD1   . LEU G 1 226 ? 32.650  41.552  24.139  1.00 33.94 ?  226 LEU J CD1   1 
ATOM   9156  C  CD2   . LEU G 1 226 ? 31.466  39.525  23.278  1.00 34.02 ?  226 LEU J CD2   1 
ATOM   9157  N  N     . PRO G 1 227 ? 33.886  38.706  27.615  1.00 32.72 ?  227 PRO J N     1 
ATOM   9158  C  CA    . PRO G 1 227 ? 33.256  38.730  28.938  1.00 30.47 ?  227 PRO J CA    1 
ATOM   9159  C  C     . PRO G 1 227 ? 33.965  39.561  30.007  1.00 27.76 ?  227 PRO J C     1 
ATOM   9160  O  O     . PRO G 1 227 ? 33.379  39.837  31.051  1.00 26.93 ?  227 PRO J O     1 
ATOM   9161  C  CB    . PRO G 1 227 ? 33.222  37.235  29.312  1.00 29.72 ?  227 PRO J CB    1 
ATOM   9162  C  CG    . PRO G 1 227 ? 33.256  36.522  27.981  1.00 31.02 ?  227 PRO J CG    1 
ATOM   9163  C  CD    . PRO G 1 227 ? 34.241  37.347  27.178  1.00 30.80 ?  227 PRO J CD    1 
ATOM   9164  N  N     . GLN G 1 228 ? 35.221  39.951  29.753  1.00 26.14 ?  228 GLN J N     1 
ATOM   9165  C  CA    . GLN G 1 228 ? 35.972  40.736  30.722  1.00 28.03 ?  228 GLN J CA    1 
ATOM   9166  C  C     . GLN G 1 228 ? 36.101  42.178  30.241  1.00 29.36 ?  228 GLN J C     1 
ATOM   9167  O  O     . GLN G 1 228 ? 36.719  43.004  30.909  1.00 27.22 ?  228 GLN J O     1 
ATOM   9168  C  CB    . GLN G 1 228 ? 37.392  40.227  30.980  1.00 30.63 ?  228 GLN J CB    1 
ATOM   9169  C  CG    . GLN G 1 228 ? 37.477  38.787  31.474  1.00 29.16 ?  228 GLN J CG    1 
ATOM   9170  C  CD    . GLN G 1 228 ? 37.800  37.802  30.372  1.00 27.10 ?  228 GLN J CD    1 
ATOM   9171  O  OE1   . GLN G 1 228 ? 38.859  37.871  29.738  1.00 28.53 ?  228 GLN J OE1   1 
ATOM   9172  N  NE2   . GLN G 1 228 ? 36.892  36.866  30.139  1.00 28.10 ?  228 GLN J NE2   1 
ATOM   9173  N  N     . ALA G 1 229 ? 35.516  42.470  29.076  1.00 31.46 ?  229 ALA J N     1 
ATOM   9174  C  CA    . ALA G 1 229 ? 35.705  43.759  28.434  1.00 32.59 ?  229 ALA J CA    1 
ATOM   9175  C  C     . ALA G 1 229 ? 34.828  44.808  29.111  1.00 32.43 ?  229 ALA J C     1 
ATOM   9176  O  O     . ALA G 1 229 ? 33.842  44.477  29.765  1.00 32.60 ?  229 ALA J O     1 
ATOM   9177  C  CB    . ALA G 1 229 ? 35.404  43.645  26.956  1.00 32.46 ?  229 ALA J CB    1 
ATOM   9178  N  N     . HIS G 1 230 ? 35.212  46.077  28.949  1.00 34.98 ?  230 HIS J N     1 
ATOM   9179  C  CA    . HIS G 1 230 ? 34.449  47.185  29.496  1.00 37.22 ?  230 HIS J CA    1 
ATOM   9180  C  C     . HIS G 1 230 ? 33.479  47.688  28.429  1.00 31.97 ?  230 HIS J C     1 
ATOM   9181  O  O     . HIS G 1 230 ? 33.895  48.301  27.449  1.00 35.50 ?  230 HIS J O     1 
ATOM   9182  C  CB    . HIS G 1 230 ? 35.392  48.280  30.007  1.00 40.42 ?  230 HIS J CB    1 
ATOM   9183  C  CG    . HIS G 1 230 ? 34.682  49.411  30.670  1.00 46.83 ?  230 HIS J CG    1 
ATOM   9184  N  ND1   . HIS G 1 230 ? 34.268  49.355  31.983  1.00 52.92 ?  230 HIS J ND1   1 
ATOM   9185  C  CD2   . HIS G 1 230 ? 34.296  50.608  30.210  1.00 51.01 ?  230 HIS J CD2   1 
ATOM   9186  C  CE1   . HIS G 1 230 ? 33.663  50.491  32.299  1.00 51.43 ?  230 HIS J CE1   1 
ATOM   9187  N  NE2   . HIS G 1 230 ? 33.669  51.267  31.237  1.00 52.86 ?  230 HIS J NE2   1 
ATOM   9188  N  N     . LEU G 1 231 ? 32.184  47.420  28.636  1.00 28.88 ?  231 LEU J N     1 
ATOM   9189  C  CA    . LEU G 1 231 ? 31.163  47.717  27.644  1.00 29.66 ?  231 LEU J CA    1 
ATOM   9190  C  C     . LEU G 1 231 ? 30.264  48.845  28.144  1.00 32.90 ?  231 LEU J C     1 
ATOM   9191  O  O     . LEU G 1 231 ? 29.973  48.935  29.335  1.00 38.02 ?  231 LEU J O     1 
ATOM   9192  C  CB    . LEU G 1 231 ? 30.350  46.459  27.340  1.00 25.06 ?  231 LEU J CB    1 
ATOM   9193  C  CG    . LEU G 1 231 ? 31.109  45.301  26.682  1.00 23.99 ?  231 LEU J CG    1 
ATOM   9194  C  CD1   . LEU G 1 231 ? 30.204  44.087  26.557  1.00 23.86 ?  231 LEU J CD1   1 
ATOM   9195  C  CD2   . LEU G 1 231 ? 31.668  45.696  25.325  1.00 21.12 ?  231 LEU J CD2   1 
ATOM   9196  N  N     . MET G 1 232 ? 29.821  49.695  27.211  1.00 34.86 ?  232 MET J N     1 
ATOM   9197  C  CA    . MET G 1 232 ? 28.950  50.815  27.529  1.00 35.60 ?  232 MET J CA    1 
ATOM   9198  C  C     . MET G 1 232 ? 27.641  50.667  26.759  1.00 32.23 ?  232 MET J C     1 
ATOM   9199  O  O     . MET G 1 232 ? 27.580  49.946  25.766  1.00 25.67 ?  232 MET J O     1 
ATOM   9200  C  CB    . MET G 1 232 ? 29.619  52.146  27.167  1.00 40.08 ?  232 MET J CB    1 
ATOM   9201  C  CG    . MET G 1 232 ? 30.878  52.435  27.963  1.00 44.02 ?  232 MET J CG    1 
ATOM   9202  S  SD    . MET G 1 232 ? 30.596  52.405  29.744  1.00 56.82 ?  232 MET J SD    1 
ATOM   9203  C  CE    . MET G 1 232 ? 29.517  53.826  29.969  1.00 59.21 ?  232 MET J CE    1 
ATOM   9204  N  N     . PRO G 1 233 ? 26.547  51.334  27.191  1.00 34.57 ?  233 PRO J N     1 
ATOM   9205  C  CA    . PRO G 1 233 ? 25.279  51.256  26.467  1.00 31.95 ?  233 PRO J CA    1 
ATOM   9206  C  C     . PRO G 1 233 ? 25.454  51.520  24.973  1.00 27.92 ?  233 PRO J C     1 
ATOM   9207  O  O     . PRO G 1 233 ? 24.756  50.929  24.153  1.00 25.05 ?  233 PRO J O     1 
ATOM   9208  C  CB    . PRO G 1 233 ? 24.425  52.325  27.171  1.00 32.82 ?  233 PRO J CB    1 
ATOM   9209  C  CG    . PRO G 1 233 ? 24.967  52.340  28.584  1.00 32.39 ?  233 PRO J CG    1 
ATOM   9210  C  CD    . PRO G 1 233 ? 26.467  52.175  28.398  1.00 35.16 ?  233 PRO J CD    1 
ATOM   9211  N  N     . ILE G 1 234 ? 26.413  52.392  24.634  1.00 24.85 ?  234 ILE J N     1 
ATOM   9212  C  CA    . ILE G 1 234 ? 26.622  52.831  23.261  1.00 23.75 ?  234 ILE J CA    1 
ATOM   9213  C  C     . ILE G 1 234 ? 27.580  51.894  22.524  1.00 23.72 ?  234 ILE J C     1 
ATOM   9214  O  O     . ILE G 1 234 ? 27.968  52.182  21.394  1.00 22.80 ?  234 ILE J O     1 
ATOM   9215  C  CB    . ILE G 1 234 ? 27.147  54.278  23.224  1.00 26.06 ?  234 ILE J CB    1 
ATOM   9216  C  CG1   . ILE G 1 234 ? 28.434  54.428  24.039  1.00 26.60 ?  234 ILE J CG1   1 
ATOM   9217  C  CG2   . ILE G 1 234 ? 26.070  55.266  23.674  1.00 27.06 ?  234 ILE J CG2   1 
ATOM   9218  C  CD1   . ILE G 1 234 ? 29.225  55.685  23.724  1.00 24.50 ?  234 ILE J CD1   1 
ATOM   9219  N  N     . SER G 1 235 ? 27.963  50.778  23.154  1.00 21.44 ?  235 SER J N     1 
ATOM   9220  C  CA    . SER G 1 235 ? 28.900  49.850  22.540  1.00 21.90 ?  235 SER J CA    1 
ATOM   9221  C  C     . SER G 1 235 ? 28.198  48.996  21.485  1.00 19.48 ?  235 SER J C     1 
ATOM   9222  O  O     . SER G 1 235 ? 27.134  48.436  21.740  1.00 19.86 ?  235 SER J O     1 
ATOM   9223  C  CB    . SER G 1 235 ? 29.572  48.986  23.582  1.00 21.95 ?  235 SER J CB    1 
ATOM   9224  O  OG    . SER G 1 235 ? 30.397  49.762  24.441  1.00 18.17 ?  235 SER J OG    1 
ATOM   9225  N  N     . THR G 1 236 ? 28.802  48.914  20.294  1.00 20.41 ?  236 THR J N     1 
ATOM   9226  C  CA    . THR G 1 236 ? 28.413  47.934  19.293  1.00 19.79 ?  236 THR J CA    1 
ATOM   9227  C  C     . THR G 1 236 ? 29.569  46.956  19.092  1.00 16.81 ?  236 THR J C     1 
ATOM   9228  O  O     . THR G 1 236 ? 30.734  47.337  19.179  1.00 15.61 ?  236 THR J O     1 
ATOM   9229  C  CB    . THR G 1 236 ? 28.024  48.634  17.992  1.00 21.29 ?  236 THR J CB    1 
ATOM   9230  O  OG1   . THR G 1 236 ? 26.871  49.406  18.314  1.00 22.92 ?  236 THR J OG1   1 
ATOM   9231  C  CG2   . THR G 1 236 ? 27.697  47.656  16.878  1.00 21.43 ?  236 THR J CG2   1 
ATOM   9232  N  N     . LEU G 1 237 ? 29.229  45.689  18.832  1.00 17.72 ?  237 LEU J N     1 
ATOM   9233  C  CA    . LEU G 1 237 ? 30.223  44.646  18.641  1.00 15.26 ?  237 LEU J CA    1 
ATOM   9234  C  C     . LEU G 1 237 ? 30.311  44.293  17.159  1.00 14.68 ?  237 LEU J C     1 
ATOM   9235  O  O     . LEU G 1 237 ? 29.323  43.885  16.552  1.00 15.86 ?  237 LEU J O     1 
ATOM   9236  C  CB    . LEU G 1 237 ? 29.858  43.425  19.483  1.00 15.44 ?  237 LEU J CB    1 
ATOM   9237  C  CG    . LEU G 1 237 ? 30.829  42.243  19.398  1.00 15.77 ?  237 LEU J CG    1 
ATOM   9238  C  CD1   . LEU G 1 237 ? 32.176  42.602  20.000  1.00 15.50 ?  237 LEU J CD1   1 
ATOM   9239  C  CD2   . LEU G 1 237 ? 30.248  41.015  20.072  1.00 15.92 ?  237 LEU J CD2   1 
ATOM   9240  N  N     . LEU G 1 238 ? 31.510  44.467  16.593  1.00 13.49 ?  238 LEU J N     1 
ATOM   9241  C  CA    . LEU G 1 238 ? 31.795  44.086  15.220  1.00 12.71 ?  238 LEU J CA    1 
ATOM   9242  C  C     . LEU G 1 238 ? 32.561  42.765  15.218  1.00 14.65 ?  238 LEU J C     1 
ATOM   9243  O  O     . LEU G 1 238 ? 33.578  42.631  15.893  1.00 15.21 ?  238 LEU J O     1 
ATOM   9244  C  CB    . LEU G 1 238 ? 32.605  45.186  14.539  1.00 11.77 ?  238 LEU J CB    1 
ATOM   9245  C  CG    . LEU G 1 238 ? 33.039  44.894  13.099  1.00 11.64 ?  238 LEU J CG    1 
ATOM   9246  C  CD1   . LEU G 1 238 ? 31.853  45.020  12.163  1.00 11.38 ?  238 LEU J CD1   1 
ATOM   9247  C  CD2   . LEU G 1 238 ? 34.178  45.796  12.661  1.00 11.75 ?  238 LEU J CD2   1 
ATOM   9248  N  N     . ILE G 1 239 ? 32.064  41.800  14.440  1.00 15.08 ?  239 ILE J N     1 
ATOM   9249  C  CA    . ILE G 1 239 ? 32.698  40.497  14.321  1.00 14.90 ?  239 ILE J CA    1 
ATOM   9250  C  C     . ILE G 1 239 ? 33.064  40.280  12.856  1.00 15.04 ?  239 ILE J C     1 
ATOM   9251  O  O     . ILE G 1 239 ? 32.225  39.843  12.071  1.00 17.54 ?  239 ILE J O     1 
ATOM   9252  C  CB    . ILE G 1 239 ? 31.752  39.411  14.865  1.00 15.94 ?  239 ILE J CB    1 
ATOM   9253  C  CG1   . ILE G 1 239 ? 31.338  39.731  16.302  1.00 16.03 ?  239 ILE J CG1   1 
ATOM   9254  C  CG2   . ILE G 1 239 ? 32.360  38.012  14.743  1.00 16.16 ?  239 ILE J CG2   1 
ATOM   9255  C  CD1   . ILE G 1 239 ? 30.313  38.778  16.888  1.00 16.52 ?  239 ILE J CD1   1 
ATOM   9256  N  N     . PRO G 1 240 ? 34.308  40.604  12.431  1.00 13.60 ?  240 PRO J N     1 
ATOM   9257  C  CA    . PRO G 1 240 ? 34.664  40.555  11.013  1.00 14.24 ?  240 PRO J CA    1 
ATOM   9258  C  C     . PRO G 1 240 ? 34.463  39.146  10.466  1.00 17.16 ?  240 PRO J C     1 
ATOM   9259  O  O     . PRO G 1 240 ? 34.225  38.214  11.231  1.00 16.54 ?  240 PRO J O     1 
ATOM   9260  C  CB    . PRO G 1 240 ? 36.137  40.999  10.993  1.00 14.38 ?  240 PRO J CB    1 
ATOM   9261  C  CG    . PRO G 1 240 ? 36.302  41.778  12.281  1.00 13.93 ?  240 PRO J CG    1 
ATOM   9262  C  CD    . PRO G 1 240 ? 35.434  41.029  13.279  1.00 13.73 ?  240 PRO J CD    1 
ATOM   9263  N  N     . PRO G 1 241 ? 34.545  38.944  9.131   1.00 18.41 ?  241 PRO J N     1 
ATOM   9264  C  CA    . PRO G 1 241 ? 34.378  37.611  8.555   1.00 21.63 ?  241 PRO J CA    1 
ATOM   9265  C  C     . PRO G 1 241 ? 35.342  36.620  9.197   1.00 20.73 ?  241 PRO J C     1 
ATOM   9266  O  O     . PRO G 1 241 ? 36.500  36.943  9.452   1.00 19.55 ?  241 PRO J O     1 
ATOM   9267  C  CB    . PRO G 1 241 ? 34.663  37.801  7.055   1.00 21.90 ?  241 PRO J CB    1 
ATOM   9268  C  CG    . PRO G 1 241 ? 34.441  39.278  6.810   1.00 20.70 ?  241 PRO J CG    1 
ATOM   9269  C  CD    . PRO G 1 241 ? 34.799  39.976  8.115   1.00 21.92 ?  241 PRO J CD    1 
ATOM   9270  N  N     . ALA G 1 242 ? 34.837  35.412  9.456   1.00 21.69 ?  242 ALA J N     1 
ATOM   9271  C  CA    . ALA G 1 242 ? 35.669  34.307  9.898   1.00 21.93 ?  242 ALA J CA    1 
ATOM   9272  C  C     . ALA G 1 242 ? 36.273  33.606  8.684   1.00 25.19 ?  242 ALA J C     1 
ATOM   9273  O  O     . ALA G 1 242 ? 37.300  32.940  8.799   1.00 28.74 ?  242 ALA J O     1 
ATOM   9274  C  CB    . ALA G 1 242 ? 34.850  33.353  10.740  1.00 19.88 ?  242 ALA J CB    1 
ATOM   9275  N  N     . LYS G 1 243 ? 35.624  33.764  7.523   1.00 25.55 ?  243 LYS J N     1 
ATOM   9276  C  CA    . LYS G 1 243 ? 36.055  33.102  6.301   1.00 31.32 ?  243 LYS J CA    1 
ATOM   9277  C  C     . LYS G 1 243 ? 36.164  34.105  5.156   1.00 36.20 ?  243 LYS J C     1 
ATOM   9278  O  O     . LYS G 1 243 ? 35.608  35.199  5.218   1.00 42.81 ?  243 LYS J O     1 
ATOM   9279  C  CB    . LYS G 1 243 ? 35.069  32.001  5.894   1.00 31.25 ?  243 LYS J CB    1 
ATOM   9280  C  CG    . LYS G 1 243 ? 35.007  30.808  6.835   1.00 31.56 ?  243 LYS J CG    1 
ATOM   9281  C  CD    . LYS G 1 243 ? 33.674  30.071  6.817   1.00 32.01 ?  243 LYS J CD    1 
ATOM   9282  C  CE    . LYS G 1 243 ? 33.200  29.729  5.442   1.00 35.13 ?  243 LYS J CE    1 
ATOM   9283  N  NZ    . LYS G 1 243 ? 31.888  29.077  5.486   1.00 37.94 1  243 LYS J NZ    1 
ATOM   9284  N  N     . LYS G 1 244 ? 36.888  33.698  4.108   1.00 35.42 ?  244 LYS J N     1 
ATOM   9285  C  CA    . LYS G 1 244 ? 37.010  34.478  2.888   1.00 36.34 ?  244 LYS J CA    1 
ATOM   9286  C  C     . LYS G 1 244 ? 35.934  34.016  1.909   1.00 31.81 ?  244 LYS J C     1 
ATOM   9287  O  O     . LYS G 1 244 ? 35.432  32.899  2.017   1.00 24.99 ?  244 LYS J O     1 
ATOM   9288  C  CB    . LYS G 1 244 ? 38.414  34.296  2.301   1.00 39.71 ?  244 LYS J CB    1 
ATOM   9289  C  CG    . LYS G 1 244 ? 39.549  34.488  3.299   1.00 43.62 ?  244 LYS J CG    1 
ATOM   9290  C  CD    . LYS G 1 244 ? 40.803  33.683  2.978   1.00 46.99 ?  244 LYS J CD    1 
ATOM   9291  C  CE    . LYS G 1 244 ? 41.736  33.587  4.145   1.00 49.38 ?  244 LYS J CE    1 
ATOM   9292  N  NZ    . LYS G 1 244 ? 42.871  32.702  3.869   1.00 49.90 1  244 LYS J NZ    1 
ATOM   9293  N  N     . LEU G 1 245 ? 35.585  34.887  0.957   1.00 34.07 ?  245 LEU J N     1 
ATOM   9294  C  CA    . LEU G 1 245 ? 34.567  34.571  -0.031  1.00 36.39 ?  245 LEU J CA    1 
ATOM   9295  C  C     . LEU G 1 245 ? 35.031  33.378  -0.865  1.00 35.63 ?  245 LEU J C     1 
ATOM   9296  O  O     . LEU G 1 245 ? 36.135  33.385  -1.404  1.00 33.40 ?  245 LEU J O     1 
ATOM   9297  C  CB    . LEU G 1 245 ? 34.268  35.779  -0.918  1.00 36.21 ?  245 LEU J CB    1 
ATOM   9298  C  CG    . LEU G 1 245 ? 33.654  36.999  -0.223  1.00 36.36 ?  245 LEU J CG    1 
ATOM   9299  C  CD1   . LEU G 1 245 ? 32.561  36.576  0.745   1.00 40.20 ?  245 LEU J CD1   1 
ATOM   9300  C  CD2   . LEU G 1 245 ? 34.707  37.833  0.483   1.00 37.05 ?  245 LEU J CD2   1 
ATOM   9301  N  N     . GLU G 1 246 ? 34.171  32.357  -0.952  1.00 38.38 ?  246 GLU J N     1 
ATOM   9302  C  CA    . GLU G 1 246 ? 34.416  31.204  -1.803  1.00 41.50 ?  246 GLU J CA    1 
ATOM   9303  C  C     . GLU G 1 246 ? 33.400  31.205  -2.945  1.00 40.44 ?  246 GLU J C     1 
ATOM   9304  O  O     . GLU G 1 246 ? 32.292  31.719  -2.797  1.00 36.37 ?  246 GLU J O     1 
ATOM   9305  C  CB    . GLU G 1 246 ? 34.372  29.912  -0.983  1.00 44.67 ?  246 GLU J CB    1 
ATOM   9306  C  CG    . GLU G 1 246 ? 35.390  29.880  0.154   1.00 49.24 ?  246 GLU J CG    1 
ATOM   9307  C  CD    . GLU G 1 246 ? 35.470  28.562  0.903   1.00 55.50 ?  246 GLU J CD    1 
ATOM   9308  O  OE1   . GLU G 1 246 ? 36.026  27.593  0.342   1.00 55.00 ?  246 GLU J OE1   1 
ATOM   9309  O  OE2   . GLU G 1 246 ? 34.968  28.500  2.045   1.00 66.74 -1 246 GLU J OE2   1 
ATOM   9310  N  N     . TYR G 1 247 ? 33.799  30.619  -4.081  1.00 37.38 ?  247 TYR J N     1 
ATOM   9311  C  CA    . TYR G 1 247 ? 33.042  30.695  -5.322  1.00 34.71 ?  247 TYR J CA    1 
ATOM   9312  C  C     . TYR G 1 247 ? 31.810  29.791  -5.234  1.00 32.65 ?  247 TYR J C     1 
ATOM   9313  O  O     . TYR G 1 247 ? 31.831  28.771  -4.548  1.00 28.63 ?  247 TYR J O     1 
ATOM   9314  C  CB    . TYR G 1 247 ? 33.970  30.338  -6.492  1.00 32.56 ?  247 TYR J CB    1 
ATOM   9315  C  CG    . TYR G 1 247 ? 35.044  31.364  -6.843  1.00 29.87 ?  247 TYR J CG    1 
ATOM   9316  C  CD1   . TYR G 1 247 ? 34.720  32.541  -7.508  1.00 29.98 ?  247 TYR J CD1   1 
ATOM   9317  C  CD2   . TYR G 1 247 ? 36.388  31.141  -6.554  1.00 28.08 ?  247 TYR J CD2   1 
ATOM   9318  C  CE1   . TYR G 1 247 ? 35.687  33.476  -7.843  1.00 28.03 ?  247 TYR J CE1   1 
ATOM   9319  C  CE2   . TYR G 1 247 ? 37.365  32.067  -6.888  1.00 25.54 ?  247 TYR J CE2   1 
ATOM   9320  C  CZ    . TYR G 1 247 ? 37.013  33.240  -7.533  1.00 26.56 ?  247 TYR J CZ    1 
ATOM   9321  O  OH    . TYR G 1 247 ? 37.960  34.167  -7.872  1.00 21.46 ?  247 TYR J OH    1 
ATOM   9322  N  N     . ASN G 1 248 ? 30.740  30.185  -5.940  1.00 32.01 ?  248 ASN J N     1 
ATOM   9323  C  CA    . ASN G 1 248 ? 29.469  29.474  -5.923  1.00 28.40 ?  248 ASN J CA    1 
ATOM   9324  C  C     . ASN G 1 248 ? 29.281  28.755  -7.260  1.00 28.48 ?  248 ASN J C     1 
ATOM   9325  O  O     . ASN G 1 248 ? 28.445  29.145  -8.073  1.00 22.79 ?  248 ASN J O     1 
ATOM   9326  C  CB    . ASN G 1 248 ? 28.323  30.428  -5.598  1.00 29.28 ?  248 ASN J CB    1 
ATOM   9327  C  CG    . ASN G 1 248 ? 27.058  29.715  -5.183  1.00 27.58 ?  248 ASN J CG    1 
ATOM   9328  O  OD1   . ASN G 1 248 ? 26.965  28.488  -5.304  1.00 24.99 ?  248 ASN J OD1   1 
ATOM   9329  N  ND2   . ASN G 1 248 ? 26.078  30.461  -4.695  1.00 25.99 ?  248 ASN J ND2   1 
ATOM   9330  N  N     . TYR G 1 249 ? 30.064  27.687  -7.461  1.00 29.20 ?  249 TYR J N     1 
ATOM   9331  C  CA    . TYR G 1 249 ? 30.128  26.974  -8.728  1.00 26.41 ?  249 TYR J CA    1 
ATOM   9332  C  C     . TYR G 1 249 ? 28.724  26.598  -9.194  1.00 25.75 ?  249 TYR J C     1 
ATOM   9333  O  O     . TYR G 1 249 ? 28.431  26.624  -10.389 1.00 23.60 ?  249 TYR J O     1 
ATOM   9334  C  CB    . TYR G 1 249 ? 31.028  25.743  -8.570  1.00 25.41 ?  249 TYR J CB    1 
ATOM   9335  C  CG    . TYR G 1 249 ? 32.503  26.080  -8.391  1.00 24.36 ?  249 TYR J CG    1 
ATOM   9336  C  CD1   . TYR G 1 249 ? 33.274  26.491  -9.470  1.00 23.89 ?  249 TYR J CD1   1 
ATOM   9337  C  CD2   . TYR G 1 249 ? 33.123  25.984  -7.151  1.00 24.21 ?  249 TYR J CD2   1 
ATOM   9338  C  CE1   . TYR G 1 249 ? 34.614  26.804  -9.323  1.00 24.54 ?  249 TYR J CE1   1 
ATOM   9339  C  CE2   . TYR G 1 249 ? 34.464  26.292  -6.990  1.00 22.51 ?  249 TYR J CE2   1 
ATOM   9340  C  CZ    . TYR G 1 249 ? 35.212  26.703  -8.079  1.00 25.63 ?  249 TYR J CZ    1 
ATOM   9341  O  OH    . TYR G 1 249 ? 36.534  27.007  -7.927  1.00 25.73 ?  249 TYR J OH    1 
ATOM   9342  N  N     . ALA G 1 250 ? 27.868  26.246  -8.233  1.00 26.55 ?  250 ALA J N     1 
ATOM   9343  C  CA    . ALA G 1 250 ? 26.508  25.818  -8.516  1.00 29.20 ?  250 ALA J CA    1 
ATOM   9344  C  C     . ALA G 1 250 ? 25.813  26.819  -9.437  1.00 28.62 ?  250 ALA J C     1 
ATOM   9345  O  O     . ALA G 1 250 ? 25.254  26.438  -10.463 1.00 31.42 ?  250 ALA J O     1 
ATOM   9346  C  CB    . ALA G 1 250 ? 25.759  25.645  -7.212  1.00 29.07 ?  250 ALA J CB    1 
ATOM   9347  N  N     . ILE G 1 251 ? 25.858  28.103  -9.061  1.00 29.38 ?  251 ILE J N     1 
ATOM   9348  C  CA    . ILE G 1 251 ? 25.126  29.146  -9.763  1.00 25.04 ?  251 ILE J CA    1 
ATOM   9349  C  C     . ILE G 1 251 ? 25.938  29.601  -10.973 1.00 23.36 ?  251 ILE J C     1 
ATOM   9350  O  O     . ILE G 1 251 ? 25.384  29.821  -12.048 1.00 21.70 ?  251 ILE J O     1 
ATOM   9351  C  CB    . ILE G 1 251 ? 24.805  30.317  -8.814  1.00 26.69 ?  251 ILE J CB    1 
ATOM   9352  C  CG1   . ILE G 1 251 ? 24.123  29.834  -7.531  1.00 28.93 ?  251 ILE J CG1   1 
ATOM   9353  C  CG2   . ILE G 1 251 ? 23.980  31.392  -9.522  1.00 24.83 ?  251 ILE J CG2   1 
ATOM   9354  C  CD1   . ILE G 1 251 ? 22.790  29.141  -7.755  1.00 28.47 ?  251 ILE J CD1   1 
ATOM   9355  N  N     . LEU G 1 252 ? 27.253  29.748  -10.778 1.00 23.87 ?  252 LEU J N     1 
ATOM   9356  C  CA    . LEU G 1 252 ? 28.164  30.090  -11.857 1.00 28.49 ?  252 LEU J CA    1 
ATOM   9357  C  C     . LEU G 1 252 ? 27.824  29.252  -13.088 1.00 30.34 ?  252 LEU J C     1 
ATOM   9358  O  O     . LEU G 1 252 ? 27.793  29.764  -14.206 1.00 26.36 ?  252 LEU J O     1 
ATOM   9359  C  CB    . LEU G 1 252 ? 29.606  29.862  -11.401 1.00 30.75 ?  252 LEU J CB    1 
ATOM   9360  C  CG    . LEU G 1 252 ? 30.287  31.017  -10.658 1.00 35.48 ?  252 LEU J CG    1 
ATOM   9361  C  CD1   . LEU G 1 252 ? 30.745  32.086  -11.635 1.00 36.02 ?  252 LEU J CD1   1 
ATOM   9362  C  CD2   . LEU G 1 252 ? 29.392  31.635  -9.598  1.00 39.48 ?  252 LEU J CD2   1 
ATOM   9363  N  N     . ALA G 1 253 ? 27.565  27.960  -12.858 1.00 31.35 ?  253 ALA J N     1 
ATOM   9364  C  CA    . ALA G 1 253 ? 27.284  27.018  -13.929 1.00 32.30 ?  253 ALA J CA    1 
ATOM   9365  C  C     . ALA G 1 253 ? 25.957  27.363  -14.602 1.00 35.73 ?  253 ALA J C     1 
ATOM   9366  O  O     . ALA G 1 253 ? 25.880  27.400  -15.828 1.00 38.13 ?  253 ALA J O     1 
ATOM   9367  C  CB    . ALA G 1 253 ? 27.286  25.604  -13.391 1.00 33.01 ?  253 ALA J CB    1 
ATOM   9368  N  N     . LYS G 1 254 ? 24.911  27.613  -13.807 1.00 35.82 ?  254 LYS J N     1 
ATOM   9369  C  CA    . LYS G 1 254 ? 23.631  27.983  -14.388 1.00 37.35 ?  254 LYS J CA    1 
ATOM   9370  C  C     . LYS G 1 254 ? 23.829  29.237  -15.239 1.00 35.71 ?  254 LYS J C     1 
ATOM   9371  O  O     . LYS G 1 254 ? 23.187  29.393  -16.275 1.00 32.36 ?  254 LYS J O     1 
ATOM   9372  C  CB    . LYS G 1 254 ? 22.527  28.191  -13.345 1.00 38.88 ?  254 LYS J CB    1 
ATOM   9373  C  CG    . LYS G 1 254 ? 22.215  26.979  -12.477 1.00 39.74 ?  254 LYS J CG    1 
ATOM   9374  C  CD    . LYS G 1 254 ? 20.869  27.070  -11.768 1.00 41.20 ?  254 LYS J CD    1 
ATOM   9375  C  CE    . LYS G 1 254 ? 20.705  26.043  -10.692 1.00 44.70 ?  254 LYS J CE    1 
ATOM   9376  N  NZ    . LYS G 1 254 ? 20.744  24.677  -11.220 1.00 43.50 1  254 LYS J NZ    1 
ATOM   9377  N  N     . LEU G 1 255 ? 24.733  30.120  -14.793 1.00 31.86 ?  255 LEU J N     1 
ATOM   9378  C  CA    . LEU G 1 255 ? 25.054  31.337  -15.524 1.00 31.78 ?  255 LEU J CA    1 
ATOM   9379  C  C     . LEU G 1 255 ? 25.991  31.008  -16.684 1.00 34.90 ?  255 LEU J C     1 
ATOM   9380  O  O     . LEU G 1 255 ? 26.272  31.865  -17.518 1.00 30.52 ?  255 LEU J O     1 
ATOM   9381  C  CB    . LEU G 1 255 ? 25.684  32.382  -14.603 1.00 34.09 ?  255 LEU J CB    1 
ATOM   9382  C  CG    . LEU G 1 255 ? 24.767  33.019  -13.555 1.00 35.18 ?  255 LEU J CG    1 
ATOM   9383  C  CD1   . LEU G 1 255 ? 25.611  33.767  -12.539 1.00 36.11 ?  255 LEU J CD1   1 
ATOM   9384  C  CD2   . LEU G 1 255 ? 23.742  33.951  -14.179 1.00 37.46 ?  255 LEU J CD2   1 
ATOM   9385  N  N     . GLY G 1 256 ? 26.486  29.766  -16.713 1.00 39.54 ?  256 GLY J N     1 
ATOM   9386  C  CA    . GLY G 1 256 ? 27.340  29.301  -17.794 1.00 35.74 ?  256 GLY J CA    1 
ATOM   9387  C  C     . GLY G 1 256 ? 28.696  30.003  -17.789 1.00 36.78 ?  256 GLY J C     1 
ATOM   9388  O  O     . GLY G 1 256 ? 29.322  30.154  -18.835 1.00 38.51 ?  256 GLY J O     1 
ATOM   9389  N  N     . ILE G 1 257 ? 29.143  30.427  -16.602 1.00 36.19 ?  257 ILE J N     1 
ATOM   9390  C  CA    . ILE G 1 257 ? 30.454  31.040  -16.460 1.00 38.15 ?  257 ILE J CA    1 
ATOM   9391  C  C     . ILE G 1 257 ? 31.224  30.325  -15.353 1.00 34.27 ?  257 ILE J C     1 
ATOM   9392  O  O     . ILE G 1 257 ? 30.747  29.345  -14.785 1.00 37.58 ?  257 ILE J O     1 
ATOM   9393  C  CB    . ILE G 1 257 ? 30.337  32.550  -16.179 1.00 39.61 ?  257 ILE J CB    1 
ATOM   9394  C  CG1   . ILE G 1 257 ? 29.756  32.821  -14.790 1.00 39.52 ?  257 ILE J CG1   1 
ATOM   9395  C  CG2   . ILE G 1 257 ? 29.534  33.245  -17.279 1.00 47.49 ?  257 ILE J CG2   1 
ATOM   9396  C  CD1   . ILE G 1 257 ? 29.921  34.253  -14.314 1.00 38.92 ?  257 ILE J CD1   1 
ATOM   9397  N  N     . GLY G 1 258 ? 32.427  30.834  -15.069 1.00 33.85 ?  258 GLY J N     1 
ATOM   9398  C  CA    . GLY G 1 258 ? 33.256  30.333  -13.986 1.00 31.74 ?  258 GLY J CA    1 
ATOM   9399  C  C     . GLY G 1 258 ? 34.083  31.455  -13.364 1.00 33.71 ?  258 GLY J C     1 
ATOM   9400  O  O     . GLY G 1 258 ? 34.059  32.590  -13.837 1.00 28.92 ?  258 GLY J O     1 
ATOM   9401  N  N     . PRO G 1 259 ? 34.834  31.167  -12.278 1.00 32.71 ?  259 PRO J N     1 
ATOM   9402  C  CA    . PRO G 1 259 ? 35.654  32.178  -11.605 1.00 36.96 ?  259 PRO J CA    1 
ATOM   9403  C  C     . PRO G 1 259 ? 36.431  33.137  -12.505 1.00 47.67 ?  259 PRO J C     1 
ATOM   9404  O  O     . PRO G 1 259 ? 36.391  34.348  -12.295 1.00 57.03 ?  259 PRO J O     1 
ATOM   9405  C  CB    . PRO G 1 259 ? 36.593  31.287  -10.771 1.00 36.10 ?  259 PRO J CB    1 
ATOM   9406  C  CG    . PRO G 1 259 ? 35.722  30.118  -10.377 1.00 34.59 ?  259 PRO J CG    1 
ATOM   9407  C  CD    . PRO G 1 259 ? 34.897  29.850  -11.623 1.00 34.09 ?  259 PRO J CD    1 
ATOM   9408  N  N     . GLU G 1 260 ? 37.143  32.596  -13.501 1.00 49.87 ?  260 GLU J N     1 
ATOM   9409  C  CA    . GLU G 1 260 ? 38.060  33.405  -14.288 1.00 50.01 ?  260 GLU J CA    1 
ATOM   9410  C  C     . GLU G 1 260 ? 37.271  34.225  -15.308 1.00 46.41 ?  260 GLU J C     1 
ATOM   9411  O  O     . GLU G 1 260 ? 37.807  35.159  -15.900 1.00 38.50 ?  260 GLU J O     1 
ATOM   9412  C  CB    . GLU G 1 260 ? 39.158  32.577  -14.960 1.00 50.37 ?  260 GLU J CB    1 
ATOM   9413  C  CG    . GLU G 1 260 ? 38.745  31.948  -16.287 1.00 51.74 ?  260 GLU J CG    1 
ATOM   9414  C  CD    . GLU G 1 260 ? 39.909  31.544  -17.177 1.00 51.87 ?  260 GLU J CD    1 
ATOM   9415  O  OE1   . GLU G 1 260 ? 39.652  31.166  -18.340 1.00 44.98 ?  260 GLU J OE1   1 
ATOM   9416  O  OE2   . GLU G 1 260 ? 41.068  31.606  -16.713 1.00 57.29 -1 260 GLU J OE2   1 
ATOM   9417  N  N     . ASP G 1 261 ? 35.993  33.877  -15.500 1.00 44.37 ?  261 ASP J N     1 
ATOM   9418  C  CA    . ASP G 1 261 ? 35.135  34.610  -16.417 1.00 39.53 ?  261 ASP J CA    1 
ATOM   9419  C  C     . ASP G 1 261 ? 34.539  35.825  -15.708 1.00 37.36 ?  261 ASP J C     1 
ATOM   9420  O  O     . ASP G 1 261 ? 33.743  36.556  -16.292 1.00 37.05 ?  261 ASP J O     1 
ATOM   9421  C  CB    . ASP G 1 261 ? 34.069  33.712  -17.028 1.00 39.08 ?  261 ASP J CB    1 
ATOM   9422  C  CG    . ASP G 1 261 ? 34.593  32.627  -17.957 1.00 35.86 ?  261 ASP J CG    1 
ATOM   9423  O  OD1   . ASP G 1 261 ? 35.372  32.966  -18.872 1.00 30.42 ?  261 ASP J OD1   1 
ATOM   9424  O  OD2   . ASP G 1 261 ? 34.213  31.454  -17.763 1.00 42.01 -1 261 ASP J OD2   1 
ATOM   9425  N  N     . LEU G 1 262 ? 34.938  36.031  -14.448 1.00 33.69 ?  262 LEU J N     1 
ATOM   9426  C  CA    . LEU G 1 262 ? 34.519  37.195  -13.683 1.00 42.27 ?  262 LEU J CA    1 
ATOM   9427  C  C     . LEU G 1 262 ? 35.436  38.372  -14.005 1.00 43.30 ?  262 LEU J C     1 
ATOM   9428  O  O     . LEU G 1 262 ? 36.651  38.211  -14.098 1.00 51.09 ?  262 LEU J O     1 
ATOM   9429  C  CB    . LEU G 1 262 ? 34.532  36.849  -12.195 1.00 40.12 ?  262 LEU J CB    1 
ATOM   9430  C  CG    . LEU G 1 262 ? 33.458  35.857  -11.737 1.00 37.10 ?  262 LEU J CG    1 
ATOM   9431  C  CD1   . LEU G 1 262 ? 33.785  35.210  -10.403 1.00 32.48 ?  262 LEU J CD1   1 
ATOM   9432  C  CD2   . LEU G 1 262 ? 32.114  36.562  -11.666 1.00 40.99 ?  262 LEU J CD2   1 
ATOM   9433  N  N     . GLY G 1 263 ? 34.834  39.555  -14.172 1.00 37.53 ?  263 GLY J N     1 
ATOM   9434  C  CA    . GLY G 1 263 ? 35.570  40.762  -14.509 1.00 39.14 ?  263 GLY J CA    1 
ATOM   9435  C  C     . GLY G 1 263 ? 36.157  41.416  -13.272 1.00 32.85 ?  263 GLY J C     1 
ATOM   9436  O  O     . GLY G 1 263 ? 37.237  42.028  -13.410 1.00 30.22 ?  263 GLY J O     1 
ATOM   9437  O  OXT   . GLY G 1 263 ? 35.518  41.296  -12.206 1.00 29.22 -1 263 GLY J OXT   1 
ATOM   9438  N  N     . LEU H 3 11  ? 32.642  76.266  26.963  1.00 24.61 ?  4   LEU K N     1 
ATOM   9439  C  CA    . LEU H 3 11  ? 33.153  74.936  26.537  1.00 26.49 ?  4   LEU K CA    1 
ATOM   9440  C  C     . LEU H 3 11  ? 32.124  74.278  25.620  1.00 24.72 ?  4   LEU K C     1 
ATOM   9441  O  O     . LEU H 3 11  ? 32.470  73.729  24.577  1.00 23.89 ?  4   LEU K O     1 
ATOM   9442  C  CB    . LEU H 3 11  ? 33.437  74.089  27.777  1.00 30.16 ?  4   LEU K CB    1 
ATOM   9443  C  CG    . LEU H 3 11  ? 34.167  72.763  27.544  1.00 35.31 ?  4   LEU K CG    1 
ATOM   9444  C  CD1   . LEU H 3 11  ? 35.400  72.938  26.676  1.00 35.75 ?  4   LEU K CD1   1 
ATOM   9445  C  CD2   . LEU H 3 11  ? 34.544  72.148  28.880  1.00 40.80 ?  4   LEU K CD2   1 
ATOM   9446  N  N     . SER H 3 12  ? 30.854  74.355  26.028  1.00 25.09 ?  5   SER K N     1 
ATOM   9447  C  CA    . SER H 3 12  ? 29.753  73.796  25.263  1.00 26.34 ?  5   SER K CA    1 
ATOM   9448  C  C     . SER H 3 12  ? 29.548  74.598  23.978  1.00 25.86 ?  5   SER K C     1 
ATOM   9449  O  O     . SER H 3 12  ? 29.042  74.072  22.990  1.00 26.79 ?  5   SER K O     1 
ATOM   9450  C  CB    . SER H 3 12  ? 28.498  73.742  26.103  1.00 23.94 ?  5   SER K CB    1 
ATOM   9451  O  OG    . SER H 3 12  ? 27.377  73.315  25.341  1.00 24.29 ?  5   SER K OG    1 
ATOM   9452  N  N     . ASP H 3 13  ? 29.963  75.871  24.005  1.00 26.79 ?  6   ASP K N     1 
ATOM   9453  C  CA    . ASP H 3 13  ? 29.852  76.758  22.857  1.00 28.07 ?  6   ASP K CA    1 
ATOM   9454  C  C     . ASP H 3 13  ? 30.926  76.425  21.824  1.00 25.31 ?  6   ASP K C     1 
ATOM   9455  O  O     . ASP H 3 13  ? 30.674  76.490  20.622  1.00 21.94 ?  6   ASP K O     1 
ATOM   9456  C  CB    . ASP H 3 13  ? 29.952  78.218  23.270  1.00 27.99 ?  6   ASP K CB    1 
ATOM   9457  C  CG    . ASP H 3 13  ? 28.734  78.776  23.991  1.00 31.96 ?  6   ASP K CG    1 
ATOM   9458  O  OD1   . ASP H 3 13  ? 27.725  78.046  24.089  1.00 33.19 ?  6   ASP K OD1   1 
ATOM   9459  O  OD2   . ASP H 3 13  ? 28.804  79.936  24.448  1.00 30.36 -1 6   ASP K OD2   1 
ATOM   9460  N  N     . PHE H 3 14  ? 32.130  76.092  22.302  1.00 23.16 ?  7   PHE K N     1 
ATOM   9461  C  CA    . PHE H 3 14  ? 33.240  75.796  21.412  1.00 23.37 ?  7   PHE K CA    1 
ATOM   9462  C  C     . PHE H 3 14  ? 32.925  74.514  20.645  1.00 24.63 ?  7   PHE K C     1 
ATOM   9463  O  O     . PHE H 3 14  ? 33.135  74.448  19.435  1.00 28.63 ?  7   PHE K O     1 
ATOM   9464  C  CB    . PHE H 3 14  ? 34.561  75.715  22.185  1.00 24.01 ?  7   PHE K CB    1 
ATOM   9465  C  CG    . PHE H 3 14  ? 35.713  75.146  21.367  1.00 25.38 ?  7   PHE K CG    1 
ATOM   9466  C  CD1   . PHE H 3 14  ? 36.313  75.895  20.360  1.00 24.90 ?  7   PHE K CD1   1 
ATOM   9467  C  CD2   . PHE H 3 14  ? 36.189  73.862  21.605  1.00 25.50 ?  7   PHE K CD2   1 
ATOM   9468  C  CE1   . PHE H 3 14  ? 37.356  75.370  19.613  1.00 25.63 ?  7   PHE K CE1   1 
ATOM   9469  C  CE2   . PHE H 3 14  ? 37.236  73.345  20.857  1.00 26.11 ?  7   PHE K CE2   1 
ATOM   9470  C  CZ    . PHE H 3 14  ? 37.815  74.098  19.863  1.00 25.28 ?  7   PHE K CZ    1 
ATOM   9471  N  N     . PHE H 3 15  ? 32.401  73.507  21.355  1.00 23.59 ?  8   PHE K N     1 
ATOM   9472  C  CA    . PHE H 3 15  ? 32.160  72.198  20.767  1.00 23.35 ?  8   PHE K CA    1 
ATOM   9473  C  C     . PHE H 3 15  ? 31.081  72.297  19.688  1.00 22.71 ?  8   PHE K C     1 
ATOM   9474  O  O     . PHE H 3 15  ? 31.184  71.635  18.658  1.00 20.50 ?  8   PHE K O     1 
ATOM   9475  C  CB    . PHE H 3 15  ? 31.783  71.157  21.827  1.00 22.85 ?  8   PHE K CB    1 
ATOM   9476  C  CG    . PHE H 3 15  ? 32.883  70.791  22.817  1.00 24.94 ?  8   PHE K CG    1 
ATOM   9477  C  CD1   . PHE H 3 15  ? 34.221  71.059  22.543  1.00 24.84 ?  8   PHE K CD1   1 
ATOM   9478  C  CD2   . PHE H 3 15  ? 32.575  70.151  24.013  1.00 25.83 ?  8   PHE K CD2   1 
ATOM   9479  C  CE1   . PHE H 3 15  ? 35.213  70.717  23.450  1.00 26.34 ?  8   PHE K CE1   1 
ATOM   9480  C  CE2   . PHE H 3 15  ? 33.571  69.808  24.913  1.00 27.33 ?  8   PHE K CE2   1 
ATOM   9481  C  CZ    . PHE H 3 15  ? 34.886  70.091  24.631  1.00 27.63 ?  8   PHE K CZ    1 
ATOM   9482  N  N     . THR H 3 16  ? 30.042  73.111  19.926  1.00 20.88 ?  9   THR K N     1 
ATOM   9483  C  CA    . THR H 3 16  ? 28.954  73.251  18.967  1.00 19.38 ?  9   THR K CA    1 
ATOM   9484  C  C     . THR H 3 16  ? 29.512  73.838  17.673  1.00 18.31 ?  9   THR K C     1 
ATOM   9485  O  O     . THR H 3 16  ? 29.252  73.317  16.589  1.00 14.00 ?  9   THR K O     1 
ATOM   9486  C  CB    . THR H 3 16  ? 27.826  74.109  19.541  1.00 19.98 ?  9   THR K CB    1 
ATOM   9487  O  OG1   . THR H 3 16  ? 27.146  73.293  20.490  1.00 19.64 ?  9   THR K OG1   1 
ATOM   9488  C  CG2   . THR H 3 16  ? 26.834  74.562  18.484  1.00 17.29 ?  9   THR K CG2   1 
ATOM   9489  N  N     . GLN H 3 17  ? 30.284  74.923  17.804  1.00 21.25 ?  10  GLN K N     1 
ATOM   9490  C  CA    . GLN H 3 17  ? 30.962  75.532  16.671  1.00 21.44 ?  10  GLN K CA    1 
ATOM   9491  C  C     . GLN H 3 17  ? 31.755  74.457  15.931  1.00 19.76 ?  10  GLN K C     1 
ATOM   9492  O  O     . GLN H 3 17  ? 31.458  74.137  14.782  1.00 18.83 ?  10  GLN K O     1 
ATOM   9493  C  CB    . GLN H 3 17  ? 31.905  76.655  17.115  1.00 22.05 ?  10  GLN K CB    1 
ATOM   9494  C  CG    . GLN H 3 17  ? 31.207  77.869  17.722  1.00 23.18 ?  10  GLN K CG    1 
ATOM   9495  C  CD    . GLN H 3 17  ? 32.163  78.859  18.353  1.00 24.85 ?  10  GLN K CD    1 
ATOM   9496  O  OE1   . GLN H 3 17  ? 33.380  78.811  18.143  1.00 30.92 ?  10  GLN K OE1   1 
ATOM   9497  N  NE2   . GLN H 3 17  ? 31.615  79.778  19.136  1.00 24.37 ?  10  GLN K NE2   1 
ATOM   9498  N  N     . LEU H 3 18  ? 32.752  73.901  16.630  1.00 18.32 ?  11  LEU K N     1 
ATOM   9499  C  CA    . LEU H 3 18  ? 33.722  72.975  16.065  1.00 16.59 ?  11  LEU K CA    1 
ATOM   9500  C  C     . LEU H 3 18  ? 33.020  71.879  15.267  1.00 16.43 ?  11  LEU K C     1 
ATOM   9501  O  O     . LEU H 3 18  ? 33.444  71.544  14.164  1.00 17.18 ?  11  LEU K O     1 
ATOM   9502  C  CB    . LEU H 3 18  ? 34.552  72.399  17.215  1.00 16.07 ?  11  LEU K CB    1 
ATOM   9503  C  CG    . LEU H 3 18  ? 35.581  71.323  16.849  1.00 16.25 ?  11  LEU K CG    1 
ATOM   9504  C  CD1   . LEU H 3 18  ? 36.545  71.830  15.792  1.00 15.85 ?  11  LEU K CD1   1 
ATOM   9505  C  CD2   . LEU H 3 18  ? 36.348  70.847  18.075  1.00 17.25 ?  11  LEU K CD2   1 
ATOM   9506  N  N     . GLY H 3 19  ? 31.946  71.327  15.839  1.00 14.62 ?  12  GLY K N     1 
ATOM   9507  C  CA    . GLY H 3 19  ? 31.266  70.180  15.261  1.00 15.29 ?  12  GLY K CA    1 
ATOM   9508  C  C     . GLY H 3 19  ? 30.507  70.536  13.985  1.00 15.13 ?  12  GLY K C     1 
ATOM   9509  O  O     . GLY H 3 19  ? 30.130  69.649  13.221  1.00 13.58 ?  12  GLY K O     1 
ATOM   9510  N  N     . GLN H 3 20  ? 30.291  71.838  13.763  1.00 17.95 ?  13  GLN K N     1 
ATOM   9511  C  CA    . GLN H 3 20  ? 29.477  72.310  12.653  1.00 18.46 ?  13  GLN K CA    1 
ATOM   9512  C  C     . GLN H 3 20  ? 30.325  73.033  11.607  1.00 17.28 ?  13  GLN K C     1 
ATOM   9513  O  O     . GLN H 3 20  ? 29.933  73.108  10.445  1.00 14.80 ?  13  GLN K O     1 
ATOM   9514  C  CB    . GLN H 3 20  ? 28.393  73.265  13.151  1.00 25.22 ?  13  GLN K CB    1 
ATOM   9515  C  CG    . GLN H 3 20  ? 27.243  72.584  13.884  1.00 29.99 ?  13  GLN K CG    1 
ATOM   9516  C  CD    . GLN H 3 20  ? 26.102  73.532  14.186  1.00 34.37 ?  13  GLN K CD    1 
ATOM   9517  O  OE1   . GLN H 3 20  ? 26.285  74.580  14.816  1.00 31.30 ?  13  GLN K OE1   1 
ATOM   9518  N  NE2   . GLN H 3 20  ? 24.911  73.178  13.725  1.00 38.26 ?  13  GLN K NE2   1 
ATOM   9519  N  N     . ASP H 3 21  ? 31.475  73.577  12.020  1.00 18.89 ?  14  ASP K N     1 
ATOM   9520  C  CA    . ASP H 3 21  ? 32.268  74.436  11.153  1.00 22.34 ?  14  ASP K CA    1 
ATOM   9521  C  C     . ASP H 3 21  ? 33.538  73.707  10.717  1.00 20.87 ?  14  ASP K C     1 
ATOM   9522  O  O     . ASP H 3 21  ? 34.442  73.494  11.522  1.00 21.02 ?  14  ASP K O     1 
ATOM   9523  C  CB    . ASP H 3 21  ? 32.581  75.758  11.837  1.00 23.80 ?  14  ASP K CB    1 
ATOM   9524  C  CG    . ASP H 3 21  ? 33.350  76.766  10.996  1.00 26.24 ?  14  ASP K CG    1 
ATOM   9525  O  OD1   . ASP H 3 21  ? 33.574  76.481  9.800   1.00 29.50 ?  14  ASP K OD1   1 
ATOM   9526  O  OD2   . ASP H 3 21  ? 33.725  77.822  11.546  1.00 29.88 -1 14  ASP K OD2   1 
ATOM   9527  N  N     . ALA H 3 22  ? 33.607  73.352  9.428   1.00 21.28 ?  15  ALA K N     1 
ATOM   9528  C  CA    . ALA H 3 22  ? 34.682  72.513  8.921   1.00 21.24 ?  15  ALA K CA    1 
ATOM   9529  C  C     . ALA H 3 22  ? 35.965  73.320  8.735   1.00 20.60 ?  15  ALA K C     1 
ATOM   9530  O  O     . ALA H 3 22  ? 37.035  72.740  8.570   1.00 16.45 ?  15  ALA K O     1 
ATOM   9531  C  CB    . ALA H 3 22  ? 34.265  71.842  7.631   1.00 19.87 ?  15  ALA K CB    1 
ATOM   9532  N  N     . GLN H 3 23  ? 35.863  74.652  8.755   1.00 22.04 ?  16  GLN K N     1 
ATOM   9533  C  CA    . GLN H 3 23  ? 37.059  75.475  8.720   1.00 26.85 ?  16  GLN K CA    1 
ATOM   9534  C  C     . GLN H 3 23  ? 37.728  75.382  10.088  1.00 27.03 ?  16  GLN K C     1 
ATOM   9535  O  O     . GLN H 3 23  ? 38.936  75.179  10.190  1.00 35.04 ?  16  GLN K O     1 
ATOM   9536  C  CB    . GLN H 3 23  ? 36.755  76.923  8.336   1.00 31.98 ?  16  GLN K CB    1 
ATOM   9537  C  CG    . GLN H 3 23  ? 37.950  77.656  7.735   1.00 39.72 ?  16  GLN K CG    1 
ATOM   9538  C  CD    . GLN H 3 23  ? 38.477  76.992  6.481   1.00 43.94 ?  16  GLN K CD    1 
ATOM   9539  O  OE1   . GLN H 3 23  ? 38.912  75.834  6.497   1.00 51.87 ?  16  GLN K OE1   1 
ATOM   9540  N  NE2   . GLN H 3 23  ? 38.443  77.722  5.376   1.00 51.50 ?  16  GLN K NE2   1 
ATOM   9541  N  N     . LEU H 3 24  ? 36.909  75.505  11.136  1.00 27.34 ?  17  LEU K N     1 
ATOM   9542  C  CA    . LEU H 3 24  ? 37.383  75.459  12.507  1.00 24.14 ?  17  LEU K CA    1 
ATOM   9543  C  C     . LEU H 3 24  ? 37.861  74.049  12.849  1.00 22.22 ?  17  LEU K C     1 
ATOM   9544  O  O     . LEU H 3 24  ? 38.884  73.888  13.510  1.00 19.77 ?  17  LEU K O     1 
ATOM   9545  C  CB    . LEU H 3 24  ? 36.254  75.921  13.423  1.00 22.93 ?  17  LEU K CB    1 
ATOM   9546  C  CG    . LEU H 3 24  ? 36.523  75.821  14.926  1.00 25.06 ?  17  LEU K CG    1 
ATOM   9547  C  CD1   . LEU H 3 24  ? 37.755  76.610  15.343  1.00 27.42 ?  17  LEU K CD1   1 
ATOM   9548  C  CD2   . LEU H 3 24  ? 35.293  76.291  15.678  1.00 24.35 ?  17  LEU K CD2   1 
ATOM   9549  N  N     . MET H 3 25  ? 37.112  73.034  12.402  1.00 21.17 ?  18  MET K N     1 
ATOM   9550  C  CA    . MET H 3 25  ? 37.512  71.650  12.606  1.00 21.24 ?  18  MET K CA    1 
ATOM   9551  C  C     . MET H 3 25  ? 38.958  71.472  12.153  1.00 19.51 ?  18  MET K C     1 
ATOM   9552  O  O     . MET H 3 25  ? 39.817  71.077  12.937  1.00 18.67 ?  18  MET K O     1 
ATOM   9553  C  CB    . MET H 3 25  ? 36.629  70.674  11.818  1.00 20.52 ?  18  MET K CB    1 
ATOM   9554  C  CG    . MET H 3 25  ? 37.045  69.219  11.968  1.00 22.26 ?  18  MET K CG    1 
ATOM   9555  S  SD    . MET H 3 25  ? 36.866  68.580  13.646  1.00 27.17 ?  18  MET K SD    1 
ATOM   9556  C  CE    . MET H 3 25  ? 35.142  68.070  13.643  1.00 27.32 ?  18  MET K CE    1 
ATOM   9557  N  N     . GLU H 3 26  ? 39.206  71.775  10.876  1.00 20.33 ?  19  GLU K N     1 
ATOM   9558  C  CA    . GLU H 3 26  ? 40.505  71.553  10.265  1.00 21.68 ?  19  GLU K CA    1 
ATOM   9559  C  C     . GLU H 3 26  ? 41.573  72.354  11.006  1.00 19.64 ?  19  GLU K C     1 
ATOM   9560  O  O     . GLU H 3 26  ? 42.667  71.849  11.247  1.00 20.54 ?  19  GLU K O     1 
ATOM   9561  C  CB    . GLU H 3 26  ? 40.412  71.876  8.774   1.00 23.15 ?  19  GLU K CB    1 
ATOM   9562  C  CG    . GLU H 3 26  ? 39.510  70.904  8.019   1.00 26.63 ?  19  GLU K CG    1 
ATOM   9563  C  CD    . GLU H 3 26  ? 39.965  69.459  8.116   1.00 31.03 ?  19  GLU K CD    1 
ATOM   9564  O  OE1   . GLU H 3 26  ? 41.117  69.185  7.719   1.00 32.39 ?  19  GLU K OE1   1 
ATOM   9565  O  OE2   . GLU H 3 26  ? 39.175  68.612  8.586   1.00 26.83 -1 19  GLU K OE2   1 
ATOM   9566  N  N     . ASP H 3 27  ? 41.251  73.599  11.373  1.00 22.14 ?  20  ASP K N     1 
ATOM   9567  C  CA    . ASP H 3 27  ? 42.173  74.418  12.141  1.00 22.98 ?  20  ASP K CA    1 
ATOM   9568  C  C     . ASP H 3 27  ? 42.454  73.735  13.478  1.00 19.03 ?  20  ASP K C     1 
ATOM   9569  O  O     . ASP H 3 27  ? 43.566  73.812  13.993  1.00 14.73 ?  20  ASP K O     1 
ATOM   9570  C  CB    . ASP H 3 27  ? 41.655  75.837  12.324  1.00 28.10 ?  20  ASP K CB    1 
ATOM   9571  C  CG    . ASP H 3 27  ? 41.590  76.682  11.059  1.00 35.74 ?  20  ASP K CG    1 
ATOM   9572  O  OD1   . ASP H 3 27  ? 42.055  76.199  10.005  1.00 37.27 ?  20  ASP K OD1   1 
ATOM   9573  O  OD2   . ASP H 3 27  ? 41.070  77.815  11.138  1.00 43.28 -1 20  ASP K OD2   1 
ATOM   9574  N  N     . TYR H 3 28  ? 41.433  73.066  14.026  1.00 18.08 ?  21  TYR K N     1 
ATOM   9575  C  CA    . TYR H 3 28  ? 41.539  72.422  15.325  1.00 18.82 ?  21  TYR K CA    1 
ATOM   9576  C  C     . TYR H 3 28  ? 42.480  71.223  15.234  1.00 21.43 ?  21  TYR K C     1 
ATOM   9577  O  O     . TYR H 3 28  ? 43.237  70.954  16.165  1.00 18.72 ?  21  TYR K O     1 
ATOM   9578  C  CB    . TYR H 3 28  ? 40.170  71.980  15.852  1.00 18.02 ?  21  TYR K CB    1 
ATOM   9579  C  CG    . TYR H 3 28  ? 40.266  71.041  17.048  1.00 15.70 ?  21  TYR K CG    1 
ATOM   9580  C  CD1   . TYR H 3 28  ? 40.458  71.532  18.334  1.00 15.20 ?  21  TYR K CD1   1 
ATOM   9581  C  CD2   . TYR H 3 28  ? 40.191  69.663  16.886  1.00 15.27 ?  21  TYR K CD2   1 
ATOM   9582  C  CE1   . TYR H 3 28  ? 40.562  70.683  19.423  1.00 14.44 ?  21  TYR K CE1   1 
ATOM   9583  C  CE2   . TYR H 3 28  ? 40.294  68.803  17.967  1.00 14.90 ?  21  TYR K CE2   1 
ATOM   9584  C  CZ    . TYR H 3 28  ? 40.478  69.314  19.239  1.00 14.56 ?  21  TYR K CZ    1 
ATOM   9585  O  OH    . TYR H 3 28  ? 40.579  68.475  20.311  1.00 14.82 ?  21  TYR K OH    1 
ATOM   9586  N  N     . LYS H 3 29  ? 42.415  70.508  14.107  1.00 23.08 ?  22  LYS K N     1 
ATOM   9587  C  CA    . LYS H 3 29  ? 43.195  69.296  13.913  1.00 25.61 ?  22  LYS K CA    1 
ATOM   9588  C  C     . LYS H 3 29  ? 44.646  69.638  13.577  1.00 26.30 ?  22  LYS K C     1 
ATOM   9589  O  O     . LYS H 3 29  ? 45.533  68.816  13.793  1.00 27.70 ?  22  LYS K O     1 
ATOM   9590  C  CB    . LYS H 3 29  ? 42.482  68.399  12.892  1.00 24.35 ?  22  LYS K CB    1 
ATOM   9591  C  CG    . LYS H 3 29  ? 41.660  67.287  13.543  1.00 24.93 ?  22  LYS K CG    1 
ATOM   9592  C  CD    . LYS H 3 29  ? 40.276  67.019  12.962  1.00 24.06 ?  22  LYS K CD    1 
ATOM   9593  C  CE    . LYS H 3 29  ? 40.262  66.488  11.566  1.00 23.13 ?  22  LYS K CE    1 
ATOM   9594  N  NZ    . LYS H 3 29  ? 38.916  66.017  11.224  1.00 23.46 1  22  LYS K NZ    1 
ATOM   9595  N  N     . GLN H 3 30  ? 44.895  70.850  13.068  1.00 29.11 ?  23  GLN K N     1 
ATOM   9596  C  CA    . GLN H 3 30  ? 46.262  71.300  12.848  1.00 31.78 ?  23  GLN K CA    1 
ATOM   9597  C  C     . GLN H 3 30  ? 46.918  71.588  14.199  1.00 27.96 ?  23  GLN K C     1 
ATOM   9598  O  O     . GLN H 3 30  ? 48.080  71.244  14.403  1.00 20.65 ?  23  GLN K O     1 
ATOM   9599  C  CB    . GLN H 3 30  ? 46.368  72.523  11.933  1.00 35.57 ?  23  GLN K CB    1 
ATOM   9600  C  CG    . GLN H 3 30  ? 46.213  72.221  10.444  1.00 39.39 ?  23  GLN K CG    1 
ATOM   9601  C  CD    . GLN H 3 30  ? 47.412  71.526  9.833   1.00 42.23 ?  23  GLN K CD    1 
ATOM   9602  O  OE1   . GLN H 3 30  ? 47.922  70.531  10.360  1.00 45.99 ?  23  GLN K OE1   1 
ATOM   9603  N  NE2   . GLN H 3 30  ? 47.874  72.045  8.704   1.00 41.61 ?  23  GLN K NE2   1 
ATOM   9604  N  N     . ASN H 3 31  ? 46.171  72.214  15.118  1.00 24.77 ?  24  ASN K N     1 
ATOM   9605  C  CA    . ASN H 3 31  ? 46.731  72.607  16.403  1.00 24.34 ?  24  ASN K CA    1 
ATOM   9606  C  C     . ASN H 3 31  ? 45.654  72.570  17.486  1.00 22.46 ?  24  ASN K C     1 
ATOM   9607  O  O     . ASN H 3 31  ? 45.149  73.615  17.893  1.00 18.54 ?  24  ASN K O     1 
ATOM   9608  C  CB    . ASN H 3 31  ? 47.366  73.992  16.328  1.00 24.16 ?  24  ASN K CB    1 
ATOM   9609  C  CG    . ASN H 3 31  ? 48.520  74.145  17.290  1.00 26.16 ?  24  ASN K CG    1 
ATOM   9610  O  OD1   . ASN H 3 31  ? 48.386  73.835  18.479  1.00 25.97 ?  24  ASN K OD1   1 
ATOM   9611  N  ND2   . ASN H 3 31  ? 49.660  74.604  16.795  1.00 25.29 ?  24  ASN K ND2   1 
ATOM   9612  N  N     . PRO H 3 32  ? 45.274  71.378  18.000  1.00 20.52 ?  25  PRO K N     1 
ATOM   9613  C  CA    . PRO H 3 32  ? 44.232  71.291  19.025  1.00 22.82 ?  25  PRO K CA    1 
ATOM   9614  C  C     . PRO H 3 32  ? 44.415  72.281  20.179  1.00 26.77 ?  25  PRO K C     1 
ATOM   9615  O  O     . PRO H 3 32  ? 43.491  73.022  20.505  1.00 24.76 ?  25  PRO K O     1 
ATOM   9616  C  CB    . PRO H 3 32  ? 44.316  69.815  19.463  1.00 23.25 ?  25  PRO K CB    1 
ATOM   9617  C  CG    . PRO H 3 32  ? 44.806  69.093  18.222  1.00 21.70 ?  25  PRO K CG    1 
ATOM   9618  C  CD    . PRO H 3 32  ? 45.796  70.061  17.595  1.00 21.82 ?  25  PRO K CD    1 
ATOM   9619  N  N     . GLU H 3 33  ? 45.613  72.309  20.778  1.00 26.23 ?  26  GLU K N     1 
ATOM   9620  C  CA    . GLU H 3 33  ? 45.875  73.145  21.942  1.00 28.19 ?  26  GLU K CA    1 
ATOM   9621  C  C     . GLU H 3 33  ? 45.725  74.629  21.608  1.00 29.29 ?  26  GLU K C     1 
ATOM   9622  O  O     . GLU H 3 33  ? 45.088  75.367  22.357  1.00 26.70 ?  26  GLU K O     1 
ATOM   9623  C  CB    . GLU H 3 33  ? 47.267  72.916  22.532  1.00 30.83 ?  26  GLU K CB    1 
ATOM   9624  C  CG    . GLU H 3 33  ? 47.347  71.718  23.473  1.00 32.84 ?  26  GLU K CG    1 
ATOM   9625  C  CD    . GLU H 3 33  ? 48.486  71.811  24.473  1.00 33.96 ?  26  GLU K CD    1 
ATOM   9626  O  OE1   . GLU H 3 33  ? 49.278  72.772  24.377  1.00 30.98 ?  26  GLU K OE1   1 
ATOM   9627  O  OE2   . GLU H 3 33  ? 48.571  70.932  25.358  1.00 38.89 -1 26  GLU K OE2   1 
ATOM   9628  N  N     . ALA H 3 34  ? 46.337  75.073  20.504  1.00 26.26 ?  27  ALA K N     1 
ATOM   9629  C  CA    . ALA H 3 34  ? 46.360  76.489  20.170  1.00 24.63 ?  27  ALA K CA    1 
ATOM   9630  C  C     . ALA H 3 34  ? 44.942  76.988  19.905  1.00 27.36 ?  27  ALA K C     1 
ATOM   9631  O  O     . ALA H 3 34  ? 44.588  78.104  20.280  1.00 24.83 ?  27  ALA K O     1 
ATOM   9632  C  CB    . ALA H 3 34  ? 47.265  76.735  18.982  1.00 24.08 ?  27  ALA K CB    1 
ATOM   9633  N  N     . VAL H 3 35  ? 44.139  76.146  19.249  1.00 25.11 ?  28  VAL K N     1 
ATOM   9634  C  CA    . VAL H 3 35  ? 42.766  76.489  18.923  1.00 25.94 ?  28  VAL K CA    1 
ATOM   9635  C  C     . VAL H 3 35  ? 41.930  76.504  20.202  1.00 27.81 ?  28  VAL K C     1 
ATOM   9636  O  O     . VAL H 3 35  ? 41.080  77.375  20.373  1.00 26.64 ?  28  VAL K O     1 
ATOM   9637  C  CB    . VAL H 3 35  ? 42.201  75.520  17.866  1.00 27.19 ?  28  VAL K CB    1 
ATOM   9638  C  CG1   . VAL H 3 35  ? 40.708  75.725  17.637  1.00 28.43 ?  28  VAL K CG1   1 
ATOM   9639  C  CG2   . VAL H 3 35  ? 42.965  75.628  16.551  1.00 27.31 ?  28  VAL K CG2   1 
ATOM   9640  N  N     . MET H 3 36  ? 42.189  75.555  21.109  1.00 28.59 ?  29  MET K N     1 
ATOM   9641  C  CA    . MET H 3 36  ? 41.424  75.460  22.343  1.00 27.40 ?  29  MET K CA    1 
ATOM   9642  C  C     . MET H 3 36  ? 41.774  76.613  23.282  1.00 29.20 ?  29  MET K C     1 
ATOM   9643  O  O     . MET H 3 36  ? 40.896  77.155  23.950  1.00 27.67 ?  29  MET K O     1 
ATOM   9644  C  CB    . MET H 3 36  ? 41.659  74.119  23.046  1.00 27.24 ?  29  MET K CB    1 
ATOM   9645  C  CG    . MET H 3 36  ? 40.891  72.974  22.418  1.00 26.58 ?  29  MET K CG    1 
ATOM   9646  S  SD    . MET H 3 36  ? 40.868  71.492  23.444  1.00 24.51 ?  29  MET K SD    1 
ATOM   9647  C  CE    . MET H 3 36  ? 42.469  70.780  23.043  1.00 30.54 ?  29  MET K CE    1 
ATOM   9648  N  N     . ARG H 3 37  ? 43.060  76.976  23.332  1.00 27.98 ?  30  ARG K N     1 
ATOM   9649  C  CA    . ARG H 3 37  ? 43.510  78.084  24.159  1.00 29.75 ?  30  ARG K CA    1 
ATOM   9650  C  C     . ARG H 3 37  ? 42.904  79.383  23.629  1.00 30.44 ?  30  ARG K C     1 
ATOM   9651  O  O     . ARG H 3 37  ? 42.532  80.260  24.406  1.00 26.79 ?  30  ARG K O     1 
ATOM   9652  C  CB    . ARG H 3 37  ? 45.042  78.124  24.224  1.00 31.45 ?  30  ARG K CB    1 
ATOM   9653  C  CG    . ARG H 3 37  ? 45.642  77.070  25.145  1.00 35.26 ?  30  ARG K CG    1 
ATOM   9654  C  CD    . ARG H 3 37  ? 47.138  77.231  25.379  1.00 39.24 ?  30  ARG K CD    1 
ATOM   9655  N  NE    . ARG H 3 37  ? 47.537  76.628  26.657  1.00 43.82 ?  30  ARG K NE    1 
ATOM   9656  C  CZ    . ARG H 3 37  ? 48.271  75.532  26.812  1.00 47.01 ?  30  ARG K CZ    1 
ATOM   9657  N  NH1   . ARG H 3 37  ? 48.710  74.865  25.759  1.00 50.04 1  30  ARG K NH1   1 
ATOM   9658  N  NH2   . ARG H 3 37  ? 48.557  75.101  28.028  1.00 49.04 ?  30  ARG K NH2   1 
ATOM   9659  N  N     . ALA H 3 38  ? 42.792  79.485  22.300  1.00 29.20 ?  31  ALA K N     1 
ATOM   9660  C  CA    . ALA H 3 38  ? 42.269  80.682  21.660  1.00 26.67 ?  31  ALA K CA    1 
ATOM   9661  C  C     . ALA H 3 38  ? 40.775  80.820  21.944  1.00 26.85 ?  31  ALA K C     1 
ATOM   9662  O  O     . ALA H 3 38  ? 40.219  81.909  21.830  1.00 28.47 ?  31  ALA K O     1 
ATOM   9663  C  CB    . ALA H 3 38  ? 42.546  80.642  20.173  1.00 27.43 ?  31  ALA K CB    1 
ATOM   9664  N  N     . HIS H 3 39  ? 40.131  79.710  22.317  1.00 24.96 ?  32  HIS K N     1 
ATOM   9665  C  CA    . HIS H 3 39  ? 38.708  79.725  22.612  1.00 24.85 ?  32  HIS K CA    1 
ATOM   9666  C  C     . HIS H 3 39  ? 38.493  79.676  24.124  1.00 25.55 ?  32  HIS K C     1 
ATOM   9667  O  O     . HIS H 3 39  ? 37.387  79.413  24.590  1.00 23.49 ?  32  HIS K O     1 
ATOM   9668  C  CB    . HIS H 3 39  ? 37.989  78.621  21.828  1.00 22.67 ?  32  HIS K CB    1 
ATOM   9669  C  CG    . HIS H 3 39  ? 37.742  78.982  20.399  1.00 21.99 ?  32  HIS K CG    1 
ATOM   9670  N  ND1   . HIS H 3 39  ? 38.711  78.916  19.421  1.00 21.49 ?  32  HIS K ND1   1 
ATOM   9671  C  CD2   . HIS H 3 39  ? 36.637  79.440  19.793  1.00 21.96 ?  32  HIS K CD2   1 
ATOM   9672  C  CE1   . HIS H 3 39  ? 38.193  79.309  18.264  1.00 21.62 ?  32  HIS K CE1   1 
ATOM   9673  N  NE2   . HIS H 3 39  ? 36.934  79.630  18.468  1.00 21.80 ?  32  HIS K NE2   1 
ATOM   9674  N  N     . GLY H 3 40  ? 39.568  79.933  24.877  1.00 24.52 ?  33  GLY K N     1 
ATOM   9675  C  CA    . GLY H 3 40  ? 39.478  80.201  26.303  1.00 26.52 ?  33  GLY K CA    1 
ATOM   9676  C  C     . GLY H 3 40  ? 39.227  78.946  27.137  1.00 29.28 ?  33  GLY K C     1 
ATOM   9677  O  O     . GLY H 3 40  ? 38.730  79.046  28.257  1.00 28.92 ?  33  GLY K O     1 
ATOM   9678  N  N     . LEU H 3 41  ? 39.578  77.769  26.604  1.00 32.29 ?  34  LEU K N     1 
ATOM   9679  C  CA    . LEU H 3 41  ? 39.522  76.547  27.393  1.00 31.61 ?  34  LEU K CA    1 
ATOM   9680  C  C     . LEU H 3 41  ? 40.633  76.583  28.439  1.00 30.53 ?  34  LEU K C     1 
ATOM   9681  O  O     . LEU H 3 41  ? 41.721  77.093  28.179  1.00 27.14 ?  34  LEU K O     1 
ATOM   9682  C  CB    . LEU H 3 41  ? 39.619  75.296  26.519  1.00 33.55 ?  34  LEU K CB    1 
ATOM   9683  C  CG    . LEU H 3 41  ? 38.307  74.817  25.887  1.00 34.20 ?  34  LEU K CG    1 
ATOM   9684  C  CD1   . LEU H 3 41  ? 37.699  75.878  24.986  1.00 33.15 ?  34  LEU K CD1   1 
ATOM   9685  C  CD2   . LEU H 3 41  ? 38.507  73.522  25.119  1.00 34.47 ?  34  LEU K CD2   1 
ATOM   9686  N  N     . THR H 3 42  ? 40.336  76.047  29.629  1.00 30.92 ?  35  THR K N     1 
ATOM   9687  C  CA    . THR H 3 42  ? 41.304  75.976  30.711  1.00 32.15 ?  35  THR K CA    1 
ATOM   9688  C  C     . THR H 3 42  ? 42.236  74.793  30.473  1.00 31.93 ?  35  THR K C     1 
ATOM   9689  O  O     . THR H 3 42  ? 41.955  73.924  29.650  1.00 26.19 ?  35  THR K O     1 
ATOM   9690  C  CB    . THR H 3 42  ? 40.597  75.840  32.059  1.00 31.35 ?  35  THR K CB    1 
ATOM   9691  O  OG1   . THR H 3 42  ? 39.800  74.664  31.962  1.00 30.27 ?  35  THR K OG1   1 
ATOM   9692  C  CG2   . THR H 3 42  ? 39.730  77.039  32.393  1.00 31.12 ?  35  THR K CG2   1 
ATOM   9693  N  N     . ASP H 3 43  ? 43.333  74.769  31.235  1.00 34.12 ?  36  ASP K N     1 
ATOM   9694  C  CA    . ASP H 3 43  ? 44.339  73.728  31.124  1.00 38.83 ?  36  ASP K CA    1 
ATOM   9695  C  C     . ASP H 3 43  ? 43.707  72.369  31.423  1.00 37.18 ?  36  ASP K C     1 
ATOM   9696  O  O     . ASP H 3 43  ? 43.945  71.404  30.700  1.00 42.62 ?  36  ASP K O     1 
ATOM   9697  C  CB    . ASP H 3 43  ? 45.531  74.035  32.017  1.00 47.25 ?  36  ASP K CB    1 
ATOM   9698  C  CG    . ASP H 3 43  ? 46.215  75.367  31.742  1.00 50.08 ?  36  ASP K CG    1 
ATOM   9699  O  OD1   . ASP H 3 43  ? 46.643  75.579  30.588  1.00 52.44 ?  36  ASP K OD1   1 
ATOM   9700  O  OD2   . ASP H 3 43  ? 46.313  76.181  32.685  1.00 57.49 -1 36  ASP K OD2   1 
ATOM   9701  N  N     . GLU H 3 44  ? 42.898  72.307  32.487  1.00 33.86 ?  37  GLU K N     1 
ATOM   9702  C  CA    . GLU H 3 44  ? 42.305  71.056  32.936  1.00 37.19 ?  37  GLU K CA    1 
ATOM   9703  C  C     . GLU H 3 44  ? 41.300  70.570  31.894  1.00 33.39 ?  37  GLU K C     1 
ATOM   9704  O  O     . GLU H 3 44  ? 41.169  69.369  31.665  1.00 31.57 ?  37  GLU K O     1 
ATOM   9705  C  CB    . GLU H 3 44  ? 41.636  71.225  34.301  1.00 41.93 ?  37  GLU K CB    1 
ATOM   9706  C  CG    . GLU H 3 44  ? 40.344  72.035  34.245  1.00 48.64 ?  37  GLU K CG    1 
ATOM   9707  C  CD    . GLU H 3 44  ? 39.743  72.397  35.592  1.00 50.86 ?  37  GLU K CD    1 
ATOM   9708  O  OE1   . GLU H 3 44  ? 39.229  71.489  36.279  1.00 53.12 ?  37  GLU K OE1   1 
ATOM   9709  O  OE2   . GLU H 3 44  ? 39.793  73.592  35.956  1.00 52.01 -1 37  GLU K OE2   1 
ATOM   9710  N  N     . GLN H 3 45  ? 40.592  71.521  31.277  1.00 28.28 ?  38  GLN K N     1 
ATOM   9711  C  CA    . GLN H 3 45  ? 39.691  71.230  30.175  1.00 28.73 ?  38  GLN K CA    1 
ATOM   9712  C  C     . GLN H 3 45  ? 40.487  70.632  29.019  1.00 25.46 ?  38  GLN K C     1 
ATOM   9713  O  O     . GLN H 3 45  ? 40.137  69.575  28.499  1.00 27.10 ?  38  GLN K O     1 
ATOM   9714  C  CB    . GLN H 3 45  ? 38.945  72.499  29.759  1.00 28.44 ?  38  GLN K CB    1 
ATOM   9715  C  CG    . GLN H 3 45  ? 37.799  72.864  30.696  1.00 29.80 ?  38  GLN K CG    1 
ATOM   9716  C  CD    . GLN H 3 45  ? 37.153  74.196  30.383  1.00 31.84 ?  38  GLN K CD    1 
ATOM   9717  O  OE1   . GLN H 3 45  ? 37.710  75.039  29.672  1.00 29.26 ?  38  GLN K OE1   1 
ATOM   9718  N  NE2   . GLN H 3 45  ? 35.967  74.403  30.937  1.00 34.73 ?  38  GLN K NE2   1 
ATOM   9719  N  N     . ILE H 3 46  ? 41.562  71.326  28.634  1.00 24.33 ?  39  ILE K N     1 
ATOM   9720  C  CA    . ILE H 3 46  ? 42.447  70.870  27.575  1.00 26.08 ?  39  ILE K CA    1 
ATOM   9721  C  C     . ILE H 3 46  ? 43.025  69.508  27.957  1.00 27.68 ?  39  ILE K C     1 
ATOM   9722  O  O     . ILE H 3 46  ? 43.079  68.602  27.129  1.00 28.51 ?  39  ILE K O     1 
ATOM   9723  C  CB    . ILE H 3 46  ? 43.540  71.921  27.299  1.00 25.62 ?  39  ILE K CB    1 
ATOM   9724  C  CG1   . ILE H 3 46  ? 42.933  73.205  26.721  1.00 27.46 ?  39  ILE K CG1   1 
ATOM   9725  C  CG2   . ILE H 3 46  ? 44.639  71.359  26.396  1.00 28.08 ?  39  ILE K CG2   1 
ATOM   9726  C  CD1   . ILE H 3 46  ? 43.935  74.316  26.462  1.00 27.75 ?  39  ILE K CD1   1 
ATOM   9727  N  N     . ASN H 3 47  ? 43.441  69.368  29.222  1.00 28.51 ?  40  ASN K N     1 
ATOM   9728  C  CA    . ASN H 3 47  ? 44.045  68.132  29.694  1.00 34.13 ?  40  ASN K CA    1 
ATOM   9729  C  C     . ASN H 3 47  ? 43.036  66.991  29.596  1.00 36.20 ?  40  ASN K C     1 
ATOM   9730  O  O     . ASN H 3 47  ? 43.407  65.852  29.320  1.00 33.29 ?  40  ASN K O     1 
ATOM   9731  C  CB    . ASN H 3 47  ? 44.581  68.264  31.116  1.00 38.13 ?  40  ASN K CB    1 
ATOM   9732  C  CG    . ASN H 3 47  ? 44.991  66.927  31.686  1.00 43.72 ?  40  ASN K CG    1 
ATOM   9733  O  OD1   . ASN H 3 47  ? 45.922  66.292  31.178  1.00 43.61 ?  40  ASN K OD1   1 
ATOM   9734  N  ND2   . ASN H 3 47  ? 44.309  66.479  32.730  1.00 47.52 ?  40  ASN K ND2   1 
ATOM   9735  N  N     . ALA H 3 48  ? 41.758  67.308  29.828  1.00 35.40 ?  41  ALA K N     1 
ATOM   9736  C  CA    . ALA H 3 48  ? 40.704  66.308  29.783  1.00 36.50 ?  41  ALA K CA    1 
ATOM   9737  C  C     . ALA H 3 48  ? 40.429  65.904  28.337  1.00 35.11 ?  41  ALA K C     1 
ATOM   9738  O  O     . ALA H 3 48  ? 40.000  64.782  28.077  1.00 32.62 ?  41  ALA K O     1 
ATOM   9739  C  CB    . ALA H 3 48  ? 39.459  66.832  30.464  1.00 36.22 ?  41  ALA K CB    1 
ATOM   9740  N  N     . VAL H 3 49  ? 40.678  66.827  27.400  1.00 32.39 ?  42  VAL K N     1 
ATOM   9741  C  CA    . VAL H 3 49  ? 40.510  66.536  25.986  1.00 33.25 ?  42  VAL K CA    1 
ATOM   9742  C  C     . VAL H 3 49  ? 41.640  65.613  25.536  1.00 30.40 ?  42  VAL K C     1 
ATOM   9743  O  O     . VAL H 3 49  ? 41.394  64.591  24.900  1.00 32.37 ?  42  VAL K O     1 
ATOM   9744  C  CB    . VAL H 3 49  ? 40.454  67.809  25.120  1.00 32.30 ?  42  VAL K CB    1 
ATOM   9745  C  CG1   . VAL H 3 49  ? 40.663  67.507  23.640  1.00 31.34 ?  42  VAL K CG1   1 
ATOM   9746  C  CG2   . VAL H 3 49  ? 39.152  68.572  25.331  1.00 35.31 ?  42  VAL K CG2   1 
ATOM   9747  N  N     . MET H 3 50  ? 42.877  65.981  25.881  1.00 32.32 ?  43  MET K N     1 
ATOM   9748  C  CA    . MET H 3 50  ? 44.044  65.288  25.365  1.00 34.54 ?  43  MET K CA    1 
ATOM   9749  C  C     . MET H 3 50  ? 44.151  63.898  25.996  1.00 32.52 ?  43  MET K C     1 
ATOM   9750  O  O     . MET H 3 50  ? 44.793  63.017  25.429  1.00 33.40 ?  43  MET K O     1 
ATOM   9751  C  CB    . MET H 3 50  ? 45.317  66.112  25.600  1.00 36.67 ?  43  MET K CB    1 
ATOM   9752  C  CG    . MET H 3 50  ? 45.242  67.531  25.052  1.00 38.09 ?  43  MET K CG    1 
ATOM   9753  S  SD    . MET H 3 50  ? 44.748  67.624  23.318  1.00 43.12 ?  43  MET K SD    1 
ATOM   9754  C  CE    . MET H 3 50  ? 46.041  66.643  22.545  1.00 44.01 ?  43  MET K CE    1 
ATOM   9755  N  N     . THR H 3 51  ? 43.505  63.695  27.153  1.00 31.51 ?  44  THR K N     1 
ATOM   9756  C  CA    . THR H 3 51  ? 43.517  62.395  27.809  1.00 33.70 ?  44  THR K CA    1 
ATOM   9757  C  C     . THR H 3 51  ? 42.222  61.644  27.503  1.00 33.96 ?  44  THR K C     1 
ATOM   9758  O  O     . THR H 3 51  ? 42.010  60.544  28.009  1.00 36.65 ?  44  THR K O     1 
ATOM   9759  C  CB    . THR H 3 51  ? 43.718  62.548  29.317  1.00 34.80 ?  44  THR K CB    1 
ATOM   9760  O  OG1   . THR H 3 51  ? 42.594  63.287  29.785  1.00 37.55 ?  44  THR K OG1   1 
ATOM   9761  C  CG2   . THR H 3 51  ? 45.013  63.258  29.667  1.00 35.06 ?  44  THR K CG2   1 
ATOM   9762  N  N     . GLY H 3 52  ? 41.363  62.250  26.677  1.00 35.10 ?  45  GLY K N     1 
ATOM   9763  C  CA    . GLY H 3 52  ? 40.123  61.623  26.249  1.00 34.40 ?  45  GLY K CA    1 
ATOM   9764  C  C     . GLY H 3 52  ? 39.225  61.257  27.429  1.00 35.94 ?  45  GLY K C     1 
ATOM   9765  O  O     . GLY H 3 52  ? 38.674  60.159  27.471  1.00 35.58 ?  45  GLY K O     1 
ATOM   9766  N  N     . ASP H 3 53  ? 39.073  62.188  28.380  1.00 33.30 ?  46  ASP K N     1 
ATOM   9767  C  CA    . ASP H 3 53  ? 38.231  61.956  29.543  1.00 30.90 ?  46  ASP K CA    1 
ATOM   9768  C  C     . ASP H 3 53  ? 36.936  62.749  29.388  1.00 33.66 ?  46  ASP K C     1 
ATOM   9769  O  O     . ASP H 3 53  ? 36.831  63.888  29.838  1.00 20.96 ?  46  ASP K O     1 
ATOM   9770  C  CB    . ASP H 3 53  ? 38.964  62.254  30.842  1.00 30.48 ?  46  ASP K CB    1 
ATOM   9771  C  CG    . ASP H 3 53  ? 38.224  61.865  32.115  1.00 33.99 ?  46  ASP K CG    1 
ATOM   9772  O  OD1   . ASP H 3 53  ? 37.018  61.545  32.022  1.00 30.11 ?  46  ASP K OD1   1 
ATOM   9773  O  OD2   . ASP H 3 53  ? 38.864  61.870  33.190  1.00 33.41 -1 46  ASP K OD2   1 
ATOM   9774  N  N     . MET H 3 54  ? 35.955  62.110  28.745  1.00 36.18 ?  47  MET K N     1 
ATOM   9775  C  CA    . MET H 3 54  ? 34.675  62.732  28.459  1.00 42.71 ?  47  MET K CA    1 
ATOM   9776  C  C     . MET H 3 54  ? 33.942  63.010  29.770  1.00 49.54 ?  47  MET K C     1 
ATOM   9777  O  O     . MET H 3 54  ? 33.282  64.038  29.908  1.00 46.46 ?  47  MET K O     1 
ATOM   9778  C  CB    . MET H 3 54  ? 33.842  61.831  27.541  1.00 43.88 ?  47  MET K CB    1 
ATOM   9779  C  CG    . MET H 3 54  ? 34.521  61.498  26.219  1.00 42.30 ?  47  MET K CG    1 
ATOM   9780  S  SD    . MET H 3 54  ? 35.053  62.945  25.279  1.00 37.85 ?  47  MET K SD    1 
ATOM   9781  C  CE    . MET H 3 54  ? 36.742  63.215  25.835  1.00 38.15 ?  47  MET K CE    1 
ATOM   9782  N  N     . GLU H 3 55  ? 34.079  62.092  30.734  1.00 51.67 ?  48  GLU K N     1 
ATOM   9783  C  CA    . GLU H 3 55  ? 33.432  62.237  32.028  1.00 58.80 ?  48  GLU K CA    1 
ATOM   9784  C  C     . GLU H 3 55  ? 33.848  63.566  32.658  1.00 62.66 ?  48  GLU K C     1 
ATOM   9785  O  O     . GLU H 3 55  ? 32.996  64.341  33.089  1.00 68.51 ?  48  GLU K O     1 
ATOM   9786  C  CB    . GLU H 3 55  ? 33.759  61.044  32.929  1.00 63.42 ?  48  GLU K CB    1 
ATOM   9787  C  CG    . GLU H 3 55  ? 33.026  61.063  34.268  1.00 66.90 ?  48  GLU K CG    1 
ATOM   9788  C  CD    . GLU H 3 55  ? 31.510  61.057  34.168  1.00 64.45 ?  48  GLU K CD    1 
ATOM   9789  O  OE1   . GLU H 3 55  ? 30.963  60.182  33.465  1.00 67.44 ?  48  GLU K OE1   1 
ATOM   9790  O  OE2   . GLU H 3 55  ? 30.877  61.924  34.806  1.00 51.54 -1 48  GLU K OE2   1 
ATOM   9791  N  N     . LYS H 3 56  ? 35.161  63.822  32.698  1.00 59.77 ?  49  LYS K N     1 
ATOM   9792  C  CA    . LYS H 3 56  ? 35.690  65.048  33.275  1.00 63.10 ?  49  LYS K CA    1 
ATOM   9793  C  C     . LYS H 3 56  ? 35.055  66.249  32.577  1.00 57.71 ?  49  LYS K C     1 
ATOM   9794  O  O     . LYS H 3 56  ? 34.627  67.197  33.230  1.00 58.39 ?  49  LYS K O     1 
ATOM   9795  C  CB    . LYS H 3 56  ? 37.215  65.133  33.133  1.00 66.01 ?  49  LYS K CB    1 
ATOM   9796  C  CG    . LYS H 3 56  ? 37.936  66.009  34.156  1.00 67.00 ?  49  LYS K CG    1 
ATOM   9797  C  CD    . LYS H 3 56  ? 38.349  65.265  35.422  1.00 69.97 ?  49  LYS K CD    1 
ATOM   9798  C  CE    . LYS H 3 56  ? 39.287  66.037  36.299  1.00 69.37 ?  49  LYS K CE    1 
ATOM   9799  N  NZ    . LYS H 3 56  ? 38.645  67.191  36.933  1.00 65.30 1  49  LYS K NZ    1 
ATOM   9800  N  N     . LEU H 3 57  ? 35.006  66.194  31.240  1.00 52.76 ?  50  LEU K N     1 
ATOM   9801  C  CA    . LEU H 3 57  ? 34.496  67.295  30.438  1.00 54.60 ?  50  LEU K CA    1 
ATOM   9802  C  C     . LEU H 3 57  ? 33.046  67.586  30.821  1.00 54.64 ?  50  LEU K C     1 
ATOM   9803  O  O     . LEU H 3 57  ? 32.656  68.745  30.947  1.00 54.81 ?  50  LEU K O     1 
ATOM   9804  C  CB    . LEU H 3 57  ? 34.623  66.973  28.949  1.00 52.91 ?  50  LEU K CB    1 
ATOM   9805  C  CG    . LEU H 3 57  ? 36.016  67.137  28.333  1.00 50.48 ?  50  LEU K CG    1 
ATOM   9806  C  CD1   . LEU H 3 57  ? 36.014  66.628  26.902  1.00 48.59 ?  50  LEU K CD1   1 
ATOM   9807  C  CD2   . LEU H 3 57  ? 36.481  68.584  28.383  1.00 49.27 ?  50  LEU K CD2   1 
ATOM   9808  N  N     . LYS H 3 58  ? 32.256  66.522  30.999  1.00 56.13 ?  51  LYS K N     1 
ATOM   9809  C  CA    . LYS H 3 58  ? 30.837  66.648  31.291  1.00 58.92 ?  51  LYS K CA    1 
ATOM   9810  C  C     . LYS H 3 58  ? 30.649  67.211  32.698  1.00 61.80 ?  51  LYS K C     1 
ATOM   9811  O  O     . LYS H 3 58  ? 29.602  67.772  33.013  1.00 70.95 ?  51  LYS K O     1 
ATOM   9812  C  CB    . LYS H 3 58  ? 30.141  65.294  31.120  1.00 57.90 ?  51  LYS K CB    1 
ATOM   9813  C  CG    . LYS H 3 58  ? 30.092  64.787  29.684  1.00 57.84 ?  51  LYS K CG    1 
ATOM   9814  C  CD    . LYS H 3 58  ? 29.471  63.405  29.527  1.00 55.80 ?  51  LYS K CD    1 
ATOM   9815  C  CE    . LYS H 3 58  ? 29.431  62.952  28.101  1.00 51.07 ?  51  LYS K CE    1 
ATOM   9816  N  NZ    . LYS H 3 58  ? 28.923  61.584  27.975  1.00 46.67 1  51  LYS K NZ    1 
ATOM   9817  N  N     . THR H 3 59  ? 31.675  67.039  33.537  1.00 67.39 ?  52  THR K N     1 
ATOM   9818  C  CA    . THR H 3 59  ? 31.727  67.681  34.840  1.00 71.94 ?  52  THR K CA    1 
ATOM   9819  C  C     . THR H 3 59  ? 32.032  69.153  34.653  1.00 72.09 ?  52  THR K C     1 
ATOM   9820  O  O     . THR H 3 59  ? 31.334  69.967  35.297  1.00 75.37 ?  52  THR K O     1 
ATOM   9821  C  CB    . THR H 3 59  ? 32.781  66.988  35.703  1.00 72.19 ?  52  THR K CB    1 
ATOM   9822  O  OG1   . THR H 3 59  ? 32.149  65.804  36.180  1.00 70.97 ?  52  THR K OG1   1 
ATOM   9823  C  CG2   . THR H 3 59  ? 33.237  67.842  36.872  1.00 71.64 ?  52  THR K CG2   1 
ATOM   9824  N  N     . SER H 3 68  ? 20.067  55.329  26.593  1.00 49.79 ?  61  SER K N     1 
ATOM   9825  C  CA    . SER H 3 68  ? 20.351  55.282  25.134  1.00 47.85 ?  61  SER K CA    1 
ATOM   9826  C  C     . SER H 3 68  ? 19.500  54.222  24.433  1.00 44.80 ?  61  SER K C     1 
ATOM   9827  O  O     . SER H 3 68  ? 19.172  54.381  23.260  1.00 53.00 ?  61  SER K O     1 
ATOM   9828  C  CB    . SER H 3 68  ? 21.825  55.067  24.882  1.00 47.76 ?  61  SER K CB    1 
ATOM   9829  O  OG    . SER H 3 68  ? 22.035  54.198  23.777  1.00 49.94 ?  61  SER K OG    1 
ATOM   9830  N  N     . TYR H 3 69  ? 19.142  53.145  25.144  1.00 43.28 ?  62  TYR K N     1 
ATOM   9831  C  CA    . TYR H 3 69  ? 18.429  52.029  24.537  1.00 45.71 ?  62  TYR K CA    1 
ATOM   9832  C  C     . TYR H 3 69  ? 17.026  52.474  24.125  1.00 51.79 ?  62  TYR K C     1 
ATOM   9833  O  O     . TYR H 3 69  ? 16.327  53.117  24.906  1.00 52.99 ?  62  TYR K O     1 
ATOM   9834  C  CB    . TYR H 3 69  ? 18.322  50.833  25.490  1.00 43.50 ?  62  TYR K CB    1 
ATOM   9835  C  CG    . TYR H 3 69  ? 19.614  50.429  26.188  1.00 42.70 ?  62  TYR K CG    1 
ATOM   9836  C  CD1   . TYR H 3 69  ? 20.827  50.402  25.511  1.00 41.33 ?  62  TYR K CD1   1 
ATOM   9837  C  CD2   . TYR H 3 69  ? 19.615  50.083  27.534  1.00 38.79 ?  62  TYR K CD2   1 
ATOM   9838  C  CE1   . TYR H 3 69  ? 22.001  50.034  26.150  1.00 42.64 ?  62  TYR K CE1   1 
ATOM   9839  C  CE2   . TYR H 3 69  ? 20.781  49.717  28.184  1.00 38.05 ?  62  TYR K CE2   1 
ATOM   9840  C  CZ    . TYR H 3 69  ? 21.977  49.693  27.491  1.00 40.98 ?  62  TYR K CZ    1 
ATOM   9841  O  OH    . TYR H 3 69  ? 23.128  49.332  28.132  1.00 37.22 ?  62  TYR K OH    1 
ATOM   9842  N  N     . LEU H 3 70  ? 16.614  52.109  22.901  1.00 53.52 ?  63  LEU K N     1 
ATOM   9843  C  CA    . LEU H 3 70  ? 15.304  52.488  22.390  1.00 53.91 ?  63  LEU K CA    1 
ATOM   9844  C  C     . LEU H 3 70  ? 14.521  51.275  21.885  1.00 52.50 ?  63  LEU K C     1 
ATOM   9845  O  O     . LEU H 3 70  ? 13.376  51.425  21.468  1.00 57.47 ?  63  LEU K O     1 
ATOM   9846  C  CB    . LEU H 3 70  ? 15.407  53.538  21.284  1.00 55.54 ?  63  LEU K CB    1 
ATOM   9847  C  CG    . LEU H 3 70  ? 15.338  55.003  21.726  1.00 57.43 ?  63  LEU K CG    1 
ATOM   9848  C  CD1   . LEU H 3 70  ? 16.646  55.728  21.462  1.00 52.94 ?  63  LEU K CD1   1 
ATOM   9849  C  CD2   . LEU H 3 70  ? 14.172  55.696  21.042  1.00 58.30 ?  63  LEU K CD2   1 
ATOM   9850  N  N     . VAL H 3 71  ? 15.127  50.082  21.905  1.00 50.42 ?  64  VAL K N     1 
ATOM   9851  C  CA    . VAL H 3 71  ? 14.417  48.871  21.514  1.00 47.38 ?  64  VAL K CA    1 
ATOM   9852  C  C     . VAL H 3 71  ? 14.683  47.786  22.571  1.00 42.70 ?  64  VAL K C     1 
ATOM   9853  O  O     . VAL H 3 71  ? 15.678  47.942  23.312  1.00 50.77 ?  64  VAL K O     1 
ATOM   9854  C  CB    . VAL H 3 71  ? 14.777  48.358  20.105  1.00 45.81 ?  64  VAL K CB    1 
ATOM   9855  C  CG1   . VAL H 3 71  ? 13.904  48.982  19.021  1.00 41.61 ?  64  VAL K CG1   1 
ATOM   9856  C  CG2   . VAL H 3 71  ? 16.257  48.537  19.790  1.00 48.09 ?  64  VAL K CG2   1 
HETATM 9857  N  N     . SAH I 4 .   ? 3.650   1.393   -9.053  0.80 22.35 ?  301 SAH A N     1 
HETATM 9858  C  CA    . SAH I 4 .   ? 2.285   0.857   -9.311  0.80 22.75 ?  301 SAH A CA    1 
HETATM 9859  C  CB    . SAH I 4 .   ? 2.349   -0.511  -9.998  0.80 24.13 ?  301 SAH A CB    1 
HETATM 9860  C  CG    . SAH I 4 .   ? 2.974   -0.477  -11.380 0.80 26.38 ?  301 SAH A CG    1 
HETATM 9861  S  SD    . SAH I 4 .   ? 3.059   -2.106  -12.171 0.80 29.48 ?  301 SAH A SD    1 
HETATM 9862  C  C     . SAH I 4 .   ? 1.536   0.718   -7.980  0.80 21.18 ?  301 SAH A C     1 
HETATM 9863  O  O     . SAH I 4 .   ? 2.057   1.242   -6.974  0.80 20.56 ?  301 SAH A O     1 
HETATM 9864  O  OXT   . SAH I 4 .   ? 0.465   0.080   -7.997  0.80 18.88 ?  301 SAH A OXT   1 
HETATM 9865  C  "C5'" . SAH I 4 .   ? 1.552   -2.111  -13.173 0.80 31.48 ?  301 SAH A "C5'" 1 
HETATM 9866  C  "C4'" . SAH I 4 .   ? 0.480   -3.028  -12.636 0.80 31.47 ?  301 SAH A "C4'" 1 
HETATM 9867  O  "O4'" . SAH I 4 .   ? -0.082  -2.460  -11.431 0.80 31.55 ?  301 SAH A "O4'" 1 
HETATM 9868  C  "C3'" . SAH I 4 .   ? -0.716  -3.246  -13.556 0.80 32.13 ?  301 SAH A "C3'" 1 
HETATM 9869  O  "O3'" . SAH I 4 .   ? -0.459  -4.265  -14.515 0.80 34.69 ?  301 SAH A "O3'" 1 
HETATM 9870  C  "C2'" . SAH I 4 .   ? -1.782  -3.654  -12.538 0.80 29.77 ?  301 SAH A "C2'" 1 
HETATM 9871  O  "O2'" . SAH I 4 .   ? -1.643  -4.990  -12.107 0.80 28.40 ?  301 SAH A "O2'" 1 
HETATM 9872  C  "C1'" . SAH I 4 .   ? -1.479  -2.662  -11.419 0.80 31.08 ?  301 SAH A "C1'" 1 
HETATM 9873  N  N9    . SAH I 4 .   ? -2.137  -1.376  -11.607 0.80 32.40 ?  301 SAH A N9    1 
HETATM 9874  C  C8    . SAH I 4 .   ? -1.558  -0.203  -12.022 0.80 33.78 ?  301 SAH A C8    1 
HETATM 9875  N  N7    . SAH I 4 .   ? -2.406  0.790   -12.114 0.80 35.41 ?  301 SAH A N7    1 
HETATM 9876  C  C5    . SAH I 4 .   ? -3.623  0.236   -11.745 0.80 32.25 ?  301 SAH A C5    1 
HETATM 9877  C  C6    . SAH I 4 .   ? -4.916  0.781   -11.639 0.80 30.70 ?  301 SAH A C6    1 
HETATM 9878  N  N6    . SAH I 4 .   ? -5.206  2.051   -11.908 0.80 32.44 ?  301 SAH A N6    1 
HETATM 9879  N  N1    . SAH I 4 .   ? -5.912  -0.046  -11.240 0.80 28.30 ?  301 SAH A N1    1 
HETATM 9880  C  C2    . SAH I 4 .   ? -5.613  -1.323  -10.973 0.80 28.45 ?  301 SAH A C2    1 
HETATM 9881  N  N3    . SAH I 4 .   ? -4.439  -1.944  -11.037 0.80 27.93 ?  301 SAH A N3    1 
HETATM 9882  C  C4    . SAH I 4 .   ? -3.472  -1.100  -11.434 0.80 31.86 ?  301 SAH A C4    1 
HETATM 9883  ZN ZN    . ZN  J 5 .   ? 0.262   -6.131  -0.070  1.00 45.66 ?  302 ZN  A ZN    1 
HETATM 9884  N  N     . SAH K 4 .   ? -3.623  0.817   9.237   0.80 24.94 ?  301 SAH C N     1 
HETATM 9885  C  CA    . SAH K 4 .   ? -2.236  0.752   9.775   0.80 25.55 ?  301 SAH C CA    1 
HETATM 9886  C  CB    . SAH K 4 .   ? -1.972  -0.591  10.462  0.80 25.71 ?  301 SAH C CB    1 
HETATM 9887  C  CG    . SAH K 4 .   ? -2.892  -0.864  11.634  0.80 25.98 ?  301 SAH C CG    1 
HETATM 9888  S  SD    . SAH K 4 .   ? -2.871  -2.593  12.166  0.80 28.26 ?  301 SAH C SD    1 
HETATM 9889  C  C     . SAH K 4 .   ? -1.237  0.931   8.626   0.80 25.78 ?  301 SAH C C     1 
HETATM 9890  O  O     . SAH K 4 .   ? -1.505  1.794   7.768   0.80 23.65 ?  301 SAH C O     1 
HETATM 9891  O  OXT   . SAH K 4 .   ? -0.229  0.197   8.631   0.80 26.65 ?  301 SAH C OXT   1 
HETATM 9892  C  "C5'" . SAH K 4 .   ? -1.587  -2.576  13.441  0.80 27.51 ?  301 SAH C "C5'" 1 
HETATM 9893  C  "C4'" . SAH K 4 .   ? -0.346  -3.303  12.986  0.80 26.58 ?  301 SAH C "C4'" 1 
HETATM 9894  O  "O4'" . SAH K 4 .   ? 0.217   -2.625  11.838  0.80 25.91 ?  301 SAH C "O4'" 1 
HETATM 9895  C  "C3'" . SAH K 4 .   ? 0.806   -3.362  13.981  0.80 23.98 ?  301 SAH C "C3'" 1 
HETATM 9896  O  "O3'" . SAH K 4 .   ? 0.597   -4.359  14.973  0.80 20.55 ?  301 SAH C "O3'" 1 
HETATM 9897  C  "C2'" . SAH K 4 .   ? 1.948   -3.695  13.019  0.80 25.90 ?  301 SAH C "C2'" 1 
HETATM 9898  O  "O2'" . SAH K 4 .   ? 1.927   -5.038  12.586  0.80 25.28 ?  301 SAH C "O2'" 1 
HETATM 9899  C  "C1'" . SAH K 4 .   ? 1.623   -2.736  11.878  0.80 27.11 ?  301 SAH C "C1'" 1 
HETATM 9900  N  N9    . SAH K 4 .   ? 2.198   -1.414  12.085  0.80 29.02 ?  301 SAH C N9    1 
HETATM 9901  C  C8    . SAH K 4 .   ? 1.571   -0.311  12.608  0.80 29.93 ?  301 SAH C C8    1 
HETATM 9902  N  N7    . SAH K 4 .   ? 2.353   0.735   12.701  0.80 31.45 ?  301 SAH C N7    1 
HETATM 9903  C  C5    . SAH K 4 .   ? 3.577   0.291   12.223  0.80 30.68 ?  301 SAH C C5    1 
HETATM 9904  C  C6    . SAH K 4 .   ? 4.820   0.933   12.065  0.80 31.24 ?  301 SAH C C6    1 
HETATM 9905  N  N6    . SAH K 4 .   ? 5.038   2.205   12.385  0.80 29.41 ?  301 SAH C N6    1 
HETATM 9906  N  N1    . SAH K 4 .   ? 5.842   0.202   11.559  0.80 28.36 ?  301 SAH C N1    1 
HETATM 9907  C  C2    . SAH K 4 .   ? 5.613   -1.078  11.238  0.80 24.49 ?  301 SAH C C2    1 
HETATM 9908  N  N3    . SAH K 4 .   ? 4.492   -1.784  11.343  0.80 24.84 ?  301 SAH C N3    1 
HETATM 9909  C  C4    . SAH K 4 .   ? 3.498   -1.035  11.848  0.80 27.43 ?  301 SAH C C4    1 
HETATM 9910  N  N     . SAH L 4 .   ? 26.478  55.219  -1.563  0.80 20.62 ?  301 SAH H N     1 
HETATM 9911  C  CA    . SAH L 4 .   ? 25.091  54.825  -1.929  0.80 21.31 ?  301 SAH H CA    1 
HETATM 9912  C  CB    . SAH L 4 .   ? 25.074  53.473  -2.649  0.80 24.87 ?  301 SAH H CB    1 
HETATM 9913  C  CG    . SAH L 4 .   ? 25.774  53.491  -3.994  0.80 27.82 ?  301 SAH H CG    1 
HETATM 9914  S  SD    . SAH L 4 .   ? 25.875  51.859  -4.768  0.80 37.50 ?  301 SAH H SD    1 
HETATM 9915  C  C     . SAH L 4 .   ? 24.240  54.730  -0.658  0.80 20.19 ?  301 SAH H C     1 
HETATM 9916  O  O     . SAH L 4 .   ? 24.686  55.286  0.367   0.80 19.66 ?  301 SAH H O     1 
HETATM 9917  O  OXT   . SAH L 4 .   ? 23.167  54.098  -0.737  0.80 16.20 ?  301 SAH H OXT   1 
HETATM 9918  C  "C5'" . SAH L 4 .   ? 24.390  51.826  -5.804  0.80 36.19 ?  301 SAH H "C5'" 1 
HETATM 9919  C  "C4'" . SAH L 4 .   ? 23.297  50.960  -5.226  0.80 36.75 ?  301 SAH H "C4'" 1 
HETATM 9920  O  "O4'" . SAH L 4 .   ? 22.732  51.615  -4.067  0.80 37.77 ?  301 SAH H "O4'" 1 
HETATM 9921  C  "C3'" . SAH L 4 .   ? 22.108  50.699  -6.144  0.80 35.07 ?  301 SAH H "C3'" 1 
HETATM 9922  O  "O3'" . SAH L 4 .   ? 22.361  49.606  -7.018  0.80 32.77 ?  301 SAH H "O3'" 1 
HETATM 9923  C  "C2'" . SAH L 4 .   ? 21.017  50.384  -5.119  0.80 32.38 ?  301 SAH H "C2'" 1 
HETATM 9924  O  "O2'" . SAH L 4 .   ? 21.091  49.066  -4.624  0.80 34.50 ?  301 SAH H "O2'" 1 
HETATM 9925  C  "C1'" . SAH L 4 .   ? 21.338  51.404  -4.030  0.80 34.04 ?  301 SAH H "C1'" 1 
HETATM 9926  N  N9    . SAH L 4 .   ? 20.668  52.681  -4.234  0.80 32.96 ?  301 SAH H N9    1 
HETATM 9927  C  C8    . SAH L 4 .   ? 21.233  53.838  -4.708  0.80 33.18 ?  301 SAH H C8    1 
HETATM 9928  N  N7    . SAH L 4 .   ? 20.383  54.829  -4.805  0.80 33.31 ?  301 SAH H N7    1 
HETATM 9929  C  C5    . SAH L 4 .   ? 19.179  54.291  -4.376  0.80 30.59 ?  301 SAH H C5    1 
HETATM 9930  C  C6    . SAH L 4 .   ? 17.891  54.843  -4.245  0.80 30.91 ?  301 SAH H C6    1 
HETATM 9931  N  N6    . SAH L 4 .   ? 17.597  56.104  -4.547  0.80 33.13 ?  301 SAH H N6    1 
HETATM 9932  N  N1    . SAH L 4 .   ? 16.907  54.032  -3.788  0.80 28.45 ?  301 SAH H N1    1 
HETATM 9933  C  C2    . SAH L 4 .   ? 17.213  52.764  -3.487  0.80 25.57 ?  301 SAH H C2    1 
HETATM 9934  N  N3    . SAH L 4 .   ? 18.383  52.138  -3.569  0.80 24.63 ?  301 SAH H N3    1 
HETATM 9935  C  C4    . SAH L 4 .   ? 19.339  52.965  -4.025  0.80 29.82 ?  301 SAH H C4    1 
HETATM 9936  ZN ZN    . ZN  M 5 .   ? 22.756  47.765  7.590   1.00 50.38 ?  302 ZN  H ZN    1 
HETATM 9937  N  N     . SAH N 4 .   ? 19.159  55.085  16.823  0.90 32.86 ?  301 SAH J N     1 
HETATM 9938  C  CA    . SAH N 4 .   ? 20.577  54.780  17.155  0.90 32.94 ?  301 SAH J CA    1 
HETATM 9939  C  CB    . SAH N 4 .   ? 20.710  53.372  17.745  0.90 31.28 ?  301 SAH J CB    1 
HETATM 9940  C  CG    . SAH N 4 .   ? 19.935  53.186  19.033  0.90 29.05 ?  301 SAH J CG    1 
HETATM 9941  S  SD    . SAH N 4 .   ? 19.885  51.470  19.600  0.90 28.36 ?  301 SAH J SD    1 
HETATM 9942  C  C     . SAH N 4 .   ? 21.427  54.883  15.883  0.90 34.77 ?  301 SAH J C     1 
HETATM 9943  O  O     . SAH N 4 .   ? 20.895  55.406  14.884  0.90 38.86 ?  301 SAH J O     1 
HETATM 9944  O  OXT   . SAH N 4 .   ? 22.589  54.435  15.939  0.90 36.02 ?  301 SAH J OXT   1 
HETATM 9945  C  "C5'" . SAH N 4 .   ? 21.199  51.482  20.842  0.90 26.33 ?  301 SAH J "C5'" 1 
HETATM 9946  C  "C4'" . SAH N 4 .   ? 22.439  50.763  20.375  0.90 24.58 ?  301 SAH J "C4'" 1 
HETATM 9947  O  "O4'" . SAH N 4 .   ? 23.017  51.458  19.246  0.90 23.30 ?  301 SAH J "O4'" 1 
HETATM 9948  C  "C3'" . SAH N 4 .   ? 23.582  50.690  21.378  0.90 22.61 ?  301 SAH J "C3'" 1 
HETATM 9949  O  "O3'" . SAH N 4 .   ? 23.353  49.702  22.374  0.90 18.77 ?  301 SAH J "O3'" 1 
HETATM 9950  C  "C2'" . SAH N 4 .   ? 24.722  50.336  20.422  0.90 22.67 ?  301 SAH J "C2'" 1 
HETATM 9951  O  "O2'" . SAH N 4 .   ? 24.674  48.991  19.998  0.90 20.86 ?  301 SAH J "O2'" 1 
HETATM 9952  C  "C1'" . SAH N 4 .   ? 24.420  51.304  19.281  0.90 24.20 ?  301 SAH J "C1'" 1 
HETATM 9953  N  N9    . SAH N 4 .   ? 25.036  52.608  19.487  0.90 26.15 ?  301 SAH J N9    1 
HETATM 9954  C  C8    . SAH N 4 .   ? 24.457  53.719  20.046  0.90 27.92 ?  301 SAH J C8    1 
HETATM 9955  N  N7    . SAH N 4 .   ? 25.270  54.742  20.127  0.90 28.67 ?  301 SAH J N7    1 
HETATM 9956  C  C5    . SAH N 4 .   ? 26.466  54.273  19.603  0.90 27.95 ?  301 SAH J C5    1 
HETATM 9957  C  C6    . SAH N 4 .   ? 27.722  54.882  19.412  0.90 27.89 ?  301 SAH J C6    1 
HETATM 9958  N  N6    . SAH N 4 .   ? 27.990  56.142  19.742  0.90 28.18 ?  301 SAH J N6    1 
HETATM 9959  N  N1    . SAH N 4 .   ? 28.703  54.130  18.860  0.90 26.83 ?  301 SAH J N1    1 
HETATM 9960  C  C2    . SAH N 4 .   ? 28.429  52.862  18.531  0.90 23.76 ?  301 SAH J C2    1 
HETATM 9961  N  N3    . SAH N 4 .   ? 27.292  52.186  18.664  0.90 25.03 ?  301 SAH J N3    1 
HETATM 9962  C  C4    . SAH N 4 .   ? 26.337  52.955  19.212  0.90 26.81 ?  301 SAH J C4    1 
HETATM 9963  O  O     . HOH O 6 .   ? 28.548  3.869   -12.924 1.00 30.53 ?  401 HOH A O     1 
HETATM 9964  O  O     . HOH O 6 .   ? -2.451  9.796   -11.906 1.00 10.97 ?  402 HOH A O     1 
HETATM 9965  O  O     . HOH O 6 .   ? 2.023   -11.182 -15.590 1.00 27.58 ?  403 HOH A O     1 
HETATM 9966  O  O     . HOH O 6 .   ? -8.935  -9.728  4.335   1.00 29.29 ?  404 HOH A O     1 
HETATM 9967  O  O     . HOH O 6 .   ? -5.484  -11.841 8.491   1.00 11.48 ?  405 HOH A O     1 
HETATM 9968  O  O     . HOH O 6 .   ? 3.241   9.883   -2.906  1.00 4.98  ?  406 HOH A O     1 
HETATM 9969  O  O     . HOH O 6 .   ? 5.833   10.218  -17.759 1.00 14.86 ?  407 HOH A O     1 
HETATM 9970  O  O     . HOH O 6 .   ? 9.665   -0.994  -2.684  1.00 55.87 ?  408 HOH A O     1 
HETATM 9971  O  O     . HOH O 6 .   ? 6.287   8.645   -2.692  1.00 28.02 ?  409 HOH A O     1 
HETATM 9972  O  O     . HOH O 6 .   ? -0.728  10.288  -10.087 1.00 6.88  ?  410 HOH A O     1 
HETATM 9973  O  O     . HOH O 6 .   ? 17.609  13.294  -4.798  1.00 15.06 ?  411 HOH A O     1 
HETATM 9974  O  O     . HOH O 6 .   ? -2.862  -6.102  -16.534 1.00 12.76 ?  412 HOH A O     1 
HETATM 9975  O  O     . HOH O 6 .   ? -7.647  13.093  -9.036  1.00 16.69 ?  413 HOH A O     1 
HETATM 9976  O  O     . HOH O 6 .   ? -19.851 -22.779 7.417   1.00 34.47 ?  414 HOH A O     1 
HETATM 9977  O  O     . HOH O 6 .   ? -0.673  13.670  -10.467 1.00 8.99  ?  415 HOH A O     1 
HETATM 9978  O  O     . HOH O 6 .   ? -2.680  3.820   -13.427 1.00 22.39 ?  416 HOH A O     1 
HETATM 9979  O  O     . HOH O 6 .   ? 1.387   8.589   -2.812  1.00 6.61  ?  417 HOH A O     1 
HETATM 9980  O  O     . HOH O 6 .   ? -16.453 -0.362  -0.526  1.00 15.16 ?  418 HOH A O     1 
HETATM 9981  O  O     . HOH O 6 .   ? -6.094  -28.609 12.062  1.00 28.91 ?  419 HOH A O     1 
HETATM 9982  O  O     . HOH O 6 .   ? 0.063   -17.985 -29.014 1.00 20.63 ?  420 HOH A O     1 
HETATM 9983  O  O     . HOH O 6 .   ? 14.186  4.427   -26.126 1.00 36.65 ?  421 HOH A O     1 
HETATM 9984  O  O     . HOH O 6 .   ? -2.050  14.809  -23.706 1.00 22.25 ?  422 HOH A O     1 
HETATM 9985  O  O     . HOH O 6 .   ? 23.522  13.855  -0.452  1.00 8.88  ?  423 HOH A O     1 
HETATM 9986  O  O     . HOH O 6 .   ? 19.031  0.307   -1.646  1.00 29.40 ?  424 HOH A O     1 
HETATM 9987  O  O     . HOH O 6 .   ? -14.292 -24.801 -4.233  1.00 35.28 ?  425 HOH A O     1 
HETATM 9988  O  O     . HOH O 6 .   ? 3.796   23.904  1.394   1.00 31.59 ?  426 HOH A O     1 
HETATM 9989  O  O     . HOH O 6 .   ? -16.918 -13.403 9.791   1.00 26.25 ?  427 HOH A O     1 
HETATM 9990  O  O     . HOH O 6 .   ? -18.563 -15.424 13.012  1.00 30.11 ?  428 HOH A O     1 
HETATM 9991  O  O     . HOH P 6 .   ? -5.505  19.054  -1.119  1.00 42.24 ?  101 HOH B O     1 
HETATM 9992  O  O     . HOH P 6 .   ? -15.439 13.410  -29.684 1.00 23.65 ?  102 HOH B O     1 
HETATM 9993  O  O     . HOH P 6 .   ? -7.859  12.936  -6.027  1.00 17.01 ?  103 HOH B O     1 
HETATM 9994  O  O     . HOH P 6 .   ? -16.911 26.236  -23.227 1.00 29.06 ?  104 HOH B O     1 
HETATM 9995  O  O     . HOH P 6 .   ? -18.485 11.624  -11.332 1.00 34.70 ?  105 HOH B O     1 
HETATM 9996  O  O     . HOH P 6 .   ? -14.834 7.119   -32.077 1.00 5.42  ?  106 HOH B O     1 
HETATM 9997  O  O     . HOH Q 6 .   ? -20.391 -2.401  12.731  1.00 34.94 ?  401 HOH C O     1 
HETATM 9998  O  O     . HOH Q 6 .   ? -5.166  -4.204  28.541  1.00 37.66 ?  402 HOH C O     1 
HETATM 9999  O  O     . HOH Q 6 .   ? 1.725   12.283  7.774   1.00 20.35 ?  403 HOH C O     1 
HETATM 10000 O  O     . HOH Q 6 .   ? -21.333 10.323  20.252  1.00 24.32 ?  404 HOH C O     1 
HETATM 10001 O  O     . HOH Q 6 .   ? -1.548  -10.908 16.449  1.00 15.24 ?  405 HOH C O     1 
HETATM 10002 O  O     . HOH Q 6 .   ? -6.415  -28.117 9.447   1.00 21.43 ?  406 HOH C O     1 
HETATM 10003 O  O     . HOH Q 6 .   ? -14.843 4.269   -0.270  1.00 21.30 ?  407 HOH C O     1 
HETATM 10004 O  O     . HOH Q 6 .   ? 8.482   -9.863  -3.534  1.00 22.80 ?  408 HOH C O     1 
HETATM 10005 O  O     . HOH Q 6 .   ? 11.198  -17.834 -26.260 1.00 47.32 ?  409 HOH C O     1 
HETATM 10006 O  O     . HOH Q 6 .   ? -4.205  -11.304 18.845  1.00 20.32 ?  410 HOH C O     1 
HETATM 10007 O  O     . HOH Q 6 .   ? 7.929   13.196  9.459   1.00 15.47 ?  411 HOH C O     1 
HETATM 10008 O  O     . HOH Q 6 .   ? 7.566   6.211   8.058   1.00 7.85  ?  412 HOH C O     1 
HETATM 10009 O  O     . HOH Q 6 .   ? -0.572  1.964   1.418   1.00 4.03  ?  413 HOH C O     1 
HETATM 10010 O  O     . HOH Q 6 .   ? -17.160 14.280  5.056   1.00 9.40  ?  414 HOH C O     1 
HETATM 10011 O  O     . HOH Q 6 .   ? 13.527  -24.826 -11.278 1.00 40.47 ?  415 HOH C O     1 
HETATM 10012 O  O     . HOH Q 6 .   ? -1.762  -26.023 -24.640 1.00 31.77 ?  416 HOH C O     1 
HETATM 10013 O  O     . HOH Q 6 .   ? -0.378  19.194  24.441  1.00 13.45 ?  417 HOH C O     1 
HETATM 10014 O  O     . HOH Q 6 .   ? 16.001  -14.312 5.185   1.00 29.07 ?  418 HOH C O     1 
HETATM 10015 O  O     . HOH Q 6 .   ? -17.082 11.522  -0.728  1.00 35.65 ?  419 HOH C O     1 
HETATM 10016 O  O     . HOH Q 6 .   ? 19.897  -6.077  12.477  1.00 37.43 ?  420 HOH C O     1 
HETATM 10017 O  O     . HOH Q 6 .   ? 8.315   3.950   15.108  1.00 3.77  ?  421 HOH C O     1 
HETATM 10018 O  O     . HOH Q 6 .   ? -13.399 23.196  12.897  1.00 23.37 ?  422 HOH C O     1 
HETATM 10019 O  O     . HOH Q 6 .   ? 4.602   -22.525 -28.273 1.00 17.85 ?  423 HOH C O     1 
HETATM 10020 O  O     . HOH Q 6 .   ? 1.900   -29.461 -21.806 1.00 29.21 ?  424 HOH C O     1 
HETATM 10021 O  O     . HOH Q 6 .   ? 6.523   11.596  5.343   1.00 12.97 ?  425 HOH C O     1 
HETATM 10022 O  O     . HOH Q 6 .   ? 6.387   -22.629 24.073  1.00 44.07 ?  426 HOH C O     1 
HETATM 10023 O  O     . HOH Q 6 .   ? -14.077 18.655  2.720   1.00 23.26 ?  427 HOH C O     1 
HETATM 10024 O  O     . HOH Q 6 .   ? 7.733   -8.824  23.289  1.00 33.50 ?  428 HOH C O     1 
HETATM 10025 O  O     . HOH Q 6 .   ? -20.503 6.240   22.611  1.00 17.67 ?  429 HOH C O     1 
HETATM 10026 O  O     . HOH Q 6 .   ? -20.792 21.712  11.802  1.00 42.68 ?  430 HOH C O     1 
HETATM 10027 O  O     . HOH Q 6 .   ? -10.783 -10.520 29.435  1.00 36.88 ?  431 HOH C O     1 
HETATM 10028 O  O     . HOH Q 6 .   ? -1.072  3.983   20.940  1.00 2.70  ?  432 HOH C O     1 
HETATM 10029 O  O     . HOH Q 6 .   ? -1.588  21.771  0.059   1.00 23.07 ?  433 HOH C O     1 
HETATM 10030 O  O     . HOH Q 6 .   ? -14.085 -5.102  14.692  1.00 37.45 ?  434 HOH C O     1 
HETATM 10031 O  O     . HOH R 6 .   ? 8.109   13.484  6.504   1.00 5.54  ?  101 HOH D O     1 
HETATM 10032 O  O     . HOH R 6 .   ? 20.024  26.386  19.558  1.00 25.01 ?  102 HOH D O     1 
HETATM 10033 O  O     . HOH R 6 .   ? 1.176   21.342  8.456   1.00 20.55 ?  103 HOH D O     1 
HETATM 10034 O  O     . HOH R 6 .   ? 27.479  22.900  10.846  1.00 32.25 ?  104 HOH D O     1 
HETATM 10035 O  O     . HOH R 6 .   ? 6.956   21.901  21.136  1.00 18.23 ?  105 HOH D O     1 
HETATM 10036 O  O     . HOH R 6 .   ? 2.584   21.441  3.537   1.00 20.99 ?  106 HOH D O     1 
HETATM 10037 O  O     . HOH R 6 .   ? 5.232   23.963  12.635  1.00 31.64 ?  107 HOH D O     1 
HETATM 10038 O  O     . HOH R 6 .   ? 27.784  15.227  3.175   1.00 46.02 ?  108 HOH D O     1 
HETATM 10039 O  O     . HOH R 6 .   ? 4.390   10.462  27.009  1.00 17.38 ?  109 HOH D O     1 
HETATM 10040 O  O     . HOH R 6 .   ? 18.215  25.316  7.375   1.00 50.86 ?  110 HOH D O     1 
HETATM 10041 O  O     . HOH R 6 .   ? 28.076  14.152  20.336  1.00 25.10 ?  111 HOH D O     1 
HETATM 10042 O  O     . HOH R 6 .   ? 23.837  23.174  2.559   1.00 11.27 ?  112 HOH D O     1 
HETATM 10043 O  O     . HOH R 6 .   ? 11.414  17.653  30.938  1.00 26.69 ?  113 HOH D O     1 
HETATM 10044 O  O     . HOH S 6 .   ? 11.559  39.015  32.138  1.00 32.10 ?  401 HOH H O     1 
HETATM 10045 O  O     . HOH S 6 .   ? 20.452  63.810  -4.623  1.00 9.69  ?  402 HOH H O     1 
HETATM 10046 O  O     . HOH S 6 .   ? 13.730  32.271  14.629  1.00 31.34 ?  403 HOH H O     1 
HETATM 10047 O  O     . HOH S 6 .   ? 47.013  72.063  1.175   1.00 21.22 ?  404 HOH H O     1 
HETATM 10048 O  O     . HOH S 6 .   ? 44.799  56.605  -14.747 1.00 30.55 ?  405 HOH H O     1 
HETATM 10049 O  O     . HOH S 6 .   ? 6.552   55.851  2.856   1.00 30.74 ?  406 HOH H O     1 
HETATM 10050 O  O     . HOH S 6 .   ? 28.494  64.249  -10.297 1.00 5.68  ?  407 HOH H O     1 
HETATM 10051 O  O     . HOH S 6 .   ? 12.900  58.521  -0.235  1.00 26.55 ?  408 HOH H O     1 
HETATM 10052 O  O     . HOH S 6 .   ? 24.003  62.814  4.741   1.00 15.77 ?  409 HOH H O     1 
HETATM 10053 O  O     . HOH S 6 .   ? 27.005  73.846  6.922   1.00 19.37 ?  410 HOH H O     1 
HETATM 10054 O  O     . HOH S 6 .   ? 46.412  70.631  2.506   1.00 37.03 ?  411 HOH H O     1 
HETATM 10055 O  O     . HOH S 6 .   ? 26.152  63.980  4.625   1.00 4.28  ?  412 HOH H O     1 
HETATM 10056 O  O     . HOH S 6 .   ? 15.114  67.282  -1.563  1.00 5.63  ?  413 HOH H O     1 
HETATM 10057 O  O     . HOH S 6 .   ? 9.684   46.869  14.595  1.00 36.61 ?  414 HOH H O     1 
HETATM 10058 O  O     . HOH S 6 .   ? 21.967  67.927  -3.087  1.00 10.84 ?  415 HOH H O     1 
HETATM 10059 O  O     . HOH S 6 .   ? 37.974  57.980  7.791   1.00 9.00  ?  416 HOH H O     1 
HETATM 10060 O  O     . HOH S 6 .   ? 10.247  46.950  11.874  1.00 24.41 ?  417 HOH H O     1 
HETATM 10061 O  O     . HOH S 6 .   ? 20.046  57.887  -5.900  1.00 20.91 ?  418 HOH H O     1 
HETATM 10062 O  O     . HOH S 6 .   ? 19.939  47.981  -9.149  1.00 10.13 ?  419 HOH H O     1 
HETATM 10063 O  O     . HOH S 6 .   ? 15.449  60.011  -0.216  1.00 14.38 ?  420 HOH H O     1 
HETATM 10064 O  O     . HOH S 6 .   ? 28.184  42.064  -0.496  1.00 22.04 ?  421 HOH H O     1 
HETATM 10065 O  O     . HOH S 6 .   ? 21.965  64.348  -2.669  1.00 9.67  ?  422 HOH H O     1 
HETATM 10066 O  O     . HOH S 6 .   ? 31.886  76.062  -11.989 1.00 21.50 ?  423 HOH H O     1 
HETATM 10067 O  O     . HOH S 6 .   ? 39.473  64.007  -17.155 1.00 30.36 ?  424 HOH H O     1 
HETATM 10068 O  O     . HOH S 6 .   ? 19.615  49.099  0.509   1.00 32.41 ?  425 HOH H O     1 
HETATM 10069 O  O     . HOH S 6 .   ? 34.812  47.472  -10.026 1.00 20.24 ?  426 HOH H O     1 
HETATM 10070 O  O     . HOH S 6 .   ? 12.332  35.074  35.493  1.00 32.16 ?  427 HOH H O     1 
HETATM 10071 O  O     . HOH S 6 .   ? 6.189   53.916  7.109   1.00 14.47 ?  428 HOH H O     1 
HETATM 10072 O  O     . HOH S 6 .   ? 6.549   66.670  -1.160  1.00 50.49 ?  429 HOH H O     1 
HETATM 10073 O  O     . HOH S 6 .   ? 43.152  55.654  -18.404 1.00 31.89 ?  430 HOH H O     1 
HETATM 10074 O  O     . HOH S 6 .   ? 9.093   24.920  26.215  1.00 42.53 ?  431 HOH H O     1 
HETATM 10075 O  O     . HOH S 6 .   ? 31.969  79.965  -0.120  1.00 46.27 ?  432 HOH H O     1 
HETATM 10076 O  O     . HOH S 6 .   ? 4.826   62.961  -2.752  1.00 27.64 ?  433 HOH H O     1 
HETATM 10077 O  O     . HOH S 6 .   ? 26.210  29.560  5.466   1.00 45.88 ?  434 HOH H O     1 
HETATM 10078 O  O     . HOH S 6 .   ? 26.415  26.948  1.199   1.00 24.72 ?  435 HOH H O     1 
HETATM 10079 O  O     . HOH S 6 .   ? 25.784  25.483  -0.814  1.00 13.34 ?  436 HOH H O     1 
HETATM 10080 O  O     . HOH S 6 .   ? 25.245  62.194  -17.229 1.00 28.71 ?  437 HOH H O     1 
HETATM 10081 O  O     . HOH S 6 .   ? 42.514  44.023  -14.012 1.00 26.05 ?  438 HOH H O     1 
HETATM 10082 O  O     . HOH T 6 .   ? 1.946   58.930  -12.783 1.00 26.55 ?  101 HOH I O     1 
HETATM 10083 O  O     . HOH T 6 .   ? 14.907  67.272  1.203   1.00 22.87 ?  102 HOH I O     1 
HETATM 10084 O  O     . HOH T 6 .   ? -5.227  74.155  -11.896 1.00 22.65 ?  103 HOH I O     1 
HETATM 10085 O  O     . HOH T 6 .   ? 5.848   65.803  7.308   1.00 28.06 ?  104 HOH I O     1 
HETATM 10086 O  O     . HOH T 6 .   ? -0.679  65.932  -19.757 1.00 22.63 ?  105 HOH I O     1 
HETATM 10087 O  O     . HOH T 6 .   ? 18.134  75.176  5.428   1.00 12.64 ?  106 HOH I O     1 
HETATM 10088 O  O     . HOH T 6 .   ? 21.060  74.507  6.177   1.00 18.95 ?  107 HOH I O     1 
HETATM 10089 O  O     . HOH U 6 .   ? 17.988  57.607  39.301  1.00 24.91 ?  401 HOH J O     1 
HETATM 10090 O  O     . HOH U 6 .   ? 16.772  32.062  11.759  1.00 26.55 ?  402 HOH J O     1 
HETATM 10091 O  O     . HOH U 6 .   ? 31.152  44.411  3.846   1.00 19.82 ?  403 HOH J O     1 
HETATM 10092 O  O     . HOH U 6 .   ? 39.376  50.487  3.870   1.00 26.25 ?  404 HOH J O     1 
HETATM 10093 O  O     . HOH U 6 .   ? 29.587  32.063  -20.384 1.00 33.64 ?  405 HOH J O     1 
HETATM 10094 O  O     . HOH U 6 .   ? 36.688  33.163  26.276  1.00 34.91 ?  406 HOH J O     1 
HETATM 10095 O  O     . HOH U 6 .   ? 16.472  47.906  31.066  1.00 27.91 ?  407 HOH J O     1 
HETATM 10096 O  O     . HOH U 6 .   ? 21.284  43.138  24.083  1.00 13.56 ?  408 HOH J O     1 
HETATM 10097 O  O     . HOH U 6 .   ? 24.467  66.370  15.096  1.00 21.45 ?  409 HOH J O     1 
HETATM 10098 O  O     . HOH U 6 .   ? 19.348  33.740  34.968  1.00 17.83 ?  410 HOH J O     1 
HETATM 10099 O  O     . HOH U 6 .   ? 16.473  62.906  9.890   1.00 9.01  ?  411 HOH J O     1 
HETATM 10100 O  O     . HOH U 6 .   ? 18.040  45.079  28.302  1.00 26.41 ?  412 HOH J O     1 
HETATM 10101 O  O     . HOH U 6 .   ? -2.209  66.039  10.635  1.00 10.17 ?  413 HOH J O     1 
HETATM 10102 O  O     . HOH U 6 .   ? -4.099  65.104  10.245  1.00 17.22 ?  414 HOH J O     1 
HETATM 10103 O  O     . HOH U 6 .   ? 25.790  48.334  24.016  1.00 23.72 ?  415 HOH J O     1 
HETATM 10104 O  O     . HOH U 6 .   ? 21.030  28.112  -17.130 1.00 16.76 ?  416 HOH J O     1 
HETATM 10105 O  O     . HOH U 6 .   ? 30.820  67.118  16.884  1.00 27.60 ?  417 HOH J O     1 
HETATM 10106 O  O     . HOH U 6 .   ? 5.609   68.219  12.682  1.00 13.01 ?  418 HOH J O     1 
HETATM 10107 O  O     . HOH U 6 .   ? 12.669  40.417  27.127  1.00 38.29 ?  419 HOH J O     1 
HETATM 10108 O  O     . HOH U 6 .   ? 22.168  31.534  -17.719 1.00 28.76 ?  420 HOH J O     1 
HETATM 10109 O  O     . HOH U 6 .   ? 27.284  31.183  -20.492 1.00 19.51 ?  421 HOH J O     1 
HETATM 10110 O  O     . HOH U 6 .   ? 24.608  30.706  -19.507 1.00 28.64 ?  422 HOH J O     1 
HETATM 10111 O  O     . HOH U 6 .   ? 23.592  75.114  16.034  1.00 23.13 ?  423 HOH J O     1 
HETATM 10112 O  O     . HOH U 6 .   ? 40.103  41.683  11.886  1.00 18.49 ?  424 HOH J O     1 
HETATM 10113 O  O     . HOH U 6 .   ? 21.965  36.161  35.335  1.00 28.46 ?  425 HOH J O     1 
HETATM 10114 O  O     . HOH U 6 .   ? 17.598  42.128  15.917  1.00 15.37 ?  426 HOH J O     1 
HETATM 10115 O  O     . HOH U 6 .   ? 20.396  48.764  37.604  1.00 28.68 ?  427 HOH J O     1 
HETATM 10116 O  O     . HOH U 6 .   ? 9.413   77.087  20.865  1.00 22.57 ?  428 HOH J O     1 
HETATM 10117 O  O     . HOH U 6 .   ? 21.160  30.057  15.665  1.00 18.43 ?  429 HOH J O     1 
HETATM 10118 O  O     . HOH U 6 .   ? 31.027  58.020  22.564  1.00 8.70  ?  430 HOH J O     1 
HETATM 10119 O  O     . HOH U 6 .   ? 31.736  34.851  35.889  1.00 23.43 ?  431 HOH J O     1 
HETATM 10120 O  O     . HOH U 6 .   ? 37.504  37.264  -8.529  1.00 23.06 ?  432 HOH J O     1 
HETATM 10121 O  O     . HOH U 6 .   ? 22.564  29.814  17.879  1.00 28.65 ?  433 HOH J O     1 
HETATM 10122 O  O     . HOH U 6 .   ? -4.865  54.762  17.247  1.00 46.15 ?  434 HOH J O     1 
HETATM 10123 O  O     . HOH U 6 .   ? 37.907  45.519  11.083  1.00 41.56 ?  435 HOH J O     1 
HETATM 10124 O  O     . HOH U 6 .   ? 33.267  55.418  29.348  1.00 40.58 ?  436 HOH J O     1 
HETATM 10125 O  O     . HOH U 6 .   ? 23.379  27.437  7.826   1.00 50.81 ?  437 HOH J O     1 
HETATM 10126 O  O     . HOH U 6 .   ? 43.292  34.292  -10.922 1.00 29.08 ?  438 HOH J O     1 
HETATM 10127 O  O     . HOH V 6 .   ? 31.043  67.555  13.894  1.00 7.70  ?  101 HOH K O     1 
HETATM 10128 O  O     . HOH V 6 .   ? 42.296  79.662  27.251  1.00 24.05 ?  102 HOH K O     1 
HETATM 10129 O  O     . HOH V 6 .   ? 30.622  73.054  35.546  1.00 24.87 ?  103 HOH K O     1 
HETATM 10130 O  O     . HOH V 6 .   ? 37.585  56.312  26.897  1.00 28.07 ?  104 HOH K O     1 
HETATM 10131 O  O     . HOH V 6 .   ? 37.312  56.906  33.338  1.00 24.39 ?  105 HOH K O     1 
HETATM 10132 O  O     . HOH V 6 .   ? 43.746  56.042  30.040  1.00 32.02 ?  106 HOH K O     1 
# 
