data_9CHI
# 
_entry.id   9CHI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9CHI         pdb_00009chi 10.2210/pdb9chi/pdb 
WWPDB D_1000285510 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CHI 
_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-Y62A) heteromeric complex (bound to SAH - structure 1)' 
9CH7 unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-L63D) heteromeric complex (bound to SAM)' 9CH5 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-L63D) heteromeric complex (bound to SAH)' 9CH3 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-L63D) heteromeric complex' 9CH2 unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (bound to SAM)' 9CH1 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (bound to SAH)' 9CH0 
unspecified 
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 Alpha-N-methyltransferase 28937.131 4   ? ?    ? ? 
2 polymer     man SonA                      7411.169  3   ? Y62A ? ? 
3 polymer     man SonA                      7397.143  1   ? Y62A ? ? 
4 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE 384.411   4   ? ?    ? ? 
5 water       nat water                     18.015    306 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        SonM 
# 
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  
;GSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILDA
VRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPTT
HLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIPP
AKKLEYNYAILAKLGIGPEDLG
;
;GSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILDA
VRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPTT
HLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIPP
AKKLEYNYAILAKLGIGPEDLG
;
A,C,E,G ? 
2 'polypeptide(L)' no yes 'GLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSALV(IML)SHGNG' 
GLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSALVISHGNG B,F,H   ? 
3 'polypeptide(L)' no no  GLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSALVISHGNG 
GLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSALVISHGNG D       ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 S-ADENOSYL-L-HOMOCYSTEINE SAH 
5 water                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   LEU n 
1 4   VAL n 
1 5   CYS n 
1 6   VAL n 
1 7   GLY n 
1 8   THR n 
1 9   GLY n 
1 10  LEU n 
1 11  GLN n 
1 12  LEU n 
1 13  ALA n 
1 14  GLY n 
1 15  GLN n 
1 16  ILE n 
1 17  SER n 
1 18  VAL n 
1 19  LEU n 
1 20  SER n 
1 21  ARG n 
1 22  SER n 
1 23  TYR n 
1 24  ILE n 
1 25  GLU n 
1 26  HIS n 
1 27  ALA n 
1 28  ASP n 
1 29  ILE n 
1 30  VAL n 
1 31  PHE n 
1 32  SER n 
1 33  LEU n 
1 34  LEU n 
1 35  PRO n 
1 36  ASP n 
1 37  GLY n 
1 38  PHE n 
1 39  SER n 
1 40  GLN n 
1 41  ARG n 
1 42  TRP n 
1 43  LEU n 
1 44  THR n 
1 45  LYS n 
1 46  LEU n 
1 47  ASN n 
1 48  PRO n 
1 49  ASN n 
1 50  VAL n 
1 51  ILE n 
1 52  ASN n 
1 53  LEU n 
1 54  GLN n 
1 55  GLN n 
1 56  PHE n 
1 57  TYR n 
1 58  ALA n 
1 59  GLN n 
1 60  ASN n 
1 61  GLY n 
1 62  GLU n 
1 63  VAL n 
1 64  LYS n 
1 65  ASN n 
1 66  ARG n 
1 67  ARG n 
1 68  ASP n 
1 69  THR n 
1 70  TYR n 
1 71  GLU n 
1 72  GLN n 
1 73  MET n 
1 74  VAL n 
1 75  ASN n 
1 76  ALA n 
1 77  ILE n 
1 78  LEU n 
1 79  ASP n 
1 80  ALA n 
1 81  VAL n 
1 82  ARG n 
1 83  ALA n 
1 84  GLY n 
1 85  LYS n 
1 86  LYS n 
1 87  THR n 
1 88  VAL n 
1 89  CYS n 
1 90  ALA n 
1 91  LEU n 
1 92  TYR n 
1 93  GLY n 
1 94  HIS n 
1 95  PRO n 
1 96  GLY n 
1 97  VAL n 
1 98  PHE n 
1 99  ALA n 
1 100 CYS n 
1 101 VAL n 
1 102 SER n 
1 103 HIS n 
1 104 MET n 
1 105 ALA n 
1 106 ILE n 
1 107 THR n 
1 108 ARG n 
1 109 ALA n 
1 110 LYS n 
1 111 ALA n 
1 112 GLU n 
1 113 GLY n 
1 114 PHE n 
1 115 SER n 
1 116 ALA n 
1 117 LYS n 
1 118 MET n 
1 119 GLU n 
1 120 PRO n 
1 121 GLY n 
1 122 ILE n 
1 123 SER n 
1 124 ALA n 
1 125 GLU n 
1 126 ALA n 
1 127 CYS n 
1 128 LEU n 
1 129 TRP n 
1 130 ALA n 
1 131 ASP n 
1 132 LEU n 
1 133 GLY n 
1 134 ILE n 
1 135 ASP n 
1 136 PRO n 
1 137 GLY n 
1 138 ASN n 
1 139 SER n 
1 140 GLY n 
1 141 HIS n 
1 142 GLN n 
1 143 SER n 
1 144 PHE n 
1 145 GLU n 
1 146 ALA n 
1 147 SER n 
1 148 GLN n 
1 149 PHE n 
1 150 MET n 
1 151 PHE n 
1 152 PHE n 
1 153 ASN n 
1 154 HIS n 
1 155 VAL n 
1 156 PRO n 
1 157 ASP n 
1 158 PRO n 
1 159 THR n 
1 160 THR n 
1 161 HIS n 
1 162 LEU n 
1 163 LEU n 
1 164 LEU n 
1 165 TRP n 
1 166 GLN n 
1 167 ILE n 
1 168 ALA n 
1 169 ILE n 
1 170 ALA n 
1 171 GLY n 
1 172 GLU n 
1 173 HIS n 
1 174 THR n 
1 175 LEU n 
1 176 THR n 
1 177 GLN n 
1 178 PHE n 
1 179 HIS n 
1 180 THR n 
1 181 SER n 
1 182 SER n 
1 183 ASP n 
1 184 ARG n 
1 185 LEU n 
1 186 GLN n 
1 187 ILE n 
1 188 LEU n 
1 189 VAL n 
1 190 GLU n 
1 191 GLN n 
1 192 LEU n 
1 193 ASN n 
1 194 GLN n 
1 195 TRP n 
1 196 TYR n 
1 197 PRO n 
1 198 LEU n 
1 199 ASP n 
1 200 HIS n 
1 201 GLU n 
1 202 VAL n 
1 203 VAL n 
1 204 ILE n 
1 205 TYR n 
1 206 GLU n 
1 207 ALA n 
1 208 ALA n 
1 209 ASN n 
1 210 LEU n 
1 211 PRO n 
1 212 ILE n 
1 213 GLN n 
1 214 ALA n 
1 215 PRO n 
1 216 ARG n 
1 217 ILE n 
1 218 GLU n 
1 219 ARG n 
1 220 LEU n 
1 221 PRO n 
1 222 LEU n 
1 223 ALA n 
1 224 ASN n 
1 225 LEU n 
1 226 PRO n 
1 227 GLN n 
1 228 ALA n 
1 229 HIS n 
1 230 LEU n 
1 231 MET n 
1 232 PRO n 
1 233 ILE n 
1 234 SER n 
1 235 THR n 
1 236 LEU n 
1 237 LEU n 
1 238 ILE n 
1 239 PRO n 
1 240 PRO n 
1 241 ALA n 
1 242 LYS n 
1 243 LYS n 
1 244 LEU n 
1 245 GLU n 
1 246 TYR n 
1 247 ASN n 
1 248 TYR n 
1 249 ALA n 
1 250 ILE n 
1 251 LEU n 
1 252 ALA n 
1 253 LYS n 
1 254 LEU n 
1 255 GLY n 
1 256 ILE n 
1 257 GLY n 
1 258 PRO n 
1 259 GLU n 
1 260 ASP n 
1 261 LEU n 
1 262 GLY n 
2 1   GLY n 
2 2   LEU n 
2 3   SER n 
2 4   ASP n 
2 5   PHE n 
2 6   PHE n 
2 7   THR n 
2 8   GLN n 
2 9   LEU n 
2 10  GLY n 
2 11  GLN n 
2 12  ASP n 
2 13  ALA n 
2 14  GLN n 
2 15  LEU n 
2 16  MET n 
2 17  GLU n 
2 18  ASP n 
2 19  TYR n 
2 20  LYS n 
2 21  GLN n 
2 22  ASN n 
2 23  PRO n 
2 24  GLU n 
2 25  ALA n 
2 26  VAL n 
2 27  MET n 
2 28  ARG n 
2 29  ALA n 
2 30  HIS n 
2 31  GLY n 
2 32  LEU n 
2 33  THR n 
2 34  ASP n 
2 35  GLU n 
2 36  GLN n 
2 37  ILE n 
2 38  ASN n 
2 39  ALA n 
2 40  VAL n 
2 41  MET n 
2 42  THR n 
2 43  GLY n 
2 44  ASP n 
2 45  MET n 
2 46  GLU n 
2 47  LYS n 
2 48  LEU n 
2 49  LYS n 
2 50  THR n 
2 51  LEU n 
2 52  SER n 
2 53  GLY n 
2 54  ASP n 
2 55  SER n 
2 56  SER n 
2 57  TYR n 
2 58  GLN n 
2 59  SER n 
2 60  ALA n 
2 61  LEU n 
2 62  VAL n 
2 63  IML n 
2 64  SER n 
2 65  HIS n 
2 66  GLY n 
2 67  ASN n 
2 68  GLY n 
3 1   GLY n 
3 2   LEU n 
3 3   SER n 
3 4   ASP n 
3 5   PHE n 
3 6   PHE n 
3 7   THR n 
3 8   GLN n 
3 9   LEU n 
3 10  GLY n 
3 11  GLN n 
3 12  ASP n 
3 13  ALA n 
3 14  GLN n 
3 15  LEU n 
3 16  MET n 
3 17  GLU n 
3 18  ASP n 
3 19  TYR n 
3 20  LYS n 
3 21  GLN n 
3 22  ASN n 
3 23  PRO n 
3 24  GLU n 
3 25  ALA n 
3 26  VAL n 
3 27  MET n 
3 28  ARG n 
3 29  ALA n 
3 30  HIS n 
3 31  GLY n 
3 32  LEU n 
3 33  THR n 
3 34  ASP n 
3 35  GLU n 
3 36  GLN n 
3 37  ILE n 
3 38  ASN n 
3 39  ALA n 
3 40  VAL n 
3 41  MET n 
3 42  THR n 
3 43  GLY n 
3 44  ASP n 
3 45  MET n 
3 46  GLU n 
3 47  LYS n 
3 48  LEU n 
3 49  LYS n 
3 50  THR n 
3 51  LEU n 
3 52  SER n 
3 53  GLY n 
3 54  ASP n 
3 55  SER n 
3 56  SER n 
3 57  TYR n 
3 58  GLN n 
3 59  SER n 
3 60  ALA n 
3 61  LEU n 
3 62  VAL n 
3 63  ILE n 
3 64  SER n 
3 65  HIS n 
3 66  GLY n 
3 67  ASN n 
3 68  GLY 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' 1 262 ? ? SO_1478 ? ? ? ? ? ? 'Shewanella oneidensis MR-1' 211586 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 68  ? ? SO_1479 ? ? ? ? ? ? 'Shewanella oneidensis MR-1' 211586 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 68  ? ? SO_1479 ? ? ? ? ? ? 'Shewanella oneidensis MR-1' 211586 ? ? ? ? ? ? ? ? 
'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 
IML 'L-peptide linking' n N-METHYL-ISOLEUCINE       ? 'C7 H15 N O2'     145.199 
LEU 'L-peptide linking' y LEUCINE                   ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                    ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE             ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                   ? 'C5 H9 N O2'      115.130 
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 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   2   GLY GLY A . n 
A 1 2   SER 2   3   3   SER SER A . n 
A 1 3   LEU 3   4   4   LEU LEU A . n 
A 1 4   VAL 4   5   5   VAL VAL A . n 
A 1 5   CYS 5   6   6   CYS CYS A . n 
A 1 6   VAL 6   7   7   VAL VAL A . n 
A 1 7   GLY 7   8   8   GLY GLY A . n 
A 1 8   THR 8   9   9   THR THR A . n 
A 1 9   GLY 9   10  10  GLY GLY A . n 
A 1 10  LEU 10  11  11  LEU LEU A . n 
A 1 11  GLN 11  12  12  GLN GLN A . n 
A 1 12  LEU 12  13  13  LEU LEU A . n 
A 1 13  ALA 13  14  14  ALA ALA A . n 
A 1 14  GLY 14  15  15  GLY GLY A . n 
A 1 15  GLN 15  16  16  GLN GLN A . n 
A 1 16  ILE 16  17  17  ILE ILE A . n 
A 1 17  SER 17  18  18  SER SER A . n 
A 1 18  VAL 18  19  19  VAL VAL A . n 
A 1 19  LEU 19  20  20  LEU LEU A . n 
A 1 20  SER 20  21  21  SER SER A . n 
A 1 21  ARG 21  22  22  ARG ARG A . n 
A 1 22  SER 22  23  23  SER SER A . n 
A 1 23  TYR 23  24  24  TYR TYR A . n 
A 1 24  ILE 24  25  25  ILE ILE A . n 
A 1 25  GLU 25  26  26  GLU GLU A . n 
A 1 26  HIS 26  27  27  HIS HIS A . n 
A 1 27  ALA 27  28  28  ALA ALA A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  ILE 29  30  30  ILE ILE A . n 
A 1 30  VAL 30  31  31  VAL VAL A . n 
A 1 31  PHE 31  32  32  PHE PHE A . n 
A 1 32  SER 32  33  33  SER SER A . n 
A 1 33  LEU 33  34  34  LEU LEU A . n 
A 1 34  LEU 34  35  35  LEU LEU A . n 
A 1 35  PRO 35  36  36  PRO PRO A . n 
A 1 36  ASP 36  37  37  ASP ASP A . n 
A 1 37  GLY 37  38  38  GLY GLY A . n 
A 1 38  PHE 38  39  39  PHE PHE A . n 
A 1 39  SER 39  40  40  SER SER A . n 
A 1 40  GLN 40  41  41  GLN GLN A . n 
A 1 41  ARG 41  42  42  ARG ARG A . n 
A 1 42  TRP 42  43  43  TRP TRP A . n 
A 1 43  LEU 43  44  44  LEU LEU A . n 
A 1 44  THR 44  45  45  THR THR A . n 
A 1 45  LYS 45  46  46  LYS LYS A . n 
A 1 46  LEU 46  47  47  LEU LEU A . n 
A 1 47  ASN 47  48  48  ASN ASN A . n 
A 1 48  PRO 48  49  49  PRO PRO A . n 
A 1 49  ASN 49  50  50  ASN ASN A . n 
A 1 50  VAL 50  51  51  VAL VAL A . n 
A 1 51  ILE 51  52  52  ILE ILE A . n 
A 1 52  ASN 52  53  53  ASN ASN A . n 
A 1 53  LEU 53  54  54  LEU LEU A . n 
A 1 54  GLN 54  55  55  GLN GLN A . n 
A 1 55  GLN 55  56  56  GLN GLN A . n 
A 1 56  PHE 56  57  57  PHE PHE A . n 
A 1 57  TYR 57  58  58  TYR TYR A . n 
A 1 58  ALA 58  59  59  ALA ALA A . n 
A 1 59  GLN 59  60  60  GLN GLN A . n 
A 1 60  ASN 60  61  61  ASN ASN A . n 
A 1 61  GLY 61  62  62  GLY GLY A . n 
A 1 62  GLU 62  63  63  GLU GLU A . n 
A 1 63  VAL 63  64  64  VAL VAL A . n 
A 1 64  LYS 64  65  65  LYS LYS A . n 
A 1 65  ASN 65  66  66  ASN ASN A . n 
A 1 66  ARG 66  67  67  ARG ARG A . n 
A 1 67  ARG 67  68  68  ARG ARG A . n 
A 1 68  ASP 68  69  69  ASP ASP A . n 
A 1 69  THR 69  70  70  THR THR A . n 
A 1 70  TYR 70  71  71  TYR TYR A . n 
A 1 71  GLU 71  72  72  GLU GLU A . n 
A 1 72  GLN 72  73  73  GLN GLN A . n 
A 1 73  MET 73  74  74  MET MET A . n 
A 1 74  VAL 74  75  75  VAL VAL A . n 
A 1 75  ASN 75  76  76  ASN ASN A . n 
A 1 76  ALA 76  77  77  ALA ALA A . n 
A 1 77  ILE 77  78  78  ILE ILE A . n 
A 1 78  LEU 78  79  79  LEU LEU A . n 
A 1 79  ASP 79  80  80  ASP ASP A . n 
A 1 80  ALA 80  81  81  ALA ALA A . n 
A 1 81  VAL 81  82  82  VAL VAL A . n 
A 1 82  ARG 82  83  83  ARG ARG A . n 
A 1 83  ALA 83  84  84  ALA ALA A . n 
A 1 84  GLY 84  85  85  GLY GLY A . n 
A 1 85  LYS 85  86  86  LYS LYS A . n 
A 1 86  LYS 86  87  87  LYS LYS A . n 
A 1 87  THR 87  88  88  THR THR A . n 
A 1 88  VAL 88  89  89  VAL VAL A . n 
A 1 89  CYS 89  90  90  CYS CYS A . n 
A 1 90  ALA 90  91  91  ALA ALA A . n 
A 1 91  LEU 91  92  92  LEU LEU A . n 
A 1 92  TYR 92  93  93  TYR TYR A . n 
A 1 93  GLY 93  94  94  GLY GLY A . n 
A 1 94  HIS 94  95  95  HIS HIS A . n 
A 1 95  PRO 95  96  96  PRO PRO A . n 
A 1 96  GLY 96  97  97  GLY GLY A . n 
A 1 97  VAL 97  98  98  VAL VAL A . n 
A 1 98  PHE 98  99  99  PHE PHE A . n 
A 1 99  ALA 99  100 100 ALA ALA A . n 
A 1 100 CYS 100 101 101 CYS CYS A . n 
A 1 101 VAL 101 102 102 VAL VAL A . n 
A 1 102 SER 102 103 103 SER SER A . n 
A 1 103 HIS 103 104 104 HIS HIS A . n 
A 1 104 MET 104 105 105 MET MET A . n 
A 1 105 ALA 105 106 106 ALA ALA A . n 
A 1 106 ILE 106 107 107 ILE ILE A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ARG 108 109 109 ARG ARG A . n 
A 1 109 ALA 109 110 110 ALA ALA A . n 
A 1 110 LYS 110 111 111 LYS LYS A . n 
A 1 111 ALA 111 112 112 ALA ALA A . n 
A 1 112 GLU 112 113 113 GLU GLU A . n 
A 1 113 GLY 113 114 114 GLY GLY A . n 
A 1 114 PHE 114 115 115 PHE PHE A . n 
A 1 115 SER 115 116 116 SER SER A . n 
A 1 116 ALA 116 117 117 ALA ALA A . n 
A 1 117 LYS 117 118 118 LYS LYS A . n 
A 1 118 MET 118 119 119 MET MET A . n 
A 1 119 GLU 119 120 120 GLU GLU A . n 
A 1 120 PRO 120 121 121 PRO PRO A . n 
A 1 121 GLY 121 122 122 GLY GLY A . n 
A 1 122 ILE 122 123 123 ILE ILE A . n 
A 1 123 SER 123 124 124 SER SER A . n 
A 1 124 ALA 124 125 125 ALA ALA A . n 
A 1 125 GLU 125 126 126 GLU GLU A . n 
A 1 126 ALA 126 127 127 ALA ALA A . n 
A 1 127 CYS 127 128 128 CYS CYS A . n 
A 1 128 LEU 128 129 129 LEU LEU A . n 
A 1 129 TRP 129 130 130 TRP TRP A . n 
A 1 130 ALA 130 131 131 ALA ALA A . n 
A 1 131 ASP 131 132 132 ASP ASP A . n 
A 1 132 LEU 132 133 133 LEU LEU A . n 
A 1 133 GLY 133 134 134 GLY GLY A . n 
A 1 134 ILE 134 135 135 ILE ILE A . n 
A 1 135 ASP 135 136 136 ASP ASP A . n 
A 1 136 PRO 136 137 137 PRO PRO A . n 
A 1 137 GLY 137 138 138 GLY GLY A . n 
A 1 138 ASN 138 139 139 ASN ASN A . n 
A 1 139 SER 139 140 140 SER SER A . n 
A 1 140 GLY 140 141 141 GLY GLY A . n 
A 1 141 HIS 141 142 142 HIS HIS A . n 
A 1 142 GLN 142 143 143 GLN GLN A . n 
A 1 143 SER 143 144 144 SER SER A . n 
A 1 144 PHE 144 145 145 PHE PHE A . n 
A 1 145 GLU 145 146 146 GLU GLU A . n 
A 1 146 ALA 146 147 147 ALA ALA A . n 
A 1 147 SER 147 148 148 SER SER A . n 
A 1 148 GLN 148 149 149 GLN GLN A . n 
A 1 149 PHE 149 150 150 PHE PHE A . n 
A 1 150 MET 150 151 151 MET MET A . n 
A 1 151 PHE 151 152 152 PHE PHE A . n 
A 1 152 PHE 152 153 153 PHE PHE A . n 
A 1 153 ASN 153 154 154 ASN ASN A . n 
A 1 154 HIS 154 155 155 HIS HIS A . n 
A 1 155 VAL 155 156 156 VAL VAL A . n 
A 1 156 PRO 156 157 157 PRO PRO A . n 
A 1 157 ASP 157 158 158 ASP ASP A . n 
A 1 158 PRO 158 159 159 PRO PRO A . n 
A 1 159 THR 159 160 160 THR THR A . n 
A 1 160 THR 160 161 161 THR THR A . n 
A 1 161 HIS 161 162 162 HIS HIS A . n 
A 1 162 LEU 162 163 163 LEU LEU A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 LEU 164 165 165 LEU LEU A . n 
A 1 165 TRP 165 166 166 TRP TRP A . n 
A 1 166 GLN 166 167 167 GLN GLN A . n 
A 1 167 ILE 167 168 168 ILE ILE A . n 
A 1 168 ALA 168 169 169 ALA ALA A . n 
A 1 169 ILE 169 170 170 ILE ILE A . n 
A 1 170 ALA 170 171 171 ALA ALA A . n 
A 1 171 GLY 171 172 172 GLY GLY A . n 
A 1 172 GLU 172 173 173 GLU GLU A . n 
A 1 173 HIS 173 174 174 HIS HIS A . n 
A 1 174 THR 174 175 175 THR THR A . n 
A 1 175 LEU 175 176 176 LEU LEU A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 GLN 177 178 178 GLN GLN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 HIS 179 180 180 HIS HIS A . n 
A 1 180 THR 180 181 181 THR THR A . n 
A 1 181 SER 181 182 182 SER SER A . n 
A 1 182 SER 182 183 183 SER SER A . n 
A 1 183 ASP 183 184 184 ASP ASP A . n 
A 1 184 ARG 184 185 185 ARG ARG A . n 
A 1 185 LEU 185 186 186 LEU LEU A . n 
A 1 186 GLN 186 187 187 GLN GLN A . n 
A 1 187 ILE 187 188 188 ILE ILE A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 VAL 189 190 190 VAL VAL A . n 
A 1 190 GLU 190 191 191 GLU GLU A . n 
A 1 191 GLN 191 192 192 GLN GLN A . n 
A 1 192 LEU 192 193 193 LEU LEU A . n 
A 1 193 ASN 193 194 194 ASN ASN A . n 
A 1 194 GLN 194 195 195 GLN GLN A . n 
A 1 195 TRP 195 196 196 TRP TRP A . n 
A 1 196 TYR 196 197 197 TYR TYR A . n 
A 1 197 PRO 197 198 198 PRO PRO A . n 
A 1 198 LEU 198 199 199 LEU LEU A . n 
A 1 199 ASP 199 200 200 ASP ASP A . n 
A 1 200 HIS 200 201 201 HIS HIS A . n 
A 1 201 GLU 201 202 202 GLU GLU A . n 
A 1 202 VAL 202 203 203 VAL VAL A . n 
A 1 203 VAL 203 204 204 VAL VAL A . n 
A 1 204 ILE 204 205 205 ILE ILE A . n 
A 1 205 TYR 205 206 206 TYR TYR A . n 
A 1 206 GLU 206 207 207 GLU GLU A . n 
A 1 207 ALA 207 208 208 ALA ALA A . n 
A 1 208 ALA 208 209 209 ALA ALA A . n 
A 1 209 ASN 209 210 210 ASN ASN A . n 
A 1 210 LEU 210 211 211 LEU LEU A . n 
A 1 211 PRO 211 212 212 PRO PRO A . n 
A 1 212 ILE 212 213 213 ILE ILE A . n 
A 1 213 GLN 213 214 214 GLN GLN A . n 
A 1 214 ALA 214 215 215 ALA ALA A . n 
A 1 215 PRO 215 216 216 PRO PRO A . n 
A 1 216 ARG 216 217 217 ARG ARG A . n 
A 1 217 ILE 217 218 218 ILE ILE A . n 
A 1 218 GLU 218 219 219 GLU GLU A . n 
A 1 219 ARG 219 220 220 ARG ARG A . n 
A 1 220 LEU 220 221 221 LEU LEU A . n 
A 1 221 PRO 221 222 222 PRO PRO A . n 
A 1 222 LEU 222 223 223 LEU LEU A . n 
A 1 223 ALA 223 224 224 ALA ALA A . n 
A 1 224 ASN 224 225 225 ASN ASN A . n 
A 1 225 LEU 225 226 226 LEU LEU A . n 
A 1 226 PRO 226 227 227 PRO PRO A . n 
A 1 227 GLN 227 228 228 GLN GLN A . n 
A 1 228 ALA 228 229 229 ALA ALA A . n 
A 1 229 HIS 229 230 230 HIS HIS A . n 
A 1 230 LEU 230 231 231 LEU LEU A . n 
A 1 231 MET 231 232 232 MET MET A . n 
A 1 232 PRO 232 233 233 PRO PRO A . n 
A 1 233 ILE 233 234 234 ILE ILE A . n 
A 1 234 SER 234 235 235 SER SER A . n 
A 1 235 THR 235 236 236 THR THR A . n 
A 1 236 LEU 236 237 237 LEU LEU A . n 
A 1 237 LEU 237 238 238 LEU LEU A . n 
A 1 238 ILE 238 239 239 ILE ILE A . n 
A 1 239 PRO 239 240 240 PRO PRO A . n 
A 1 240 PRO 240 241 241 PRO PRO A . n 
A 1 241 ALA 241 242 242 ALA ALA A . n 
A 1 242 LYS 242 243 243 LYS LYS A . n 
A 1 243 LYS 243 244 244 LYS LYS A . n 
A 1 244 LEU 244 245 245 LEU LEU A . n 
A 1 245 GLU 245 246 246 GLU GLU A . n 
A 1 246 TYR 246 247 247 TYR TYR A . n 
A 1 247 ASN 247 248 248 ASN ASN A . n 
A 1 248 TYR 248 249 249 TYR TYR A . n 
A 1 249 ALA 249 250 250 ALA ALA A . n 
A 1 250 ILE 250 251 251 ILE ILE A . n 
A 1 251 LEU 251 252 252 LEU LEU A . n 
A 1 252 ALA 252 253 253 ALA ALA A . n 
A 1 253 LYS 253 254 254 LYS LYS A . n 
A 1 254 LEU 254 255 255 LEU LEU A . n 
A 1 255 GLY 255 256 256 GLY GLY A . n 
A 1 256 ILE 256 257 257 ILE ILE A . n 
A 1 257 GLY 257 258 258 GLY GLY A . n 
A 1 258 PRO 258 259 259 PRO PRO A . n 
A 1 259 GLU 259 260 260 GLU GLU A . n 
A 1 260 ASP 260 261 261 ASP ASP A . n 
A 1 261 LEU 261 262 262 LEU LEU A . n 
A 1 262 GLY 262 263 263 GLY GLY A . n 
B 2 1   GLY 1   3   3   GLY GLY B . n 
B 2 2   LEU 2   4   4   LEU LEU B . n 
B 2 3   SER 3   5   5   SER SER B . n 
B 2 4   ASP 4   6   6   ASP ASP B . n 
B 2 5   PHE 5   7   7   PHE PHE B . n 
B 2 6   PHE 6   8   8   PHE PHE B . n 
B 2 7   THR 7   9   9   THR THR B . n 
B 2 8   GLN 8   10  10  GLN GLN B . n 
B 2 9   LEU 9   11  11  LEU LEU B . n 
B 2 10  GLY 10  12  12  GLY GLY B . n 
B 2 11  GLN 11  13  13  GLN GLN B . n 
B 2 12  ASP 12  14  14  ASP ASP B . n 
B 2 13  ALA 13  15  15  ALA ALA B . n 
B 2 14  GLN 14  16  16  GLN GLN B . n 
B 2 15  LEU 15  17  17  LEU LEU B . n 
B 2 16  MET 16  18  18  MET MET B . n 
B 2 17  GLU 17  19  19  GLU GLU B . n 
B 2 18  ASP 18  20  20  ASP ASP B . n 
B 2 19  TYR 19  21  21  TYR TYR B . n 
B 2 20  LYS 20  22  22  LYS LYS B . n 
B 2 21  GLN 21  23  23  GLN GLN B . n 
B 2 22  ASN 22  24  24  ASN ASN B . n 
B 2 23  PRO 23  25  25  PRO PRO B . n 
B 2 24  GLU 24  26  26  GLU GLU B . n 
B 2 25  ALA 25  27  27  ALA ALA B . n 
B 2 26  VAL 26  28  28  VAL VAL B . n 
B 2 27  MET 27  29  29  MET MET B . n 
B 2 28  ARG 28  30  30  ARG ARG B . n 
B 2 29  ALA 29  31  31  ALA ALA B . n 
B 2 30  HIS 30  32  32  HIS HIS B . n 
B 2 31  GLY 31  33  33  GLY GLY B . n 
B 2 32  LEU 32  34  34  LEU LEU B . n 
B 2 33  THR 33  35  35  THR THR B . n 
B 2 34  ASP 34  36  36  ASP ASP B . n 
B 2 35  GLU 35  37  37  GLU GLU B . n 
B 2 36  GLN 36  38  38  GLN GLN B . n 
B 2 37  ILE 37  39  39  ILE ILE B . n 
B 2 38  ASN 38  40  40  ASN ASN B . n 
B 2 39  ALA 39  41  41  ALA ALA B . n 
B 2 40  VAL 40  42  42  VAL VAL B . n 
B 2 41  MET 41  43  43  MET MET B . n 
B 2 42  THR 42  44  44  THR THR B . n 
B 2 43  GLY 43  45  45  GLY GLY B . n 
B 2 44  ASP 44  46  46  ASP ASP B . n 
B 2 45  MET 45  47  47  MET MET B . n 
B 2 46  GLU 46  48  48  GLU GLU B . n 
B 2 47  LYS 47  49  49  LYS LYS B . n 
B 2 48  LEU 48  50  50  LEU LEU B . n 
B 2 49  LYS 49  51  51  LYS LYS B . n 
B 2 50  THR 50  52  52  THR THR B . n 
B 2 51  LEU 51  53  53  LEU LEU B . n 
B 2 52  SER 52  54  54  SER SER B . n 
B 2 53  GLY 53  55  55  GLY GLY B . n 
B 2 54  ASP 54  56  56  ASP ASP B . n 
B 2 55  SER 55  57  ?   ?   ?   B . n 
B 2 56  SER 56  58  ?   ?   ?   B . n 
B 2 57  TYR 57  59  ?   ?   ?   B . n 
B 2 58  GLN 58  60  ?   ?   ?   B . n 
B 2 59  SER 59  61  ?   ?   ?   B . n 
B 2 60  ALA 60  62  62  ALA ALA B . n 
B 2 61  LEU 61  63  63  LEU LEU B . n 
B 2 62  VAL 62  64  64  VAL VAL B . n 
B 2 63  IML 63  65  65  IML IML B . n 
B 2 64  SER 64  66  66  SER SER B . n 
B 2 65  HIS 65  67  67  HIS HIS B . n 
B 2 66  GLY 66  68  68  GLY GLY B . n 
B 2 67  ASN 67  69  69  ASN ASN B . n 
B 2 68  GLY 68  70  70  GLY GLY B . n 
C 1 1   GLY 1   2   2   GLY GLY C . n 
C 1 2   SER 2   3   3   SER SER C . n 
C 1 3   LEU 3   4   4   LEU LEU C . n 
C 1 4   VAL 4   5   5   VAL VAL C . n 
C 1 5   CYS 5   6   6   CYS CYS C . n 
C 1 6   VAL 6   7   7   VAL VAL C . n 
C 1 7   GLY 7   8   8   GLY GLY C . n 
C 1 8   THR 8   9   9   THR THR C . n 
C 1 9   GLY 9   10  10  GLY GLY C . n 
C 1 10  LEU 10  11  11  LEU LEU C . n 
C 1 11  GLN 11  12  12  GLN GLN C . n 
C 1 12  LEU 12  13  13  LEU LEU C . n 
C 1 13  ALA 13  14  14  ALA ALA C . n 
C 1 14  GLY 14  15  15  GLY GLY C . n 
C 1 15  GLN 15  16  16  GLN GLN C . n 
C 1 16  ILE 16  17  17  ILE ILE C . n 
C 1 17  SER 17  18  18  SER SER C . n 
C 1 18  VAL 18  19  19  VAL VAL C . n 
C 1 19  LEU 19  20  20  LEU LEU C . n 
C 1 20  SER 20  21  21  SER SER C . n 
C 1 21  ARG 21  22  22  ARG ARG C . n 
C 1 22  SER 22  23  23  SER SER C . n 
C 1 23  TYR 23  24  24  TYR TYR C . n 
C 1 24  ILE 24  25  25  ILE ILE C . n 
C 1 25  GLU 25  26  26  GLU GLU C . n 
C 1 26  HIS 26  27  27  HIS HIS C . n 
C 1 27  ALA 27  28  28  ALA ALA C . n 
C 1 28  ASP 28  29  29  ASP ASP C . n 
C 1 29  ILE 29  30  30  ILE ILE C . n 
C 1 30  VAL 30  31  31  VAL VAL C . n 
C 1 31  PHE 31  32  32  PHE PHE C . n 
C 1 32  SER 32  33  33  SER SER C . n 
C 1 33  LEU 33  34  34  LEU LEU C . n 
C 1 34  LEU 34  35  35  LEU LEU C . n 
C 1 35  PRO 35  36  36  PRO PRO C . n 
C 1 36  ASP 36  37  37  ASP ASP C . n 
C 1 37  GLY 37  38  38  GLY GLY C . n 
C 1 38  PHE 38  39  39  PHE PHE C . n 
C 1 39  SER 39  40  40  SER SER C . n 
C 1 40  GLN 40  41  41  GLN GLN C . n 
C 1 41  ARG 41  42  42  ARG ARG C . n 
C 1 42  TRP 42  43  43  TRP TRP C . n 
C 1 43  LEU 43  44  44  LEU LEU C . n 
C 1 44  THR 44  45  45  THR THR C . n 
C 1 45  LYS 45  46  46  LYS LYS C . n 
C 1 46  LEU 46  47  47  LEU LEU C . n 
C 1 47  ASN 47  48  48  ASN ASN C . n 
C 1 48  PRO 48  49  49  PRO PRO C . n 
C 1 49  ASN 49  50  50  ASN ASN C . n 
C 1 50  VAL 50  51  51  VAL VAL C . n 
C 1 51  ILE 51  52  52  ILE ILE C . n 
C 1 52  ASN 52  53  53  ASN ASN C . n 
C 1 53  LEU 53  54  54  LEU LEU C . n 
C 1 54  GLN 54  55  55  GLN GLN C . n 
C 1 55  GLN 55  56  56  GLN GLN C . n 
C 1 56  PHE 56  57  57  PHE PHE C . n 
C 1 57  TYR 57  58  58  TYR TYR C . n 
C 1 58  ALA 58  59  59  ALA ALA C . n 
C 1 59  GLN 59  60  60  GLN GLN C . n 
C 1 60  ASN 60  61  61  ASN ASN C . n 
C 1 61  GLY 61  62  62  GLY GLY C . n 
C 1 62  GLU 62  63  63  GLU GLU C . n 
C 1 63  VAL 63  64  64  VAL VAL C . n 
C 1 64  LYS 64  65  65  LYS LYS C . n 
C 1 65  ASN 65  66  66  ASN ASN C . n 
C 1 66  ARG 66  67  67  ARG ARG C . n 
C 1 67  ARG 67  68  68  ARG ARG C . n 
C 1 68  ASP 68  69  69  ASP ASP C . n 
C 1 69  THR 69  70  70  THR THR C . n 
C 1 70  TYR 70  71  71  TYR TYR C . n 
C 1 71  GLU 71  72  72  GLU GLU C . n 
C 1 72  GLN 72  73  73  GLN GLN C . n 
C 1 73  MET 73  74  74  MET MET C . n 
C 1 74  VAL 74  75  75  VAL VAL C . n 
C 1 75  ASN 75  76  76  ASN ASN C . n 
C 1 76  ALA 76  77  77  ALA ALA C . n 
C 1 77  ILE 77  78  78  ILE ILE C . n 
C 1 78  LEU 78  79  79  LEU LEU C . n 
C 1 79  ASP 79  80  80  ASP ASP C . n 
C 1 80  ALA 80  81  81  ALA ALA C . n 
C 1 81  VAL 81  82  82  VAL VAL C . n 
C 1 82  ARG 82  83  83  ARG ARG C . n 
C 1 83  ALA 83  84  84  ALA ALA C . n 
C 1 84  GLY 84  85  85  GLY GLY C . n 
C 1 85  LYS 85  86  86  LYS LYS C . n 
C 1 86  LYS 86  87  87  LYS LYS C . n 
C 1 87  THR 87  88  88  THR THR C . n 
C 1 88  VAL 88  89  89  VAL VAL C . n 
C 1 89  CYS 89  90  90  CYS CYS C . n 
C 1 90  ALA 90  91  91  ALA ALA C . n 
C 1 91  LEU 91  92  92  LEU LEU C . n 
C 1 92  TYR 92  93  93  TYR TYR C . n 
C 1 93  GLY 93  94  94  GLY GLY C . n 
C 1 94  HIS 94  95  95  HIS HIS C . n 
C 1 95  PRO 95  96  96  PRO PRO C . n 
C 1 96  GLY 96  97  97  GLY GLY C . n 
C 1 97  VAL 97  98  98  VAL VAL C . n 
C 1 98  PHE 98  99  99  PHE PHE C . n 
C 1 99  ALA 99  100 100 ALA ALA C . n 
C 1 100 CYS 100 101 101 CYS CYS C . n 
C 1 101 VAL 101 102 102 VAL VAL C . n 
C 1 102 SER 102 103 103 SER SER C . n 
C 1 103 HIS 103 104 104 HIS HIS C . n 
C 1 104 MET 104 105 105 MET MET C . n 
C 1 105 ALA 105 106 106 ALA ALA C . n 
C 1 106 ILE 106 107 107 ILE ILE C . n 
C 1 107 THR 107 108 108 THR THR C . n 
C 1 108 ARG 108 109 109 ARG ARG C . n 
C 1 109 ALA 109 110 110 ALA ALA C . n 
C 1 110 LYS 110 111 111 LYS LYS C . n 
C 1 111 ALA 111 112 112 ALA ALA C . n 
C 1 112 GLU 112 113 113 GLU GLU C . n 
C 1 113 GLY 113 114 114 GLY GLY C . n 
C 1 114 PHE 114 115 115 PHE PHE C . n 
C 1 115 SER 115 116 116 SER SER C . n 
C 1 116 ALA 116 117 117 ALA ALA C . n 
C 1 117 LYS 117 118 118 LYS LYS C . n 
C 1 118 MET 118 119 119 MET MET C . n 
C 1 119 GLU 119 120 120 GLU GLU C . n 
C 1 120 PRO 120 121 121 PRO PRO C . n 
C 1 121 GLY 121 122 122 GLY GLY C . n 
C 1 122 ILE 122 123 123 ILE ILE C . n 
C 1 123 SER 123 124 124 SER SER C . n 
C 1 124 ALA 124 125 125 ALA ALA C . n 
C 1 125 GLU 125 126 126 GLU GLU C . n 
C 1 126 ALA 126 127 127 ALA ALA C . n 
C 1 127 CYS 127 128 128 CYS CYS C . n 
C 1 128 LEU 128 129 129 LEU LEU C . n 
C 1 129 TRP 129 130 130 TRP TRP C . n 
C 1 130 ALA 130 131 131 ALA ALA C . n 
C 1 131 ASP 131 132 132 ASP ASP C . n 
C 1 132 LEU 132 133 133 LEU LEU C . n 
C 1 133 GLY 133 134 134 GLY GLY C . n 
C 1 134 ILE 134 135 135 ILE ILE C . n 
C 1 135 ASP 135 136 136 ASP ASP C . n 
C 1 136 PRO 136 137 137 PRO PRO C . n 
C 1 137 GLY 137 138 138 GLY GLY C . n 
C 1 138 ASN 138 139 139 ASN ASN C . n 
C 1 139 SER 139 140 140 SER SER C . n 
C 1 140 GLY 140 141 141 GLY GLY C . n 
C 1 141 HIS 141 142 142 HIS HIS C . n 
C 1 142 GLN 142 143 143 GLN GLN C . n 
C 1 143 SER 143 144 144 SER SER C . n 
C 1 144 PHE 144 145 145 PHE PHE C . n 
C 1 145 GLU 145 146 146 GLU GLU C . n 
C 1 146 ALA 146 147 147 ALA ALA C . n 
C 1 147 SER 147 148 148 SER SER C . n 
C 1 148 GLN 148 149 149 GLN GLN C . n 
C 1 149 PHE 149 150 150 PHE PHE C . n 
C 1 150 MET 150 151 151 MET MET C . n 
C 1 151 PHE 151 152 152 PHE PHE C . n 
C 1 152 PHE 152 153 153 PHE PHE C . n 
C 1 153 ASN 153 154 154 ASN ASN C . n 
C 1 154 HIS 154 155 155 HIS HIS C . n 
C 1 155 VAL 155 156 156 VAL VAL C . n 
C 1 156 PRO 156 157 157 PRO PRO C . n 
C 1 157 ASP 157 158 158 ASP ASP C . n 
C 1 158 PRO 158 159 159 PRO PRO C . n 
C 1 159 THR 159 160 160 THR THR C . n 
C 1 160 THR 160 161 161 THR THR C . n 
C 1 161 HIS 161 162 162 HIS HIS C . n 
C 1 162 LEU 162 163 163 LEU LEU C . n 
C 1 163 LEU 163 164 164 LEU LEU C . n 
C 1 164 LEU 164 165 165 LEU LEU C . n 
C 1 165 TRP 165 166 166 TRP TRP C . n 
C 1 166 GLN 166 167 167 GLN GLN C . n 
C 1 167 ILE 167 168 168 ILE ILE C . n 
C 1 168 ALA 168 169 169 ALA ALA C . n 
C 1 169 ILE 169 170 170 ILE ILE C . n 
C 1 170 ALA 170 171 171 ALA ALA C . n 
C 1 171 GLY 171 172 172 GLY GLY C . n 
C 1 172 GLU 172 173 173 GLU GLU C . n 
C 1 173 HIS 173 174 174 HIS HIS C . n 
C 1 174 THR 174 175 175 THR THR C . n 
C 1 175 LEU 175 176 176 LEU LEU C . n 
C 1 176 THR 176 177 177 THR THR C . n 
C 1 177 GLN 177 178 178 GLN GLN C . n 
C 1 178 PHE 178 179 179 PHE PHE C . n 
C 1 179 HIS 179 180 180 HIS HIS C . n 
C 1 180 THR 180 181 181 THR THR C . n 
C 1 181 SER 181 182 182 SER SER C . n 
C 1 182 SER 182 183 183 SER SER C . n 
C 1 183 ASP 183 184 184 ASP ASP C . n 
C 1 184 ARG 184 185 185 ARG ARG C . n 
C 1 185 LEU 185 186 186 LEU LEU C . n 
C 1 186 GLN 186 187 187 GLN GLN C . n 
C 1 187 ILE 187 188 188 ILE ILE C . n 
C 1 188 LEU 188 189 189 LEU LEU C . n 
C 1 189 VAL 189 190 190 VAL VAL C . n 
C 1 190 GLU 190 191 191 GLU GLU C . n 
C 1 191 GLN 191 192 192 GLN GLN C . n 
C 1 192 LEU 192 193 193 LEU LEU C . n 
C 1 193 ASN 193 194 194 ASN ASN C . n 
C 1 194 GLN 194 195 195 GLN GLN C . n 
C 1 195 TRP 195 196 196 TRP TRP C . n 
C 1 196 TYR 196 197 197 TYR TYR C . n 
C 1 197 PRO 197 198 198 PRO PRO C . n 
C 1 198 LEU 198 199 199 LEU LEU C . n 
C 1 199 ASP 199 200 200 ASP ASP C . n 
C 1 200 HIS 200 201 201 HIS HIS C . n 
C 1 201 GLU 201 202 202 GLU GLU C . n 
C 1 202 VAL 202 203 203 VAL VAL C . n 
C 1 203 VAL 203 204 204 VAL VAL C . n 
C 1 204 ILE 204 205 205 ILE ILE C . n 
C 1 205 TYR 205 206 206 TYR TYR C . n 
C 1 206 GLU 206 207 207 GLU GLU C . n 
C 1 207 ALA 207 208 208 ALA ALA C . n 
C 1 208 ALA 208 209 209 ALA ALA C . n 
C 1 209 ASN 209 210 210 ASN ASN C . n 
C 1 210 LEU 210 211 211 LEU LEU C . n 
C 1 211 PRO 211 212 212 PRO PRO C . n 
C 1 212 ILE 212 213 213 ILE ILE C . n 
C 1 213 GLN 213 214 214 GLN GLN C . n 
C 1 214 ALA 214 215 215 ALA ALA C . n 
C 1 215 PRO 215 216 216 PRO PRO C . n 
C 1 216 ARG 216 217 217 ARG ARG C . n 
C 1 217 ILE 217 218 218 ILE ILE C . n 
C 1 218 GLU 218 219 219 GLU GLU C . n 
C 1 219 ARG 219 220 220 ARG ARG C . n 
C 1 220 LEU 220 221 221 LEU LEU C . n 
C 1 221 PRO 221 222 222 PRO PRO C . n 
C 1 222 LEU 222 223 223 LEU LEU C . n 
C 1 223 ALA 223 224 224 ALA ALA C . n 
C 1 224 ASN 224 225 225 ASN ASN C . n 
C 1 225 LEU 225 226 226 LEU LEU C . n 
C 1 226 PRO 226 227 227 PRO PRO C . n 
C 1 227 GLN 227 228 228 GLN GLN C . n 
C 1 228 ALA 228 229 229 ALA ALA C . n 
C 1 229 HIS 229 230 230 HIS HIS C . n 
C 1 230 LEU 230 231 231 LEU LEU C . n 
C 1 231 MET 231 232 232 MET MET C . n 
C 1 232 PRO 232 233 233 PRO PRO C . n 
C 1 233 ILE 233 234 234 ILE ILE C . n 
C 1 234 SER 234 235 235 SER SER C . n 
C 1 235 THR 235 236 236 THR THR C . n 
C 1 236 LEU 236 237 237 LEU LEU C . n 
C 1 237 LEU 237 238 238 LEU LEU C . n 
C 1 238 ILE 238 239 239 ILE ILE C . n 
C 1 239 PRO 239 240 240 PRO PRO C . n 
C 1 240 PRO 240 241 241 PRO PRO C . n 
C 1 241 ALA 241 242 242 ALA ALA C . n 
C 1 242 LYS 242 243 243 LYS LYS C . n 
C 1 243 LYS 243 244 244 LYS LYS C . n 
C 1 244 LEU 244 245 245 LEU LEU C . n 
C 1 245 GLU 245 246 246 GLU GLU C . n 
C 1 246 TYR 246 247 247 TYR TYR C . n 
C 1 247 ASN 247 248 248 ASN ASN C . n 
C 1 248 TYR 248 249 249 TYR TYR C . n 
C 1 249 ALA 249 250 250 ALA ALA C . n 
C 1 250 ILE 250 251 251 ILE ILE C . n 
C 1 251 LEU 251 252 252 LEU LEU C . n 
C 1 252 ALA 252 253 253 ALA ALA C . n 
C 1 253 LYS 253 254 254 LYS LYS C . n 
C 1 254 LEU 254 255 255 LEU LEU C . n 
C 1 255 GLY 255 256 256 GLY GLY C . n 
C 1 256 ILE 256 257 257 ILE ILE C . n 
C 1 257 GLY 257 258 258 GLY GLY C . n 
C 1 258 PRO 258 259 259 PRO PRO C . n 
C 1 259 GLU 259 260 260 GLU GLU C . n 
C 1 260 ASP 260 261 261 ASP ASP C . n 
C 1 261 LEU 261 262 262 LEU LEU C . n 
C 1 262 GLY 262 263 263 GLY GLY C . n 
D 3 1   GLY 1   3   ?   ?   ?   D . n 
D 3 2   LEU 2   4   4   LEU LEU D . n 
D 3 3   SER 3   5   5   SER SER D . n 
D 3 4   ASP 4   6   6   ASP ASP D . n 
D 3 5   PHE 5   7   7   PHE PHE D . n 
D 3 6   PHE 6   8   8   PHE PHE D . n 
D 3 7   THR 7   9   9   THR THR D . n 
D 3 8   GLN 8   10  10  GLN GLN D . n 
D 3 9   LEU 9   11  11  LEU LEU D . n 
D 3 10  GLY 10  12  12  GLY GLY D . n 
D 3 11  GLN 11  13  13  GLN GLN D . n 
D 3 12  ASP 12  14  14  ASP ASP D . n 
D 3 13  ALA 13  15  15  ALA ALA D . n 
D 3 14  GLN 14  16  16  GLN GLN D . n 
D 3 15  LEU 15  17  17  LEU LEU D . n 
D 3 16  MET 16  18  18  MET MET D . n 
D 3 17  GLU 17  19  19  GLU GLU D . n 
D 3 18  ASP 18  20  20  ASP ASP D . n 
D 3 19  TYR 19  21  21  TYR TYR D . n 
D 3 20  LYS 20  22  22  LYS LYS D . n 
D 3 21  GLN 21  23  23  GLN GLN D . n 
D 3 22  ASN 22  24  24  ASN ASN D . n 
D 3 23  PRO 23  25  25  PRO PRO D . n 
D 3 24  GLU 24  26  26  GLU GLU D . n 
D 3 25  ALA 25  27  27  ALA ALA D . n 
D 3 26  VAL 26  28  28  VAL VAL D . n 
D 3 27  MET 27  29  29  MET MET D . n 
D 3 28  ARG 28  30  30  ARG ARG D . n 
D 3 29  ALA 29  31  31  ALA ALA D . n 
D 3 30  HIS 30  32  32  HIS HIS D . n 
D 3 31  GLY 31  33  33  GLY GLY D . n 
D 3 32  LEU 32  34  34  LEU LEU D . n 
D 3 33  THR 33  35  35  THR THR D . n 
D 3 34  ASP 34  36  36  ASP ASP D . n 
D 3 35  GLU 35  37  37  GLU GLU D . n 
D 3 36  GLN 36  38  38  GLN GLN D . n 
D 3 37  ILE 37  39  39  ILE ILE D . n 
D 3 38  ASN 38  40  40  ASN ASN D . n 
D 3 39  ALA 39  41  41  ALA ALA D . n 
D 3 40  VAL 40  42  42  VAL VAL D . n 
D 3 41  MET 41  43  43  MET MET D . n 
D 3 42  THR 42  44  44  THR THR D . n 
D 3 43  GLY 43  45  45  GLY GLY D . n 
D 3 44  ASP 44  46  46  ASP ASP D . n 
D 3 45  MET 45  47  47  MET MET D . n 
D 3 46  GLU 46  48  48  GLU GLU D . n 
D 3 47  LYS 47  49  49  LYS LYS D . n 
D 3 48  LEU 48  50  50  LEU LEU D . n 
D 3 49  LYS 49  51  51  LYS LYS D . n 
D 3 50  THR 50  52  52  THR THR D . n 
D 3 51  LEU 51  53  53  LEU LEU D . n 
D 3 52  SER 52  54  54  SER SER D . n 
D 3 53  GLY 53  55  55  GLY GLY D . n 
D 3 54  ASP 54  56  56  ASP ASP D . n 
D 3 55  SER 55  57  57  SER SER D . n 
D 3 56  SER 56  58  ?   ?   ?   D . n 
D 3 57  TYR 57  59  ?   ?   ?   D . n 
D 3 58  GLN 58  60  ?   ?   ?   D . n 
D 3 59  SER 59  61  ?   ?   ?   D . n 
D 3 60  ALA 60  62  62  ALA ALA D . n 
D 3 61  LEU 61  63  63  LEU LEU D . n 
D 3 62  VAL 62  64  64  VAL VAL D . n 
D 3 63  ILE 63  65  65  ILE ILE D . n 
D 3 64  SER 64  66  66  SER SER D . n 
D 3 65  HIS 65  67  67  HIS HIS D . n 
D 3 66  GLY 66  68  68  GLY GLY D . n 
D 3 67  ASN 67  69  69  ASN ASN D . n 
D 3 68  GLY 68  70  70  GLY GLY D . n 
E 1 1   GLY 1   2   2   GLY GLY E . n 
E 1 2   SER 2   3   3   SER SER E . n 
E 1 3   LEU 3   4   4   LEU LEU E . n 
E 1 4   VAL 4   5   5   VAL VAL E . n 
E 1 5   CYS 5   6   6   CYS CYS E . n 
E 1 6   VAL 6   7   7   VAL VAL E . n 
E 1 7   GLY 7   8   8   GLY GLY E . n 
E 1 8   THR 8   9   9   THR THR E . n 
E 1 9   GLY 9   10  10  GLY GLY E . n 
E 1 10  LEU 10  11  11  LEU LEU E . n 
E 1 11  GLN 11  12  12  GLN GLN E . n 
E 1 12  LEU 12  13  13  LEU LEU E . n 
E 1 13  ALA 13  14  14  ALA ALA E . n 
E 1 14  GLY 14  15  15  GLY GLY E . n 
E 1 15  GLN 15  16  16  GLN GLN E . n 
E 1 16  ILE 16  17  17  ILE ILE E . n 
E 1 17  SER 17  18  18  SER SER E . n 
E 1 18  VAL 18  19  19  VAL VAL E . n 
E 1 19  LEU 19  20  20  LEU LEU E . n 
E 1 20  SER 20  21  21  SER SER E . n 
E 1 21  ARG 21  22  22  ARG ARG E . n 
E 1 22  SER 22  23  23  SER SER E . n 
E 1 23  TYR 23  24  24  TYR TYR E . n 
E 1 24  ILE 24  25  25  ILE ILE E . n 
E 1 25  GLU 25  26  26  GLU GLU E . n 
E 1 26  HIS 26  27  27  HIS HIS E . n 
E 1 27  ALA 27  28  28  ALA ALA E . n 
E 1 28  ASP 28  29  29  ASP ASP E . n 
E 1 29  ILE 29  30  30  ILE ILE E . n 
E 1 30  VAL 30  31  31  VAL VAL E . n 
E 1 31  PHE 31  32  32  PHE PHE E . n 
E 1 32  SER 32  33  33  SER SER E . n 
E 1 33  LEU 33  34  34  LEU LEU E . n 
E 1 34  LEU 34  35  35  LEU LEU E . n 
E 1 35  PRO 35  36  36  PRO PRO E . n 
E 1 36  ASP 36  37  37  ASP ASP E . n 
E 1 37  GLY 37  38  38  GLY GLY E . n 
E 1 38  PHE 38  39  39  PHE PHE E . n 
E 1 39  SER 39  40  40  SER SER E . n 
E 1 40  GLN 40  41  41  GLN GLN E . n 
E 1 41  ARG 41  42  42  ARG ARG E . n 
E 1 42  TRP 42  43  43  TRP TRP E . n 
E 1 43  LEU 43  44  44  LEU LEU E . n 
E 1 44  THR 44  45  45  THR THR E . n 
E 1 45  LYS 45  46  46  LYS LYS E . n 
E 1 46  LEU 46  47  47  LEU LEU E . n 
E 1 47  ASN 47  48  48  ASN ASN E . n 
E 1 48  PRO 48  49  49  PRO PRO E . n 
E 1 49  ASN 49  50  50  ASN ASN E . n 
E 1 50  VAL 50  51  51  VAL VAL E . n 
E 1 51  ILE 51  52  52  ILE ILE E . n 
E 1 52  ASN 52  53  53  ASN ASN E . n 
E 1 53  LEU 53  54  54  LEU LEU E . n 
E 1 54  GLN 54  55  55  GLN GLN E . n 
E 1 55  GLN 55  56  56  GLN GLN E . n 
E 1 56  PHE 56  57  57  PHE PHE E . n 
E 1 57  TYR 57  58  58  TYR TYR E . n 
E 1 58  ALA 58  59  59  ALA ALA E . n 
E 1 59  GLN 59  60  60  GLN GLN E . n 
E 1 60  ASN 60  61  61  ASN ASN E . n 
E 1 61  GLY 61  62  62  GLY GLY E . n 
E 1 62  GLU 62  63  63  GLU GLU E . n 
E 1 63  VAL 63  64  64  VAL VAL E . n 
E 1 64  LYS 64  65  65  LYS LYS E . n 
E 1 65  ASN 65  66  66  ASN ASN E . n 
E 1 66  ARG 66  67  67  ARG ARG E . n 
E 1 67  ARG 67  68  68  ARG ARG E . n 
E 1 68  ASP 68  69  69  ASP ASP E . n 
E 1 69  THR 69  70  70  THR THR E . n 
E 1 70  TYR 70  71  71  TYR TYR E . n 
E 1 71  GLU 71  72  72  GLU GLU E . n 
E 1 72  GLN 72  73  73  GLN GLN E . n 
E 1 73  MET 73  74  74  MET MET E . n 
E 1 74  VAL 74  75  75  VAL VAL E . n 
E 1 75  ASN 75  76  76  ASN ASN E . n 
E 1 76  ALA 76  77  77  ALA ALA E . n 
E 1 77  ILE 77  78  78  ILE ILE E . n 
E 1 78  LEU 78  79  79  LEU LEU E . n 
E 1 79  ASP 79  80  80  ASP ASP E . n 
E 1 80  ALA 80  81  81  ALA ALA E . n 
E 1 81  VAL 81  82  82  VAL VAL E . n 
E 1 82  ARG 82  83  83  ARG ARG E . n 
E 1 83  ALA 83  84  84  ALA ALA E . n 
E 1 84  GLY 84  85  85  GLY GLY E . n 
E 1 85  LYS 85  86  86  LYS LYS E . n 
E 1 86  LYS 86  87  87  LYS LYS E . n 
E 1 87  THR 87  88  88  THR THR E . n 
E 1 88  VAL 88  89  89  VAL VAL E . n 
E 1 89  CYS 89  90  90  CYS CYS E . n 
E 1 90  ALA 90  91  91  ALA ALA E . n 
E 1 91  LEU 91  92  92  LEU LEU E . n 
E 1 92  TYR 92  93  93  TYR TYR E . n 
E 1 93  GLY 93  94  94  GLY GLY E . n 
E 1 94  HIS 94  95  95  HIS HIS E . n 
E 1 95  PRO 95  96  96  PRO PRO E . n 
E 1 96  GLY 96  97  97  GLY GLY E . n 
E 1 97  VAL 97  98  98  VAL VAL E . n 
E 1 98  PHE 98  99  99  PHE PHE E . n 
E 1 99  ALA 99  100 100 ALA ALA E . n 
E 1 100 CYS 100 101 101 CYS CYS E . n 
E 1 101 VAL 101 102 102 VAL VAL E . n 
E 1 102 SER 102 103 103 SER SER E . n 
E 1 103 HIS 103 104 104 HIS HIS E . n 
E 1 104 MET 104 105 105 MET MET E . n 
E 1 105 ALA 105 106 106 ALA ALA E . n 
E 1 106 ILE 106 107 107 ILE ILE E . n 
E 1 107 THR 107 108 108 THR THR E . n 
E 1 108 ARG 108 109 109 ARG ARG E . n 
E 1 109 ALA 109 110 110 ALA ALA E . n 
E 1 110 LYS 110 111 111 LYS LYS E . n 
E 1 111 ALA 111 112 112 ALA ALA E . n 
E 1 112 GLU 112 113 113 GLU GLU E . n 
E 1 113 GLY 113 114 114 GLY GLY E . n 
E 1 114 PHE 114 115 115 PHE PHE E . n 
E 1 115 SER 115 116 116 SER SER E . n 
E 1 116 ALA 116 117 117 ALA ALA E . n 
E 1 117 LYS 117 118 118 LYS LYS E . n 
E 1 118 MET 118 119 119 MET MET E . n 
E 1 119 GLU 119 120 120 GLU GLU E . n 
E 1 120 PRO 120 121 121 PRO PRO E . n 
E 1 121 GLY 121 122 122 GLY GLY E . n 
E 1 122 ILE 122 123 123 ILE ILE E . n 
E 1 123 SER 123 124 124 SER SER E . n 
E 1 124 ALA 124 125 125 ALA ALA E . n 
E 1 125 GLU 125 126 126 GLU GLU E . n 
E 1 126 ALA 126 127 127 ALA ALA E . n 
E 1 127 CYS 127 128 128 CYS CYS E . n 
E 1 128 LEU 128 129 129 LEU LEU E . n 
E 1 129 TRP 129 130 130 TRP TRP E . n 
E 1 130 ALA 130 131 131 ALA ALA E . n 
E 1 131 ASP 131 132 132 ASP ASP E . n 
E 1 132 LEU 132 133 133 LEU LEU E . n 
E 1 133 GLY 133 134 134 GLY GLY E . n 
E 1 134 ILE 134 135 135 ILE ILE E . n 
E 1 135 ASP 135 136 136 ASP ASP E . n 
E 1 136 PRO 136 137 137 PRO PRO E . n 
E 1 137 GLY 137 138 138 GLY GLY E . n 
E 1 138 ASN 138 139 139 ASN ASN E . n 
E 1 139 SER 139 140 140 SER SER E . n 
E 1 140 GLY 140 141 141 GLY GLY E . n 
E 1 141 HIS 141 142 142 HIS HIS E . n 
E 1 142 GLN 142 143 143 GLN GLN E . n 
E 1 143 SER 143 144 144 SER SER E . n 
E 1 144 PHE 144 145 145 PHE PHE E . n 
E 1 145 GLU 145 146 146 GLU GLU E . n 
E 1 146 ALA 146 147 147 ALA ALA E . n 
E 1 147 SER 147 148 148 SER SER E . n 
E 1 148 GLN 148 149 149 GLN GLN E . n 
E 1 149 PHE 149 150 150 PHE PHE E . n 
E 1 150 MET 150 151 151 MET MET E . n 
E 1 151 PHE 151 152 152 PHE PHE E . n 
E 1 152 PHE 152 153 153 PHE PHE E . n 
E 1 153 ASN 153 154 154 ASN ASN E . n 
E 1 154 HIS 154 155 155 HIS HIS E . n 
E 1 155 VAL 155 156 156 VAL VAL E . n 
E 1 156 PRO 156 157 157 PRO PRO E . n 
E 1 157 ASP 157 158 158 ASP ASP E . n 
E 1 158 PRO 158 159 159 PRO PRO E . n 
E 1 159 THR 159 160 160 THR THR E . n 
E 1 160 THR 160 161 161 THR THR E . n 
E 1 161 HIS 161 162 162 HIS HIS E . n 
E 1 162 LEU 162 163 163 LEU LEU E . n 
E 1 163 LEU 163 164 164 LEU LEU E . n 
E 1 164 LEU 164 165 165 LEU LEU E . n 
E 1 165 TRP 165 166 166 TRP TRP E . n 
E 1 166 GLN 166 167 167 GLN GLN E . n 
E 1 167 ILE 167 168 168 ILE ILE E . n 
E 1 168 ALA 168 169 169 ALA ALA E . n 
E 1 169 ILE 169 170 170 ILE ILE E . n 
E 1 170 ALA 170 171 171 ALA ALA E . n 
E 1 171 GLY 171 172 172 GLY GLY E . n 
E 1 172 GLU 172 173 173 GLU GLU E . n 
E 1 173 HIS 173 174 174 HIS HIS E . n 
E 1 174 THR 174 175 175 THR THR E . n 
E 1 175 LEU 175 176 176 LEU LEU E . n 
E 1 176 THR 176 177 177 THR THR E . n 
E 1 177 GLN 177 178 178 GLN GLN E . n 
E 1 178 PHE 178 179 179 PHE PHE E . n 
E 1 179 HIS 179 180 180 HIS HIS E . n 
E 1 180 THR 180 181 181 THR THR E . n 
E 1 181 SER 181 182 182 SER SER E . n 
E 1 182 SER 182 183 183 SER SER E . n 
E 1 183 ASP 183 184 184 ASP ASP E . n 
E 1 184 ARG 184 185 185 ARG ARG E . n 
E 1 185 LEU 185 186 186 LEU LEU E . n 
E 1 186 GLN 186 187 187 GLN GLN E . n 
E 1 187 ILE 187 188 188 ILE ILE E . n 
E 1 188 LEU 188 189 189 LEU LEU E . n 
E 1 189 VAL 189 190 190 VAL VAL E . n 
E 1 190 GLU 190 191 191 GLU GLU E . n 
E 1 191 GLN 191 192 192 GLN GLN E . n 
E 1 192 LEU 192 193 193 LEU LEU E . n 
E 1 193 ASN 193 194 194 ASN ASN E . n 
E 1 194 GLN 194 195 195 GLN GLN E . n 
E 1 195 TRP 195 196 196 TRP TRP E . n 
E 1 196 TYR 196 197 197 TYR TYR E . n 
E 1 197 PRO 197 198 198 PRO PRO E . n 
E 1 198 LEU 198 199 199 LEU LEU E . n 
E 1 199 ASP 199 200 200 ASP ASP E . n 
E 1 200 HIS 200 201 201 HIS HIS E . n 
E 1 201 GLU 201 202 202 GLU GLU E . n 
E 1 202 VAL 202 203 203 VAL VAL E . n 
E 1 203 VAL 203 204 204 VAL VAL E . n 
E 1 204 ILE 204 205 205 ILE ILE E . n 
E 1 205 TYR 205 206 206 TYR TYR E . n 
E 1 206 GLU 206 207 207 GLU GLU E . n 
E 1 207 ALA 207 208 208 ALA ALA E . n 
E 1 208 ALA 208 209 209 ALA ALA E . n 
E 1 209 ASN 209 210 210 ASN ASN E . n 
E 1 210 LEU 210 211 211 LEU LEU E . n 
E 1 211 PRO 211 212 212 PRO PRO E . n 
E 1 212 ILE 212 213 213 ILE ILE E . n 
E 1 213 GLN 213 214 214 GLN GLN E . n 
E 1 214 ALA 214 215 215 ALA ALA E . n 
E 1 215 PRO 215 216 216 PRO PRO E . n 
E 1 216 ARG 216 217 217 ARG ARG E . n 
E 1 217 ILE 217 218 218 ILE ILE E . n 
E 1 218 GLU 218 219 219 GLU GLU E . n 
E 1 219 ARG 219 220 220 ARG ARG E . n 
E 1 220 LEU 220 221 221 LEU LEU E . n 
E 1 221 PRO 221 222 222 PRO PRO E . n 
E 1 222 LEU 222 223 223 LEU LEU E . n 
E 1 223 ALA 223 224 224 ALA ALA E . n 
E 1 224 ASN 224 225 225 ASN ASN E . n 
E 1 225 LEU 225 226 226 LEU LEU E . n 
E 1 226 PRO 226 227 227 PRO PRO E . n 
E 1 227 GLN 227 228 228 GLN GLN E . n 
E 1 228 ALA 228 229 229 ALA ALA E . n 
E 1 229 HIS 229 230 230 HIS HIS E . n 
E 1 230 LEU 230 231 231 LEU LEU E . n 
E 1 231 MET 231 232 232 MET MET E . n 
E 1 232 PRO 232 233 233 PRO PRO E . n 
E 1 233 ILE 233 234 234 ILE ILE E . n 
E 1 234 SER 234 235 235 SER SER E . n 
E 1 235 THR 235 236 236 THR THR E . n 
E 1 236 LEU 236 237 237 LEU LEU E . n 
E 1 237 LEU 237 238 238 LEU LEU E . n 
E 1 238 ILE 238 239 239 ILE ILE E . n 
E 1 239 PRO 239 240 240 PRO PRO E . n 
E 1 240 PRO 240 241 241 PRO PRO E . n 
E 1 241 ALA 241 242 242 ALA ALA E . n 
E 1 242 LYS 242 243 243 LYS LYS E . n 
E 1 243 LYS 243 244 244 LYS LYS E . n 
E 1 244 LEU 244 245 245 LEU LEU E . n 
E 1 245 GLU 245 246 246 GLU GLU E . n 
E 1 246 TYR 246 247 247 TYR TYR E . n 
E 1 247 ASN 247 248 248 ASN ASN E . n 
E 1 248 TYR 248 249 249 TYR TYR E . n 
E 1 249 ALA 249 250 250 ALA ALA E . n 
E 1 250 ILE 250 251 251 ILE ILE E . n 
E 1 251 LEU 251 252 252 LEU LEU E . n 
E 1 252 ALA 252 253 253 ALA ALA E . n 
E 1 253 LYS 253 254 254 LYS LYS E . n 
E 1 254 LEU 254 255 255 LEU LEU E . n 
E 1 255 GLY 255 256 256 GLY GLY E . n 
E 1 256 ILE 256 257 257 ILE ILE E . n 
E 1 257 GLY 257 258 258 GLY GLY E . n 
E 1 258 PRO 258 259 259 PRO PRO E . n 
E 1 259 GLU 259 260 260 GLU GLU E . n 
E 1 260 ASP 260 261 261 ASP ASP E . n 
E 1 261 LEU 261 262 262 LEU LEU E . n 
E 1 262 GLY 262 263 263 GLY GLY E . n 
F 2 1   GLY 1   3   3   GLY GLY F . n 
F 2 2   LEU 2   4   4   LEU LEU F . n 
F 2 3   SER 3   5   5   SER SER F . n 
F 2 4   ASP 4   6   6   ASP ASP F . n 
F 2 5   PHE 5   7   7   PHE PHE F . n 
F 2 6   PHE 6   8   8   PHE PHE F . n 
F 2 7   THR 7   9   9   THR THR F . n 
F 2 8   GLN 8   10  10  GLN GLN F . n 
F 2 9   LEU 9   11  11  LEU LEU F . n 
F 2 10  GLY 10  12  12  GLY GLY F . n 
F 2 11  GLN 11  13  13  GLN GLN F . n 
F 2 12  ASP 12  14  14  ASP ASP F . n 
F 2 13  ALA 13  15  15  ALA ALA F . n 
F 2 14  GLN 14  16  16  GLN GLN F . n 
F 2 15  LEU 15  17  17  LEU LEU F . n 
F 2 16  MET 16  18  18  MET MET F . n 
F 2 17  GLU 17  19  19  GLU GLU F . n 
F 2 18  ASP 18  20  20  ASP ASP F . n 
F 2 19  TYR 19  21  21  TYR TYR F . n 
F 2 20  LYS 20  22  22  LYS LYS F . n 
F 2 21  GLN 21  23  23  GLN GLN F . n 
F 2 22  ASN 22  24  24  ASN ASN F . n 
F 2 23  PRO 23  25  25  PRO PRO F . n 
F 2 24  GLU 24  26  26  GLU GLU F . n 
F 2 25  ALA 25  27  27  ALA ALA F . n 
F 2 26  VAL 26  28  28  VAL VAL F . n 
F 2 27  MET 27  29  29  MET MET F . n 
F 2 28  ARG 28  30  30  ARG ARG F . n 
F 2 29  ALA 29  31  31  ALA ALA F . n 
F 2 30  HIS 30  32  32  HIS HIS F . n 
F 2 31  GLY 31  33  33  GLY GLY F . n 
F 2 32  LEU 32  34  34  LEU LEU F . n 
F 2 33  THR 33  35  35  THR THR F . n 
F 2 34  ASP 34  36  36  ASP ASP F . n 
F 2 35  GLU 35  37  37  GLU GLU F . n 
F 2 36  GLN 36  38  38  GLN GLN F . n 
F 2 37  ILE 37  39  39  ILE ILE F . n 
F 2 38  ASN 38  40  40  ASN ASN F . n 
F 2 39  ALA 39  41  41  ALA ALA F . n 
F 2 40  VAL 40  42  42  VAL VAL F . n 
F 2 41  MET 41  43  43  MET MET F . n 
F 2 42  THR 42  44  44  THR THR F . n 
F 2 43  GLY 43  45  45  GLY GLY F . n 
F 2 44  ASP 44  46  46  ASP ASP F . n 
F 2 45  MET 45  47  47  MET MET F . n 
F 2 46  GLU 46  48  48  GLU GLU F . n 
F 2 47  LYS 47  49  49  LYS LYS F . n 
F 2 48  LEU 48  50  50  LEU LEU F . n 
F 2 49  LYS 49  51  51  LYS LYS F . n 
F 2 50  THR 50  52  52  THR THR F . n 
F 2 51  LEU 51  53  53  LEU LEU F . n 
F 2 52  SER 52  54  54  SER SER F . n 
F 2 53  GLY 53  55  55  GLY GLY F . n 
F 2 54  ASP 54  56  56  ASP ASP F . n 
F 2 55  SER 55  57  ?   ?   ?   F . n 
F 2 56  SER 56  58  ?   ?   ?   F . n 
F 2 57  TYR 57  59  ?   ?   ?   F . n 
F 2 58  GLN 58  60  ?   ?   ?   F . n 
F 2 59  SER 59  61  ?   ?   ?   F . n 
F 2 60  ALA 60  62  ?   ?   ?   F . n 
F 2 61  LEU 61  63  63  LEU LEU F . n 
F 2 62  VAL 62  64  64  VAL VAL F . n 
F 2 63  IML 63  65  65  IML IML F . n 
F 2 64  SER 64  66  66  SER SER F . n 
F 2 65  HIS 65  67  67  HIS HIS F . n 
F 2 66  GLY 66  68  68  GLY GLY F . n 
F 2 67  ASN 67  69  69  ASN ASN F . n 
F 2 68  GLY 68  70  70  GLY GLY F . n 
G 1 1   GLY 1   2   2   GLY GLY G . n 
G 1 2   SER 2   3   3   SER SER G . n 
G 1 3   LEU 3   4   4   LEU LEU G . n 
G 1 4   VAL 4   5   5   VAL VAL G . n 
G 1 5   CYS 5   6   6   CYS CYS G . n 
G 1 6   VAL 6   7   7   VAL VAL G . n 
G 1 7   GLY 7   8   8   GLY GLY G . n 
G 1 8   THR 8   9   9   THR THR G . n 
G 1 9   GLY 9   10  10  GLY GLY G . n 
G 1 10  LEU 10  11  11  LEU LEU G . n 
G 1 11  GLN 11  12  12  GLN GLN G . n 
G 1 12  LEU 12  13  13  LEU LEU G . n 
G 1 13  ALA 13  14  14  ALA ALA G . n 
G 1 14  GLY 14  15  15  GLY GLY G . n 
G 1 15  GLN 15  16  16  GLN GLN G . n 
G 1 16  ILE 16  17  17  ILE ILE G . n 
G 1 17  SER 17  18  18  SER SER G . n 
G 1 18  VAL 18  19  19  VAL VAL G . n 
G 1 19  LEU 19  20  20  LEU LEU G . n 
G 1 20  SER 20  21  21  SER SER G . n 
G 1 21  ARG 21  22  22  ARG ARG G . n 
G 1 22  SER 22  23  23  SER SER G . n 
G 1 23  TYR 23  24  24  TYR TYR G . n 
G 1 24  ILE 24  25  25  ILE ILE G . n 
G 1 25  GLU 25  26  26  GLU GLU G . n 
G 1 26  HIS 26  27  27  HIS HIS G . n 
G 1 27  ALA 27  28  28  ALA ALA G . n 
G 1 28  ASP 28  29  29  ASP ASP G . n 
G 1 29  ILE 29  30  30  ILE ILE G . n 
G 1 30  VAL 30  31  31  VAL VAL G . n 
G 1 31  PHE 31  32  32  PHE PHE G . n 
G 1 32  SER 32  33  33  SER SER G . n 
G 1 33  LEU 33  34  34  LEU LEU G . n 
G 1 34  LEU 34  35  35  LEU LEU G . n 
G 1 35  PRO 35  36  36  PRO PRO G . n 
G 1 36  ASP 36  37  37  ASP ASP G . n 
G 1 37  GLY 37  38  38  GLY GLY G . n 
G 1 38  PHE 38  39  39  PHE PHE G . n 
G 1 39  SER 39  40  40  SER SER G . n 
G 1 40  GLN 40  41  41  GLN GLN G . n 
G 1 41  ARG 41  42  42  ARG ARG G . n 
G 1 42  TRP 42  43  43  TRP TRP G . n 
G 1 43  LEU 43  44  44  LEU LEU G . n 
G 1 44  THR 44  45  45  THR THR G . n 
G 1 45  LYS 45  46  46  LYS LYS G . n 
G 1 46  LEU 46  47  47  LEU LEU G . n 
G 1 47  ASN 47  48  48  ASN ASN G . n 
G 1 48  PRO 48  49  49  PRO PRO G . n 
G 1 49  ASN 49  50  50  ASN ASN G . n 
G 1 50  VAL 50  51  51  VAL VAL G . n 
G 1 51  ILE 51  52  52  ILE ILE G . n 
G 1 52  ASN 52  53  53  ASN ASN G . n 
G 1 53  LEU 53  54  54  LEU LEU G . n 
G 1 54  GLN 54  55  55  GLN GLN G . n 
G 1 55  GLN 55  56  56  GLN GLN G . n 
G 1 56  PHE 56  57  57  PHE PHE G . n 
G 1 57  TYR 57  58  58  TYR TYR G . n 
G 1 58  ALA 58  59  59  ALA ALA G . n 
G 1 59  GLN 59  60  60  GLN GLN G . n 
G 1 60  ASN 60  61  61  ASN ASN G . n 
G 1 61  GLY 61  62  62  GLY GLY G . n 
G 1 62  GLU 62  63  63  GLU GLU G . n 
G 1 63  VAL 63  64  64  VAL VAL G . n 
G 1 64  LYS 64  65  65  LYS LYS G . n 
G 1 65  ASN 65  66  66  ASN ASN G . n 
G 1 66  ARG 66  67  67  ARG ARG G . n 
G 1 67  ARG 67  68  68  ARG ARG G . n 
G 1 68  ASP 68  69  69  ASP ASP G . n 
G 1 69  THR 69  70  70  THR THR G . n 
G 1 70  TYR 70  71  71  TYR TYR G . n 
G 1 71  GLU 71  72  72  GLU GLU G . n 
G 1 72  GLN 72  73  73  GLN GLN G . n 
G 1 73  MET 73  74  74  MET MET G . n 
G 1 74  VAL 74  75  75  VAL VAL G . n 
G 1 75  ASN 75  76  76  ASN ASN G . n 
G 1 76  ALA 76  77  77  ALA ALA G . n 
G 1 77  ILE 77  78  78  ILE ILE G . n 
G 1 78  LEU 78  79  79  LEU LEU G . n 
G 1 79  ASP 79  80  80  ASP ASP G . n 
G 1 80  ALA 80  81  81  ALA ALA G . n 
G 1 81  VAL 81  82  82  VAL VAL G . n 
G 1 82  ARG 82  83  83  ARG ARG G . n 
G 1 83  ALA 83  84  84  ALA ALA G . n 
G 1 84  GLY 84  85  85  GLY GLY G . n 
G 1 85  LYS 85  86  86  LYS LYS G . n 
G 1 86  LYS 86  87  87  LYS LYS G . n 
G 1 87  THR 87  88  88  THR THR G . n 
G 1 88  VAL 88  89  89  VAL VAL G . n 
G 1 89  CYS 89  90  90  CYS CYS G . n 
G 1 90  ALA 90  91  91  ALA ALA G . n 
G 1 91  LEU 91  92  92  LEU LEU G . n 
G 1 92  TYR 92  93  93  TYR TYR G . n 
G 1 93  GLY 93  94  94  GLY GLY G . n 
G 1 94  HIS 94  95  95  HIS HIS G . n 
G 1 95  PRO 95  96  96  PRO PRO G . n 
G 1 96  GLY 96  97  97  GLY GLY G . n 
G 1 97  VAL 97  98  98  VAL VAL G . n 
G 1 98  PHE 98  99  99  PHE PHE G . n 
G 1 99  ALA 99  100 100 ALA ALA G . n 
G 1 100 CYS 100 101 101 CYS CYS G . n 
G 1 101 VAL 101 102 102 VAL VAL G . n 
G 1 102 SER 102 103 103 SER SER G . n 
G 1 103 HIS 103 104 104 HIS HIS G . n 
G 1 104 MET 104 105 105 MET MET G . n 
G 1 105 ALA 105 106 106 ALA ALA G . n 
G 1 106 ILE 106 107 107 ILE ILE G . n 
G 1 107 THR 107 108 108 THR THR G . n 
G 1 108 ARG 108 109 109 ARG ARG G . n 
G 1 109 ALA 109 110 110 ALA ALA G . n 
G 1 110 LYS 110 111 111 LYS LYS G . n 
G 1 111 ALA 111 112 112 ALA ALA G . n 
G 1 112 GLU 112 113 113 GLU GLU G . n 
G 1 113 GLY 113 114 114 GLY GLY G . n 
G 1 114 PHE 114 115 115 PHE PHE G . n 
G 1 115 SER 115 116 116 SER SER G . n 
G 1 116 ALA 116 117 117 ALA ALA G . n 
G 1 117 LYS 117 118 118 LYS LYS G . n 
G 1 118 MET 118 119 119 MET MET G . n 
G 1 119 GLU 119 120 120 GLU GLU G . n 
G 1 120 PRO 120 121 121 PRO PRO G . n 
G 1 121 GLY 121 122 122 GLY GLY G . n 
G 1 122 ILE 122 123 123 ILE ILE G . n 
G 1 123 SER 123 124 124 SER SER G . n 
G 1 124 ALA 124 125 125 ALA ALA G . n 
G 1 125 GLU 125 126 126 GLU GLU G . n 
G 1 126 ALA 126 127 127 ALA ALA G . n 
G 1 127 CYS 127 128 128 CYS CYS G . n 
G 1 128 LEU 128 129 129 LEU LEU G . n 
G 1 129 TRP 129 130 130 TRP TRP G . n 
G 1 130 ALA 130 131 131 ALA ALA G . n 
G 1 131 ASP 131 132 132 ASP ASP G . n 
G 1 132 LEU 132 133 133 LEU LEU G . n 
G 1 133 GLY 133 134 134 GLY GLY G . n 
G 1 134 ILE 134 135 135 ILE ILE G . n 
G 1 135 ASP 135 136 136 ASP ASP G . n 
G 1 136 PRO 136 137 137 PRO PRO G . n 
G 1 137 GLY 137 138 138 GLY GLY G . n 
G 1 138 ASN 138 139 139 ASN ASN G . n 
G 1 139 SER 139 140 140 SER SER G . n 
G 1 140 GLY 140 141 141 GLY GLY G . n 
G 1 141 HIS 141 142 142 HIS HIS G . n 
G 1 142 GLN 142 143 143 GLN GLN G . n 
G 1 143 SER 143 144 144 SER SER G . n 
G 1 144 PHE 144 145 145 PHE PHE G . n 
G 1 145 GLU 145 146 146 GLU GLU G . n 
G 1 146 ALA 146 147 147 ALA ALA G . n 
G 1 147 SER 147 148 148 SER SER G . n 
G 1 148 GLN 148 149 149 GLN GLN G . n 
G 1 149 PHE 149 150 150 PHE PHE G . n 
G 1 150 MET 150 151 151 MET MET G . n 
G 1 151 PHE 151 152 152 PHE PHE G . n 
G 1 152 PHE 152 153 153 PHE PHE G . n 
G 1 153 ASN 153 154 154 ASN ASN G . n 
G 1 154 HIS 154 155 155 HIS HIS G . n 
G 1 155 VAL 155 156 156 VAL VAL G . n 
G 1 156 PRO 156 157 157 PRO PRO G . n 
G 1 157 ASP 157 158 158 ASP ASP G . n 
G 1 158 PRO 158 159 159 PRO PRO G . n 
G 1 159 THR 159 160 160 THR THR G . n 
G 1 160 THR 160 161 161 THR THR G . n 
G 1 161 HIS 161 162 162 HIS HIS G . n 
G 1 162 LEU 162 163 163 LEU LEU G . n 
G 1 163 LEU 163 164 164 LEU LEU G . n 
G 1 164 LEU 164 165 165 LEU LEU G . n 
G 1 165 TRP 165 166 166 TRP TRP G . n 
G 1 166 GLN 166 167 167 GLN GLN G . n 
G 1 167 ILE 167 168 168 ILE ILE G . n 
G 1 168 ALA 168 169 169 ALA ALA G . n 
G 1 169 ILE 169 170 170 ILE ILE G . n 
G 1 170 ALA 170 171 171 ALA ALA G . n 
G 1 171 GLY 171 172 172 GLY GLY G . n 
G 1 172 GLU 172 173 173 GLU GLU G . n 
G 1 173 HIS 173 174 174 HIS HIS G . n 
G 1 174 THR 174 175 175 THR THR G . n 
G 1 175 LEU 175 176 176 LEU LEU G . n 
G 1 176 THR 176 177 177 THR THR G . n 
G 1 177 GLN 177 178 178 GLN GLN G . n 
G 1 178 PHE 178 179 179 PHE PHE G . n 
G 1 179 HIS 179 180 180 HIS HIS G . n 
G 1 180 THR 180 181 181 THR THR G . n 
G 1 181 SER 181 182 182 SER SER G . n 
G 1 182 SER 182 183 183 SER SER G . n 
G 1 183 ASP 183 184 184 ASP ASP G . n 
G 1 184 ARG 184 185 185 ARG ARG G . n 
G 1 185 LEU 185 186 186 LEU LEU G . n 
G 1 186 GLN 186 187 187 GLN GLN G . n 
G 1 187 ILE 187 188 188 ILE ILE G . n 
G 1 188 LEU 188 189 189 LEU LEU G . n 
G 1 189 VAL 189 190 190 VAL VAL G . n 
G 1 190 GLU 190 191 191 GLU GLU G . n 
G 1 191 GLN 191 192 192 GLN GLN G . n 
G 1 192 LEU 192 193 193 LEU LEU G . n 
G 1 193 ASN 193 194 194 ASN ASN G . n 
G 1 194 GLN 194 195 195 GLN GLN G . n 
G 1 195 TRP 195 196 196 TRP TRP G . n 
G 1 196 TYR 196 197 197 TYR TYR G . n 
G 1 197 PRO 197 198 198 PRO PRO G . n 
G 1 198 LEU 198 199 199 LEU LEU G . n 
G 1 199 ASP 199 200 200 ASP ASP G . n 
G 1 200 HIS 200 201 201 HIS HIS G . n 
G 1 201 GLU 201 202 202 GLU GLU G . n 
G 1 202 VAL 202 203 203 VAL VAL G . n 
G 1 203 VAL 203 204 204 VAL VAL G . n 
G 1 204 ILE 204 205 205 ILE ILE G . n 
G 1 205 TYR 205 206 206 TYR TYR G . n 
G 1 206 GLU 206 207 207 GLU GLU G . n 
G 1 207 ALA 207 208 208 ALA ALA G . n 
G 1 208 ALA 208 209 209 ALA ALA G . n 
G 1 209 ASN 209 210 210 ASN ASN G . n 
G 1 210 LEU 210 211 211 LEU LEU G . n 
G 1 211 PRO 211 212 212 PRO PRO G . n 
G 1 212 ILE 212 213 213 ILE ILE G . n 
G 1 213 GLN 213 214 214 GLN GLN G . n 
G 1 214 ALA 214 215 215 ALA ALA G . n 
G 1 215 PRO 215 216 216 PRO PRO G . n 
G 1 216 ARG 216 217 217 ARG ARG G . n 
G 1 217 ILE 217 218 218 ILE ILE G . n 
G 1 218 GLU 218 219 219 GLU GLU G . n 
G 1 219 ARG 219 220 220 ARG ARG G . n 
G 1 220 LEU 220 221 221 LEU LEU G . n 
G 1 221 PRO 221 222 222 PRO PRO G . n 
G 1 222 LEU 222 223 223 LEU LEU G . n 
G 1 223 ALA 223 224 224 ALA ALA G . n 
G 1 224 ASN 224 225 225 ASN ASN G . n 
G 1 225 LEU 225 226 226 LEU LEU G . n 
G 1 226 PRO 226 227 227 PRO PRO G . n 
G 1 227 GLN 227 228 228 GLN GLN G . n 
G 1 228 ALA 228 229 229 ALA ALA G . n 
G 1 229 HIS 229 230 230 HIS HIS G . n 
G 1 230 LEU 230 231 231 LEU LEU G . n 
G 1 231 MET 231 232 232 MET MET G . n 
G 1 232 PRO 232 233 233 PRO PRO G . n 
G 1 233 ILE 233 234 234 ILE ILE G . n 
G 1 234 SER 234 235 235 SER SER G . n 
G 1 235 THR 235 236 236 THR THR G . n 
G 1 236 LEU 236 237 237 LEU LEU G . n 
G 1 237 LEU 237 238 238 LEU LEU G . n 
G 1 238 ILE 238 239 239 ILE ILE G . n 
G 1 239 PRO 239 240 240 PRO PRO G . n 
G 1 240 PRO 240 241 241 PRO PRO G . n 
G 1 241 ALA 241 242 242 ALA ALA G . n 
G 1 242 LYS 242 243 243 LYS LYS G . n 
G 1 243 LYS 243 244 244 LYS LYS G . n 
G 1 244 LEU 244 245 245 LEU LEU G . n 
G 1 245 GLU 245 246 246 GLU GLU G . n 
G 1 246 TYR 246 247 247 TYR TYR G . n 
G 1 247 ASN 247 248 248 ASN ASN G . n 
G 1 248 TYR 248 249 249 TYR TYR G . n 
G 1 249 ALA 249 250 250 ALA ALA G . n 
G 1 250 ILE 250 251 251 ILE ILE G . n 
G 1 251 LEU 251 252 252 LEU LEU G . n 
G 1 252 ALA 252 253 253 ALA ALA G . n 
G 1 253 LYS 253 254 254 LYS LYS G . n 
G 1 254 LEU 254 255 255 LEU LEU G . n 
G 1 255 GLY 255 256 256 GLY GLY G . n 
G 1 256 ILE 256 257 257 ILE ILE G . n 
G 1 257 GLY 257 258 258 GLY GLY G . n 
G 1 258 PRO 258 259 259 PRO PRO G . n 
G 1 259 GLU 259 260 260 GLU GLU G . n 
G 1 260 ASP 260 261 261 ASP ASP G . n 
G 1 261 LEU 261 262 262 LEU LEU G . n 
G 1 262 GLY 262 263 263 GLY GLY G . n 
H 2 1   GLY 1   3   ?   ?   ?   H . n 
H 2 2   LEU 2   4   4   LEU LEU H . n 
H 2 3   SER 3   5   5   SER SER H . n 
H 2 4   ASP 4   6   6   ASP ASP H . n 
H 2 5   PHE 5   7   7   PHE PHE H . n 
H 2 6   PHE 6   8   8   PHE PHE H . n 
H 2 7   THR 7   9   9   THR THR H . n 
H 2 8   GLN 8   10  10  GLN GLN H . n 
H 2 9   LEU 9   11  11  LEU LEU H . n 
H 2 10  GLY 10  12  12  GLY GLY H . n 
H 2 11  GLN 11  13  13  GLN GLN H . n 
H 2 12  ASP 12  14  14  ASP ASP H . n 
H 2 13  ALA 13  15  15  ALA ALA H . n 
H 2 14  GLN 14  16  16  GLN GLN H . n 
H 2 15  LEU 15  17  17  LEU LEU H . n 
H 2 16  MET 16  18  18  MET MET H . n 
H 2 17  GLU 17  19  19  GLU GLU H . n 
H 2 18  ASP 18  20  20  ASP ASP H . n 
H 2 19  TYR 19  21  21  TYR TYR H . n 
H 2 20  LYS 20  22  22  LYS LYS H . n 
H 2 21  GLN 21  23  23  GLN GLN H . n 
H 2 22  ASN 22  24  24  ASN ASN H . n 
H 2 23  PRO 23  25  25  PRO PRO H . n 
H 2 24  GLU 24  26  26  GLU GLU H . n 
H 2 25  ALA 25  27  27  ALA ALA H . n 
H 2 26  VAL 26  28  28  VAL VAL H . n 
H 2 27  MET 27  29  29  MET MET H . n 
H 2 28  ARG 28  30  30  ARG ARG H . n 
H 2 29  ALA 29  31  31  ALA ALA H . n 
H 2 30  HIS 30  32  32  HIS HIS H . n 
H 2 31  GLY 31  33  33  GLY GLY H . n 
H 2 32  LEU 32  34  34  LEU LEU H . n 
H 2 33  THR 33  35  35  THR THR H . n 
H 2 34  ASP 34  36  36  ASP ASP H . n 
H 2 35  GLU 35  37  37  GLU GLU H . n 
H 2 36  GLN 36  38  38  GLN GLN H . n 
H 2 37  ILE 37  39  39  ILE ILE H . n 
H 2 38  ASN 38  40  40  ASN ASN H . n 
H 2 39  ALA 39  41  41  ALA ALA H . n 
H 2 40  VAL 40  42  42  VAL VAL H . n 
H 2 41  MET 41  43  43  MET MET H . n 
H 2 42  THR 42  44  44  THR THR H . n 
H 2 43  GLY 43  45  45  GLY GLY H . n 
H 2 44  ASP 44  46  46  ASP ASP H . n 
H 2 45  MET 45  47  47  MET MET H . n 
H 2 46  GLU 46  48  48  GLU GLU H . n 
H 2 47  LYS 47  49  49  LYS LYS H . n 
H 2 48  LEU 48  50  50  LEU LEU H . n 
H 2 49  LYS 49  51  51  LYS LYS H . n 
H 2 50  THR 50  52  52  THR THR H . n 
H 2 51  LEU 51  53  53  LEU LEU H . n 
H 2 52  SER 52  54  54  SER SER H . n 
H 2 53  GLY 53  55  55  GLY GLY H . n 
H 2 54  ASP 54  56  56  ASP ASP H . n 
H 2 55  SER 55  57  57  SER SER H . n 
H 2 56  SER 56  58  58  SER SER H . n 
H 2 57  TYR 57  59  ?   ?   ?   H . n 
H 2 58  GLN 58  60  ?   ?   ?   H . n 
H 2 59  SER 59  61  ?   ?   ?   H . n 
H 2 60  ALA 60  62  62  ALA ALA H . n 
H 2 61  LEU 61  63  63  LEU LEU H . n 
H 2 62  VAL 62  64  64  VAL VAL H . n 
H 2 63  IML 63  65  65  IML IML H . n 
H 2 64  SER 64  66  66  SER SER H . n 
H 2 65  HIS 65  67  67  HIS HIS H . n 
H 2 66  GLY 66  68  68  GLY GLY H . n 
H 2 67  ASN 67  69  69  ASN ASN H . n 
H 2 68  GLY 68  70  70  GLY GLY H . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SAH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SAH 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
I 4 SAH 1  301 301 SAH SAH A . 
J 4 SAH 1  301 301 SAH SAH C . 
K 4 SAH 1  301 301 SAH SAH E . 
L 4 SAH 1  301 301 SAH SAH G . 
M 5 HOH 1  401 249 HOH HOH A . 
M 5 HOH 2  402 287 HOH HOH A . 
M 5 HOH 3  403 195 HOH HOH A . 
M 5 HOH 4  404 129 HOH HOH A . 
M 5 HOH 5  405 75  HOH HOH A . 
M 5 HOH 6  406 84  HOH HOH A . 
M 5 HOH 7  407 244 HOH HOH A . 
M 5 HOH 8  408 33  HOH HOH A . 
M 5 HOH 9  409 166 HOH HOH A . 
M 5 HOH 10 410 253 HOH HOH A . 
M 5 HOH 11 411 29  HOH HOH A . 
M 5 HOH 12 412 12  HOH HOH A . 
M 5 HOH 13 413 137 HOH HOH A . 
M 5 HOH 14 414 260 HOH HOH A . 
M 5 HOH 15 415 179 HOH HOH A . 
M 5 HOH 16 416 64  HOH HOH A . 
M 5 HOH 17 417 182 HOH HOH A . 
M 5 HOH 18 418 38  HOH HOH A . 
M 5 HOH 19 419 73  HOH HOH A . 
M 5 HOH 20 420 16  HOH HOH A . 
M 5 HOH 21 421 196 HOH HOH A . 
M 5 HOH 22 422 264 HOH HOH A . 
M 5 HOH 23 423 165 HOH HOH A . 
M 5 HOH 24 424 251 HOH HOH A . 
M 5 HOH 25 425 139 HOH HOH A . 
M 5 HOH 26 426 256 HOH HOH A . 
M 5 HOH 27 427 298 HOH HOH A . 
M 5 HOH 28 428 187 HOH HOH A . 
M 5 HOH 29 429 28  HOH HOH A . 
M 5 HOH 30 430 101 HOH HOH A . 
M 5 HOH 31 431 233 HOH HOH A . 
M 5 HOH 32 432 113 HOH HOH A . 
M 5 HOH 33 433 191 HOH HOH A . 
M 5 HOH 34 434 172 HOH HOH A . 
M 5 HOH 35 435 117 HOH HOH A . 
M 5 HOH 36 436 218 HOH HOH A . 
M 5 HOH 37 437 61  HOH HOH A . 
M 5 HOH 38 438 142 HOH HOH A . 
M 5 HOH 39 439 121 HOH HOH A . 
M 5 HOH 40 440 266 HOH HOH A . 
M 5 HOH 41 441 27  HOH HOH A . 
M 5 HOH 42 442 284 HOH HOH A . 
M 5 HOH 43 443 167 HOH HOH A . 
M 5 HOH 44 444 199 HOH HOH A . 
M 5 HOH 45 445 65  HOH HOH A . 
M 5 HOH 46 446 138 HOH HOH A . 
M 5 HOH 47 447 261 HOH HOH A . 
M 5 HOH 48 448 8   HOH HOH A . 
M 5 HOH 49 449 140 HOH HOH A . 
M 5 HOH 50 450 70  HOH HOH A . 
M 5 HOH 51 451 9   HOH HOH A . 
M 5 HOH 52 452 234 HOH HOH A . 
M 5 HOH 53 453 6   HOH HOH A . 
M 5 HOH 54 454 208 HOH HOH A . 
M 5 HOH 55 455 104 HOH HOH A . 
M 5 HOH 56 456 212 HOH HOH A . 
M 5 HOH 57 457 286 HOH HOH A . 
M 5 HOH 58 458 136 HOH HOH A . 
M 5 HOH 59 459 110 HOH HOH A . 
M 5 HOH 60 460 321 HOH HOH A . 
M 5 HOH 61 461 147 HOH HOH A . 
M 5 HOH 62 462 30  HOH HOH A . 
M 5 HOH 63 463 224 HOH HOH A . 
M 5 HOH 64 464 273 HOH HOH A . 
M 5 HOH 65 465 83  HOH HOH A . 
M 5 HOH 66 466 202 HOH HOH A . 
M 5 HOH 67 467 4   HOH HOH A . 
M 5 HOH 68 468 238 HOH HOH A . 
M 5 HOH 69 469 271 HOH HOH A . 
M 5 HOH 70 470 82  HOH HOH A . 
M 5 HOH 71 471 303 HOH HOH A . 
M 5 HOH 72 472 317 HOH HOH A . 
M 5 HOH 73 473 316 HOH HOH A . 
M 5 HOH 74 474 111 HOH HOH A . 
M 5 HOH 75 475 315 HOH HOH A . 
N 5 HOH 1  101 269 HOH HOH B . 
N 5 HOH 2  102 36  HOH HOH B . 
N 5 HOH 3  103 151 HOH HOH B . 
N 5 HOH 4  104 125 HOH HOH B . 
N 5 HOH 5  105 198 HOH HOH B . 
N 5 HOH 6  106 193 HOH HOH B . 
N 5 HOH 7  107 236 HOH HOH B . 
N 5 HOH 8  108 153 HOH HOH B . 
N 5 HOH 9  109 88  HOH HOH B . 
N 5 HOH 10 110 93  HOH HOH B . 
N 5 HOH 11 111 106 HOH HOH B . 
N 5 HOH 12 112 43  HOH HOH B . 
O 5 HOH 1  401 66  HOH HOH C . 
O 5 HOH 2  402 232 HOH HOH C . 
O 5 HOH 3  403 305 HOH HOH C . 
O 5 HOH 4  404 81  HOH HOH C . 
O 5 HOH 5  405 24  HOH HOH C . 
O 5 HOH 6  406 91  HOH HOH C . 
O 5 HOH 7  407 130 HOH HOH C . 
O 5 HOH 8  408 235 HOH HOH C . 
O 5 HOH 9  409 109 HOH HOH C . 
O 5 HOH 10 410 170 HOH HOH C . 
O 5 HOH 11 411 103 HOH HOH C . 
O 5 HOH 12 412 135 HOH HOH C . 
O 5 HOH 13 413 22  HOH HOH C . 
O 5 HOH 14 414 146 HOH HOH C . 
O 5 HOH 15 415 23  HOH HOH C . 
O 5 HOH 16 416 161 HOH HOH C . 
O 5 HOH 17 417 252 HOH HOH C . 
O 5 HOH 18 418 114 HOH HOH C . 
O 5 HOH 19 419 320 HOH HOH C . 
O 5 HOH 20 420 79  HOH HOH C . 
O 5 HOH 21 421 13  HOH HOH C . 
O 5 HOH 22 422 105 HOH HOH C . 
O 5 HOH 23 423 51  HOH HOH C . 
O 5 HOH 24 424 245 HOH HOH C . 
O 5 HOH 25 425 7   HOH HOH C . 
O 5 HOH 26 426 211 HOH HOH C . 
O 5 HOH 27 427 177 HOH HOH C . 
O 5 HOH 28 428 214 HOH HOH C . 
O 5 HOH 29 429 131 HOH HOH C . 
O 5 HOH 30 430 248 HOH HOH C . 
O 5 HOH 31 431 100 HOH HOH C . 
O 5 HOH 32 432 204 HOH HOH C . 
O 5 HOH 33 433 155 HOH HOH C . 
O 5 HOH 34 434 299 HOH HOH C . 
O 5 HOH 35 435 243 HOH HOH C . 
O 5 HOH 36 436 35  HOH HOH C . 
O 5 HOH 37 437 132 HOH HOH C . 
O 5 HOH 38 438 63  HOH HOH C . 
O 5 HOH 39 439 15  HOH HOH C . 
O 5 HOH 40 440 2   HOH HOH C . 
O 5 HOH 41 441 164 HOH HOH C . 
O 5 HOH 42 442 120 HOH HOH C . 
O 5 HOH 43 443 134 HOH HOH C . 
O 5 HOH 44 444 41  HOH HOH C . 
O 5 HOH 45 445 159 HOH HOH C . 
O 5 HOH 46 446 89  HOH HOH C . 
O 5 HOH 47 447 237 HOH HOH C . 
O 5 HOH 48 448 3   HOH HOH C . 
O 5 HOH 49 449 297 HOH HOH C . 
O 5 HOH 50 450 282 HOH HOH C . 
O 5 HOH 51 451 119 HOH HOH C . 
O 5 HOH 52 452 312 HOH HOH C . 
O 5 HOH 53 453 246 HOH HOH C . 
O 5 HOH 54 454 223 HOH HOH C . 
O 5 HOH 55 455 201 HOH HOH C . 
O 5 HOH 56 456 302 HOH HOH C . 
O 5 HOH 57 457 272 HOH HOH C . 
O 5 HOH 58 458 318 HOH HOH C . 
O 5 HOH 59 459 319 HOH HOH C . 
O 5 HOH 60 460 311 HOH HOH C . 
O 5 HOH 61 461 226 HOH HOH C . 
O 5 HOH 62 462 309 HOH HOH C . 
P 5 HOH 1  101 32  HOH HOH D . 
P 5 HOH 2  102 308 HOH HOH D . 
P 5 HOH 3  103 143 HOH HOH D . 
P 5 HOH 4  104 1   HOH HOH D . 
P 5 HOH 5  105 300 HOH HOH D . 
P 5 HOH 6  106 281 HOH HOH D . 
P 5 HOH 7  107 90  HOH HOH D . 
P 5 HOH 8  108 56  HOH HOH D . 
P 5 HOH 9  109 133 HOH HOH D . 
P 5 HOH 10 110 200 HOH HOH D . 
P 5 HOH 11 111 80  HOH HOH D . 
P 5 HOH 12 112 57  HOH HOH D . 
P 5 HOH 13 113 221 HOH HOH D . 
P 5 HOH 14 114 184 HOH HOH D . 
P 5 HOH 15 115 277 HOH HOH D . 
P 5 HOH 16 116 220 HOH HOH D . 
Q 5 HOH 1  401 17  HOH HOH E . 
Q 5 HOH 2  402 162 HOH HOH E . 
Q 5 HOH 3  403 230 HOH HOH E . 
Q 5 HOH 4  404 31  HOH HOH E . 
Q 5 HOH 5  405 267 HOH HOH E . 
Q 5 HOH 6  406 296 HOH HOH E . 
Q 5 HOH 7  407 99  HOH HOH E . 
Q 5 HOH 8  408 289 HOH HOH E . 
Q 5 HOH 9  409 190 HOH HOH E . 
Q 5 HOH 10 410 205 HOH HOH E . 
Q 5 HOH 11 411 285 HOH HOH E . 
Q 5 HOH 12 412 60  HOH HOH E . 
Q 5 HOH 13 413 217 HOH HOH E . 
Q 5 HOH 14 414 247 HOH HOH E . 
Q 5 HOH 15 415 213 HOH HOH E . 
Q 5 HOH 16 416 71  HOH HOH E . 
Q 5 HOH 17 417 25  HOH HOH E . 
Q 5 HOH 18 418 259 HOH HOH E . 
Q 5 HOH 19 419 241 HOH HOH E . 
Q 5 HOH 20 420 54  HOH HOH E . 
Q 5 HOH 21 421 74  HOH HOH E . 
Q 5 HOH 22 422 126 HOH HOH E . 
Q 5 HOH 23 423 95  HOH HOH E . 
Q 5 HOH 24 424 52  HOH HOH E . 
Q 5 HOH 25 425 141 HOH HOH E . 
Q 5 HOH 26 426 58  HOH HOH E . 
Q 5 HOH 27 427 210 HOH HOH E . 
Q 5 HOH 28 428 20  HOH HOH E . 
Q 5 HOH 29 429 108 HOH HOH E . 
Q 5 HOH 30 430 215 HOH HOH E . 
Q 5 HOH 31 431 85  HOH HOH E . 
Q 5 HOH 32 432 128 HOH HOH E . 
Q 5 HOH 33 433 94  HOH HOH E . 
Q 5 HOH 34 434 180 HOH HOH E . 
Q 5 HOH 35 435 150 HOH HOH E . 
Q 5 HOH 36 436 144 HOH HOH E . 
Q 5 HOH 37 437 107 HOH HOH E . 
Q 5 HOH 38 438 275 HOH HOH E . 
Q 5 HOH 39 439 158 HOH HOH E . 
Q 5 HOH 40 440 171 HOH HOH E . 
Q 5 HOH 41 441 37  HOH HOH E . 
Q 5 HOH 42 442 231 HOH HOH E . 
Q 5 HOH 43 443 268 HOH HOH E . 
Q 5 HOH 44 444 203 HOH HOH E . 
Q 5 HOH 45 445 293 HOH HOH E . 
Q 5 HOH 46 446 250 HOH HOH E . 
Q 5 HOH 47 447 76  HOH HOH E . 
Q 5 HOH 48 448 19  HOH HOH E . 
Q 5 HOH 49 449 72  HOH HOH E . 
Q 5 HOH 50 450 118 HOH HOH E . 
Q 5 HOH 51 451 229 HOH HOH E . 
Q 5 HOH 52 452 274 HOH HOH E . 
Q 5 HOH 53 453 227 HOH HOH E . 
Q 5 HOH 54 454 152 HOH HOH E . 
R 5 HOH 1  101 194 HOH HOH F . 
R 5 HOH 2  102 181 HOH HOH F . 
R 5 HOH 3  103 21  HOH HOH F . 
R 5 HOH 4  104 290 HOH HOH F . 
R 5 HOH 5  105 176 HOH HOH F . 
R 5 HOH 6  106 18  HOH HOH F . 
R 5 HOH 7  107 59  HOH HOH F . 
R 5 HOH 8  108 206 HOH HOH F . 
R 5 HOH 9  109 11  HOH HOH F . 
R 5 HOH 10 110 98  HOH HOH F . 
R 5 HOH 11 111 45  HOH HOH F . 
R 5 HOH 12 112 242 HOH HOH F . 
R 5 HOH 13 113 228 HOH HOH F . 
R 5 HOH 14 114 34  HOH HOH F . 
R 5 HOH 15 115 314 HOH HOH F . 
R 5 HOH 16 116 219 HOH HOH F . 
S 5 HOH 1  401 44  HOH HOH G . 
S 5 HOH 2  402 306 HOH HOH G . 
S 5 HOH 3  403 163 HOH HOH G . 
S 5 HOH 4  404 78  HOH HOH G . 
S 5 HOH 5  405 255 HOH HOH G . 
S 5 HOH 6  406 154 HOH HOH G . 
S 5 HOH 7  407 62  HOH HOH G . 
S 5 HOH 8  408 50  HOH HOH G . 
S 5 HOH 9  409 186 HOH HOH G . 
S 5 HOH 10 410 127 HOH HOH G . 
S 5 HOH 11 411 183 HOH HOH G . 
S 5 HOH 12 412 265 HOH HOH G . 
S 5 HOH 13 413 97  HOH HOH G . 
S 5 HOH 14 414 53  HOH HOH G . 
S 5 HOH 15 415 288 HOH HOH G . 
S 5 HOH 16 416 46  HOH HOH G . 
S 5 HOH 17 417 49  HOH HOH G . 
S 5 HOH 18 418 188 HOH HOH G . 
S 5 HOH 19 419 304 HOH HOH G . 
S 5 HOH 20 420 55  HOH HOH G . 
S 5 HOH 21 421 42  HOH HOH G . 
S 5 HOH 22 422 5   HOH HOH G . 
S 5 HOH 23 423 189 HOH HOH G . 
S 5 HOH 24 424 216 HOH HOH G . 
S 5 HOH 25 425 239 HOH HOH G . 
S 5 HOH 26 426 96  HOH HOH G . 
S 5 HOH 27 427 115 HOH HOH G . 
S 5 HOH 28 428 39  HOH HOH G . 
S 5 HOH 29 429 209 HOH HOH G . 
S 5 HOH 30 430 14  HOH HOH G . 
S 5 HOH 31 431 278 HOH HOH G . 
S 5 HOH 32 432 174 HOH HOH G . 
S 5 HOH 33 433 40  HOH HOH G . 
S 5 HOH 34 434 68  HOH HOH G . 
S 5 HOH 35 435 123 HOH HOH G . 
S 5 HOH 36 436 301 HOH HOH G . 
S 5 HOH 37 437 173 HOH HOH G . 
S 5 HOH 38 438 69  HOH HOH G . 
S 5 HOH 39 439 160 HOH HOH G . 
S 5 HOH 40 440 148 HOH HOH G . 
S 5 HOH 41 441 157 HOH HOH G . 
S 5 HOH 42 442 207 HOH HOH G . 
S 5 HOH 43 443 175 HOH HOH G . 
S 5 HOH 44 444 149 HOH HOH G . 
S 5 HOH 45 445 67  HOH HOH G . 
S 5 HOH 46 446 168 HOH HOH G . 
S 5 HOH 47 447 48  HOH HOH G . 
S 5 HOH 48 448 47  HOH HOH G . 
S 5 HOH 49 449 122 HOH HOH G . 
S 5 HOH 50 450 263 HOH HOH G . 
S 5 HOH 51 451 283 HOH HOH G . 
S 5 HOH 52 452 169 HOH HOH G . 
S 5 HOH 53 453 112 HOH HOH G . 
S 5 HOH 54 454 254 HOH HOH G . 
S 5 HOH 55 455 225 HOH HOH G . 
S 5 HOH 56 456 240 HOH HOH G . 
S 5 HOH 57 457 222 HOH HOH G . 
S 5 HOH 58 458 276 HOH HOH G . 
T 5 HOH 1  101 280 HOH HOH H . 
T 5 HOH 2  102 26  HOH HOH H . 
T 5 HOH 3  103 10  HOH HOH H . 
T 5 HOH 4  104 292 HOH HOH H . 
T 5 HOH 5  105 102 HOH HOH H . 
T 5 HOH 6  106 197 HOH HOH H . 
T 5 HOH 7  107 258 HOH HOH H . 
T 5 HOH 8  108 156 HOH HOH H . 
T 5 HOH 9  109 279 HOH HOH H . 
T 5 HOH 10 110 77  HOH HOH H . 
T 5 HOH 11 111 86  HOH HOH H . 
T 5 HOH 12 112 313 HOH HOH H . 
T 5 HOH 13 113 124 HOH HOH H . 
# 
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                  89.95 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.11 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  85.97 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CHI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.050 
_cell.length_a_esd                 ? 
_cell.length_b                     59.060 
_cell.length_b_esd                 ? 
_cell.length_c                     108.580 
_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                         9CHI 
_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                   9CHI 
_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             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.65 
_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              6 
_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 6, 12% 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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-02-26 
_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   1.0332 
_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        1.0332 
_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                                       9CHI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               19.64 
_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                                     56505 
_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                           86.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.01 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.15 
_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                                0.09 
_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                             7177 
_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                               0.39 
_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                                  0.931 
_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]                            -13.96 
_refine.aniso_B[1][2]                            16.39 
_refine.aniso_B[1][3]                            9.39 
_refine.aniso_B[2][2]                            2.70 
_refine.aniso_B[2][3]                            -0.44 
_refine.aniso_B[3][3]                            11.26 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               38.435 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.923 
_refine.correlation_coeff_Fo_to_Fc_free          0.894 
_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                                 9CHI 
_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                             19.64 
_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                     53632 
_refine.ls_number_reflns_R_free                  2872 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    85.87 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.26703 
_refine.ls_R_factor_R_free                       0.30880 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.26469 
_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                       0.126 
_refine.pdbx_overall_ESU_R_Free                  0.068 
_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                             17.493 
_refine.overall_SU_ML                            0.232 
_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                        19.64 
_refine_hist.number_atoms_solvent             306 
_refine_hist.number_atoms_total               10478 
_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        10068 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         104 
_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' ? 0.001 0.012  10477 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.000 0.016  9897  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.448 1.809  14253 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.152 1.741  22795 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 4.526 5.000  1303  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 1.163 5.000  44    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.060 10.000 1713  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.021 0.200  1602  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.001 0.020  12320 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.000 0.020  2328  ? 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' ? 2.639 3.045  5233  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.639 3.045  5232  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.858 5.454  6524  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.857 5.454  6525  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.070 3.383  5244  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.069 3.383  5245  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.761 6.062  7726  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.718 32.48  12193 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.714 32.42  12170 ? 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                        2.252 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             198 
_refine_ls_shell.number_reflns_R_work             3641 
_refine_ls_shell.percent_reflns_obs               79.58 
_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                  0.328 
_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                  0.378 
# 
_struct.entry_id                     9CHI 
_struct.title                        
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-Y62A) heteromeric complex (bound to SAH - structure 2)' 
_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        9CHI 
_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 3 ? 
E N N 1 ? 
F N N 2 ? 
G N N 1 ? 
H N N 2 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 5 ? 
R N N 5 ? 
S N N 5 ? 
T N N 5 ? 
# 
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 
;GSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILDA
VRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPTT
HLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIPP
AKKLEYNYAILAKLGIGPEDLG
;
2 
2 UNP Q8EGW2_SHEON Q8EGW2 ? 2 GLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYLVISHGNG 3 
3 UNP Q8EGW2_SHEON Q8EGW2 ? 3 GLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYLVISHGNG 3 
# 
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 9CHI A 1 ? 262 ? Q8EGW3 2 ? 263 ? 2 263 
2 2 9CHI B 1 ? 68  ? Q8EGW2 3 ? 70  ? 3 70  
3 1 9CHI C 1 ? 262 ? Q8EGW3 2 ? 263 ? 2 263 
4 3 9CHI D 1 ? 68  ? Q8EGW2 3 ? 70  ? 3 70  
5 1 9CHI E 1 ? 262 ? Q8EGW3 2 ? 263 ? 2 263 
6 2 9CHI F 1 ? 68  ? Q8EGW2 3 ? 70  ? 3 70  
7 1 9CHI G 1 ? 262 ? Q8EGW3 2 ? 263 ? 2 263 
8 2 9CHI H 1 ? 68  ? Q8EGW2 3 ? 70  ? 3 70  
# 
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 9CHI ALA B 60 ? UNP Q8EGW2 TYR 62 'engineered mutation' 62 1 
4 9CHI ALA D 60 ? UNP Q8EGW2 TYR 62 'engineered mutation' 62 2 
6 9CHI ALA F 60 ? UNP Q8EGW2 TYR 62 'engineered mutation' 62 3 
8 9CHI ALA H 60 ? UNP Q8EGW2 TYR 62 'engineered mutation' 62 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_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)' 12830 ? 
1 MORE         -77   ? 
1 'SSA (A^2)'  23400 ? 
2 'ABSA (A^2)' 12730 ? 
2 MORE         -78   ? 
2 'SSA (A^2)'  23360 ? 
# 
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,M,N,O,P 
2 1 E,F,G,H,K,L,Q,R,S,T 
# 
_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 17  ? HIS A 26  ? SER A 18  HIS A 27  1 ? 10 
HELX_P HELX_P2  AA2 ASP A 36  ? ASN A 47  ? ASP A 37  ASN A 48  1 ? 12 
HELX_P HELX_P3  AA3 GLN A 54  ? TYR A 57  ? GLN A 55  TYR A 58  5 ? 4  
HELX_P HELX_P4  AA4 ASN A 65  ? GLY A 84  ? ASN A 66  GLY A 85  1 ? 20 
HELX_P HELX_P5  AA5 ALA A 99  ? GLU A 112 ? ALA A 100 GLU A 113 1 ? 14 
HELX_P HELX_P6  AA6 SER A 123 ? GLY A 133 ? SER A 124 GLY A 134 1 ? 11 
HELX_P HELX_P7  AA7 SER A 147 ? PHE A 152 ? SER A 148 PHE A 153 1 ? 6  
HELX_P HELX_P8  AA8 GLN A 166 ? ALA A 170 ? GLN A 167 ALA A 171 5 ? 5  
HELX_P HELX_P9  AA9 SER A 181 ? ASN A 193 ? SER A 182 ASN A 194 1 ? 13 
HELX_P HELX_P10 AB1 ALA A 223 ? ALA A 228 ? ALA A 224 ALA A 229 5 ? 6  
HELX_P HELX_P11 AB2 ASN A 247 ? GLY A 255 ? ASN A 248 GLY A 256 1 ? 9  
HELX_P HELX_P12 AB3 GLY A 257 ? LEU A 261 ? GLY A 258 LEU A 262 5 ? 5  
HELX_P HELX_P13 AB4 LEU B 2   ? GLY B 10  ? LEU B 4   GLY B 12  1 ? 9  
HELX_P HELX_P14 AB5 ASP B 12  ? ASN B 22  ? ASP B 14  ASN B 24  1 ? 11 
HELX_P HELX_P15 AB6 ASN B 22  ? HIS B 30  ? ASN B 24  HIS B 32  1 ? 9  
HELX_P HELX_P16 AB7 THR B 33  ? GLY B 43  ? THR B 35  GLY B 45  1 ? 11 
HELX_P HELX_P17 AB8 ASP B 44  ? GLY B 53  ? ASP B 46  GLY B 55  1 ? 10 
HELX_P HELX_P18 AB9 SER C 17  ? HIS C 26  ? SER C 18  HIS C 27  1 ? 10 
HELX_P HELX_P19 AC1 ASP C 36  ? ASN C 47  ? ASP C 37  ASN C 48  1 ? 12 
HELX_P HELX_P20 AC2 GLN C 54  ? TYR C 57  ? GLN C 55  TYR C 58  5 ? 4  
HELX_P HELX_P21 AC3 ASN C 65  ? GLY C 84  ? ASN C 66  GLY C 85  1 ? 20 
HELX_P HELX_P22 AC4 ALA C 99  ? GLU C 112 ? ALA C 100 GLU C 113 1 ? 14 
HELX_P HELX_P23 AC5 SER C 123 ? LEU C 132 ? SER C 124 LEU C 133 1 ? 10 
HELX_P HELX_P24 AC6 ALA C 146 ? PHE C 152 ? ALA C 147 PHE C 153 1 ? 7  
HELX_P HELX_P25 AC7 GLN C 166 ? ALA C 170 ? GLN C 167 ALA C 171 5 ? 5  
HELX_P HELX_P26 AC8 SER C 181 ? ASN C 193 ? SER C 182 ASN C 194 1 ? 13 
HELX_P HELX_P27 AC9 ALA C 223 ? ALA C 228 ? ALA C 224 ALA C 229 5 ? 6  
HELX_P HELX_P28 AD1 ASN C 247 ? LEU C 254 ? ASN C 248 LEU C 255 1 ? 8  
HELX_P HELX_P29 AD2 GLY C 257 ? LEU C 261 ? GLY C 258 LEU C 262 5 ? 5  
HELX_P HELX_P30 AD3 SER D 3   ? ASP D 12  ? SER D 5   ASP D 14  1 ? 10 
HELX_P HELX_P31 AD4 ASP D 12  ? ASN D 22  ? ASP D 14  ASN D 24  1 ? 11 
HELX_P HELX_P32 AD5 ASN D 22  ? HIS D 30  ? ASN D 24  HIS D 32  1 ? 9  
HELX_P HELX_P33 AD6 THR D 33  ? GLY D 43  ? THR D 35  GLY D 45  1 ? 11 
HELX_P HELX_P34 AD7 ASP D 44  ? SER D 52  ? ASP D 46  SER D 54  1 ? 9  
HELX_P HELX_P35 AD8 SER E 17  ? HIS E 26  ? SER E 18  HIS E 27  1 ? 10 
HELX_P HELX_P36 AD9 ASP E 36  ? ASN E 47  ? ASP E 37  ASN E 48  1 ? 12 
HELX_P HELX_P37 AE1 GLN E 54  ? TYR E 57  ? GLN E 55  TYR E 58  5 ? 4  
HELX_P HELX_P38 AE2 ASN E 65  ? GLY E 84  ? ASN E 66  GLY E 85  1 ? 20 
HELX_P HELX_P39 AE3 ALA E 99  ? GLU E 112 ? ALA E 100 GLU E 113 1 ? 14 
HELX_P HELX_P40 AE4 SER E 123 ? GLY E 133 ? SER E 124 GLY E 134 1 ? 11 
HELX_P HELX_P41 AE5 SER E 147 ? PHE E 152 ? SER E 148 PHE E 153 1 ? 6  
HELX_P HELX_P42 AE6 GLN E 166 ? ALA E 170 ? GLN E 167 ALA E 171 5 ? 5  
HELX_P HELX_P43 AE7 SER E 181 ? ASN E 193 ? SER E 182 ASN E 194 1 ? 13 
HELX_P HELX_P44 AE8 ALA E 223 ? ALA E 228 ? ALA E 224 ALA E 229 5 ? 6  
HELX_P HELX_P45 AE9 ASN E 247 ? GLY E 255 ? ASN E 248 GLY E 256 1 ? 9  
HELX_P HELX_P46 AF1 GLY E 257 ? LEU E 261 ? GLY E 258 LEU E 262 5 ? 5  
HELX_P HELX_P47 AF2 LEU F 2   ? GLY F 10  ? LEU F 4   GLY F 12  1 ? 9  
HELX_P HELX_P48 AF3 ASP F 12  ? ASN F 22  ? ASP F 14  ASN F 24  1 ? 11 
HELX_P HELX_P49 AF4 ASN F 22  ? HIS F 30  ? ASN F 24  HIS F 32  1 ? 9  
HELX_P HELX_P50 AF5 THR F 33  ? GLY F 43  ? THR F 35  GLY F 45  1 ? 11 
HELX_P HELX_P51 AF6 ASP F 44  ? LEU F 51  ? ASP F 46  LEU F 53  1 ? 8  
HELX_P HELX_P52 AF7 SER G 17  ? HIS G 26  ? SER G 18  HIS G 27  1 ? 10 
HELX_P HELX_P53 AF8 ASP G 36  ? ASN G 47  ? ASP G 37  ASN G 48  1 ? 12 
HELX_P HELX_P54 AF9 GLN G 54  ? TYR G 57  ? GLN G 55  TYR G 58  5 ? 4  
HELX_P HELX_P55 AG1 ASN G 65  ? GLY G 84  ? ASN G 66  GLY G 85  1 ? 20 
HELX_P HELX_P56 AG2 ALA G 99  ? GLU G 112 ? ALA G 100 GLU G 113 1 ? 14 
HELX_P HELX_P57 AG3 SER G 123 ? LEU G 132 ? SER G 124 LEU G 133 1 ? 10 
HELX_P HELX_P58 AG4 ALA G 146 ? PHE G 152 ? ALA G 147 PHE G 153 1 ? 7  
HELX_P HELX_P59 AG5 GLN G 166 ? ALA G 170 ? GLN G 167 ALA G 171 5 ? 5  
HELX_P HELX_P60 AG6 SER G 181 ? ASN G 193 ? SER G 182 ASN G 194 1 ? 13 
HELX_P HELX_P61 AG7 ALA G 223 ? ALA G 228 ? ALA G 224 ALA G 229 5 ? 6  
HELX_P HELX_P62 AG8 ASN G 247 ? GLY G 255 ? ASN G 248 GLY G 256 1 ? 9  
HELX_P HELX_P63 AG9 GLY G 257 ? LEU G 261 ? GLY G 258 LEU G 262 5 ? 5  
HELX_P HELX_P64 AH1 SER H 3   ? ASP H 12  ? SER H 5   ASP H 14  1 ? 10 
HELX_P HELX_P65 AH2 ASP H 12  ? ASN H 22  ? ASP H 14  ASN H 24  1 ? 11 
HELX_P HELX_P66 AH3 ASN H 22  ? HIS H 30  ? ASN H 24  HIS H 32  1 ? 9  
HELX_P HELX_P67 AH4 THR H 33  ? GLY H 43  ? THR H 35  GLY H 45  1 ? 11 
HELX_P HELX_P68 AH5 ASP H 44  ? SER H 52  ? ASP H 46  SER H 54  1 ? 9  
# 
_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 VAL 62 C ? ? ? 1_555 B IML 63 N ? ? B VAL 64 B IML 65 1_555 ? ? ? ? ? ? ? 1.358 ? ? 
covale2 covale both ? B IML 63 C ? ? ? 1_555 B SER 64 N ? ? B IML 65 B SER 66 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale3 covale both ? F VAL 62 C ? ? ? 1_555 F IML 63 N ? ? F VAL 64 F IML 65 1_555 ? ? ? ? ? ? ? 1.356 ? ? 
covale4 covale both ? F IML 63 C ? ? ? 1_555 F SER 64 N ? ? F IML 65 F SER 66 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale5 covale both ? H VAL 62 C ? ? ? 1_555 H IML 63 N ? ? H VAL 64 H IML 65 1_555 ? ? ? ? ? ? ? 1.355 ? ? 
covale6 covale both ? H IML 63 C ? ? ? 1_555 H SER 64 N ? ? H IML 65 H SER 66 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 IML B 63 ? . . . . IML B 65 ? 1_555 . . . . . . . ILE 1 IML Methylation 'Named protein modification' 
2 IML F 63 ? . . . . IML F 65 ? 1_555 . . . . . . . ILE 1 IML Methylation 'Named protein modification' 
3 IML H 63 ? . . . . IML H 65 ? 1_555 . . . . . . . ILE 1 IML Methylation '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 50  ? ASN A 52  ? VAL A 51  ASN A 53  
AA1 2  ILE A 29  ? LEU A 33  ? ILE A 30  LEU A 34  
AA1 3  LYS A 86  ? LEU A 91  ? LYS A 87  LEU A 92  
AA1 4  SER A 2   ? GLY A 7   ? SER A 3   GLY A 8   
AA1 5  SER A 115 ? MET A 118 ? SER A 116 MET A 119 
AA2 1  ARG A 216 ? PRO A 221 ? ARG A 217 PRO A 222 
AA2 2  GLU A 201 ? GLU A 206 ? GLU A 202 GLU A 207 
AA2 3  THR A 235 ? ILE A 238 ? THR A 236 ILE A 239 
AA2 4  HIS A 161 ? TRP A 165 ? HIS A 162 TRP A 166 
AA2 5  HIS A 141 ? GLU A 145 ? HIS A 142 GLU A 146 
AA2 6  HIS C 141 ? GLU C 145 ? HIS C 142 GLU C 146 
AA2 7  HIS C 161 ? TRP C 165 ? HIS C 162 TRP C 166 
AA2 8  THR C 235 ? ILE C 238 ? THR C 236 ILE C 239 
AA2 9  GLU C 201 ? GLU C 206 ? GLU C 202 GLU C 207 
AA2 10 ARG C 216 ? PRO C 221 ? ARG C 217 PRO C 222 
AA3 1  VAL C 50  ? ASN C 52  ? VAL C 51  ASN C 53  
AA3 2  ILE C 29  ? LEU C 33  ? ILE C 30  LEU C 34  
AA3 3  LYS C 86  ? LEU C 91  ? LYS C 87  LEU C 92  
AA3 4  SER C 2   ? GLY C 7   ? SER C 3   GLY C 8   
AA3 5  SER C 115 ? MET C 118 ? SER C 116 MET C 119 
AA4 1  VAL E 50  ? ASN E 52  ? VAL E 51  ASN E 53  
AA4 2  ILE E 29  ? LEU E 33  ? ILE E 30  LEU E 34  
AA4 3  LYS E 86  ? LEU E 91  ? LYS E 87  LEU E 92  
AA4 4  SER E 2   ? GLY E 7   ? SER E 3   GLY E 8   
AA4 5  SER E 115 ? MET E 118 ? SER E 116 MET E 119 
AA5 1  ARG E 216 ? PRO E 221 ? ARG E 217 PRO E 222 
AA5 2  GLU E 201 ? GLU E 206 ? GLU E 202 GLU E 207 
AA5 3  THR E 235 ? ILE E 238 ? THR E 236 ILE E 239 
AA5 4  HIS E 161 ? TRP E 165 ? HIS E 162 TRP E 166 
AA5 5  HIS E 141 ? GLU E 145 ? HIS E 142 GLU E 146 
AA5 6  HIS G 141 ? GLU G 145 ? HIS G 142 GLU G 146 
AA5 7  HIS G 161 ? TRP G 165 ? HIS G 162 TRP G 166 
AA5 8  THR G 235 ? ILE G 238 ? THR G 236 ILE G 239 
AA5 9  GLU G 201 ? GLU G 206 ? GLU G 202 GLU G 207 
AA5 10 ARG G 216 ? PRO G 221 ? ARG G 217 PRO G 222 
AA6 1  VAL G 50  ? ASN G 52  ? VAL G 51  ASN G 53  
AA6 2  ILE G 29  ? LEU G 33  ? ILE G 30  LEU G 34  
AA6 3  LYS G 86  ? LEU G 91  ? LYS G 87  LEU G 92  
AA6 4  SER G 2   ? GLY G 7   ? SER G 3   GLY G 8   
AA6 5  SER G 115 ? MET G 118 ? SER G 116 MET G 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 51  ? O ILE A 52  N VAL A 30  ? N VAL A 31  
AA1 2 3  N PHE A 31  ? N PHE A 32  O ALA A 90  ? O ALA A 91  
AA1 3 4  O CYS A 89  ? O CYS A 90  N VAL A 6   ? N VAL A 7   
AA1 4 5  N LEU A 3   ? N LEU A 4   O SER A 115 ? O SER A 116 
AA2 1 2  O LEU A 220 ? O LEU A 221 N VAL A 202 ? N VAL A 203 
AA2 2 3  N VAL A 203 ? N VAL A 204 O LEU A 237 ? O LEU A 238 
AA2 3 4  O ILE A 238 ? O ILE A 239 N LEU A 162 ? N LEU A 163 
AA2 4 5  O LEU A 163 ? O LEU A 164 N PHE A 144 ? N PHE A 145 
AA2 5 6  N SER A 143 ? N SER A 144 O HIS C 141 ? O HIS C 142 
AA2 6 7  N GLN C 142 ? N GLN C 143 O LEU C 163 ? O LEU C 164 
AA2 7 8  N LEU C 162 ? N LEU C 163 O ILE C 238 ? O ILE C 239 
AA2 8 9  O LEU C 237 ? O LEU C 238 N VAL C 203 ? N VAL C 204 
AA2 9 10 N GLU C 206 ? N GLU C 207 O ARG C 216 ? O ARG C 217 
AA3 1 2  O ILE C 51  ? O ILE C 52  N VAL C 30  ? N VAL C 31  
AA3 2 3  N PHE C 31  ? N PHE C 32  O ALA C 90  ? O ALA C 91  
AA3 3 4  O CYS C 89  ? O CYS C 90  N VAL C 6   ? N VAL C 7   
AA3 4 5  N LEU C 3   ? N LEU C 4   O SER C 115 ? O SER C 116 
AA4 1 2  O ILE E 51  ? O ILE E 52  N VAL E 30  ? N VAL E 31  
AA4 2 3  N PHE E 31  ? N PHE E 32  O ALA E 90  ? O ALA E 91  
AA4 3 4  O CYS E 89  ? O CYS E 90  N VAL E 6   ? N VAL E 7   
AA4 4 5  N LEU E 3   ? N LEU E 4   O SER E 115 ? O SER E 116 
AA5 1 2  O LEU E 220 ? O LEU E 221 N VAL E 202 ? N VAL E 203 
AA5 2 3  N VAL E 203 ? N VAL E 204 O LEU E 237 ? O LEU E 238 
AA5 3 4  O ILE E 238 ? O ILE E 239 N LEU E 162 ? N LEU E 163 
AA5 4 5  O LEU E 163 ? O LEU E 164 N GLN E 142 ? N GLN E 143 
AA5 5 6  N HIS E 141 ? N HIS E 142 O SER G 143 ? O SER G 144 
AA5 6 7  N PHE G 144 ? N PHE G 145 O TRP G 165 ? O TRP G 166 
AA5 7 8  N LEU G 162 ? N LEU G 163 O ILE G 238 ? O ILE G 239 
AA5 8 9  O LEU G 237 ? O LEU G 238 N VAL G 203 ? N VAL G 204 
AA5 9 10 N VAL G 202 ? N VAL G 203 O LEU G 220 ? O LEU G 221 
AA6 1 2  O ILE G 51  ? O ILE G 52  N VAL G 30  ? N VAL G 31  
AA6 2 3  N PHE G 31  ? N PHE G 32  O VAL G 88  ? O VAL G 89  
AA6 3 4  O CYS G 89  ? O CYS G 90  N VAL G 6   ? N VAL G 7   
AA6 4 5  N LEU G 3   ? N LEU G 4   O SER G 115 ? O SER G 116 
# 
_pdbx_entry_details.entry_id                   9CHI 
_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 NH2 C ARG 42  ? B OD2 D ASP 56  ? ? 1.41 
2 1 OG  A SER 182 ? ? OD1 A ASP 184 ? ? 2.05 
3 1 OE2 C GLU 207 ? ? OG  C SER 235 ? ? 2.06 
4 1 OG  G SER 182 ? ? OD1 G ASP 184 ? ? 2.10 
5 1 OG  E SER 182 ? ? OD1 E ASP 184 ? ? 2.12 
6 1 OH  C TYR 58  ? ? O   D VAL 64  ? ? 2.14 
# 
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 CD  F GLU 48 ? ? 1_555 OE1 G GLN 60 ? ? 1_565 1.35 
2 1 OE2 F GLU 48 ? ? 1_555 OE1 G GLN 60 ? ? 1_565 1.45 
3 1 OE1 F GLU 48 ? ? 1_555 OE1 G GLN 60 ? ? 1_565 1.57 
4 1 OE1 F GLU 48 ? ? 1_555 NE2 G GLN 60 ? ? 1_565 1.76 
5 1 OE1 F GLU 48 ? ? 1_555 CD  G GLN 60 ? ? 1_565 1.84 
# 
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  ? ? 80.45   -36.13  
2  1 ASN A 61  ? ? 72.83   79.35   
3  1 LYS A 87  ? ? -66.90  92.08   
4  1 SER A 140 ? ? -140.17 19.77   
5  1 LEU A 176 ? ? 70.08   31.72   
6  1 THR A 181 ? ? -106.44 -166.64 
7  1 ALA C 14  ? ? 84.02   -43.33  
8  1 ASN C 61  ? ? 73.44   74.27   
9  1 THR C 181 ? ? -96.94  -158.20 
10 1 ASN D 24  ? ? -153.94 80.11   
11 1 ALA E 14  ? ? 78.09   -29.75  
12 1 ASN E 61  ? ? 80.06   69.69   
13 1 LYS E 87  ? ? -64.51  94.98   
14 1 SER E 140 ? ? -140.66 19.42   
15 1 PRO E 159 ? ? -69.22  3.92    
16 1 THR E 181 ? ? -104.71 -159.70 
17 1 ALA G 14  ? ? 87.42   -46.63  
18 1 GLN G 60  ? ? -64.00  -82.02  
19 1 THR G 181 ? ? -99.66  -159.44 
20 1 PRO G 240 ? ? -58.48  170.19  
21 1 ASN H 24  ? ? -154.36 81.77   
22 1 ASP H 56  ? ? -109.84 58.02   
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 B IML 63 B IML 65 ? ILE 'modified residue' 
2 F IML 63 F IML 65 ? ILE 'modified residue' 
3 H IML 63 H IML 65 ? ILE 'modified residue' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 14.551 -16.012 -3.071 0.0588 0.0448 0.0398 -0.0254 0.0463 -0.0292 0.2946 0.2366 0.3812 -0.0359 
0.1502  -0.0968 0.0100  0.0049  -0.0149 0.0211  0.0097  -0.0314 -0.0268 -0.0551 -0.0383 
'X-RAY DIFFRACTION' 2 ? refined 0.940  -9.938  14.518 0.0810 0.0425 0.0535 -0.0300 0.0566 -0.0382 1.9985 0.2046 1.0443 -0.5100 
-0.6265 0.4105  0.0983  -0.0180 -0.0803 -0.0308 0.1528  -0.0441 -0.0668 -0.1852 -0.0603 
'X-RAY DIFFRACTION' 3 ? refined 11.611 -35.227 -3.062 0.0652 0.0517 0.0429 -0.0332 0.0329 -0.0444 0.1542 0.2984 0.3215 -0.0743 
-0.0138 0.0213  0.0338  -0.0332 -0.0006 0.0272  -0.0368 0.0207  -0.0316 0.0394  0.0351  
'X-RAY DIFFRACTION' 4 ? refined 25.053 -41.354 14.510 0.1050 0.0480 0.0530 -0.0458 0.0279 -0.0371 1.3307 0.0487 0.7196 -0.1886 
0.7535  -0.0667 0.1237  -0.0028 -0.1209 0.0609  -0.0960 0.0015  0.0027  0.1047  0.0184  
'X-RAY DIFFRACTION' 5 ? refined 37.054 -23.142 51.207 0.0605 0.0302 0.0332 -0.0416 0.0433 -0.0313 0.2361 0.2439 0.3260 0.0078  
0.1579  0.0682  -0.0015 0.0086  -0.0071 -0.0006 0.0109  -0.0039 -0.0313 -0.0349 0.0071  
'X-RAY DIFFRACTION' 6 ? refined 23.321 -17.158 68.917 0.0606 0.0449 0.0713 -0.0461 0.0510 -0.0409 2.3120 0.2723 0.8080 -0.5638 
-0.9282 0.2650  0.0996  0.0179  -0.1176 -0.0757 0.1378  0.0090  -0.0418 -0.0950 0.0138  
'X-RAY DIFFRACTION' 7 ? refined 34.126 -42.372 51.217 0.0509 0.0444 0.0480 -0.0388 0.0430 -0.0277 0.2538 0.3179 0.3595 -0.0789 
-0.1553 0.0724  -0.0048 -0.0321 0.0369  -0.0210 -0.0569 -0.0055 -0.0250 0.0189  0.0004  
'X-RAY DIFFRACTION' 8 ? refined 47.470 -48.617 68.696 0.0947 0.1132 0.0756 -0.0416 0.0410 -0.0186 1.7880 0.1624 1.7645 -0.1433 
1.2526  0.1897  0.1095  0.0925  -0.2020 -0.0893 -0.2273 -0.0212 -0.0110 0.1648  -0.0477 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1 A 2   A 263 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  1 A 301 A 301 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  2 B 10  B 70  ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  3 C 2   C 263 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  3 C 301 C 301 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  4 D 11  D 70  ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  5 E 2   E 263 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  5 E 301 E 301 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  6 F 10  F 70  ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 7 G 2   G 263 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 7 G 301 G 301 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 8 H 11  H 70  ? ? ? ? ? ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       475 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.13 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B SER 57 ? B SER 55 
2  1 Y 1 B SER 58 ? B SER 56 
3  1 Y 1 B TYR 59 ? B TYR 57 
4  1 Y 1 B GLN 60 ? B GLN 58 
5  1 Y 1 B SER 61 ? B SER 59 
6  1 Y 1 D GLY 3  ? D GLY 1  
7  1 Y 1 D SER 58 ? D SER 56 
8  1 Y 1 D TYR 59 ? D TYR 57 
9  1 Y 1 D GLN 60 ? D GLN 58 
10 1 Y 1 D SER 61 ? D SER 59 
11 1 Y 1 F SER 57 ? F SER 55 
12 1 Y 1 F SER 58 ? F SER 56 
13 1 Y 1 F TYR 59 ? F TYR 57 
14 1 Y 1 F GLN 60 ? F GLN 58 
15 1 Y 1 F SER 61 ? F SER 59 
16 1 Y 1 F ALA 62 ? F ALA 60 
17 1 Y 1 H GLY 3  ? H GLY 1  
18 1 Y 1 H TYR 59 ? H TYR 57 
19 1 Y 1 H GLN 60 ? H GLN 58 
20 1 Y 1 H SER 61 ? H SER 59 
# 
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 
IML N      N N N 183 
IML CA     C N S 184 
IML C      C N N 185 
IML O      O N N 186 
IML OXT    O N N 187 
IML CB     C N S 188 
IML CN     C N N 189 
IML CG2    C N N 190 
IML CG1    C N N 191 
IML CD1    C N N 192 
IML H      H N N 193 
IML HA     H N N 194 
IML HXT    H N N 195 
IML HB     H N N 196 
IML HN1    H N N 197 
IML HN2    H N N 198 
IML HN3    H N N 199 
IML HG21   H N N 200 
IML HG22   H N N 201 
IML HG23   H N N 202 
IML HG12   H N N 203 
IML HG13   H N N 204 
IML HD11   H N N 205 
IML HD12   H N N 206 
IML HD13   H N N 207 
LEU N      N N N 208 
LEU CA     C N S 209 
LEU C      C N N 210 
LEU O      O N N 211 
LEU CB     C N N 212 
LEU CG     C N N 213 
LEU CD1    C N N 214 
LEU CD2    C N N 215 
LEU OXT    O N N 216 
LEU H      H N N 217 
LEU H2     H N N 218 
LEU HA     H N N 219 
LEU HB2    H N N 220 
LEU HB3    H N N 221 
LEU HG     H N N 222 
LEU HD11   H N N 223 
LEU HD12   H N N 224 
LEU HD13   H N N 225 
LEU HD21   H N N 226 
LEU HD22   H N N 227 
LEU HD23   H N N 228 
LEU HXT    H N N 229 
LYS N      N N N 230 
LYS CA     C N S 231 
LYS C      C N N 232 
LYS O      O N N 233 
LYS CB     C N N 234 
LYS CG     C N N 235 
LYS CD     C N N 236 
LYS CE     C N N 237 
LYS NZ     N N N 238 
LYS OXT    O N N 239 
LYS H      H N N 240 
LYS H2     H N N 241 
LYS HA     H N N 242 
LYS HB2    H N N 243 
LYS HB3    H N N 244 
LYS HG2    H N N 245 
LYS HG3    H N N 246 
LYS HD2    H N N 247 
LYS HD3    H N N 248 
LYS HE2    H N N 249 
LYS HE3    H N N 250 
LYS HZ1    H N N 251 
LYS HZ2    H N N 252 
LYS HZ3    H N N 253 
LYS HXT    H N N 254 
MET N      N N N 255 
MET CA     C N S 256 
MET C      C N N 257 
MET O      O N N 258 
MET CB     C N N 259 
MET CG     C N N 260 
MET SD     S N N 261 
MET CE     C N N 262 
MET OXT    O N N 263 
MET H      H N N 264 
MET H2     H N N 265 
MET HA     H N N 266 
MET HB2    H N N 267 
MET HB3    H N N 268 
MET HG2    H N N 269 
MET HG3    H N N 270 
MET HE1    H N N 271 
MET HE2    H N N 272 
MET HE3    H N N 273 
MET 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 
# 
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 
IML N     CA     sing N N 173 
IML N     CN     sing N N 174 
IML N     H      sing N N 175 
IML CA    C      sing N N 176 
IML CA    CB     sing N N 177 
IML CA    HA     sing N N 178 
IML C     O      doub N N 179 
IML C     OXT    sing N N 180 
IML OXT   HXT    sing N N 181 
IML CB    CG2    sing N N 182 
IML CB    CG1    sing N N 183 
IML CB    HB     sing N N 184 
IML CN    HN1    sing N N 185 
IML CN    HN2    sing N N 186 
IML CN    HN3    sing N N 187 
IML CG2   HG21   sing N N 188 
IML CG2   HG22   sing N N 189 
IML CG2   HG23   sing N N 190 
IML CG1   CD1    sing N N 191 
IML CG1   HG12   sing N N 192 
IML CG1   HG13   sing N N 193 
IML CD1   HD11   sing N N 194 
IML CD1   HD12   sing N N 195 
IML CD1   HD13   sing N N 196 
LEU N     CA     sing N N 197 
LEU N     H      sing N N 198 
LEU N     H2     sing N N 199 
LEU CA    C      sing N N 200 
LEU CA    CB     sing N N 201 
LEU CA    HA     sing N N 202 
LEU C     O      doub N N 203 
LEU C     OXT    sing N N 204 
LEU CB    CG     sing N N 205 
LEU CB    HB2    sing N N 206 
LEU CB    HB3    sing N N 207 
LEU CG    CD1    sing N N 208 
LEU CG    CD2    sing N N 209 
LEU CG    HG     sing N N 210 
LEU CD1   HD11   sing N N 211 
LEU CD1   HD12   sing N N 212 
LEU CD1   HD13   sing N N 213 
LEU CD2   HD21   sing N N 214 
LEU CD2   HD22   sing N N 215 
LEU CD2   HD23   sing N N 216 
LEU OXT   HXT    sing N N 217 
LYS N     CA     sing N N 218 
LYS N     H      sing N N 219 
LYS N     H2     sing N N 220 
LYS CA    C      sing N N 221 
LYS CA    CB     sing N N 222 
LYS CA    HA     sing N N 223 
LYS C     O      doub N N 224 
LYS C     OXT    sing N N 225 
LYS CB    CG     sing N N 226 
LYS CB    HB2    sing N N 227 
LYS CB    HB3    sing N N 228 
LYS CG    CD     sing N N 229 
LYS CG    HG2    sing N N 230 
LYS CG    HG3    sing N N 231 
LYS CD    CE     sing N N 232 
LYS CD    HD2    sing N N 233 
LYS CD    HD3    sing N N 234 
LYS CE    NZ     sing N N 235 
LYS CE    HE2    sing N N 236 
LYS CE    HE3    sing N N 237 
LYS NZ    HZ1    sing N N 238 
LYS NZ    HZ2    sing N N 239 
LYS NZ    HZ3    sing N N 240 
LYS OXT   HXT    sing N N 241 
MET N     CA     sing N N 242 
MET N     H      sing N N 243 
MET N     H2     sing N N 244 
MET CA    C      sing N N 245 
MET CA    CB     sing N N 246 
MET CA    HA     sing N N 247 
MET C     O      doub N N 248 
MET C     OXT    sing N N 249 
MET CB    CG     sing N N 250 
MET CB    HB2    sing N N 251 
MET CB    HB3    sing N N 252 
MET CG    SD     sing N N 253 
MET CG    HG2    sing N N 254 
MET CG    HG3    sing N N 255 
MET SD    CE     sing N N 256 
MET CE    HE1    sing N N 257 
MET CE    HE2    sing N N 258 
MET CE    HE3    sing N N 259 
MET 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                    9CHI 
_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]   0.019212 
_atom_sites.fract_transf_matrix[1][2]   -0.001354 
_atom_sites.fract_transf_matrix[1][3]   0.000038 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016974 
_atom_sites.fract_transf_matrix[2][3]   -0.000018 
_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]   0.009210 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N     . GLY A 1 1   ? 38.385  -19.152 14.922  1.00 36.49  ? 2   GLY A N     1 
ATOM   2     C CA    . GLY A 1 1   ? 37.118  -18.602 14.402  1.00 38.07  ? 2   GLY A CA    1 
ATOM   3     C C     . GLY A 1 1   ? 36.498  -19.532 13.364  1.00 38.77  ? 2   GLY A C     1 
ATOM   4     O O     . GLY A 1 1   ? 37.207  -20.266 12.678  1.00 40.69  ? 2   GLY A O     1 
ATOM   5     N N     . SER A 1 2   ? 35.165  -19.490 13.263  1.00 35.05  ? 3   SER A N     1 
ATOM   6     C CA    . SER A 1 2   ? 34.434  -20.329 12.329  1.00 33.24  ? 3   SER A CA    1 
ATOM   7     C C     . SER A 1 2   ? 33.181  -19.599 11.856  1.00 32.24  ? 3   SER A C     1 
ATOM   8     O O     . SER A 1 2   ? 32.796  -18.582 12.428  1.00 32.08  ? 3   SER A O     1 
ATOM   9     C CB    . SER A 1 2   ? 34.091  -21.661 12.946  1.00 35.26  ? 3   SER A CB    1 
ATOM   10    O OG    . SER A 1 2   ? 33.219  -21.500 14.057  1.00 34.71  ? 3   SER A OG    1 
ATOM   11    N N     . LEU A 1 3   ? 32.552  -20.136 10.807  1.00 33.11  ? 4   LEU A N     1 
ATOM   12    C CA    . LEU A 1 3   ? 31.371  -19.522 10.226  1.00 31.68  ? 4   LEU A CA    1 
ATOM   13    C C     . LEU A 1 3   ? 30.292  -20.579 10.022  1.00 30.83  ? 4   LEU A C     1 
ATOM   14    O O     . LEU A 1 3   ? 30.538  -21.618 9.415   1.00 31.72  ? 4   LEU A O     1 
ATOM   15    C CB    . LEU A 1 3   ? 31.734  -18.839 8.909   1.00 33.79  ? 4   LEU A CB    1 
ATOM   16    C CG    . LEU A 1 3   ? 30.565  -18.220 8.134   1.00 36.19  ? 4   LEU A CG    1 
ATOM   17    C CD1   . LEU A 1 3   ? 29.941  -17.076 8.914   1.00 36.33  ? 4   LEU A CD1   1 
ATOM   18    C CD2   . LEU A 1 3   ? 31.008  -17.755 6.758   1.00 34.59  ? 4   LEU A CD2   1 
ATOM   19    N N     . VAL A 1 4   ? 29.096  -20.291 10.544  1.00 31.95  ? 5   VAL A N     1 
ATOM   20    C CA    . VAL A 1 4   ? 27.920  -21.101 10.284  1.00 31.20  ? 5   VAL A CA    1 
ATOM   21    C C     . VAL A 1 4   ? 26.818  -20.180 9.771   1.00 31.12  ? 5   VAL A C     1 
ATOM   22    O O     . VAL A 1 4   ? 26.434  -19.230 10.449  1.00 33.48  ? 5   VAL A O     1 
ATOM   23    C CB    . VAL A 1 4   ? 27.454  -21.881 11.529  1.00 35.45  ? 5   VAL A CB    1 
ATOM   24    C CG1   . VAL A 1 4   ? 26.125  -22.586 11.289  1.00 37.24  ? 5   VAL A CG1   1 
ATOM   25    C CG2   . VAL A 1 4   ? 28.509  -22.872 12.007  1.00 36.99  ? 5   VAL A CG2   1 
ATOM   26    N N     . CYS A 1 5   ? 26.335  -20.463 8.558   1.00 29.55  ? 6   CYS A N     1 
ATOM   27    C CA    . CYS A 1 5   ? 25.254  -19.698 7.960   1.00 29.79  ? 6   CYS A CA    1 
ATOM   28    C C     . CYS A 1 5   ? 23.948  -20.470 8.113   1.00 28.12  ? 6   CYS A C     1 
ATOM   29    O O     . CYS A 1 5   ? 23.865  -21.638 7.739   1.00 25.74  ? 6   CYS A O     1 
ATOM   30    C CB    . CYS A 1 5   ? 25.540  -19.401 6.492   1.00 33.64  ? 6   CYS A CB    1 
ATOM   31    S SG    . CYS A 1 5   ? 27.004  -18.363 6.238   1.00 43.60  ? 6   CYS A SG    1 
ATOM   32    N N     . VAL A 1 6   ? 22.931  -19.801 8.668   1.00 28.33  ? 7   VAL A N     1 
ATOM   33    C CA    . VAL A 1 6   ? 21.660  -20.446 8.951   1.00 27.87  ? 7   VAL A CA    1 
ATOM   34    C C     . VAL A 1 6   ? 20.528  -19.612 8.359   1.00 28.12  ? 7   VAL A C     1 
ATOM   35    O O     . VAL A 1 6   ? 20.704  -18.434 8.053   1.00 24.47  ? 7   VAL A O     1 
ATOM   36    C CB    . VAL A 1 6   ? 21.459  -20.653 10.465  1.00 30.90  ? 7   VAL A CB    1 
ATOM   37    C CG1   . VAL A 1 6   ? 22.587  -21.474 11.079  1.00 30.59  ? 7   VAL A CG1   1 
ATOM   38    C CG2   . VAL A 1 6   ? 21.295  -19.327 11.202  1.00 27.62  ? 7   VAL A CG2   1 
ATOM   39    N N     . GLY A 1 7   ? 19.365  -20.252 8.205   1.00 28.02  ? 8   GLY A N     1 
ATOM   40    C CA    . GLY A 1 7   ? 18.155  -19.572 7.776   1.00 28.43  ? 8   GLY A CA    1 
ATOM   41    C C     . GLY A 1 7   ? 17.124  -19.540 8.901   1.00 25.55  ? 8   GLY A C     1 
ATOM   42    O O     . GLY A 1 7   ? 17.038  -20.472 9.696   1.00 27.80  ? 8   GLY A O     1 
ATOM   43    N N     . THR A 1 8   ? 16.350  -18.453 8.960   1.00 25.07  ? 9   THR A N     1 
ATOM   44    C CA    . THR A 1 8   ? 15.352  -18.287 10.002  1.00 27.99  ? 9   THR A CA    1 
ATOM   45    C C     . THR A 1 8   ? 13.971  -18.576 9.423   1.00 26.72  ? 9   THR A C     1 
ATOM   46    O O     . THR A 1 8   ? 13.002  -18.721 10.163  1.00 29.29  ? 9   THR A O     1 
ATOM   47    C CB    . THR A 1 8   ? 15.445  -16.874 10.578  1.00 27.66  ? 9   THR A CB    1 
ATOM   48    O OG1   . THR A 1 8   ? 15.176  -15.996 9.491   1.00 30.51  ? 9   THR A OG1   1 
ATOM   49    C CG2   . THR A 1 8   ? 16.813  -16.576 11.166  1.00 29.17  ? 9   THR A CG2   1 
ATOM   50    N N     . GLY A 1 9   ? 13.900  -18.672 8.091   1.00 29.96  ? 10  GLY A N     1 
ATOM   51    C CA    . GLY A 1 9   ? 12.634  -18.851 7.401   1.00 26.44  ? 10  GLY A CA    1 
ATOM   52    C C     . GLY A 1 9   ? 11.978  -17.504 7.113   1.00 30.11  ? 10  GLY A C     1 
ATOM   53    O O     . GLY A 1 9   ? 12.647  -16.473 7.124   1.00 32.39  ? 10  GLY A O     1 
ATOM   54    N N     . LEU A 1 10  ? 10.664  -17.525 6.865   1.00 26.74  ? 11  LEU A N     1 
ATOM   55    C CA    . LEU A 1 10  ? 9.925   -16.315 6.544   1.00 27.77  ? 11  LEU A CA    1 
ATOM   56    C C     . LEU A 1 10  ? 9.055   -15.904 7.729   1.00 27.25  ? 11  LEU A C     1 
ATOM   57    O O     . LEU A 1 10  ? 8.861   -14.716 7.972   1.00 28.57  ? 11  LEU A O     1 
ATOM   58    C CB    . LEU A 1 10  ? 9.093   -16.528 5.280   1.00 29.02  ? 11  LEU A CB    1 
ATOM   59    C CG    . LEU A 1 10  ? 9.861   -16.445 3.958   1.00 32.79  ? 11  LEU A CG    1 
ATOM   60    C CD1   . LEU A 1 10  ? 8.965   -16.786 2.782   1.00 33.73  ? 11  LEU A CD1   1 
ATOM   61    C CD2   . LEU A 1 10  ? 10.471  -15.063 3.782   1.00 33.59  ? 11  LEU A CD2   1 
ATOM   62    N N     . GLN A 1 11  ? 8.530   -16.895 8.457   1.00 31.28  ? 12  GLN A N     1 
ATOM   63    C CA    . GLN A 1 11  ? 7.693   -16.627 9.615   1.00 35.74  ? 12  GLN A CA    1 
ATOM   64    C C     . GLN A 1 11  ? 8.576   -16.272 10.809  1.00 37.00  ? 12  GLN A C     1 
ATOM   65    O O     . GLN A 1 11  ? 9.732   -16.679 10.881  1.00 41.22  ? 12  GLN A O     1 
ATOM   66    C CB    . GLN A 1 11  ? 6.778   -17.811 9.931   1.00 35.93  ? 12  GLN A CB    1 
ATOM   67    C CG    . GLN A 1 11  ? 5.499   -17.844 9.100   1.00 38.04  ? 12  GLN A CG    1 
ATOM   68    C CD    . GLN A 1 11  ? 4.583   -16.671 9.377   1.00 42.71  ? 12  GLN A CD    1 
ATOM   69    O OE1   . GLN A 1 11  ? 4.922   -15.749 10.129  1.00 43.42  ? 12  GLN A OE1   1 
ATOM   70    N NE2   . GLN A 1 11  ? 3.407   -16.692 8.768   1.00 43.11  ? 12  GLN A NE2   1 
ATOM   71    N N     . LEU A 1 12  ? 8.000   -15.507 11.741  1.00 39.18  ? 13  LEU A N     1 
ATOM   72    C CA    . LEU A 1 12  ? 8.718   -15.011 12.902  1.00 34.46  ? 13  LEU A CA    1 
ATOM   73    C C     . LEU A 1 12  ? 8.887   -16.125 13.931  1.00 30.58  ? 13  LEU A C     1 
ATOM   74    O O     . LEU A 1 12  ? 7.906   -16.683 14.416  1.00 28.17  ? 13  LEU A O     1 
ATOM   75    C CB    . LEU A 1 12  ? 7.941   -13.829 13.481  1.00 35.68  ? 13  LEU A CB    1 
ATOM   76    C CG    . LEU A 1 12  ? 8.440   -13.281 14.822  1.00 34.02  ? 13  LEU A CG    1 
ATOM   77    C CD1   . LEU A 1 12  ? 9.767   -12.558 14.671  1.00 35.57  ? 13  LEU A CD1   1 
ATOM   78    C CD2   . LEU A 1 12  ? 7.398   -12.368 15.445  1.00 33.69  ? 13  LEU A CD2   1 
ATOM   79    N N     . ALA A 1 13  ? 10.149  -16.457 14.228  1.00 28.65  ? 14  ALA A N     1 
ATOM   80    C CA    . ALA A 1 13  ? 10.501  -17.203 15.426  1.00 28.97  ? 14  ALA A CA    1 
ATOM   81    C C     . ALA A 1 13  ? 10.261  -18.702 15.252  1.00 32.06  ? 14  ALA A C     1 
ATOM   82    O O     . ALA A 1 13  ? 11.021  -19.512 15.779  1.00 34.00  ? 14  ALA A O     1 
ATOM   83    C CB    . ALA A 1 13  ? 9.720   -16.661 16.604  1.00 31.58  ? 14  ALA A CB    1 
ATOM   84    N N     . GLY A 1 14  ? 9.199   -19.066 14.526  1.00 30.87  ? 15  GLY A N     1 
ATOM   85    C CA    . GLY A 1 14  ? 8.694   -20.430 14.559  1.00 31.00  ? 15  GLY A CA    1 
ATOM   86    C C     . GLY A 1 14  ? 9.161   -21.269 13.371  1.00 31.26  ? 15  GLY A C     1 
ATOM   87    O O     . GLY A 1 14  ? 9.007   -22.488 13.382  1.00 32.80  ? 15  GLY A O     1 
ATOM   88    N N     . GLN A 1 15  ? 9.731   -20.616 12.353  1.00 30.10  ? 16  GLN A N     1 
ATOM   89    C CA    . GLN A 1 15  ? 10.008  -21.288 11.094  1.00 30.08  ? 16  GLN A CA    1 
ATOM   90    C C     . GLN A 1 15  ? 11.508  -21.537 10.940  1.00 30.79  ? 16  GLN A C     1 
ATOM   91    O O     . GLN A 1 15  ? 11.964  -21.937 9.871   1.00 29.35  ? 16  GLN A O     1 
ATOM   92    C CB    . GLN A 1 15  ? 9.438   -20.476 9.930   1.00 29.41  ? 16  GLN A CB    1 
ATOM   93    C CG    . GLN A 1 15  ? 9.267   -21.279 8.644   1.00 31.04  ? 16  GLN A CG    1 
ATOM   94    C CD    . GLN A 1 15  ? 8.441   -20.563 7.598   1.00 30.62  ? 16  GLN A CD    1 
ATOM   95    O OE1   . GLN A 1 15  ? 8.839   -19.523 7.060   1.00 27.07  ? 16  GLN A OE1   1 
ATOM   96    N NE2   . GLN A 1 15  ? 7.281   -21.124 7.289   1.00 32.71  ? 16  GLN A NE2   1 
ATOM   97    N N     . ILE A 1 16  ? 12.268  -21.314 12.018  1.00 29.36  ? 17  ILE A N     1 
ATOM   98    C CA    . ILE A 1 16  ? 13.683  -21.649 12.037  1.00 26.70  ? 17  ILE A CA    1 
ATOM   99    C C     . ILE A 1 16  ? 13.832  -23.073 12.563  1.00 25.93  ? 17  ILE A C     1 
ATOM   100   O O     . ILE A 1 16  ? 13.043  -23.515 13.395  1.00 26.80  ? 17  ILE A O     1 
ATOM   101   C CB    . ILE A 1 16  ? 14.484  -20.646 12.887  1.00 30.92  ? 17  ILE A CB    1 
ATOM   102   C CG1   . ILE A 1 16  ? 15.992  -20.870 12.749  1.00 30.40  ? 17  ILE A CG1   1 
ATOM   103   C CG2   . ILE A 1 16  ? 14.039  -20.688 14.350  1.00 30.18  ? 17  ILE A CG2   1 
ATOM   104   C CD1   . ILE A 1 16  ? 16.841  -19.854 13.492  1.00 33.53  ? 17  ILE A CD1   1 
ATOM   105   N N     A SER A 1 17  ? 14.853  -23.780 12.066  0.50 25.30  ? 18  SER A N     1 
ATOM   106   N N     B SER A 1 17  ? 14.852  -23.785 12.069  0.50 22.87  ? 18  SER A N     1 
ATOM   107   C CA    A SER A 1 17  ? 15.143  -25.130 12.516  0.50 27.16  ? 18  SER A CA    1 
ATOM   108   C CA    B SER A 1 17  ? 15.119  -25.141 12.517  0.50 22.75  ? 18  SER A CA    1 
ATOM   109   C C     A SER A 1 17  ? 15.595  -25.095 13.972  0.50 26.08  ? 18  SER A C     1 
ATOM   110   C C     B SER A 1 17  ? 15.611  -25.107 13.961  0.50 23.80  ? 18  SER A C     1 
ATOM   111   O O     A SER A 1 17  ? 16.115  -24.085 14.440  0.50 28.58  ? 18  SER A O     1 
ATOM   112   O O     B SER A 1 17  ? 16.174  -24.110 14.407  0.50 26.29  ? 18  SER A O     1 
ATOM   113   C CB    A SER A 1 17  ? 16.178  -25.785 11.637  0.50 29.70  ? 18  SER A CB    1 
ATOM   114   C CB    B SER A 1 17  ? 16.106  -25.843 11.614  0.50 21.94  ? 18  SER A CB    1 
ATOM   115   O OG    A SER A 1 17  ? 15.744  -25.830 10.285  0.50 33.80  ? 18  SER A OG    1 
ATOM   116   O OG    B SER A 1 17  ? 17.416  -25.315 11.765  0.50 19.81  ? 18  SER A OG    1 
ATOM   117   N N     . VAL A 1 18  ? 15.386  -26.210 14.681  1.00 25.22  ? 19  VAL A N     1 
ATOM   118   C CA    . VAL A 1 18  ? 15.758  -26.308 16.081  1.00 24.79  ? 19  VAL A CA    1 
ATOM   119   C C     . VAL A 1 18  ? 17.269  -26.126 16.209  1.00 25.59  ? 19  VAL A C     1 
ATOM   120   O O     . VAL A 1 18  ? 17.736  -25.384 17.070  1.00 26.95  ? 19  VAL A O     1 
ATOM   121   C CB    . VAL A 1 18  ? 15.297  -27.647 16.689  1.00 26.21  ? 19  VAL A CB    1 
ATOM   122   C CG1   . VAL A 1 18  ? 15.801  -27.827 18.116  1.00 27.13  ? 19  VAL A CG1   1 
ATOM   123   C CG2   . VAL A 1 18  ? 13.781  -27.800 16.632  1.00 26.53  ? 19  VAL A CG2   1 
ATOM   124   N N     . LEU A 1 19  ? 18.025  -26.804 15.337  1.00 27.42  ? 20  LEU A N     1 
ATOM   125   C CA    . LEU A 1 19  ? 19.477  -26.771 15.394  1.00 26.58  ? 20  LEU A CA    1 
ATOM   126   C C     . LEU A 1 19  ? 19.975  -25.375 15.025  1.00 25.53  ? 20  LEU A C     1 
ATOM   127   O O     . LEU A 1 19  ? 20.923  -24.873 15.626  1.00 25.72  ? 20  LEU A O     1 
ATOM   128   C CB    . LEU A 1 19  ? 20.072  -27.832 14.470  1.00 30.63  ? 20  LEU A CB    1 
ATOM   129   C CG    . LEU A 1 19  ? 21.602  -27.868 14.399  1.00 34.36  ? 20  LEU A CG    1 
ATOM   130   C CD1   . LEU A 1 19  ? 22.198  -28.265 15.739  1.00 37.86  ? 20  LEU A CD1   1 
ATOM   131   C CD2   . LEU A 1 19  ? 22.081  -28.800 13.299  1.00 34.89  ? 20  LEU A CD2   1 
ATOM   132   N N     . SER A 1 20  ? 19.332  -24.763 14.025  1.00 22.73  ? 21  SER A N     1 
ATOM   133   C CA    . SER A 1 20  ? 19.746  -23.461 13.527  1.00 26.15  ? 21  SER A CA    1 
ATOM   134   C C     . SER A 1 20  ? 19.517  -22.396 14.596  1.00 26.13  ? 21  SER A C     1 
ATOM   135   O O     . SER A 1 20  ? 20.272  -21.431 14.688  1.00 29.63  ? 21  SER A O     1 
ATOM   136   C CB    . SER A 1 20  ? 19.033  -23.117 12.245  1.00 24.22  ? 21  SER A CB    1 
ATOM   137   O OG    . SER A 1 20  ? 19.394  -24.017 11.207  1.00 24.54  ? 21  SER A OG    1 
ATOM   138   N N     . ARG A 1 21  ? 18.462  -22.585 15.395  1.00 29.55  ? 22  ARG A N     1 
ATOM   139   C CA    . ARG A 1 21  ? 18.158  -21.688 16.497  1.00 30.07  ? 22  ARG A CA    1 
ATOM   140   C C     . ARG A 1 21  ? 19.248  -21.813 17.556  1.00 28.29  ? 22  ARG A C     1 
ATOM   141   O O     . ARG A 1 21  ? 19.666  -20.820 18.148  1.00 25.50  ? 22  ARG A O     1 
ATOM   142   C CB    . ARG A 1 21  ? 16.783  -22.023 17.088  1.00 33.74  ? 22  ARG A CB    1 
ATOM   143   C CG    . ARG A 1 21  ? 16.338  -21.099 18.214  1.00 33.96  ? 22  ARG A CG    1 
ATOM   144   C CD    . ARG A 1 21  ? 14.924  -21.413 18.682  1.00 35.96  ? 22  ARG A CD    1 
ATOM   145   N NE    . ARG A 1 21  ? 14.423  -20.443 19.663  1.00 36.78  ? 22  ARG A NE    1 
ATOM   146   C CZ    . ARG A 1 21  ? 14.873  -20.313 20.905  1.00 39.66  ? 22  ARG A CZ    1 
ATOM   147   N NH1   . ARG A 1 21  ? 15.817  -21.118 21.357  1.00 38.94  ? 22  ARG A NH1   1 
ATOM   148   N NH2   . ARG A 1 21  ? 14.362  -19.386 21.696  1.00 44.27  ? 22  ARG A NH2   1 
ATOM   149   N N     . SER A 1 22  ? 19.707  -23.050 17.772  1.00 28.97  ? 23  SER A N     1 
ATOM   150   C CA    . SER A 1 22  ? 20.701  -23.349 18.789  1.00 29.50  ? 23  SER A CA    1 
ATOM   151   C C     . SER A 1 22  ? 22.038  -22.701 18.435  1.00 29.00  ? 23  SER A C     1 
ATOM   152   O O     . SER A 1 22  ? 22.776  -22.279 19.322  1.00 30.54  ? 23  SER A O     1 
ATOM   153   C CB    . SER A 1 22  ? 20.850  -24.838 18.975  1.00 29.54  ? 23  SER A CB    1 
ATOM   154   O OG    . SER A 1 22  ? 21.801  -25.135 19.987  1.00 29.03  ? 23  SER A OG    1 
ATOM   155   N N     . TYR A 1 23  ? 22.347  -22.641 17.134  1.00 29.74  ? 24  TYR A N     1 
ATOM   156   C CA    . TYR A 1 23  ? 23.592  -22.046 16.671  1.00 26.72  ? 24  TYR A CA    1 
ATOM   157   C C     . TYR A 1 23  ? 23.609  -20.561 17.027  1.00 28.09  ? 24  TYR A C     1 
ATOM   158   O O     . TYR A 1 23  ? 24.626  -20.038 17.477  1.00 29.91  ? 24  TYR A O     1 
ATOM   159   C CB    . TYR A 1 23  ? 23.800  -22.239 15.165  1.00 24.54  ? 24  TYR A CB    1 
ATOM   160   C CG    . TYR A 1 23  ? 24.525  -23.522 14.781  1.00 25.98  ? 24  TYR A CG    1 
ATOM   161   C CD1   . TYR A 1 23  ? 25.893  -23.659 14.988  1.00 24.20  ? 24  TYR A CD1   1 
ATOM   162   C CD2   . TYR A 1 23  ? 23.854  -24.579 14.180  1.00 25.88  ? 24  TYR A CD2   1 
ATOM   163   C CE1   . TYR A 1 23  ? 26.564  -24.817 14.638  1.00 24.52  ? 24  TYR A CE1   1 
ATOM   164   C CE2   . TYR A 1 23  ? 24.515  -25.742 13.819  1.00 26.02  ? 24  TYR A CE2   1 
ATOM   165   C CZ    . TYR A 1 23  ? 25.874  -25.861 14.048  1.00 26.89  ? 24  TYR A CZ    1 
ATOM   166   O OH    . TYR A 1 23  ? 26.532  -27.003 13.695  1.00 28.56  ? 24  TYR A OH    1 
ATOM   167   N N     . ILE A 1 24  ? 22.475  -19.889 16.803  1.00 26.25  ? 25  ILE A N     1 
ATOM   168   C CA    . ILE A 1 24  ? 22.364  -18.464 17.069  1.00 29.31  ? 25  ILE A CA    1 
ATOM   169   C C     . ILE A 1 24  ? 22.574  -18.218 18.561  1.00 32.35  ? 25  ILE A C     1 
ATOM   170   O O     . ILE A 1 24  ? 23.268  -17.282 18.950  1.00 30.32  ? 25  ILE A O     1 
ATOM   171   C CB    . ILE A 1 24  ? 21.006  -17.920 16.588  1.00 28.02  ? 25  ILE A CB    1 
ATOM   172   C CG1   . ILE A 1 24  ? 20.886  -17.976 15.066  1.00 29.20  ? 25  ILE A CG1   1 
ATOM   173   C CG2   . ILE A 1 24  ? 20.766  -16.507 17.120  1.00 32.19  ? 25  ILE A CG2   1 
ATOM   174   C CD1   . ILE A 1 24  ? 19.577  -17.428 14.527  1.00 29.19  ? 25  ILE A CD1   1 
ATOM   175   N N     . GLU A 1 25  ? 21.973  -19.084 19.382  1.00 34.08  ? 26  GLU A N     1 
ATOM   176   C CA    . GLU A 1 25  ? 21.974  -18.918 20.825  1.00 38.74  ? 26  GLU A CA    1 
ATOM   177   C C     . GLU A 1 25  ? 23.406  -18.929 21.356  1.00 38.43  ? 26  GLU A C     1 
ATOM   178   O O     . GLU A 1 25  ? 23.765  -18.103 22.192  1.00 40.71  ? 26  GLU A O     1 
ATOM   179   C CB    . GLU A 1 25  ? 21.138  -20.023 21.473  1.00 44.70  ? 26  GLU A CB    1 
ATOM   180   C CG    . GLU A 1 25  ? 21.102  -19.946 22.996  1.00 53.65  ? 26  GLU A CG    1 
ATOM   181   C CD    . GLU A 1 25  ? 20.279  -21.042 23.652  1.00 61.39  ? 26  GLU A CD    1 
ATOM   182   O OE1   . GLU A 1 25  ? 19.693  -21.863 22.915  1.00 62.47  ? 26  GLU A OE1   1 
ATOM   183   O OE2   . GLU A 1 25  ? 20.227  -21.076 24.899  1.00 63.71  ? 26  GLU A OE2   1 
ATOM   184   N N     . HIS A 1 26  ? 24.218  -19.869 20.860  1.00 36.31  ? 27  HIS A N     1 
ATOM   185   C CA    . HIS A 1 26  ? 25.548  -20.093 21.405  1.00 35.81  ? 27  HIS A CA    1 
ATOM   186   C C     . HIS A 1 26  ? 26.608  -19.404 20.548  1.00 34.75  ? 27  HIS A C     1 
ATOM   187   O O     . HIS A 1 26  ? 27.800  -19.636 20.736  1.00 35.77  ? 27  HIS A O     1 
ATOM   188   C CB    . HIS A 1 26  ? 25.840  -21.593 21.528  1.00 37.83  ? 27  HIS A CB    1 
ATOM   189   C CG    . HIS A 1 26  ? 24.980  -22.305 22.518  1.00 40.78  ? 27  HIS A CG    1 
ATOM   190   N ND1   . HIS A 1 26  ? 23.931  -23.121 22.154  1.00 44.37  ? 27  HIS A ND1   1 
ATOM   191   C CD2   . HIS A 1 26  ? 25.038  -22.353 23.856  1.00 45.38  ? 27  HIS A CD2   1 
ATOM   192   C CE1   . HIS A 1 26  ? 23.370  -23.624 23.244  1.00 47.19  ? 27  HIS A CE1   1 
ATOM   193   N NE2   . HIS A 1 26  ? 24.025  -23.169 24.289  1.00 48.25  ? 27  HIS A NE2   1 
ATOM   194   N N     . ALA A 1 27  ? 26.169  -18.554 19.614  1.00 34.74  ? 28  ALA A N     1 
ATOM   195   C CA    . ALA A 1 27  ? 27.086  -17.844 18.737  1.00 30.22  ? 28  ALA A CA    1 
ATOM   196   C C     . ALA A 1 27  ? 27.777  -16.721 19.506  1.00 34.41  ? 28  ALA A C     1 
ATOM   197   O O     . ALA A 1 27  ? 27.184  -16.119 20.399  1.00 39.24  ? 28  ALA A O     1 
ATOM   198   C CB    . ALA A 1 27  ? 26.343  -17.311 17.532  1.00 27.15  ? 28  ALA A CB    1 
ATOM   199   N N     . ASP A 1 28  ? 29.038  -16.453 19.146  1.00 32.68  ? 29  ASP A N     1 
ATOM   200   C CA    . ASP A 1 28  ? 29.796  -15.359 19.730  1.00 34.11  ? 29  ASP A CA    1 
ATOM   201   C C     . ASP A 1 28  ? 29.296  -14.040 19.151  1.00 31.98  ? 29  ASP A C     1 
ATOM   202   O O     . ASP A 1 28  ? 29.288  -13.018 19.834  1.00 30.62  ? 29  ASP A O     1 
ATOM   203   C CB    . ASP A 1 28  ? 31.290  -15.527 19.498  1.00 40.27  ? 29  ASP A CB    1 
ATOM   204   C CG    . ASP A 1 28  ? 31.957  -16.647 20.284  1.00 46.44  ? 29  ASP A CG    1 
ATOM   205   O OD1   . ASP A 1 28  ? 31.270  -17.262 21.126  1.00 48.78  ? 29  ASP A OD1   1 
ATOM   206   O OD2   . ASP A 1 28  ? 33.157  -16.896 20.045  1.00 54.62  ? 29  ASP A OD2   1 
ATOM   207   N N     . ILE A 1 29  ? 28.888  -14.080 17.879  1.00 30.99  ? 30  ILE A N     1 
ATOM   208   C CA    . ILE A 1 29  ? 28.394  -12.901 17.188  1.00 29.36  ? 30  ILE A CA    1 
ATOM   209   C C     . ILE A 1 29  ? 27.509  -13.353 16.030  1.00 28.60  ? 30  ILE A C     1 
ATOM   210   O O     . ILE A 1 29  ? 27.768  -14.383 15.412  1.00 29.53  ? 30  ILE A O     1 
ATOM   211   C CB    . ILE A 1 29  ? 29.559  -12.017 16.707  1.00 30.47  ? 30  ILE A CB    1 
ATOM   212   C CG1   . ILE A 1 29  ? 29.065  -10.664 16.197  1.00 31.69  ? 30  ILE A CG1   1 
ATOM   213   C CG2   . ILE A 1 29  ? 30.400  -12.744 15.657  1.00 30.77  ? 30  ILE A CG2   1 
ATOM   214   C CD1   . ILE A 1 29  ? 30.176  -9.689  15.851  1.00 33.42  ? 30  ILE A CD1   1 
ATOM   215   N N     . VAL A 1 30  ? 26.467  -12.565 15.746  1.00 28.24  ? 31  VAL A N     1 
ATOM   216   C CA    . VAL A 1 30  ? 25.493  -12.916 14.727  1.00 28.89  ? 31  VAL A CA    1 
ATOM   217   C C     . VAL A 1 30  ? 25.353  -11.757 13.743  1.00 31.42  ? 31  VAL A C     1 
ATOM   218   O O     . VAL A 1 30  ? 25.058  -10.632 14.138  1.00 38.37  ? 31  VAL A O     1 
ATOM   219   C CB    . VAL A 1 30  ? 24.133  -13.275 15.356  1.00 27.51  ? 31  VAL A CB    1 
ATOM   220   C CG1   . VAL A 1 30  ? 23.096  -13.632 14.297  1.00 25.64  ? 31  VAL A CG1   1 
ATOM   221   C CG2   . VAL A 1 30  ? 24.261  -14.395 16.382  1.00 28.05  ? 31  VAL A CG2   1 
ATOM   222   N N     . PHE A 1 31  ? 25.573  -12.054 12.458  1.00 28.71  ? 32  PHE A N     1 
ATOM   223   C CA    . PHE A 1 31  ? 25.319  -11.106 11.387  1.00 29.77  ? 32  PHE A CA    1 
ATOM   224   C C     . PHE A 1 31  ? 23.940  -11.403 10.806  1.00 28.62  ? 32  PHE A C     1 
ATOM   225   O O     . PHE A 1 31  ? 23.706  -12.488 10.277  1.00 31.32  ? 32  PHE A O     1 
ATOM   226   C CB    . PHE A 1 31  ? 26.433  -11.183 10.339  1.00 28.73  ? 32  PHE A CB    1 
ATOM   227   C CG    . PHE A 1 31  ? 27.773  -10.637 10.813  1.00 32.75  ? 32  PHE A CG    1 
ATOM   228   C CD1   . PHE A 1 31  ? 28.612  -11.402 11.617  1.00 34.33  ? 32  PHE A CD1   1 
ATOM   229   C CD2   . PHE A 1 31  ? 28.194  -9.363  10.448  1.00 33.14  ? 32  PHE A CD2   1 
ATOM   230   C CE1   . PHE A 1 31  ? 29.830  -10.900 12.048  1.00 35.20  ? 32  PHE A CE1   1 
ATOM   231   C CE2   . PHE A 1 31  ? 29.416  -8.870  10.880  1.00 32.02  ? 32  PHE A CE2   1 
ATOM   232   C CZ    . PHE A 1 31  ? 30.229  -9.638  11.678  1.00 32.18  ? 32  PHE A CZ    1 
ATOM   233   N N     . SER A 1 32  ? 23.039  -10.423 10.911  1.00 28.55  ? 33  SER A N     1 
ATOM   234   C CA    . SER A 1 32  ? 21.626  -10.651 10.661  1.00 29.93  ? 33  SER A CA    1 
ATOM   235   C C     . SER A 1 32  ? 21.156  -9.875  9.434   1.00 30.86  ? 33  SER A C     1 
ATOM   236   O O     . SER A 1 32  ? 21.618  -8.767  9.170   1.00 32.00  ? 33  SER A O     1 
ATOM   237   C CB    . SER A 1 32  ? 20.807  -10.287 11.872  1.00 30.36  ? 33  SER A CB    1 
ATOM   238   O OG    . SER A 1 32  ? 21.007  -8.927  12.233  1.00 29.97  ? 33  SER A OG    1 
ATOM   239   N N     . LEU A 1 33  ? 20.224  -10.486 8.696   1.00 31.55  ? 34  LEU A N     1 
ATOM   240   C CA    . LEU A 1 33  ? 19.484  -9.805  7.648   1.00 31.80  ? 34  LEU A CA    1 
ATOM   241   C C     . LEU A 1 33  ? 18.058  -10.351 7.649   1.00 30.32  ? 34  LEU A C     1 
ATOM   242   O O     . LEU A 1 33  ? 17.761  -11.324 6.960   1.00 33.15  ? 34  LEU A O     1 
ATOM   243   C CB    . LEU A 1 33  ? 20.169  -10.007 6.297   1.00 32.99  ? 34  LEU A CB    1 
ATOM   244   C CG    . LEU A 1 33  ? 19.820  -8.986  5.210   1.00 35.09  ? 34  LEU A CG    1 
ATOM   245   C CD1   . LEU A 1 33  ? 20.422  -9.393  3.876   1.00 36.21  ? 34  LEU A CD1   1 
ATOM   246   C CD2   . LEU A 1 33  ? 18.317  -8.793  5.085   1.00 36.81  ? 34  LEU A CD2   1 
ATOM   247   N N     . LEU A 1 34  ? 17.190  -9.724  8.452   1.00 31.42  ? 35  LEU A N     1 
ATOM   248   C CA    . LEU A 1 34  ? 15.855  -10.244 8.701   1.00 33.07  ? 35  LEU A CA    1 
ATOM   249   C C     . LEU A 1 34  ? 14.809  -9.333  8.064   1.00 35.49  ? 35  LEU A C     1 
ATOM   250   O O     . LEU A 1 34  ? 15.087  -8.177  7.754   1.00 37.64  ? 35  LEU A O     1 
ATOM   251   C CB    . LEU A 1 34  ? 15.636  -10.388 10.207  1.00 35.08  ? 35  LEU A CB    1 
ATOM   252   C CG    . LEU A 1 34  ? 16.398  -11.532 10.886  1.00 39.98  ? 35  LEU A CG    1 
ATOM   253   C CD1   . LEU A 1 34  ? 17.887  -11.446 10.606  1.00 44.43  ? 35  LEU A CD1   1 
ATOM   254   C CD2   . LEU A 1 34  ? 16.138  -11.543 12.382  1.00 41.20  ? 35  LEU A CD2   1 
ATOM   255   N N     . PRO A 1 35  ? 13.569  -9.834  7.860   1.00 38.13  ? 36  PRO A N     1 
ATOM   256   C CA    . PRO A 1 35  ? 12.535  -9.081  7.149   1.00 41.63  ? 36  PRO A CA    1 
ATOM   257   C C     . PRO A 1 35  ? 12.131  -7.777  7.836   1.00 46.47  ? 36  PRO A C     1 
ATOM   258   O O     . PRO A 1 35  ? 12.087  -6.728  7.198   1.00 44.89  ? 36  PRO A O     1 
ATOM   259   C CB    . PRO A 1 35  ? 11.354  -10.079 7.069   1.00 42.29  ? 36  PRO A CB    1 
ATOM   260   C CG    . PRO A 1 35  ? 11.986  -11.439 7.301   1.00 43.79  ? 36  PRO A CG    1 
ATOM   261   C CD    . PRO A 1 35  ? 13.118  -11.170 8.273   1.00 41.20  ? 36  PRO A CD    1 
ATOM   262   N N     . ASP A 1 36  ? 11.833  -7.856  9.138   1.00 46.65  ? 37  ASP A N     1 
ATOM   263   C CA    . ASP A 1 36  ? 11.241  -6.736  9.851   1.00 47.71  ? 37  ASP A CA    1 
ATOM   264   C C     . ASP A 1 36  ? 11.901  -6.567  11.217  1.00 42.63  ? 37  ASP A C     1 
ATOM   265   O O     . ASP A 1 36  ? 12.879  -7.242  11.533  1.00 41.78  ? 37  ASP A O     1 
ATOM   266   C CB    . ASP A 1 36  ? 9.736   -6.910  9.977   1.00 49.89  ? 37  ASP A CB    1 
ATOM   267   C CG    . ASP A 1 36  ? 9.283   -8.247  10.545  1.00 53.81  ? 37  ASP A CG    1 
ATOM   268   O OD1   . ASP A 1 36  ? 9.701   -8.575  11.676  1.00 53.92  ? 37  ASP A OD1   1 
ATOM   269   O OD2   . ASP A 1 36  ? 8.520   -8.950  9.849   1.00 56.40  ? 37  ASP A OD2   1 
ATOM   270   N N     . GLY A 1 37  ? 11.338  -5.653  12.017  1.00 43.33  ? 38  GLY A N     1 
ATOM   271   C CA    . GLY A 1 37  ? 11.871  -5.325  13.329  1.00 40.83  ? 38  GLY A CA    1 
ATOM   272   C C     . GLY A 1 37  ? 11.447  -6.346  14.381  1.00 37.72  ? 38  GLY A C     1 
ATOM   273   O O     . GLY A 1 37  ? 12.185  -6.606  15.329  1.00 41.34  ? 38  GLY A O     1 
ATOM   274   N N     . PHE A 1 38  ? 10.247  -6.912  14.209  1.00 33.54  ? 39  PHE A N     1 
ATOM   275   C CA    . PHE A 1 38  ? 9.763   -7.950  15.102  1.00 31.90  ? 39  PHE A CA    1 
ATOM   276   C C     . PHE A 1 38  ? 10.772  -9.093  15.103  1.00 31.29  ? 39  PHE A C     1 
ATOM   277   O O     . PHE A 1 38  ? 11.099  -9.641  16.153  1.00 30.40  ? 39  PHE A O     1 
ATOM   278   C CB    . PHE A 1 38  ? 8.370   -8.449  14.699  1.00 32.26  ? 39  PHE A CB    1 
ATOM   279   C CG    . PHE A 1 38  ? 7.248   -7.439  14.896  1.00 32.86  ? 39  PHE A CG    1 
ATOM   280   C CD1   . PHE A 1 38  ? 6.791   -7.122  16.171  1.00 33.12  ? 39  PHE A CD1   1 
ATOM   281   C CD2   . PHE A 1 38  ? 6.624   -6.840  13.807  1.00 32.53  ? 39  PHE A CD2   1 
ATOM   282   C CE1   . PHE A 1 38  ? 5.764   -6.209  16.350  1.00 35.14  ? 39  PHE A CE1   1 
ATOM   283   C CE2   . PHE A 1 38  ? 5.594   -5.931  13.992  1.00 33.78  ? 39  PHE A CE2   1 
ATOM   284   C CZ    . PHE A 1 38  ? 5.168   -5.617  15.262  1.00 35.05  ? 39  PHE A CZ    1 
ATOM   285   N N     . SER A 1 39  ? 11.268  -9.426  13.907  1.00 32.92  ? 40  SER A N     1 
ATOM   286   C CA    . SER A 1 39  ? 12.223  -10.507 13.737  1.00 35.14  ? 40  SER A CA    1 
ATOM   287   C C     . SER A 1 39  ? 13.574  -10.102 14.320  1.00 35.57  ? 40  SER A C     1 
ATOM   288   O O     . SER A 1 39  ? 14.299  -10.937 14.855  1.00 39.62  ? 40  SER A O     1 
ATOM   289   C CB    . SER A 1 39  ? 12.346  -10.893 12.285  1.00 35.13  ? 40  SER A CB    1 
ATOM   290   O OG    . SER A 1 39  ? 13.160  -12.047 12.131  1.00 39.94  ? 40  SER A OG    1 
ATOM   291   N N     . GLN A 1 40  ? 13.897  -8.809  14.215  1.00 37.59  ? 41  GLN A N     1 
ATOM   292   C CA    . GLN A 1 40  ? 15.171  -8.298  14.691  1.00 35.40  ? 41  GLN A CA    1 
ATOM   293   C C     . GLN A 1 40  ? 15.192  -8.348  16.216  1.00 30.93  ? 41  GLN A C     1 
ATOM   294   O O     . GLN A 1 40  ? 16.211  -8.684  16.816  1.00 28.81  ? 41  GLN A O     1 
ATOM   295   C CB    . GLN A 1 40  ? 15.417  -6.879  14.179  1.00 39.03  ? 41  GLN A CB    1 
ATOM   296   C CG    . GLN A 1 40  ? 16.872  -6.436  14.280  1.00 41.46  ? 41  GLN A CG    1 
ATOM   297   C CD    . GLN A 1 40  ? 17.811  -7.319  13.488  1.00 41.21  ? 41  GLN A CD    1 
ATOM   298   O OE1   . GLN A 1 40  ? 17.383  -8.214  12.750  1.00 47.91  ? 41  GLN A OE1   1 
ATOM   299   N NE2   . GLN A 1 40  ? 19.105  -7.074  13.629  1.00 39.03  ? 41  GLN A NE2   1 
ATOM   300   N N     . ARG A 1 41  ? 14.055  -8.009  16.832  1.00 31.96  ? 42  ARG A N     1 
ATOM   301   C CA    A ARG A 1 41  ? 13.911  -8.047  18.279  0.50 32.97  ? 42  ARG A CA    1 
ATOM   302   C CA    B ARG A 1 41  ? 13.930  -8.043  18.280  0.50 32.66  ? 42  ARG A CA    1 
ATOM   303   C C     . ARG A 1 41  ? 14.055  -9.485  18.765  1.00 31.07  ? 42  ARG A C     1 
ATOM   304   O O     . ARG A 1 41  ? 14.800  -9.761  19.704  1.00 30.47  ? 42  ARG A O     1 
ATOM   305   C CB    A ARG A 1 41  ? 12.545  -7.500  18.709  0.50 34.53  ? 42  ARG A CB    1 
ATOM   306   C CB    B ARG A 1 41  ? 12.627  -7.362  18.719  0.50 33.83  ? 42  ARG A CB    1 
ATOM   307   C CG    A ARG A 1 41  ? 12.312  -6.025  18.416  0.50 36.69  ? 42  ARG A CG    1 
ATOM   308   C CG    B ARG A 1 41  ? 12.786  -5.868  18.974  0.50 35.40  ? 42  ARG A CG    1 
ATOM   309   C CD    A ARG A 1 41  ? 13.279  -5.122  19.165  0.50 36.37  ? 42  ARG A CD    1 
ATOM   310   C CD    B ARG A 1 41  ? 11.461  -5.138  19.150  0.50 35.76  ? 42  ARG A CD    1 
ATOM   311   N NE    A ARG A 1 41  ? 12.849  -3.720  19.150  0.50 36.26  ? 42  ARG A NE    1 
ATOM   312   N NE    B ARG A 1 41  ? 10.866  -4.745  17.867  0.50 36.52  ? 42  ARG A NE    1 
ATOM   313   C CZ    A ARG A 1 41  ? 11.692  -3.291  18.659  0.50 38.80  ? 42  ARG A CZ    1 
ATOM   314   C CZ    B ARG A 1 41  ? 9.671   -5.123  17.435  0.50 35.57  ? 42  ARG A CZ    1 
ATOM   315   N NH1   A ARG A 1 41  ? 10.837  -4.150  18.134  0.50 37.63  ? 42  ARG A NH1   1 
ATOM   316   N NH1   B ARG A 1 41  ? 8.929   -5.932  18.168  0.50 36.47  ? 42  ARG A NH1   1 
ATOM   317   N NH2   A ARG A 1 41  ? 11.392  -2.005  18.699  0.50 39.57  ? 42  ARG A NH2   1 
ATOM   318   N NH2   B ARG A 1 41  ? 9.224   -4.696  16.267  0.50 34.84  ? 42  ARG A NH2   1 
ATOM   319   N N     . TRP A 1 42  ? 13.324  -10.397 18.114  1.00 31.22  ? 43  TRP A N     1 
ATOM   320   C CA    . TRP A 1 42  ? 13.371  -11.810 18.453  1.00 29.14  ? 43  TRP A CA    1 
ATOM   321   C C     . TRP A 1 42  ? 14.820  -12.286 18.515  1.00 28.25  ? 43  TRP A C     1 
ATOM   322   O O     . TRP A 1 42  ? 15.222  -12.947 19.470  1.00 28.32  ? 43  TRP A O     1 
ATOM   323   C CB    . TRP A 1 42  ? 12.565  -12.631 17.437  1.00 31.07  ? 43  TRP A CB    1 
ATOM   324   C CG    . TRP A 1 42  ? 12.898  -14.101 17.435  1.00 31.12  ? 43  TRP A CG    1 
ATOM   325   C CD1   . TRP A 1 42  ? 12.437  -15.050 18.300  1.00 32.21  ? 43  TRP A CD1   1 
ATOM   326   C CD2   . TRP A 1 42  ? 13.758  -14.793 16.503  1.00 31.48  ? 43  TRP A CD2   1 
ATOM   327   N NE1   . TRP A 1 42  ? 12.957  -16.277 17.982  1.00 29.68  ? 43  TRP A NE1   1 
ATOM   328   C CE2   . TRP A 1 42  ? 13.766  -16.153 16.884  1.00 30.62  ? 43  TRP A CE2   1 
ATOM   329   C CE3   . TRP A 1 42  ? 14.517  -14.401 15.394  1.00 30.81  ? 43  TRP A CE3   1 
ATOM   330   C CZ2   . TRP A 1 42  ? 14.502  -17.114 16.194  1.00 28.44  ? 43  TRP A CZ2   1 
ATOM   331   C CZ3   . TRP A 1 42  ? 15.242  -15.354 14.712  1.00 31.82  ? 43  TRP A CZ3   1 
ATOM   332   C CH2   . TRP A 1 42  ? 15.234  -16.691 15.109  1.00 31.43  ? 43  TRP A CH2   1 
ATOM   333   N N     . LEU A 1 43  ? 15.592  -11.943 17.479  1.00 28.92  ? 44  LEU A N     1 
ATOM   334   C CA    . LEU A 1 43  ? 16.967  -12.397 17.356  1.00 29.76  ? 44  LEU A CA    1 
ATOM   335   C C     . LEU A 1 43  ? 17.792  -11.866 18.525  1.00 27.03  ? 44  LEU A C     1 
ATOM   336   O O     . LEU A 1 43  ? 18.572  -12.601 19.124  1.00 25.62  ? 44  LEU A O     1 
ATOM   337   C CB    . LEU A 1 43  ? 17.538  -11.935 16.017  1.00 32.43  ? 44  LEU A CB    1 
ATOM   338   C CG    . LEU A 1 43  ? 19.020  -12.246 15.778  1.00 35.01  ? 44  LEU A CG    1 
ATOM   339   C CD1   . LEU A 1 43  ? 19.266  -13.744 15.771  1.00 35.02  ? 44  LEU A CD1   1 
ATOM   340   C CD2   . LEU A 1 43  ? 19.508  -11.614 14.485  1.00 34.07  ? 44  LEU A CD2   1 
ATOM   341   N N     . THR A 1 44  ? 17.608  -10.579 18.833  1.00 27.26  ? 45  THR A N     1 
ATOM   342   C CA    . THR A 1 44  ? 18.416  -9.900  19.832  1.00 29.89  ? 45  THR A CA    1 
ATOM   343   C C     . THR A 1 44  ? 18.205  -10.554 21.196  1.00 33.83  ? 45  THR A C     1 
ATOM   344   O O     . THR A 1 44  ? 19.098  -10.532 22.040  1.00 32.45  ? 45  THR A O     1 
ATOM   345   C CB    . THR A 1 44  ? 18.055  -8.415  19.851  1.00 31.30  ? 45  THR A CB    1 
ATOM   346   O OG1   . THR A 1 44  ? 18.396  -7.931  18.556  1.00 37.13  ? 45  THR A OG1   1 
ATOM   347   C CG2   . THR A 1 44  ? 18.817  -7.642  20.912  1.00 31.72  ? 45  THR A CG2   1 
ATOM   348   N N     . LYS A 1 45  ? 17.017  -11.134 21.400  1.00 37.51  ? 46  LYS A N     1 
ATOM   349   C CA    . LYS A 1 45  ? 16.688  -11.778 22.662  1.00 40.05  ? 46  LYS A CA    1 
ATOM   350   C C     . LYS A 1 45  ? 17.390  -13.131 22.741  1.00 38.54  ? 46  LYS A C     1 
ATOM   351   O O     . LYS A 1 45  ? 17.771  -13.571 23.824  1.00 33.64  ? 46  LYS A O     1 
ATOM   352   C CB    . LYS A 1 45  ? 15.171  -11.919 22.830  1.00 47.53  ? 46  LYS A CB    1 
ATOM   353   C CG    . LYS A 1 45  ? 14.414  -10.602 22.936  1.00 52.91  ? 46  LYS A CG    1 
ATOM   354   C CD    . LYS A 1 45  ? 12.954  -10.752 23.349  1.00 60.17  ? 46  LYS A CD    1 
ATOM   355   C CE    . LYS A 1 45  ? 12.805  -11.330 24.722  1.00 66.56  ? 46  LYS A CE    1 
ATOM   356   N NZ    . LYS A 1 45  ? 11.399  -11.422 25.125  1.00 69.43  ? 46  LYS A NZ    1 
ATOM   357   N N     . LEU A 1 46  ? 17.552  -13.784 21.584  1.00 37.67  ? 47  LEU A N     1 
ATOM   358   C CA    . LEU A 1 46  ? 18.299  -15.029 21.507  1.00 37.30  ? 47  LEU A CA    1 
ATOM   359   C C     . LEU A 1 46  ? 19.768  -14.741 21.800  1.00 36.54  ? 47  LEU A C     1 
ATOM   360   O O     . LEU A 1 46  ? 20.370  -15.374 22.664  1.00 40.45  ? 47  LEU A O     1 
ATOM   361   C CB    . LEU A 1 46  ? 18.130  -15.689 20.139  1.00 39.89  ? 47  LEU A CB    1 
ATOM   362   C CG    . LEU A 1 46  ? 16.861  -16.523 19.941  1.00 40.12  ? 47  LEU A CG    1 
ATOM   363   C CD1   . LEU A 1 46  ? 16.874  -17.213 18.586  1.00 39.18  ? 47  LEU A CD1   1 
ATOM   364   C CD2   . LEU A 1 46  ? 16.706  -17.540 21.058  1.00 41.18  ? 47  LEU A CD2   1 
ATOM   365   N N     . ASN A 1 47  ? 20.326  -13.772 21.067  1.00 33.45  ? 48  ASN A N     1 
ATOM   366   C CA    . ASN A 1 47  ? 21.729  -13.418 21.188  1.00 30.87  ? 48  ASN A CA    1 
ATOM   367   C C     . ASN A 1 47  ? 21.863  -11.901 21.087  1.00 27.98  ? 48  ASN A C     1 
ATOM   368   O O     . ASN A 1 47  ? 21.543  -11.314 20.056  1.00 29.16  ? 48  ASN A O     1 
ATOM   369   C CB    . ASN A 1 47  ? 22.566  -14.132 20.132  1.00 31.57  ? 48  ASN A CB    1 
ATOM   370   C CG    . ASN A 1 47  ? 24.046  -14.039 20.413  1.00 31.65  ? 48  ASN A CG    1 
ATOM   371   O OD1   . ASN A 1 47  ? 24.559  -12.952 20.701  1.00 33.62  ? 48  ASN A OD1   1 
ATOM   372   N ND2   . ASN A 1 47  ? 24.744  -15.164 20.353  1.00 30.43  ? 48  ASN A ND2   1 
ATOM   373   N N     . PRO A 1 48  ? 22.342  -11.220 22.153  1.00 31.20  ? 49  PRO A N     1 
ATOM   374   C CA    . PRO A 1 48  ? 22.411  -9.756  22.163  1.00 33.45  ? 49  PRO A CA    1 
ATOM   375   C C     . PRO A 1 48  ? 23.466  -9.176  21.224  1.00 34.74  ? 49  PRO A C     1 
ATOM   376   O O     . PRO A 1 48  ? 23.340  -8.041  20.771  1.00 35.26  ? 49  PRO A O     1 
ATOM   377   C CB    . PRO A 1 48  ? 22.723  -9.453  23.640  1.00 33.23  ? 49  PRO A CB    1 
ATOM   378   C CG    . PRO A 1 48  ? 23.509  -10.662 24.101  1.00 33.95  ? 49  PRO A CG    1 
ATOM   379   C CD    . PRO A 1 48  ? 22.843  -11.828 23.395  1.00 31.23  ? 49  PRO A CD    1 
ATOM   380   N N     . ASN A 1 49  ? 24.508  -9.965  20.944  1.00 39.12  ? 50  ASN A N     1 
ATOM   381   C CA    . ASN A 1 49  ? 25.617  -9.507  20.123  1.00 44.07  ? 50  ASN A CA    1 
ATOM   382   C C     . ASN A 1 49  ? 25.274  -9.714  18.650  1.00 41.85  ? 50  ASN A C     1 
ATOM   383   O O     . ASN A 1 49  ? 25.712  -10.685 18.038  1.00 39.10  ? 50  ASN A O     1 
ATOM   384   C CB    . ASN A 1 49  ? 26.916  -10.211 20.499  1.00 49.40  ? 50  ASN A CB    1 
ATOM   385   C CG    . ASN A 1 49  ? 28.108  -9.628  19.780  1.00 56.10  ? 50  ASN A CG    1 
ATOM   386   O OD1   . ASN A 1 49  ? 27.973  -8.641  19.047  1.00 53.25  ? 50  ASN A OD1   1 
ATOM   387   N ND2   . ASN A 1 49  ? 29.281  -10.212 19.981  1.00 59.12  ? 50  ASN A ND2   1 
ATOM   388   N N     . VAL A 1 50  ? 24.497  -8.779  18.091  1.00 38.30  ? 51  VAL A N     1 
ATOM   389   C CA    . VAL A 1 50  ? 24.042  -8.878  16.714  1.00 37.78  ? 51  VAL A CA    1 
ATOM   390   C C     . VAL A 1 50  ? 24.550  -7.674  15.926  1.00 34.67  ? 51  VAL A C     1 
ATOM   391   O O     . VAL A 1 50  ? 24.533  -6.548  16.418  1.00 35.65  ? 51  VAL A O     1 
ATOM   392   C CB    . VAL A 1 50  ? 22.506  -8.976  16.636  1.00 38.55  ? 51  VAL A CB    1 
ATOM   393   C CG1   . VAL A 1 50  ? 22.003  -8.860  15.202  1.00 38.86  ? 51  VAL A CG1   1 
ATOM   394   C CG2   . VAL A 1 50  ? 21.984  -10.250 17.289  1.00 40.67  ? 51  VAL A CG2   1 
ATOM   395   N N     . ILE A 1 51  ? 25.001  -7.935  14.695  1.00 33.15  ? 52  ILE A N     1 
ATOM   396   C CA    . ILE A 1 51  ? 25.332  -6.882  13.749  1.00 31.27  ? 52  ILE A CA    1 
ATOM   397   C C     . ILE A 1 51  ? 24.386  -6.997  12.557  1.00 29.42  ? 52  ILE A C     1 
ATOM   398   O O     . ILE A 1 51  ? 24.253  -8.066  11.965  1.00 26.43  ? 52  ILE A O     1 
ATOM   399   C CB    . ILE A 1 51  ? 26.810  -6.958  13.323  1.00 34.06  ? 52  ILE A CB    1 
ATOM   400   C CG1   . ILE A 1 51  ? 27.747  -6.745  14.513  1.00 34.23  ? 52  ILE A CG1   1 
ATOM   401   C CG2   . ILE A 1 51  ? 27.103  -5.971  12.192  1.00 36.59  ? 52  ILE A CG2   1 
ATOM   402   C CD1   . ILE A 1 51  ? 29.220  -6.729  14.148  1.00 37.87  ? 52  ILE A CD1   1 
ATOM   403   N N     . ASN A 1 52  ? 23.723  -5.884  12.228  1.00 27.49  ? 53  ASN A N     1 
ATOM   404   C CA    . ASN A 1 52  ? 22.712  -5.866  11.184  1.00 30.02  ? 53  ASN A CA    1 
ATOM   405   C C     . ASN A 1 52  ? 23.373  -5.549  9.845   1.00 31.00  ? 53  ASN A C     1 
ATOM   406   O O     . ASN A 1 52  ? 23.933  -4.470  9.661   1.00 28.44  ? 53  ASN A O     1 
ATOM   407   C CB    . ASN A 1 52  ? 21.595  -4.883  11.521  1.00 31.35  ? 53  ASN A CB    1 
ATOM   408   C CG    . ASN A 1 52  ? 20.445  -4.968  10.547  1.00 34.41  ? 53  ASN A CG    1 
ATOM   409   O OD1   . ASN A 1 52  ? 20.531  -5.684  9.543   1.00 35.25  ? 53  ASN A OD1   1 
ATOM   410   N ND2   . ASN A 1 52  ? 19.366  -4.249  10.820  1.00 34.20  ? 53  ASN A ND2   1 
ATOM   411   N N     . LEU A 1 53  ? 23.292  -6.506  8.913   1.00 32.36  ? 54  LEU A N     1 
ATOM   412   C CA    . LEU A 1 53  ? 23.899  -6.366  7.598   1.00 30.96  ? 54  LEU A CA    1 
ATOM   413   C C     . LEU A 1 53  ? 23.151  -5.303  6.800   1.00 28.81  ? 54  LEU A C     1 
ATOM   414   O O     . LEU A 1 53  ? 23.681  -4.754  5.837   1.00 29.48  ? 54  LEU A O     1 
ATOM   415   C CB    . LEU A 1 53  ? 23.883  -7.715  6.878   1.00 33.19  ? 54  LEU A CB    1 
ATOM   416   C CG    . LEU A 1 53  ? 24.755  -8.816  7.490   1.00 32.93  ? 54  LEU A CG    1 
ATOM   417   C CD1   . LEU A 1 53  ? 24.612  -10.118 6.718   1.00 31.07  ? 54  LEU A CD1   1 
ATOM   418   C CD2   . LEU A 1 53  ? 26.209  -8.385  7.545   1.00 32.26  ? 54  LEU A CD2   1 
ATOM   419   N N     . GLN A 1 54  ? 21.911  -5.028  7.214   1.00 28.39  ? 55  GLN A N     1 
ATOM   420   C CA    . GLN A 1 54  ? 21.044  -4.094  6.517   1.00 34.46  ? 55  GLN A CA    1 
ATOM   421   C C     . GLN A 1 54  ? 21.778  -2.773  6.298   1.00 37.54  ? 55  GLN A C     1 
ATOM   422   O O     . GLN A 1 54  ? 21.472  -2.033  5.365   1.00 37.66  ? 55  GLN A O     1 
ATOM   423   C CB    . GLN A 1 54  ? 19.773  -3.884  7.341   1.00 42.44  ? 55  GLN A CB    1 
ATOM   424   C CG    . GLN A 1 54  ? 18.651  -3.170  6.594   1.00 46.34  ? 55  GLN A CG    1 
ATOM   425   C CD    . GLN A 1 54  ? 18.039  -4.012  5.496   1.00 52.92  ? 55  GLN A CD    1 
ATOM   426   O OE1   . GLN A 1 54  ? 18.018  -3.625  4.323   1.00 61.99  ? 55  GLN A OE1   1 
ATOM   427   N NE2   . GLN A 1 54  ? 17.525  -5.174  5.871   1.00 50.75  ? 55  GLN A NE2   1 
ATOM   428   N N     . GLN A 1 55  ? 22.762  -2.501  7.161   1.00 35.88  ? 56  GLN A N     1 
ATOM   429   C CA    . GLN A 1 55  ? 23.406  -1.199  7.222   1.00 36.72  ? 56  GLN A CA    1 
ATOM   430   C C     . GLN A 1 55  ? 24.274  -0.969  5.987   1.00 38.61  ? 56  GLN A C     1 
ATOM   431   O O     . GLN A 1 55  ? 24.722  0.150   5.748   1.00 38.43  ? 56  GLN A O     1 
ATOM   432   C CB    . GLN A 1 55  ? 24.257  -1.097  8.488   1.00 37.34  ? 56  GLN A CB    1 
ATOM   433   C CG    . GLN A 1 55  ? 25.488  -1.997  8.482   1.00 35.69  ? 56  GLN A CG    1 
ATOM   434   C CD    . GLN A 1 55  ? 26.213  -2.020  9.809   1.00 37.20  ? 56  GLN A CD    1 
ATOM   435   O OE1   . GLN A 1 55  ? 25.697  -2.516  10.817  1.00 41.22  ? 56  GLN A OE1   1 
ATOM   436   N NE2   . GLN A 1 55  ? 27.428  -1.490  9.821   1.00 37.02  ? 56  GLN A NE2   1 
ATOM   437   N N     . PHE A 1 56  ? 24.507  -2.030  5.206   1.00 37.77  ? 57  PHE A N     1 
ATOM   438   C CA    . PHE A 1 56  ? 25.425  -1.952  4.081   1.00 36.29  ? 57  PHE A CA    1 
ATOM   439   C C     . PHE A 1 56  ? 24.658  -1.630  2.800   1.00 36.86  ? 57  PHE A C     1 
ATOM   440   O O     . PHE A 1 56  ? 25.263  -1.452  1.745   1.00 32.04  ? 57  PHE A O     1 
ATOM   441   C CB    . PHE A 1 56  ? 26.237  -3.245  3.952   1.00 35.88  ? 57  PHE A CB    1 
ATOM   442   C CG    . PHE A 1 56  ? 27.223  -3.472  5.090   1.00 35.58  ? 57  PHE A CG    1 
ATOM   443   C CD1   . PHE A 1 56  ? 28.358  -2.678  5.216   1.00 37.30  ? 57  PHE A CD1   1 
ATOM   444   C CD2   . PHE A 1 56  ? 27.026  -4.488  6.018   1.00 35.71  ? 57  PHE A CD2   1 
ATOM   445   C CE1   . PHE A 1 56  ? 29.255  -2.882  6.253   1.00 38.99  ? 57  PHE A CE1   1 
ATOM   446   C CE2   . PHE A 1 56  ? 27.930  -4.691  7.049   1.00 37.50  ? 57  PHE A CE2   1 
ATOM   447   C CZ    . PHE A 1 56  ? 29.041  -3.889  7.164   1.00 37.43  ? 57  PHE A CZ    1 
ATOM   448   N N     . TYR A 1 57  ? 23.326  -1.550  2.899   1.00 37.29  ? 58  TYR A N     1 
ATOM   449   C CA    . TYR A 1 57  ? 22.504  -1.168  1.762   1.00 37.24  ? 58  TYR A CA    1 
ATOM   450   C C     . TYR A 1 57  ? 22.574  0.346   1.586   1.00 39.03  ? 58  TYR A C     1 
ATOM   451   O O     . TYR A 1 57  ? 22.840  1.076   2.539   1.00 37.66  ? 58  TYR A O     1 
ATOM   452   C CB    . TYR A 1 57  ? 21.052  -1.628  1.922   1.00 37.58  ? 58  TYR A CB    1 
ATOM   453   C CG    . TYR A 1 57  ? 20.840  -3.119  1.706   1.00 39.23  ? 58  TYR A CG    1 
ATOM   454   C CD1   . TYR A 1 57  ? 20.771  -3.655  0.426   1.00 41.03  ? 58  TYR A CD1   1 
ATOM   455   C CD2   . TYR A 1 57  ? 20.694  -3.988  2.780   1.00 38.37  ? 58  TYR A CD2   1 
ATOM   456   C CE1   . TYR A 1 57  ? 20.576  -5.011  0.220   1.00 40.41  ? 58  TYR A CE1   1 
ATOM   457   C CE2   . TYR A 1 57  ? 20.498  -5.345  2.588   1.00 39.23  ? 58  TYR A CE2   1 
ATOM   458   C CZ    . TYR A 1 57  ? 20.439  -5.858  1.305   1.00 38.45  ? 58  TYR A CZ    1 
ATOM   459   O OH    . TYR A 1 57  ? 20.247  -7.195  1.109   1.00 41.15  ? 58  TYR A OH    1 
ATOM   460   N N     . ALA A 1 58  ? 22.327  0.799   0.352   1.00 38.00  ? 59  ALA A N     1 
ATOM   461   C CA    . ALA A 1 58  ? 22.347  2.215   0.024   1.00 40.95  ? 59  ALA A CA    1 
ATOM   462   C C     . ALA A 1 58  ? 21.591  3.004   1.089   1.00 47.12  ? 59  ALA A C     1 
ATOM   463   O O     . ALA A 1 58  ? 20.527  2.585   1.541   1.00 48.53  ? 59  ALA A O     1 
ATOM   464   C CB    . ALA A 1 58  ? 21.754  2.432   -1.350  1.00 39.26  ? 59  ALA A CB    1 
ATOM   465   N N     . GLN A 1 59  ? 22.155  4.153   1.475   1.00 54.17  ? 60  GLN A N     1 
ATOM   466   C CA    . GLN A 1 59  ? 21.566  4.997   2.501   1.00 62.40  ? 60  GLN A CA    1 
ATOM   467   C C     . GLN A 1 59  ? 21.357  6.404   1.948   1.00 67.87  ? 60  GLN A C     1 
ATOM   468   O O     . GLN A 1 59  ? 22.312  7.066   1.546   1.00 68.00  ? 60  GLN A O     1 
ATOM   469   C CB    . GLN A 1 59  ? 22.464  5.043   3.737   1.00 67.66  ? 60  GLN A CB    1 
ATOM   470   C CG    . GLN A 1 59  ? 22.648  3.694   4.426   1.00 69.70  ? 60  GLN A CG    1 
ATOM   471   C CD    . GLN A 1 59  ? 21.380  3.173   5.065   1.00 68.58  ? 60  GLN A CD    1 
ATOM   472   O OE1   . GLN A 1 59  ? 20.778  3.824   5.928   1.00 65.36  ? 60  GLN A OE1   1 
ATOM   473   N NE2   . GLN A 1 59  ? 20.959  1.988   4.649   1.00 65.01  ? 60  GLN A NE2   1 
ATOM   474   N N     . ASN A 1 60  ? 20.096  6.847   1.936   1.00 71.10  ? 61  ASN A N     1 
ATOM   475   C CA    . ASN A 1 60  ? 19.753  8.205   1.546   1.00 70.36  ? 61  ASN A CA    1 
ATOM   476   C C     . ASN A 1 60  ? 19.912  8.359   0.036   1.00 65.09  ? 61  ASN A C     1 
ATOM   477   O O     . ASN A 1 60  ? 20.908  8.902   -0.435  1.00 77.63  ? 61  ASN A O     1 
ATOM   478   C CB    . ASN A 1 60  ? 20.594  9.230   2.300   1.00 72.29  ? 61  ASN A CB    1 
ATOM   479   C CG    . ASN A 1 60  ? 20.507  9.051   3.797   1.00 74.00  ? 61  ASN A CG    1 
ATOM   480   O OD1   . ASN A 1 60  ? 19.412  9.099   4.367   1.00 75.31  ? 61  ASN A OD1   1 
ATOM   481   N ND2   . ASN A 1 60  ? 21.642  8.843   4.448   1.00 75.28  ? 61  ASN A ND2   1 
ATOM   482   N N     . GLY A 1 61  ? 18.912  7.878   -0.710  1.00 61.20  ? 62  GLY A N     1 
ATOM   483   C CA    . GLY A 1 61  ? 18.891  8.008   -2.158  1.00 55.19  ? 62  GLY A CA    1 
ATOM   484   C C     . GLY A 1 61  ? 20.299  7.985   -2.745  1.00 49.86  ? 62  GLY A C     1 
ATOM   485   O O     . GLY A 1 61  ? 20.607  8.743   -3.662  1.00 50.37  ? 62  GLY A O     1 
ATOM   486   N N     . GLU A 1 62  ? 21.141  7.095   -2.210  1.00 52.88  ? 63  GLU A N     1 
ATOM   487   C CA    . GLU A 1 62  ? 22.516  6.957   -2.660  1.00 50.54  ? 63  GLU A CA    1 
ATOM   488   C C     . GLU A 1 62  ? 22.577  5.964   -3.817  1.00 46.31  ? 63  GLU A C     1 
ATOM   489   O O     . GLU A 1 62  ? 21.859  4.967   -3.823  1.00 36.57  ? 63  GLU A O     1 
ATOM   490   C CB    . GLU A 1 62  ? 23.399  6.498   -1.499  1.00 53.96  ? 63  GLU A CB    1 
ATOM   491   C CG    . GLU A 1 62  ? 24.807  6.096   -1.926  1.00 57.55  ? 63  GLU A CG    1 
ATOM   492   C CD    . GLU A 1 62  ? 25.679  5.598   -0.788  1.00 63.46  ? 63  GLU A CD    1 
ATOM   493   O OE1   . GLU A 1 62  ? 25.261  4.646   -0.095  1.00 67.66  ? 63  GLU A OE1   1 
ATOM   494   O OE2   . GLU A 1 62  ? 26.780  6.157   -0.598  1.00 69.68  ? 63  GLU A OE2   1 
ATOM   495   N N     . VAL A 1 63  ? 23.446  6.253   -4.792  1.00 44.58  ? 64  VAL A N     1 
ATOM   496   C CA    . VAL A 1 63  ? 23.659  5.369   -5.926  1.00 45.07  ? 64  VAL A CA    1 
ATOM   497   C C     . VAL A 1 63  ? 24.770  4.385   -5.570  1.00 43.74  ? 64  VAL A C     1 
ATOM   498   O O     . VAL A 1 63  ? 25.944  4.749   -5.550  1.00 42.60  ? 64  VAL A O     1 
ATOM   499   C CB    . VAL A 1 63  ? 24.002  6.156   -7.205  1.00 47.14  ? 64  VAL A CB    1 
ATOM   500   C CG1   . VAL A 1 63  ? 24.433  5.234   -8.339  1.00 48.09  ? 64  VAL A CG1   1 
ATOM   501   C CG2   . VAL A 1 63  ? 22.850  7.051   -7.647  1.00 46.95  ? 64  VAL A CG2   1 
ATOM   502   N N     . LYS A 1 64  ? 24.381  3.135   -5.297  1.00 41.09  ? 65  LYS A N     1 
ATOM   503   C CA    . LYS A 1 64  ? 25.317  2.120   -4.844  1.00 42.49  ? 65  LYS A CA    1 
ATOM   504   C C     . LYS A 1 64  ? 24.954  0.773   -5.466  1.00 40.46  ? 65  LYS A C     1 
ATOM   505   O O     . LYS A 1 64  ? 23.822  0.309   -5.342  1.00 32.11  ? 65  LYS A O     1 
ATOM   506   C CB    . LYS A 1 64  ? 25.298  2.052   -3.312  1.00 44.23  ? 65  LYS A CB    1 
ATOM   507   C CG    . LYS A 1 64  ? 26.298  1.090   -2.689  1.00 48.10  ? 65  LYS A CG    1 
ATOM   508   C CD    . LYS A 1 64  ? 26.288  1.099   -1.164  1.00 51.59  ? 65  LYS A CD    1 
ATOM   509   C CE    . LYS A 1 64  ? 27.304  0.174   -0.575  1.00 53.35  ? 65  LYS A CE    1 
ATOM   510   N NZ    . LYS A 1 64  ? 27.287  0.215   0.889   1.00 55.88  ? 65  LYS A NZ    1 
ATOM   511   N N     . ASN A 1 65  ? 25.937  0.159   -6.134  1.00 39.74  ? 66  ASN A N     1 
ATOM   512   C CA    . ASN A 1 65  ? 25.764  -1.139  -6.764  1.00 42.91  ? 66  ASN A CA    1 
ATOM   513   C C     . ASN A 1 65  ? 25.703  -2.213  -5.679  1.00 40.92  ? 66  ASN A C     1 
ATOM   514   O O     . ASN A 1 65  ? 26.567  -2.266  -4.807  1.00 44.33  ? 66  ASN A O     1 
ATOM   515   C CB    . ASN A 1 65  ? 26.876  -1.413  -7.771  1.00 43.54  ? 66  ASN A CB    1 
ATOM   516   C CG    . ASN A 1 65  ? 26.641  -2.681  -8.555  1.00 42.95  ? 66  ASN A CG    1 
ATOM   517   O OD1   . ASN A 1 65  ? 26.461  -3.753  -7.967  1.00 41.89  ? 66  ASN A OD1   1 
ATOM   518   N ND2   . ASN A 1 65  ? 26.632  -2.581  -9.877  1.00 40.28  ? 66  ASN A ND2   1 
ATOM   519   N N     . ARG A 1 66  ? 24.679  -3.071  -5.751  1.00 41.41  ? 67  ARG A N     1 
ATOM   520   C CA    . ARG A 1 66  ? 24.435  -4.063  -4.716  1.00 41.16  ? 67  ARG A CA    1 
ATOM   521   C C     . ARG A 1 66  ? 25.628  -5.010  -4.610  1.00 41.38  ? 67  ARG A C     1 
ATOM   522   O O     . ARG A 1 66  ? 25.860  -5.601  -3.558  1.00 35.28  ? 67  ARG A O     1 
ATOM   523   C CB    . ARG A 1 66  ? 23.144  -4.849  -4.977  1.00 41.85  ? 67  ARG A CB    1 
ATOM   524   C CG    . ARG A 1 66  ? 21.867  -4.032  -4.845  1.00 43.40  ? 67  ARG A CG    1 
ATOM   525   C CD    . ARG A 1 66  ? 20.654  -4.910  -4.565  1.00 45.61  ? 67  ARG A CD    1 
ATOM   526   N NE    . ARG A 1 66  ? 20.416  -5.921  -5.602  1.00 48.76  ? 67  ARG A NE    1 
ATOM   527   C CZ    . ARG A 1 66  ? 19.980  -5.663  -6.829  1.00 53.59  ? 67  ARG A CZ    1 
ATOM   528   N NH1   . ARG A 1 66  ? 19.711  -4.421  -7.190  1.00 53.04  ? 67  ARG A NH1   1 
ATOM   529   N NH2   . ARG A 1 66  ? 19.802  -6.652  -7.687  1.00 56.54  ? 67  ARG A NH2   1 
ATOM   530   N N     . ARG A 1 67  ? 26.377  -5.148  -5.708  1.00 43.16  ? 68  ARG A N     1 
ATOM   531   C CA    . ARG A 1 67  ? 27.531  -6.031  -5.738  1.00 49.13  ? 68  ARG A CA    1 
ATOM   532   C C     . ARG A 1 67  ? 28.559  -5.546  -4.718  1.00 44.80  ? 68  ARG A C     1 
ATOM   533   O O     . ARG A 1 67  ? 29.308  -6.342  -4.157  1.00 42.54  ? 68  ARG A O     1 
ATOM   534   C CB    . ARG A 1 67  ? 28.117  -6.098  -7.153  1.00 55.86  ? 68  ARG A CB    1 
ATOM   535   C CG    . ARG A 1 67  ? 27.112  -6.528  -8.212  1.00 62.57  ? 68  ARG A CG    1 
ATOM   536   C CD    . ARG A 1 67  ? 27.718  -6.595  -9.606  1.00 67.61  ? 68  ARG A CD    1 
ATOM   537   N NE    . ARG A 1 67  ? 28.679  -7.695  -9.744  1.00 71.67  ? 68  ARG A NE    1 
ATOM   538   C CZ    . ARG A 1 67  ? 28.557  -8.694  -10.610 1.00 70.10  ? 68  ARG A CZ    1 
ATOM   539   N NH1   . ARG A 1 67  ? 27.520  -8.738  -11.428 1.00 71.01  ? 68  ARG A NH1   1 
ATOM   540   N NH2   . ARG A 1 67  ? 29.474  -9.644  -10.657 1.00 72.71  ? 68  ARG A NH2   1 
ATOM   541   N N     . ASP A 1 68  ? 28.573  -4.229  -4.481  1.00 41.77  ? 69  ASP A N     1 
ATOM   542   C CA    . ASP A 1 68  ? 29.467  -3.629  -3.504  1.00 38.93  ? 69  ASP A CA    1 
ATOM   543   C C     . ASP A 1 68  ? 28.893  -3.840  -2.105  1.00 36.51  ? 69  ASP A C     1 
ATOM   544   O O     . ASP A 1 68  ? 29.635  -4.077  -1.154  1.00 35.70  ? 69  ASP A O     1 
ATOM   545   C CB    . ASP A 1 68  ? 29.707  -2.157  -3.805  1.00 38.42  ? 69  ASP A CB    1 
ATOM   546   C CG    . ASP A 1 68  ? 30.383  -1.866  -5.138  1.00 40.76  ? 69  ASP A CG    1 
ATOM   547   O OD1   . ASP A 1 68  ? 31.491  -2.396  -5.361  1.00 41.87  ? 69  ASP A OD1   1 
ATOM   548   O OD2   . ASP A 1 68  ? 29.799  -1.106  -5.939  1.00 40.91  ? 69  ASP A OD2   1 
ATOM   549   N N     . THR A 1 69  ? 27.564  -3.745  -1.996  1.00 33.38  ? 70  THR A N     1 
ATOM   550   C CA    . THR A 1 69  ? 26.872  -3.967  -0.737  1.00 34.08  ? 70  THR A CA    1 
ATOM   551   C C     . THR A 1 69  ? 27.153  -5.386  -0.252  1.00 31.96  ? 70  THR A C     1 
ATOM   552   O O     . THR A 1 69  ? 27.467  -5.598  0.918   1.00 29.07  ? 70  THR A O     1 
ATOM   553   C CB    . THR A 1 69  ? 25.375  -3.726  -0.925  1.00 35.40  ? 70  THR A CB    1 
ATOM   554   O OG1   . THR A 1 69  ? 25.233  -2.323  -1.126  1.00 42.60  ? 70  THR A OG1   1 
ATOM   555   C CG2   . THR A 1 69  ? 24.560  -4.161  0.279   1.00 36.38  ? 70  THR A CG2   1 
ATOM   556   N N     . TYR A 1 70  ? 27.028  -6.351  -1.167  1.00 30.08  ? 71  TYR A N     1 
ATOM   557   C CA    . TYR A 1 70  ? 27.205  -7.756  -0.841  1.00 30.87  ? 71  TYR A CA    1 
ATOM   558   C C     . TYR A 1 70  ? 28.656  -8.005  -0.441  1.00 33.78  ? 71  TYR A C     1 
ATOM   559   O O     . TYR A 1 70  ? 28.927  -8.773  0.480   1.00 37.57  ? 71  TYR A O     1 
ATOM   560   C CB    . TYR A 1 70  ? 26.775  -8.606  -2.041  1.00 29.77  ? 71  TYR A CB    1 
ATOM   561   C CG    . TYR A 1 70  ? 25.320  -8.422  -2.450  1.00 30.06  ? 71  TYR A CG    1 
ATOM   562   C CD1   . TYR A 1 70  ? 24.331  -8.199  -1.501  1.00 29.99  ? 71  TYR A CD1   1 
ATOM   563   C CD2   . TYR A 1 70  ? 24.938  -8.458  -3.786  1.00 33.32  ? 71  TYR A CD2   1 
ATOM   564   C CE1   . TYR A 1 70  ? 23.005  -8.029  -1.864  1.00 30.81  ? 71  TYR A CE1   1 
ATOM   565   C CE2   . TYR A 1 70  ? 23.615  -8.289  -4.164  1.00 33.58  ? 71  TYR A CE2   1 
ATOM   566   C CZ    . TYR A 1 70  ? 22.646  -8.073  -3.200  1.00 32.33  ? 71  TYR A CZ    1 
ATOM   567   O OH    . TYR A 1 70  ? 21.341  -7.903  -3.562  1.00 36.88  ? 71  TYR A OH    1 
ATOM   568   N N     . GLU A 1 71  ? 29.581  -7.346  -1.145  1.00 34.49  ? 72  GLU A N     1 
ATOM   569   C CA    . GLU A 1 71  ? 31.004  -7.512  -0.897  1.00 36.38  ? 72  GLU A CA    1 
ATOM   570   C C     . GLU A 1 71  ? 31.346  -6.973  0.490   1.00 37.21  ? 72  GLU A C     1 
ATOM   571   O O     . GLU A 1 71  ? 32.189  -7.533  1.188   1.00 37.40  ? 72  GLU A O     1 
ATOM   572   C CB    . GLU A 1 71  ? 31.825  -6.795  -1.970  1.00 41.46  ? 72  GLU A CB    1 
ATOM   573   C CG    . GLU A 1 71  ? 33.330  -6.867  -1.726  1.00 45.56  ? 72  GLU A CG    1 
ATOM   574   C CD    . GLU A 1 71  ? 33.888  -8.278  -1.706  1.00 49.13  ? 72  GLU A CD    1 
ATOM   575   O OE1   . GLU A 1 71  ? 33.110  -9.226  -1.946  1.00 49.25  ? 72  GLU A OE1   1 
ATOM   576   O OE2   . GLU A 1 71  ? 35.101  -8.432  -1.448  1.00 55.42  ? 72  GLU A OE2   1 
ATOM   577   N N     . GLN A 1 72  ? 30.690  -5.872  0.870   1.00 33.92  ? 73  GLN A N     1 
ATOM   578   C CA    . GLN A 1 72  ? 30.910  -5.254  2.166   1.00 34.25  ? 73  GLN A CA    1 
ATOM   579   C C     . GLN A 1 72  ? 30.334  -6.153  3.257   1.00 31.39  ? 73  GLN A C     1 
ATOM   580   O O     . GLN A 1 72  ? 30.885  -6.236  4.353   1.00 31.29  ? 73  GLN A O     1 
ATOM   581   C CB    . GLN A 1 72  ? 30.286  -3.858  2.201   1.00 34.86  ? 73  GLN A CB    1 
ATOM   582   C CG    . GLN A 1 72  ? 30.975  -2.854  1.284   1.00 35.02  ? 73  GLN A CG    1 
ATOM   583   C CD    . GLN A 1 72  ? 30.304  -1.497  1.275   1.00 37.41  ? 73  GLN A CD    1 
ATOM   584   O OE1   . GLN A 1 72  ? 29.255  -1.290  1.896   1.00 37.78  ? 73  GLN A OE1   1 
ATOM   585   N NE2   . GLN A 1 72  ? 30.902  -0.557  0.558   1.00 37.45  ? 73  GLN A NE2   1 
ATOM   586   N N     . MET A 1 73  ? 29.221  -6.822  2.939   1.00 30.30  ? 74  MET A N     1 
ATOM   587   C CA    . MET A 1 73  ? 28.594  -7.752  3.863   1.00 28.80  ? 74  MET A CA    1 
ATOM   588   C C     . MET A 1 73  ? 29.547  -8.912  4.136   1.00 30.04  ? 74  MET A C     1 
ATOM   589   O O     . MET A 1 73  ? 29.812  -9.246  5.288   1.00 31.48  ? 74  MET A O     1 
ATOM   590   C CB    . MET A 1 73  ? 27.276  -8.294  3.296   1.00 27.21  ? 74  MET A CB    1 
ATOM   591   C CG    . MET A 1 73  ? 26.132  -7.298  3.317   1.00 26.96  ? 74  MET A CG    1 
ATOM   592   S SD    . MET A 1 73  ? 24.599  -8.004  2.679   1.00 27.10  ? 74  MET A SD    1 
ATOM   593   C CE    . MET A 1 73  ? 23.483  -6.596  2.748   1.00 28.96  ? 74  MET A CE    1 
ATOM   594   N N     . VAL A 1 74  ? 30.062  -9.512  3.057   1.00 31.56  ? 75  VAL A N     1 
ATOM   595   C CA    . VAL A 1 74  ? 30.924  -10.677 3.159   1.00 30.05  ? 75  VAL A CA    1 
ATOM   596   C C     . VAL A 1 74  ? 32.153  -10.320 3.992   1.00 33.52  ? 75  VAL A C     1 
ATOM   597   O O     . VAL A 1 74  ? 32.562  -11.088 4.861   1.00 35.76  ? 75  VAL A O     1 
ATOM   598   C CB    . VAL A 1 74  ? 31.325  -11.200 1.766   1.00 28.45  ? 75  VAL A CB    1 
ATOM   599   C CG1   . VAL A 1 74  ? 32.380  -12.297 1.853   1.00 27.47  ? 75  VAL A CG1   1 
ATOM   600   C CG2   . VAL A 1 74  ? 30.116  -11.681 0.971   1.00 31.09  ? 75  VAL A CG2   1 
ATOM   601   N N     . ASN A 1 75  ? 32.730  -9.146  3.718   1.00 32.72  ? 76  ASN A N     1 
ATOM   602   C CA    . ASN A 1 75  ? 33.953  -8.715  4.376   1.00 36.10  ? 76  ASN A CA    1 
ATOM   603   C C     . ASN A 1 75  ? 33.715  -8.604  5.880   1.00 34.54  ? 76  ASN A C     1 
ATOM   604   O O     . ASN A 1 75  ? 34.519  -9.084  6.676   1.00 37.66  ? 76  ASN A O     1 
ATOM   605   C CB    . ASN A 1 75  ? 34.467  -7.401  3.799   1.00 36.49  ? 76  ASN A CB    1 
ATOM   606   C CG    . ASN A 1 75  ? 35.714  -6.921  4.503   1.00 46.34  ? 76  ASN A CG    1 
ATOM   607   O OD1   . ASN A 1 75  ? 35.709  -5.848  5.117   1.00 46.13  ? 76  ASN A OD1   1 
ATOM   608   N ND2   . ASN A 1 75  ? 36.785  -7.698  4.433   1.00 49.89  ? 76  ASN A ND2   1 
ATOM   609   N N     . ALA A 1 76  ? 32.608  -7.954  6.253   1.00 32.53  ? 77  ALA A N     1 
ATOM   610   C CA    . ALA A 1 76  ? 32.263  -7.761  7.652   1.00 29.20  ? 77  ALA A CA    1 
ATOM   611   C C     . ALA A 1 76  ? 32.212  -9.111  8.363   1.00 27.69  ? 77  ALA A C     1 
ATOM   612   O O     . ALA A 1 76  ? 32.756  -9.265  9.455   1.00 25.73  ? 77  ALA A O     1 
ATOM   613   C CB    . ALA A 1 76  ? 30.943  -7.027  7.759   1.00 29.04  ? 77  ALA A CB    1 
ATOM   614   N N     . ILE A 1 77  ? 31.551  -10.084 7.727   1.00 24.78  ? 78  ILE A N     1 
ATOM   615   C CA    . ILE A 1 77  ? 31.392  -11.410 8.299   1.00 23.48  ? 78  ILE A CA    1 
ATOM   616   C C     . ILE A 1 77  ? 32.769  -12.030 8.521   1.00 23.66  ? 78  ILE A C     1 
ATOM   617   O O     . ILE A 1 77  ? 33.061  -12.521 9.609   1.00 24.40  ? 78  ILE A O     1 
ATOM   618   C CB    . ILE A 1 77  ? 30.505  -12.290 7.398   1.00 22.05  ? 78  ILE A CB    1 
ATOM   619   C CG1   . ILE A 1 77  ? 29.111  -11.687 7.227   1.00 21.61  ? 78  ILE A CG1   1 
ATOM   620   C CG2   . ILE A 1 77  ? 30.441  -13.724 7.927   1.00 23.50  ? 78  ILE A CG2   1 
ATOM   621   C CD1   . ILE A 1 77  ? 28.222  -12.440 6.253   1.00 20.92  ? 78  ILE A CD1   1 
ATOM   622   N N     . LEU A 1 78  ? 33.610  -11.992 7.482   1.00 26.11  ? 79  LEU A N     1 
ATOM   623   C CA    . LEU A 1 78  ? 34.916  -12.630 7.524   1.00 30.95  ? 79  LEU A CA    1 
ATOM   624   C C     . LEU A 1 78  ? 35.793  -11.962 8.580   1.00 31.87  ? 79  LEU A C     1 
ATOM   625   O O     . LEU A 1 78  ? 36.607  -12.624 9.219   1.00 34.85  ? 79  LEU A O     1 
ATOM   626   C CB    . LEU A 1 78  ? 35.571  -12.591 6.144   1.00 34.25  ? 79  LEU A CB    1 
ATOM   627   C CG    . LEU A 1 78  ? 35.102  -13.659 5.150   1.00 37.10  ? 79  LEU A CG    1 
ATOM   628   C CD1   . LEU A 1 78  ? 35.335  -15.050 5.717   1.00 39.68  ? 79  LEU A CD1   1 
ATOM   629   C CD2   . LEU A 1 78  ? 33.643  -13.472 4.775   1.00 38.83  ? 79  LEU A CD2   1 
ATOM   630   N N     . ASP A 1 79  ? 35.626  -10.646 8.750   1.00 32.56  ? 80  ASP A N     1 
ATOM   631   C CA    . ASP A 1 79  ? 36.388  -9.903  9.741   1.00 37.27  ? 80  ASP A CA    1 
ATOM   632   C C     . ASP A 1 79  ? 36.193  -10.547 11.112  1.00 37.17  ? 80  ASP A C     1 
ATOM   633   O O     . ASP A 1 79  ? 37.154  -10.750 11.850  1.00 38.08  ? 80  ASP A O     1 
ATOM   634   C CB    . ASP A 1 79  ? 36.014  -8.428  9.739   1.00 40.45  ? 80  ASP A CB    1 
ATOM   635   C CG    . ASP A 1 79  ? 36.528  -7.628  8.551   1.00 44.74  ? 80  ASP A CG    1 
ATOM   636   O OD1   . ASP A 1 79  ? 37.255  -8.213  7.722   1.00 53.90  ? 80  ASP A OD1   1 
ATOM   637   O OD2   . ASP A 1 79  ? 36.199  -6.426  8.467   1.00 47.80  ? 80  ASP A OD2   1 
ATOM   638   N N     . ALA A 1 80  ? 34.937  -10.868 11.436  1.00 33.99  ? 81  ALA A N     1 
ATOM   639   C CA    . ALA A 1 80  ? 34.606  -11.484 12.710  1.00 33.96  ? 81  ALA A CA    1 
ATOM   640   C C     . ALA A 1 80  ? 35.319  -12.827 12.835  1.00 31.41  ? 81  ALA A C     1 
ATOM   641   O O     . ALA A 1 80  ? 35.900  -13.134 13.873  1.00 26.95  ? 81  ALA A O     1 
ATOM   642   C CB    . ALA A 1 80  ? 33.105  -11.641 12.832  1.00 33.53  ? 81  ALA A CB    1 
ATOM   643   N N     . VAL A 1 81  ? 35.271  -13.617 11.757  1.00 30.57  ? 82  VAL A N     1 
ATOM   644   C CA    . VAL A 1 81  ? 35.856  -14.947 11.744  1.00 31.40  ? 82  VAL A CA    1 
ATOM   645   C C     . VAL A 1 81  ? 37.367  -14.829 11.930  1.00 31.70  ? 82  VAL A C     1 
ATOM   646   O O     . VAL A 1 81  ? 37.955  -15.541 12.740  1.00 32.62  ? 82  VAL A O     1 
ATOM   647   C CB    . VAL A 1 81  ? 35.506  -15.688 10.439  1.00 29.94  ? 82  VAL A CB    1 
ATOM   648   C CG1   . VAL A 1 81  ? 36.179  -17.054 10.363  1.00 29.69  ? 82  VAL A CG1   1 
ATOM   649   C CG2   . VAL A 1 81  ? 33.999  -15.819 10.249  1.00 28.54  ? 82  VAL A CG2   1 
ATOM   650   N N     . ARG A 1 82  ? 37.979  -13.911 11.175  1.00 32.98  ? 83  ARG A N     1 
ATOM   651   C CA    . ARG A 1 82  ? 39.420  -13.721 11.196  1.00 34.11  ? 83  ARG A CA    1 
ATOM   652   C C     . ARG A 1 82  ? 39.865  -13.303 12.596  1.00 32.81  ? 83  ARG A C     1 
ATOM   653   O O     . ARG A 1 82  ? 40.982  -13.602 13.011  1.00 28.20  ? 83  ARG A O     1 
ATOM   654   C CB    . ARG A 1 82  ? 39.819  -12.676 10.148  1.00 38.31  ? 83  ARG A CB    1 
ATOM   655   C CG    . ARG A 1 82  ? 39.511  -13.091 8.717   1.00 39.04  ? 83  ARG A CG    1 
ATOM   656   C CD    . ARG A 1 82  ? 39.568  -11.918 7.751   1.00 43.42  ? 83  ARG A CD    1 
ATOM   657   N NE    . ARG A 1 82  ? 39.176  -12.305 6.392   1.00 46.17  ? 83  ARG A NE    1 
ATOM   658   C CZ    . ARG A 1 82  ? 38.899  -11.451 5.415   1.00 46.84  ? 83  ARG A CZ    1 
ATOM   659   N NH1   . ARG A 1 82  ? 38.931  -10.151 5.647   1.00 49.82  ? 83  ARG A NH1   1 
ATOM   660   N NH2   . ARG A 1 82  ? 38.572  -11.899 4.216   1.00 46.36  ? 83  ARG A NH2   1 
ATOM   661   N N     . ALA A 1 83  ? 38.976  -12.610 13.314  1.00 32.53  ? 84  ALA A N     1 
ATOM   662   C CA    . ALA A 1 83  ? 39.263  -12.151 14.663  1.00 32.33  ? 84  ALA A CA    1 
ATOM   663   C C     . ALA A 1 83  ? 39.262  -13.335 15.627  1.00 29.97  ? 84  ALA A C     1 
ATOM   664   O O     . ALA A 1 83  ? 39.864  -13.271 16.697  1.00 30.18  ? 84  ALA A O     1 
ATOM   665   C CB    . ALA A 1 83  ? 38.257  -11.097 15.074  1.00 33.87  ? 84  ALA A CB    1 
ATOM   666   N N     . GLY A 1 84  ? 38.568  -14.411 15.237  1.00 28.07  ? 85  GLY A N     1 
ATOM   667   C CA    . GLY A 1 84  ? 38.540  -15.635 16.019  1.00 28.46  ? 85  GLY A CA    1 
ATOM   668   C C     . GLY A 1 84  ? 37.183  -15.850 16.687  1.00 30.87  ? 85  GLY A C     1 
ATOM   669   O O     . GLY A 1 84  ? 37.073  -16.615 17.643  1.00 34.06  ? 85  GLY A O     1 
ATOM   670   N N     . LYS A 1 85  ? 36.152  -15.178 16.163  1.00 30.25  ? 86  LYS A N     1 
ATOM   671   C CA    . LYS A 1 85  ? 34.815  -15.262 16.725  1.00 34.71  ? 86  LYS A CA    1 
ATOM   672   C C     . LYS A 1 85  ? 34.049  -16.410 16.076  1.00 32.99  ? 86  LYS A C     1 
ATOM   673   O O     . LYS A 1 85  ? 34.046  -16.549 14.855  1.00 31.51  ? 86  LYS A O     1 
ATOM   674   C CB    . LYS A 1 85  ? 34.035  -13.962 16.497  1.00 37.96  ? 86  LYS A CB    1 
ATOM   675   C CG    . LYS A 1 85  ? 34.683  -12.697 17.036  1.00 38.22  ? 86  LYS A CG    1 
ATOM   676   C CD    . LYS A 1 85  ? 33.856  -11.442 16.783  1.00 41.26  ? 86  LYS A CD    1 
ATOM   677   C CE    . LYS A 1 85  ? 34.538  -10.195 17.245  1.00 41.68  ? 86  LYS A CE    1 
ATOM   678   N NZ    . LYS A 1 85  ? 34.833  -10.243 18.679  1.00 43.77  ? 86  LYS A NZ    1 
ATOM   679   N N     . LYS A 1 86  ? 33.393  -17.224 16.910  1.00 34.34  ? 87  LYS A N     1 
ATOM   680   C CA    . LYS A 1 86  ? 32.452  -18.218 16.423  1.00 33.92  ? 87  LYS A CA    1 
ATOM   681   C C     . LYS A 1 86  ? 31.258  -17.482 15.822  1.00 33.18  ? 87  LYS A C     1 
ATOM   682   O O     . LYS A 1 86  ? 30.311  -17.141 16.526  1.00 39.39  ? 87  LYS A O     1 
ATOM   683   C CB    . LYS A 1 86  ? 32.036  -19.165 17.555  1.00 32.79  ? 87  LYS A CB    1 
ATOM   684   C CG    . LYS A 1 86  ? 31.094  -20.287 17.141  1.00 34.19  ? 87  LYS A CG    1 
ATOM   685   C CD    . LYS A 1 86  ? 30.861  -21.336 18.222  1.00 37.18  ? 87  LYS A CD    1 
ATOM   686   C CE    . LYS A 1 86  ? 30.301  -20.757 19.481  1.00 39.89  ? 87  LYS A CE    1 
ATOM   687   N NZ    . LYS A 1 86  ? 30.088  -21.789 20.499  1.00 41.90  ? 87  LYS A NZ    1 
ATOM   688   N N     . THR A 1 87  ? 31.330  -17.231 14.511  1.00 31.42  ? 88  THR A N     1 
ATOM   689   C CA    . THR A 1 87  ? 30.406  -16.331 13.844  1.00 27.46  ? 88  THR A CA    1 
ATOM   690   C C     . THR A 1 87  ? 29.238  -17.123 13.265  1.00 28.37  ? 88  THR A C     1 
ATOM   691   O O     . THR A 1 87  ? 29.420  -18.217 12.734  1.00 29.11  ? 88  THR A O     1 
ATOM   692   C CB    . THR A 1 87  ? 31.157  -15.560 12.758  1.00 28.96  ? 88  THR A CB    1 
ATOM   693   O OG1   . THR A 1 87  ? 32.254  -14.941 13.423  1.00 25.23  ? 88  THR A OG1   1 
ATOM   694   C CG2   . THR A 1 87  ? 30.291  -14.514 12.080  1.00 29.28  ? 88  THR A CG2   1 
ATOM   695   N N     . VAL A 1 88  ? 28.038  -16.543 13.375  1.00 28.28  ? 89  VAL A N     1 
ATOM   696   C CA    . VAL A 1 88  ? 26.844  -17.107 12.770  1.00 27.04  ? 89  VAL A CA    1 
ATOM   697   C C     . VAL A 1 88  ? 26.210  -16.050 11.872  1.00 26.28  ? 89  VAL A C     1 
ATOM   698   O O     . VAL A 1 88  ? 26.032  -14.905 12.280  1.00 26.57  ? 89  VAL A O     1 
ATOM   699   C CB    . VAL A 1 88  ? 25.840  -17.608 13.827  1.00 28.25  ? 89  VAL A CB    1 
ATOM   700   C CG1   . VAL A 1 88  ? 24.460  -17.850 13.226  1.00 30.53  ? 89  VAL A CG1   1 
ATOM   701   C CG2   . VAL A 1 88  ? 26.346  -18.855 14.542  1.00 28.83  ? 89  VAL A CG2   1 
ATOM   702   N N     . CYS A 1 89  ? 25.887  -16.452 10.640  1.00 30.79  ? 90  CYS A N     1 
ATOM   703   C CA    . CYS A 1 89  ? 25.194  -15.586 9.702   1.00 32.34  ? 90  CYS A CA    1 
ATOM   704   C C     . CYS A 1 89  ? 23.728  -16.003 9.632   1.00 33.23  ? 90  CYS A C     1 
ATOM   705   O O     . CYS A 1 89  ? 23.419  -17.134 9.263   1.00 34.13  ? 90  CYS A O     1 
ATOM   706   C CB    . CYS A 1 89  ? 25.849  -15.636 8.326   1.00 37.81  ? 90  CYS A CB    1 
ATOM   707   S SG    . CYS A 1 89  ? 25.014  -14.611 7.087   1.00 52.20  ? 90  CYS A SG    1 
ATOM   708   N N     . ALA A 1 90  ? 22.836  -15.083 10.011  1.00 30.50  ? 91  ALA A N     1 
ATOM   709   C CA    . ALA A 1 90  ? 21.413  -15.369 10.061  1.00 29.17  ? 91  ALA A CA    1 
ATOM   710   C C     . ALA A 1 90  ? 20.686  -14.577 8.979   1.00 30.04  ? 91  ALA A C     1 
ATOM   711   O O     . ALA A 1 90  ? 20.497  -13.369 9.106   1.00 34.69  ? 91  ALA A O     1 
ATOM   712   C CB    . ALA A 1 90  ? 20.872  -15.052 11.438  1.00 28.87  ? 91  ALA A CB    1 
ATOM   713   N N     . LEU A 1 91  ? 20.289  -15.277 7.913   1.00 33.41  ? 92  LEU A N     1 
ATOM   714   C CA    . LEU A 1 91  ? 19.538  -14.671 6.828   1.00 35.18  ? 92  LEU A CA    1 
ATOM   715   C C     . LEU A 1 91  ? 18.131  -15.260 6.817   1.00 34.20  ? 92  LEU A C     1 
ATOM   716   O O     . LEU A 1 91  ? 17.929  -16.402 7.223   1.00 41.18  ? 92  LEU A O     1 
ATOM   717   C CB    . LEU A 1 91  ? 20.254  -14.900 5.497   1.00 37.86  ? 92  LEU A CB    1 
ATOM   718   C CG    . LEU A 1 91  ? 21.723  -14.468 5.441   1.00 40.39  ? 92  LEU A CG    1 
ATOM   719   C CD1   . LEU A 1 91  ? 22.248  -14.534 4.017   1.00 42.31  ? 92  LEU A CD1   1 
ATOM   720   C CD2   . LEU A 1 91  ? 21.915  -13.077 6.020   1.00 43.47  ? 92  LEU A CD2   1 
ATOM   721   N N     . TYR A 1 92  ? 17.164  -14.466 6.352   1.00 31.89  ? 93  TYR A N     1 
ATOM   722   C CA    . TYR A 1 92  ? 15.777  -14.895 6.324   1.00 32.95  ? 93  TYR A CA    1 
ATOM   723   C C     . TYR A 1 92  ? 15.625  -15.992 5.273   1.00 35.30  ? 93  TYR A C     1 
ATOM   724   O O     . TYR A 1 92  ? 16.384  -16.042 4.306   1.00 35.87  ? 93  TYR A O     1 
ATOM   725   C CB    . TYR A 1 92  ? 14.856  -13.700 6.057   1.00 34.09  ? 93  TYR A CB    1 
ATOM   726   C CG    . TYR A 1 92  ? 14.912  -13.151 4.638   1.00 32.97  ? 93  TYR A CG    1 
ATOM   727   C CD1   . TYR A 1 92  ? 15.893  -12.246 4.253   1.00 32.98  ? 93  TYR A CD1   1 
ATOM   728   C CD2   . TYR A 1 92  ? 13.968  -13.524 3.689   1.00 34.53  ? 93  TYR A CD2   1 
ATOM   729   C CE1   . TYR A 1 92  ? 15.944  -11.741 2.964   1.00 32.82  ? 93  TYR A CE1   1 
ATOM   730   C CE2   . TYR A 1 92  ? 14.005  -13.024 2.399   1.00 32.56  ? 93  TYR A CE2   1 
ATOM   731   C CZ    . TYR A 1 92  ? 14.995  -12.130 2.035   1.00 33.22  ? 93  TYR A CZ    1 
ATOM   732   O OH    . TYR A 1 92  ? 15.036  -11.635 0.763   1.00 39.78  ? 93  TYR A OH    1 
ATOM   733   N N     . GLY A 1 93  ? 14.640  -16.870 5.485   1.00 29.21  ? 94  GLY A N     1 
ATOM   734   C CA    . GLY A 1 93  ? 14.424  -18.009 4.609   1.00 31.16  ? 94  GLY A CA    1 
ATOM   735   C C     . GLY A 1 93  ? 15.642  -18.927 4.593   1.00 31.74  ? 94  GLY A C     1 
ATOM   736   O O     . GLY A 1 93  ? 16.256  -19.170 5.630   1.00 33.49  ? 94  GLY A O     1 
ATOM   737   N N     . HIS A 1 94  ? 15.982  -19.424 3.398   1.00 28.17  ? 95  HIS A N     1 
ATOM   738   C CA    . HIS A 1 94  ? 17.127  -20.300 3.215   1.00 29.63  ? 95  HIS A CA    1 
ATOM   739   C C     . HIS A 1 94  ? 18.351  -19.444 2.890   1.00 30.62  ? 95  HIS A C     1 
ATOM   740   O O     . HIS A 1 94  ? 18.309  -18.606 1.992   1.00 28.24  ? 95  HIS A O     1 
ATOM   741   C CB    . HIS A 1 94  ? 16.811  -21.351 2.143   1.00 30.01  ? 95  HIS A CB    1 
ATOM   742   C CG    . HIS A 1 94  ? 17.863  -22.394 1.956   1.00 31.93  ? 95  HIS A CG    1 
ATOM   743   N ND1   . HIS A 1 94  ? 19.215  -22.137 2.021   1.00 35.69  ? 95  HIS A ND1   1 
ATOM   744   C CD2   . HIS A 1 94  ? 17.748  -23.698 1.669   1.00 33.77  ? 95  HIS A CD2   1 
ATOM   745   C CE1   . HIS A 1 94  ? 19.884  -23.259 1.795   1.00 33.55  ? 95  HIS A CE1   1 
ATOM   746   N NE2   . HIS A 1 94  ? 19.012  -24.220 1.579   1.00 34.67  ? 95  HIS A NE2   1 
ATOM   747   N N     . PRO A 1 95  ? 19.478  -19.628 3.613   1.00 31.71  ? 96  PRO A N     1 
ATOM   748   C CA    . PRO A 1 95  ? 20.628  -18.730 3.482   1.00 33.75  ? 96  PRO A CA    1 
ATOM   749   C C     . PRO A 1 95  ? 21.386  -18.877 2.165   1.00 33.58  ? 96  PRO A C     1 
ATOM   750   O O     . PRO A 1 95  ? 22.278  -18.084 1.872   1.00 32.71  ? 96  PRO A O     1 
ATOM   751   C CB    . PRO A 1 95  ? 21.491  -19.124 4.696   1.00 31.13  ? 96  PRO A CB    1 
ATOM   752   C CG    . PRO A 1 95  ? 21.180  -20.590 4.905   1.00 30.03  ? 96  PRO A CG    1 
ATOM   753   C CD    . PRO A 1 95  ? 19.703  -20.716 4.576   1.00 29.14  ? 96  PRO A CD    1 
ATOM   754   N N     . GLY A 1 96  ? 21.014  -19.889 1.374   1.00 32.89  ? 97  GLY A N     1 
ATOM   755   C CA    . GLY A 1 96  ? 21.723  -20.195 0.143   1.00 34.50  ? 97  GLY A CA    1 
ATOM   756   C C     . GLY A 1 96  ? 20.793  -20.206 -1.068  1.00 34.90  ? 97  GLY A C     1 
ATOM   757   O O     . GLY A 1 96  ? 21.170  -20.682 -2.136  1.00 36.99  ? 97  GLY A O     1 
ATOM   758   N N     . VAL A 1 97  ? 19.579  -19.673 -0.892  1.00 34.14  ? 98  VAL A N     1 
ATOM   759   C CA    . VAL A 1 97  ? 18.615  -19.595 -1.978  1.00 37.10  ? 98  VAL A CA    1 
ATOM   760   C C     . VAL A 1 97  ? 18.499  -18.140 -2.422  1.00 37.91  ? 98  VAL A C     1 
ATOM   761   O O     . VAL A 1 97  ? 18.069  -17.284 -1.652  1.00 37.14  ? 98  VAL A O     1 
ATOM   762   C CB    . VAL A 1 97  ? 17.243  -20.170 -1.574  1.00 39.56  ? 98  VAL A CB    1 
ATOM   763   C CG1   . VAL A 1 97  ? 16.182  -19.903 -2.634  1.00 38.90  ? 98  VAL A CG1   1 
ATOM   764   C CG2   . VAL A 1 97  ? 17.325  -21.659 -1.261  1.00 38.70  ? 98  VAL A CG2   1 
ATOM   765   N N     . PHE A 1 98  ? 18.890  -17.879 -3.674  1.00 37.09  ? 99  PHE A N     1 
ATOM   766   C CA    . PHE A 1 98  ? 18.922  -16.527 -4.209  1.00 33.62  ? 99  PHE A CA    1 
ATOM   767   C C     . PHE A 1 98  ? 19.607  -15.613 -3.197  1.00 33.83  ? 99  PHE A C     1 
ATOM   768   O O     . PHE A 1 98  ? 19.187  -14.476 -2.990  1.00 30.06  ? 99  PHE A O     1 
ATOM   769   C CB    . PHE A 1 98  ? 17.501  -16.080 -4.564  1.00 31.84  ? 99  PHE A CB    1 
ATOM   770   C CG    . PHE A 1 98  ? 16.944  -16.718 -5.830  1.00 30.42  ? 99  PHE A CG    1 
ATOM   771   C CD1   . PHE A 1 98  ? 16.454  -18.019 -5.818  1.00 28.78  ? 99  PHE A CD1   1 
ATOM   772   C CD2   . PHE A 1 98  ? 16.901  -16.010 -7.027  1.00 29.99  ? 99  PHE A CD2   1 
ATOM   773   C CE1   . PHE A 1 98  ? 15.949  -18.597 -6.973  1.00 31.00  ? 99  PHE A CE1   1 
ATOM   774   C CE2   . PHE A 1 98  ? 16.389  -16.592 -8.176  1.00 31.21  ? 99  PHE A CE2   1 
ATOM   775   C CZ    . PHE A 1 98  ? 15.916  -17.882 -8.148  1.00 29.31  ? 99  PHE A CZ    1 
ATOM   776   N N     . ALA A 1 99  ? 20.668  -16.135 -2.574  1.00 37.73  ? 100 ALA A N     1 
ATOM   777   C CA    . ALA A 1 99  ? 21.464  -15.385 -1.616  1.00 39.80  ? 100 ALA A CA    1 
ATOM   778   C C     . ALA A 1 99  ? 22.936  -15.741 -1.800  1.00 44.71  ? 100 ALA A C     1 
ATOM   779   O O     . ALA A 1 99  ? 23.354  -16.854 -1.489  1.00 50.51  ? 100 ALA A O     1 
ATOM   780   C CB    . ALA A 1 99  ? 20.991  -15.679 -0.209  1.00 41.04  ? 100 ALA A CB    1 
ATOM   781   N N     . CYS A 1 100 ? 23.712  -14.778 -2.310  1.00 41.58  ? 101 CYS A N     1 
ATOM   782   C CA    . CYS A 1 100 ? 25.100  -15.014 -2.672  1.00 39.99  ? 101 CYS A CA    1 
ATOM   783   C C     . CYS A 1 100 ? 26.011  -14.769 -1.470  1.00 36.72  ? 101 CYS A C     1 
ATOM   784   O O     . CYS A 1 100 ? 27.080  -15.366 -1.367  1.00 34.04  ? 101 CYS A O     1 
ATOM   785   C CB    . CYS A 1 100 ? 25.516  -14.123 -3.837  1.00 42.40  ? 101 CYS A CB    1 
ATOM   786   S SG    . CYS A 1 100 ? 25.440  -12.353 -3.457  1.00 46.46  ? 101 CYS A SG    1 
ATOM   787   N N     . VAL A 1 101 ? 25.573  -13.887 -0.566  1.00 41.14  ? 102 VAL A N     1 
ATOM   788   C CA    . VAL A 1 101 ? 26.387  -13.476 0.567   1.00 37.29  ? 102 VAL A CA    1 
ATOM   789   C C     . VAL A 1 101 ? 26.928  -14.715 1.277   1.00 33.68  ? 102 VAL A C     1 
ATOM   790   O O     . VAL A 1 101 ? 28.133  -14.834 1.492   1.00 37.50  ? 102 VAL A O     1 
ATOM   791   C CB    . VAL A 1 101 ? 25.594  -12.581 1.538   1.00 39.25  ? 102 VAL A CB    1 
ATOM   792   C CG1   . VAL A 1 101 ? 26.375  -12.302 2.816   1.00 36.95  ? 102 VAL A CG1   1 
ATOM   793   C CG2   . VAL A 1 101 ? 25.157  -11.278 0.879   1.00 42.70  ? 102 VAL A CG2   1 
ATOM   794   N N     . SER A 1 102 ? 26.023  -15.631 1.638   1.00 31.80  ? 103 SER A N     1 
ATOM   795   C CA    . SER A 1 102 ? 26.381  -16.810 2.410   1.00 36.57  ? 103 SER A CA    1 
ATOM   796   C C     . SER A 1 102 ? 27.366  -17.677 1.629   1.00 34.97  ? 103 SER A C     1 
ATOM   797   O O     . SER A 1 102 ? 28.394  -18.087 2.162   1.00 36.65  ? 103 SER A O     1 
ATOM   798   C CB    . SER A 1 102 ? 25.154  -17.596 2.800   1.00 41.82  ? 103 SER A CB    1 
ATOM   799   O OG    . SER A 1 102 ? 24.280  -16.813 3.601   1.00 48.24  ? 103 SER A OG    1 
ATOM   800   N N     . HIS A 1 103 ? 27.034  -17.957 0.364   1.00 33.72  ? 104 HIS A N     1 
ATOM   801   C CA    . HIS A 1 103 ? 27.882  -18.775 -0.486  1.00 30.56  ? 104 HIS A CA    1 
ATOM   802   C C     . HIS A 1 103 ? 29.266  -18.138 -0.585  1.00 27.35  ? 104 HIS A C     1 
ATOM   803   O O     . HIS A 1 103 ? 30.280  -18.823 -0.466  1.00 24.21  ? 104 HIS A O     1 
ATOM   804   C CB    . HIS A 1 103 ? 27.249  -18.969 -1.869  1.00 30.62  ? 104 HIS A CB    1 
ATOM   805   C CG    . HIS A 1 103 ? 26.028  -19.831 -1.869  1.00 25.57  ? 104 HIS A CG    1 
ATOM   806   N ND1   . HIS A 1 103 ? 26.090  -21.208 -1.842  1.00 24.46  ? 104 HIS A ND1   1 
ATOM   807   C CD2   . HIS A 1 103 ? 24.727  -19.520 -1.888  1.00 24.93  ? 104 HIS A CD2   1 
ATOM   808   C CE1   . HIS A 1 103 ? 24.860  -21.701 -1.848  1.00 26.13  ? 104 HIS A CE1   1 
ATOM   809   N NE2   . HIS A 1 103 ? 24.016  -20.693 -1.876  1.00 25.66  ? 104 HIS A NE2   1 
ATOM   810   N N     . MET A 1 104 ? 29.293  -16.820 -0.803  1.00 26.19  ? 105 MET A N     1 
ATOM   811   C CA    . MET A 1 104 ? 30.541  -16.093 -0.969  1.00 29.76  ? 105 MET A CA    1 
ATOM   812   C C     . MET A 1 104 ? 31.359  -16.172 0.317   1.00 29.15  ? 105 MET A C     1 
ATOM   813   O O     . MET A 1 104 ? 32.555  -16.450 0.278   1.00 29.91  ? 105 MET A O     1 
ATOM   814   C CB    . MET A 1 104 ? 30.281  -14.626 -1.331  1.00 32.42  ? 105 MET A CB    1 
ATOM   815   C CG    . MET A 1 104 ? 29.806  -14.420 -2.759  1.00 34.75  ? 105 MET A CG    1 
ATOM   816   S SD    . MET A 1 104 ? 29.300  -12.723 -3.103  1.00 41.61  ? 105 MET A SD    1 
ATOM   817   C CE    . MET A 1 104 ? 30.857  -11.834 -2.967  1.00 42.23  ? 105 MET A CE    1 
ATOM   818   N N     . ALA A 1 105 ? 30.697  -15.929 1.453   1.00 28.27  ? 106 ALA A N     1 
ATOM   819   C CA    . ALA A 1 105 ? 31.364  -15.909 2.744   1.00 29.38  ? 106 ALA A CA    1 
ATOM   820   C C     . ALA A 1 105 ? 32.004  -17.267 3.022   1.00 29.03  ? 106 ALA A C     1 
ATOM   821   O O     . ALA A 1 105 ? 33.181  -17.342 3.367   1.00 29.89  ? 106 ALA A O     1 
ATOM   822   C CB    . ALA A 1 105 ? 30.381  -15.526 3.829   1.00 31.69  ? 106 ALA A CB    1 
ATOM   823   N N     . ILE A 1 106 ? 31.214  -18.334 2.868   1.00 29.73  ? 107 ILE A N     1 
ATOM   824   C CA    . ILE A 1 106 ? 31.682  -19.684 3.139   1.00 28.24  ? 107 ILE A CA    1 
ATOM   825   C C     . ILE A 1 106 ? 32.868  -19.996 2.229   1.00 28.68  ? 107 ILE A C     1 
ATOM   826   O O     . ILE A 1 106 ? 33.867  -20.556 2.675   1.00 31.00  ? 107 ILE A O     1 
ATOM   827   C CB    . ILE A 1 106 ? 30.543  -20.706 2.969   1.00 28.23  ? 107 ILE A CB    1 
ATOM   828   C CG1   . ILE A 1 106 ? 29.471  -20.535 4.046   1.00 27.28  ? 107 ILE A CG1   1 
ATOM   829   C CG2   . ILE A 1 106 ? 31.089  -22.134 2.942   1.00 29.50  ? 107 ILE A CG2   1 
ATOM   830   C CD1   . ILE A 1 106 ? 28.324  -21.524 3.946   1.00 25.55  ? 107 ILE A CD1   1 
ATOM   831   N N     . THR A 1 107 ? 32.742  -19.626 0.951   1.00 30.03  ? 108 THR A N     1 
ATOM   832   C CA    . THR A 1 107 ? 33.789  -19.870 -0.027  1.00 31.14  ? 108 THR A CA    1 
ATOM   833   C C     . THR A 1 107 ? 35.087  -19.225 0.449   1.00 31.70  ? 108 THR A C     1 
ATOM   834   O O     . THR A 1 107 ? 36.130  -19.873 0.492   1.00 33.24  ? 108 THR A O     1 
ATOM   835   C CB    . THR A 1 107 ? 33.355  -19.321 -1.385  1.00 33.34  ? 108 THR A CB    1 
ATOM   836   O OG1   . THR A 1 107 ? 32.245  -20.123 -1.775  1.00 32.39  ? 108 THR A OG1   1 
ATOM   837   C CG2   . THR A 1 107 ? 34.454  -19.406 -2.428  1.00 37.53  ? 108 THR A CG2   1 
ATOM   838   N N     . ARG A 1 108 ? 35.004  -17.941 0.808   1.00 31.25  ? 109 ARG A N     1 
ATOM   839   C CA    . ARG A 1 108 ? 36.176  -17.158 1.160   1.00 32.56  ? 109 ARG A CA    1 
ATOM   840   C C     . ARG A 1 108 ? 36.758  -17.666 2.477   1.00 31.35  ? 109 ARG A C     1 
ATOM   841   O O     . ARG A 1 108 ? 37.975  -17.729 2.637   1.00 33.85  ? 109 ARG A O     1 
ATOM   842   C CB    . ARG A 1 108 ? 35.802  -15.674 1.240   1.00 34.56  ? 109 ARG A CB    1 
ATOM   843   C CG    . ARG A 1 108 ? 36.993  -14.734 1.351   1.00 39.01  ? 109 ARG A CG    1 
ATOM   844   C CD    . ARG A 1 108 ? 36.581  -13.275 1.243   1.00 42.42  ? 109 ARG A CD    1 
ATOM   845   N NE    . ARG A 1 108 ? 35.870  -12.998 -0.010  1.00 44.41  ? 109 ARG A NE    1 
ATOM   846   C CZ    . ARG A 1 108 ? 35.449  -11.798 -0.390  1.00 44.60  ? 109 ARG A CZ    1 
ATOM   847   N NH1   . ARG A 1 108 ? 35.682  -10.744 0.371   1.00 44.69  ? 109 ARG A NH1   1 
ATOM   848   N NH2   . ARG A 1 108 ? 34.803  -11.657 -1.534  1.00 44.19  ? 109 ARG A NH2   1 
ATOM   849   N N     . ALA A 1 109 ? 35.875  -18.027 3.414   1.00 29.86  ? 110 ALA A N     1 
ATOM   850   C CA    . ALA A 1 109 ? 36.294  -18.509 4.720   1.00 31.16  ? 110 ALA A CA    1 
ATOM   851   C C     . ALA A 1 109 ? 37.131  -19.777 4.564   1.00 31.50  ? 110 ALA A C     1 
ATOM   852   O O     . ALA A 1 109 ? 38.153  -19.935 5.225   1.00 31.40  ? 110 ALA A O     1 
ATOM   853   C CB    . ALA A 1 109 ? 35.084  -18.749 5.595   1.00 34.82  ? 110 ALA A CB    1 
ATOM   854   N N     . LYS A 1 110 ? 36.679  -20.674 3.681   1.00 34.51  ? 111 LYS A N     1 
ATOM   855   C CA    . LYS A 1 110 ? 37.370  -21.930 3.433   1.00 38.69  ? 111 LYS A CA    1 
ATOM   856   C C     . LYS A 1 110 ? 38.745  -21.650 2.835   1.00 37.80  ? 111 LYS A C     1 
ATOM   857   O O     . LYS A 1 110 ? 39.728  -22.288 3.204   1.00 35.11  ? 111 LYS A O     1 
ATOM   858   C CB    . LYS A 1 110 ? 36.560  -22.825 2.489   1.00 38.00  ? 111 LYS A CB    1 
ATOM   859   C CG    . LYS A 1 110 ? 35.308  -23.450 3.087   1.00 38.67  ? 111 LYS A CG    1 
ATOM   860   C CD    . LYS A 1 110 ? 34.522  -24.301 2.096   1.00 40.56  ? 111 LYS A CD    1 
ATOM   861   C CE    . LYS A 1 110 ? 33.397  -25.049 2.736   1.00 42.23  ? 111 LYS A CE    1 
ATOM   862   N NZ    . LYS A 1 110 ? 33.885  -26.035 3.704   1.00 45.58  ? 111 LYS A NZ    1 
ATOM   863   N N     . ALA A 1 111 ? 38.796  -20.693 1.902   1.00 42.53  ? 112 ALA A N     1 
ATOM   864   C CA    . ALA A 1 111 ? 40.020  -20.374 1.187   1.00 40.86  ? 112 ALA A CA    1 
ATOM   865   C C     . ALA A 1 111 ? 41.075  -19.850 2.158   1.00 39.74  ? 112 ALA A C     1 
ATOM   866   O O     . ALA A 1 111 ? 42.270  -19.946 1.890   1.00 41.06  ? 112 ALA A O     1 
ATOM   867   C CB    . ALA A 1 111 ? 39.730  -19.371 0.092   1.00 39.89  ? 112 ALA A CB    1 
ATOM   868   N N     . GLU A 1 112 ? 40.618  -19.294 3.285   1.00 37.63  ? 113 GLU A N     1 
ATOM   869   C CA    . GLU A 1 112 ? 41.515  -18.737 4.284   1.00 37.52  ? 113 GLU A CA    1 
ATOM   870   C C     . GLU A 1 112 ? 41.749  -19.769 5.385   1.00 36.65  ? 113 GLU A C     1 
ATOM   871   O O     . GLU A 1 112 ? 42.456  -19.501 6.354   1.00 36.01  ? 113 GLU A O     1 
ATOM   872   C CB    . GLU A 1 112 ? 40.950  -17.423 4.826   1.00 44.36  ? 113 GLU A CB    1 
ATOM   873   C CG    . GLU A 1 112 ? 40.763  -16.362 3.745   1.00 48.01  ? 113 GLU A CG    1 
ATOM   874   C CD    . GLU A 1 112 ? 40.281  -15.016 4.253   1.00 50.75  ? 113 GLU A CD    1 
ATOM   875   O OE1   . GLU A 1 112 ? 40.117  -14.868 5.482   1.00 53.16  ? 113 GLU A OE1   1 
ATOM   876   O OE2   . GLU A 1 112 ? 40.067  -14.113 3.415   1.00 48.21  ? 113 GLU A OE2   1 
ATOM   877   N N     . GLY A 1 113 ? 41.146  -20.951 5.217   1.00 34.68  ? 114 GLY A N     1 
ATOM   878   C CA    . GLY A 1 113 ? 41.415  -22.088 6.081   1.00 33.67  ? 114 GLY A CA    1 
ATOM   879   C C     . GLY A 1 113 ? 40.572  -22.056 7.352   1.00 32.13  ? 114 GLY A C     1 
ATOM   880   O O     . GLY A 1 113 ? 40.996  -22.556 8.392   1.00 28.15  ? 114 GLY A O     1 
ATOM   881   N N     . PHE A 1 114 ? 39.371  -21.477 7.255   1.00 28.77  ? 115 PHE A N     1 
ATOM   882   C CA    . PHE A 1 114 ? 38.455  -21.436 8.382   1.00 30.67  ? 115 PHE A CA    1 
ATOM   883   C C     . PHE A 1 114 ? 37.350  -22.464 8.170   1.00 32.40  ? 115 PHE A C     1 
ATOM   884   O O     . PHE A 1 114 ? 36.963  -22.748 7.038   1.00 28.64  ? 115 PHE A O     1 
ATOM   885   C CB    . PHE A 1 114 ? 37.849  -20.043 8.578   1.00 29.80  ? 115 PHE A CB    1 
ATOM   886   C CG    . PHE A 1 114 ? 38.856  -18.963 8.950   1.00 28.62  ? 115 PHE A CG    1 
ATOM   887   C CD1   . PHE A 1 114 ? 39.495  -18.982 10.184  1.00 26.77  ? 115 PHE A CD1   1 
ATOM   888   C CD2   . PHE A 1 114 ? 39.132  -17.913 8.081   1.00 28.38  ? 115 PHE A CD2   1 
ATOM   889   C CE1   . PHE A 1 114 ? 40.408  -17.996 10.524  1.00 29.18  ? 115 PHE A CE1   1 
ATOM   890   C CE2   . PHE A 1 114 ? 40.041  -16.926 8.430   1.00 27.79  ? 115 PHE A CE2   1 
ATOM   891   C CZ    . PHE A 1 114 ? 40.676  -16.970 9.648   1.00 27.54  ? 115 PHE A CZ    1 
ATOM   892   N N     . SER A 1 115 ? 36.859  -23.020 9.280   1.00 30.54  ? 116 SER A N     1 
ATOM   893   C CA    . SER A 1 115 ? 35.686  -23.874 9.254   1.00 39.12  ? 116 SER A CA    1 
ATOM   894   C C     . SER A 1 115 ? 34.468  -23.032 8.886   1.00 35.40  ? 116 SER A C     1 
ATOM   895   O O     . SER A 1 115 ? 34.205  -22.008 9.513   1.00 34.05  ? 116 SER A O     1 
ATOM   896   C CB    . SER A 1 115 ? 35.494  -24.577 10.575  1.00 41.94  ? 116 SER A CB    1 
ATOM   897   O OG    . SER A 1 115 ? 34.367  -25.441 10.534  1.00 46.31  ? 116 SER A OG    1 
ATOM   898   N N     . ALA A 1 116 ? 33.753  -23.463 7.844   1.00 31.66  ? 117 ALA A N     1 
ATOM   899   C CA    . ALA A 1 116 ? 32.569  -22.763 7.378   1.00 29.53  ? 117 ALA A CA    1 
ATOM   900   C C     . ALA A 1 116 ? 31.596  -23.763 6.761   1.00 27.06  ? 117 ALA A C     1 
ATOM   901   O O     . ALA A 1 116 ? 32.001  -24.652 6.017   1.00 25.00  ? 117 ALA A O     1 
ATOM   902   C CB    . ALA A 1 116 ? 32.959  -21.687 6.390   1.00 30.01  ? 117 ALA A CB    1 
ATOM   903   N N     . LYS A 1 117 ? 30.310  -23.611 7.092   1.00 26.27  ? 118 LYS A N     1 
ATOM   904   C CA    . LYS A 1 117 ? 29.276  -24.477 6.552   1.00 27.70  ? 118 LYS A CA    1 
ATOM   905   C C     . LYS A 1 117 ? 27.955  -23.718 6.504   1.00 24.91  ? 118 LYS A C     1 
ATOM   906   O O     . LYS A 1 117 ? 27.833  -22.630 7.062   1.00 28.73  ? 118 LYS A O     1 
ATOM   907   C CB    . LYS A 1 117 ? 29.138  -25.758 7.382   1.00 28.10  ? 118 LYS A CB    1 
ATOM   908   C CG    . LYS A 1 117 ? 28.707  -25.556 8.826   1.00 28.40  ? 118 LYS A CG    1 
ATOM   909   C CD    . LYS A 1 117 ? 28.481  -26.859 9.582   1.00 31.62  ? 118 LYS A CD    1 
ATOM   910   C CE    . LYS A 1 117 ? 28.035  -26.639 10.994  1.00 32.68  ? 118 LYS A CE    1 
ATOM   911   N NZ    . LYS A 1 117 ? 27.854  -27.907 11.706  1.00 30.47  ? 118 LYS A NZ    1 
ATOM   912   N N     . MET A 1 118 ? 26.978  -24.309 5.815   1.00 25.84  ? 119 MET A N     1 
ATOM   913   C CA    . MET A 1 118 ? 25.665  -23.712 5.657   1.00 28.55  ? 119 MET A CA    1 
ATOM   914   C C     . MET A 1 118 ? 24.607  -24.716 6.101   1.00 32.82  ? 119 MET A C     1 
ATOM   915   O O     . MET A 1 118 ? 24.637  -25.875 5.694   1.00 37.23  ? 119 MET A O     1 
ATOM   916   C CB    . MET A 1 118 ? 25.424  -23.315 4.196   1.00 30.75  ? 119 MET A CB    1 
ATOM   917   C CG    . MET A 1 118 ? 24.014  -22.835 3.904   1.00 31.45  ? 119 MET A CG    1 
ATOM   918   S SD    . MET A 1 118 ? 23.766  -22.442 2.160   1.00 31.96  ? 119 MET A SD    1 
ATOM   919   C CE    . MET A 1 118 ? 25.054  -21.215 1.904   1.00 34.85  ? 119 MET A CE    1 
ATOM   920   N N     . GLU A 1 119 ? 23.686  -24.255 6.953   1.00 31.64  ? 120 GLU A N     1 
ATOM   921   C CA    . GLU A 1 119 ? 22.565  -25.068 7.393   1.00 30.42  ? 120 GLU A CA    1 
ATOM   922   C C     . GLU A 1 119 ? 21.329  -24.676 6.591   1.00 30.40  ? 120 GLU A C     1 
ATOM   923   O O     . GLU A 1 119 ? 21.005  -23.496 6.476   1.00 29.41  ? 120 GLU A O     1 
ATOM   924   C CB    . GLU A 1 119 ? 22.326  -24.895 8.894   1.00 30.03  ? 120 GLU A CB    1 
ATOM   925   C CG    . GLU A 1 119 ? 23.433  -25.493 9.757   1.00 34.47  ? 120 GLU A CG    1 
ATOM   926   C CD    . GLU A 1 119 ? 23.505  -27.009 9.714   1.00 39.26  ? 120 GLU A CD    1 
ATOM   927   O OE1   . GLU A 1 119 ? 22.614  -27.626 9.092   1.00 40.78  ? 120 GLU A OE1   1 
ATOM   928   O OE2   . GLU A 1 119 ? 24.455  -27.573 10.299  1.00 44.41  ? 120 GLU A OE2   1 
ATOM   929   N N     . PRO A 1 120 ? 20.601  -25.655 6.011   1.00 26.63  ? 121 PRO A N     1 
ATOM   930   C CA    . PRO A 1 120 ? 19.434  -25.353 5.183   1.00 27.25  ? 121 PRO A CA    1 
ATOM   931   C C     . PRO A 1 120 ? 18.283  -24.761 5.993   1.00 26.80  ? 121 PRO A C     1 
ATOM   932   O O     . PRO A 1 120 ? 18.106  -25.084 7.166   1.00 22.03  ? 121 PRO A O     1 
ATOM   933   C CB    . PRO A 1 120 ? 19.080  -26.719 4.566   1.00 28.70  ? 121 PRO A CB    1 
ATOM   934   C CG    . PRO A 1 120 ? 19.599  -27.725 5.573   1.00 29.98  ? 121 PRO A CG    1 
ATOM   935   C CD    . PRO A 1 120 ? 20.863  -27.097 6.135   1.00 27.02  ? 121 PRO A CD    1 
ATOM   936   N N     . GLY A 1 121 ? 17.512  -23.883 5.346   1.00 25.51  ? 122 GLY A N     1 
ATOM   937   C CA    . GLY A 1 121 ? 16.352  -23.268 5.967   1.00 27.24  ? 122 GLY A CA    1 
ATOM   938   C C     . GLY A 1 121 ? 15.134  -23.358 5.053   1.00 25.35  ? 122 GLY A C     1 
ATOM   939   O O     . GLY A 1 121 ? 15.220  -23.891 3.949   1.00 25.49  ? 122 GLY A O     1 
ATOM   940   N N     . ILE A 1 122 ? 14.005  -22.830 5.533   1.00 26.56  ? 123 ILE A N     1 
ATOM   941   C CA    . ILE A 1 122 ? 12.767  -22.822 4.773   1.00 26.63  ? 123 ILE A CA    1 
ATOM   942   C C     . ILE A 1 122 ? 12.720  -21.551 3.929   1.00 28.38  ? 123 ILE A C     1 
ATOM   943   O O     . ILE A 1 122 ? 12.669  -20.447 4.467   1.00 30.80  ? 123 ILE A O     1 
ATOM   944   C CB    . ILE A 1 122 ? 11.558  -22.935 5.721   1.00 30.05  ? 123 ILE A CB    1 
ATOM   945   C CG1   . ILE A 1 122 ? 11.644  -24.198 6.583   1.00 29.82  ? 123 ILE A CG1   1 
ATOM   946   C CG2   . ILE A 1 122 ? 10.243  -22.866 4.945   1.00 31.57  ? 123 ILE A CG2   1 
ATOM   947   C CD1   . ILE A 1 122 ? 10.609  -24.269 7.691   1.00 28.06  ? 123 ILE A CD1   1 
ATOM   948   N N     . SER A 1 123 ? 12.740  -21.724 2.602   1.00 26.18  ? 124 SER A N     1 
ATOM   949   C CA    . SER A 1 123 ? 12.767  -20.605 1.674   1.00 27.90  ? 124 SER A CA    1 
ATOM   950   C C     . SER A 1 123 ? 11.344  -20.164 1.341   1.00 29.95  ? 124 SER A C     1 
ATOM   951   O O     . SER A 1 123 ? 10.378  -20.798 1.761   1.00 33.39  ? 124 SER A O     1 
ATOM   952   C CB    . SER A 1 123 ? 13.531  -20.957 0.421   1.00 28.75  ? 124 SER A CB    1 
ATOM   953   O OG    . SER A 1 123 ? 12.843  -21.942 -0.339  1.00 32.71  ? 124 SER A OG    1 
ATOM   954   N N     . ALA A 1 124 ? 11.238  -19.075 0.571   1.00 28.43  ? 125 ALA A N     1 
ATOM   955   C CA    . ALA A 1 124 ? 9.953   -18.546 0.144   1.00 29.92  ? 125 ALA A CA    1 
ATOM   956   C C     . ALA A 1 124 ? 9.275   -19.538 -0.795  1.00 29.91  ? 125 ALA A C     1 
ATOM   957   O O     . ALA A 1 124 ? 8.051   -19.558 -0.913  1.00 28.59  ? 125 ALA A O     1 
ATOM   958   C CB    . ALA A 1 124 ? 10.145  -17.199 -0.519  1.00 31.74  ? 125 ALA A CB    1 
ATOM   959   N N     . GLU A 1 125 ? 10.095  -20.355 -1.463  1.00 30.55  ? 126 GLU A N     1 
ATOM   960   C CA    . GLU A 1 125 ? 9.604   -21.386 -2.361  1.00 33.20  ? 126 GLU A CA    1 
ATOM   961   C C     . GLU A 1 125 ? 8.897   -22.465 -1.545  1.00 30.82  ? 126 GLU A C     1 
ATOM   962   O O     . GLU A 1 125 ? 7.788   -22.876 -1.878  1.00 31.35  ? 126 GLU A O     1 
ATOM   963   C CB    . GLU A 1 125 ? 10.774  -21.966 -3.155  1.00 38.42  ? 126 GLU A CB    1 
ATOM   964   C CG    . GLU A 1 125 ? 10.370  -23.081 -4.114  1.00 41.45  ? 126 GLU A CG    1 
ATOM   965   C CD    . GLU A 1 125 ? 11.550  -23.804 -4.737  1.00 47.98  ? 126 GLU A CD    1 
ATOM   966   O OE1   . GLU A 1 125 ? 12.384  -23.132 -5.381  1.00 49.23  ? 126 GLU A OE1   1 
ATOM   967   O OE2   . GLU A 1 125 ? 11.636  -25.040 -4.576  1.00 55.29  ? 126 GLU A OE2   1 
ATOM   968   N N     . ALA A 1 126 ? 9.557   -22.909 -0.471  1.00 29.58  ? 127 ALA A N     1 
ATOM   969   C CA    . ALA A 1 126 ? 9.007   -23.921 0.416   1.00 28.63  ? 127 ALA A CA    1 
ATOM   970   C C     . ALA A 1 126 ? 7.640   -23.473 0.930   1.00 26.70  ? 127 ALA A C     1 
ATOM   971   O O     . ALA A 1 126 ? 6.710   -24.272 1.014   1.00 26.51  ? 127 ALA A O     1 
ATOM   972   C CB    . ALA A 1 126 ? 9.970   -24.183 1.553   1.00 30.08  ? 127 ALA A CB    1 
ATOM   973   N N     . CYS A 1 127 ? 7.536   -22.183 1.266   1.00 23.77  ? 128 CYS A N     1 
ATOM   974   C CA    . CYS A 1 127 ? 6.308   -21.616 1.800   1.00 23.70  ? 128 CYS A CA    1 
ATOM   975   C C     . CYS A 1 127 ? 5.227   -21.588 0.722   1.00 25.75  ? 128 CYS A C     1 
ATOM   976   O O     . CYS A 1 127 ? 4.044   -21.732 1.022   1.00 26.79  ? 128 CYS A O     1 
ATOM   977   C CB    . CYS A 1 127 ? 6.543   -20.208 2.336   1.00 25.05  ? 128 CYS A CB    1 
ATOM   978   S SG    . CYS A 1 127 ? 7.659   -20.146 3.764   1.00 30.54  ? 128 CYS A SG    1 
ATOM   979   N N     . LEU A 1 128 ? 5.647   -21.394 -0.532  1.00 27.75  ? 129 LEU A N     1 
ATOM   980   C CA    . LEU A 1 128 ? 4.720   -21.245 -1.642  1.00 28.87  ? 129 LEU A CA    1 
ATOM   981   C C     . LEU A 1 128 ? 3.950   -22.547 -1.847  1.00 27.22  ? 129 LEU A C     1 
ATOM   982   O O     . LEU A 1 128 ? 2.722   -22.552 -1.861  1.00 26.77  ? 129 LEU A O     1 
ATOM   983   C CB    . LEU A 1 128 ? 5.493   -20.837 -2.896  1.00 31.17  ? 129 LEU A CB    1 
ATOM   984   C CG    . LEU A 1 128 ? 4.651   -20.568 -4.147  1.00 33.61  ? 129 LEU A CG    1 
ATOM   985   C CD1   . LEU A 1 128 ? 5.508   -19.991 -5.263  1.00 35.80  ? 129 LEU A CD1   1 
ATOM   986   C CD2   . LEU A 1 128 ? 3.950   -21.830 -4.615  1.00 32.25  ? 129 LEU A CD2   1 
ATOM   987   N N     . TRP A 1 129 ? 4.690   -23.649 -2.003  1.00 27.58  ? 130 TRP A N     1 
ATOM   988   C CA    . TRP A 1 129 ? 4.091   -24.951 -2.246  1.00 26.27  ? 130 TRP A CA    1 
ATOM   989   C C     . TRP A 1 129 ? 2.986   -25.215 -1.227  1.00 27.09  ? 130 TRP A C     1 
ATOM   990   O O     . TRP A 1 129 ? 1.903   -25.673 -1.586  1.00 23.67  ? 130 TRP A O     1 
ATOM   991   C CB    . TRP A 1 129 ? 5.165   -26.047 -2.193  1.00 27.66  ? 130 TRP A CB    1 
ATOM   992   C CG    . TRP A 1 129 ? 6.309   -25.830 -3.150  1.00 29.38  ? 130 TRP A CG    1 
ATOM   993   C CD1   . TRP A 1 129 ? 7.637   -25.997 -2.886  1.00 30.95  ? 130 TRP A CD1   1 
ATOM   994   C CD2   . TRP A 1 129 ? 6.223   -25.420 -4.533  1.00 27.09  ? 130 TRP A CD2   1 
ATOM   995   N NE1   . TRP A 1 129 ? 8.383   -25.707 -3.997  1.00 31.30  ? 130 TRP A NE1   1 
ATOM   996   C CE2   . TRP A 1 129 ? 7.546   -25.355 -5.023  1.00 30.50  ? 130 TRP A CE2   1 
ATOM   997   C CE3   . TRP A 1 129 ? 5.169   -25.103 -5.397  1.00 27.87  ? 130 TRP A CE3   1 
ATOM   998   C CZ2   . TRP A 1 129 ? 7.834   -24.986 -6.335  1.00 28.28  ? 130 TRP A CZ2   1 
ATOM   999   C CZ3   . TRP A 1 129 ? 5.458   -24.741 -6.695  1.00 29.94  ? 130 TRP A CZ3   1 
ATOM   1000  C CH2   . TRP A 1 129 ? 6.772   -24.686 -7.155  1.00 26.29  ? 130 TRP A CH2   1 
ATOM   1001  N N     . ALA A 1 130 ? 3.273   -24.911 0.045   1.00 25.94  ? 131 ALA A N     1 
ATOM   1002  C CA    . ALA A 1 130 ? 2.367   -25.222 1.139   1.00 28.11  ? 131 ALA A CA    1 
ATOM   1003  C C     . ALA A 1 130 ? 1.143   -24.310 1.091   1.00 29.07  ? 131 ALA A C     1 
ATOM   1004  O O     . ALA A 1 130 ? 0.014   -24.778 1.209   1.00 29.46  ? 131 ALA A O     1 
ATOM   1005  C CB    . ALA A 1 130 ? 3.096   -25.101 2.461   1.00 26.90  ? 131 ALA A CB    1 
ATOM   1006  N N     . ASP A 1 131 ? 1.384   -23.006 0.914   1.00 31.21  ? 132 ASP A N     1 
ATOM   1007  C CA    . ASP A 1 131 ? 0.325   -22.012 0.957   1.00 32.04  ? 132 ASP A CA    1 
ATOM   1008  C C     . ASP A 1 131 ? -0.624  -22.210 -0.224  1.00 34.56  ? 132 ASP A C     1 
ATOM   1009  O O     . ASP A 1 131 ? -1.838  -22.093 -0.070  1.00 34.83  ? 132 ASP A O     1 
ATOM   1010  C CB    . ASP A 1 131 ? 0.891   -20.601 1.006   1.00 33.31  ? 132 ASP A CB    1 
ATOM   1011  C CG    . ASP A 1 131 ? 1.637   -20.241 2.283   1.00 36.41  ? 132 ASP A CG    1 
ATOM   1012  O OD1   . ASP A 1 131 ? 1.748   -21.117 3.166   1.00 46.90  ? 132 ASP A OD1   1 
ATOM   1013  O OD2   . ASP A 1 131 ? 2.098   -19.084 2.387   1.00 39.72  ? 132 ASP A OD2   1 
ATOM   1014  N N     . LEU A 1 132 ? -0.062  -22.499 -1.402  1.00 34.24  ? 133 LEU A N     1 
ATOM   1015  C CA    . LEU A 1 132 ? -0.862  -22.665 -2.606  1.00 37.41  ? 133 LEU A CA    1 
ATOM   1016  C C     . LEU A 1 132 ? -1.266  -24.129 -2.757  1.00 38.64  ? 133 LEU A C     1 
ATOM   1017  O O     . LEU A 1 132 ? -2.115  -24.459 -3.582  1.00 39.14  ? 133 LEU A O     1 
ATOM   1018  C CB    . LEU A 1 132 ? -0.099  -22.169 -3.833  1.00 39.60  ? 133 LEU A CB    1 
ATOM   1019  C CG    . LEU A 1 132 ? 0.086   -20.652 -3.941  1.00 42.68  ? 133 LEU A CG    1 
ATOM   1020  C CD1   . LEU A 1 132 ? 1.049   -20.139 -2.885  1.00 43.89  ? 133 LEU A CD1   1 
ATOM   1021  C CD2   . LEU A 1 132 ? 0.552   -20.260 -5.332  1.00 46.10  ? 133 LEU A CD2   1 
ATOM   1022  N N     . GLY A 1 133 ? -0.655  -24.998 -1.947  1.00 36.85  ? 134 GLY A N     1 
ATOM   1023  C CA    . GLY A 1 133 ? -0.918  -26.425 -2.021  1.00 42.13  ? 134 GLY A CA    1 
ATOM   1024  C C     . GLY A 1 133 ? -0.563  -26.975 -3.399  1.00 40.43  ? 134 GLY A C     1 
ATOM   1025  O O     . GLY A 1 133 ? -1.374  -27.644 -4.035  1.00 36.80  ? 134 GLY A O     1 
ATOM   1026  N N     . ILE A 1 134 ? 0.658   -26.666 -3.849  1.00 40.45  ? 135 ILE A N     1 
ATOM   1027  C CA    . ILE A 1 134 ? 1.162   -27.143 -5.126  1.00 37.00  ? 135 ILE A CA    1 
ATOM   1028  C C     . ILE A 1 134 ? 2.413   -27.979 -4.875  1.00 34.50  ? 135 ILE A C     1 
ATOM   1029  O O     . ILE A 1 134 ? 3.301   -27.566 -4.133  1.00 31.29  ? 135 ILE A O     1 
ATOM   1030  C CB    . ILE A 1 134 ? 1.456   -25.967 -6.076  1.00 38.06  ? 135 ILE A CB    1 
ATOM   1031  C CG1   . ILE A 1 134 ? 0.209   -25.121 -6.337  1.00 40.26  ? 135 ILE A CG1   1 
ATOM   1032  C CG2   . ILE A 1 134 ? 2.085   -26.465 -7.378  1.00 39.90  ? 135 ILE A CG2   1 
ATOM   1033  C CD1   . ILE A 1 134 ? 0.459   -23.909 -7.216  1.00 43.05  ? 135 ILE A CD1   1 
ATOM   1034  N N     . ASP A 1 135 ? 2.469   -29.155 -5.507  1.00 38.12  ? 136 ASP A N     1 
ATOM   1035  C CA    . ASP A 1 135 ? 3.642   -30.010 -5.431  1.00 41.86  ? 136 ASP A CA    1 
ATOM   1036  C C     . ASP A 1 135 ? 4.513   -29.758 -6.659  1.00 41.31  ? 136 ASP A C     1 
ATOM   1037  O O     . ASP A 1 135 ? 4.068   -29.943 -7.789  1.00 41.41  ? 136 ASP A O     1 
ATOM   1038  C CB    . ASP A 1 135 ? 3.254   -31.475 -5.294  1.00 43.65  ? 136 ASP A CB    1 
ATOM   1039  C CG    . ASP A 1 135 ? 4.417   -32.447 -5.156  1.00 41.30  ? 136 ASP A CG    1 
ATOM   1040  O OD1   . ASP A 1 135 ? 5.576   -31.992 -5.246  1.00 43.81  ? 136 ASP A OD1   1 
ATOM   1041  O OD2   . ASP A 1 135 ? 4.154   -33.651 -4.949  1.00 43.51  ? 136 ASP A OD2   1 
ATOM   1042  N N     . PRO A 1 136 ? 5.782   -29.332 -6.473  1.00 38.28  ? 137 PRO A N     1 
ATOM   1043  C CA    . PRO A 1 136 ? 6.666   -29.034 -7.600  1.00 35.10  ? 137 PRO A CA    1 
ATOM   1044  C C     . PRO A 1 136 ? 6.890   -30.257 -8.485  1.00 35.26  ? 137 PRO A C     1 
ATOM   1045  O O     . PRO A 1 136 ? 7.210   -30.127 -9.664  1.00 36.41  ? 137 PRO A O     1 
ATOM   1046  C CB    . PRO A 1 136 ? 7.966   -28.553 -6.921  1.00 34.86  ? 137 PRO A CB    1 
ATOM   1047  C CG    . PRO A 1 136 ? 7.908   -29.157 -5.531  1.00 33.95  ? 137 PRO A CG    1 
ATOM   1048  C CD    . PRO A 1 136 ? 6.435   -29.146 -5.169  1.00 36.03  ? 137 PRO A CD    1 
ATOM   1049  N N     . GLY A 1 137 ? 6.709   -31.444 -7.897  1.00 35.20  ? 138 GLY A N     1 
ATOM   1050  C CA    . GLY A 1 137 ? 6.915   -32.694 -8.608  1.00 40.42  ? 138 GLY A CA    1 
ATOM   1051  C C     . GLY A 1 137 ? 5.712   -33.049 -9.479  1.00 37.99  ? 138 GLY A C     1 
ATOM   1052  O O     . GLY A 1 137 ? 5.818   -33.883 -10.374 1.00 42.48  ? 138 GLY A O     1 
ATOM   1053  N N     . ASN A 1 138 ? 4.575   -32.399 -9.207  1.00 37.03  ? 139 ASN A N     1 
ATOM   1054  C CA    . ASN A 1 138 ? 3.329   -32.701 -9.894  1.00 37.86  ? 139 ASN A CA    1 
ATOM   1055  C C     . ASN A 1 138 ? 3.551   -32.646 -11.403 1.00 31.91  ? 139 ASN A C     1 
ATOM   1056  O O     . ASN A 1 138 ? 3.202   -33.581 -12.117 1.00 29.00  ? 139 ASN A O     1 
ATOM   1057  C CB    . ASN A 1 138 ? 2.204   -31.766 -9.462  1.00 40.03  ? 139 ASN A CB    1 
ATOM   1058  C CG    . ASN A 1 138 ? 0.875   -32.165 -10.058 1.00 41.95  ? 139 ASN A CG    1 
ATOM   1059  O OD1   . ASN A 1 138 ? 0.386   -33.271 -9.805  1.00 45.20  ? 139 ASN A OD1   1 
ATOM   1060  N ND2   . ASN A 1 138 ? 0.277   -31.286 -10.849 1.00 41.31  ? 139 ASN A ND2   1 
ATOM   1061  N N     . SER A 1 139 ? 4.121   -31.533 -11.879 1.00 31.23  ? 140 SER A N     1 
ATOM   1062  C CA    . SER A 1 139 ? 4.423   -31.372 -13.292 1.00 32.71  ? 140 SER A CA    1 
ATOM   1063  C C     . SER A 1 139 ? 5.772   -30.680 -13.466 1.00 30.34  ? 140 SER A C     1 
ATOM   1064  O O     . SER A 1 139 ? 6.054   -30.124 -14.524 1.00 34.54  ? 140 SER A O     1 
ATOM   1065  C CB    . SER A 1 139 ? 3.329   -30.617 -14.006 1.00 32.59  ? 140 SER A CB    1 
ATOM   1066  O OG    . SER A 1 139 ? 3.222   -29.286 -13.520 1.00 30.73  ? 140 SER A OG    1 
ATOM   1067  N N     . GLY A 1 140 ? 6.597   -30.718 -12.413 1.00 28.97  ? 141 GLY A N     1 
ATOM   1068  C CA    . GLY A 1 140 ? 7.945   -30.176 -12.473 1.00 30.96  ? 141 GLY A CA    1 
ATOM   1069  C C     . GLY A 1 140 ? 7.984   -28.712 -12.041 1.00 29.83  ? 141 GLY A C     1 
ATOM   1070  O O     . GLY A 1 140 ? 6.949   -28.058 -11.947 1.00 27.60  ? 141 GLY A O     1 
ATOM   1071  N N     . HIS A 1 141 ? 9.201   -28.205 -11.819 1.00 32.70  ? 142 HIS A N     1 
ATOM   1072  C CA    . HIS A 1 141 ? 9.401   -26.892 -11.229 1.00 28.99  ? 142 HIS A CA    1 
ATOM   1073  C C     . HIS A 1 141 ? 10.596  -26.202 -11.884 1.00 28.81  ? 142 HIS A C     1 
ATOM   1074  O O     . HIS A 1 141 ? 11.621  -26.831 -12.139 1.00 27.50  ? 142 HIS A O     1 
ATOM   1075  C CB    . HIS A 1 141 ? 9.575   -27.029 -9.712  1.00 31.51  ? 142 HIS A CB    1 
ATOM   1076  C CG    . HIS A 1 141 ? 10.244  -25.868 -9.055  1.00 31.97  ? 142 HIS A CG    1 
ATOM   1077  N ND1   . HIS A 1 141 ? 11.056  -26.024 -7.952  1.00 32.35  ? 142 HIS A ND1   1 
ATOM   1078  C CD2   . HIS A 1 141 ? 10.240  -24.556 -9.330  1.00 30.55  ? 142 HIS A CD2   1 
ATOM   1079  C CE1   . HIS A 1 141 ? 11.517  -24.839 -7.578  1.00 32.94  ? 142 HIS A CE1   1 
ATOM   1080  N NE2   . HIS A 1 141 ? 11.033  -23.933 -8.400  1.00 30.41  ? 142 HIS A NE2   1 
ATOM   1081  N N     . GLN A 1 142 ? 10.444  -24.899 -12.145 1.00 26.44  ? 143 GLN A N     1 
ATOM   1082  C CA    . GLN A 1 142 ? 11.522  -24.080 -12.674 1.00 27.27  ? 143 GLN A CA    1 
ATOM   1083  C C     . GLN A 1 142 ? 11.592  -22.769 -11.898 1.00 22.93  ? 143 GLN A C     1 
ATOM   1084  O O     . GLN A 1 142 ? 10.566  -22.150 -11.624 1.00 21.40  ? 143 GLN A O     1 
ATOM   1085  C CB    . GLN A 1 142 ? 11.314  -23.759 -14.153 1.00 28.38  ? 143 GLN A CB    1 
ATOM   1086  C CG    . GLN A 1 142 ? 11.337  -24.974 -15.072 1.00 34.58  ? 143 GLN A CG    1 
ATOM   1087  C CD    . GLN A 1 142 ? 11.157  -24.606 -16.528 1.00 34.04  ? 143 GLN A CD    1 
ATOM   1088  O OE1   . GLN A 1 142 ? 11.995  -24.915 -17.382 1.00 37.84  ? 143 GLN A OE1   1 
ATOM   1089  N NE2   . GLN A 1 142 ? 10.057  -23.930 -16.823 1.00 32.88  ? 143 GLN A NE2   1 
ATOM   1090  N N     . SER A 1 143 ? 12.817  -22.344 -11.574 1.00 24.21  ? 144 SER A N     1 
ATOM   1091  C CA    . SER A 1 143 ? 13.041  -21.076 -10.898 1.00 23.60  ? 144 SER A CA    1 
ATOM   1092  C C     . SER A 1 143 ? 14.098  -20.268 -11.642 1.00 25.91  ? 144 SER A C     1 
ATOM   1093  O O     . SER A 1 143 ? 15.158  -20.787 -11.983 1.00 30.56  ? 144 SER A O     1 
ATOM   1094  C CB    . SER A 1 143 ? 13.435  -21.283 -9.457  1.00 22.11  ? 144 SER A CB    1 
ATOM   1095  O OG    . SER A 1 143 ? 12.310  -21.630 -8.663  1.00 22.15  ? 144 SER A OG    1 
ATOM   1096  N N     . PHE A 1 144 ? 13.790  -18.990 -11.883 1.00 24.73  ? 145 PHE A N     1 
ATOM   1097  C CA    . PHE A 1 144 ? 14.741  -18.066 -12.476 1.00 27.43  ? 145 PHE A CA    1 
ATOM   1098  C C     . PHE A 1 144 ? 14.631  -16.719 -11.773 1.00 25.10  ? 145 PHE A C     1 
ATOM   1099  O O     . PHE A 1 144 ? 13.545  -16.315 -11.364 1.00 24.79  ? 145 PHE A O     1 
ATOM   1100  C CB    . PHE A 1 144 ? 14.505  -17.854 -13.975 1.00 25.72  ? 145 PHE A CB    1 
ATOM   1101  C CG    . PHE A 1 144 ? 14.553  -19.114 -14.826 1.00 25.74  ? 145 PHE A CG    1 
ATOM   1102  C CD1   . PHE A 1 144 ? 15.769  -19.675 -15.201 1.00 26.64  ? 145 PHE A CD1   1 
ATOM   1103  C CD2   . PHE A 1 144 ? 13.384  -19.714 -15.279 1.00 27.61  ? 145 PHE A CD2   1 
ATOM   1104  C CE1   . PHE A 1 144 ? 15.810  -20.818 -15.983 1.00 28.54  ? 145 PHE A CE1   1 
ATOM   1105  C CE2   . PHE A 1 144 ? 13.431  -20.856 -16.062 1.00 28.98  ? 145 PHE A CE2   1 
ATOM   1106  C CZ    . PHE A 1 144 ? 14.642  -21.404 -16.414 1.00 29.66  ? 145 PHE A CZ    1 
ATOM   1107  N N     . GLU A 1 145 ? 15.771  -16.035 -11.646 1.00 26.17  ? 146 GLU A N     1 
ATOM   1108  C CA    . GLU A 1 145 ? 15.786  -14.634 -11.264 1.00 29.37  ? 146 GLU A CA    1 
ATOM   1109  C C     . GLU A 1 145 ? 15.213  -13.835 -12.433 1.00 29.49  ? 146 GLU A C     1 
ATOM   1110  O O     . GLU A 1 145 ? 15.593  -14.054 -13.580 1.00 28.76  ? 146 GLU A O     1 
ATOM   1111  C CB    . GLU A 1 145 ? 17.211  -14.232 -10.883 1.00 33.84  ? 146 GLU A CB    1 
ATOM   1112  C CG    . GLU A 1 145 ? 17.298  -12.920 -10.108 1.00 38.08  ? 146 GLU A CG    1 
ATOM   1113  C CD    . GLU A 1 145 ? 17.085  -11.670 -10.942 1.00 41.51  ? 146 GLU A CD    1 
ATOM   1114  O OE1   . GLU A 1 145 ? 16.891  -11.802 -12.168 1.00 48.02  ? 146 GLU A OE1   1 
ATOM   1115  O OE2   . GLU A 1 145 ? 17.118  -10.563 -10.364 1.00 45.35  ? 146 GLU A OE2   1 
ATOM   1116  N N     . ALA A 1 146 ? 14.277  -12.930 -12.128 1.00 33.83  ? 147 ALA A N     1 
ATOM   1117  C CA    . ALA A 1 146 ? 13.452  -12.293 -13.143 1.00 33.22  ? 147 ALA A CA    1 
ATOM   1118  C C     . ALA A 1 146 ? 14.316  -11.543 -14.155 1.00 35.56  ? 147 ALA A C     1 
ATOM   1119  O O     . ALA A 1 146 ? 14.051  -11.591 -15.355 1.00 35.97  ? 147 ALA A O     1 
ATOM   1120  C CB    . ALA A 1 146 ? 12.449  -11.371 -12.485 1.00 31.32  ? 147 ALA A CB    1 
ATOM   1121  N N     . SER A 1 147 ? 15.336  -10.837 -13.657 1.00 36.30  ? 148 SER A N     1 
ATOM   1122  C CA    . SER A 1 147 ? 16.172  -9.998  -14.501 1.00 35.96  ? 148 SER A CA    1 
ATOM   1123  C C     . SER A 1 147 ? 17.106  -10.862 -15.344 1.00 35.29  ? 148 SER A C     1 
ATOM   1124  O O     . SER A 1 147 ? 17.402  -10.525 -16.488 1.00 34.21  ? 148 SER A O     1 
ATOM   1125  C CB    . SER A 1 147 ? 16.943  -8.995  -13.681 1.00 39.25  ? 148 SER A CB    1 
ATOM   1126  O OG    . SER A 1 147 ? 16.070  -8.045  -13.086 1.00 40.78  ? 148 SER A OG    1 
ATOM   1127  N N     . GLN A 1 148 ? 17.565  -11.977 -14.766 1.00 33.70  ? 149 GLN A N     1 
ATOM   1128  C CA    . GLN A 1 148 ? 18.448  -12.889 -15.473 1.00 36.31  ? 149 GLN A CA    1 
ATOM   1129  C C     . GLN A 1 148 ? 17.673  -13.555 -16.607 1.00 36.00  ? 149 GLN A C     1 
ATOM   1130  O O     . GLN A 1 148 ? 18.248  -13.902 -17.635 1.00 38.34  ? 149 GLN A O     1 
ATOM   1131  C CB    . GLN A 1 148 ? 19.037  -13.946 -14.538 1.00 35.73  ? 149 GLN A CB    1 
ATOM   1132  C CG    . GLN A 1 148 ? 20.067  -14.851 -15.207 1.00 37.34  ? 149 GLN A CG    1 
ATOM   1133  C CD    . GLN A 1 148 ? 20.532  -15.988 -14.324 1.00 39.73  ? 149 GLN A CD    1 
ATOM   1134  O OE1   . GLN A 1 148 ? 20.317  -17.167 -14.625 1.00 37.69  ? 149 GLN A OE1   1 
ATOM   1135  N NE2   . GLN A 1 148 ? 21.178  -15.643 -13.220 1.00 36.92  ? 149 GLN A NE2   1 
ATOM   1136  N N     . PHE A 1 149 ? 16.361  -13.720 -16.404 1.00 32.62  ? 150 PHE A N     1 
ATOM   1137  C CA    . PHE A 1 149 ? 15.509  -14.383 -17.379 1.00 31.46  ? 150 PHE A CA    1 
ATOM   1138  C C     . PHE A 1 149 ? 15.275  -13.451 -18.566 1.00 31.66  ? 150 PHE A C     1 
ATOM   1139  O O     . PHE A 1 149 ? 14.741  -13.870 -19.589 1.00 30.48  ? 150 PHE A O     1 
ATOM   1140  C CB    . PHE A 1 149 ? 14.181  -14.809 -16.743 1.00 29.45  ? 150 PHE A CB    1 
ATOM   1141  C CG    . PHE A 1 149 ? 13.228  -15.504 -17.706 1.00 32.00  ? 150 PHE A CG    1 
ATOM   1142  C CD1   . PHE A 1 149 ? 13.265  -16.884 -17.876 1.00 32.84  ? 150 PHE A CD1   1 
ATOM   1143  C CD2   . PHE A 1 149 ? 12.312  -14.774 -18.457 1.00 31.76  ? 150 PHE A CD2   1 
ATOM   1144  C CE1   . PHE A 1 149 ? 12.407  -17.512 -18.766 1.00 31.84  ? 150 PHE A CE1   1 
ATOM   1145  C CE2   . PHE A 1 149 ? 11.456  -15.409 -19.343 1.00 34.11  ? 150 PHE A CE2   1 
ATOM   1146  C CZ    . PHE A 1 149 ? 11.504  -16.775 -19.494 1.00 31.28  ? 150 PHE A CZ    1 
ATOM   1147  N N     . MET A 1 150 ? 15.677  -12.183 -18.415 1.00 34.32  ? 151 MET A N     1 
ATOM   1148  C CA    . MET A 1 150 ? 15.474  -11.185 -19.453 1.00 35.51  ? 151 MET A CA    1 
ATOM   1149  C C     . MET A 1 150 ? 16.806  -10.847 -20.119 1.00 40.27  ? 151 MET A C     1 
ATOM   1150  O O     . MET A 1 150 ? 16.852  -10.579 -21.318 1.00 45.55  ? 151 MET A O     1 
ATOM   1151  C CB    . MET A 1 150 ? 14.858  -9.902  -18.880 1.00 37.05  ? 151 MET A CB    1 
ATOM   1152  C CG    . MET A 1 150 ? 13.400  -10.038 -18.478 1.00 36.38  ? 151 MET A CG    1 
ATOM   1153  S SD    . MET A 1 150 ? 12.701  -8.509  -17.823 1.00 38.80  ? 151 MET A SD    1 
ATOM   1154  C CE    . MET A 1 150 ? 12.726  -7.423  -19.255 1.00 41.24  ? 151 MET A CE    1 
ATOM   1155  N N     . PHE A 1 151 ? 17.885  -10.861 -19.328 1.00 36.63  ? 152 PHE A N     1 
ATOM   1156  C CA    . PHE A 1 151 ? 19.189  -10.425 -19.800 1.00 37.62  ? 152 PHE A CA    1 
ATOM   1157  C C     . PHE A 1 151 ? 19.906  -11.581 -20.492 1.00 38.33  ? 152 PHE A C     1 
ATOM   1158  O O     . PHE A 1 151 ? 20.764  -11.358 -21.344 1.00 34.25  ? 152 PHE A O     1 
ATOM   1159  C CB    . PHE A 1 151 ? 20.020  -9.877  -18.635 1.00 38.53  ? 152 PHE A CB    1 
ATOM   1160  C CG    . PHE A 1 151 ? 19.423  -8.659  -17.942 1.00 38.44  ? 152 PHE A CG    1 
ATOM   1161  C CD1   . PHE A 1 151 ? 18.528  -7.826  -18.606 1.00 39.74  ? 152 PHE A CD1   1 
ATOM   1162  C CD2   . PHE A 1 151 ? 19.767  -8.343  -16.632 1.00 40.17  ? 152 PHE A CD2   1 
ATOM   1163  C CE1   . PHE A 1 151 ? 17.988  -6.718  -17.971 1.00 43.79  ? 152 PHE A CE1   1 
ATOM   1164  C CE2   . PHE A 1 151 ? 19.225  -7.231  -16.005 1.00 36.95  ? 152 PHE A CE2   1 
ATOM   1165  C CZ    . PHE A 1 151 ? 18.339  -6.423  -16.675 1.00 40.03  ? 152 PHE A CZ    1 
ATOM   1166  N N     . PHE A 1 152 ? 19.551  -12.814 -20.116 1.00 37.38  ? 153 PHE A N     1 
ATOM   1167  C CA    . PHE A 1 152 ? 20.226  -13.993 -20.636 1.00 37.42  ? 153 PHE A CA    1 
ATOM   1168  C C     . PHE A 1 152 ? 19.213  -14.890 -21.343 1.00 34.76  ? 153 PHE A C     1 
ATOM   1169  O O     . PHE A 1 152 ? 18.020  -14.597 -21.362 1.00 33.63  ? 153 PHE A O     1 
ATOM   1170  C CB    . PHE A 1 152 ? 20.959  -14.703 -19.493 1.00 37.93  ? 153 PHE A CB    1 
ATOM   1171  C CG    . PHE A 1 152 ? 22.073  -13.875 -18.866 1.00 42.52  ? 153 PHE A CG    1 
ATOM   1172  C CD1   . PHE A 1 152 ? 23.322  -13.788 -19.471 1.00 44.89  ? 153 PHE A CD1   1 
ATOM   1173  C CD2   . PHE A 1 152 ? 21.871  -13.190 -17.673 1.00 48.77  ? 153 PHE A CD2   1 
ATOM   1174  C CE1   . PHE A 1 152 ? 24.335  -13.033 -18.900 1.00 48.98  ? 153 PHE A CE1   1 
ATOM   1175  C CE2   . PHE A 1 152 ? 22.889  -12.438 -17.107 1.00 46.58  ? 153 PHE A CE2   1 
ATOM   1176  C CZ    . PHE A 1 152 ? 24.117  -12.362 -17.721 1.00 48.58  ? 153 PHE A CZ    1 
ATOM   1177  N N     . ASN A 1 153 ? 19.715  -15.983 -21.928 1.00 33.61  ? 154 ASN A N     1 
ATOM   1178  C CA    . ASN A 1 153 ? 18.898  -16.869 -22.740 1.00 35.20  ? 154 ASN A CA    1 
ATOM   1179  C C     . ASN A 1 153 ? 18.402  -18.033 -21.887 1.00 34.50  ? 154 ASN A C     1 
ATOM   1180  O O     . ASN A 1 153 ? 19.153  -18.959 -21.587 1.00 34.41  ? 154 ASN A O     1 
ATOM   1181  C CB    . ASN A 1 153 ? 19.658  -17.350 -23.972 1.00 37.73  ? 154 ASN A CB    1 
ATOM   1182  C CG    . ASN A 1 153 ? 20.066  -16.203 -24.865 1.00 37.83  ? 154 ASN A CG    1 
ATOM   1183  O OD1   . ASN A 1 153 ? 19.209  -15.451 -25.341 1.00 38.90  ? 154 ASN A OD1   1 
ATOM   1184  N ND2   . ASN A 1 153 ? 21.360  -16.047 -25.098 1.00 41.02  ? 154 ASN A ND2   1 
ATOM   1185  N N     . HIS A 1 154 ? 17.123  -17.964 -21.510 1.00 31.90  ? 155 HIS A N     1 
ATOM   1186  C CA    . HIS A 1 154 ? 16.471  -19.015 -20.749 1.00 31.09  ? 155 HIS A CA    1 
ATOM   1187  C C     . HIS A 1 154 ? 15.185  -19.414 -21.465 1.00 30.90  ? 155 HIS A C     1 
ATOM   1188  O O     . HIS A 1 154 ? 14.380  -18.556 -21.821 1.00 29.18  ? 155 HIS A O     1 
ATOM   1189  C CB    . HIS A 1 154 ? 16.185  -18.547 -19.317 1.00 30.55  ? 155 HIS A CB    1 
ATOM   1190  C CG    . HIS A 1 154 ? 17.385  -18.520 -18.429 1.00 29.41  ? 155 HIS A CG    1 
ATOM   1191  N ND1   . HIS A 1 154 ? 18.273  -19.570 -18.338 1.00 29.57  ? 155 HIS A ND1   1 
ATOM   1192  C CD2   . HIS A 1 154 ? 17.814  -17.597 -17.558 1.00 29.33  ? 155 HIS A CD2   1 
ATOM   1193  C CE1   . HIS A 1 154 ? 19.217  -19.268 -17.459 1.00 31.29  ? 155 HIS A CE1   1 
ATOM   1194  N NE2   . HIS A 1 154 ? 18.959  -18.073 -16.975 1.00 28.79  ? 155 HIS A NE2   1 
ATOM   1195  N N     . VAL A 1 155 ? 15.014  -20.723 -21.678 1.00 33.69  ? 156 VAL A N     1 
ATOM   1196  C CA    . VAL A 1 155 ? 13.816  -21.253 -22.305 1.00 35.22  ? 156 VAL A CA    1 
ATOM   1197  C C     . VAL A 1 155 ? 13.062  -22.092 -21.278 1.00 39.71  ? 156 VAL A C     1 
ATOM   1198  O O     . VAL A 1 155 ? 13.539  -23.143 -20.858 1.00 44.86  ? 156 VAL A O     1 
ATOM   1199  C CB    . VAL A 1 155 ? 14.143  -22.080 -23.563 1.00 35.28  ? 156 VAL A CB    1 
ATOM   1200  C CG1   . VAL A 1 155 ? 12.898  -22.739 -24.145 1.00 32.78  ? 156 VAL A CG1   1 
ATOM   1201  C CG2   . VAL A 1 155 ? 14.854  -21.245 -24.621 1.00 35.87  ? 156 VAL A CG2   1 
ATOM   1202  N N     . PRO A 1 156 ? 11.861  -21.650 -20.842 1.00 38.08  ? 157 PRO A N     1 
ATOM   1203  C CA    . PRO A 1 156 ? 11.090  -22.385 -19.840 1.00 37.73  ? 157 PRO A CA    1 
ATOM   1204  C C     . PRO A 1 156 ? 10.286  -23.541 -20.428 1.00 38.50  ? 157 PRO A C     1 
ATOM   1205  O O     . PRO A 1 156 ? 9.902   -23.507 -21.596 1.00 34.96  ? 157 PRO A O     1 
ATOM   1206  C CB    . PRO A 1 156 ? 10.189  -21.275 -19.278 1.00 37.63  ? 157 PRO A CB    1 
ATOM   1207  C CG    . PRO A 1 156 ? 9.902   -20.400 -20.483 1.00 39.29  ? 157 PRO A CG    1 
ATOM   1208  C CD    . PRO A 1 156 ? 11.193  -20.417 -21.288 1.00 37.02  ? 157 PRO A CD    1 
ATOM   1209  N N     . ASP A 1 157 ? 10.051  -24.565 -19.602 1.00 36.31  ? 158 ASP A N     1 
ATOM   1210  C CA    . ASP A 1 157 ? 9.156   -25.653 -19.953 1.00 40.54  ? 158 ASP A CA    1 
ATOM   1211  C C     . ASP A 1 157 ? 7.739   -25.262 -19.541 1.00 39.46  ? 158 ASP A C     1 
ATOM   1212  O O     . ASP A 1 157 ? 7.425   -25.214 -18.354 1.00 39.64  ? 158 ASP A O     1 
ATOM   1213  C CB    . ASP A 1 157 ? 9.604   -26.963 -19.326 1.00 39.38  ? 158 ASP A CB    1 
ATOM   1214  C CG    . ASP A 1 157 ? 8.671   -28.145 -19.547 1.00 39.80  ? 158 ASP A CG    1 
ATOM   1215  O OD1   . ASP A 1 157 ? 7.578   -27.930 -20.109 1.00 41.36  ? 158 ASP A OD1   1 
ATOM   1216  O OD2   . ASP A 1 157 ? 9.049   -29.271 -19.164 1.00 43.29  ? 158 ASP A OD2   1 
ATOM   1217  N N     . PRO A 1 158 ? 6.845   -24.970 -20.510 1.00 44.57  ? 159 PRO A N     1 
ATOM   1218  C CA    . PRO A 1 158 ? 5.512   -24.449 -20.198 1.00 47.24  ? 159 PRO A CA    1 
ATOM   1219  C C     . PRO A 1 158 ? 4.570   -25.457 -19.542 1.00 45.78  ? 159 PRO A C     1 
ATOM   1220  O O     . PRO A 1 158 ? 3.393   -25.167 -19.346 1.00 45.17  ? 159 PRO A O     1 
ATOM   1221  C CB    . PRO A 1 158 ? 5.003   -23.994 -21.583 1.00 50.68  ? 159 PRO A CB    1 
ATOM   1222  C CG    . PRO A 1 158 ? 5.705   -24.919 -22.556 1.00 50.98  ? 159 PRO A CG    1 
ATOM   1223  C CD    . PRO A 1 158 ? 7.081   -25.125 -21.954 1.00 48.52  ? 159 PRO A CD    1 
ATOM   1224  N N     . THR A 1 159 ? 5.101   -26.636 -19.195 1.00 43.20  ? 160 THR A N     1 
ATOM   1225  C CA    . THR A 1 159 ? 4.301   -27.678 -18.570 1.00 43.86  ? 160 THR A CA    1 
ATOM   1226  C C     . THR A 1 159 ? 4.566   -27.693 -17.067 1.00 42.37  ? 160 THR A C     1 
ATOM   1227  O O     . THR A 1 159 ? 3.901   -28.413 -16.326 1.00 45.85  ? 160 THR A O     1 
ATOM   1228  C CB    . THR A 1 159 ? 4.623   -29.031 -19.203 1.00 43.90  ? 160 THR A CB    1 
ATOM   1229  O OG1   . THR A 1 159 ? 5.999   -29.263 -18.918 1.00 41.39  ? 160 THR A OG1   1 
ATOM   1230  C CG2   . THR A 1 159 ? 4.380   -29.051 -20.701 1.00 45.66  ? 160 THR A CG2   1 
ATOM   1231  N N     . THR A 1 160 ? 5.544   -26.893 -16.627 1.00 41.82  ? 161 THR A N     1 
ATOM   1232  C CA    . THR A 1 160 ? 5.971   -26.901 -15.238 1.00 39.26  ? 161 THR A CA    1 
ATOM   1233  C C     . THR A 1 160 ? 5.465   -25.643 -14.539 1.00 40.00  ? 161 THR A C     1 
ATOM   1234  O O     . THR A 1 160 ? 4.964   -24.723 -15.182 1.00 40.73  ? 161 THR A O     1 
ATOM   1235  C CB    . THR A 1 160 ? 7.495   -26.988 -15.167 1.00 34.94  ? 161 THR A CB    1 
ATOM   1236  O OG1   . THR A 1 160 ? 7.955   -25.682 -15.498 1.00 40.52  ? 161 THR A OG1   1 
ATOM   1237  C CG2   . THR A 1 160 ? 8.069   -28.021 -16.119 1.00 37.66  ? 161 THR A CG2   1 
ATOM   1238  N N     . HIS A 1 161 ? 5.608   -25.624 -13.210 1.00 37.93  ? 162 HIS A N     1 
ATOM   1239  C CA    . HIS A 1 161 ? 5.371   -24.426 -12.423 1.00 36.69  ? 162 HIS A CA    1 
ATOM   1240  C C     . HIS A 1 161 ? 6.617   -23.548 -12.480 1.00 34.22  ? 162 HIS A C     1 
ATOM   1241  O O     . HIS A 1 161 ? 7.680   -23.939 -12.002 1.00 30.95  ? 162 HIS A O     1 
ATOM   1242  C CB    . HIS A 1 161 ? 4.991   -24.784 -10.982 1.00 38.73  ? 162 HIS A CB    1 
ATOM   1243  C CG    . HIS A 1 161 ? 3.581   -25.243 -10.826 1.00 35.66  ? 162 HIS A CG    1 
ATOM   1244  N ND1   . HIS A 1 161 ? 2.549   -24.376 -10.536 1.00 31.21  ? 162 HIS A ND1   1 
ATOM   1245  C CD2   . HIS A 1 161 ? 3.028   -26.460 -10.916 1.00 34.34  ? 162 HIS A CD2   1 
ATOM   1246  C CE1   . HIS A 1 161 ? 1.416   -25.057 -10.457 1.00 31.11  ? 162 HIS A CE1   1 
ATOM   1247  N NE2   . HIS A 1 161 ? 1.683   -26.324 -10.684 1.00 33.24  ? 162 HIS A NE2   1 
ATOM   1248  N N     . LEU A 1 162 ? 6.466   -22.361 -13.074 1.00 30.46  ? 163 LEU A N     1 
ATOM   1249  C CA    . LEU A 1 162 ? 7.577   -21.445 -13.262 1.00 31.73  ? 163 LEU A CA    1 
ATOM   1250  C C     . LEU A 1 162 ? 7.547   -20.379 -12.170 1.00 26.53  ? 163 LEU A C     1 
ATOM   1251  O O     . LEU A 1 162 ? 6.497   -19.813 -11.877 1.00 26.28  ? 163 LEU A O     1 
ATOM   1252  C CB    . LEU A 1 162 ? 7.488   -20.829 -14.658 1.00 28.51  ? 163 LEU A CB    1 
ATOM   1253  C CG    . LEU A 1 162 ? 8.525   -19.751 -14.986 1.00 30.67  ? 163 LEU A CG    1 
ATOM   1254  C CD1   . LEU A 1 162 ? 9.935   -20.314 -14.949 1.00 31.74  ? 163 LEU A CD1   1 
ATOM   1255  C CD2   . LEU A 1 162 ? 8.236   -19.119 -16.336 1.00 30.09  ? 163 LEU A CD2   1 
ATOM   1256  N N     . LEU A 1 163 ? 8.715   -20.123 -11.571 1.00 25.95  ? 164 LEU A N     1 
ATOM   1257  C CA    . LEU A 1 163 ? 8.861   -19.075 -10.574 1.00 26.06  ? 164 LEU A CA    1 
ATOM   1258  C C     . LEU A 1 163 ? 9.868   -18.046 -11.076 1.00 26.51  ? 164 LEU A C     1 
ATOM   1259  O O     . LEU A 1 163 ? 10.995  -18.392 -11.419 1.00 27.65  ? 164 LEU A O     1 
ATOM   1260  C CB    . LEU A 1 163 ? 9.305   -19.659 -9.234  1.00 27.07  ? 164 LEU A CB    1 
ATOM   1261  C CG    . LEU A 1 163 ? 8.302   -20.567 -8.519  1.00 30.42  ? 164 LEU A CG    1 
ATOM   1262  C CD1   . LEU A 1 163 ? 8.817   -20.939 -7.138  1.00 29.07  ? 164 LEU A CD1   1 
ATOM   1263  C CD2   . LEU A 1 163 ? 6.938   -19.909 -8.425  1.00 36.70  ? 164 LEU A CD2   1 
ATOM   1264  N N     . LEU A 1 164 ? 9.446   -16.778 -11.106 1.00 25.39  ? 165 LEU A N     1 
ATOM   1265  C CA    . LEU A 1 164 ? 10.342  -15.676 -11.410 1.00 25.98  ? 165 LEU A CA    1 
ATOM   1266  C C     . LEU A 1 164 ? 10.559  -14.860 -10.139 1.00 25.07  ? 165 LEU A C     1 
ATOM   1267  O O     . LEU A 1 164 ? 9.666   -14.138 -9.701  1.00 26.94  ? 165 LEU A O     1 
ATOM   1268  C CB    . LEU A 1 164 ? 9.775   -14.812 -12.536 1.00 25.21  ? 165 LEU A CB    1 
ATOM   1269  C CG    . LEU A 1 164 ? 9.571   -15.509 -13.884 1.00 25.59  ? 165 LEU A CG    1 
ATOM   1270  C CD1   . LEU A 1 164 ? 9.223   -14.495 -14.963 1.00 25.19  ? 165 LEU A CD1   1 
ATOM   1271  C CD2   . LEU A 1 164 ? 10.796  -16.316 -14.280 1.00 25.59  ? 165 LEU A CD2   1 
ATOM   1272  N N     . TRP A 1 165 ? 11.751  -14.996 -9.550  1.00 23.70  ? 166 TRP A N     1 
ATOM   1273  C CA    . TRP A 1 165 ? 12.069  -14.320 -8.304  1.00 24.11  ? 166 TRP A CA    1 
ATOM   1274  C C     . TRP A 1 165 ? 12.458  -12.871 -8.583  1.00 27.40  ? 166 TRP A C     1 
ATOM   1275  O O     . TRP A 1 165 ? 12.769  -12.511 -9.718  1.00 26.59  ? 166 TRP A O     1 
ATOM   1276  C CB    . TRP A 1 165 ? 13.190  -15.054 -7.557  1.00 24.41  ? 166 TRP A CB    1 
ATOM   1277  C CG    . TRP A 1 165 ? 12.885  -16.494 -7.240  1.00 22.88  ? 166 TRP A CG    1 
ATOM   1278  C CD1   . TRP A 1 165 ? 12.432  -17.453 -8.099  1.00 23.31  ? 166 TRP A CD1   1 
ATOM   1279  C CD2   . TRP A 1 165 ? 12.998  -17.133 -5.950  1.00 21.52  ? 166 TRP A CD2   1 
ATOM   1280  N NE1   . TRP A 1 165 ? 12.273  -18.644 -7.442  1.00 20.03  ? 166 TRP A NE1   1 
ATOM   1281  C CE2   . TRP A 1 165 ? 12.606  -18.478 -6.123  1.00 21.46  ? 166 TRP A CE2   1 
ATOM   1282  C CE3   . TRP A 1 165 ? 13.390  -16.703 -4.677  1.00 20.63  ? 166 TRP A CE3   1 
ATOM   1283  C CZ2   . TRP A 1 165 ? 12.599  -19.390 -5.070  1.00 19.80  ? 166 TRP A CZ2   1 
ATOM   1284  C CZ3   . TRP A 1 165 ? 13.378  -17.605 -3.637  1.00 21.52  ? 166 TRP A CZ3   1 
ATOM   1285  C CH2   . TRP A 1 165 ? 12.989  -18.929 -3.833  1.00 20.98  ? 166 TRP A CH2   1 
ATOM   1286  N N     . GLN A 1 166 ? 12.437  -12.052 -7.525  1.00 26.39  ? 167 GLN A N     1 
ATOM   1287  C CA    . GLN A 1 166 ? 12.785  -10.644 -7.622  1.00 26.90  ? 167 GLN A CA    1 
ATOM   1288  C C     . GLN A 1 166 ? 12.114  -10.036 -8.851  1.00 27.63  ? 167 GLN A C     1 
ATOM   1289  O O     . GLN A 1 166 ? 12.772  -9.409  -9.677  1.00 28.42  ? 167 GLN A O     1 
ATOM   1290  C CB    . GLN A 1 166 ? 14.304  -10.477 -7.670  1.00 29.78  ? 167 GLN A CB    1 
ATOM   1291  C CG    . GLN A 1 166 ? 15.017  -10.951 -6.408  1.00 32.62  ? 167 GLN A CG    1 
ATOM   1292  C CD    . GLN A 1 166 ? 16.508  -10.691 -6.431  1.00 34.73  ? 167 GLN A CD    1 
ATOM   1293  O OE1   . GLN A 1 166 ? 17.066  -10.218 -7.427  1.00 41.88  ? 167 GLN A OE1   1 
ATOM   1294  N NE2   . GLN A 1 166 ? 17.170  -11.004 -5.326  1.00 33.80  ? 167 GLN A NE2   1 
ATOM   1295  N N     . ILE A 1 167 ? 10.792  -10.219 -8.948  1.00 28.14  ? 168 ILE A N     1 
ATOM   1296  C CA    . ILE A 1 167 ? 10.019  -9.704  -10.066 1.00 30.38  ? 168 ILE A CA    1 
ATOM   1297  C C     . ILE A 1 167 ? 9.906   -8.187  -9.939  1.00 34.74  ? 168 ILE A C     1 
ATOM   1298  O O     . ILE A 1 167 ? 9.603   -7.500  -10.913 1.00 37.82  ? 168 ILE A O     1 
ATOM   1299  C CB    . ILE A 1 167 ? 8.632   -10.375 -10.127 1.00 29.35  ? 168 ILE A CB    1 
ATOM   1300  C CG1   . ILE A 1 167 ? 7.848   -9.950  -11.373 1.00 27.88  ? 168 ILE A CG1   1 
ATOM   1301  C CG2   . ILE A 1 167 ? 7.841   -10.110 -8.846  1.00 26.73  ? 168 ILE A CG2   1 
ATOM   1302  C CD1   . ILE A 1 167 ? 8.478   -10.391 -12.683 1.00 27.26  ? 168 ILE A CD1   1 
ATOM   1303  N N     . ALA A 1 168 ? 10.165  -7.676  -8.730  1.00 35.18  ? 169 ALA A N     1 
ATOM   1304  C CA    . ALA A 1 168 ? 9.985   -6.264  -8.431  1.00 36.42  ? 169 ALA A CA    1 
ATOM   1305  C C     . ALA A 1 168 ? 11.020  -5.422  -9.172  1.00 33.37  ? 169 ALA A C     1 
ATOM   1306  O O     . ALA A 1 168 ? 10.756  -4.272  -9.516  1.00 35.51  ? 169 ALA A O     1 
ATOM   1307  C CB    . ALA A 1 168 ? 10.066  -6.042  -6.935  1.00 39.95  ? 169 ALA A CB    1 
ATOM   1308  N N     . ILE A 1 169 ? 12.202  -6.002  -9.405  1.00 36.55  ? 170 ILE A N     1 
ATOM   1309  C CA    . ILE A 1 169 ? 13.298  -5.286  -10.039 1.00 34.47  ? 170 ILE A CA    1 
ATOM   1310  C C     . ILE A 1 169 ? 13.616  -5.939  -11.382 1.00 36.31  ? 170 ILE A C     1 
ATOM   1311  O O     . ILE A 1 169 ? 14.746  -5.867  -11.860 1.00 38.84  ? 170 ILE A O     1 
ATOM   1312  C CB    . ILE A 1 169 ? 14.531  -5.249  -9.118  1.00 36.49  ? 170 ILE A CB    1 
ATOM   1313  C CG1   . ILE A 1 169 ? 14.970  -6.656  -8.709  1.00 39.79  ? 170 ILE A CG1   1 
ATOM   1314  C CG2   . ILE A 1 169 ? 14.275  -4.362  -7.900  1.00 39.94  ? 170 ILE A CG2   1 
ATOM   1315  C CD1   . ILE A 1 169 ? 16.193  -6.688  -7.811  1.00 39.78  ? 170 ILE A CD1   1 
ATOM   1316  N N     . ALA A 1 170 ? 12.603  -6.567  -11.984 1.00 33.33  ? 171 ALA A N     1 
ATOM   1317  C CA    . ALA A 1 170 ? 12.757  -7.211  -13.276 1.00 31.34  ? 171 ALA A CA    1 
ATOM   1318  C C     . ALA A 1 170 ? 13.198  -6.184  -14.316 1.00 30.71  ? 171 ALA A C     1 
ATOM   1319  O O     . ALA A 1 170 ? 12.477  -5.230  -14.598 1.00 30.35  ? 171 ALA A O     1 
ATOM   1320  C CB    . ALA A 1 170 ? 11.460  -7.879  -13.676 1.00 30.70  ? 171 ALA A CB    1 
ATOM   1321  N N     . GLY A 1 171 ? 14.396  -6.389  -14.873 1.00 31.97  ? 172 GLY A N     1 
ATOM   1322  C CA    . GLY A 1 171 ? 14.890  -5.565  -15.963 1.00 32.82  ? 172 GLY A CA    1 
ATOM   1323  C C     . GLY A 1 171 ? 15.684  -4.364  -15.454 1.00 33.68  ? 172 GLY A C     1 
ATOM   1324  O O     . GLY A 1 171 ? 16.071  -3.500  -16.237 1.00 30.40  ? 172 GLY A O     1 
ATOM   1325  N N     . GLU A 1 172 ? 15.914  -4.321  -14.137 1.00 36.67  ? 173 GLU A N     1 
ATOM   1326  C CA    . GLU A 1 172 ? 16.709  -3.264  -13.531 1.00 39.44  ? 173 GLU A CA    1 
ATOM   1327  C C     . GLU A 1 172 ? 18.182  -3.656  -13.628 1.00 35.95  ? 173 GLU A C     1 
ATOM   1328  O O     . GLU A 1 172 ? 18.668  -4.462  -12.839 1.00 37.45  ? 173 GLU A O     1 
ATOM   1329  C CB    . GLU A 1 172 ? 16.272  -3.031  -12.085 1.00 47.72  ? 173 GLU A CB    1 
ATOM   1330  C CG    . GLU A 1 172 ? 16.662  -1.656  -11.550 1.00 54.76  ? 173 GLU A CG    1 
ATOM   1331  C CD    . GLU A 1 172 ? 18.148  -1.354  -11.614 1.00 55.33  ? 173 GLU A CD    1 
ATOM   1332  O OE1   . GLU A 1 172 ? 18.919  -2.006  -10.879 1.00 58.61  ? 173 GLU A OE1   1 
ATOM   1333  O OE2   . GLU A 1 172 ? 18.534  -0.473  -12.410 1.00 52.77  ? 173 GLU A OE2   1 
ATOM   1334  N N     . HIS A 1 173 ? 18.882  -3.058  -14.599 1.00 37.34  ? 174 HIS A N     1 
ATOM   1335  C CA    . HIS A 1 173 ? 20.170  -3.560  -15.052 1.00 33.74  ? 174 HIS A CA    1 
ATOM   1336  C C     . HIS A 1 173 ? 21.320  -2.943  -14.258 1.00 31.20  ? 174 HIS A C     1 
ATOM   1337  O O     . HIS A 1 173 ? 22.427  -3.475  -14.268 1.00 32.21  ? 174 HIS A O     1 
ATOM   1338  C CB    . HIS A 1 173 ? 20.343  -3.289  -16.551 1.00 35.65  ? 174 HIS A CB    1 
ATOM   1339  C CG    . HIS A 1 173 ? 20.317  -1.839  -16.905 1.00 37.59  ? 174 HIS A CG    1 
ATOM   1340  N ND1   . HIS A 1 173 ? 19.150  -1.149  -17.153 1.00 40.80  ? 174 HIS A ND1   1 
ATOM   1341  C CD2   . HIS A 1 173 ? 21.309  -0.949  -17.038 1.00 39.81  ? 174 HIS A CD2   1 
ATOM   1342  C CE1   . HIS A 1 173 ? 19.439  0.113   -17.432 1.00 42.67  ? 174 HIS A CE1   1 
ATOM   1343  N NE2   . HIS A 1 173 ? 20.745  0.257   -17.368 1.00 42.96  ? 174 HIS A NE2   1 
ATOM   1344  N N     . THR A 1 174 ? 21.059  -1.822  -13.577 1.00 31.48  ? 175 THR A N     1 
ATOM   1345  C CA    . THR A 1 174 ? 22.123  -1.060  -12.937 1.00 36.74  ? 175 THR A CA    1 
ATOM   1346  C C     . THR A 1 174 ? 22.433  -1.647  -11.560 1.00 39.96  ? 175 THR A C     1 
ATOM   1347  O O     . THR A 1 174 ? 23.555  -1.528  -11.073 1.00 44.54  ? 175 THR A O     1 
ATOM   1348  C CB    . THR A 1 174 ? 21.724  0.413   -12.847 1.00 34.46  ? 175 THR A CB    1 
ATOM   1349  O OG1   . THR A 1 174 ? 20.609  0.469   -11.963 1.00 32.93  ? 175 THR A OG1   1 
ATOM   1350  C CG2   . THR A 1 174 ? 21.358  1.000   -14.198 1.00 35.16  ? 175 THR A CG2   1 
ATOM   1351  N N     . LEU A 1 175 ? 21.428  -2.273  -10.940 1.00 41.12  ? 176 LEU A N     1 
ATOM   1352  C CA    . LEU A 1 175 ? 21.581  -2.863  -9.619  1.00 41.28  ? 176 LEU A CA    1 
ATOM   1353  C C     . LEU A 1 175 ? 21.724  -1.757  -8.575  1.00 43.17  ? 176 LEU A C     1 
ATOM   1354  O O     . LEU A 1 175 ? 22.404  -1.941  -7.568  1.00 41.03  ? 176 LEU A O     1 
ATOM   1355  C CB    . LEU A 1 175 ? 22.786  -3.804  -9.581  1.00 43.74  ? 176 LEU A CB    1 
ATOM   1356  C CG    . LEU A 1 175 ? 22.772  -4.976  -10.567 1.00 46.50  ? 176 LEU A CG    1 
ATOM   1357  C CD1   . LEU A 1 175 ? 23.903  -5.942  -10.252 1.00 47.34  ? 176 LEU A CD1   1 
ATOM   1358  C CD2   . LEU A 1 175 ? 21.435  -5.695  -10.563 1.00 52.80  ? 176 LEU A CD2   1 
ATOM   1359  N N     . THR A 1 176 ? 21.077  -0.612  -8.820  1.00 48.23  ? 177 THR A N     1 
ATOM   1360  C CA    . THR A 1 176 ? 21.153  0.516   -7.904  1.00 43.49  ? 177 THR A CA    1 
ATOM   1361  C C     . THR A 1 176 ? 19.744  1.005   -7.579  1.00 43.90  ? 177 THR A C     1 
ATOM   1362  O O     . THR A 1 176 ? 19.569  1.885   -6.740  1.00 46.15  ? 177 THR A O     1 
ATOM   1363  C CB    . THR A 1 176 ? 22.010  1.625   -8.514  1.00 43.23  ? 177 THR A CB    1 
ATOM   1364  O OG1   . THR A 1 176 ? 21.264  2.134   -9.615  1.00 43.83  ? 177 THR A OG1   1 
ATOM   1365  C CG2   . THR A 1 176 ? 23.367  1.126   -8.977  1.00 43.70  ? 177 THR A CG2   1 
ATOM   1366  N N     . GLN A 1 177 ? 18.747  0.432   -8.263  1.00 41.26  ? 178 GLN A N     1 
ATOM   1367  C CA    . GLN A 1 177 ? 17.350  0.721   -7.985  1.00 40.97  ? 178 GLN A CA    1 
ATOM   1368  C C     . GLN A 1 177 ? 16.753  -0.461  -7.224  1.00 43.03  ? 178 GLN A C     1 
ATOM   1369  O O     . GLN A 1 177 ? 17.270  -1.573  -7.300  1.00 38.69  ? 178 GLN A O     1 
ATOM   1370  C CB    . GLN A 1 177 ? 16.593  0.981   -9.289  1.00 41.92  ? 178 GLN A CB    1 
ATOM   1371  C CG    . GLN A 1 177 ? 17.141  2.144   -10.111 1.00 45.74  ? 178 GLN A CG    1 
ATOM   1372  C CD    . GLN A 1 177 ? 16.758  3.501   -9.560  1.00 49.04  ? 178 GLN A CD    1 
ATOM   1373  O OE1   . GLN A 1 177 ? 16.033  3.614   -8.565  1.00 47.14  ? 178 GLN A OE1   1 
ATOM   1374  N NE2   . GLN A 1 177 ? 17.235  4.550   -10.214 1.00 47.84  ? 178 GLN A NE2   1 
ATOM   1375  N N     . PHE A 1 178 ? 15.665  -0.208  -6.486  1.00 45.59  ? 179 PHE A N     1 
ATOM   1376  C CA    . PHE A 1 178 ? 15.035  -1.242  -5.679  1.00 45.37  ? 179 PHE A CA    1 
ATOM   1377  C C     . PHE A 1 178 ? 13.642  -1.545  -6.224  1.00 39.89  ? 179 PHE A C     1 
ATOM   1378  O O     . PHE A 1 178 ? 12.873  -2.273  -5.600  1.00 47.24  ? 179 PHE A O     1 
ATOM   1379  C CB    . PHE A 1 178 ? 15.003  -0.838  -4.201  1.00 45.16  ? 179 PHE A CB    1 
ATOM   1380  C CG    . PHE A 1 178 ? 16.280  -1.177  -3.445  1.00 48.06  ? 179 PHE A CG    1 
ATOM   1381  C CD1   . PHE A 1 178 ? 16.550  -2.487  -3.064  1.00 49.44  ? 179 PHE A CD1   1 
ATOM   1382  C CD2   . PHE A 1 178 ? 17.200  -0.191  -3.105  1.00 51.93  ? 179 PHE A CD2   1 
ATOM   1383  C CE1   . PHE A 1 178 ? 17.712  -2.802  -2.378  1.00 50.93  ? 179 PHE A CE1   1 
ATOM   1384  C CE2   . PHE A 1 178 ? 18.359  -0.512  -2.414  1.00 53.87  ? 179 PHE A CE2   1 
ATOM   1385  C CZ    . PHE A 1 178 ? 18.612  -1.815  -2.053  1.00 55.27  ? 179 PHE A CZ    1 
ATOM   1386  N N     . HIS A 1 179 ? 13.333  -0.983  -7.395  1.00 39.82  ? 180 HIS A N     1 
ATOM   1387  C CA    . HIS A 1 179 ? 12.126  -1.336  -8.123  1.00 45.31  ? 180 HIS A CA    1 
ATOM   1388  C C     . HIS A 1 179 ? 12.333  -1.006  -9.597  1.00 45.72  ? 180 HIS A C     1 
ATOM   1389  O O     . HIS A 1 179 ? 13.204  -0.212  -9.942  1.00 47.77  ? 180 HIS A O     1 
ATOM   1390  C CB    . HIS A 1 179 ? 10.903  -0.612  -7.551  1.00 50.82  ? 180 HIS A CB    1 
ATOM   1391  C CG    . HIS A 1 179 ? 10.891  0.854   -7.823  1.00 57.45  ? 180 HIS A CG    1 
ATOM   1392  N ND1   . HIS A 1 179 ? 10.420  1.385   -9.004  1.00 61.08  ? 180 HIS A ND1   1 
ATOM   1393  C CD2   . HIS A 1 179 ? 11.298  1.895   -7.085  1.00 61.13  ? 180 HIS A CD2   1 
ATOM   1394  C CE1   . HIS A 1 179 ? 10.536  2.704   -8.967  1.00 66.47  ? 180 HIS A CE1   1 
ATOM   1395  N NE2   . HIS A 1 179 ? 11.066  3.036   -7.810  1.00 70.09  ? 180 HIS A NE2   1 
ATOM   1396  N N     . THR A 1 180 ? 11.522  -1.629  -10.457 1.00 49.25  ? 181 THR A N     1 
ATOM   1397  C CA    . THR A 1 180 ? 11.606  -1.397  -11.889 1.00 49.40  ? 181 THR A CA    1 
ATOM   1398  C C     . THR A 1 180 ? 10.414  -0.549  -12.321 1.00 46.68  ? 181 THR A C     1 
ATOM   1399  O O     . THR A 1 180 ? 9.720   0.024   -11.484 1.00 39.18  ? 181 THR A O     1 
ATOM   1400  C CB    . THR A 1 180 ? 11.650  -2.735  -12.627 1.00 48.30  ? 181 THR A CB    1 
ATOM   1401  O OG1   . THR A 1 180 ? 11.975  -2.413  -13.975 1.00 55.91  ? 181 THR A OG1   1 
ATOM   1402  C CG2   . THR A 1 180 ? 10.329  -3.480  -12.569 1.00 50.08  ? 181 THR A CG2   1 
ATOM   1403  N N     . SER A 1 181 ? 10.190  -0.477  -13.636 1.00 50.44  ? 182 SER A N     1 
ATOM   1404  C CA    . SER A 1 181 ? 9.089   0.296   -14.186 1.00 48.99  ? 182 SER A CA    1 
ATOM   1405  C C     . SER A 1 181 ? 8.121   -0.628  -14.919 1.00 50.69  ? 182 SER A C     1 
ATOM   1406  O O     . SER A 1 181 ? 8.457   -1.768  -15.230 1.00 44.00  ? 182 SER A O     1 
ATOM   1407  C CB    . SER A 1 181 ? 9.593   1.392   -15.089 1.00 52.53  ? 182 SER A CB    1 
ATOM   1408  O OG    . SER A 1 181 ? 10.354  0.860   -16.164 1.00 58.52  ? 182 SER A OG    1 
ATOM   1409  N N     . SER A 1 182 ? 6.916   -0.114  -15.186 1.00 52.41  ? 183 SER A N     1 
ATOM   1410  C CA    . SER A 1 182 ? 5.874   -0.885  -15.843 1.00 52.08  ? 183 SER A CA    1 
ATOM   1411  C C     . SER A 1 182 ? 6.295   -1.223  -17.270 1.00 51.47  ? 183 SER A C     1 
ATOM   1412  O O     . SER A 1 182 ? 5.884   -2.244  -17.816 1.00 53.38  ? 183 SER A O     1 
ATOM   1413  C CB    . SER A 1 182 ? 4.558   -0.146  -15.821 1.00 49.62  ? 183 SER A CB    1 
ATOM   1414  O OG    . SER A 1 182 ? 4.662   1.100   -16.496 1.00 48.16  ? 183 SER A OG    1 
ATOM   1415  N N     . ASP A 1 183 ? 7.118   -0.352  -17.863 1.00 50.02  ? 184 ASP A N     1 
ATOM   1416  C CA    . ASP A 1 183 ? 7.581   -0.538  -19.228 1.00 48.54  ? 184 ASP A CA    1 
ATOM   1417  C C     . ASP A 1 183 ? 8.495   -1.759  -19.288 1.00 46.48  ? 184 ASP A C     1 
ATOM   1418  O O     . ASP A 1 183 ? 8.454   -2.524  -20.249 1.00 40.72  ? 184 ASP A O     1 
ATOM   1419  C CB    . ASP A 1 183 ? 8.255   0.718   -19.760 1.00 52.63  ? 184 ASP A CB    1 
ATOM   1420  C CG    . ASP A 1 183 ? 9.461   1.202   -18.967 1.00 60.98  ? 184 ASP A CG    1 
ATOM   1421  O OD1   . ASP A 1 183 ? 9.285   1.529   -17.775 1.00 62.46  ? 184 ASP A OD1   1 
ATOM   1422  O OD2   . ASP A 1 183 ? 10.565  1.251   -19.549 1.00 62.32  ? 184 ASP A OD2   1 
ATOM   1423  N N     . ARG A 1 184 ? 9.317   -1.929  -18.246 1.00 45.30  ? 185 ARG A N     1 
ATOM   1424  C CA    . ARG A 1 184 ? 10.231  -3.057  -18.157 1.00 43.69  ? 185 ARG A CA    1 
ATOM   1425  C C     . ARG A 1 184 ? 9.433   -4.349  -18.000 1.00 41.57  ? 185 ARG A C     1 
ATOM   1426  O O     . ARG A 1 184 ? 9.836   -5.397  -18.499 1.00 36.45  ? 185 ARG A O     1 
ATOM   1427  C CB    . ARG A 1 184 ? 11.192  -2.890  -16.974 1.00 47.85  ? 185 ARG A CB    1 
ATOM   1428  C CG    . ARG A 1 184 ? 12.173  -1.732  -17.096 1.00 53.21  ? 185 ARG A CG    1 
ATOM   1429  C CD    . ARG A 1 184 ? 13.194  -1.951  -18.203 1.00 57.65  ? 185 ARG A CD    1 
ATOM   1430  N NE    . ARG A 1 184 ? 14.232  -0.913  -18.212 1.00 62.26  ? 185 ARG A NE    1 
ATOM   1431  C CZ    . ARG A 1 184 ? 14.528  -0.140  -19.250 1.00 66.94  ? 185 ARG A CZ    1 
ATOM   1432  N NH1   . ARG A 1 184 ? 13.874  -0.278  -20.390 1.00 71.53  ? 185 ARG A NH1   1 
ATOM   1433  N NH2   . ARG A 1 184 ? 15.482  0.768   -19.145 1.00 68.66  ? 185 ARG A NH2   1 
ATOM   1434  N N     . LEU A 1 185 ? 8.303   -4.257  -17.291 1.00 41.62  ? 186 LEU A N     1 
ATOM   1435  C CA    . LEU A 1 185 ? 7.468   -5.414  -17.017 1.00 39.99  ? 186 LEU A CA    1 
ATOM   1436  C C     . LEU A 1 185 ? 6.705   -5.804  -18.281 1.00 38.20  ? 186 LEU A C     1 
ATOM   1437  O O     . LEU A 1 185 ? 6.361   -6.969  -18.465 1.00 41.36  ? 186 LEU A O     1 
ATOM   1438  C CB    . LEU A 1 185 ? 6.520   -5.106  -15.857 1.00 40.46  ? 186 LEU A CB    1 
ATOM   1439  C CG    . LEU A 1 185 ? 7.180   -4.856  -14.497 1.00 39.89  ? 186 LEU A CG    1 
ATOM   1440  C CD1   . LEU A 1 185 ? 6.136   -4.572  -13.428 1.00 39.12  ? 186 LEU A CD1   1 
ATOM   1441  C CD2   . LEU A 1 185 ? 8.055   -6.030  -14.090 1.00 40.49  ? 186 LEU A CD2   1 
ATOM   1442  N N     . GLN A 1 186 ? 6.455   -4.820  -19.151 1.00 39.04  ? 187 GLN A N     1 
ATOM   1443  C CA    . GLN A 1 186 ? 5.707   -5.048  -20.377 1.00 42.63  ? 187 GLN A CA    1 
ATOM   1444  C C     . GLN A 1 186 ? 6.566   -5.845  -21.356 1.00 42.81  ? 187 GLN A C     1 
ATOM   1445  O O     . GLN A 1 186 ? 6.064   -6.721  -22.057 1.00 42.00  ? 187 GLN A O     1 
ATOM   1446  C CB    . GLN A 1 186 ? 5.255   -3.717  -20.981 1.00 41.64  ? 187 GLN A CB    1 
ATOM   1447  C CG    . GLN A 1 186 ? 4.493   -3.854  -22.296 1.00 40.90  ? 187 GLN A CG    1 
ATOM   1448  C CD    . GLN A 1 186 ? 3.221   -4.665  -22.172 1.00 40.91  ? 187 GLN A CD    1 
ATOM   1449  O OE1   . GLN A 1 186 ? 2.357   -4.387  -21.333 1.00 41.41  ? 187 GLN A OE1   1 
ATOM   1450  N NE2   . GLN A 1 186 ? 3.092   -5.680  -23.013 1.00 43.71  ? 187 GLN A NE2   1 
ATOM   1451  N N     . ILE A 1 187 ? 7.865   -5.528  -21.393 1.00 41.11  ? 188 ILE A N     1 
ATOM   1452  C CA    . ILE A 1 187 ? 8.811   -6.233  -22.242 1.00 42.98  ? 188 ILE A CA    1 
ATOM   1453  C C     . ILE A 1 187 ? 8.891   -7.691  -21.798 1.00 39.76  ? 188 ILE A C     1 
ATOM   1454  O O     . ILE A 1 187 ? 8.950   -8.595  -22.629 1.00 40.68  ? 188 ILE A O     1 
ATOM   1455  C CB    . ILE A 1 187 ? 10.187  -5.543  -22.210 1.00 44.86  ? 188 ILE A CB    1 
ATOM   1456  C CG1   . ILE A 1 187 ? 10.192  -4.278  -23.071 1.00 46.34  ? 188 ILE A CG1   1 
ATOM   1457  C CG2   . ILE A 1 187 ? 11.295  -6.511  -22.625 1.00 47.26  ? 188 ILE A CG2   1 
ATOM   1458  C CD1   . ILE A 1 187 ? 11.266  -3.274  -22.696 1.00 48.64  ? 188 ILE A CD1   1 
ATOM   1459  N N     . LEU A 1 188 ? 8.890   -7.903  -20.478 1.00 36.17  ? 189 LEU A N     1 
ATOM   1460  C CA    . LEU A 1 188 ? 8.940   -9.240  -19.911 1.00 34.68  ? 189 LEU A CA    1 
ATOM   1461  C C     . LEU A 1 188 ? 7.679   -10.004 -20.308 1.00 33.67  ? 189 LEU A C     1 
ATOM   1462  O O     . LEU A 1 188 ? 7.746   -11.178 -20.663 1.00 30.88  ? 189 LEU A O     1 
ATOM   1463  C CB    . LEU A 1 188 ? 9.098   -9.144  -18.394 1.00 36.74  ? 189 LEU A CB    1 
ATOM   1464  C CG    . LEU A 1 188 ? 9.029   -10.465 -17.621 1.00 39.19  ? 189 LEU A CG    1 
ATOM   1465  C CD1   . LEU A 1 188 ? 10.026  -11.481 -18.154 1.00 37.51  ? 189 LEU A CD1   1 
ATOM   1466  C CD2   . LEU A 1 188 ? 9.260   -10.219 -16.139 1.00 40.27  ? 189 LEU A CD2   1 
ATOM   1467  N N     . VAL A 1 189 ? 6.532   -9.317  -20.248 1.00 35.14  ? 190 VAL A N     1 
ATOM   1468  C CA    . VAL A 1 189 ? 5.261   -9.901  -20.642 1.00 39.62  ? 190 VAL A CA    1 
ATOM   1469  C C     . VAL A 1 189 ? 5.356   -10.352 -22.097 1.00 40.85  ? 190 VAL A C     1 
ATOM   1470  O O     . VAL A 1 189 ? 4.938   -11.456 -22.439 1.00 45.28  ? 190 VAL A O     1 
ATOM   1471  C CB    . VAL A 1 189 ? 4.092   -8.915  -20.444 1.00 40.30  ? 190 VAL A CB    1 
ATOM   1472  C CG1   . VAL A 1 189 ? 2.828   -9.382  -21.155 1.00 41.89  ? 190 VAL A CG1   1 
ATOM   1473  C CG2   . VAL A 1 189 ? 3.815   -8.650  -18.969 1.00 42.55  ? 190 VAL A CG2   1 
ATOM   1474  N N     . GLU A 1 190 ? 5.911   -9.481  -22.945 1.00 41.60  ? 191 GLU A N     1 
ATOM   1475  C CA    . GLU A 1 190 ? 6.019   -9.747  -24.370 1.00 47.34  ? 191 GLU A CA    1 
ATOM   1476  C C     . GLU A 1 190 ? 6.923   -10.957 -24.598 1.00 41.29  ? 191 GLU A C     1 
ATOM   1477  O O     . GLU A 1 190 ? 6.666   -11.770 -25.483 1.00 39.87  ? 191 GLU A O     1 
ATOM   1478  C CB    . GLU A 1 190 ? 6.542   -8.508  -25.096 1.00 53.76  ? 191 GLU A CB    1 
ATOM   1479  C CG    . GLU A 1 190 ? 5.590   -7.317  -25.019 1.00 57.24  ? 191 GLU A CG    1 
ATOM   1480  C CD    . GLU A 1 190 ? 6.130   -6.038  -25.632 1.00 65.24  ? 191 GLU A CD    1 
ATOM   1481  O OE1   . GLU A 1 190 ? 7.282   -6.052  -26.117 1.00 71.99  ? 191 GLU A OE1   1 
ATOM   1482  O OE2   . GLU A 1 190 ? 5.398   -5.026  -25.624 1.00 69.95  ? 191 GLU A OE2   1 
ATOM   1483  N N     . GLN A 1 191 ? 7.977   -11.065 -23.784 1.00 35.98  ? 192 GLN A N     1 
ATOM   1484  C CA    . GLN A 1 191 ? 8.933   -12.155 -23.889 1.00 35.03  ? 192 GLN A CA    1 
ATOM   1485  C C     . GLN A 1 191 ? 8.274   -13.466 -23.465 1.00 36.94  ? 192 GLN A C     1 
ATOM   1486  O O     . GLN A 1 191 ? 8.550   -14.517 -24.040 1.00 35.19  ? 192 GLN A O     1 
ATOM   1487  C CB    . GLN A 1 191 ? 10.165  -11.839 -23.041 1.00 37.35  ? 192 GLN A CB    1 
ATOM   1488  C CG    . GLN A 1 191 ? 10.931  -13.068 -22.565 1.00 37.23  ? 192 GLN A CG    1 
ATOM   1489  C CD    . GLN A 1 191 ? 12.123  -12.719 -21.701 1.00 39.96  ? 192 GLN A CD    1 
ATOM   1490  O OE1   . GLN A 1 191 ? 12.060  -11.823 -20.853 1.00 39.43  ? 192 GLN A OE1   1 
ATOM   1491  N NE2   . GLN A 1 191 ? 13.233  -13.407 -21.928 1.00 35.76  ? 192 GLN A NE2   1 
ATOM   1492  N N     . LEU A 1 192 ? 7.402   -13.390 -22.454 1.00 38.73  ? 193 LEU A N     1 
ATOM   1493  C CA    . LEU A 1 192 ? 6.739   -14.569 -21.919 1.00 37.08  ? 193 LEU A CA    1 
ATOM   1494  C C     . LEU A 1 192 ? 5.645   -15.027 -22.880 1.00 34.88  ? 193 LEU A C     1 
ATOM   1495  O O     . LEU A 1 192 ? 5.164   -16.154 -22.786 1.00 34.62  ? 193 LEU A O     1 
ATOM   1496  C CB    . LEU A 1 192 ? 6.176   -14.261 -20.532 1.00 38.20  ? 193 LEU A CB    1 
ATOM   1497  C CG    . LEU A 1 192 ? 7.195   -14.211 -19.390 1.00 40.11  ? 193 LEU A CG    1 
ATOM   1498  C CD1   . LEU A 1 192 ? 6.567   -13.668 -18.118 1.00 38.18  ? 193 LEU A CD1   1 
ATOM   1499  C CD2   . LEU A 1 192 ? 7.791   -15.588 -19.143 1.00 40.73  ? 193 LEU A CD2   1 
ATOM   1500  N N     . ASN A 1 193 ? 5.270   -14.146 -23.813 1.00 37.64  ? 194 ASN A N     1 
ATOM   1501  C CA    . ASN A 1 193 ? 4.171   -14.418 -24.725 1.00 39.75  ? 194 ASN A CA    1 
ATOM   1502  C C     . ASN A 1 193 ? 4.626   -15.418 -25.786 1.00 40.42  ? 194 ASN A C     1 
ATOM   1503  O O     . ASN A 1 193 ? 3.848   -15.796 -26.659 1.00 41.73  ? 194 ASN A O     1 
ATOM   1504  C CB    . ASN A 1 193 ? 3.625   -13.132 -25.338 1.00 40.20  ? 194 ASN A CB    1 
ATOM   1505  C CG    . ASN A 1 193 ? 2.294   -13.345 -26.020 1.00 39.39  ? 194 ASN A CG    1 
ATOM   1506  O OD1   . ASN A 1 193 ? 1.394   -13.970 -25.447 1.00 37.70  ? 194 ASN A OD1   1 
ATOM   1507  N ND2   . ASN A 1 193 ? 2.151   -12.848 -27.239 1.00 39.63  ? 194 ASN A ND2   1 
ATOM   1508  N N     . GLN A 1 194 ? 5.891   -15.843 -25.695 1.00 37.43  ? 195 GLN A N     1 
ATOM   1509  C CA    . GLN A 1 194 ? 6.423   -16.866 -26.581 1.00 39.26  ? 195 GLN A CA    1 
ATOM   1510  C C     . GLN A 1 194 ? 5.819   -18.219 -26.213 1.00 39.54  ? 195 GLN A C     1 
ATOM   1511  O O     . GLN A 1 194 ? 5.577   -19.050 -27.085 1.00 38.80  ? 195 GLN A O     1 
ATOM   1512  C CB    . GLN A 1 194 ? 7.947   -16.947 -26.495 1.00 40.40  ? 195 GLN A CB    1 
ATOM   1513  C CG    . GLN A 1 194 ? 8.671   -15.728 -27.056 1.00 38.15  ? 195 GLN A CG    1 
ATOM   1514  C CD    . GLN A 1 194 ? 10.159  -15.748 -26.780 1.00 41.39  ? 195 GLN A CD    1 
ATOM   1515  O OE1   . GLN A 1 194 ? 10.893  -16.621 -27.257 1.00 45.98  ? 195 GLN A OE1   1 
ATOM   1516  N NE2   . GLN A 1 194 ? 10.619  -14.783 -25.998 1.00 42.91  ? 195 GLN A NE2   1 
ATOM   1517  N N     . TRP A 1 195 ? 5.579   -18.426 -24.912 1.00 40.71  ? 196 TRP A N     1 
ATOM   1518  C CA    . TRP A 1 195 ? 5.127   -19.716 -24.416 1.00 40.13  ? 196 TRP A CA    1 
ATOM   1519  C C     . TRP A 1 195 ? 3.776   -19.584 -23.711 1.00 38.92  ? 196 TRP A C     1 
ATOM   1520  O O     . TRP A 1 195 ? 3.024   -20.553 -23.635 1.00 41.83  ? 196 TRP A O     1 
ATOM   1521  C CB    . TRP A 1 195 ? 6.177   -20.323 -23.473 1.00 40.74  ? 196 TRP A CB    1 
ATOM   1522  C CG    . TRP A 1 195 ? 7.587   -20.305 -24.007 1.00 36.48  ? 196 TRP A CG    1 
ATOM   1523  C CD1   . TRP A 1 195 ? 8.225   -21.297 -24.693 1.00 33.11  ? 196 TRP A CD1   1 
ATOM   1524  C CD2   . TRP A 1 195 ? 8.546   -19.234 -23.870 1.00 32.59  ? 196 TRP A CD2   1 
ATOM   1525  N NE1   . TRP A 1 195 ? 9.506   -20.919 -24.998 1.00 32.51  ? 196 TRP A NE1   1 
ATOM   1526  C CE2   . TRP A 1 195 ? 9.732   -19.660 -24.507 1.00 33.74  ? 196 TRP A CE2   1 
ATOM   1527  C CE3   . TRP A 1 195 ? 8.517   -17.967 -23.278 1.00 34.96  ? 196 TRP A CE3   1 
ATOM   1528  C CZ2   . TRP A 1 195 ? 10.872  -18.860 -24.566 1.00 31.73  ? 196 TRP A CZ2   1 
ATOM   1529  C CZ3   . TRP A 1 195 ? 9.645   -17.179 -23.337 1.00 35.36  ? 196 TRP A CZ3   1 
ATOM   1530  C CH2   . TRP A 1 195 ? 10.805  -17.621 -23.971 1.00 32.75  ? 196 TRP A CH2   1 
ATOM   1531  N N     . TYR A 1 196 ? 3.472   -18.385 -23.196 1.00 36.56  ? 197 TYR A N     1 
ATOM   1532  C CA    . TYR A 1 196 ? 2.287   -18.190 -22.373 1.00 35.26  ? 197 TYR A CA    1 
ATOM   1533  C C     . TYR A 1 196 ? 1.382   -17.124 -22.987 1.00 34.36  ? 197 TYR A C     1 
ATOM   1534  O O     . TYR A 1 196 ? 1.842   -16.042 -23.344 1.00 36.43  ? 197 TYR A O     1 
ATOM   1535  C CB    . TYR A 1 196 ? 2.673   -17.786 -20.946 1.00 33.06  ? 197 TYR A CB    1 
ATOM   1536  C CG    . TYR A 1 196 ? 3.580   -18.770 -20.220 1.00 31.85  ? 197 TYR A CG    1 
ATOM   1537  C CD1   . TYR A 1 196 ? 3.053   -19.841 -19.509 1.00 33.59  ? 197 TYR A CD1   1 
ATOM   1538  C CD2   . TYR A 1 196 ? 4.961   -18.616 -20.230 1.00 31.46  ? 197 TYR A CD2   1 
ATOM   1539  C CE1   . TYR A 1 196 ? 3.872   -20.738 -18.844 1.00 32.24  ? 197 TYR A CE1   1 
ATOM   1540  C CE2   . TYR A 1 196 ? 5.791   -19.505 -19.567 1.00 32.52  ? 197 TYR A CE2   1 
ATOM   1541  C CZ    . TYR A 1 196 ? 5.245   -20.569 -18.872 1.00 31.18  ? 197 TYR A CZ    1 
ATOM   1542  O OH    . TYR A 1 196 ? 6.052   -21.451 -18.212 1.00 34.32  ? 197 TYR A OH    1 
ATOM   1543  N N     . PRO A 1 197 ? 0.060   -17.391 -23.099 1.00 37.14  ? 198 PRO A N     1 
ATOM   1544  C CA    . PRO A 1 197 ? -0.896  -16.394 -23.589 1.00 40.69  ? 198 PRO A CA    1 
ATOM   1545  C C     . PRO A 1 197 ? -0.971  -15.179 -22.667 1.00 40.65  ? 198 PRO A C     1 
ATOM   1546  O O     . PRO A 1 197 ? -0.518  -15.231 -21.526 1.00 43.05  ? 198 PRO A O     1 
ATOM   1547  C CB    . PRO A 1 197 ? -2.232  -17.169 -23.648 1.00 39.84  ? 198 PRO A CB    1 
ATOM   1548  C CG    . PRO A 1 197 ? -1.824  -18.632 -23.647 1.00 40.86  ? 198 PRO A CG    1 
ATOM   1549  C CD    . PRO A 1 197 ? -0.573  -18.680 -22.791 1.00 38.41  ? 198 PRO A CD    1 
ATOM   1550  N N     . LEU A 1 198 ? -1.563  -14.091 -23.174 1.00 43.62  ? 199 LEU A N     1 
ATOM   1551  C CA    . LEU A 1 198 ? -1.632  -12.838 -22.439 1.00 45.83  ? 199 LEU A CA    1 
ATOM   1552  C C     . LEU A 1 198 ? -2.681  -12.945 -21.334 1.00 46.15  ? 199 LEU A C     1 
ATOM   1553  O O     . LEU A 1 198 ? -2.582  -12.265 -20.315 1.00 44.31  ? 199 LEU A O     1 
ATOM   1554  C CB    . LEU A 1 198 ? -1.940  -11.683 -23.392 1.00 44.96  ? 199 LEU A CB    1 
ATOM   1555  C CG    . LEU A 1 198 ? -0.873  -11.383 -24.450 1.00 49.26  ? 199 LEU A CG    1 
ATOM   1556  C CD1   . LEU A 1 198 ? -1.200  -10.107 -25.211 1.00 47.82  ? 199 LEU A CD1   1 
ATOM   1557  C CD2   . LEU A 1 198 ? 0.506   -11.294 -23.818 1.00 49.25  ? 199 LEU A CD2   1 
ATOM   1558  N N     . ASP A 1 199 ? -3.679  -13.809 -21.547 1.00 44.70  ? 200 ASP A N     1 
ATOM   1559  C CA    . ASP A 1 199 ? -4.769  -13.968 -20.599 1.00 46.88  ? 200 ASP A CA    1 
ATOM   1560  C C     . ASP A 1 199 ? -4.454  -15.117 -19.645 1.00 44.72  ? 200 ASP A C     1 
ATOM   1561  O O     . ASP A 1 199 ? -5.305  -15.524 -18.857 1.00 43.75  ? 200 ASP A O     1 
ATOM   1562  C CB    . ASP A 1 199 ? -6.096  -14.179 -21.312 1.00 52.53  ? 200 ASP A CB    1 
ATOM   1563  C CG    . ASP A 1 199 ? -6.174  -15.420 -22.189 1.00 59.06  ? 200 ASP A CG    1 
ATOM   1564  O OD1   . ASP A 1 199 ? -5.164  -16.151 -22.260 1.00 63.97  ? 200 ASP A OD1   1 
ATOM   1565  O OD2   . ASP A 1 199 ? -7.245  -15.645 -22.792 1.00 69.28  ? 200 ASP A OD2   1 
ATOM   1566  N N     . HIS A 1 200 ? -3.223  -15.633 -19.726 1.00 40.15  ? 201 HIS A N     1 
ATOM   1567  C CA    . HIS A 1 200 ? -2.784  -16.708 -18.852 1.00 41.78  ? 201 HIS A CA    1 
ATOM   1568  C C     . HIS A 1 200 ? -2.756  -16.199 -17.413 1.00 37.36  ? 201 HIS A C     1 
ATOM   1569  O O     . HIS A 1 200 ? -2.112  -15.195 -17.118 1.00 32.64  ? 201 HIS A O     1 
ATOM   1570  C CB    . HIS A 1 200 ? -1.423  -17.252 -19.303 1.00 41.07  ? 201 HIS A CB    1 
ATOM   1571  C CG    . HIS A 1 200 ? -0.930  -18.398 -18.483 1.00 39.41  ? 201 HIS A CG    1 
ATOM   1572  N ND1   . HIS A 1 200 ? -1.356  -19.694 -18.683 1.00 36.70  ? 201 HIS A ND1   1 
ATOM   1573  C CD2   . HIS A 1 200 ? -0.068  -18.447 -17.458 1.00 38.62  ? 201 HIS A CD2   1 
ATOM   1574  C CE1   . HIS A 1 200 ? -0.759  -20.490 -17.809 1.00 37.00  ? 201 HIS A CE1   1 
ATOM   1575  N NE2   . HIS A 1 200 ? 0.027   -19.754 -17.054 1.00 37.53  ? 201 HIS A NE2   1 
ATOM   1576  N N     . GLU A 1 201 ? -3.472  -16.901 -16.529 1.00 35.95  ? 202 GLU A N     1 
ATOM   1577  C CA    . GLU A 1 201 ? -3.571  -16.505 -15.135 1.00 38.15  ? 202 GLU A CA    1 
ATOM   1578  C C     . GLU A 1 201 ? -2.245  -16.785 -14.434 1.00 35.57  ? 202 GLU A C     1 
ATOM   1579  O O     . GLU A 1 201 ? -1.779  -17.922 -14.411 1.00 34.24  ? 202 GLU A O     1 
ATOM   1580  C CB    . GLU A 1 201 ? -4.714  -17.243 -14.437 1.00 39.20  ? 202 GLU A CB    1 
ATOM   1581  C CG    . GLU A 1 201 ? -4.876  -16.853 -12.970 1.00 45.15  ? 202 GLU A CG    1 
ATOM   1582  C CD    . GLU A 1 201 ? -5.981  -17.595 -12.240 1.00 47.55  ? 202 GLU A CD    1 
ATOM   1583  O OE1   . GLU A 1 201 ? -6.924  -16.928 -11.765 1.00 46.48  ? 202 GLU A OE1   1 
ATOM   1584  O OE2   . GLU A 1 201 ? -5.898  -18.838 -12.143 1.00 46.13  ? 202 GLU A OE2   1 
ATOM   1585  N N     . VAL A 1 202 ? -1.647  -15.727 -13.876 1.00 35.22  ? 203 VAL A N     1 
ATOM   1586  C CA    . VAL A 1 202 ? -0.435  -15.845 -13.083 1.00 34.95  ? 203 VAL A CA    1 
ATOM   1587  C C     . VAL A 1 202 ? -0.778  -15.512 -11.633 1.00 34.45  ? 203 VAL A C     1 
ATOM   1588  O O     . VAL A 1 202 ? -1.902  -15.114 -11.336 1.00 35.69  ? 203 VAL A O     1 
ATOM   1589  C CB    . VAL A 1 202 ? 0.692   -14.939 -13.618 1.00 37.05  ? 203 VAL A CB    1 
ATOM   1590  C CG1   . VAL A 1 202 ? 1.233   -15.437 -14.953 1.00 42.17  ? 203 VAL A CG1   1 
ATOM   1591  C CG2   . VAL A 1 202 ? 0.251   -13.484 -13.725 1.00 37.19  ? 203 VAL A CG2   1 
ATOM   1592  N N     . VAL A 1 203 ? 0.202   -15.674 -10.738 1.00 35.71  ? 204 VAL A N     1 
ATOM   1593  C CA    . VAL A 1 203 ? -0.027  -15.493 -9.315  1.00 31.12  ? 204 VAL A CA    1 
ATOM   1594  C C     . VAL A 1 203 ? 1.129   -14.701 -8.710  1.00 31.13  ? 204 VAL A C     1 
ATOM   1595  O O     . VAL A 1 203 ? 2.286   -15.102 -8.820  1.00 32.12  ? 204 VAL A O     1 
ATOM   1596  C CB    . VAL A 1 203 ? -0.193  -16.852 -8.608  1.00 31.77  ? 204 VAL A CB    1 
ATOM   1597  C CG1   . VAL A 1 203 ? -0.344  -16.692 -7.099  1.00 32.69  ? 204 VAL A CG1   1 
ATOM   1598  C CG2   . VAL A 1 203 ? -1.354  -17.654 -9.184  1.00 31.79  ? 204 VAL A CG2   1 
ATOM   1599  N N     . ILE A 1 204 ? 0.796   -13.576 -8.067  1.00 30.61  ? 205 ILE A N     1 
ATOM   1600  C CA    . ILE A 1 204 ? 1.758   -12.829 -7.274  1.00 30.36  ? 205 ILE A CA    1 
ATOM   1601  C C     . ILE A 1 204 ? 1.675   -13.328 -5.836  1.00 30.42  ? 205 ILE A C     1 
ATOM   1602  O O     . ILE A 1 204 ? 0.660   -13.141 -5.168  1.00 30.62  ? 205 ILE A O     1 
ATOM   1603  C CB    . ILE A 1 204 ? 1.504   -11.313 -7.362  1.00 30.50  ? 205 ILE A CB    1 
ATOM   1604  C CG1   . ILE A 1 204 ? 1.580   -10.808 -8.802  1.00 31.39  ? 205 ILE A CG1   1 
ATOM   1605  C CG2   . ILE A 1 204 ? 2.461   -10.549 -6.446  1.00 28.96  ? 205 ILE A CG2   1 
ATOM   1606  C CD1   . ILE A 1 204 ? 1.253   -9.334  -8.958  1.00 33.87  ? 205 ILE A CD1   1 
ATOM   1607  N N     . TYR A 1 205 ? 2.753   -13.967 -5.371  1.00 28.81  ? 206 TYR A N     1 
ATOM   1608  C CA    . TYR A 1 205 ? 2.766   -14.584 -4.056  1.00 30.46  ? 206 TYR A CA    1 
ATOM   1609  C C     . TYR A 1 205 ? 3.670   -13.785 -3.121  1.00 30.72  ? 206 TYR A C     1 
ATOM   1610  O O     . TYR A 1 205 ? 4.712   -13.282 -3.532  1.00 31.86  ? 206 TYR A O     1 
ATOM   1611  C CB    . TYR A 1 205 ? 3.217   -16.045 -4.159  1.00 31.99  ? 206 TYR A CB    1 
ATOM   1612  C CG    . TYR A 1 205 ? 3.462   -16.713 -2.813  1.00 34.43  ? 206 TYR A CG    1 
ATOM   1613  C CD1   . TYR A 1 205 ? 2.403   -17.108 -2.005  1.00 34.63  ? 206 TYR A CD1   1 
ATOM   1614  C CD2   . TYR A 1 205 ? 4.751   -16.957 -2.356  1.00 35.78  ? 206 TYR A CD2   1 
ATOM   1615  C CE1   . TYR A 1 205 ? 2.618   -17.713 -0.778  1.00 38.11  ? 206 TYR A CE1   1 
ATOM   1616  C CE2   . TYR A 1 205 ? 4.980   -17.565 -1.132  1.00 35.89  ? 206 TYR A CE2   1 
ATOM   1617  C CZ    . TYR A 1 205 ? 3.910   -17.943 -0.341  1.00 37.13  ? 206 TYR A CZ    1 
ATOM   1618  O OH    . TYR A 1 205 ? 4.127   -18.543 0.866   1.00 40.84  ? 206 TYR A OH    1 
ATOM   1619  N N     . GLU A 1 206 ? 3.243   -13.680 -1.859  1.00 29.82  ? 207 GLU A N     1 
ATOM   1620  C CA    . GLU A 1 206 ? 4.051   -13.077 -0.812  1.00 33.30  ? 207 GLU A CA    1 
ATOM   1621  C C     . GLU A 1 206 ? 3.804   -13.826 0.494   1.00 34.29  ? 207 GLU A C     1 
ATOM   1622  O O     . GLU A 1 206 ? 2.750   -13.680 1.108   1.00 41.54  ? 207 GLU A O     1 
ATOM   1623  C CB    . GLU A 1 206 ? 3.725   -11.595 -0.630  1.00 33.40  ? 207 GLU A CB    1 
ATOM   1624  C CG    . GLU A 1 206 ? 4.057   -10.738 -1.848  1.00 35.26  ? 207 GLU A CG    1 
ATOM   1625  C CD    . GLU A 1 206 ? 3.749   -9.263  -1.658  1.00 38.97  ? 207 GLU A CD    1 
ATOM   1626  O OE1   . GLU A 1 206 ? 3.259   -8.897  -0.568  1.00 47.77  ? 207 GLU A OE1   1 
ATOM   1627  O OE2   . GLU A 1 206 ? 3.997   -8.480  -2.598  1.00 39.91  ? 207 GLU A OE2   1 
ATOM   1628  N N     . ALA A 1 207 ? 4.788   -14.633 0.903   1.00 33.48  ? 208 ALA A N     1 
ATOM   1629  C CA    . ALA A 1 207 ? 4.702   -15.375 2.148   1.00 34.85  ? 208 ALA A CA    1 
ATOM   1630  C C     . ALA A 1 207 ? 4.583   -14.399 3.314   1.00 31.26  ? 208 ALA A C     1 
ATOM   1631  O O     . ALA A 1 207 ? 5.182   -13.326 3.296   1.00 33.87  ? 208 ALA A O     1 
ATOM   1632  C CB    . ALA A 1 207 ? 5.909   -16.275 2.299   1.00 36.24  ? 208 ALA A CB    1 
ATOM   1633  N N     . ALA A 1 208 ? 3.795   -14.784 4.321   1.00 30.27  ? 209 ALA A N     1 
ATOM   1634  C CA    . ALA A 1 208 ? 3.601   -13.963 5.504   1.00 27.43  ? 209 ALA A CA    1 
ATOM   1635  C C     . ALA A 1 208 ? 4.858   -14.004 6.368   1.00 23.59  ? 209 ALA A C     1 
ATOM   1636  O O     . ALA A 1 208 ? 5.510   -15.040 6.477   1.00 22.42  ? 209 ALA A O     1 
ATOM   1637  C CB    . ALA A 1 208 ? 2.384   -14.437 6.268   1.00 27.42  ? 209 ALA A CB    1 
ATOM   1638  N N     . ASN A 1 209 ? 5.186   -12.857 6.973   1.00 21.08  ? 210 ASN A N     1 
ATOM   1639  C CA    . ASN A 1 209 ? 6.334   -12.747 7.856   1.00 21.87  ? 210 ASN A CA    1 
ATOM   1640  C C     . ASN A 1 209 ? 5.866   -12.781 9.309   1.00 21.89  ? 210 ASN A C     1 
ATOM   1641  O O     . ASN A 1 209 ? 6.673   -12.958 10.217  1.00 21.53  ? 210 ASN A O     1 
ATOM   1642  C CB    . ASN A 1 209 ? 7.138   -11.482 7.575   1.00 23.50  ? 210 ASN A CB    1 
ATOM   1643  C CG    . ASN A 1 209 ? 7.779   -11.504 6.208   1.00 23.33  ? 210 ASN A CG    1 
ATOM   1644  O OD1   . ASN A 1 209 ? 8.638   -12.351 5.938   1.00 24.90  ? 210 ASN A OD1   1 
ATOM   1645  N ND2   . ASN A 1 209 ? 7.385   -10.585 5.340   1.00 24.64  ? 210 ASN A ND2   1 
ATOM   1646  N N     . LEU A 1 210 ? 4.555   -12.606 9.514   1.00 22.40  ? 211 LEU A N     1 
ATOM   1647  C CA    . LEU A 1 210 ? 3.989   -12.546 10.852  1.00 23.93  ? 211 LEU A CA    1 
ATOM   1648  C C     . LEU A 1 210 ? 2.941   -13.642 11.017  1.00 22.55  ? 211 LEU A C     1 
ATOM   1649  O O     . LEU A 1 210 ? 2.236   -13.987 10.070  1.00 21.64  ? 211 LEU A O     1 
ATOM   1650  C CB    . LEU A 1 210 ? 3.396   -11.162 11.110  1.00 26.91  ? 211 LEU A CB    1 
ATOM   1651  C CG    . LEU A 1 210 ? 4.399   -10.008 11.208  1.00 29.45  ? 211 LEU A CG    1 
ATOM   1652  C CD1   . LEU A 1 210 ? 3.695   -8.711  11.571  1.00 31.66  ? 211 LEU A CD1   1 
ATOM   1653  C CD2   . LEU A 1 210 ? 5.497   -10.321 12.212  1.00 30.12  ? 211 LEU A CD2   1 
ATOM   1654  N N     . PRO A 1 211 ? 2.796   -14.201 12.240  1.00 21.15  ? 212 PRO A N     1 
ATOM   1655  C CA    . PRO A 1 211 ? 1.866   -15.306 12.480  1.00 21.84  ? 212 PRO A CA    1 
ATOM   1656  C C     . PRO A 1 211 ? 0.398   -14.898 12.365  1.00 26.30  ? 212 PRO A C     1 
ATOM   1657  O O     . PRO A 1 211 ? -0.476  -15.751 12.222  1.00 26.61  ? 212 PRO A O     1 
ATOM   1658  C CB    . PRO A 1 211 ? 2.237   -15.759 13.909  1.00 21.68  ? 212 PRO A CB    1 
ATOM   1659  C CG    . PRO A 1 211 ? 2.787   -14.507 14.563  1.00 20.82  ? 212 PRO A CG    1 
ATOM   1660  C CD    . PRO A 1 211 ? 3.526   -13.790 13.448  1.00 20.14  ? 212 PRO A CD    1 
ATOM   1661  N N     . ILE A 1 212 ? 0.142   -13.588 12.429  1.00 27.06  ? 213 ILE A N     1 
ATOM   1662  C CA    . ILE A 1 212 ? -1.213  -13.066 12.352  1.00 29.28  ? 213 ILE A CA    1 
ATOM   1663  C C     . ILE A 1 212 ? -1.469  -12.546 10.939  1.00 29.79  ? 213 ILE A C     1 
ATOM   1664  O O     . ILE A 1 212 ? -2.543  -12.025 10.650  1.00 32.11  ? 213 ILE A O     1 
ATOM   1665  C CB    . ILE A 1 212 ? -1.442  -11.975 13.415  1.00 33.99  ? 213 ILE A CB    1 
ATOM   1666  C CG1   . ILE A 1 212 ? -0.456  -10.815 13.262  1.00 36.37  ? 213 ILE A CG1   1 
ATOM   1667  C CG2   . ILE A 1 212 ? -1.396  -12.569 14.824  1.00 36.13  ? 213 ILE A CG2   1 
ATOM   1668  C CD1   . ILE A 1 212 ? -0.574  -10.066 11.946  1.00 38.06  ? 213 ILE A CD1   1 
ATOM   1669  N N     . GLN A 1 213 ? -0.474  -12.713 10.063  1.00 30.39  ? 214 GLN A N     1 
ATOM   1670  C CA    . GLN A 1 213 ? -0.549  -12.202 8.704   1.00 30.04  ? 214 GLN A CA    1 
ATOM   1671  C C     . GLN A 1 213 ? -0.960  -13.325 7.755   1.00 30.47  ? 214 GLN A C     1 
ATOM   1672  O O     . GLN A 1 213 ? -0.492  -14.455 7.878   1.00 29.64  ? 214 GLN A O     1 
ATOM   1673  C CB    . GLN A 1 213 ? 0.801   -11.612 8.295   1.00 32.42  ? 214 GLN A CB    1 
ATOM   1674  C CG    . GLN A 1 213 ? 0.822   -11.020 6.890   1.00 31.89  ? 214 GLN A CG    1 
ATOM   1675  C CD    . GLN A 1 213 ? 2.200   -10.565 6.460   1.00 33.65  ? 214 GLN A CD    1 
ATOM   1676  O OE1   . GLN A 1 213 ? 3.188   -10.727 7.185   1.00 33.94  ? 214 GLN A OE1   1 
ATOM   1677  N NE2   . GLN A 1 213 ? 2.281   -9.999  5.265   1.00 34.15  ? 214 GLN A NE2   1 
ATOM   1678  N N     . ALA A 1 214 ? -1.845  -12.993 6.811   1.00 35.30  ? 215 ALA A N     1 
ATOM   1679  C CA    . ALA A 1 214 ? -2.237  -13.918 5.761   1.00 36.86  ? 215 ALA A CA    1 
ATOM   1680  C C     . ALA A 1 214 ? -1.349  -13.696 4.541   1.00 34.81  ? 215 ALA A C     1 
ATOM   1681  O O     . ALA A 1 214 ? -0.983  -12.564 4.234   1.00 34.39  ? 215 ALA A O     1 
ATOM   1682  C CB    . ALA A 1 214 ? -3.700  -13.729 5.423   1.00 36.72  ? 215 ALA A CB    1 
ATOM   1683  N N     . PRO A 1 215 ? -0.972  -14.768 3.809   1.00 34.82  ? 216 PRO A N     1 
ATOM   1684  C CA    . PRO A 1 215 ? -0.130  -14.624 2.623   1.00 37.28  ? 216 PRO A CA    1 
ATOM   1685  C C     . PRO A 1 215 ? -0.864  -13.898 1.500   1.00 36.02  ? 216 PRO A C     1 
ATOM   1686  O O     . PRO A 1 215 ? -2.092  -13.889 1.459   1.00 40.44  ? 216 PRO A O     1 
ATOM   1687  C CB    . PRO A 1 215 ? 0.212   -16.081 2.259   1.00 37.51  ? 216 PRO A CB    1 
ATOM   1688  C CG    . PRO A 1 215 ? -0.960  -16.878 2.797   1.00 36.69  ? 216 PRO A CG    1 
ATOM   1689  C CD    . PRO A 1 215 ? -1.356  -16.162 4.076   1.00 35.54  ? 216 PRO A CD    1 
ATOM   1690  N N     . ARG A 1 216 ? -0.093  -13.279 0.601   1.00 34.50  ? 217 ARG A N     1 
ATOM   1691  C CA    . ARG A 1 216 ? -0.653  -12.634 -0.573  1.00 32.44  ? 217 ARG A CA    1 
ATOM   1692  C C     . ARG A 1 216 ? -0.676  -13.637 -1.721  1.00 30.39  ? 217 ARG A C     1 
ATOM   1693  O O     . ARG A 1 216 ? 0.359   -14.186 -2.092  1.00 25.31  ? 217 ARG A O     1 
ATOM   1694  C CB    . ARG A 1 216 ? 0.157   -11.393 -0.968  1.00 31.01  ? 217 ARG A CB    1 
ATOM   1695  C CG    . ARG A 1 216 ? -0.399  -10.653 -2.177  1.00 31.58  ? 217 ARG A CG    1 
ATOM   1696  C CD    . ARG A 1 216 ? 0.513   -9.529  -2.640  1.00 32.88  ? 217 ARG A CD    1 
ATOM   1697  N NE    . ARG A 1 216 ? -0.041  -8.796  -3.784  1.00 34.15  ? 217 ARG A NE    1 
ATOM   1698  C CZ    . ARG A 1 216 ? 0.596   -7.838  -4.447  1.00 36.02  ? 217 ARG A CZ    1 
ATOM   1699  N NH1   . ARG A 1 216 ? 1.828   -7.505  -4.105  1.00 36.16  ? 217 ARG A NH1   1 
ATOM   1700  N NH2   . ARG A 1 216 ? 0.004   -7.222  -5.454  1.00 35.83  ? 217 ARG A NH2   1 
ATOM   1701  N N     . ILE A 1 217 ? -1.875  -13.882 -2.258  1.00 32.86  ? 218 ILE A N     1 
ATOM   1702  C CA    . ILE A 1 217 ? -2.046  -14.756 -3.405  1.00 34.45  ? 218 ILE A CA    1 
ATOM   1703  C C     . ILE A 1 217 ? -2.949  -14.049 -4.410  1.00 38.32  ? 218 ILE A C     1 
ATOM   1704  O O     . ILE A 1 217 ? -4.145  -14.323 -4.478  1.00 35.95  ? 218 ILE A O     1 
ATOM   1705  C CB    . ILE A 1 217 ? -2.616  -16.123 -2.982  1.00 36.90  ? 218 ILE A CB    1 
ATOM   1706  C CG1   . ILE A 1 217 ? -1.785  -16.762 -1.869  1.00 34.29  ? 218 ILE A CG1   1 
ATOM   1707  C CG2   . ILE A 1 217 ? -2.753  -17.054 -4.189  1.00 39.63  ? 218 ILE A CG2   1 
ATOM   1708  C CD1   . ILE A 1 217 ? -2.292  -18.120 -1.419  1.00 36.52  ? 218 ILE A CD1   1 
ATOM   1709  N N     . GLU A 1 218 ? -2.356  -13.129 -5.178  1.00 38.55  ? 219 GLU A N     1 
ATOM   1710  C CA    . GLU A 1 218 ? -3.105  -12.302 -6.109  1.00 41.27  ? 219 GLU A CA    1 
ATOM   1711  C C     . GLU A 1 218 ? -3.048  -12.924 -7.501  1.00 39.07  ? 219 GLU A C     1 
ATOM   1712  O O     . GLU A 1 218 ? -1.981  -13.007 -8.108  1.00 32.26  ? 219 GLU A O     1 
ATOM   1713  C CB    . GLU A 1 218 ? -2.549  -10.878 -6.104  1.00 43.61  ? 219 GLU A CB    1 
ATOM   1714  C CG    . GLU A 1 218 ? -3.299  -9.931  -7.035  1.00 47.59  ? 219 GLU A CG    1 
ATOM   1715  C CD    . GLU A 1 218 ? -2.825  -8.490  -6.971  1.00 53.65  ? 219 GLU A CD    1 
ATOM   1716  O OE1   . GLU A 1 218 ? -1.956  -8.190  -6.125  1.00 51.55  ? 219 GLU A OE1   1 
ATOM   1717  O OE2   . GLU A 1 218 ? -3.318  -7.669  -7.774  1.00 58.88  ? 219 GLU A OE2   1 
ATOM   1718  N N     . ARG A 1 219 ? -4.214  -13.359 -7.990  1.00 40.62  ? 220 ARG A N     1 
ATOM   1719  C CA    . ARG A 1 219 ? -4.331  -13.955 -9.311  1.00 39.51  ? 220 ARG A CA    1 
ATOM   1720  C C     . ARG A 1 219 ? -4.754  -12.879 -10.307 1.00 38.65  ? 220 ARG A C     1 
ATOM   1721  O O     . ARG A 1 219 ? -5.641  -12.078 -10.022 1.00 38.57  ? 220 ARG A O     1 
ATOM   1722  C CB    . ARG A 1 219 ? -5.344  -15.105 -9.282  1.00 42.03  ? 220 ARG A CB    1 
ATOM   1723  C CG    . ARG A 1 219 ? -4.999  -16.214 -8.298  1.00 46.81  ? 220 ARG A CG    1 
ATOM   1724  C CD    . ARG A 1 219 ? -6.101  -17.259 -8.196  1.00 48.77  ? 220 ARG A CD    1 
ATOM   1725  N NE    . ARG A 1 219 ? -5.784  -18.301 -7.213  1.00 50.80  ? 220 ARG A NE    1 
ATOM   1726  C CZ    . ARG A 1 219 ? -4.827  -19.211 -7.354  1.00 54.13  ? 220 ARG A CZ    1 
ATOM   1727  N NH1   . ARG A 1 219 ? -4.128  -19.269 -8.473  1.00 57.52  ? 220 ARG A NH1   1 
ATOM   1728  N NH2   . ARG A 1 219 ? -4.589  -20.075 -6.383  1.00 51.07  ? 220 ARG A NH2   1 
ATOM   1729  N N     . LEU A 1 220 ? -4.108  -12.873 -11.478 1.00 38.37  ? 221 LEU A N     1 
ATOM   1730  C CA    . LEU A 1 220 ? -4.401  -11.892 -12.508 1.00 37.71  ? 221 LEU A CA    1 
ATOM   1731  C C     . LEU A 1 220 ? -3.837  -12.372 -13.841 1.00 39.34  ? 221 LEU A C     1 
ATOM   1732  O O     . LEU A 1 220 ? -2.889  -13.154 -13.875 1.00 36.15  ? 221 LEU A O     1 
ATOM   1733  C CB    . LEU A 1 220 ? -3.814  -10.537 -12.117 1.00 40.29  ? 221 LEU A CB    1 
ATOM   1734  C CG    . LEU A 1 220 ? -2.284  -10.451 -12.094 1.00 38.87  ? 221 LEU A CG    1 
ATOM   1735  C CD1   . LEU A 1 220 ? -1.828  -9.052  -11.717 1.00 41.02  ? 221 LEU A CD1   1 
ATOM   1736  C CD2   . LEU A 1 220 ? -1.687  -11.479 -11.149 1.00 38.19  ? 221 LEU A CD2   1 
ATOM   1737  N N     . PRO A 1 221 ? -4.398  -11.905 -14.978 1.00 38.34  ? 222 PRO A N     1 
ATOM   1738  C CA    . PRO A 1 221 ? -3.864  -12.247 -16.296 1.00 40.08  ? 222 PRO A CA    1 
ATOM   1739  C C     . PRO A 1 221 ? -2.465  -11.669 -16.491 1.00 39.42  ? 222 PRO A C     1 
ATOM   1740  O O     . PRO A 1 221 ? -2.189  -10.544 -16.080 1.00 36.31  ? 222 PRO A O     1 
ATOM   1741  C CB    . PRO A 1 221 ? -4.896  -11.650 -17.272 1.00 39.49  ? 222 PRO A CB    1 
ATOM   1742  C CG    . PRO A 1 221 ? -5.546  -10.529 -16.485 1.00 41.20  ? 222 PRO A CG    1 
ATOM   1743  C CD    . PRO A 1 221 ? -5.571  -11.022 -15.047 1.00 40.51  ? 222 PRO A CD    1 
ATOM   1744  N N     . LEU A 1 222 ? -1.592  -12.460 -17.121 1.00 39.94  ? 223 LEU A N     1 
ATOM   1745  C CA    . LEU A 1 222 ? -0.207  -12.075 -17.335 1.00 41.87  ? 223 LEU A CA    1 
ATOM   1746  C C     . LEU A 1 222 ? -0.139  -10.632 -17.830 1.00 39.27  ? 223 LEU A C     1 
ATOM   1747  O O     . LEU A 1 222 ? 0.789   -9.899  -17.495 1.00 40.18  ? 223 LEU A O     1 
ATOM   1748  C CB    . LEU A 1 222 ? 0.426   -13.040 -18.336 1.00 44.32  ? 223 LEU A CB    1 
ATOM   1749  C CG    . LEU A 1 222 ? 1.890   -12.768 -18.699 1.00 47.12  ? 223 LEU A CG    1 
ATOM   1750  C CD1   . LEU A 1 222 ? 2.798   -12.985 -17.501 1.00 47.19  ? 223 LEU A CD1   1 
ATOM   1751  C CD2   . LEU A 1 222 ? 2.326   -13.633 -19.869 1.00 47.31  ? 223 LEU A CD2   1 
ATOM   1752  N N     . ALA A 1 223 ? -1.143  -10.236 -18.619 1.00 37.20  ? 224 ALA A N     1 
ATOM   1753  C CA    . ALA A 1 223 ? -1.128  -8.959  -19.313 1.00 38.14  ? 224 ALA A CA    1 
ATOM   1754  C C     . ALA A 1 223 ? -1.144  -7.799  -18.321 1.00 37.79  ? 224 ALA A C     1 
ATOM   1755  O O     . ALA A 1 223 ? -0.640  -6.720  -18.623 1.00 33.84  ? 224 ALA A O     1 
ATOM   1756  C CB    . ALA A 1 223 ? -2.304  -8.883  -20.262 1.00 41.59  ? 224 ALA A CB    1 
ATOM   1757  N N     . ASN A 1 224 ? -1.723  -8.032  -17.137 1.00 37.28  ? 225 ASN A N     1 
ATOM   1758  C CA    . ASN A 1 224 ? -1.966  -6.966  -16.177 1.00 38.82  ? 225 ASN A CA    1 
ATOM   1759  C C     . ASN A 1 224 ? -0.784  -6.831  -15.220 1.00 37.77  ? 225 ASN A C     1 
ATOM   1760  O O     . ASN A 1 224 ? -0.787  -5.964  -14.350 1.00 40.85  ? 225 ASN A O     1 
ATOM   1761  C CB    . ASN A 1 224 ? -3.262  -7.194  -15.406 1.00 41.77  ? 225 ASN A CB    1 
ATOM   1762  C CG    . ASN A 1 224 ? -4.477  -7.143  -16.300 1.00 43.40  ? 225 ASN A CG    1 
ATOM   1763  O OD1   . ASN A 1 224 ? -4.350  -6.950  -17.515 1.00 48.86  ? 225 ASN A OD1   1 
ATOM   1764  N ND2   . ASN A 1 224 ? -5.659  -7.311  -15.724 1.00 44.53  ? 225 ASN A ND2   1 
ATOM   1765  N N     . LEU A 1 225 ? 0.226   -7.690  -15.392 1.00 41.24  ? 226 LEU A N     1 
ATOM   1766  C CA    . LEU A 1 225 ? 1.381   -7.700  -14.509 1.00 38.31  ? 226 LEU A CA    1 
ATOM   1767  C C     . LEU A 1 225 ? 1.973   -6.296  -14.418 1.00 38.99  ? 226 LEU A C     1 
ATOM   1768  O O     . LEU A 1 225 ? 2.260   -5.808  -13.327 1.00 35.26  ? 226 LEU A O     1 
ATOM   1769  C CB    . LEU A 1 225 ? 2.418   -8.703  -15.011 1.00 39.97  ? 226 LEU A CB    1 
ATOM   1770  C CG    . LEU A 1 225 ? 3.717   -8.778  -14.203 1.00 42.02  ? 226 LEU A CG    1 
ATOM   1771  C CD1   . LEU A 1 225 ? 3.467   -9.391  -12.835 1.00 44.14  ? 226 LEU A CD1   1 
ATOM   1772  C CD2   . LEU A 1 225 ? 4.790   -9.550  -14.952 1.00 42.11  ? 226 LEU A CD2   1 
ATOM   1773  N N     . PRO A 1 226 ? 2.191   -5.612  -15.564 1.00 37.22  ? 227 PRO A N     1 
ATOM   1774  C CA    . PRO A 1 226 ? 2.856   -4.307  -15.570 1.00 37.88  ? 227 PRO A CA    1 
ATOM   1775  C C     . PRO A 1 226 ? 2.166   -3.247  -14.713 1.00 34.88  ? 227 PRO A C     1 
ATOM   1776  O O     . PRO A 1 226 ? 2.793   -2.267  -14.319 1.00 34.51  ? 227 PRO A O     1 
ATOM   1777  C CB    . PRO A 1 226 ? 2.858   -3.923  -17.067 1.00 38.12  ? 227 PRO A CB    1 
ATOM   1778  C CG    . PRO A 1 226 ? 2.739   -5.246  -17.795 1.00 37.93  ? 227 PRO A CG    1 
ATOM   1779  C CD    . PRO A 1 226 ? 1.838   -6.082  -16.911 1.00 35.77  ? 227 PRO A CD    1 
ATOM   1780  N N     . GLN A 1 227 ? 0.872   -3.450  -14.437 1.00 35.13  ? 228 GLN A N     1 
ATOM   1781  C CA    . GLN A 1 227 ? 0.085   -2.482  -13.688 1.00 37.41  ? 228 GLN A CA    1 
ATOM   1782  C C     . GLN A 1 227 ? -0.105  -2.960  -12.250 1.00 35.40  ? 228 GLN A C     1 
ATOM   1783  O O     . GLN A 1 227 ? -0.722  -2.270  -11.441 1.00 33.78  ? 228 GLN A O     1 
ATOM   1784  C CB    . GLN A 1 227 ? -1.280  -2.253  -14.338 1.00 44.33  ? 228 GLN A CB    1 
ATOM   1785  C CG    . GLN A 1 227 ? -1.231  -1.477  -15.651 1.00 49.03  ? 228 GLN A CG    1 
ATOM   1786  C CD    . GLN A 1 227 ? -0.596  -2.253  -16.783 1.00 50.86  ? 228 GLN A CD    1 
ATOM   1787  O OE1   . GLN A 1 227 ? -1.047  -3.343  -17.152 1.00 56.49  ? 228 GLN A OE1   1 
ATOM   1788  N NE2   . GLN A 1 227 ? 0.460   -1.691  -17.353 1.00 56.48  ? 228 GLN A NE2   1 
ATOM   1789  N N     . ALA A 1 228 ? 0.433   -4.144  -11.942 1.00 30.24  ? 229 ALA A N     1 
ATOM   1790  C CA    . ALA A 1 228 ? 0.252   -4.750  -10.634 1.00 30.48  ? 229 ALA A CA    1 
ATOM   1791  C C     . ALA A 1 228 ? 1.109   -4.029  -9.597  1.00 33.26  ? 229 ALA A C     1 
ATOM   1792  O O     . ALA A 1 228 ? 2.067   -3.340  -9.942  1.00 33.58  ? 229 ALA A O     1 
ATOM   1793  C CB    . ALA A 1 228 ? 0.587   -6.223  -10.699 1.00 32.03  ? 229 ALA A CB    1 
ATOM   1794  N N     . HIS A 1 229 ? 0.743   -4.198  -8.322  1.00 35.95  ? 230 HIS A N     1 
ATOM   1795  C CA    . HIS A 1 229 ? 1.502   -3.636  -7.217  1.00 39.11  ? 230 HIS A CA    1 
ATOM   1796  C C     . HIS A 1 229 ? 2.504   -4.676  -6.726  1.00 38.31  ? 230 HIS A C     1 
ATOM   1797  O O     . HIS A 1 229 ? 2.120   -5.686  -6.140  1.00 43.53  ? 230 HIS A O     1 
ATOM   1798  C CB    . HIS A 1 229 ? 0.563   -3.167  -6.100  1.00 45.10  ? 230 HIS A CB    1 
ATOM   1799  C CG    . HIS A 1 229 ? 1.272   -2.593  -4.918  1.00 47.49  ? 230 HIS A CG    1 
ATOM   1800  N ND1   . HIS A 1 229 ? 1.730   -1.294  -4.882  1.00 53.06  ? 230 HIS A ND1   1 
ATOM   1801  C CD2   . HIS A 1 229 ? 1.617   -3.139  -3.744  1.00 48.18  ? 230 HIS A CD2   1 
ATOM   1802  C CE1   . HIS A 1 229 ? 2.320   -1.070  -3.717  1.00 54.74  ? 230 HIS A CE1   1 
ATOM   1803  N NE2   . HIS A 1 229 ? 2.262   -2.177  -3.010  1.00 49.41  ? 230 HIS A NE2   1 
ATOM   1804  N N     . LEU A 1 230 ? 3.791   -4.416  -6.978  1.00 38.02  ? 231 LEU A N     1 
ATOM   1805  C CA    . LEU A 1 230 ? 4.845   -5.354  -6.634  1.00 38.38  ? 231 LEU A CA    1 
ATOM   1806  C C     . LEU A 1 230 ? 5.670   -4.800  -5.477  1.00 38.32  ? 231 LEU A C     1 
ATOM   1807  O O     . LEU A 1 230 ? 5.814   -3.588  -5.329  1.00 39.84  ? 231 LEU A O     1 
ATOM   1808  C CB    . LEU A 1 230 ? 5.716   -5.631  -7.859  1.00 37.89  ? 231 LEU A CB    1 
ATOM   1809  C CG    . LEU A 1 230 ? 5.016   -6.314  -9.038  1.00 36.16  ? 231 LEU A CG    1 
ATOM   1810  C CD1   . LEU A 1 230 ? 5.999   -6.632  -10.152 1.00 36.02  ? 231 LEU A CD1   1 
ATOM   1811  C CD2   . LEU A 1 230 ? 4.299   -7.570  -8.580  1.00 36.59  ? 231 LEU A CD2   1 
ATOM   1812  N N     . MET A 1 231 ? 6.196   -5.715  -4.658  1.00 36.10  ? 232 MET A N     1 
ATOM   1813  C CA    . MET A 1 231 ? 7.103   -5.368  -3.578  1.00 34.72  ? 232 MET A CA    1 
ATOM   1814  C C     . MET A 1 231 ? 8.352   -6.239  -3.688  1.00 30.49  ? 232 MET A C     1 
ATOM   1815  O O     . MET A 1 231 ? 8.337   -7.266  -4.361  1.00 30.03  ? 232 MET A O     1 
ATOM   1816  C CB    . MET A 1 231 ? 6.440   -5.574  -2.211  1.00 38.56  ? 232 MET A CB    1 
ATOM   1817  C CG    . MET A 1 231 ? 5.298   -4.615  -1.926  1.00 45.01  ? 232 MET A CG    1 
ATOM   1818  S SD    . MET A 1 231 ? 5.815   -2.886  -1.932  1.00 53.47  ? 232 MET A SD    1 
ATOM   1819  C CE    . MET A 1 231 ? 7.142   -2.922  -0.719  1.00 56.36  ? 232 MET A CE    1 
ATOM   1820  N N     . PRO A 1 232 ? 9.471   -5.852  -3.038  1.00 33.77  ? 233 PRO A N     1 
ATOM   1821  C CA    . PRO A 1 232 ? 10.713  -6.623  -3.119  1.00 35.06  ? 233 PRO A CA    1 
ATOM   1822  C C     . PRO A 1 232 ? 10.521  -8.112  -2.841  1.00 38.88  ? 233 PRO A C     1 
ATOM   1823  O O     . PRO A 1 232 ? 11.202  -8.950  -3.428  1.00 37.50  ? 233 PRO A O     1 
ATOM   1824  C CB    . PRO A 1 232 ? 11.606  -5.948  -2.059  1.00 34.99  ? 233 PRO A CB    1 
ATOM   1825  C CG    . PRO A 1 232 ? 11.095  -4.524  -1.995  1.00 34.54  ? 233 PRO A CG    1 
ATOM   1826  C CD    . PRO A 1 232 ? 9.597   -4.642  -2.211  1.00 35.37  ? 233 PRO A CD    1 
ATOM   1827  N N     . ILE A 1 233 ? 9.581   -8.428  -1.943  1.00 41.06  ? 234 ILE A N     1 
ATOM   1828  C CA    . ILE A 1 233 ? 9.393   -9.791  -1.472  1.00 45.00  ? 234 ILE A CA    1 
ATOM   1829  C C     . ILE A 1 233 ? 8.380   -10.506 -2.364  1.00 41.50  ? 234 ILE A C     1 
ATOM   1830  O O     . ILE A 1 233 ? 7.901   -11.583 -2.016  1.00 47.15  ? 234 ILE A O     1 
ATOM   1831  C CB    . ILE A 1 233 ? 8.947   -9.803  0.002   1.00 50.18  ? 234 ILE A CB    1 
ATOM   1832  C CG1   . ILE A 1 233 ? 7.570   -9.161  0.177   1.00 52.66  ? 234 ILE A CG1   1 
ATOM   1833  C CG2   . ILE A 1 233 ? 9.998   -9.144  0.896   1.00 53.23  ? 234 ILE A CG2   1 
ATOM   1834  C CD1   . ILE A 1 233 ? 7.040   -9.211  1.599   1.00 58.88  ? 234 ILE A CD1   1 
ATOM   1835  N N     . SER A 1 234 ? 8.062   -9.901  -3.513  1.00 38.50  ? 235 SER A N     1 
ATOM   1836  C CA    . SER A 1 234 ? 7.077   -10.463 -4.423  1.00 36.81  ? 235 SER A CA    1 
ATOM   1837  C C     . SER A 1 234 ? 7.720   -11.531 -5.305  1.00 34.54  ? 235 SER A C     1 
ATOM   1838  O O     . SER A 1 234 ? 8.777   -11.309 -5.889  1.00 39.87  ? 235 SER A O     1 
ATOM   1839  C CB    . SER A 1 234 ? 6.429   -9.388  -5.258  1.00 38.21  ? 235 SER A CB    1 
ATOM   1840  O OG    . SER A 1 234 ? 5.667   -8.502  -4.450  1.00 36.59  ? 235 SER A OG    1 
ATOM   1841  N N     . THR A 1 235 ? 7.059   -12.691 -5.385  1.00 36.43  ? 236 THR A N     1 
ATOM   1842  C CA    . THR A 1 235 ? 7.463   -13.756 -6.288  1.00 32.33  ? 236 THR A CA    1 
ATOM   1843  C C     . THR A 1 235 ? 6.337   -13.992 -7.289  1.00 31.51  ? 236 THR A C     1 
ATOM   1844  O O     . THR A 1 235 ? 5.167   -14.012 -6.916  1.00 29.71  ? 236 THR A O     1 
ATOM   1845  C CB    . THR A 1 235 ? 7.782   -15.020 -5.491  1.00 33.52  ? 236 THR A CB    1 
ATOM   1846  O OG1   . THR A 1 235 ? 8.771   -14.642 -4.538  1.00 38.50  ? 236 THR A OG1   1 
ATOM   1847  C CG2   . THR A 1 235 ? 8.307   -16.144 -6.367  1.00 33.06  ? 236 THR A CG2   1 
ATOM   1848  N N     . LEU A 1 236 ? 6.705   -14.157 -8.564  1.00 30.07  ? 237 LEU A N     1 
ATOM   1849  C CA    . LEU A 1 236 ? 5.731   -14.383 -9.618  1.00 25.48  ? 237 LEU A CA    1 
ATOM   1850  C C     . LEU A 1 236 ? 5.669   -15.873 -9.938  1.00 26.34  ? 237 LEU A C     1 
ATOM   1851  O O     . LEU A 1 236 ? 6.665   -16.469 -10.343 1.00 23.37  ? 237 LEU A O     1 
ATOM   1852  C CB    . LEU A 1 236 ? 6.090   -13.565 -10.858 1.00 24.06  ? 237 LEU A CB    1 
ATOM   1853  C CG    . LEU A 1 236 ? 5.188   -13.775 -12.079 1.00 23.16  ? 237 LEU A CG    1 
ATOM   1854  C CD1   . LEU A 1 236 ? 3.753   -13.381 -11.772 1.00 23.31  ? 237 LEU A CD1   1 
ATOM   1855  C CD2   . LEU A 1 236 ? 5.707   -13.007 -13.282 1.00 24.18  ? 237 LEU A CD2   1 
ATOM   1856  N N     . LEU A 1 237 ? 4.484   -16.461 -9.747  1.00 26.52  ? 238 LEU A N     1 
ATOM   1857  C CA    . LEU A 1 237 ? 4.249   -17.852 -10.096 1.00 28.89  ? 238 LEU A CA    1 
ATOM   1858  C C     . LEU A 1 237 ? 3.503   -17.910 -11.425 1.00 34.50  ? 238 LEU A C     1 
ATOM   1859  O O     . LEU A 1 237 ? 2.416   -17.352 -11.557 1.00 36.30  ? 238 LEU A O     1 
ATOM   1860  C CB    . LEU A 1 237 ? 3.464   -18.560 -8.995  1.00 30.50  ? 238 LEU A CB    1 
ATOM   1861  C CG    . LEU A 1 237 ? 2.987   -19.979 -9.324  1.00 31.32  ? 238 LEU A CG    1 
ATOM   1862  C CD1   . LEU A 1 237 ? 4.150   -20.955 -9.362  1.00 30.91  ? 238 LEU A CD1   1 
ATOM   1863  C CD2   . LEU A 1 237 ? 1.929   -20.441 -8.340  1.00 31.41  ? 238 LEU A CD2   1 
ATOM   1864  N N     . ILE A 1 238 ? 4.103   -18.594 -12.401 1.00 36.48  ? 239 ILE A N     1 
ATOM   1865  C CA    . ILE A 1 238 ? 3.479   -18.796 -13.696 1.00 37.25  ? 239 ILE A CA    1 
ATOM   1866  C C     . ILE A 1 238 ? 3.108   -20.270 -13.829 1.00 34.53  ? 239 ILE A C     1 
ATOM   1867  O O     . ILE A 1 238 ? 3.960   -21.107 -14.117 1.00 35.24  ? 239 ILE A O     1 
ATOM   1868  C CB    . ILE A 1 238 ? 4.407   -18.324 -14.830 1.00 38.88  ? 239 ILE A CB    1 
ATOM   1869  C CG1   . ILE A 1 238 ? 4.799   -16.855 -14.653 1.00 40.11  ? 239 ILE A CG1   1 
ATOM   1870  C CG2   . ILE A 1 238 ? 3.775   -18.581 -16.198 1.00 36.17  ? 239 ILE A CG2   1 
ATOM   1871  C CD1   . ILE A 1 238 ? 5.737   -16.329 -15.725 1.00 40.91  ? 239 ILE A CD1   1 
ATOM   1872  N N     . PRO A 1 239 ? 1.825   -20.630 -13.599 1.00 32.65  ? 240 PRO A N     1 
ATOM   1873  C CA    . PRO A 1 239 ? 1.385   -22.023 -13.679 1.00 30.21  ? 240 PRO A CA    1 
ATOM   1874  C C     . PRO A 1 239 ? 1.550   -22.591 -15.085 1.00 26.87  ? 240 PRO A C     1 
ATOM   1875  O O     . PRO A 1 239 ? 1.741   -21.844 -16.044 1.00 22.88  ? 240 PRO A O     1 
ATOM   1876  C CB    . PRO A 1 239 ? -0.098  -21.974 -13.244 1.00 30.00  ? 240 PRO A CB    1 
ATOM   1877  C CG    . PRO A 1 239 ? -0.254  -20.631 -12.553 1.00 32.86  ? 240 PRO A CG    1 
ATOM   1878  C CD    . PRO A 1 239 ? 0.738   -19.710 -13.237 1.00 32.78  ? 240 PRO A CD    1 
ATOM   1879  N N     . PRO A 1 240 ? 1.479   -23.932 -15.244 1.00 25.79  ? 241 PRO A N     1 
ATOM   1880  C CA    . PRO A 1 240 ? 1.581   -24.559 -16.562 1.00 26.59  ? 241 PRO A CA    1 
ATOM   1881  C C     . PRO A 1 240 ? 0.676   -23.891 -17.594 1.00 26.70  ? 241 PRO A C     1 
ATOM   1882  O O     . PRO A 1 240 ? -0.427  -23.455 -17.271 1.00 28.34  ? 241 PRO A O     1 
ATOM   1883  C CB    . PRO A 1 240 ? 1.170   -26.018 -16.283 1.00 26.65  ? 241 PRO A CB    1 
ATOM   1884  C CG    . PRO A 1 240 ? 1.561   -26.244 -14.838 1.00 27.64  ? 241 PRO A CG    1 
ATOM   1885  C CD    . PRO A 1 240 ? 1.319   -24.908 -14.155 1.00 27.87  ? 241 PRO A CD    1 
ATOM   1886  N N     . ALA A 1 241 ? 1.162   -23.813 -18.836 1.00 29.57  ? 242 ALA A N     1 
ATOM   1887  C CA    . ALA A 1 241 ? 0.365   -23.313 -19.943 1.00 29.81  ? 242 ALA A CA    1 
ATOM   1888  C C     . ALA A 1 241 ? -0.220  -24.492 -20.716 1.00 32.95  ? 242 ALA A C     1 
ATOM   1889  O O     . ALA A 1 241 ? -1.301  -24.388 -21.293 1.00 32.94  ? 242 ALA A O     1 
ATOM   1890  C CB    . ALA A 1 241 ? 1.207   -22.424 -20.830 1.00 30.94  ? 242 ALA A CB    1 
ATOM   1891  N N     . LYS A 1 242 ? 0.510   -25.613 -20.714 1.00 35.22  ? 243 LYS A N     1 
ATOM   1892  C CA    . LYS A 1 242 ? 0.041   -26.843 -21.329 1.00 43.60  ? 243 LYS A CA    1 
ATOM   1893  C C     . LYS A 1 242 ? 0.050   -27.960 -20.291 1.00 48.05  ? 243 LYS A C     1 
ATOM   1894  O O     . LYS A 1 242 ? 0.650   -27.823 -19.227 1.00 44.92  ? 243 LYS A O     1 
ATOM   1895  C CB    . LYS A 1 242 ? 0.938   -27.296 -22.483 1.00 43.41  ? 243 LYS A CB    1 
ATOM   1896  C CG    . LYS A 1 242 ? 1.291   -26.257 -23.531 1.00 45.35  ? 243 LYS A CG    1 
ATOM   1897  C CD    . LYS A 1 242 ? 2.437   -26.761 -24.396 1.00 48.25  ? 243 LYS A CD    1 
ATOM   1898  C CE    . LYS A 1 242 ? 3.525   -27.318 -23.529 1.00 47.81  ? 243 LYS A CE    1 
ATOM   1899  N NZ    . LYS A 1 242 ? 4.342   -28.318 -24.219 1.00 52.29  ? 243 LYS A NZ    1 
ATOM   1900  N N     . LYS A 1 243 ? -0.604  -29.075 -20.631 1.00 52.18  ? 244 LYS A N     1 
ATOM   1901  C CA    . LYS A 1 243 ? -0.574  -30.266 -19.802 1.00 53.91  ? 244 LYS A CA    1 
ATOM   1902  C C     . LYS A 1 243 ? 0.555   -31.171 -20.282 1.00 51.38  ? 244 LYS A C     1 
ATOM   1903  O O     . LYS A 1 243 ? 1.214   -30.878 -21.277 1.00 51.46  ? 244 LYS A O     1 
ATOM   1904  C CB    . LYS A 1 243 ? -1.903  -31.025 -19.874 1.00 59.79  ? 244 LYS A CB    1 
ATOM   1905  C CG    . LYS A 1 243 ? -3.150  -30.157 -19.844 1.00 61.52  ? 244 LYS A CG    1 
ATOM   1906  C CD    . LYS A 1 243 ? -4.439  -30.927 -20.103 1.00 60.14  ? 244 LYS A CD    1 
ATOM   1907  C CE    . LYS A 1 243 ? -4.399  -32.326 -19.572 1.00 59.35  ? 244 LYS A CE    1 
ATOM   1908  N NZ    . LYS A 1 243 ? -3.793  -33.252 -20.534 1.00 55.05  ? 244 LYS A NZ    1 
ATOM   1909  N N     . LEU A 1 244 ? 0.751   -32.284 -19.569 1.00 53.68  ? 245 LEU A N     1 
ATOM   1910  C CA    . LEU A 1 244 ? 1.808   -33.230 -19.880 1.00 54.18  ? 245 LEU A CA    1 
ATOM   1911  C C     . LEU A 1 244 ? 1.406   -34.075 -21.087 1.00 54.36  ? 245 LEU A C     1 
ATOM   1912  O O     . LEU A 1 244 ? 0.446   -34.839 -21.022 1.00 49.74  ? 245 LEU A O     1 
ATOM   1913  C CB    . LEU A 1 244 ? 2.064   -34.090 -18.644 1.00 55.25  ? 245 LEU A CB    1 
ATOM   1914  C CG    . LEU A 1 244 ? 2.488   -33.331 -17.383 1.00 53.62  ? 245 LEU A CG    1 
ATOM   1915  C CD1   . LEU A 1 244 ? 2.516   -34.242 -16.167 1.00 55.91  ? 245 LEU A CD1   1 
ATOM   1916  C CD2   . LEU A 1 244 ? 3.841   -32.673 -17.590 1.00 51.98  ? 245 LEU A CD2   1 
ATOM   1917  N N     . GLU A 1 245 ? 2.153   -33.919 -22.187 1.00 58.56  ? 246 GLU A N     1 
ATOM   1918  C CA    . GLU A 1 245 ? 1.966   -34.739 -23.374 1.00 58.90  ? 246 GLU A CA    1 
ATOM   1919  C C     . GLU A 1 245 ? 2.876   -35.961 -23.278 1.00 60.12  ? 246 GLU A C     1 
ATOM   1920  O O     . GLU A 1 245 ? 3.957   -35.889 -22.697 1.00 61.15  ? 246 GLU A O     1 
ATOM   1921  C CB    . GLU A 1 245 ? 2.252   -33.935 -24.643 1.00 59.52  ? 246 GLU A CB    1 
ATOM   1922  C CG    . GLU A 1 245 ? 1.188   -32.884 -24.949 1.00 60.38  ? 246 GLU A CG    1 
ATOM   1923  C CD    . GLU A 1 245 ? 1.475   -32.044 -26.181 1.00 61.00  ? 246 GLU A CD    1 
ATOM   1924  O OE1   . GLU A 1 245 ? 0.671   -32.100 -27.135 1.00 61.12  ? 246 GLU A OE1   1 
ATOM   1925  O OE2   . GLU A 1 245 ? 2.499   -31.329 -26.184 1.00 65.91  ? 246 GLU A OE2   1 
ATOM   1926  N N     . TYR A 1 246 ? 2.424   -37.080 -23.856 1.00 57.96  ? 247 TYR A N     1 
ATOM   1927  C CA    . TYR A 1 246 ? 3.147   -38.338 -23.767 1.00 57.00  ? 247 TYR A CA    1 
ATOM   1928  C C     . TYR A 1 246 ? 4.394   -38.276 -24.645 1.00 52.27  ? 247 TYR A C     1 
ATOM   1929  O O     . TYR A 1 246 ? 4.406   -37.603 -25.674 1.00 52.33  ? 247 TYR A O     1 
ATOM   1930  C CB    . TYR A 1 246 ? 2.255   -39.519 -24.163 1.00 57.81  ? 247 TYR A CB    1 
ATOM   1931  C CG    . TYR A 1 246 ? 1.183   -39.876 -23.142 1.00 60.85  ? 247 TYR A CG    1 
ATOM   1932  C CD1   . TYR A 1 246 ? 1.510   -40.535 -21.963 1.00 60.91  ? 247 TYR A CD1   1 
ATOM   1933  C CD2   . TYR A 1 246 ? -0.157  -39.585 -23.371 1.00 61.18  ? 247 TYR A CD2   1 
ATOM   1934  C CE1   . TYR A 1 246 ? 0.542   -40.870 -21.031 1.00 60.44  ? 247 TYR A CE1   1 
ATOM   1935  C CE2   . TYR A 1 246 ? -1.135  -39.919 -22.448 1.00 55.93  ? 247 TYR A CE2   1 
ATOM   1936  C CZ    . TYR A 1 246 ? -0.784  -40.562 -21.275 1.00 59.90  ? 247 TYR A CZ    1 
ATOM   1937  O OH    . TYR A 1 246 ? -1.740  -40.894 -20.358 1.00 59.35  ? 247 TYR A OH    1 
ATOM   1938  N N     . ASN A 1 247 ? 5.436   -38.998 -24.218 1.00 51.04  ? 248 ASN A N     1 
ATOM   1939  C CA    . ASN A 1 247 ? 6.689   -39.072 -24.950 1.00 50.14  ? 248 ASN A CA    1 
ATOM   1940  C C     . ASN A 1 247 ? 6.818   -40.465 -25.563 1.00 48.35  ? 248 ASN A C     1 
ATOM   1941  O O     . ASN A 1 247 ? 7.473   -41.338 -24.998 1.00 46.63  ? 248 ASN A O     1 
ATOM   1942  C CB    . ASN A 1 247 ? 7.874   -38.736 -24.050 1.00 47.89  ? 248 ASN A CB    1 
ATOM   1943  C CG    . ASN A 1 247 ? 9.161   -38.593 -24.825 1.00 49.85  ? 248 ASN A CG    1 
ATOM   1944  O OD1   . ASN A 1 247 ? 9.168   -38.727 -26.054 1.00 55.22  ? 248 ASN A OD1   1 
ATOM   1945  N ND2   . ASN A 1 247 ? 10.255  -38.313 -24.132 1.00 52.22  ? 248 ASN A ND2   1 
ATOM   1946  N N     . TYR A 1 248 ? 6.190   -40.650 -26.729 1.00 46.97  ? 249 TYR A N     1 
ATOM   1947  C CA    . TYR A 1 248 ? 6.094   -41.955 -27.362 1.00 44.72  ? 249 TYR A CA    1 
ATOM   1948  C C     . TYR A 1 248 ? 7.492   -42.500 -27.647 1.00 44.04  ? 249 TYR A C     1 
ATOM   1949  O O     . TYR A 1 248 ? 7.744   -43.691 -27.473 1.00 41.09  ? 249 TYR A O     1 
ATOM   1950  C CB    . TYR A 1 248 ? 5.252   -41.851 -28.638 1.00 43.45  ? 249 TYR A CB    1 
ATOM   1951  C CG    . TYR A 1 248 ? 3.812   -41.412 -28.405 1.00 44.16  ? 249 TYR A CG    1 
ATOM   1952  C CD1   . TYR A 1 248 ? 2.872   -42.291 -27.882 1.00 44.91  ? 249 TYR A CD1   1 
ATOM   1953  C CD2   . TYR A 1 248 ? 3.388   -40.129 -28.728 1.00 45.86  ? 249 TYR A CD2   1 
ATOM   1954  C CE1   . TYR A 1 248 ? 1.560   -41.903 -27.669 1.00 46.11  ? 249 TYR A CE1   1 
ATOM   1955  C CE2   . TYR A 1 248 ? 2.077   -39.729 -28.524 1.00 49.65  ? 249 TYR A CE2   1 
ATOM   1956  C CZ    . TYR A 1 248 ? 1.161   -40.619 -27.993 1.00 47.06  ? 249 TYR A CZ    1 
ATOM   1957  O OH    . TYR A 1 248 ? -0.131  -40.230 -27.790 1.00 48.28  ? 249 TYR A OH    1 
ATOM   1958  N N     . ALA A 1 249 ? 8.392   -41.615 -28.084 1.00 45.73  ? 250 ALA A N     1 
ATOM   1959  C CA    . ALA A 1 249 ? 9.739   -42.011 -28.463 1.00 46.70  ? 250 ALA A CA    1 
ATOM   1960  C C     . ALA A 1 249 ? 10.359  -42.877 -27.370 1.00 43.94  ? 250 ALA A C     1 
ATOM   1961  O O     . ALA A 1 249 ? 10.876  -43.957 -27.646 1.00 45.50  ? 250 ALA A O     1 
ATOM   1962  C CB    . ALA A 1 249 ? 10.578  -40.783 -28.738 1.00 49.09  ? 250 ALA A CB    1 
ATOM   1963  N N     . ILE A 1 250 ? 10.297  -42.390 -26.127 1.00 45.98  ? 251 ILE A N     1 
ATOM   1964  C CA    . ILE A 1 250 ? 10.942  -43.053 -25.006 1.00 44.88  ? 251 ILE A CA    1 
ATOM   1965  C C     . ILE A 1 250 ? 10.098  -44.248 -24.572 1.00 40.41  ? 251 ILE A C     1 
ATOM   1966  O O     . ILE A 1 250 ? 10.633  -45.313 -24.270 1.00 36.92  ? 251 ILE A O     1 
ATOM   1967  C CB    . ILE A 1 250 ? 11.177  -42.064 -23.849 1.00 46.53  ? 251 ILE A CB    1 
ATOM   1968  C CG1   . ILE A 1 250 ? 12.026  -40.874 -24.295 1.00 50.44  ? 251 ILE A CG1   1 
ATOM   1969  C CG2   . ILE A 1 250 ? 11.789  -42.772 -22.639 1.00 45.51  ? 251 ILE A CG2   1 
ATOM   1970  C CD1   . ILE A 1 250 ? 13.386  -41.256 -24.850 1.00 56.03  ? 251 ILE A CD1   1 
ATOM   1971  N N     . LEU A 1 251 ? 8.775   -44.058 -24.540 1.00 44.12  ? 252 LEU A N     1 
ATOM   1972  C CA    . LEU A 1 251 ? 7.856   -45.120 -24.161 1.00 43.68  ? 252 LEU A CA    1 
ATOM   1973  C C     . LEU A 1 251 ? 8.120   -46.344 -25.034 1.00 42.89  ? 252 LEU A C     1 
ATOM   1974  O O     . LEU A 1 251 ? 8.127   -47.471 -24.543 1.00 40.90  ? 252 LEU A O     1 
ATOM   1975  C CB    . LEU A 1 251 ? 6.409   -44.642 -24.288 1.00 42.04  ? 252 LEU A CB    1 
ATOM   1976  C CG    . LEU A 1 251 ? 5.971   -43.544 -23.314 1.00 39.73  ? 252 LEU A CG    1 
ATOM   1977  C CD1   . LEU A 1 251 ? 4.524   -43.153 -23.560 1.00 39.73  ? 252 LEU A CD1   1 
ATOM   1978  C CD2   . LEU A 1 251 ? 6.167   -43.975 -21.870 1.00 38.78  ? 252 LEU A CD2   1 
ATOM   1979  N N     . ALA A 1 252 ? 8.340   -46.103 -26.331 1.00 44.70  ? 253 ALA A N     1 
ATOM   1980  C CA    . ALA A 1 252 ? 8.576   -47.172 -27.288 1.00 47.41  ? 253 ALA A CA    1 
ATOM   1981  C C     . ALA A 1 252 ? 9.851   -47.926 -26.917 1.00 45.61  ? 253 ALA A C     1 
ATOM   1982  O O     . ALA A 1 252 ? 9.867   -49.155 -26.901 1.00 43.28  ? 253 ALA A O     1 
ATOM   1983  C CB    . ALA A 1 252 ? 8.654   -46.605 -28.689 1.00 46.18  ? 253 ALA A CB    1 
ATOM   1984  N N     . LYS A 1 253 ? 10.916  -47.172 -26.626 1.00 46.27  ? 254 LYS A N     1 
ATOM   1985  C CA    . LYS A 1 253 ? 12.181  -47.756 -26.212 1.00 47.88  ? 254 LYS A CA    1 
ATOM   1986  C C     . LYS A 1 253 ? 11.971  -48.544 -24.923 1.00 49.51  ? 254 LYS A C     1 
ATOM   1987  O O     . LYS A 1 253 ? 12.613  -49.569 -24.705 1.00 48.17  ? 254 LYS A O     1 
ATOM   1988  C CB    . LYS A 1 253 ? 13.249  -46.671 -26.030 1.00 50.31  ? 254 LYS A CB    1 
ATOM   1989  C CG    . LYS A 1 253 ? 13.781  -46.066 -27.322 1.00 50.63  ? 254 LYS A CG    1 
ATOM   1990  C CD    . LYS A 1 253 ? 14.788  -44.942 -27.110 1.00 55.59  ? 254 LYS A CD    1 
ATOM   1991  C CE    . LYS A 1 253 ? 15.459  -44.518 -28.379 1.00 58.86  ? 254 LYS A CE    1 
ATOM   1992  N NZ    . LYS A 1 253 ? 14.494  -44.093 -29.396 1.00 59.89  ? 254 LYS A NZ    1 
ATOM   1993  N N     . LEU A 1 254 ? 11.063  -48.048 -24.074 1.00 52.87  ? 255 LEU A N     1 
ATOM   1994  C CA    . LEU A 1 254 ? 10.711  -48.728 -22.839 1.00 53.66  ? 255 LEU A CA    1 
ATOM   1995  C C     . LEU A 1 254 ? 9.802   -49.912 -23.161 1.00 56.25  ? 255 LEU A C     1 
ATOM   1996  O O     . LEU A 1 254 ? 9.585   -50.781 -22.319 1.00 57.78  ? 255 LEU A O     1 
ATOM   1997  C CB    . LEU A 1 254 ? 10.041  -47.752 -21.873 1.00 51.09  ? 255 LEU A CB    1 
ATOM   1998  C CG    . LEU A 1 254 ? 10.938  -46.648 -21.302 1.00 50.80  ? 255 LEU A CG    1 
ATOM   1999  C CD1   . LEU A 1 254 ? 10.155  -45.743 -20.368 1.00 47.53  ? 255 LEU A CD1   1 
ATOM   2000  C CD2   . LEU A 1 254 ? 12.142  -47.238 -20.586 1.00 51.05  ? 255 LEU A CD2   1 
ATOM   2001  N N     . GLY A 1 255 ? 9.275   -49.928 -24.389 1.00 56.04  ? 256 GLY A N     1 
ATOM   2002  C CA    . GLY A 1 255 ? 8.408   -51.002 -24.845 1.00 56.86  ? 256 GLY A CA    1 
ATOM   2003  C C     . GLY A 1 255 ? 7.060   -50.972 -24.129 1.00 58.99  ? 256 GLY A C     1 
ATOM   2004  O O     . GLY A 1 255 ? 6.453   -52.015 -23.894 1.00 56.03  ? 256 GLY A O     1 
ATOM   2005  N N     . ILE A 1 256 ? 6.603   -49.762 -23.788 1.00 57.04  ? 257 ILE A N     1 
ATOM   2006  C CA    . ILE A 1 256 ? 5.339   -49.584 -23.095 1.00 54.51  ? 257 ILE A CA    1 
ATOM   2007  C C     . ILE A 1 256 ? 4.545   -48.480 -23.788 1.00 48.27  ? 257 ILE A C     1 
ATOM   2008  O O     . ILE A 1 256 ? 4.995   -47.913 -24.781 1.00 45.99  ? 257 ILE A O     1 
ATOM   2009  C CB    . ILE A 1 256 ? 5.566   -49.266 -21.605 1.00 55.52  ? 257 ILE A CB    1 
ATOM   2010  C CG1   . ILE A 1 256 ? 6.166   -47.872 -21.410 1.00 55.72  ? 257 ILE A CG1   1 
ATOM   2011  C CG2   . ILE A 1 256 ? 6.418   -50.348 -20.940 1.00 60.73  ? 257 ILE A CG2   1 
ATOM   2012  C CD1   . ILE A 1 256 ? 6.414   -47.501 -19.960 1.00 56.75  ? 257 ILE A CD1   1 
ATOM   2013  N N     . GLY A 1 257 ? 3.361   -48.188 -23.242 1.00 49.34  ? 258 GLY A N     1 
ATOM   2014  C CA    . GLY A 1 257 ? 2.500   -47.140 -23.763 1.00 46.04  ? 258 GLY A CA    1 
ATOM   2015  C C     . GLY A 1 257 ? 1.599   -46.576 -22.668 1.00 43.98  ? 258 GLY A C     1 
ATOM   2016  O O     . GLY A 1 257 ? 1.620   -47.054 -21.535 1.00 39.17  ? 258 GLY A O     1 
ATOM   2017  N N     . PRO A 1 258 ? 0.784   -45.543 -22.973 1.00 42.10  ? 259 PRO A N     1 
ATOM   2018  C CA    . PRO A 1 258 ? -0.091  -44.925 -21.973 1.00 44.05  ? 259 PRO A CA    1 
ATOM   2019  C C     . PRO A 1 258 ? -0.898  -45.911 -21.130 1.00 47.42  ? 259 PRO A C     1 
ATOM   2020  O O     . PRO A 1 258 ? -0.998  -45.752 -19.915 1.00 50.53  ? 259 PRO A O     1 
ATOM   2021  C CB    . PRO A 1 258 ? -0.993  -44.038 -22.853 1.00 40.39  ? 259 PRO A CB    1 
ATOM   2022  C CG    . PRO A 1 258 ? -0.088  -43.628 -23.991 1.00 39.50  ? 259 PRO A CG    1 
ATOM   2023  C CD    . PRO A 1 258 ? 0.698   -44.891 -24.290 1.00 41.39  ? 259 PRO A CD    1 
ATOM   2024  N N     . GLU A 1 259 ? -1.471  -46.926 -21.785 1.00 48.04  ? 260 GLU A N     1 
ATOM   2025  C CA    . GLU A 1 259 ? -2.382  -47.848 -21.125 1.00 51.30  ? 260 GLU A CA    1 
ATOM   2026  C C     . GLU A 1 259 ? -1.615  -48.709 -20.124 1.00 51.70  ? 260 GLU A C     1 
ATOM   2027  O O     . GLU A 1 259 ? -2.218  -49.362 -19.275 1.00 46.56  ? 260 GLU A O     1 
ATOM   2028  C CB    . GLU A 1 259 ? -3.102  -48.723 -22.152 1.00 53.00  ? 260 GLU A CB    1 
ATOM   2029  C CG    . GLU A 1 259 ? -4.240  -49.547 -21.555 1.00 57.00  ? 260 GLU A CG    1 
ATOM   2030  C CD    . GLU A 1 259 ? -5.068  -50.293 -22.586 1.00 59.54  ? 260 GLU A CD    1 
ATOM   2031  O OE1   . GLU A 1 259 ? -5.667  -49.627 -23.456 1.00 59.03  ? 260 GLU A OE1   1 
ATOM   2032  O OE2   . GLU A 1 259 ? -5.109  -51.540 -22.522 1.00 60.53  ? 260 GLU A OE2   1 
ATOM   2033  N N     . ASP A 1 260 ? -0.282  -48.696 -20.230 1.00 51.81  ? 261 ASP A N     1 
ATOM   2034  C CA    . ASP A 1 260 ? 0.561   -49.538 -19.397 1.00 52.86  ? 261 ASP A CA    1 
ATOM   2035  C C     . ASP A 1 260 ? 1.054   -48.741 -18.192 1.00 53.34  ? 261 ASP A C     1 
ATOM   2036  O O     . ASP A 1 260 ? 1.649   -49.304 -17.275 1.00 58.46  ? 261 ASP A O     1 
ATOM   2037  C CB    . ASP A 1 260 ? 1.710   -50.130 -20.198 1.00 54.99  ? 261 ASP A CB    1 
ATOM   2038  C CG    . ASP A 1 260 ? 1.304   -50.874 -21.461 1.00 53.19  ? 261 ASP A CG    1 
ATOM   2039  O OD1   . ASP A 1 260 ? 0.469   -51.797 -21.355 1.00 52.54  ? 261 ASP A OD1   1 
ATOM   2040  O OD2   . ASP A 1 260 ? 1.827   -50.526 -22.540 1.00 61.42  ? 261 ASP A OD2   1 
ATOM   2041  N N     . LEU A 1 261 ? 0.801   -47.429 -18.204 1.00 50.75  ? 262 LEU A N     1 
ATOM   2042  C CA    . LEU A 1 261 ? 1.203   -46.565 -17.107 1.00 54.32  ? 262 LEU A CA    1 
ATOM   2043  C C     . LEU A 1 261 ? 0.341   -46.879 -15.887 1.00 54.89  ? 262 LEU A C     1 
ATOM   2044  O O     . LEU A 1 261 ? -0.885  -46.852 -15.963 1.00 62.85  ? 262 LEU A O     1 
ATOM   2045  C CB    . LEU A 1 261 ? 1.094   -45.097 -17.516 1.00 52.38  ? 262 LEU A CB    1 
ATOM   2046  C CG    . LEU A 1 261 ? 1.892   -44.690 -18.760 1.00 55.66  ? 262 LEU A CG    1 
ATOM   2047  C CD1   . LEU A 1 261 ? 2.054   -43.180 -18.841 1.00 53.15  ? 262 LEU A CD1   1 
ATOM   2048  C CD2   . LEU A 1 261 ? 3.245   -45.380 -18.787 1.00 58.07  ? 262 LEU A CD2   1 
ATOM   2049  N N     . GLY A 1 262 ? 1.004   -47.184 -14.766 1.00 56.09  ? 263 GLY A N     1 
ATOM   2050  C CA    . GLY A 1 262 ? 0.322   -47.578 -13.544 1.00 56.40  ? 263 GLY A CA    1 
ATOM   2051  C C     . GLY A 1 262 ? -0.331  -46.390 -12.862 1.00 54.37  ? 263 GLY A C     1 
ATOM   2052  O O     . GLY A 1 262 ? 0.278   -45.300 -12.909 1.00 53.96  ? 263 GLY A O     1 
ATOM   2053  O OXT   . GLY A 1 262 ? -1.428  -46.590 -12.300 1.00 53.09  ? 263 GLY A OXT   1 
ATOM   2054  N N     . GLY B 2 1   ? 5.095   -6.134  24.544  1.00 38.78  ? 3   GLY B N     1 
ATOM   2055  C CA    . GLY B 2 1   ? 3.650   -6.421  24.450  1.00 36.45  ? 3   GLY B CA    1 
ATOM   2056  C C     . GLY B 2 1   ? 3.297   -7.040  23.100  1.00 35.97  ? 3   GLY B C     1 
ATOM   2057  O O     . GLY B 2 1   ? 3.114   -8.251  22.996  1.00 37.60  ? 3   GLY B O     1 
ATOM   2058  N N     . LEU B 2 2   ? 3.213   -6.191  22.072  1.00 33.20  ? 4   LEU B N     1 
ATOM   2059  C CA    . LEU B 2 2   ? 2.842   -6.625  20.736  1.00 36.13  ? 4   LEU B CA    1 
ATOM   2060  C C     . LEU B 2 2   ? 3.901   -7.587  20.203  1.00 35.90  ? 4   LEU B C     1 
ATOM   2061  O O     . LEU B 2 2   ? 3.576   -8.601  19.590  1.00 36.54  ? 4   LEU B O     1 
ATOM   2062  C CB    . LEU B 2 2   ? 2.694   -5.399  19.836  1.00 37.22  ? 4   LEU B CB    1 
ATOM   2063  C CG    . LEU B 2 2   ? 2.154   -5.662  18.426  1.00 41.26  ? 4   LEU B CG    1 
ATOM   2064  C CD1   . LEU B 2 2   ? 0.688   -6.057  18.474  1.00 41.36  ? 4   LEU B CD1   1 
ATOM   2065  C CD2   . LEU B 2 2   ? 2.359   -4.454  17.527  1.00 41.07  ? 4   LEU B CD2   1 
ATOM   2066  N N     . SER B 2 3   ? 5.170   -7.252  20.455  1.00 34.34  ? 5   SER B N     1 
ATOM   2067  C CA    . SER B 2 3   ? 6.293   -8.005  19.923  1.00 32.75  ? 5   SER B CA    1 
ATOM   2068  C C     . SER B 2 3   ? 6.395   -9.362  20.614  1.00 33.03  ? 5   SER B C     1 
ATOM   2069  O O     . SER B 2 3   ? 6.655   -10.374 19.966  1.00 28.16  ? 5   SER B O     1 
ATOM   2070  C CB    . SER B 2 3   ? 7.574   -7.225  20.067  1.00 34.29  ? 5   SER B CB    1 
ATOM   2071  O OG    . SER B 2 3   ? 8.670   -7.932  19.504  1.00 36.68  ? 5   SER B OG    1 
ATOM   2072  N N     . ASP B 2 4   ? 6.197   -9.364  21.936  1.00 29.37  ? 6   ASP B N     1 
ATOM   2073  C CA    . ASP B 2 4   ? 6.327   -10.572 22.733  1.00 28.02  ? 6   ASP B CA    1 
ATOM   2074  C C     . ASP B 2 4   ? 5.217   -11.550 22.359  1.00 27.27  ? 6   ASP B C     1 
ATOM   2075  O O     . ASP B 2 4   ? 5.423   -12.762 22.370  1.00 27.63  ? 6   ASP B O     1 
ATOM   2076  C CB    . ASP B 2 4   ? 6.319   -10.256 24.220  1.00 32.42  ? 6   ASP B CB    1 
ATOM   2077  C CG    . ASP B 2 4   ? 7.424   -9.325  24.697  1.00 37.85  ? 6   ASP B CG    1 
ATOM   2078  O OD1   . ASP B 2 4   ? 8.242   -8.903  23.851  1.00 41.36  ? 6   ASP B OD1   1 
ATOM   2079  O OD2   . ASP B 2 4   ? 7.455   -9.027  25.909  1.00 42.33  ? 6   ASP B OD2   1 
ATOM   2080  N N     . PHE B 2 5   ? 4.039   -11.007 22.030  1.00 25.28  ? 7   PHE B N     1 
ATOM   2081  C CA    . PHE B 2 5   ? 2.886   -11.825 21.695  1.00 25.42  ? 7   PHE B CA    1 
ATOM   2082  C C     . PHE B 2 5   ? 3.137   -12.534 20.366  1.00 27.06  ? 7   PHE B C     1 
ATOM   2083  O O     . PHE B 2 5   ? 2.970   -13.748 20.270  1.00 26.00  ? 7   PHE B O     1 
ATOM   2084  C CB    . PHE B 2 5   ? 1.610   -10.976 21.663  1.00 24.58  ? 7   PHE B CB    1 
ATOM   2085  C CG    . PHE B 2 5   ? 0.403   -11.698 21.080  1.00 24.62  ? 7   PHE B CG    1 
ATOM   2086  C CD1   . PHE B 2 5   ? -0.203  -12.743 21.769  1.00 26.16  ? 7   PHE B CD1   1 
ATOM   2087  C CD2   . PHE B 2 5   ? -0.132  -11.323 19.852  1.00 24.75  ? 7   PHE B CD2   1 
ATOM   2088  C CE1   . PHE B 2 5   ? -1.299  -13.402 21.234  1.00 27.00  ? 7   PHE B CE1   1 
ATOM   2089  C CE2   . PHE B 2 5   ? -1.231  -11.983 19.326  1.00 25.06  ? 7   PHE B CE2   1 
ATOM   2090  C CZ    . PHE B 2 5   ? -1.811  -13.021 20.016  1.00 25.13  ? 7   PHE B CZ    1 
ATOM   2091  N N     . PHE B 2 6   ? 3.541   -11.767 19.348  1.00 26.51  ? 8   PHE B N     1 
ATOM   2092  C CA    . PHE B 2 6   ? 3.773   -12.319 18.023  1.00 28.92  ? 8   PHE B CA    1 
ATOM   2093  C C     . PHE B 2 6   ? 4.841   -13.406 18.107  1.00 28.60  ? 8   PHE B C     1 
ATOM   2094  O O     . PHE B 2 6   ? 4.718   -14.450 17.469  1.00 26.63  ? 8   PHE B O     1 
ATOM   2095  C CB    . PHE B 2 6   ? 4.183   -11.239 17.017  1.00 31.85  ? 8   PHE B CB    1 
ATOM   2096  C CG    . PHE B 2 6   ? 3.074   -10.270 16.630  1.00 33.21  ? 8   PHE B CG    1 
ATOM   2097  C CD1   . PHE B 2 6   ? 1.741   -10.572 16.882  1.00 35.46  ? 8   PHE B CD1   1 
ATOM   2098  C CD2   . PHE B 2 6   ? 3.366   -9.077  15.977  1.00 34.06  ? 8   PHE B CD2   1 
ATOM   2099  C CE1   . PHE B 2 6   ? 0.734   -9.691  16.519  1.00 33.93  ? 8   PHE B CE1   1 
ATOM   2100  C CE2   . PHE B 2 6   ? 2.354   -8.203  15.613  1.00 36.27  ? 8   PHE B CE2   1 
ATOM   2101  C CZ    . PHE B 2 6   ? 1.043   -8.512  15.885  1.00 37.05  ? 8   PHE B CZ    1 
ATOM   2102  N N     . THR B 2 7   ? 5.888   -13.144 18.898  1.00 25.56  ? 9   THR B N     1 
ATOM   2103  C CA    . THR B 2 7   ? 7.017   -14.053 19.013  1.00 27.40  ? 9   THR B CA    1 
ATOM   2104  C C     . THR B 2 7   ? 6.546   -15.389 19.582  1.00 29.03  ? 9   THR B C     1 
ATOM   2105  O O     . THR B 2 7   ? 6.968   -16.446 19.119  1.00 27.08  ? 9   THR B O     1 
ATOM   2106  C CB    . THR B 2 7   ? 8.100   -13.422 19.887  1.00 25.41  ? 9   THR B CB    1 
ATOM   2107  O OG1   . THR B 2 7   ? 8.618   -12.338 19.123  1.00 25.20  ? 9   THR B OG1   1 
ATOM   2108  C CG2   . THR B 2 7   ? 9.217   -14.393 20.223  1.00 24.53  ? 9   THR B CG2   1 
ATOM   2109  N N     . GLN B 2 8   ? 5.675   -15.325 20.595  1.00 33.13  ? 10  GLN B N     1 
ATOM   2110  C CA    . GLN B 2 8   ? 5.216   -16.516 21.292  1.00 36.39  ? 10  GLN B CA    1 
ATOM   2111  C C     . GLN B 2 8   ? 4.210   -17.265 20.421  1.00 33.03  ? 10  GLN B C     1 
ATOM   2112  O O     . GLN B 2 8   ? 4.224   -18.492 20.365  1.00 41.37  ? 10  GLN B O     1 
ATOM   2113  C CB    . GLN B 2 8   ? 4.602   -16.139 22.640  1.00 42.92  ? 10  GLN B CB    1 
ATOM   2114  C CG    . GLN B 2 8   ? 4.182   -17.335 23.487  1.00 49.20  ? 10  GLN B CG    1 
ATOM   2115  C CD    . GLN B 2 8   ? 3.654   -16.942 24.850  1.00 57.45  ? 10  GLN B CD    1 
ATOM   2116  O OE1   . GLN B 2 8   ? 4.335   -16.273 25.636  1.00 63.05  ? 10  GLN B OE1   1 
ATOM   2117  N NE2   . GLN B 2 8   ? 2.429   -17.352 25.142  1.00 56.71  ? 10  GLN B NE2   1 
ATOM   2118  N N     . LEU B 2 9   ? 3.341   -16.507 19.745  1.00 31.69  ? 11  LEU B N     1 
ATOM   2119  C CA    . LEU B 2 9   ? 2.299   -17.079 18.910  1.00 33.12  ? 11  LEU B CA    1 
ATOM   2120  C C     . LEU B 2 9   ? 2.932   -17.893 17.784  1.00 34.00  ? 11  LEU B C     1 
ATOM   2121  O O     . LEU B 2 9   ? 2.430   -18.954 17.422  1.00 39.32  ? 11  LEU B O     1 
ATOM   2122  C CB    . LEU B 2 9   ? 1.418   -15.956 18.363  1.00 34.40  ? 11  LEU B CB    1 
ATOM   2123  C CG    . LEU B 2 9   ? 0.333   -16.375 17.366  1.00 35.72  ? 11  LEU B CG    1 
ATOM   2124  C CD1   . LEU B 2 9   ? -0.697  -17.282 18.019  1.00 34.03  ? 11  LEU B CD1   1 
ATOM   2125  C CD2   . LEU B 2 9   ? -0.336  -15.155 16.756  1.00 35.42  ? 11  LEU B CD2   1 
ATOM   2126  N N     . GLY B 2 10  ? 4.046   -17.384 17.247  1.00 33.29  ? 12  GLY B N     1 
ATOM   2127  C CA    . GLY B 2 10  ? 4.689   -17.984 16.090  1.00 33.15  ? 12  GLY B CA    1 
ATOM   2128  C C     . GLY B 2 10  ? 5.476   -19.241 16.458  1.00 32.81  ? 12  GLY B C     1 
ATOM   2129  O O     . GLY B 2 10  ? 5.936   -19.963 15.577  1.00 32.21  ? 12  GLY B O     1 
ATOM   2130  N N     . GLN B 2 11  ? 5.615   -19.498 17.764  1.00 33.93  ? 13  GLN B N     1 
ATOM   2131  C CA    . GLN B 2 11  ? 6.445   -20.591 18.246  1.00 33.62  ? 13  GLN B CA    1 
ATOM   2132  C C     . GLN B 2 11  ? 5.589   -21.666 18.911  1.00 32.10  ? 13  GLN B C     1 
ATOM   2133  O O     . GLN B 2 11  ? 5.963   -22.836 18.918  1.00 32.46  ? 13  GLN B O     1 
ATOM   2134  C CB    . GLN B 2 11  ? 7.480   -20.091 19.253  1.00 37.78  ? 13  GLN B CB    1 
ATOM   2135  C CG    . GLN B 2 11  ? 8.504   -19.123 18.672  1.00 41.98  ? 13  GLN B CG    1 
ATOM   2136  C CD    . GLN B 2 11  ? 9.561   -18.715 19.675  1.00 44.46  ? 13  GLN B CD    1 
ATOM   2137  O OE1   . GLN B 2 11  ? 10.290  -19.551 20.220  1.00 52.83  ? 13  GLN B OE1   1 
ATOM   2138  N NE2   . GLN B 2 11  ? 9.649   -17.419 19.935  1.00 49.22  ? 13  GLN B NE2   1 
ATOM   2139  N N     . ASP B 2 12  ? 4.451   -21.255 19.484  1.00 31.20  ? 14  ASP B N     1 
ATOM   2140  C CA    . ASP B 2 12  ? 3.648   -22.140 20.313  1.00 30.96  ? 14  ASP B CA    1 
ATOM   2141  C C     . ASP B 2 12  ? 2.415   -22.599 19.536  1.00 28.29  ? 14  ASP B C     1 
ATOM   2142  O O     . ASP B 2 12  ? 1.492   -21.821 19.308  1.00 27.70  ? 14  ASP B O     1 
ATOM   2143  C CB    . ASP B 2 12  ? 3.283   -21.473 21.630  1.00 31.98  ? 14  ASP B CB    1 
ATOM   2144  C CG    . ASP B 2 12  ? 2.573   -22.362 22.641  1.00 40.42  ? 14  ASP B CG    1 
ATOM   2145  O OD1   . ASP B 2 12  ? 2.321   -23.541 22.312  1.00 44.60  ? 14  ASP B OD1   1 
ATOM   2146  O OD2   . ASP B 2 12  ? 2.285   -21.870 23.753  1.00 42.68  ? 14  ASP B OD2   1 
ATOM   2147  N N     . ALA B 2 13  ? 2.406   -23.885 19.168  1.00 26.62  ? 15  ALA B N     1 
ATOM   2148  C CA    . ALA B 2 13  ? 1.331   -24.463 18.377  1.00 27.35  ? 15  ALA B CA    1 
ATOM   2149  C C     . ALA B 2 13  ? 0.034   -24.474 19.182  1.00 29.89  ? 15  ALA B C     1 
ATOM   2150  O O     . ALA B 2 13  ? -1.055  -24.442 18.614  1.00 28.89  ? 15  ALA B O     1 
ATOM   2151  C CB    . ALA B 2 13  ? 1.715   -25.857 17.933  1.00 27.66  ? 15  ALA B CB    1 
ATOM   2152  N N     . GLN B 2 14  ? 0.166   -24.531 20.511  1.00 31.02  ? 16  GLN B N     1 
ATOM   2153  C CA    . GLN B 2 14  ? -0.983  -24.536 21.398  1.00 34.30  ? 16  GLN B CA    1 
ATOM   2154  C C     . GLN B 2 14  ? -1.697  -23.191 21.297  1.00 33.48  ? 16  GLN B C     1 
ATOM   2155  O O     . GLN B 2 14  ? -2.890  -23.134 21.006  1.00 36.36  ? 16  GLN B O     1 
ATOM   2156  C CB    . GLN B 2 14  ? -0.541  -24.819 22.833  1.00 39.62  ? 16  GLN B CB    1 
ATOM   2157  C CG    . GLN B 2 14  ? -1.696  -24.997 23.811  1.00 48.05  ? 16  GLN B CG    1 
ATOM   2158  C CD    . GLN B 2 14  ? -2.603  -26.153 23.450  1.00 55.79  ? 16  GLN B CD    1 
ATOM   2159  O OE1   . GLN B 2 14  ? -2.393  -26.850 22.451  1.00 59.46  ? 16  GLN B OE1   1 
ATOM   2160  N NE2   . GLN B 2 14  ? -3.625  -26.369 24.265  1.00 61.23  ? 16  GLN B NE2   1 
ATOM   2161  N N     . LEU B 2 15  ? -0.942  -22.114 21.531  1.00 32.67  ? 17  LEU B N     1 
ATOM   2162  C CA    . LEU B 2 15  ? -1.477  -20.765 21.481  1.00 35.07  ? 17  LEU B CA    1 
ATOM   2163  C C     . LEU B 2 15  ? -1.945  -20.452 20.062  1.00 35.07  ? 17  LEU B C     1 
ATOM   2164  O O     . LEU B 2 15  ? -2.943  -19.760 19.873  1.00 40.91  ? 17  LEU B O     1 
ATOM   2165  C CB    . LEU B 2 15  ? -0.408  -19.779 21.951  1.00 33.48  ? 17  LEU B CB    1 
ATOM   2166  C CG    . LEU B 2 15  ? -0.806  -18.300 21.936  1.00 38.46  ? 17  LEU B CG    1 
ATOM   2167  C CD1   . LEU B 2 15  ? -1.968  -18.037 22.880  1.00 39.34  ? 17  LEU B CD1   1 
ATOM   2168  C CD2   . LEU B 2 15  ? 0.380   -17.416 22.286  1.00 33.83  ? 17  LEU B CD2   1 
ATOM   2169  N N     . MET B 2 16  ? -1.214  -20.971 19.070  1.00 36.78  ? 18  MET B N     1 
ATOM   2170  C CA    . MET B 2 16  ? -1.534  -20.725 17.673  1.00 38.60  ? 18  MET B CA    1 
ATOM   2171  C C     . MET B 2 16  ? -2.932  -21.258 17.371  1.00 36.67  ? 18  MET B C     1 
ATOM   2172  O O     . MET B 2 16  ? -3.735  -20.580 16.734  1.00 29.25  ? 18  MET B O     1 
ATOM   2173  C CB    . MET B 2 16  ? -0.517  -21.392 16.740  1.00 42.82  ? 18  MET B CB    1 
ATOM   2174  C CG    . MET B 2 16  ? -0.893  -21.312 15.271  1.00 46.39  ? 18  MET B CG    1 
ATOM   2175  S SD    . MET B 2 16  ? -0.931  -19.625 14.632  1.00 55.65  ? 18  MET B SD    1 
ATOM   2176  C CE    . MET B 2 16  ? 0.822   -19.297 14.397  1.00 44.02  ? 18  MET B CE    1 
ATOM   2177  N N     . GLU B 2 17  ? -3.211  -22.480 17.836  1.00 41.00  ? 19  GLU B N     1 
ATOM   2178  C CA    . GLU B 2 17  ? -4.503  -23.108 17.613  1.00 45.27  ? 19  GLU B CA    1 
ATOM   2179  C C     . GLU B 2 17  ? -5.575  -22.340 18.382  1.00 44.09  ? 19  GLU B C     1 
ATOM   2180  O O     . GLU B 2 17  ? -6.713  -22.236 17.931  1.00 41.25  ? 19  GLU B O     1 
ATOM   2181  C CB    . GLU B 2 17  ? -4.460  -24.581 18.019  1.00 52.92  ? 19  GLU B CB    1 
ATOM   2182  C CG    . GLU B 2 17  ? -3.601  -25.436 17.091  1.00 58.39  ? 19  GLU B CG    1 
ATOM   2183  C CD    . GLU B 2 17  ? -4.089  -25.467 15.654  1.00 66.07  ? 19  GLU B CD    1 
ATOM   2184  O OE1   . GLU B 2 17  ? -5.228  -25.926 15.427  1.00 76.77  ? 19  GLU B OE1   1 
ATOM   2185  O OE2   . GLU B 2 17  ? -3.333  -25.028 14.761  1.00 71.69  ? 19  GLU B OE2   1 
ATOM   2186  N N     . ASP B 2 18  ? -5.192  -21.798 19.543  1.00 44.38  ? 20  ASP B N     1 
ATOM   2187  C CA    . ASP B 2 18  ? -6.095  -20.998 20.352  1.00 46.56  ? 20  ASP B CA    1 
ATOM   2188  C C     . ASP B 2 18  ? -6.449  -19.724 19.590  1.00 40.73  ? 20  ASP B C     1 
ATOM   2189  O O     . ASP B 2 18  ? -7.593  -19.277 19.617  1.00 36.32  ? 20  ASP B O     1 
ATOM   2190  C CB    . ASP B 2 18  ? -5.493  -20.693 21.715  1.00 50.29  ? 20  ASP B CB    1 
ATOM   2191  C CG    . ASP B 2 18  ? -5.190  -21.906 22.583  1.00 54.02  ? 20  ASP B CG    1 
ATOM   2192  O OD1   . ASP B 2 18  ? -5.525  -23.031 22.157  1.00 57.79  ? 20  ASP B OD1   1 
ATOM   2193  O OD2   . ASP B 2 18  ? -4.613  -21.715 23.675  1.00 54.95  ? 20  ASP B OD2   1 
ATOM   2194  N N     . TYR B 2 19  ? -5.450  -19.155 18.905  1.00 36.16  ? 21  TYR B N     1 
ATOM   2195  C CA    . TYR B 2 19  ? -5.631  -17.926 18.151  1.00 36.24  ? 21  TYR B CA    1 
ATOM   2196  C C     . TYR B 2 19  ? -6.592  -18.178 16.993  1.00 39.00  ? 21  TYR B C     1 
ATOM   2197  O O     . TYR B 2 19  ? -7.499  -17.385 16.752  1.00 40.30  ? 21  TYR B O     1 
ATOM   2198  C CB    . TYR B 2 19  ? -4.285  -17.393 17.646  1.00 33.01  ? 21  TYR B CB    1 
ATOM   2199  C CG    . TYR B 2 19  ? -4.403  -16.177 16.736  1.00 30.49  ? 21  TYR B CG    1 
ATOM   2200  C CD1   . TYR B 2 19  ? -4.504  -14.895 17.262  1.00 31.64  ? 21  TYR B CD1   1 
ATOM   2201  C CD2   . TYR B 2 19  ? -4.420  -16.312 15.353  1.00 29.60  ? 21  TYR B CD2   1 
ATOM   2202  C CE1   . TYR B 2 19  ? -4.620  -13.785 16.442  1.00 30.45  ? 21  TYR B CE1   1 
ATOM   2203  C CE2   . TYR B 2 19  ? -4.535  -15.210 14.521  1.00 28.14  ? 21  TYR B CE2   1 
ATOM   2204  C CZ    . TYR B 2 19  ? -4.633  -13.943 15.068  1.00 29.79  ? 21  TYR B CZ    1 
ATOM   2205  O OH    . TYR B 2 19  ? -4.745  -12.851 14.257  1.00 33.53  ? 21  TYR B OH    1 
ATOM   2206  N N     . LYS B 2 20  ? -6.376  -19.289 16.280  1.00 42.73  ? 22  LYS B N     1 
ATOM   2207  C CA    . LYS B 2 20  ? -7.194  -19.641 15.132  1.00 46.02  ? 22  LYS B CA    1 
ATOM   2208  C C     . LYS B 2 20  ? -8.668  -19.636 15.532  1.00 47.49  ? 22  LYS B C     1 
ATOM   2209  O O     . LYS B 2 20  ? -9.511  -19.118 14.803  1.00 52.69  ? 22  LYS B O     1 
ATOM   2210  C CB    . LYS B 2 20  ? -6.787  -21.013 14.582  1.00 51.31  ? 22  LYS B CB    1 
ATOM   2211  C CG    . LYS B 2 20  ? -5.409  -21.074 13.933  1.00 56.62  ? 22  LYS B CG    1 
ATOM   2212  C CD    . LYS B 2 20  ? -5.270  -20.212 12.684  1.00 60.12  ? 22  LYS B CD    1 
ATOM   2213  C CE    . LYS B 2 20  ? -3.922  -20.337 12.046  1.00 68.05  ? 22  LYS B CE    1 
ATOM   2214  N NZ    . LYS B 2 20  ? -3.815  -19.518 10.835  1.00 67.88  ? 22  LYS B NZ    1 
ATOM   2215  N N     . GLN B 2 21  ? -8.961  -20.215 16.701  1.00 47.11  ? 23  GLN B N     1 
ATOM   2216  C CA    . GLN B 2 21  ? -10.329 -20.378 17.166  1.00 44.56  ? 23  GLN B CA    1 
ATOM   2217  C C     . GLN B 2 21  ? -10.973 -19.016 17.411  1.00 41.32  ? 23  GLN B C     1 
ATOM   2218  O O     . GLN B 2 21  ? -12.117 -18.790 17.021  1.00 39.10  ? 23  GLN B O     1 
ATOM   2219  C CB    . GLN B 2 21  ? -10.371 -21.218 18.443  1.00 48.74  ? 23  GLN B CB    1 
ATOM   2220  C CG    . GLN B 2 21  ? -10.121 -22.705 18.215  1.00 53.24  ? 23  GLN B CG    1 
ATOM   2221  C CD    . GLN B 2 21  ? -11.155 -23.347 17.317  1.00 52.87  ? 23  GLN B CD    1 
ATOM   2222  O OE1   . GLN B 2 21  ? -10.837 -23.893 16.255  1.00 58.05  ? 23  GLN B OE1   1 
ATOM   2223  N NE2   . GLN B 2 21  ? -12.411 -23.281 17.735  1.00 53.57  ? 23  GLN B NE2   1 
ATOM   2224  N N     . ASN B 2 22  ? -10.238 -18.120 18.079  1.00 33.02  ? 24  ASN B N     1 
ATOM   2225  C CA    . ASN B 2 22  ? -10.786 -16.834 18.472  1.00 32.86  ? 24  ASN B CA    1 
ATOM   2226  C C     . ASN B 2 22  ? -9.676  -15.786 18.480  1.00 31.03  ? 24  ASN B C     1 
ATOM   2227  O O     . ASN B 2 22  ? -9.094  -15.500 19.524  1.00 31.41  ? 24  ASN B O     1 
ATOM   2228  C CB    . ASN B 2 22  ? -11.477 -16.923 19.828  1.00 35.85  ? 24  ASN B CB    1 
ATOM   2229  C CG    . ASN B 2 22  ? -12.429 -15.774 20.056  1.00 38.43  ? 24  ASN B CG    1 
ATOM   2230  O OD1   . ASN B 2 22  ? -12.072 -14.614 19.824  1.00 37.88  ? 24  ASN B OD1   1 
ATOM   2231  N ND2   . ASN B 2 22  ? -13.649 -16.075 20.477  1.00 39.50  ? 24  ASN B ND2   1 
ATOM   2232  N N     . PRO B 2 23  ? -9.355  -15.180 17.315  1.00 28.80  ? 25  PRO B N     1 
ATOM   2233  C CA    . PRO B 2 23  ? -8.273  -14.196 17.224  1.00 31.37  ? 25  PRO B CA    1 
ATOM   2234  C C     . PRO B 2 23  ? -8.403  -13.029 18.203  1.00 30.59  ? 25  PRO B C     1 
ATOM   2235  O O     . PRO B 2 23  ? -7.456  -12.717 18.923  1.00 28.46  ? 25  PRO B O     1 
ATOM   2236  C CB    . PRO B 2 23  ? -8.355  -13.729 15.755  1.00 30.59  ? 25  PRO B CB    1 
ATOM   2237  C CG    . PRO B 2 23  ? -8.976  -14.903 15.028  1.00 29.71  ? 25  PRO B CG    1 
ATOM   2238  C CD    . PRO B 2 23  ? -9.985  -15.459 16.015  1.00 30.47  ? 25  PRO B CD    1 
ATOM   2239  N N     . GLU B 2 24  ? -9.575  -12.383 18.208  1.00 31.42  ? 26  GLU B N     1 
ATOM   2240  C CA    . GLU B 2 24  ? -9.790  -11.199 19.025  1.00 37.98  ? 26  GLU B CA    1 
ATOM   2241  C C     . GLU B 2 24  ? -9.655  -11.560 20.502  1.00 38.11  ? 26  GLU B C     1 
ATOM   2242  O O     . GLU B 2 24  ? -9.005  -10.845 21.261  1.00 34.73  ? 26  GLU B O     1 
ATOM   2243  C CB    . GLU B 2 24  ? -11.153 -10.557 18.763  1.00 47.23  ? 26  GLU B CB    1 
ATOM   2244  C CG    . GLU B 2 24  ? -11.229 -9.800  17.440  1.00 54.45  ? 26  GLU B CG    1 
ATOM   2245  C CD    . GLU B 2 24  ? -12.401 -8.837  17.353  1.00 64.28  ? 26  GLU B CD    1 
ATOM   2246  O OE1   . GLU B 2 24  ? -13.554 -9.290  17.514  1.00 73.41  ? 26  GLU B OE1   1 
ATOM   2247  O OE2   . GLU B 2 24  ? -12.160 -7.632  17.128  1.00 63.11  ? 26  GLU B OE2   1 
ATOM   2248  N N     . ALA B 2 25  ? -10.286 -12.670 20.900  1.00 36.52  ? 27  ALA B N     1 
ATOM   2249  C CA    . ALA B 2 25  ? -10.275 -13.102 22.288  1.00 36.49  ? 27  ALA B CA    1 
ATOM   2250  C C     . ALA B 2 25  ? -8.836  -13.264 22.771  1.00 36.42  ? 27  ALA B C     1 
ATOM   2251  O O     . ALA B 2 25  ? -8.474  -12.767 23.835  1.00 35.55  ? 27  ALA B O     1 
ATOM   2252  C CB    . ALA B 2 25  ? -11.055 -14.390 22.436  1.00 36.42  ? 27  ALA B CB    1 
ATOM   2253  N N     . VAL B 2 26  ? -8.023  -13.961 21.970  1.00 34.86  ? 28  VAL B N     1 
ATOM   2254  C CA    . VAL B 2 26  ? -6.647  -14.256 22.331  1.00 33.51  ? 28  VAL B CA    1 
ATOM   2255  C C     . VAL B 2 26  ? -5.848  -12.955 22.380  1.00 33.76  ? 28  VAL B C     1 
ATOM   2256  O O     . VAL B 2 26  ? -5.055  -12.744 23.295  1.00 34.47  ? 28  VAL B O     1 
ATOM   2257  C CB    . VAL B 2 26  ? -6.016  -15.262 21.348  1.00 32.52  ? 28  VAL B CB    1 
ATOM   2258  C CG1   . VAL B 2 26  ? -4.536  -15.484 21.635  1.00 30.67  ? 28  VAL B CG1   1 
ATOM   2259  C CG2   . VAL B 2 26  ? -6.766  -16.589 21.338  1.00 33.10  ? 28  VAL B CG2   1 
ATOM   2260  N N     . MET B 2 27  ? -6.067  -12.086 21.387  1.00 34.26  ? 29  MET B N     1 
ATOM   2261  C CA    . MET B 2 27  ? -5.310  -10.849 21.271  1.00 33.96  ? 29  MET B CA    1 
ATOM   2262  C C     . MET B 2 27  ? -5.640  -9.919  22.436  1.00 34.49  ? 29  MET B C     1 
ATOM   2263  O O     . MET B 2 27  ? -4.744  -9.302  23.007  1.00 33.58  ? 29  MET B O     1 
ATOM   2264  C CB    . MET B 2 27  ? -5.597  -10.144 19.941  1.00 32.56  ? 29  MET B CB    1 
ATOM   2265  C CG    . MET B 2 27  ? -4.792  -10.693 18.776  1.00 35.43  ? 29  MET B CG    1 
ATOM   2266  S SD    . MET B 2 27  ? -5.059  -9.792  17.237  1.00 34.74  ? 29  MET B SD    1 
ATOM   2267  C CE    . MET B 2 27  ? -6.783  -10.190 16.917  1.00 35.42  ? 29  MET B CE    1 
ATOM   2268  N N     . ARG B 2 28  ? -6.930  -9.822  22.777  1.00 33.94  ? 30  ARG B N     1 
ATOM   2269  C CA    . ARG B 2 28  ? -7.374  -8.921  23.828  1.00 39.52  ? 30  ARG B CA    1 
ATOM   2270  C C     . ARG B 2 28  ? -6.841  -9.414  25.171  1.00 39.82  ? 30  ARG B C     1 
ATOM   2271  O O     . ARG B 2 28  ? -6.581  -8.619  26.071  1.00 39.37  ? 30  ARG B O     1 
ATOM   2272  C CB    . ARG B 2 28  ? -8.904  -8.820  23.856  1.00 46.57  ? 30  ARG B CB    1 
ATOM   2273  C CG    . ARG B 2 28  ? -9.541  -8.715  22.478  1.00 54.29  ? 30  ARG B CG    1 
ATOM   2274  C CD    . ARG B 2 28  ? -10.991 -8.263  22.530  1.00 55.79  ? 30  ARG B CD    1 
ATOM   2275  N NE    . ARG B 2 28  ? -11.103 -6.827  22.807  1.00 58.84  ? 30  ARG B NE    1 
ATOM   2276  C CZ    . ARG B 2 28  ? -11.548 -5.928  21.937  1.00 63.03  ? 30  ARG B CZ    1 
ATOM   2277  N NH1   . ARG B 2 28  ? -11.926 -6.307  20.729  1.00 63.89  ? 30  ARG B NH1   1 
ATOM   2278  N NH2   . ARG B 2 28  ? -11.608 -4.653  22.275  1.00 61.26  ? 30  ARG B NH2   1 
ATOM   2279  N N     . ALA B 2 29  ? -6.681  -10.737 25.285  1.00 33.70  ? 31  ALA B N     1 
ATOM   2280  C CA    . ALA B 2 29  ? -6.209  -11.354 26.513  1.00 36.80  ? 31  ALA B CA    1 
ATOM   2281  C C     . ALA B 2 29  ? -4.720  -11.074 26.700  1.00 36.76  ? 31  ALA B C     1 
ATOM   2282  O O     . ALA B 2 29  ? -4.209  -11.143 27.815  1.00 38.40  ? 31  ALA B O     1 
ATOM   2283  C CB    . ALA B 2 29  ? -6.491  -12.840 26.483  1.00 39.79  ? 31  ALA B CB    1 
ATOM   2284  N N     . HIS B 2 30  ? -4.035  -10.756 25.596  1.00 32.88  ? 32  HIS B N     1 
ATOM   2285  C CA    . HIS B 2 30  ? -2.607  -10.485 25.630  1.00 36.06  ? 32  HIS B CA    1 
ATOM   2286  C C     . HIS B 2 30  ? -2.372  -8.976  25.624  1.00 33.63  ? 32  HIS B C     1 
ATOM   2287  O O     . HIS B 2 30  ? -1.243  -8.520  25.457  1.00 33.19  ? 32  HIS B O     1 
ATOM   2288  C CB    . HIS B 2 30  ? -1.892  -11.215 24.487  1.00 35.15  ? 32  HIS B CB    1 
ATOM   2289  C CG    . HIS B 2 30  ? -1.778  -12.689 24.700  1.00 37.75  ? 32  HIS B CG    1 
ATOM   2290  N ND1   . HIS B 2 30  ? -2.814  -13.566 24.457  1.00 37.59  ? 32  HIS B ND1   1 
ATOM   2291  C CD2   . HIS B 2 30  ? -0.763  -13.434 25.159  1.00 39.86  ? 32  HIS B CD2   1 
ATOM   2292  C CE1   . HIS B 2 30  ? -2.420  -14.798 24.749  1.00 42.27  ? 32  HIS B CE1   1 
ATOM   2293  N NE2   . HIS B 2 30  ? -1.178  -14.741 25.176  1.00 43.42  ? 32  HIS B NE2   1 
ATOM   2294  N N     . GLY B 2 31  ? -3.458  -8.215  25.794  1.00 35.24  ? 33  GLY B N     1 
ATOM   2295  C CA    . GLY B 2 31  ? -3.372  -6.794  26.087  1.00 37.43  ? 33  GLY B CA    1 
ATOM   2296  C C     . GLY B 2 31  ? -3.146  -5.950  24.835  1.00 39.54  ? 33  GLY B C     1 
ATOM   2297  O O     . GLY B 2 31  ? -2.650  -4.830  24.927  1.00 36.38  ? 33  GLY B O     1 
ATOM   2298  N N     . LEU B 2 32  ? -3.521  -6.487  23.669  1.00 39.98  ? 34  LEU B N     1 
ATOM   2299  C CA    . LEU B 2 32  ? -3.433  -5.734  22.428  1.00 41.16  ? 34  LEU B CA    1 
ATOM   2300  C C     . LEU B 2 32  ? -4.575  -4.722  22.379  1.00 44.17  ? 34  LEU B C     1 
ATOM   2301  O O     . LEU B 2 32  ? -5.722  -5.059  22.663  1.00 42.81  ? 34  LEU B O     1 
ATOM   2302  C CB    . LEU B 2 32  ? -3.457  -6.660  21.212  1.00 42.52  ? 34  LEU B CB    1 
ATOM   2303  C CG    . LEU B 2 32  ? -2.147  -7.390  20.898  1.00 42.59  ? 34  LEU B CG    1 
ATOM   2304  C CD1   . LEU B 2 32  ? -1.827  -8.441  21.946  1.00 44.30  ? 34  LEU B CD1   1 
ATOM   2305  C CD2   . LEU B 2 32  ? -2.202  -8.010  19.512  1.00 46.24  ? 34  LEU B CD2   1 
ATOM   2306  N N     . THR B 2 33  ? -4.239  -3.483  22.006  1.00 49.11  ? 35  THR B N     1 
ATOM   2307  C CA    . THR B 2 33  ? -5.207  -2.400  21.958  1.00 49.35  ? 35  THR B CA    1 
ATOM   2308  C C     . THR B 2 33  ? -6.170  -2.635  20.798  1.00 48.02  ? 35  THR B C     1 
ATOM   2309  O O     . THR B 2 33  ? -5.935  -3.495  19.952  1.00 35.72  ? 35  THR B O     1 
ATOM   2310  C CB    . THR B 2 33  ? -4.477  -1.065  21.821  1.00 53.13  ? 35  THR B CB    1 
ATOM   2311  O OG1   . THR B 2 33  ? -3.773  -1.153  20.586  1.00 56.67  ? 35  THR B OG1   1 
ATOM   2312  C CG2   . THR B 2 33  ? -3.512  -0.807  22.964  1.00 53.63  ? 35  THR B CG2   1 
ATOM   2313  N N     . ASP B 2 34  ? -7.250  -1.846  20.770  1.00 48.49  ? 36  ASP B N     1 
ATOM   2314  C CA    . ASP B 2 34  ? -8.281  -1.973  19.754  1.00 53.96  ? 36  ASP B CA    1 
ATOM   2315  C C     . ASP B 2 34  ? -7.689  -1.645  18.386  1.00 51.42  ? 36  ASP B C     1 
ATOM   2316  O O     . ASP B 2 34  ? -8.025  -2.285  17.392  1.00 52.00  ? 36  ASP B O     1 
ATOM   2317  C CB    . ASP B 2 34  ? -9.474  -1.081  20.064  1.00 56.37  ? 36  ASP B CB    1 
ATOM   2318  C CG    . ASP B 2 34  ? -10.171 -1.355  21.388  1.00 61.93  ? 36  ASP B CG    1 
ATOM   2319  O OD1   . ASP B 2 34  ? -10.689 -2.479  21.557  1.00 63.80  ? 36  ASP B OD1   1 
ATOM   2320  O OD2   . ASP B 2 34  ? -10.191 -0.441  22.239  1.00 74.52  ? 36  ASP B OD2   1 
ATOM   2321  N N     . GLU B 2 35  ? -6.812  -0.637  18.353  1.00 47.93  ? 37  GLU B N     1 
ATOM   2322  C CA    . GLU B 2 35  ? -6.204  -0.179  17.115  1.00 50.97  ? 37  GLU B CA    1 
ATOM   2323  C C     . GLU B 2 35  ? -5.239  -1.242  16.597  1.00 49.89  ? 37  GLU B C     1 
ATOM   2324  O O     . GLU B 2 35  ? -5.113  -1.438  15.390  1.00 45.06  ? 37  GLU B O     1 
ATOM   2325  C CB    . GLU B 2 35  ? -5.489  1.155   17.334  1.00 57.01  ? 37  GLU B CB    1 
ATOM   2326  C CG    . GLU B 2 35  ? -4.382  1.087   18.383  1.00 64.86  ? 37  GLU B CG    1 
ATOM   2327  C CD    . GLU B 2 35  ? -3.693  2.414   18.650  1.00 70.58  ? 37  GLU B CD    1 
ATOM   2328  O OE1   . GLU B 2 35  ? -3.108  2.979   17.702  1.00 74.16  ? 37  GLU B OE1   1 
ATOM   2329  O OE2   . GLU B 2 35  ? -3.742  2.882   19.807  1.00 71.31  ? 37  GLU B OE2   1 
ATOM   2330  N N     . GLN B 2 36  ? -4.558  -1.919  17.528  1.00 46.95  ? 38  GLN B N     1 
ATOM   2331  C CA    . GLN B 2 36  ? -3.619  -2.973  17.182  1.00 44.91  ? 38  GLN B CA    1 
ATOM   2332  C C     . GLN B 2 36  ? -4.388  -4.167  16.624  1.00 43.83  ? 38  GLN B C     1 
ATOM   2333  O O     . GLN B 2 36  ? -3.926  -4.832  15.699  1.00 39.55  ? 38  GLN B O     1 
ATOM   2334  C CB    . GLN B 2 36  ? -2.792  -3.371  18.404  1.00 43.56  ? 38  GLN B CB    1 
ATOM   2335  C CG    . GLN B 2 36  ? -1.846  -2.281  18.895  1.00 47.43  ? 38  GLN B CG    1 
ATOM   2336  C CD    . GLN B 2 36  ? -1.154  -2.633  20.193  1.00 46.59  ? 38  GLN B CD    1 
ATOM   2337  O OE1   . GLN B 2 36  ? -1.458  -3.646  20.833  1.00 45.59  ? 38  GLN B OE1   1 
ATOM   2338  N NE2   . GLN B 2 36  ? -0.221  -1.787  20.604  1.00 50.26  ? 38  GLN B NE2   1 
ATOM   2339  N N     . ILE B 2 37  ? -5.567  -4.423  17.199  1.00 43.08  ? 39  ILE B N     1 
ATOM   2340  C CA    . ILE B 2 37  ? -6.404  -5.536  16.783  1.00 39.78  ? 39  ILE B CA    1 
ATOM   2341  C C     . ILE B 2 37  ? -7.005  -5.220  15.417  1.00 39.76  ? 39  ILE B C     1 
ATOM   2342  O O     . ILE B 2 37  ? -7.067  -6.085  14.546  1.00 39.76  ? 39  ILE B O     1 
ATOM   2343  C CB    . ILE B 2 37  ? -7.488  -5.828  17.836  1.00 37.14  ? 39  ILE B CB    1 
ATOM   2344  C CG1   . ILE B 2 37  ? -6.872  -6.266  19.165  1.00 40.44  ? 39  ILE B CG1   1 
ATOM   2345  C CG2   . ILE B 2 37  ? -8.496  -6.854  17.316  1.00 37.02  ? 39  ILE B CG2   1 
ATOM   2346  C CD1   . ILE B 2 37  ? -7.888  -6.553  20.256  1.00 44.70  ? 39  ILE B CD1   1 
ATOM   2347  N N     . ASN B 2 38  ? -7.441  -3.968  15.242  1.00 42.10  ? 40  ASN B N     1 
ATOM   2348  C CA    . ASN B 2 38  ? -8.044  -3.529  13.995  1.00 45.18  ? 40  ASN B CA    1 
ATOM   2349  C C     . ASN B 2 38  ? -7.041  -3.702  12.859  1.00 45.04  ? 40  ASN B C     1 
ATOM   2350  O O     . ASN B 2 38  ? -7.390  -4.180  11.782  1.00 45.83  ? 40  ASN B O     1 
ATOM   2351  C CB    . ASN B 2 38  ? -8.530  -2.087  14.084  1.00 48.13  ? 40  ASN B CB    1 
ATOM   2352  C CG    . ASN B 2 38  ? -9.144  -1.616  12.787  1.00 47.91  ? 40  ASN B CG    1 
ATOM   2353  O OD1   . ASN B 2 38  ? -10.180 -2.140  12.364  1.00 49.23  ? 40  ASN B OD1   1 
ATOM   2354  N ND2   . ASN B 2 38  ? -8.527  -0.635  12.146  1.00 49.17  ? 40  ASN B ND2   1 
ATOM   2355  N N     . ALA B 2 39  ? -5.793  -3.298  13.117  1.00 46.07  ? 41  ALA B N     1 
ATOM   2356  C CA    . ALA B 2 39  ? -4.732  -3.390  12.128  1.00 44.04  ? 41  ALA B CA    1 
ATOM   2357  C C     . ALA B 2 39  ? -4.548  -4.843  11.699  1.00 38.67  ? 41  ALA B C     1 
ATOM   2358  O O     . ALA B 2 39  ? -4.343  -5.127  10.521  1.00 42.25  ? 41  ALA B O     1 
ATOM   2359  C CB    . ALA B 2 39  ? -3.452  -2.814  12.693  1.00 44.18  ? 41  ALA B CB    1 
ATOM   2360  N N     . VAL B 2 40  ? -4.624  -5.754  12.674  1.00 34.74  ? 42  VAL B N     1 
ATOM   2361  C CA    . VAL B 2 40  ? -4.438  -7.173  12.421  1.00 33.93  ? 42  VAL B CA    1 
ATOM   2362  C C     . VAL B 2 40  ? -5.604  -7.684  11.578  1.00 34.33  ? 42  VAL B C     1 
ATOM   2363  O O     . VAL B 2 40  ? -5.406  -8.449  10.638  1.00 33.66  ? 42  VAL B O     1 
ATOM   2364  C CB    . VAL B 2 40  ? -4.314  -7.968  13.735  1.00 33.23  ? 42  VAL B CB    1 
ATOM   2365  C CG1   . VAL B 2 40  ? -4.392  -9.473  13.497  1.00 32.11  ? 42  VAL B CG1   1 
ATOM   2366  C CG2   . VAL B 2 40  ? -3.046  -7.607  14.499  1.00 32.71  ? 42  VAL B CG2   1 
ATOM   2367  N N     . MET B 2 41  ? -6.818  -7.248  11.927  1.00 38.12  ? 43  MET B N     1 
ATOM   2368  C CA    . MET B 2 41  ? -8.025  -7.733  11.278  1.00 41.15  ? 43  MET B CA    1 
ATOM   2369  C C     . MET B 2 41  ? -8.110  -7.185  9.856   1.00 40.19  ? 43  MET B C     1 
ATOM   2370  O O     . MET B 2 41  ? -8.624  -7.854  8.963   1.00 37.01  ? 43  MET B O     1 
ATOM   2371  C CB    . MET B 2 41  ? -9.276  -7.329  12.067  1.00 43.25  ? 43  MET B CB    1 
ATOM   2372  C CG    . MET B 2 41  ? -9.404  -8.023  13.411  1.00 46.32  ? 43  MET B CG    1 
ATOM   2373  S SD    . MET B 2 41  ? -9.224  -9.814  13.288  1.00 56.00  ? 43  MET B SD    1 
ATOM   2374  C CE    . MET B 2 41  ? -10.347 -10.175 11.931  1.00 53.46  ? 43  MET B CE    1 
ATOM   2375  N N     . THR B 2 42  ? -7.605  -5.963  9.657   1.00 42.81  ? 44  THR B N     1 
ATOM   2376  C CA    . THR B 2 42  ? -7.614  -5.337  8.344   1.00 44.70  ? 44  THR B CA    1 
ATOM   2377  C C     . THR B 2 42  ? -6.321  -5.690  7.613   1.00 46.52  ? 44  THR B C     1 
ATOM   2378  O O     . THR B 2 42  ? -6.198  -5.455  6.412   1.00 52.96  ? 44  THR B O     1 
ATOM   2379  C CB    . THR B 2 42  ? -7.796  -3.826  8.488   1.00 46.75  ? 44  THR B CB    1 
ATOM   2380  O OG1   . THR B 2 42  ? -6.753  -3.391  9.354   1.00 49.81  ? 44  THR B OG1   1 
ATOM   2381  C CG2   . THR B 2 42  ? -9.147  -3.457  9.075   1.00 48.24  ? 44  THR B CG2   1 
ATOM   2382  N N     . GLY B 2 43  ? -5.361  -6.252  8.355   1.00 49.15  ? 45  GLY B N     1 
ATOM   2383  C CA    . GLY B 2 43  ? -4.121  -6.743  7.778   1.00 52.50  ? 45  GLY B CA    1 
ATOM   2384  C C     . GLY B 2 43  ? -3.212  -5.602  7.329   1.00 56.92  ? 45  GLY B C     1 
ATOM   2385  O O     . GLY B 2 43  ? -2.489  -5.731  6.343   1.00 56.65  ? 45  GLY B O     1 
ATOM   2386  N N     . ASP B 2 44  ? -3.252  -4.489  8.070   1.00 55.57  ? 46  ASP B N     1 
ATOM   2387  C CA    . ASP B 2 44  ? -2.408  -3.342  7.780   1.00 54.03  ? 46  ASP B CA    1 
ATOM   2388  C C     . ASP B 2 44  ? -1.069  -3.519  8.491   1.00 48.93  ? 46  ASP B C     1 
ATOM   2389  O O     . ASP B 2 44  ? -0.871  -3.007  9.591   1.00 41.89  ? 46  ASP B O     1 
ATOM   2390  C CB    . ASP B 2 44  ? -3.092  -2.040  8.168   1.00 61.48  ? 46  ASP B CB    1 
ATOM   2391  C CG    . ASP B 2 44  ? -2.306  -0.773  7.862   1.00 67.35  ? 46  ASP B CG    1 
ATOM   2392  O OD1   . ASP B 2 44  ? -1.181  -0.894  7.333   1.00 68.47  ? 46  ASP B OD1   1 
ATOM   2393  O OD2   . ASP B 2 44  ? -2.827  0.325   8.152   1.00 72.50  ? 46  ASP B OD2   1 
ATOM   2394  N N     . MET B 2 45  ? -0.154  -4.246  7.841   1.00 48.78  ? 47  MET B N     1 
ATOM   2395  C CA    . MET B 2 45  ? 1.142   -4.554  8.421   1.00 49.98  ? 47  MET B CA    1 
ATOM   2396  C C     . MET B 2 45  ? 1.885   -3.259  8.743   1.00 53.06  ? 47  MET B C     1 
ATOM   2397  O O     . MET B 2 45  ? 2.562   -3.166  9.765   1.00 55.08  ? 47  MET B O     1 
ATOM   2398  C CB    . MET B 2 45  ? 1.986   -5.403  7.463   1.00 49.36  ? 47  MET B CB    1 
ATOM   2399  C CG    . MET B 2 45  ? 1.401   -6.772  7.153   1.00 48.66  ? 47  MET B CG    1 
ATOM   2400  S SD    . MET B 2 45  ? 1.139   -7.798  8.614   1.00 42.77  ? 47  MET B SD    1 
ATOM   2401  C CE    . MET B 2 45  ? -0.470  -7.230  9.178   1.00 44.39  ? 47  MET B CE    1 
ATOM   2402  N N     . GLU B 2 46  ? 1.750   -2.265  7.859   1.00 53.58  ? 48  GLU B N     1 
ATOM   2403  C CA    . GLU B 2 46  ? 2.434   -0.993  8.018   1.00 56.56  ? 48  GLU B CA    1 
ATOM   2404  C C     . GLU B 2 46  ? 2.186   -0.445  9.421   1.00 54.32  ? 48  GLU B C     1 
ATOM   2405  O O     . GLU B 2 46  ? 3.128   -0.132  10.145  1.00 53.12  ? 48  GLU B O     1 
ATOM   2406  C CB    . GLU B 2 46  ? 1.969   0.009   6.961   1.00 62.58  ? 48  GLU B CB    1 
ATOM   2407  C CG    . GLU B 2 46  ? 2.437   -0.333  5.549   1.00 72.20  ? 48  GLU B CG    1 
ATOM   2408  C CD    . GLU B 2 46  ? 3.942   -0.275  5.359   1.00 80.34  ? 48  GLU B CD    1 
ATOM   2409  O OE1   . GLU B 2 46  ? 4.406   -0.540  4.230   1.00 92.27  ? 48  GLU B OE1   1 
ATOM   2410  O OE2   . GLU B 2 46  ? 4.651   0.038   6.339   1.00 86.77  ? 48  GLU B OE2   1 
ATOM   2411  N N     . LYS B 2 47  ? 0.906   -0.335  9.791   1.00 54.60  ? 49  LYS B N     1 
ATOM   2412  C CA    . LYS B 2 47  ? 0.517   0.264   11.058  1.00 54.89  ? 49  LYS B CA    1 
ATOM   2413  C C     . LYS B 2 47  ? 1.112   -0.537  12.213  1.00 49.62  ? 49  LYS B C     1 
ATOM   2414  O O     . LYS B 2 47  ? 1.538   0.037   13.213  1.00 52.06  ? 49  LYS B O     1 
ATOM   2415  C CB    . LYS B 2 47  ? -1.010  0.339   11.173  1.00 57.66  ? 49  LYS B CB    1 
ATOM   2416  C CG    . LYS B 2 47  ? -1.527  0.985   12.452  1.00 62.54  ? 49  LYS B CG    1 
ATOM   2417  C CD    . LYS B 2 47  ? -3.047  1.051   12.547  1.00 67.16  ? 49  LYS B CD    1 
ATOM   2418  C CE    . LYS B 2 47  ? -3.669  1.849   11.443  1.00 68.70  ? 49  LYS B CE    1 
ATOM   2419  N NZ    . LYS B 2 47  ? -3.232  3.247   11.464  1.00 68.58  ? 49  LYS B NZ    1 
ATOM   2420  N N     . LEU B 2 48  ? 1.133   -1.866  12.064  1.00 42.43  ? 50  LEU B N     1 
ATOM   2421  C CA    . LEU B 2 48  ? 1.621   -2.748  13.112  1.00 43.01  ? 50  LEU B CA    1 
ATOM   2422  C C     . LEU B 2 48  ? 3.053   -2.368  13.477  1.00 44.19  ? 50  LEU B C     1 
ATOM   2423  O O     . LEU B 2 48  ? 3.430   -2.404  14.646  1.00 40.60  ? 50  LEU B O     1 
ATOM   2424  C CB    . LEU B 2 48  ? 1.530   -4.208  12.668  1.00 42.35  ? 50  LEU B CB    1 
ATOM   2425  C CG    . LEU B 2 48  ? 0.117   -4.780  12.526  1.00 45.49  ? 50  LEU B CG    1 
ATOM   2426  C CD1   . LEU B 2 48  ? 0.167   -6.278  12.275  1.00 45.62  ? 50  LEU B CD1   1 
ATOM   2427  C CD2   . LEU B 2 48  ? -0.724  -4.468  13.752  1.00 45.74  ? 50  LEU B CD2   1 
ATOM   2428  N N     . LYS B 2 49  ? 3.844   -2.011  12.460  1.00 53.40  ? 51  LYS B N     1 
ATOM   2429  C CA    . LYS B 2 49  ? 5.239   -1.658  12.657  1.00 61.74  ? 51  LYS B CA    1 
ATOM   2430  C C     . LYS B 2 49  ? 5.326   -0.296  13.339  1.00 60.04  ? 51  LYS B C     1 
ATOM   2431  O O     . LYS B 2 49  ? 6.159   -0.088  14.218  1.00 66.26  ? 51  LYS B O     1 
ATOM   2432  C CB    . LYS B 2 49  ? 5.981   -1.658  11.315  1.00 68.69  ? 51  LYS B CB    1 
ATOM   2433  C CG    . LYS B 2 49  ? 5.998   -3.002  10.598  1.00 74.43  ? 51  LYS B CG    1 
ATOM   2434  C CD    . LYS B 2 49  ? 6.747   -2.994  9.271   1.00 78.82  ? 51  LYS B CD    1 
ATOM   2435  C CE    . LYS B 2 49  ? 6.762   -4.340  8.618   1.00 78.85  ? 51  LYS B CE    1 
ATOM   2436  N NZ    . LYS B 2 49  ? 7.488   -4.319  7.346   1.00 80.81  ? 51  LYS B NZ    1 
ATOM   2437  N N     . THR B 2 50  ? 4.449   0.623   12.922  1.00 59.76  ? 52  THR B N     1 
ATOM   2438  C CA    . THR B 2 50  ? 4.414   1.967   13.473  1.00 61.25  ? 52  THR B CA    1 
ATOM   2439  C C     . THR B 2 50  ? 4.029   1.899   14.949  1.00 60.54  ? 52  THR B C     1 
ATOM   2440  O O     . THR B 2 50  ? 4.542   2.661   15.765  1.00 55.53  ? 52  THR B O     1 
ATOM   2441  C CB    . THR B 2 50  ? 3.428   2.818   12.673  1.00 61.49  ? 52  THR B CB    1 
ATOM   2442  O OG1   . THR B 2 50  ? 4.002   2.945   11.376  1.00 65.42  ? 52  THR B OG1   1 
ATOM   2443  C CG2   . THR B 2 50  ? 3.213   4.191   13.283  1.00 66.55  ? 52  THR B CG2   1 
ATOM   2444  N N     . LEU B 2 51  ? 3.118   0.975   15.274  1.00 56.85  ? 53  LEU B N     1 
ATOM   2445  C CA    . LEU B 2 51  ? 2.606   0.840   16.627  1.00 54.60  ? 53  LEU B CA    1 
ATOM   2446  C C     . LEU B 2 51  ? 3.626   0.102   17.489  1.00 56.38  ? 53  LEU B C     1 
ATOM   2447  O O     . LEU B 2 51  ? 3.550   0.141   18.715  1.00 59.77  ? 53  LEU B O     1 
ATOM   2448  C CB    . LEU B 2 51  ? 1.261   0.114   16.600  1.00 52.18  ? 53  LEU B CB    1 
ATOM   2449  C CG    . LEU B 2 51  ? 0.127   0.835   15.863  1.00 50.82  ? 53  LEU B CG    1 
ATOM   2450  C CD1   . LEU B 2 51  ? -1.165  0.040   15.937  1.00 47.71  ? 53  LEU B CD1   1 
ATOM   2451  C CD2   . LEU B 2 51  ? -0.074  2.235   16.416  1.00 50.54  ? 53  LEU B CD2   1 
ATOM   2452  N N     . SER B 2 52  ? 4.577   -0.571  16.833  1.00 60.10  ? 54  SER B N     1 
ATOM   2453  C CA    . SER B 2 52  ? 5.622   -1.300  17.532  1.00 61.68  ? 54  SER B CA    1 
ATOM   2454  C C     . SER B 2 52  ? 6.797   -0.367  17.815  1.00 67.19  ? 54  SER B C     1 
ATOM   2455  O O     . SER B 2 52  ? 7.297   -0.315  18.936  1.00 70.90  ? 54  SER B O     1 
ATOM   2456  C CB    . SER B 2 52  ? 6.059   -2.512  16.749  1.00 59.48  ? 54  SER B CB    1 
ATOM   2457  O OG    . SER B 2 52  ? 6.976   -3.300  17.496  1.00 59.08  ? 54  SER B OG    1 
ATOM   2458  N N     . GLY B 2 53  ? 7.225   0.368   16.782  1.00 73.70  ? 55  GLY B N     1 
ATOM   2459  C CA    . GLY B 2 53  ? 8.313   1.322   16.914  1.00 73.08  ? 55  GLY B CA    1 
ATOM   2460  C C     . GLY B 2 53  ? 9.127   1.426   15.627  1.00 73.97  ? 55  GLY B C     1 
ATOM   2461  O O     . GLY B 2 53  ? 8.887   0.691   14.672  1.00 67.24  ? 55  GLY B O     1 
ATOM   2462  N N     . ASP B 2 54  ? 10.091  2.354   15.623  1.00 82.82  ? 56  ASP B N     1 
ATOM   2463  C CA    . ASP B 2 54  ? 10.957  2.573   14.477  1.00 85.44  ? 56  ASP B CA    1 
ATOM   2464  C C     . ASP B 2 54  ? 10.254  3.506   13.484  1.00 88.03  ? 56  ASP B C     1 
ATOM   2465  O O     . ASP B 2 54  ? 10.946  4.408   12.960  1.00 89.03  ? 56  ASP B O     1 
ATOM   2466  C CB    . ASP B 2 54  ? 11.368  1.259   13.830  1.00 86.58  ? 56  ASP B CB    1 
ATOM   2467  C CG    . ASP B 2 54  ? 12.157  0.313   14.723  1.00 88.35  ? 56  ASP B CG    1 
ATOM   2468  O OD1   . ASP B 2 54  ? 13.221  0.732   15.226  1.00 87.80  ? 56  ASP B OD1   1 
ATOM   2469  O OD2   . ASP B 2 54  ? 11.703  -0.837  14.906  1.00 87.79  ? 56  ASP B OD2   1 
ATOM   2470  N N     . ALA B 2 60  ? 15.815  -3.386  3.123   1.00 69.90  ? 62  ALA B N     1 
ATOM   2471  C CA    . ALA B 2 60  ? 15.928  -4.076  1.814   1.00 68.68  ? 62  ALA B CA    1 
ATOM   2472  C C     . ALA B 2 60  ? 16.176  -5.566  2.042   1.00 66.25  ? 62  ALA B C     1 
ATOM   2473  O O     . ALA B 2 60  ? 16.862  -5.945  2.988   1.00 72.14  ? 62  ALA B O     1 
ATOM   2474  C CB    . ALA B 2 60  ? 17.030  -3.440  0.994   1.00 67.86  ? 62  ALA B CB    1 
ATOM   2475  N N     . LEU B 2 61  ? 15.612  -6.402  1.161   1.00 62.13  ? 63  LEU B N     1 
ATOM   2476  C CA    . LEU B 2 61  ? 15.662  -7.848  1.328   1.00 58.89  ? 63  LEU B CA    1 
ATOM   2477  C C     . LEU B 2 61  ? 16.228  -8.521  0.078   1.00 54.81  ? 63  LEU B C     1 
ATOM   2478  O O     . LEU B 2 61  ? 16.160  -9.741  -0.049  1.00 46.59  ? 63  LEU B O     1 
ATOM   2479  C CB    . LEU B 2 61  ? 14.269  -8.384  1.658   1.00 60.41  ? 63  LEU B CB    1 
ATOM   2480  C CG    . LEU B 2 61  ? 14.042  -8.825  3.109   1.00 66.61  ? 63  LEU B CG    1 
ATOM   2481  C CD1   . LEU B 2 61  ? 14.146  -7.667  4.086   1.00 65.90  ? 63  LEU B CD1   1 
ATOM   2482  C CD2   . LEU B 2 61  ? 12.699  -9.525  3.245   1.00 66.91  ? 63  LEU B CD2   1 
ATOM   2483  N N     . VAL B 2 62  ? 16.792  -7.723  -0.833  1.00 53.16  ? 64  VAL B N     1 
ATOM   2484  C CA    . VAL B 2 62  ? 17.403  -8.256  -2.041  1.00 52.93  ? 64  VAL B CA    1 
ATOM   2485  C C     . VAL B 2 62  ? 18.808  -8.757  -1.718  1.00 49.65  ? 64  VAL B C     1 
ATOM   2486  O O     . VAL B 2 62  ? 19.664  -7.960  -1.331  1.00 46.52  ? 64  VAL B O     1 
ATOM   2487  C CB    . VAL B 2 62  ? 17.447  -7.181  -3.145  1.00 55.15  ? 64  VAL B CB    1 
ATOM   2488  C CG1   . VAL B 2 62  ? 17.715  -7.790  -4.516  1.00 54.04  ? 64  VAL B CG1   1 
ATOM   2489  C CG2   . VAL B 2 62  ? 16.176  -6.341  -3.174  1.00 58.60  ? 64  VAL B CG2   1 
HETATM 2490  N N     . IML B 2 63  ? 19.107  -10.074 -1.858  1.00 46.61  ? 65  IML B N     1 
HETATM 2491  C CA    . IML B 2 63  ? 20.471  -10.540 -1.580  1.00 47.31  ? 65  IML B CA    1 
HETATM 2492  C C     . IML B 2 63  ? 21.068  -11.246 -2.797  1.00 47.61  ? 65  IML B C     1 
HETATM 2493  O O     . IML B 2 63  ? 21.828  -12.203 -2.653  1.00 45.30  ? 65  IML B O     1 
HETATM 2494  C CB    . IML B 2 63  ? 20.484  -11.454 -0.332  1.00 42.62  ? 65  IML B CB    1 
HETATM 2495  C CN    . IML B 2 63  ? 18.142  -11.090 -2.250  1.00 43.73  ? 65  IML B CN    1 
HETATM 2496  C CG2   . IML B 2 63  ? 21.890  -11.616 0.224   1.00 43.40  ? 65  IML B CG2   1 
HETATM 2497  C CG1   . IML B 2 63  ? 19.509  -10.950 0.736   1.00 41.92  ? 65  IML B CG1   1 
HETATM 2498  C CD1   . IML B 2 63  ? 19.250  -11.938 1.851   1.00 38.89  ? 65  IML B CD1   1 
ATOM   2499  N N     . SER B 2 64  ? 20.735  -10.746 -3.994  1.00 49.63  ? 66  SER B N     1 
ATOM   2500  C CA    . SER B 2 64  ? 21.193  -11.351 -5.235  1.00 50.44  ? 66  SER B CA    1 
ATOM   2501  C C     . SER B 2 64  ? 20.860  -10.448 -6.421  1.00 51.31  ? 66  SER B C     1 
ATOM   2502  O O     . SER B 2 64  ? 20.128  -9.471  -6.277  1.00 55.58  ? 66  SER B O     1 
ATOM   2503  C CB    . SER B 2 64  ? 20.598  -12.727 -5.413  1.00 50.61  ? 66  SER B CB    1 
ATOM   2504  O OG    . SER B 2 64  ? 19.178  -12.676 -5.413  1.00 49.41  ? 66  SER B OG    1 
ATOM   2505  N N     . HIS B 2 65  ? 21.410  -10.794 -7.592  1.00 48.06  ? 67  HIS B N     1 
ATOM   2506  C CA    . HIS B 2 65  ? 21.158  -10.058 -8.822  1.00 49.64  ? 67  HIS B CA    1 
ATOM   2507  C C     . HIS B 2 65  ? 21.082  -11.032 -9.995  1.00 50.59  ? 67  HIS B C     1 
ATOM   2508  O O     . HIS B 2 65  ? 21.380  -12.215 -9.846  1.00 51.52  ? 67  HIS B O     1 
ATOM   2509  C CB    . HIS B 2 65  ? 22.240  -8.997  -9.055  1.00 51.38  ? 67  HIS B CB    1 
ATOM   2510  C CG    . HIS B 2 65  ? 23.629  -9.545  -9.088  1.00 52.69  ? 67  HIS B CG    1 
ATOM   2511  N ND1   . HIS B 2 65  ? 24.145  -10.217 -10.175 1.00 50.82  ? 67  HIS B ND1   1 
ATOM   2512  C CD2   . HIS B 2 65  ? 24.599  -9.541  -8.163  1.00 51.96  ? 67  HIS B CD2   1 
ATOM   2513  C CE1   . HIS B 2 65  ? 25.388  -10.591 -9.909  1.00 51.75  ? 67  HIS B CE1   1 
ATOM   2514  N NE2   . HIS B 2 65  ? 25.685  -10.188 -8.694  1.00 52.16  ? 67  HIS B NE2   1 
ATOM   2515  N N     . GLY B 2 66  ? 20.690  -10.512 -11.164 1.00 53.97  ? 68  GLY B N     1 
ATOM   2516  C CA    . GLY B 2 66  ? 20.560  -11.318 -12.368 1.00 53.57  ? 68  GLY B CA    1 
ATOM   2517  C C     . GLY B 2 66  ? 21.400  -10.755 -13.513 1.00 56.98  ? 68  GLY B C     1 
ATOM   2518  O O     . GLY B 2 66  ? 21.009  -10.844 -14.675 1.00 53.93  ? 68  GLY B O     1 
ATOM   2519  N N     . ASN B 2 67  ? 22.556  -10.178 -13.167 1.00 55.81  ? 69  ASN B N     1 
ATOM   2520  C CA    . ASN B 2 67  ? 23.473  -9.637  -14.156 1.00 56.98  ? 69  ASN B CA    1 
ATOM   2521  C C     . ASN B 2 67  ? 24.679  -10.563 -14.287 1.00 57.21  ? 69  ASN B C     1 
ATOM   2522  O O     . ASN B 2 67  ? 25.662  -10.221 -14.941 1.00 54.74  ? 69  ASN B O     1 
ATOM   2523  C CB    . ASN B 2 67  ? 23.897  -8.213  -13.812 1.00 55.56  ? 69  ASN B CB    1 
ATOM   2524  C CG    . ASN B 2 67  ? 22.751  -7.237  -13.913 1.00 54.76  ? 69  ASN B CG    1 
ATOM   2525  O OD1   . ASN B 2 67  ? 21.612  -7.639  -14.175 1.00 57.28  ? 69  ASN B OD1   1 
ATOM   2526  N ND2   . ASN B 2 67  ? 23.027  -5.957  -13.710 1.00 55.31  ? 69  ASN B ND2   1 
ATOM   2527  N N     . GLY B 2 68  ? 24.588  -11.739 -13.657 1.00 57.92  ? 70  GLY B N     1 
ATOM   2528  C CA    . GLY B 2 68  ? 25.649  -12.730 -13.714 1.00 58.82  ? 70  GLY B CA    1 
ATOM   2529  C C     . GLY B 2 68  ? 26.843  -12.312 -12.877 1.00 57.98  ? 70  GLY B C     1 
ATOM   2530  O O     . GLY B 2 68  ? 26.969  -11.094 -12.634 1.00 58.96  ? 70  GLY B O     1 
ATOM   2531  N N     . GLY C 1 1   ? -12.342 -32.011 14.789  1.00 47.66  ? 2   GLY C N     1 
ATOM   2532  C CA    . GLY C 1 1   ? -11.113 -32.584 14.207  1.00 43.65  ? 2   GLY C CA    1 
ATOM   2533  C C     . GLY C 1 1   ? -10.406 -31.576 13.306  1.00 43.64  ? 2   GLY C C     1 
ATOM   2534  O O     . GLY C 1 1   ? -11.031 -30.652 12.788  1.00 37.94  ? 2   GLY C O     1 
ATOM   2535  N N     . SER C 1 2   ? -9.094  -31.768 13.131  1.00 38.82  ? 3   SER C N     1 
ATOM   2536  C CA    . SER C 1 2   ? -8.291  -30.897 12.291  1.00 35.34  ? 3   SER C CA    1 
ATOM   2537  C C     . SER C 1 2   ? -7.053  -31.647 11.812  1.00 33.28  ? 3   SER C C     1 
ATOM   2538  O O     . SER C 1 2   ? -6.648  -32.637 12.417  1.00 30.88  ? 3   SER C O     1 
ATOM   2539  C CB    . SER C 1 2   ? -7.914  -29.633 13.021  1.00 34.39  ? 3   SER C CB    1 
ATOM   2540  O OG    . SER C 1 2   ? -7.134  -29.925 14.172  1.00 37.33  ? 3   SER C OG    1 
ATOM   2541  N N     . LEU C 1 3   ? -6.461  -31.161 10.717  1.00 32.52  ? 4   LEU C N     1 
ATOM   2542  C CA    . LEU C 1 3   ? -5.270  -31.775 10.155  1.00 30.29  ? 4   LEU C CA    1 
ATOM   2543  C C     . LEU C 1 3   ? -4.189  -30.716 9.972   1.00 28.78  ? 4   LEU C C     1 
ATOM   2544  O O     . LEU C 1 3   ? -4.451  -29.630 9.459   1.00 26.57  ? 4   LEU C O     1 
ATOM   2545  C CB    . LEU C 1 3   ? -5.604  -32.455 8.829   1.00 33.00  ? 4   LEU C CB    1 
ATOM   2546  C CG    . LEU C 1 3   ? -4.414  -33.052 8.071   1.00 29.80  ? 4   LEU C CG    1 
ATOM   2547  C CD1   . LEU C 1 3   ? -3.785  -34.185 8.863   1.00 29.96  ? 4   LEU C CD1   1 
ATOM   2548  C CD2   . LEU C 1 3   ? -4.823  -33.522 6.686   1.00 30.61  ? 4   LEU C CD2   1 
ATOM   2549  N N     . VAL C 1 4   ? -2.969  -31.053 10.400  1.00 26.96  ? 5   VAL C N     1 
ATOM   2550  C CA    . VAL C 1 4   ? -1.807  -30.224 10.142  1.00 25.25  ? 5   VAL C CA    1 
ATOM   2551  C C     . VAL C 1 4   ? -0.668  -31.131 9.689   1.00 23.83  ? 5   VAL C C     1 
ATOM   2552  O O     . VAL C 1 4   ? -0.219  -31.996 10.439  1.00 21.54  ? 5   VAL C O     1 
ATOM   2553  C CB    . VAL C 1 4   ? -1.394  -29.380 11.362  1.00 26.00  ? 5   VAL C CB    1 
ATOM   2554  C CG1   . VAL C 1 4   ? -0.077  -28.651 11.122  1.00 26.59  ? 5   VAL C CG1   1 
ATOM   2555  C CG2   . VAL C 1 4   ? -2.486  -28.397 11.767  1.00 27.03  ? 5   VAL C CG2   1 
ATOM   2556  N N     . CYS C 1 5   ? -0.224  -30.928 8.446   1.00 23.95  ? 6   CYS C N     1 
ATOM   2557  C CA    . CYS C 1 5   ? 0.882   -31.683 7.886   1.00 24.87  ? 6   CYS C CA    1 
ATOM   2558  C C     . CYS C 1 5   ? 2.169   -30.883 8.057   1.00 24.83  ? 6   CYS C C     1 
ATOM   2559  O O     . CYS C 1 5   ? 2.232   -29.711 7.690   1.00 22.52  ? 6   CYS C O     1 
ATOM   2560  C CB    . CYS C 1 5   ? 0.634   -32.006 6.417   1.00 28.33  ? 6   CYS C CB    1 
ATOM   2561  S SG    . CYS C 1 5   ? -0.860  -32.994 6.137   1.00 33.55  ? 6   CYS C SG    1 
ATOM   2562  N N     . VAL C 1 6   ? 3.189   -31.530 8.626   1.00 25.78  ? 7   VAL C N     1 
ATOM   2563  C CA    . VAL C 1 6   ? 4.452   -30.870 8.901   1.00 26.11  ? 7   VAL C CA    1 
ATOM   2564  C C     . VAL C 1 6   ? 5.583   -31.702 8.306   1.00 27.19  ? 7   VAL C C     1 
ATOM   2565  O O     . VAL C 1 6   ? 5.413   -32.886 8.020   1.00 29.87  ? 7   VAL C O     1 
ATOM   2566  C CB    . VAL C 1 6   ? 4.660   -30.656 10.413  1.00 27.50  ? 7   VAL C CB    1 
ATOM   2567  C CG1   . VAL C 1 6   ? 3.493   -29.904 11.042  1.00 24.68  ? 7   VAL C CG1   1 
ATOM   2568  C CG2   . VAL C 1 6   ? 4.906   -31.971 11.143  1.00 28.43  ? 7   VAL C CG2   1 
ATOM   2569  N N     . GLY C 1 7   ? 6.734   -31.052 8.113   1.00 27.66  ? 8   GLY C N     1 
ATOM   2570  C CA    . GLY C 1 7   ? 7.951   -31.733 7.714   1.00 27.18  ? 8   GLY C CA    1 
ATOM   2571  C C     . GLY C 1 7   ? 8.932   -31.798 8.879   1.00 31.29  ? 8   GLY C C     1 
ATOM   2572  O O     . GLY C 1 7   ? 8.968   -30.896 9.713   1.00 30.29  ? 8   GLY C O     1 
ATOM   2573  N N     . THR C 1 8   ? 9.718   -32.877 8.929   1.00 30.63  ? 9   THR C N     1 
ATOM   2574  C CA    . THR C 1 8   ? 10.667  -33.081 10.009  1.00 34.13  ? 9   THR C CA    1 
ATOM   2575  C C     . THR C 1 8   ? 12.081  -32.868 9.481   1.00 29.95  ? 9   THR C C     1 
ATOM   2576  O O     . THR C 1 8   ? 13.055  -33.049 10.208  1.00 29.29  ? 9   THR C O     1 
ATOM   2577  C CB    . THR C 1 8   ? 10.481  -34.482 10.590  1.00 35.07  ? 9   THR C CB    1 
ATOM   2578  O OG1   . THR C 1 8   ? 10.690  -35.371 9.498   1.00 33.09  ? 9   THR C OG1   1 
ATOM   2579  C CG2   . THR C 1 8   ? 9.098   -34.686 11.181  1.00 35.43  ? 9   THR C CG2   1 
ATOM   2580  N N     . GLY C 1 9   ? 12.175  -32.463 8.211   1.00 27.90  ? 10  GLY C N     1 
ATOM   2581  C CA    . GLY C 1 9   ? 13.459  -32.304 7.551   1.00 28.44  ? 10  GLY C CA    1 
ATOM   2582  C C     . GLY C 1 9   ? 14.098  -33.662 7.282   1.00 27.45  ? 10  GLY C C     1 
ATOM   2583  O O     . GLY C 1 9   ? 13.449  -34.695 7.429   1.00 40.68  ? 10  GLY C O     1 
ATOM   2584  N N     . LEU C 1 10  ? 15.375  -33.645 6.891   1.00 27.21  ? 11  LEU C N     1 
ATOM   2585  C CA    . LEU C 1 10  ? 16.100  -34.867 6.588   1.00 26.26  ? 11  LEU C CA    1 
ATOM   2586  C C     . LEU C 1 10  ? 16.898  -35.310 7.812   1.00 24.26  ? 11  LEU C C     1 
ATOM   2587  O O     . LEU C 1 10  ? 16.927  -36.494 8.140   1.00 26.06  ? 11  LEU C O     1 
ATOM   2588  C CB    . LEU C 1 10  ? 17.001  -34.653 5.372   1.00 25.61  ? 11  LEU C CB    1 
ATOM   2589  C CG    . LEU C 1 10  ? 16.293  -34.613 4.013   1.00 25.75  ? 11  LEU C CG    1 
ATOM   2590  C CD1   . LEU C 1 10  ? 15.530  -35.904 3.775   1.00 27.11  ? 11  LEU C CD1   1 
ATOM   2591  C CD2   . LEU C 1 10  ? 15.367  -33.416 3.900   1.00 27.69  ? 11  LEU C CD2   1 
ATOM   2592  N N     . GLN C 1 11  ? 17.542  -34.346 8.479   1.00 24.65  ? 12  GLN C N     1 
ATOM   2593  C CA    . GLN C 1 11  ? 18.378  -34.637 9.634   1.00 27.93  ? 12  GLN C CA    1 
ATOM   2594  C C     . GLN C 1 11  ? 17.503  -34.996 10.832  1.00 29.69  ? 12  GLN C C     1 
ATOM   2595  O O     . GLN C 1 11  ? 16.353  -34.572 10.926  1.00 35.63  ? 12  GLN C O     1 
ATOM   2596  C CB    . GLN C 1 11  ? 19.306  -33.467 9.961   1.00 28.23  ? 12  GLN C CB    1 
ATOM   2597  C CG    . GLN C 1 11  ? 20.657  -33.533 9.255   1.00 28.82  ? 12  GLN C CG    1 
ATOM   2598  C CD    . GLN C 1 11  ? 21.519  -34.683 9.731   1.00 28.41  ? 12  GLN C CD    1 
ATOM   2599  O OE1   . GLN C 1 11  ? 21.077  -35.548 10.496  1.00 24.18  ? 12  GLN C OE1   1 
ATOM   2600  N NE2   . GLN C 1 11  ? 22.764  -34.708 9.279   1.00 32.36  ? 12  GLN C NE2   1 
ATOM   2601  N N     . LEU C 1 12  ? 18.083  -35.776 11.748  1.00 29.79  ? 13  LEU C N     1 
ATOM   2602  C CA    . LEU C 1 12  ? 17.374  -36.288 12.907  1.00 28.11  ? 13  LEU C CA    1 
ATOM   2603  C C     . LEU C 1 12  ? 17.219  -35.194 13.960  1.00 25.83  ? 13  LEU C C     1 
ATOM   2604  O O     . LEU C 1 12  ? 18.207  -34.648 14.446  1.00 27.72  ? 13  LEU C O     1 
ATOM   2605  C CB    . LEU C 1 12  ? 18.154  -37.482 13.455  1.00 27.08  ? 13  LEU C CB    1 
ATOM   2606  C CG    . LEU C 1 12  ? 17.675  -38.043 14.797  1.00 24.01  ? 13  LEU C CG    1 
ATOM   2607  C CD1   . LEU C 1 12  ? 16.347  -38.763 14.649  1.00 27.60  ? 13  LEU C CD1   1 
ATOM   2608  C CD2   . LEU C 1 12  ? 18.725  -38.962 15.395  1.00 22.57  ? 13  LEU C CD2   1 
ATOM   2609  N N     . ALA C 1 13  ? 15.961  -34.865 14.276  1.00 26.62  ? 14  ALA C N     1 
ATOM   2610  C CA    . ALA C 1 13  ? 15.618  -34.142 15.491  1.00 28.20  ? 14  ALA C CA    1 
ATOM   2611  C C     . ALA C 1 13  ? 15.776  -32.632 15.312  1.00 28.93  ? 14  ALA C C     1 
ATOM   2612  O O     . ALA C 1 13  ? 14.921  -31.867 15.754  1.00 31.37  ? 14  ALA C O     1 
ATOM   2613  C CB    . ALA C 1 13  ? 16.467  -34.650 16.640  1.00 26.48  ? 14  ALA C CB    1 
ATOM   2614  N N     . GLY C 1 14  ? 16.871  -32.210 14.672  1.00 27.05  ? 15  GLY C N     1 
ATOM   2615  C CA    . GLY C 1 14  ? 17.300  -30.821 14.740  1.00 24.18  ? 15  GLY C CA    1 
ATOM   2616  C C     . GLY C 1 14  ? 16.952  -30.020 13.486  1.00 26.06  ? 15  GLY C C     1 
ATOM   2617  O O     . GLY C 1 14  ? 17.198  -28.816 13.438  1.00 21.77  ? 15  GLY C O     1 
ATOM   2618  N N     . GLN C 1 15  ? 16.376  -30.678 12.476  1.00 24.83  ? 16  GLN C N     1 
ATOM   2619  C CA    . GLN C 1 15  ? 16.131  -30.012 11.206  1.00 29.38  ? 16  GLN C CA    1 
ATOM   2620  C C     . GLN C 1 15  ? 14.645  -29.689 11.055  1.00 29.75  ? 16  GLN C C     1 
ATOM   2621  O O     . GLN C 1 15  ? 14.223  -29.179 10.020  1.00 34.66  ? 16  GLN C O     1 
ATOM   2622  C CB    . GLN C 1 15  ? 16.652  -30.848 10.038  1.00 31.41  ? 16  GLN C CB    1 
ATOM   2623  C CG    . GLN C 1 15  ? 16.840  -30.054 8.750   1.00 33.71  ? 16  GLN C CG    1 
ATOM   2624  C CD    . GLN C 1 15  ? 17.772  -30.730 7.769   1.00 36.03  ? 16  GLN C CD    1 
ATOM   2625  O OE1   . GLN C 1 15  ? 17.503  -31.830 7.274   1.00 31.40  ? 16  GLN C OE1   1 
ATOM   2626  N NE2   . GLN C 1 15  ? 18.887  -30.073 7.481   1.00 34.71  ? 16  GLN C NE2   1 
ATOM   2627  N N     . ILE C 1 16  ? 13.861  -29.977 12.100  1.00 26.68  ? 17  ILE C N     1 
ATOM   2628  C CA    . ILE C 1 16  ? 12.454  -29.612 12.115  1.00 26.30  ? 17  ILE C CA    1 
ATOM   2629  C C     . ILE C 1 16  ? 12.335  -28.171 12.604  1.00 24.82  ? 17  ILE C C     1 
ATOM   2630  O O     . ILE C 1 16  ? 13.191  -27.689 13.344  1.00 20.61  ? 17  ILE C O     1 
ATOM   2631  C CB    . ILE C 1 16  ? 11.637  -30.585 12.987  1.00 26.98  ? 17  ILE C CB    1 
ATOM   2632  C CG1   . ILE C 1 16  ? 10.134  -30.322 12.870  1.00 26.21  ? 17  ILE C CG1   1 
ATOM   2633  C CG2   . ILE C 1 16  ? 12.107  -30.547 14.442  1.00 25.92  ? 17  ILE C CG2   1 
ATOM   2634  C CD1   . ILE C 1 16  ? 9.270   -31.314 13.628  1.00 26.21  ? 17  ILE C CD1   1 
ATOM   2635  N N     . SER C 1 17  ? 11.274  -27.484 12.165  1.00 23.28  ? 18  SER C N     1 
ATOM   2636  C CA    . SER C 1 17  ? 11.022  -26.120 12.598  1.00 28.89  ? 18  SER C CA    1 
ATOM   2637  C C     . SER C 1 17  ? 10.577  -26.129 14.058  1.00 31.06  ? 18  SER C C     1 
ATOM   2638  O O     . SER C 1 17  ? 10.159  -27.162 14.577  1.00 26.52  ? 18  SER C O     1 
ATOM   2639  C CB    . SER C 1 17  ? 10.005  -25.437 11.715  1.00 29.18  ? 18  SER C CB    1 
ATOM   2640  O OG    . SER C 1 17  ? 8.704   -25.977 11.913  1.00 28.47  ? 18  SER C OG    1 
ATOM   2641  N N     . VAL C 1 18  ? 10.691  -24.970 14.714  1.00 29.84  ? 19  VAL C N     1 
ATOM   2642  C CA    . VAL C 1 18  ? 10.339  -24.848 16.118  1.00 30.33  ? 19  VAL C CA    1 
ATOM   2643  C C     . VAL C 1 18  ? 8.830   -25.019 16.263  1.00 28.24  ? 19  VAL C C     1 
ATOM   2644  O O     . VAL C 1 18  ? 8.360   -25.633 17.217  1.00 23.94  ? 19  VAL C O     1 
ATOM   2645  C CB    . VAL C 1 18  ? 10.807  -23.502 16.705  1.00 29.59  ? 19  VAL C CB    1 
ATOM   2646  C CG1   . VAL C 1 18  ? 10.287  -23.291 18.121  1.00 28.95  ? 19  VAL C CG1   1 
ATOM   2647  C CG2   . VAL C 1 18  ? 12.323  -23.363 16.663  1.00 31.11  ? 19  VAL C CG2   1 
ATOM   2648  N N     . LEU C 1 19  ? 8.083   -24.474 15.295  1.00 26.14  ? 20  LEU C N     1 
ATOM   2649  C CA    . LEU C 1 19  ? 6.631   -24.488 15.341  1.00 29.01  ? 20  LEU C CA    1 
ATOM   2650  C C     . LEU C 1 19  ? 6.123   -25.898 15.052  1.00 28.68  ? 20  LEU C C     1 
ATOM   2651  O O     . LEU C 1 19  ? 5.238   -26.396 15.742  1.00 30.24  ? 20  LEU C O     1 
ATOM   2652  C CB    . LEU C 1 19  ? 6.068   -23.476 14.345  1.00 28.45  ? 20  LEU C CB    1 
ATOM   2653  C CG    . LEU C 1 19  ? 4.542   -23.338 14.320  1.00 32.29  ? 20  LEU C CG    1 
ATOM   2654  C CD1   . LEU C 1 19  ? 4.016   -22.854 15.662  1.00 34.02  ? 20  LEU C CD1   1 
ATOM   2655  C CD2   . LEU C 1 19  ? 4.094   -22.411 13.205  1.00 32.13  ? 20  LEU C CD2   1 
ATOM   2656  N N     . SER C 1 20  ? 6.696   -26.530 14.022  1.00 28.82  ? 21  SER C N     1 
ATOM   2657  C CA    . SER C 1 20  ? 6.249   -27.841 13.580  1.00 27.98  ? 21  SER C CA    1 
ATOM   2658  C C     . SER C 1 20  ? 6.439   -28.863 14.698  1.00 27.94  ? 21  SER C C     1 
ATOM   2659  O O     . SER C 1 20  ? 5.591   -29.728 14.901  1.00 32.24  ? 21  SER C O     1 
ATOM   2660  C CB    . SER C 1 20  ? 6.964   -28.261 12.322  1.00 27.37  ? 21  SER C CB    1 
ATOM   2661  O OG    . SER C 1 20  ? 6.667   -27.373 11.254  1.00 26.05  ? 21  SER C OG    1 
ATOM   2662  N N     . ARG C 1 21  ? 7.564   -28.754 15.412  1.00 26.98  ? 22  ARG C N     1 
ATOM   2663  C CA    . ARG C 1 21  ? 7.844   -29.627 16.539  1.00 26.94  ? 22  ARG C CA    1 
ATOM   2664  C C     . ARG C 1 21  ? 6.736   -29.460 17.573  1.00 25.58  ? 22  ARG C C     1 
ATOM   2665  O O     . ARG C 1 21  ? 6.231   -30.438 18.119  1.00 22.22  ? 22  ARG C O     1 
ATOM   2666  C CB    . ARG C 1 21  ? 9.216   -29.298 17.138  1.00 31.86  ? 22  ARG C CB    1 
ATOM   2667  C CG    . ARG C 1 21  ? 9.661   -30.223 18.263  1.00 32.57  ? 22  ARG C CG    1 
ATOM   2668  C CD    . ARG C 1 21  ? 11.019  -29.820 18.820  1.00 34.03  ? 22  ARG C CD    1 
ATOM   2669  N NE    . ARG C 1 21  ? 11.562  -30.804 19.762  1.00 34.56  ? 22  ARG C NE    1 
ATOM   2670  C CZ    . ARG C 1 21  ? 11.059  -31.073 20.960  1.00 38.03  ? 22  ARG C CZ    1 
ATOM   2671  N NH1   . ARG C 1 21  ? 10.015  -30.400 21.408  1.00 44.21  ? 22  ARG C NH1   1 
ATOM   2672  N NH2   . ARG C 1 21  ? 11.613  -32.007 21.714  1.00 37.64  ? 22  ARG C NH2   1 
ATOM   2673  N N     . SER C 1 22  ? 6.358   -28.200 17.812  1.00 27.36  ? 23  SER C N     1 
ATOM   2674  C CA    . SER C 1 22  ? 5.326   -27.862 18.776  1.00 26.08  ? 23  SER C CA    1 
ATOM   2675  C C     . SER C 1 22  ? 4.013   -28.548 18.403  1.00 26.83  ? 23  SER C C     1 
ATOM   2676  O O     . SER C 1 22  ? 3.296   -29.035 19.276  1.00 27.28  ? 23  SER C O     1 
ATOM   2677  C CB    . SER C 1 22  ? 5.156   -26.365 18.874  1.00 27.83  ? 23  SER C CB    1 
ATOM   2678  O OG    . SER C 1 22  ? 4.247   -26.016 19.909  1.00 26.27  ? 23  SER C OG    1 
ATOM   2679  N N     . TYR C 1 23  ? 3.707   -28.579 17.101  1.00 24.52  ? 24  TYR C N     1 
ATOM   2680  C CA    . TYR C 1 23  ? 2.471   -29.176 16.616  1.00 22.67  ? 24  TYR C CA    1 
ATOM   2681  C C     . TYR C 1 23  ? 2.456   -30.667 16.944  1.00 21.40  ? 24  TYR C C     1 
ATOM   2682  O O     . TYR C 1 23  ? 1.432   -31.202 17.360  1.00 22.00  ? 24  TYR C O     1 
ATOM   2683  C CB    . TYR C 1 23  ? 2.289   -28.960 15.110  1.00 24.01  ? 24  TYR C CB    1 
ATOM   2684  C CG    . TYR C 1 23  ? 1.603   -27.656 14.727  1.00 25.40  ? 24  TYR C CG    1 
ATOM   2685  C CD1   . TYR C 1 23  ? 0.245   -27.469 14.956  1.00 28.05  ? 24  TYR C CD1   1 
ATOM   2686  C CD2   . TYR C 1 23  ? 2.298   -26.634 14.094  1.00 27.48  ? 24  TYR C CD2   1 
ATOM   2687  C CE1   . TYR C 1 23  ? -0.393  -26.293 14.599  1.00 29.26  ? 24  TYR C CE1   1 
ATOM   2688  C CE2   . TYR C 1 23  ? 1.672   -25.455 13.726  1.00 28.40  ? 24  TYR C CE2   1 
ATOM   2689  C CZ    . TYR C 1 23  ? 0.323   -25.283 13.980  1.00 32.41  ? 24  TYR C CZ    1 
ATOM   2690  O OH    . TYR C 1 23  ? -0.298  -24.122 13.620  1.00 39.14  ? 24  TYR C OH    1 
ATOM   2691  N N     . ILE C 1 24  ? 3.594   -31.332 16.728  1.00 21.28  ? 25  ILE C N     1 
ATOM   2692  C CA    . ILE C 1 24  ? 3.711   -32.758 16.981  1.00 23.52  ? 25  ILE C CA    1 
ATOM   2693  C C     . ILE C 1 24  ? 3.498   -33.020 18.470  1.00 25.73  ? 25  ILE C C     1 
ATOM   2694  O O     . ILE C 1 24  ? 2.913   -34.031 18.852  1.00 26.64  ? 25  ILE C O     1 
ATOM   2695  C CB    . ILE C 1 24  ? 5.074   -33.288 16.497  1.00 22.74  ? 25  ILE C CB    1 
ATOM   2696  C CG1   . ILE C 1 24  ? 5.205   -33.194 14.976  1.00 20.68  ? 25  ILE C CG1   1 
ATOM   2697  C CG2   . ILE C 1 24  ? 5.319   -34.712 16.997  1.00 21.92  ? 25  ILE C CG2   1 
ATOM   2698  C CD1   . ILE C 1 24  ? 6.541   -33.673 14.438  1.00 20.43  ? 25  ILE C CD1   1 
ATOM   2699  N N     . GLU C 1 25  ? 3.973   -32.087 19.299  1.00 25.76  ? 26  GLU C N     1 
ATOM   2700  C CA    . GLU C 1 25  ? 3.972   -32.263 20.741  1.00 29.21  ? 26  GLU C CA    1 
ATOM   2701  C C     . GLU C 1 25  ? 2.541   -32.214 21.275  1.00 29.40  ? 26  GLU C C     1 
ATOM   2702  O O     . GLU C 1 25  ? 2.187   -32.974 22.173  1.00 28.43  ? 26  GLU C O     1 
ATOM   2703  C CB    . GLU C 1 25  ? 4.832   -31.182 21.397  1.00 30.83  ? 26  GLU C CB    1 
ATOM   2704  C CG    . GLU C 1 25  ? 4.957   -31.339 22.909  1.00 34.00  ? 26  GLU C CG    1 
ATOM   2705  C CD    . GLU C 1 25  ? 5.732   -30.222 23.585  1.00 36.77  ? 26  GLU C CD    1 
ATOM   2706  O OE1   . GLU C 1 25  ? 6.153   -29.283 22.878  1.00 39.79  ? 26  GLU C OE1   1 
ATOM   2707  O OE2   . GLU C 1 25  ? 5.913   -30.290 24.819  1.00 43.35  ? 26  GLU C OE2   1 
ATOM   2708  N N     . HIS C 1 26  ? 1.727   -31.315 20.712  1.00 29.34  ? 27  HIS C N     1 
ATOM   2709  C CA    . HIS C 1 26  ? 0.396   -31.053 21.239  1.00 30.84  ? 27  HIS C CA    1 
ATOM   2710  C C     . HIS C 1 26  ? -0.664  -31.773 20.410  1.00 31.40  ? 27  HIS C C     1 
ATOM   2711  O O     . HIS C 1 26  ? -1.857  -31.560 20.612  1.00 30.27  ? 27  HIS C O     1 
ATOM   2712  C CB    . HIS C 1 26  ? 0.118   -29.546 21.293  1.00 31.79  ? 27  HIS C CB    1 
ATOM   2713  C CG    . HIS C 1 26  ? 0.950   -28.810 22.291  1.00 32.92  ? 27  HIS C CG    1 
ATOM   2714  N ND1   . HIS C 1 26  ? 2.022   -28.017 21.942  1.00 36.93  ? 27  HIS C ND1   1 
ATOM   2715  C CD2   . HIS C 1 26  ? 0.841   -28.718 23.624  1.00 34.57  ? 27  HIS C CD2   1 
ATOM   2716  C CE1   . HIS C 1 26  ? 2.547   -27.485 23.037  1.00 34.58  ? 27  HIS C CE1   1 
ATOM   2717  N NE2   . HIS C 1 26  ? 1.847   -27.900 24.070  1.00 35.24  ? 27  HIS C NE2   1 
ATOM   2718  N N     . ALA C 1 27  ? -0.221  -32.628 19.483  1.00 31.77  ? 28  ALA C N     1 
ATOM   2719  C CA    . ALA C 1 27  ? -1.137  -33.385 18.645  1.00 32.46  ? 28  ALA C CA    1 
ATOM   2720  C C     . ALA C 1 27  ? -1.788  -34.497 19.464  1.00 29.55  ? 28  ALA C C     1 
ATOM   2721  O O     . ALA C 1 27  ? -1.163  -35.060 20.359  1.00 31.58  ? 28  ALA C O     1 
ATOM   2722  C CB    . ALA C 1 27  ? -0.403  -33.941 17.446  1.00 31.74  ? 28  ALA C CB    1 
ATOM   2723  N N     . ASP C 1 28  ? -3.053  -34.795 19.150  1.00 32.10  ? 29  ASP C N     1 
ATOM   2724  C CA    . ASP C 1 28  ? -3.757  -35.912 19.759  1.00 32.16  ? 29  ASP C CA    1 
ATOM   2725  C C     . ASP C 1 28  ? -3.184  -37.215 19.216  1.00 33.50  ? 29  ASP C C     1 
ATOM   2726  O O     . ASP C 1 28  ? -3.005  -38.180 19.957  1.00 32.60  ? 29  ASP C O     1 
ATOM   2727  C CB    . ASP C 1 28  ? -5.253  -35.850 19.487  1.00 35.42  ? 29  ASP C CB    1 
ATOM   2728  C CG    . ASP C 1 28  ? -5.980  -34.645 20.064  1.00 38.22  ? 29  ASP C CG    1 
ATOM   2729  O OD1   . ASP C 1 28  ? -5.323  -33.841 20.760  1.00 45.67  ? 29  ASP C OD1   1 
ATOM   2730  O OD2   . ASP C 1 28  ? -7.195  -34.516 19.805  1.00 37.03  ? 29  ASP C OD2   1 
ATOM   2731  N N     . ILE C 1 29  ? -2.912  -37.223 17.907  1.00 31.27  ? 30  ILE C N     1 
ATOM   2732  C CA    . ILE C 1 29  ? -2.418  -38.403 17.218  1.00 31.05  ? 30  ILE C CA    1 
ATOM   2733  C C     . ILE C 1 29  ? -1.500  -37.948 16.088  1.00 31.00  ? 30  ILE C C     1 
ATOM   2734  O O     . ILE C 1 29  ? -1.713  -36.890 15.499  1.00 30.98  ? 30  ILE C O     1 
ATOM   2735  C CB    . ILE C 1 29  ? -3.590  -39.256 16.696  1.00 30.15  ? 30  ILE C CB    1 
ATOM   2736  C CG1   . ILE C 1 29  ? -3.130  -40.644 16.251  1.00 32.35  ? 30  ILE C CG1   1 
ATOM   2737  C CG2   . ILE C 1 29  ? -4.341  -38.524 15.583  1.00 30.75  ? 30  ILE C CG2   1 
ATOM   2738  C CD1   . ILE C 1 29  ? -4.261  -41.555 15.808  1.00 33.87  ? 30  ILE C CD1   1 
ATOM   2739  N N     . VAL C 1 30  ? -0.479  -38.760 15.796  1.00 27.64  ? 31  VAL C N     1 
ATOM   2740  C CA    . VAL C 1 30  ? 0.496   -38.417 14.776  1.00 26.70  ? 31  VAL C CA    1 
ATOM   2741  C C     . VAL C 1 30  ? 0.633   -39.583 13.804  1.00 24.98  ? 31  VAL C C     1 
ATOM   2742  O O     . VAL C 1 30  ? 0.863   -40.718 14.214  1.00 24.90  ? 31  VAL C O     1 
ATOM   2743  C CB    . VAL C 1 30  ? 1.861   -38.051 15.389  1.00 26.24  ? 31  VAL C CB    1 
ATOM   2744  C CG1   . VAL C 1 30  ? 2.887   -37.709 14.315  1.00 26.34  ? 31  VAL C CG1   1 
ATOM   2745  C CG2   . VAL C 1 30  ? 1.742   -36.917 16.400  1.00 26.58  ? 31  VAL C CG2   1 
ATOM   2746  N N     . PHE C 1 31  ? 0.481   -39.278 12.512  1.00 25.92  ? 32  PHE C N     1 
ATOM   2747  C CA    . PHE C 1 31  ? 0.791   -40.221 11.452  1.00 28.70  ? 32  PHE C CA    1 
ATOM   2748  C C     . PHE C 1 31  ? 2.177   -39.884 10.916  1.00 31.17  ? 32  PHE C C     1 
ATOM   2749  O O     . PHE C 1 31  ? 2.432   -38.753 10.506  1.00 35.30  ? 32  PHE C O     1 
ATOM   2750  C CB    . PHE C 1 31  ? -0.290  -40.176 10.368  1.00 29.14  ? 32  PHE C CB    1 
ATOM   2751  C CG    . PHE C 1 31  ? -1.650  -40.689 10.822  1.00 29.71  ? 32  PHE C CG    1 
ATOM   2752  C CD1   . PHE C 1 31  ? -2.534  -39.860 11.504  1.00 30.09  ? 32  PHE C CD1   1 
ATOM   2753  C CD2   . PHE C 1 31  ? -2.043  -41.998 10.562  1.00 28.88  ? 32  PHE C CD2   1 
ATOM   2754  C CE1   . PHE C 1 31  ? -3.771  -40.331 11.915  1.00 30.98  ? 32  PHE C CE1   1 
ATOM   2755  C CE2   . PHE C 1 31  ? -3.280  -42.461 10.976  1.00 28.22  ? 32  PHE C CE2   1 
ATOM   2756  C CZ    . PHE C 1 31  ? -4.141  -41.628 11.651  1.00 29.19  ? 32  PHE C CZ    1 
ATOM   2757  N N     . SER C 1 32  ? 3.068   -40.878 10.935  1.00 32.26  ? 33  SER C N     1 
ATOM   2758  C CA    . SER C 1 32  ? 4.475   -40.647 10.659  1.00 32.75  ? 33  SER C CA    1 
ATOM   2759  C C     . SER C 1 32  ? 4.894   -41.360 9.377   1.00 30.79  ? 33  SER C C     1 
ATOM   2760  O O     . SER C 1 32  ? 4.330   -42.390 9.012   1.00 31.52  ? 33  SER C O     1 
ATOM   2761  C CB    . SER C 1 32  ? 5.324   -41.086 11.824  1.00 28.17  ? 33  SER C CB    1 
ATOM   2762  O OG    . SER C 1 32  ? 5.156   -42.474 12.079  1.00 29.47  ? 33  SER C OG    1 
ATOM   2763  N N     . LEU C 1 33  ? 5.885   -40.777 8.699   1.00 33.04  ? 34  LEU C N     1 
ATOM   2764  C CA    . LEU C 1 33  ? 6.574   -41.429 7.599   1.00 37.80  ? 34  LEU C CA    1 
ATOM   2765  C C     . LEU C 1 33  ? 8.024   -40.953 7.611   1.00 37.20  ? 34  LEU C C     1 
ATOM   2766  O O     . LEU C 1 33  ? 8.384   -40.023 6.891   1.00 39.61  ? 34  LEU C O     1 
ATOM   2767  C CB    . LEU C 1 33  ? 5.888   -41.123 6.269   1.00 40.61  ? 34  LEU C CB    1 
ATOM   2768  C CG    . LEU C 1 33  ? 6.202   -42.086 5.119   1.00 42.46  ? 34  LEU C CG    1 
ATOM   2769  C CD1   . LEU C 1 33  ? 5.620   -41.577 3.811   1.00 47.38  ? 34  LEU C CD1   1 
ATOM   2770  C CD2   . LEU C 1 33  ? 7.696   -42.326 4.986   1.00 41.91  ? 34  LEU C CD2   1 
ATOM   2771  N N     . LEU C 1 34  ? 8.839   -41.590 8.458   1.00 39.33  ? 35  LEU C N     1 
ATOM   2772  C CA    . LEU C 1 34  ? 10.181  -41.113 8.741   1.00 46.71  ? 35  LEU C CA    1 
ATOM   2773  C C     . LEU C 1 34  ? 11.209  -42.021 8.071   1.00 48.62  ? 35  LEU C C     1 
ATOM   2774  O O     . LEU C 1 34  ? 10.919  -43.172 7.753   1.00 46.22  ? 35  LEU C O     1 
ATOM   2775  C CB    . LEU C 1 34  ? 10.379  -41.048 10.254  1.00 50.66  ? 35  LEU C CB    1 
ATOM   2776  C CG    . LEU C 1 34  ? 9.367   -40.190 11.020  1.00 51.63  ? 35  LEU C CG    1 
ATOM   2777  C CD1   . LEU C 1 34  ? 9.723   -40.114 12.493  1.00 50.11  ? 35  LEU C CD1   1 
ATOM   2778  C CD2   . LEU C 1 34  ? 9.266   -38.798 10.418  1.00 50.62  ? 35  LEU C CD2   1 
ATOM   2779  N N     . PRO C 1 35  ? 12.447  -41.523 7.848   1.00 48.66  ? 36  PRO C N     1 
ATOM   2780  C CA    . PRO C 1 35  ? 13.460  -42.267 7.097   1.00 47.93  ? 36  PRO C CA    1 
ATOM   2781  C C     . PRO C 1 35  ? 13.957  -43.529 7.800   1.00 45.32  ? 36  PRO C C     1 
ATOM   2782  O O     . PRO C 1 35  ? 14.201  -44.543 7.151   1.00 49.31  ? 36  PRO C O     1 
ATOM   2783  C CB    . PRO C 1 35  ? 14.598  -41.234 6.902   1.00 49.30  ? 36  PRO C CB    1 
ATOM   2784  C CG    . PRO C 1 35  ? 13.963  -39.891 7.222   1.00 51.61  ? 36  PRO C CG    1 
ATOM   2785  C CD    . PRO C 1 35  ? 12.914  -40.198 8.271   1.00 48.02  ? 36  PRO C CD    1 
ATOM   2786  N N     . ASP C 1 36  ? 14.108  -43.454 9.128   1.00 40.85  ? 37  ASP C N     1 
ATOM   2787  C CA    . ASP C 1 36  ? 14.745  -44.523 9.881   1.00 40.88  ? 37  ASP C CA    1 
ATOM   2788  C C     . ASP C 1 36  ? 14.083  -44.676 11.248  1.00 38.52  ? 37  ASP C C     1 
ATOM   2789  O O     . ASP C 1 36  ? 13.117  -43.984 11.562  1.00 36.81  ? 37  ASP C O     1 
ATOM   2790  C CB    . ASP C 1 36  ? 16.240  -44.276 10.010  1.00 43.75  ? 37  ASP C CB    1 
ATOM   2791  C CG    . ASP C 1 36  ? 16.627  -42.913 10.566  1.00 45.14  ? 37  ASP C CG    1 
ATOM   2792  O OD1   . ASP C 1 36  ? 16.231  -42.613 11.712  1.00 43.82  ? 37  ASP C OD1   1 
ATOM   2793  O OD2   . ASP C 1 36  ? 17.315  -42.160 9.846   1.00 51.86  ? 37  ASP C OD2   1 
ATOM   2794  N N     . GLY C 1 37  ? 14.633  -45.592 12.054  1.00 38.41  ? 38  GLY C N     1 
ATOM   2795  C CA    . GLY C 1 37  ? 14.085  -45.918 13.360  1.00 33.58  ? 38  GLY C CA    1 
ATOM   2796  C C     . GLY C 1 37  ? 14.624  -44.993 14.448  1.00 32.57  ? 38  GLY C C     1 
ATOM   2797  O O     . GLY C 1 37  ? 14.077  -44.940 15.549  1.00 23.61  ? 38  GLY C O     1 
ATOM   2798  N N     . PHE C 1 38  ? 15.710  -44.279 14.135  1.00 31.62  ? 39  PHE C N     1 
ATOM   2799  C CA    . PHE C 1 38  ? 16.248  -43.279 15.043  1.00 32.04  ? 39  PHE C CA    1 
ATOM   2800  C C     . PHE C 1 38  ? 15.287  -42.096 15.083  1.00 30.56  ? 39  PHE C C     1 
ATOM   2801  O O     . PHE C 1 38  ? 15.005  -41.552 16.148  1.00 32.03  ? 39  PHE C O     1 
ATOM   2802  C CB    . PHE C 1 38  ? 17.657  -42.839 14.631  1.00 32.85  ? 39  PHE C CB    1 
ATOM   2803  C CG    . PHE C 1 38  ? 18.739  -43.888 14.850  1.00 33.82  ? 39  PHE C CG    1 
ATOM   2804  C CD1   . PHE C 1 38  ? 19.233  -44.145 16.124  1.00 34.90  ? 39  PHE C CD1   1 
ATOM   2805  C CD2   . PHE C 1 38  ? 19.281  -44.590 13.780  1.00 31.55  ? 39  PHE C CD2   1 
ATOM   2806  C CE1   . PHE C 1 38  ? 20.221  -45.096 16.322  1.00 34.53  ? 39  PHE C CE1   1 
ATOM   2807  C CE2   . PHE C 1 38  ? 20.271  -45.538 13.985  1.00 31.24  ? 39  PHE C CE2   1 
ATOM   2808  C CZ    . PHE C 1 38  ? 20.738  -45.788 15.253  1.00 32.86  ? 39  PHE C CZ    1 
ATOM   2809  N N     . SER C 1 39  ? 14.785  -41.719 13.903  1.00 31.39  ? 40  SER C N     1 
ATOM   2810  C CA    . SER C 1 39  ? 13.827  -40.635 13.779  1.00 35.31  ? 40  SER C CA    1 
ATOM   2811  C C     . SER C 1 39  ? 12.477  -41.078 14.334  1.00 33.59  ? 40  SER C C     1 
ATOM   2812  O O     . SER C 1 39  ? 11.678  -40.253 14.771  1.00 33.13  ? 40  SER C O     1 
ATOM   2813  C CB    . SER C 1 39  ? 13.710  -40.181 12.344  1.00 37.00  ? 40  SER C CB    1 
ATOM   2814  O OG    . SER C 1 39  ? 12.798  -39.099 12.222  1.00 44.95  ? 40  SER C OG    1 
ATOM   2815  N N     . GLN C 1 40  ? 12.244  -42.395 14.318  1.00 33.36  ? 41  GLN C N     1 
ATOM   2816  C CA    . GLN C 1 40  ? 10.987  -42.965 14.772  1.00 32.30  ? 41  GLN C CA    1 
ATOM   2817  C C     . GLN C 1 40  ? 10.937  -42.916 16.298  1.00 30.13  ? 41  GLN C C     1 
ATOM   2818  O O     . GLN C 1 40  ? 9.904   -42.588 16.877  1.00 28.22  ? 41  GLN C O     1 
ATOM   2819  C CB    . GLN C 1 40  ? 10.840  -44.397 14.254  1.00 34.22  ? 41  GLN C CB    1 
ATOM   2820  C CG    . GLN C 1 40  ? 9.412   -44.931 14.294  1.00 34.44  ? 41  GLN C CG    1 
ATOM   2821  C CD    . GLN C 1 40  ? 8.468   -44.167 13.390  1.00 36.89  ? 41  GLN C CD    1 
ATOM   2822  O OE1   . GLN C 1 40  ? 8.740   -43.956 12.203  1.00 35.15  ? 41  GLN C OE1   1 
ATOM   2823  N NE2   . GLN C 1 40  ? 7.346   -43.736 13.948  1.00 39.58  ? 41  GLN C NE2   1 
ATOM   2824  N N     A ARG C 1 41  ? 12.064  -43.254 16.934  0.50 29.98  ? 42  ARG C N     1 
ATOM   2825  N N     B ARG C 1 41  ? 12.065  -43.243 16.937  0.50 30.76  ? 42  ARG C N     1 
ATOM   2826  C CA    A ARG C 1 41  ? 12.177  -43.200 18.383  0.50 32.93  ? 42  ARG C CA    1 
ATOM   2827  C CA    B ARG C 1 41  ? 12.163  -43.199 18.387  0.50 34.40  ? 42  ARG C CA    1 
ATOM   2828  C C     A ARG C 1 41  ? 12.017  -41.755 18.848  0.50 32.44  ? 42  ARG C C     1 
ATOM   2829  C C     B ARG C 1 41  ? 12.029  -41.754 18.861  0.50 33.16  ? 42  ARG C C     1 
ATOM   2830  O O     A ARG C 1 41  ? 11.267  -41.478 19.781  0.50 34.22  ? 42  ARG C O     1 
ATOM   2831  O O     B ARG C 1 41  ? 11.306  -41.476 19.816  0.50 34.76  ? 42  ARG C O     1 
ATOM   2832  C CB    A ARG C 1 41  ? 13.516  -43.767 18.867  0.50 32.57  ? 42  ARG C CB    1 
ATOM   2833  C CB    B ARG C 1 41  ? 13.475  -43.822 18.879  0.50 35.23  ? 42  ARG C CB    1 
ATOM   2834  C CG    A ARG C 1 41  ? 13.603  -45.287 18.864  0.50 35.81  ? 42  ARG C CG    1 
ATOM   2835  C CG    B ARG C 1 41  ? 13.452  -45.342 18.937  0.50 40.03  ? 42  ARG C CG    1 
ATOM   2836  C CD    A ARG C 1 41  ? 14.831  -45.781 19.618  0.50 36.65  ? 42  ARG C CD    1 
ATOM   2837  C CD    B ARG C 1 41  ? 14.677  -45.917 19.632  0.50 41.66  ? 42  ARG C CD    1 
ATOM   2838  N NE    A ARG C 1 41  ? 14.820  -47.233 19.826  0.50 37.06  ? 42  ARG C NE    1 
ATOM   2839  N NE    B ARG C 1 41  ? 15.893  -45.798 18.821  0.50 42.97  ? 42  ARG C NE    1 
ATOM   2840  C CZ    A ARG C 1 41  ? 15.797  -48.057 19.468  0.50 39.85  ? 42  ARG C CZ    1 
ATOM   2841  C CZ    B ARG C 1 41  ? 16.046  -46.342 17.621  0.50 43.13  ? 42  ARG C CZ    1 
ATOM   2842  N NH1   A ARG C 1 41  ? 16.881  -47.582 18.880  0.50 41.02  ? 42  ARG C NH1   1 
ATOM   2843  N NH1   B ARG C 1 41  ? 17.195  -46.226 16.981  0.50 41.47  ? 42  ARG C NH1   1 
ATOM   2844  N NH2   A ARG C 1 41  ? 15.688  -49.353 19.702  0.50 40.20  ? 42  ARG C NH2   1 
ATOM   2845  N NH2   B ARG C 1 41  ? 15.051  -47.014 17.072  0.50 44.14  ? 42  ARG C NH2   1 
ATOM   2846  N N     . TRP C 1 42  ? 12.736  -40.844 18.185  1.00 33.56  ? 43  TRP C N     1 
ATOM   2847  C CA    . TRP C 1 42  ? 12.682  -39.429 18.516  1.00 28.86  ? 43  TRP C CA    1 
ATOM   2848  C C     . TRP C 1 42  ? 11.232  -38.954 18.550  1.00 32.74  ? 43  TRP C C     1 
ATOM   2849  O O     . TRP C 1 42  ? 10.816  -38.288 19.495  1.00 31.97  ? 43  TRP C O     1 
ATOM   2850  C CB    . TRP C 1 42  ? 13.506  -38.614 17.511  1.00 27.62  ? 43  TRP C CB    1 
ATOM   2851  C CG    . TRP C 1 42  ? 13.189  -37.142 17.519  1.00 23.93  ? 43  TRP C CG    1 
ATOM   2852  C CD1   . TRP C 1 42  ? 13.641  -36.209 18.404  1.00 22.16  ? 43  TRP C CD1   1 
ATOM   2853  C CD2   . TRP C 1 42  ? 12.360  -36.432 16.574  1.00 25.21  ? 43  TRP C CD2   1 
ATOM   2854  N NE1   . TRP C 1 42  ? 13.143  -34.973 18.088  1.00 22.14  ? 43  TRP C NE1   1 
ATOM   2855  C CE2   . TRP C 1 42  ? 12.358  -35.076 16.970  1.00 23.60  ? 43  TRP C CE2   1 
ATOM   2856  C CE3   . TRP C 1 42  ? 11.622  -36.806 15.446  1.00 25.30  ? 43  TRP C CE3   1 
ATOM   2857  C CZ2   . TRP C 1 42  ? 11.649  -34.101 16.274  1.00 24.48  ? 43  TRP C CZ2   1 
ATOM   2858  C CZ3   . TRP C 1 42  ? 10.925  -35.838 14.756  1.00 27.12  ? 43  TRP C CZ3   1 
ATOM   2859  C CH2   . TRP C 1 42  ? 10.940  -34.505 15.165  1.00 26.21  ? 43  TRP C CH2   1 
ATOM   2860  N N     . LEU C 1 43  ? 10.473  -39.310 17.509  1.00 30.31  ? 44  LEU C N     1 
ATOM   2861  C CA    . LEU C 1 43  ? 9.092   -38.875 17.381  1.00 31.66  ? 44  LEU C CA    1 
ATOM   2862  C C     . LEU C 1 43  ? 8.262   -39.455 18.523  1.00 32.28  ? 44  LEU C C     1 
ATOM   2863  O O     . LEU C 1 43  ? 7.424   -38.766 19.100  1.00 28.06  ? 44  LEU C O     1 
ATOM   2864  C CB    . LEU C 1 43  ? 8.537   -39.300 16.023  1.00 34.40  ? 44  LEU C CB    1 
ATOM   2865  C CG    . LEU C 1 43  ? 7.072   -38.935 15.763  1.00 37.28  ? 44  LEU C CG    1 
ATOM   2866  C CD1   . LEU C 1 43  ? 6.905   -37.427 15.671  1.00 38.55  ? 44  LEU C CD1   1 
ATOM   2867  C CD2   . LEU C 1 43  ? 6.545   -39.613 14.511  1.00 38.37  ? 44  LEU C CD2   1 
ATOM   2868  N N     . THR C 1 44  ? 8.506   -40.732 18.831  1.00 33.26  ? 45  THR C N     1 
ATOM   2869  C CA    . THR C 1 44  ? 7.717   -41.459 19.811  1.00 40.40  ? 45  THR C CA    1 
ATOM   2870  C C     . THR C 1 44  ? 7.859   -40.802 21.182  1.00 39.76  ? 45  THR C C     1 
ATOM   2871  O O     . THR C 1 44  ? 6.897   -40.741 21.944  1.00 40.65  ? 45  THR C O     1 
ATOM   2872  C CB    . THR C 1 44  ? 8.162   -42.920 19.838  1.00 43.44  ? 45  THR C CB    1 
ATOM   2873  O OG1   . THR C 1 44  ? 7.857   -43.425 18.542  1.00 41.14  ? 45  THR C OG1   1 
ATOM   2874  C CG2   . THR C 1 44  ? 7.442   -43.729 20.902  1.00 42.01  ? 45  THR C CG2   1 
ATOM   2875  N N     . LYS C 1 45  ? 9.069   -40.321 21.488  1.00 43.38  ? 46  LYS C N     1 
ATOM   2876  C CA    . LYS C 1 45  ? 9.344   -39.699 22.773  1.00 44.57  ? 46  LYS C CA    1 
ATOM   2877  C C     . LYS C 1 45  ? 8.723   -38.305 22.808  1.00 43.19  ? 46  LYS C C     1 
ATOM   2878  O O     . LYS C 1 45  ? 8.433   -37.777 23.880  1.00 42.17  ? 46  LYS C O     1 
ATOM   2879  C CB    . LYS C 1 45  ? 10.853  -39.633 23.036  1.00 53.73  ? 46  LYS C CB    1 
ATOM   2880  C CG    . LYS C 1 45  ? 11.553  -40.983 23.119  1.00 59.10  ? 46  LYS C CG    1 
ATOM   2881  C CD    . LYS C 1 45  ? 13.023  -40.897 23.513  1.00 65.42  ? 46  LYS C CD    1 
ATOM   2882  C CE    . LYS C 1 45  ? 13.218  -40.312 24.876  1.00 69.53  ? 46  LYS C CE    1 
ATOM   2883  N NZ    . LYS C 1 45  ? 14.633  -40.277 25.255  1.00 72.50  ? 46  LYS C NZ    1 
ATOM   2884  N N     . LEU C 1 46  ? 8.524   -37.719 21.623  1.00 38.89  ? 47  LEU C N     1 
ATOM   2885  C CA    . LEU C 1 46  ? 7.944   -36.392 21.506  1.00 34.44  ? 47  LEU C CA    1 
ATOM   2886  C C     . LEU C 1 46  ? 6.430   -36.496 21.668  1.00 35.73  ? 47  LEU C C     1 
ATOM   2887  O O     . LEU C 1 46  ? 5.802   -35.634 22.279  1.00 36.28  ? 47  LEU C O     1 
ATOM   2888  C CB    . LEU C 1 46  ? 8.325   -35.789 20.155  1.00 36.63  ? 47  LEU C CB    1 
ATOM   2889  C CG    . LEU C 1 46  ? 8.323   -34.258 20.075  1.00 41.62  ? 47  LEU C CG    1 
ATOM   2890  C CD1   . LEU C 1 46  ? 8.486   -33.798 18.635  1.00 43.45  ? 47  LEU C CD1   1 
ATOM   2891  C CD2   . LEU C 1 46  ? 7.069   -33.664 20.690  1.00 45.14  ? 47  LEU C CD2   1 
ATOM   2892  N N     . ASN C 1 47  ? 5.858   -37.564 21.100  1.00 29.72  ? 48  ASN C N     1 
ATOM   2893  C CA    . ASN C 1 47  ? 4.435   -37.841 21.203  1.00 32.98  ? 48  ASN C CA    1 
ATOM   2894  C C     . ASN C 1 47  ? 4.218   -39.342 21.035  1.00 34.16  ? 48  ASN C C     1 
ATOM   2895  O O     . ASN C 1 47  ? 4.504   -39.898 19.977  1.00 37.19  ? 48  ASN C O     1 
ATOM   2896  C CB    . ASN C 1 47  ? 3.632   -37.043 20.182  1.00 33.64  ? 48  ASN C CB    1 
ATOM   2897  C CG    . ASN C 1 47  ? 2.144   -37.141 20.423  1.00 28.73  ? 48  ASN C CG    1 
ATOM   2898  O OD1   . ASN C 1 47  ? 1.608   -38.244 20.576  1.00 30.81  ? 48  ASN C OD1   1 
ATOM   2899  N ND2   . ASN C 1 47  ? 1.464   -36.005 20.472  1.00 26.34  ? 48  ASN C ND2   1 
ATOM   2900  N N     . PRO C 1 48  ? 3.710   -40.043 22.072  1.00 38.74  ? 49  PRO C N     1 
ATOM   2901  C CA    . PRO C 1 48  ? 3.594   -41.503 22.031  1.00 43.55  ? 49  PRO C CA    1 
ATOM   2902  C C     . PRO C 1 48  ? 2.530   -42.024 21.067  1.00 44.52  ? 49  PRO C C     1 
ATOM   2903  O O     . PRO C 1 48  ? 2.665   -43.120 20.527  1.00 42.28  ? 49  PRO C O     1 
ATOM   2904  C CB    . PRO C 1 48  ? 3.272   -41.855 23.499  1.00 43.31  ? 49  PRO C CB    1 
ATOM   2905  C CG    . PRO C 1 48  ? 2.552   -40.631 24.024  1.00 42.44  ? 49  PRO C CG    1 
ATOM   2906  C CD    . PRO C 1 48  ? 3.232   -39.462 23.336  1.00 44.11  ? 49  PRO C CD    1 
ATOM   2907  N N     . ASN C 1 49  ? 1.472   -41.231 20.862  1.00 43.37  ? 50  ASN C N     1 
ATOM   2908  C CA    . ASN C 1 49  ? 0.357   -41.640 20.024  1.00 42.39  ? 50  ASN C CA    1 
ATOM   2909  C C     . ASN C 1 49  ? 0.739   -41.467 18.556  1.00 41.11  ? 50  ASN C C     1 
ATOM   2910  O O     . ASN C 1 49  ? 0.400   -40.461 17.937  1.00 38.15  ? 50  ASN C O     1 
ATOM   2911  C CB    . ASN C 1 49  ? -0.912  -40.864 20.362  1.00 46.14  ? 50  ASN C CB    1 
ATOM   2912  C CG    . ASN C 1 49  ? -2.132  -41.441 19.685  1.00 47.72  ? 50  ASN C CG    1 
ATOM   2913  O OD1   . ASN C 1 49  ? -2.059  -42.515 19.078  1.00 51.04  ? 50  ASN C OD1   1 
ATOM   2914  N ND2   . ASN C 1 49  ? -3.263  -40.759 19.793  1.00 48.54  ? 50  ASN C ND2   1 
ATOM   2915  N N     . VAL C 1 50  ? 1.435   -42.468 18.007  1.00 40.86  ? 51  VAL C N     1 
ATOM   2916  C CA    . VAL C 1 50  ? 1.925   -42.403 16.641  1.00 34.31  ? 51  VAL C CA    1 
ATOM   2917  C C     . VAL C 1 50  ? 1.466   -43.642 15.878  1.00 32.81  ? 51  VAL C C     1 
ATOM   2918  O O     . VAL C 1 50  ? 1.595   -44.763 16.365  1.00 31.93  ? 51  VAL C O     1 
ATOM   2919  C CB    . VAL C 1 50  ? 3.459   -42.274 16.598  1.00 35.66  ? 51  VAL C CB    1 
ATOM   2920  C CG1   . VAL C 1 50  ? 3.996   -42.370 15.174  1.00 34.40  ? 51  VAL C CG1   1 
ATOM   2921  C CG2   . VAL C 1 50  ? 3.940   -40.993 17.269  1.00 33.41  ? 51  VAL C CG2   1 
ATOM   2922  N N     . ILE C 1 51  ? 0.926   -43.416 14.676  1.00 34.51  ? 52  ILE C N     1 
ATOM   2923  C CA    . ILE C 1 51  ? 0.689   -44.483 13.719  1.00 34.71  ? 52  ILE C CA    1 
ATOM   2924  C C     . ILE C 1 51  ? 1.633   -44.278 12.538  1.00 31.86  ? 52  ILE C C     1 
ATOM   2925  O O     . ILE C 1 51  ? 1.643   -43.212 11.928  1.00 33.72  ? 52  ILE C O     1 
ATOM   2926  C CB    . ILE C 1 51  ? -0.783  -44.518 13.268  1.00 39.01  ? 52  ILE C CB    1 
ATOM   2927  C CG1   . ILE C 1 51  ? -1.729  -44.764 14.442  1.00 38.61  ? 52  ILE C CG1   1 
ATOM   2928  C CG2   . ILE C 1 51  ? -0.986  -45.547 12.155  1.00 36.60  ? 52  ILE C CG2   1 
ATOM   2929  C CD1   . ILE C 1 51  ? -1.756  -43.642 15.462  1.00 43.36  ? 52  ILE C CD1   1 
ATOM   2930  N N     . ASN C 1 52  ? 2.427   -45.310 12.233  1.00 30.58  ? 53  ASN C N     1 
ATOM   2931  C CA    . ASN C 1 52  ? 3.395   -45.245 11.150  1.00 29.60  ? 53  ASN C CA    1 
ATOM   2932  C C     . ASN C 1 52  ? 2.698   -45.591 9.836   1.00 28.92  ? 53  ASN C C     1 
ATOM   2933  O O     . ASN C 1 52  ? 2.033   -46.619 9.731   1.00 29.83  ? 53  ASN C O     1 
ATOM   2934  C CB    . ASN C 1 52  ? 4.591   -46.150 11.427  1.00 30.17  ? 53  ASN C CB    1 
ATOM   2935  C CG    . ASN C 1 52  ? 5.690   -45.981 10.405  1.00 31.46  ? 53  ASN C CG    1 
ATOM   2936  O OD1   . ASN C 1 52  ? 5.515   -45.266 9.412   1.00 36.43  ? 53  ASN C OD1   1 
ATOM   2937  N ND2   . ASN C 1 52  ? 6.824   -46.629 10.626  1.00 34.08  ? 53  ASN C ND2   1 
ATOM   2938  N N     . LEU C 1 53  ? 2.864   -44.717 8.836   1.00 30.68  ? 54  LEU C N     1 
ATOM   2939  C CA    . LEU C 1 53  ? 2.221   -44.889 7.543   1.00 32.05  ? 54  LEU C CA    1 
ATOM   2940  C C     . LEU C 1 53  ? 2.979   -45.933 6.727   1.00 36.29  ? 54  LEU C C     1 
ATOM   2941  O O     . LEU C 1 53  ? 2.480   -46.419 5.715   1.00 35.79  ? 54  LEU C O     1 
ATOM   2942  C CB    . LEU C 1 53  ? 2.164   -43.544 6.818   1.00 30.10  ? 54  LEU C CB    1 
ATOM   2943  C CG    . LEU C 1 53  ? 1.314   -42.458 7.487   1.00 31.22  ? 54  LEU C CG    1 
ATOM   2944  C CD1   . LEU C 1 53  ? 1.317   -41.175 6.672   1.00 29.34  ? 54  LEU C CD1   1 
ATOM   2945  C CD2   . LEU C 1 53  ? -0.106  -42.951 7.706   1.00 33.21  ? 54  LEU C CD2   1 
ATOM   2946  N N     . GLN C 1 54  ? 4.181   -46.280 7.197   1.00 40.31  ? 55  GLN C N     1 
ATOM   2947  C CA    . GLN C 1 54  ? 5.067   -47.189 6.489   1.00 44.16  ? 55  GLN C CA    1 
ATOM   2948  C C     . GLN C 1 54  ? 4.376   -48.536 6.278   1.00 41.66  ? 55  GLN C C     1 
ATOM   2949  O O     . GLN C 1 54  ? 4.753   -49.300 5.392   1.00 36.03  ? 55  GLN C O     1 
ATOM   2950  C CB    . GLN C 1 54  ? 6.351   -47.370 7.299   1.00 49.28  ? 55  GLN C CB    1 
ATOM   2951  C CG    . GLN C 1 54  ? 7.531   -47.904 6.495   1.00 55.66  ? 55  GLN C CG    1 
ATOM   2952  C CD    . GLN C 1 54  ? 8.096   -46.887 5.527   1.00 63.67  ? 55  GLN C CD    1 
ATOM   2953  O OE1   . GLN C 1 54  ? 8.132   -47.103 4.311   1.00 70.32  ? 55  GLN C OE1   1 
ATOM   2954  N NE2   . GLN C 1 54  ? 8.546   -45.762 6.063   1.00 68.58  ? 55  GLN C NE2   1 
ATOM   2955  N N     . GLN C 1 55  ? 3.360   -48.810 7.103   1.00 37.78  ? 56  GLN C N     1 
ATOM   2956  C CA    . GLN C 1 55  ? 2.732   -50.120 7.155   1.00 40.21  ? 56  GLN C CA    1 
ATOM   2957  C C     . GLN C 1 55  ? 1.889   -50.362 5.905   1.00 40.23  ? 56  GLN C C     1 
ATOM   2958  O O     . GLN C 1 55  ? 1.559   -51.503 5.593   1.00 40.81  ? 56  GLN C O     1 
ATOM   2959  C CB    . GLN C 1 55  ? 1.853   -50.237 8.400   1.00 41.31  ? 56  GLN C CB    1 
ATOM   2960  C CG    . GLN C 1 55  ? 0.741   -49.195 8.472   1.00 39.97  ? 56  GLN C CG    1 
ATOM   2961  C CD    . GLN C 1 55  ? -0.130  -49.338 9.701   1.00 39.54  ? 56  GLN C CD    1 
ATOM   2962  O OE1   . GLN C 1 55  ? -0.854  -50.325 9.868   1.00 43.19  ? 56  GLN C OE1   1 
ATOM   2963  N NE2   . GLN C 1 55  ? -0.072  -48.343 10.575  1.00 39.32  ? 56  GLN C NE2   1 
ATOM   2964  N N     . PHE C 1 56  ? 1.543   -49.281 5.198   1.00 42.28  ? 57  PHE C N     1 
ATOM   2965  C CA    . PHE C 1 56  ? 0.594   -49.363 4.100   1.00 40.48  ? 57  PHE C CA    1 
ATOM   2966  C C     . PHE C 1 56  ? 1.323   -49.688 2.799   1.00 37.89  ? 57  PHE C C     1 
ATOM   2967  O O     . PHE C 1 56  ? 0.684   -49.946 1.781   1.00 30.78  ? 57  PHE C O     1 
ATOM   2968  C CB    . PHE C 1 56  ? -0.215  -48.065 4.006   1.00 43.09  ? 57  PHE C CB    1 
ATOM   2969  C CG    . PHE C 1 56  ? -1.159  -47.843 5.180   1.00 43.42  ? 57  PHE C CG    1 
ATOM   2970  C CD1   . PHE C 1 56  ? -2.302  -48.621 5.328   1.00 43.39  ? 57  PHE C CD1   1 
ATOM   2971  C CD2   . PHE C 1 56  ? -0.911  -46.851 6.123   1.00 46.41  ? 57  PHE C CD2   1 
ATOM   2972  C CE1   . PHE C 1 56  ? -3.160  -48.423 6.398   1.00 41.54  ? 57  PHE C CE1   1 
ATOM   2973  C CE2   . PHE C 1 56  ? -1.777  -46.655 7.188   1.00 41.66  ? 57  PHE C CE2   1 
ATOM   2974  C CZ    . PHE C 1 56  ? -2.898  -47.440 7.322   1.00 43.48  ? 57  PHE C CZ    1 
ATOM   2975  N N     . TYR C 1 57  ? 2.659   -49.678 2.839   1.00 41.23  ? 58  TYR C N     1 
ATOM   2976  C CA    . TYR C 1 57  ? 3.455   -50.054 1.681   1.00 40.74  ? 58  TYR C CA    1 
ATOM   2977  C C     . TYR C 1 57  ? 3.361   -51.564 1.487   1.00 44.21  ? 58  TYR C C     1 
ATOM   2978  O O     . TYR C 1 57  ? 2.986   -52.290 2.405   1.00 47.02  ? 58  TYR C O     1 
ATOM   2979  C CB    . TYR C 1 57  ? 4.915   -49.613 1.827   1.00 38.98  ? 58  TYR C CB    1 
ATOM   2980  C CG    . TYR C 1 57  ? 5.151   -48.125 1.607   1.00 39.82  ? 58  TYR C CG    1 
ATOM   2981  C CD1   . TYR C 1 57  ? 5.202   -47.591 0.325   1.00 42.18  ? 58  TYR C CD1   1 
ATOM   2982  C CD2   . TYR C 1 57  ? 5.350   -47.261 2.677   1.00 38.33  ? 58  TYR C CD2   1 
ATOM   2983  C CE1   . TYR C 1 57  ? 5.423   -46.240 0.114   1.00 43.12  ? 58  TYR C CE1   1 
ATOM   2984  C CE2   . TYR C 1 57  ? 5.575   -45.909 2.480   1.00 39.79  ? 58  TYR C CE2   1 
ATOM   2985  C CZ    . TYR C 1 57  ? 5.611   -45.397 1.195   1.00 41.20  ? 58  TYR C CZ    1 
ATOM   2986  O OH    . TYR C 1 57  ? 5.832   -44.066 0.996   1.00 46.35  ? 58  TYR C OH    1 
ATOM   2987  N N     . ALA C 1 58  ? 3.702   -52.022 0.278   1.00 45.69  ? 59  ALA C N     1 
ATOM   2988  C CA    . ALA C 1 58  ? 3.700   -53.441 -0.035  1.00 47.67  ? 59  ALA C CA    1 
ATOM   2989  C C     . ALA C 1 58  ? 4.517   -54.192 1.011   1.00 46.67  ? 59  ALA C C     1 
ATOM   2990  O O     . ALA C 1 58  ? 5.602   -53.755 1.388   1.00 44.72  ? 59  ALA C O     1 
ATOM   2991  C CB    . ALA C 1 58  ? 4.242   -53.664 -1.430  1.00 48.58  ? 59  ALA C CB    1 
ATOM   2992  N N     . GLN C 1 59  ? 3.979   -55.324 1.475   1.00 53.50  ? 60  GLN C N     1 
ATOM   2993  C CA    . GLN C 1 59  ? 4.627   -56.113 2.508   1.00 61.98  ? 60  GLN C CA    1 
ATOM   2994  C C     . GLN C 1 59  ? 4.846   -57.536 2.000   1.00 63.95  ? 60  GLN C C     1 
ATOM   2995  O O     . GLN C 1 59  ? 3.898   -58.214 1.609   1.00 60.16  ? 60  GLN C O     1 
ATOM   2996  C CB    . GLN C 1 59  ? 3.782   -56.121 3.782   1.00 71.13  ? 60  GLN C CB    1 
ATOM   2997  C CG    . GLN C 1 59  ? 3.461   -54.733 4.328   1.00 76.03  ? 60  GLN C CG    1 
ATOM   2998  C CD    . GLN C 1 59  ? 4.692   -53.946 4.724   1.00 77.95  ? 60  GLN C CD    1 
ATOM   2999  O OE1   . GLN C 1 59  ? 5.502   -54.386 5.547   1.00 78.47  ? 60  GLN C OE1   1 
ATOM   3000  N NE2   . GLN C 1 59  ? 4.843   -52.766 4.140   1.00 74.05  ? 60  GLN C NE2   1 
ATOM   3001  N N     . ASN C 1 60  ? 6.110   -57.971 2.012   1.00 66.18  ? 61  ASN C N     1 
ATOM   3002  C CA    . ASN C 1 60  ? 6.466   -59.334 1.650   1.00 68.51  ? 61  ASN C CA    1 
ATOM   3003  C C     . ASN C 1 60  ? 6.342   -59.511 0.139   1.00 60.97  ? 61  ASN C C     1 
ATOM   3004  O O     . ASN C 1 60  ? 5.404   -60.144 -0.340  1.00 62.00  ? 61  ASN C O     1 
ATOM   3005  C CB    . ASN C 1 60  ? 5.610   -60.350 2.398   1.00 77.60  ? 61  ASN C CB    1 
ATOM   3006  C CG    . ASN C 1 60  ? 5.651   -60.142 3.893   1.00 84.43  ? 61  ASN C CG    1 
ATOM   3007  O OD1   . ASN C 1 60  ? 6.728   -60.191 4.499   1.00 82.16  ? 61  ASN C OD1   1 
ATOM   3008  N ND2   . ASN C 1 60  ? 4.499   -59.907 4.503   1.00 87.18  ? 61  ASN C ND2   1 
ATOM   3009  N N     . GLY C 1 61  ? 7.304   -58.946 -0.598  1.00 52.10  ? 62  GLY C N     1 
ATOM   3010  C CA    . GLY C 1 61  ? 7.348   -59.070 -2.045  1.00 50.00  ? 62  GLY C CA    1 
ATOM   3011  C C     . GLY C 1 61  ? 5.946   -59.112 -2.648  1.00 48.40  ? 62  GLY C C     1 
ATOM   3012  O O     . GLY C 1 61  ? 5.683   -59.887 -3.565  1.00 52.28  ? 62  GLY C O     1 
ATOM   3013  N N     . GLU C 1 62  ? 5.056   -58.266 -2.121  1.00 49.60  ? 63  GLU C N     1 
ATOM   3014  C CA    . GLU C 1 62  ? 3.693   -58.172 -2.616  1.00 48.88  ? 63  GLU C CA    1 
ATOM   3015  C C     . GLU C 1 62  ? 3.635   -57.176 -3.771  1.00 46.37  ? 63  GLU C C     1 
ATOM   3016  O O     . GLU C 1 62  ? 4.364   -56.187 -3.782  1.00 48.37  ? 63  GLU C O     1 
ATOM   3017  C CB    . GLU C 1 62  ? 2.740   -57.737 -1.503  1.00 52.92  ? 63  GLU C CB    1 
ATOM   3018  C CG    . GLU C 1 62  ? 1.382   -57.275 -2.023  1.00 57.75  ? 63  GLU C CG    1 
ATOM   3019  C CD    . GLU C 1 62  ? 0.432   -56.775 -0.951  1.00 61.65  ? 63  GLU C CD    1 
ATOM   3020  O OE1   . GLU C 1 62  ? 0.802   -55.825 -0.229  1.00 67.00  ? 63  GLU C OE1   1 
ATOM   3021  O OE2   . GLU C 1 62  ? -0.681  -57.329 -0.844  1.00 64.07  ? 63  GLU C OE2   1 
ATOM   3022  N N     . VAL C 1 63  ? 2.753   -57.454 -4.736  1.00 45.73  ? 64  VAL C N     1 
ATOM   3023  C CA    . VAL C 1 63  ? 2.519   -56.556 -5.854  1.00 45.14  ? 64  VAL C CA    1 
ATOM   3024  C C     . VAL C 1 63  ? 1.391   -55.603 -5.473  1.00 43.27  ? 64  VAL C C     1 
ATOM   3025  O O     . VAL C 1 63  ? 0.240   -56.015 -5.355  1.00 43.34  ? 64  VAL C O     1 
ATOM   3026  C CB    . VAL C 1 63  ? 2.182   -57.324 -7.146  1.00 48.34  ? 64  VAL C CB    1 
ATOM   3027  C CG1   . VAL C 1 63  ? 1.861   -56.379 -8.298  1.00 47.10  ? 64  VAL C CG1   1 
ATOM   3028  C CG2   . VAL C 1 63  ? 3.292   -58.292 -7.537  1.00 46.38  ? 64  VAL C CG2   1 
ATOM   3029  N N     . LYS C 1 64  ? 1.738   -54.326 -5.285  1.00 43.58  ? 65  LYS C N     1 
ATOM   3030  C CA    . LYS C 1 64  ? 0.776   -53.328 -4.849  1.00 41.82  ? 65  LYS C CA    1 
ATOM   3031  C C     . LYS C 1 64  ? 1.120   -51.981 -5.477  1.00 37.68  ? 65  LYS C C     1 
ATOM   3032  O O     . LYS C 1 64  ? 2.230   -51.481 -5.316  1.00 36.77  ? 65  LYS C O     1 
ATOM   3033  C CB    . LYS C 1 64  ? 0.781   -53.247 -3.318  1.00 43.46  ? 65  LYS C CB    1 
ATOM   3034  C CG    . LYS C 1 64  ? -0.252  -52.311 -2.709  1.00 43.12  ? 65  LYS C CG    1 
ATOM   3035  C CD    . LYS C 1 64  ? -0.255  -52.326 -1.185  1.00 43.01  ? 65  LYS C CD    1 
ATOM   3036  C CE    . LYS C 1 64  ? -1.356  -51.504 -0.597  1.00 40.38  ? 65  LYS C CE    1 
ATOM   3037  N NZ    . LYS C 1 64  ? -1.355  -51.580 0.866   1.00 39.89  ? 65  LYS C NZ    1 
ATOM   3038  N N     . ASN C 1 65  ? 0.150   -51.407 -6.196  1.00 36.87  ? 66  ASN C N     1 
ATOM   3039  C CA    . ASN C 1 65  ? 0.310   -50.093 -6.793  1.00 39.62  ? 66  ASN C CA    1 
ATOM   3040  C C     . ASN C 1 65  ? 0.448   -49.068 -5.671  1.00 37.99  ? 66  ASN C C     1 
ATOM   3041  O O     . ASN C 1 65  ? -0.253  -49.149 -4.665  1.00 41.49  ? 66  ASN C O     1 
ATOM   3042  C CB    . ASN C 1 65  ? -0.848  -49.763 -7.729  1.00 39.95  ? 66  ASN C CB    1 
ATOM   3043  C CG    . ASN C 1 65  ? -0.545  -48.581 -8.619  1.00 44.95  ? 66  ASN C CG    1 
ATOM   3044  O OD1   . ASN C 1 65  ? -0.155  -47.515 -8.129  1.00 45.49  ? 66  ASN C OD1   1 
ATOM   3045  N ND2   . ASN C 1 65  ? -0.705  -48.750 -9.924  1.00 43.38  ? 66  ASN C ND2   1 
ATOM   3046  N N     . ARG C 1 66  ? 1.367   -48.112 -5.847  1.00 40.12  ? 67  ARG C N     1 
ATOM   3047  C CA    . ARG C 1 66  ? 1.613   -47.098 -4.835  1.00 42.71  ? 67  ARG C CA    1 
ATOM   3048  C C     . ARG C 1 66  ? 0.429   -46.134 -4.781  1.00 40.76  ? 67  ARG C C     1 
ATOM   3049  O O     . ARG C 1 66  ? 0.261   -45.411 -3.802  1.00 41.93  ? 67  ARG C O     1 
ATOM   3050  C CB    . ARG C 1 66  ? 2.929   -46.354 -5.089  1.00 46.54  ? 67  ARG C CB    1 
ATOM   3051  C CG    . ARG C 1 66  ? 4.176   -47.216 -4.953  1.00 47.46  ? 67  ARG C CG    1 
ATOM   3052  C CD    . ARG C 1 66  ? 5.414   -46.389 -4.628  1.00 46.41  ? 67  ARG C CD    1 
ATOM   3053  N NE    . ARG C 1 66  ? 5.688   -45.346 -5.624  1.00 46.96  ? 67  ARG C NE    1 
ATOM   3054  C CZ    . ARG C 1 66  ? 6.134   -45.567 -6.854  1.00 45.44  ? 67  ARG C CZ    1 
ATOM   3055  N NH1   . ARG C 1 66  ? 6.397   -46.798 -7.255  1.00 42.16  ? 67  ARG C NH1   1 
ATOM   3056  N NH2   . ARG C 1 66  ? 6.334   -44.550 -7.674  1.00 44.55  ? 67  ARG C NH2   1 
ATOM   3057  N N     . ARG C 1 67  ? -0.387  -46.134 -5.841  1.00 40.42  ? 68  ARG C N     1 
ATOM   3058  C CA    . ARG C 1 67  ? -1.593  -45.323 -5.878  1.00 40.44  ? 68  ARG C CA    1 
ATOM   3059  C C     . ARG C 1 67  ? -2.532  -45.773 -4.762  1.00 38.02  ? 68  ARG C C     1 
ATOM   3060  O O     . ARG C 1 67  ? -3.214  -44.954 -4.150  1.00 42.12  ? 68  ARG C O     1 
ATOM   3061  C CB    . ARG C 1 67  ? -2.308  -45.426 -7.230  1.00 40.81  ? 68  ARG C CB    1 
ATOM   3062  C CG    . ARG C 1 67  ? -1.598  -44.748 -8.393  1.00 43.64  ? 68  ARG C CG    1 
ATOM   3063  C CD    . ARG C 1 67  ? -2.371  -44.924 -9.694  1.00 45.90  ? 68  ARG C CD    1 
ATOM   3064  N NE    . ARG C 1 67  ? -1.767  -44.203 -10.820 1.00 45.51  ? 68  ARG C NE    1 
ATOM   3065  C CZ    . ARG C 1 67  ? -1.686  -42.882 -10.917 1.00 51.03  ? 68  ARG C CZ    1 
ATOM   3066  N NH1   . ARG C 1 67  ? -2.189  -42.116 -9.966  1.00 53.94  ? 68  ARG C NH1   1 
ATOM   3067  N NH2   . ARG C 1 67  ? -1.108  -42.332 -11.971 1.00 50.93  ? 68  ARG C NH2   1 
ATOM   3068  N N     . ASP C 1 68  ? -2.558  -47.088 -4.515  1.00 39.95  ? 69  ASP C N     1 
ATOM   3069  C CA    . ASP C 1 68  ? -3.405  -47.665 -3.485  1.00 41.18  ? 69  ASP C CA    1 
ATOM   3070  C C     . ASP C 1 68  ? -2.803  -47.369 -2.114  1.00 40.69  ? 69  ASP C C     1 
ATOM   3071  O O     . ASP C 1 68  ? -3.521  -47.035 -1.175  1.00 45.90  ? 69  ASP C O     1 
ATOM   3072  C CB    . ASP C 1 68  ? -3.607  -49.157 -3.705  1.00 45.31  ? 69  ASP C CB    1 
ATOM   3073  C CG    . ASP C 1 68  ? -4.363  -49.535 -4.971  1.00 47.01  ? 69  ASP C CG    1 
ATOM   3074  O OD1   . ASP C 1 68  ? -5.533  -49.117 -5.104  1.00 46.37  ? 69  ASP C OD1   1 
ATOM   3075  O OD2   . ASP C 1 68  ? -3.777  -50.247 -5.813  1.00 48.89  ? 69  ASP C OD2   1 
ATOM   3076  N N     . THR C 1 69  ? -1.476  -47.504 -2.014  1.00 33.46  ? 70  THR C N     1 
ATOM   3077  C CA    . THR C 1 69  ? -0.763  -47.236 -0.777  1.00 28.44  ? 70  THR C CA    1 
ATOM   3078  C C     . THR C 1 69  ? -1.117  -45.833 -0.288  1.00 31.57  ? 70  THR C C     1 
ATOM   3079  O O     . THR C 1 69  ? -1.565  -45.659 0.844   1.00 30.61  ? 70  THR C O     1 
ATOM   3080  C CB    . THR C 1 69  ? 0.740   -47.391 -1.006  1.00 29.54  ? 70  THR C CB    1 
ATOM   3081  O OG1   . THR C 1 69  ? 0.951   -48.764 -1.320  1.00 26.82  ? 70  THR C OG1   1 
ATOM   3082  C CG2   . THR C 1 69  ? 1.559   -47.020 0.218   1.00 30.79  ? 70  THR C CG2   1 
ATOM   3083  N N     . TYR C 1 70  ? -0.915  -44.841 -1.162  1.00 27.56  ? 71  TYR C N     1 
ATOM   3084  C CA    . TYR C 1 70  ? -1.133  -43.447 -0.812  1.00 29.59  ? 71  TYR C CA    1 
ATOM   3085  C C     . TYR C 1 70  ? -2.597  -43.246 -0.427  1.00 32.65  ? 71  TYR C C     1 
ATOM   3086  O O     . TYR C 1 70  ? -2.900  -42.493 0.495   1.00 38.46  ? 71  TYR C O     1 
ATOM   3087  C CB    . TYR C 1 70  ? -0.707  -42.541 -1.973  1.00 27.51  ? 71  TYR C CB    1 
ATOM   3088  C CG    . TYR C 1 70  ? 0.752   -42.696 -2.384  1.00 26.83  ? 71  TYR C CG    1 
ATOM   3089  C CD1   . TYR C 1 70  ? 1.707   -43.139 -1.477  1.00 25.63  ? 71  TYR C CD1   1 
ATOM   3090  C CD2   . TYR C 1 70  ? 1.173   -42.402 -3.675  1.00 27.03  ? 71  TYR C CD2   1 
ATOM   3091  C CE1   . TYR C 1 70  ? 3.034   -43.287 -1.841  1.00 28.72  ? 71  TYR C CE1   1 
ATOM   3092  C CE2   . TYR C 1 70  ? 2.499   -42.544 -4.051  1.00 28.31  ? 71  TYR C CE2   1 
ATOM   3093  C CZ    . TYR C 1 70  ? 3.432   -42.988 -3.131  1.00 27.86  ? 71  TYR C CZ    1 
ATOM   3094  O OH    . TYR C 1 70  ? 4.741   -43.132 -3.489  1.00 30.49  ? 71  TYR C OH    1 
ATOM   3095  N N     . GLU C 1 71  ? -3.495  -43.930 -1.144  1.00 33.69  ? 72  GLU C N     1 
ATOM   3096  C CA    . GLU C 1 71  ? -4.921  -43.841 -0.877  1.00 33.52  ? 72  GLU C CA    1 
ATOM   3097  C C     . GLU C 1 71  ? -5.199  -44.317 0.547   1.00 35.53  ? 72  GLU C C     1 
ATOM   3098  O O     . GLU C 1 71  ? -5.931  -43.667 1.291   1.00 31.87  ? 72  GLU C O     1 
ATOM   3099  C CB    . GLU C 1 71  ? -5.715  -44.665 -1.891  1.00 34.43  ? 72  GLU C CB    1 
ATOM   3100  C CG    . GLU C 1 71  ? -7.217  -44.668 -1.624  1.00 34.42  ? 72  GLU C CG    1 
ATOM   3101  C CD    . GLU C 1 71  ? -7.821  -43.282 -1.476  1.00 37.67  ? 72  GLU C CD    1 
ATOM   3102  O OE1   . GLU C 1 71  ? -7.660  -42.466 -2.408  1.00 39.60  ? 72  GLU C OE1   1 
ATOM   3103  O OE2   . GLU C 1 71  ? -8.456  -43.018 -0.432  1.00 36.74  ? 72  GLU C OE2   1 
ATOM   3104  N N     . GLN C 1 72  ? -4.604  -45.457 0.912   1.00 35.34  ? 73  GLN C N     1 
ATOM   3105  C CA    . GLN C 1 72  ? -4.800  -46.041 2.229   1.00 38.72  ? 73  GLN C CA    1 
ATOM   3106  C C     . GLN C 1 72  ? -4.174  -45.132 3.284   1.00 39.68  ? 73  GLN C C     1 
ATOM   3107  O O     . GLN C 1 72  ? -4.669  -45.045 4.405   1.00 46.75  ? 73  GLN C O     1 
ATOM   3108  C CB    . GLN C 1 72  ? -4.215  -47.453 2.277   1.00 38.81  ? 73  GLN C CB    1 
ATOM   3109  C CG    . GLN C 1 72  ? -4.949  -48.454 1.389   1.00 39.81  ? 73  GLN C CG    1 
ATOM   3110  C CD    . GLN C 1 72  ? -4.348  -49.842 1.431   1.00 39.37  ? 73  GLN C CD    1 
ATOM   3111  O OE1   . GLN C 1 72  ? -3.332  -50.087 2.090   1.00 34.15  ? 73  GLN C OE1   1 
ATOM   3112  N NE2   . GLN C 1 72  ? -4.974  -50.768 0.718   1.00 43.94  ? 73  GLN C NE2   1 
ATOM   3113  N N     . MET C 1 73  ? -3.082  -44.459 2.908   1.00 39.39  ? 74  MET C N     1 
ATOM   3114  C CA    . MET C 1 73  ? -2.413  -43.521 3.793   1.00 37.16  ? 74  MET C CA    1 
ATOM   3115  C C     . MET C 1 73  ? -3.341  -42.344 4.084   1.00 35.45  ? 74  MET C C     1 
ATOM   3116  O O     . MET C 1 73  ? -3.504  -41.947 5.235   1.00 36.29  ? 74  MET C O     1 
ATOM   3117  C CB    . MET C 1 73  ? -1.115  -42.997 3.168   1.00 39.88  ? 74  MET C CB    1 
ATOM   3118  C CG    . MET C 1 73  ? 0.029   -43.990 3.194   1.00 42.22  ? 74  MET C CG    1 
ATOM   3119  S SD    . MET C 1 73  ? 1.501   -43.370 2.356   1.00 41.17  ? 74  MET C SD    1 
ATOM   3120  C CE    . MET C 1 73  ? 2.614   -44.763 2.583   1.00 38.43  ? 74  MET C CE    1 
ATOM   3121  N N     . VAL C 1 74  ? -3.939  -41.794 3.023   1.00 34.25  ? 75  VAL C N     1 
ATOM   3122  C CA    . VAL C 1 74  ? -4.802  -40.630 3.139   1.00 34.26  ? 75  VAL C CA    1 
ATOM   3123  C C     . VAL C 1 74  ? -6.014  -40.993 3.991   1.00 32.67  ? 75  VAL C C     1 
ATOM   3124  O O     . VAL C 1 74  ? -6.439  -40.210 4.838   1.00 34.10  ? 75  VAL C O     1 
ATOM   3125  C CB    . VAL C 1 74  ? -5.230  -40.108 1.753   1.00 32.79  ? 75  VAL C CB    1 
ATOM   3126  C CG1   . VAL C 1 74  ? -6.329  -39.057 1.856   1.00 30.51  ? 75  VAL C CG1   1 
ATOM   3127  C CG2   . VAL C 1 74  ? -4.045  -39.571 0.960   1.00 34.46  ? 75  VAL C CG2   1 
ATOM   3128  N N     . ASN C 1 75  ? -6.556  -42.193 3.759   1.00 30.88  ? 76  ASN C N     1 
ATOM   3129  C CA    . ASN C 1 75  ? -7.779  -42.628 4.411   1.00 31.35  ? 76  ASN C CA    1 
ATOM   3130  C C     . ASN C 1 75  ? -7.535  -42.786 5.911   1.00 28.43  ? 76  ASN C C     1 
ATOM   3131  O O     . ASN C 1 75  ? -8.386  -42.432 6.722   1.00 29.38  ? 76  ASN C O     1 
ATOM   3132  C CB    . ASN C 1 75  ? -8.313  -43.911 3.784   1.00 34.12  ? 76  ASN C CB    1 
ATOM   3133  C CG    . ASN C 1 75  ? -9.623  -44.342 4.397   1.00 35.14  ? 76  ASN C CG    1 
ATOM   3134  O OD1   . ASN C 1 75  ? -10.580 -43.561 4.431   1.00 41.85  ? 76  ASN C OD1   1 
ATOM   3135  N ND2   . ASN C 1 75  ? -9.685  -45.571 4.890   1.00 41.13  ? 76  ASN C ND2   1 
ATOM   3136  N N     . ALA C 1 76  ? -6.365  -43.326 6.266   1.00 28.86  ? 77  ALA C N     1 
ATOM   3137  C CA    . ALA C 1 76  ? -6.008  -43.540 7.659   1.00 30.38  ? 77  ALA C CA    1 
ATOM   3138  C C     . ALA C 1 76  ? -5.923  -42.199 8.386   1.00 35.08  ? 77  ALA C C     1 
ATOM   3139  O O     . ALA C 1 76  ? -6.326  -42.088 9.543   1.00 31.54  ? 77  ALA C O     1 
ATOM   3140  C CB    . ALA C 1 76  ? -4.703  -44.302 7.744   1.00 27.62  ? 77  ALA C CB    1 
ATOM   3141  N N     . ILE C 1 77  ? -5.397  -41.183 7.692   1.00 33.33  ? 78  ILE C N     1 
ATOM   3142  C CA    . ILE C 1 77  ? -5.234  -39.858 8.269   1.00 33.54  ? 78  ILE C CA    1 
ATOM   3143  C C     . ILE C 1 77  ? -6.609  -39.231 8.490   1.00 33.11  ? 78  ILE C C     1 
ATOM   3144  O O     . ILE C 1 77  ? -6.876  -38.677 9.554   1.00 36.15  ? 78  ILE C O     1 
ATOM   3145  C CB    . ILE C 1 77  ? -4.341  -38.976 7.375   1.00 29.28  ? 78  ILE C CB    1 
ATOM   3146  C CG1   . ILE C 1 77  ? -2.929  -39.553 7.248   1.00 29.39  ? 78  ILE C CG1   1 
ATOM   3147  C CG2   . ILE C 1 77  ? -4.316  -37.533 7.882   1.00 30.12  ? 78  ILE C CG2   1 
ATOM   3148  C CD1   . ILE C 1 77  ? -2.014  -38.763 6.329   1.00 27.53  ? 78  ILE C CD1   1 
ATOM   3149  N N     . LEU C 1 78  ? -7.476  -39.327 7.476   1.00 32.03  ? 79  LEU C N     1 
ATOM   3150  C CA    . LEU C 1 78  ? -8.785  -38.695 7.521   1.00 35.39  ? 79  LEU C CA    1 
ATOM   3151  C C     . LEU C 1 78  ? -9.638  -39.334 8.615   1.00 36.58  ? 79  LEU C C     1 
ATOM   3152  O O     . LEU C 1 78  ? -10.372 -38.637 9.313   1.00 36.79  ? 79  LEU C O     1 
ATOM   3153  C CB    . LEU C 1 78  ? -9.465  -38.781 6.154   1.00 39.27  ? 79  LEU C CB    1 
ATOM   3154  C CG    . LEU C 1 78  ? -9.083  -37.690 5.147   1.00 42.38  ? 79  LEU C CG    1 
ATOM   3155  C CD1   . LEU C 1 78  ? -9.462  -36.320 5.684   1.00 44.39  ? 79  LEU C CD1   1 
ATOM   3156  C CD2   . LEU C 1 78  ? -7.606  -37.736 4.800   1.00 47.28  ? 79  LEU C CD2   1 
ATOM   3157  N N     . ASP C 1 79  ? -9.539  -40.661 8.756   1.00 36.53  ? 80  ASP C N     1 
ATOM   3158  C CA    . ASP C 1 79  ? -10.307 -41.380 9.759   1.00 38.01  ? 80  ASP C CA    1 
ATOM   3159  C C     . ASP C 1 79  ? -10.113 -40.716 11.120  1.00 37.30  ? 80  ASP C C     1 
ATOM   3160  O O     . ASP C 1 79  ? -11.069 -40.548 11.875  1.00 40.86  ? 80  ASP C O     1 
ATOM   3161  C CB    . ASP C 1 79  ? -9.948  -42.858 9.792   1.00 38.08  ? 80  ASP C CB    1 
ATOM   3162  C CG    . ASP C 1 79  ? -10.636 -43.720 8.743   1.00 40.27  ? 80  ASP C CG    1 
ATOM   3163  O OD1   . ASP C 1 79  ? -11.468 -43.174 7.989   1.00 42.29  ? 80  ASP C OD1   1 
ATOM   3164  O OD2   . ASP C 1 79  ? -10.341 -44.933 8.697   1.00 49.06  ? 80  ASP C OD2   1 
ATOM   3165  N N     . ALA C 1 80  ? -8.866  -40.340 11.418  1.00 33.39  ? 81  ALA C N     1 
ATOM   3166  C CA    . ALA C 1 80  ? -8.537  -39.709 12.685  1.00 31.40  ? 81  ALA C CA    1 
ATOM   3167  C C     . ALA C 1 80  ? -9.239  -38.357 12.788  1.00 29.02  ? 81  ALA C C     1 
ATOM   3168  O O     . ALA C 1 80  ? -9.804  -38.023 13.827  1.00 26.62  ? 81  ALA C O     1 
ATOM   3169  C CB    . ALA C 1 80  ? -7.036  -39.566 12.816  1.00 31.90  ? 81  ALA C CB    1 
ATOM   3170  N N     . VAL C 1 81  ? -9.206  -37.596 11.688  1.00 26.05  ? 82  VAL C N     1 
ATOM   3171  C CA    . VAL C 1 81  ? -9.762  -36.253 11.655  1.00 26.92  ? 82  VAL C CA    1 
ATOM   3172  C C     . VAL C 1 81  ? -11.277 -36.332 11.825  1.00 27.98  ? 82  VAL C C     1 
ATOM   3173  O O     . VAL C 1 81  ? -11.857 -35.581 12.607  1.00 26.79  ? 82  VAL C O     1 
ATOM   3174  C CB    . VAL C 1 81  ? -9.381  -35.526 10.350  1.00 27.73  ? 82  VAL C CB    1 
ATOM   3175  C CG1   . VAL C 1 81  ? -10.024 -34.148 10.257  1.00 27.97  ? 82  VAL C CG1   1 
ATOM   3176  C CG2   . VAL C 1 81  ? -7.870  -35.423 10.179  1.00 28.22  ? 82  VAL C CG2   1 
ATOM   3177  N N     . ARG C 1 82  ? -11.908 -37.246 11.079  1.00 29.89  ? 83  ARG C N     1 
ATOM   3178  C CA    . ARG C 1 82  ? -13.350 -37.423 11.133  1.00 30.20  ? 83  ARG C CA    1 
ATOM   3179  C C     . ARG C 1 82  ? -13.748 -37.915 12.523  1.00 29.72  ? 83  ARG C C     1 
ATOM   3180  O O     . ARG C 1 82  ? -14.849 -37.637 12.993  1.00 28.01  ? 83  ARG C O     1 
ATOM   3181  C CB    . ARG C 1 82  ? -13.821 -38.385 10.034  1.00 33.15  ? 83  ARG C CB    1 
ATOM   3182  C CG    . ARG C 1 82  ? -13.787 -37.786 8.634   1.00 34.16  ? 83  ARG C CG    1 
ATOM   3183  C CD    . ARG C 1 82  ? -14.292 -38.751 7.569   1.00 35.93  ? 83  ARG C CD    1 
ATOM   3184  N NE    . ARG C 1 82  ? -13.377 -39.878 7.355   1.00 36.42  ? 83  ARG C NE    1 
ATOM   3185  C CZ    . ARG C 1 82  ? -12.795 -40.173 6.197   1.00 35.80  ? 83  ARG C CZ    1 
ATOM   3186  N NH1   . ARG C 1 82  ? -13.044 -39.446 5.123   1.00 37.52  ? 83  ARG C NH1   1 
ATOM   3187  N NH2   . ARG C 1 82  ? -11.970 -41.202 6.117   1.00 34.51  ? 83  ARG C NH2   1 
ATOM   3188  N N     . ALA C 1 83  ? -12.836 -38.644 13.173  1.00 29.09  ? 84  ALA C N     1 
ATOM   3189  C CA    . ALA C 1 83  ? -13.059 -39.122 14.527  1.00 29.21  ? 84  ALA C CA    1 
ATOM   3190  C C     . ALA C 1 83  ? -13.134 -37.934 15.483  1.00 27.99  ? 84  ALA C C     1 
ATOM   3191  O O     . ALA C 1 83  ? -13.857 -37.975 16.475  1.00 29.54  ? 84  ALA C O     1 
ATOM   3192  C CB    . ALA C 1 83  ? -11.966 -40.090 14.924  1.00 29.62  ? 84  ALA C CB    1 
ATOM   3193  N N     . GLY C 1 84  ? -12.378 -36.876 15.165  1.00 27.76  ? 85  GLY C N     1 
ATOM   3194  C CA    . GLY C 1 84  ? -12.401 -35.648 15.942  1.00 27.78  ? 85  GLY C CA    1 
ATOM   3195  C C     . GLY C 1 84  ? -11.033 -35.337 16.543  1.00 29.39  ? 85  GLY C C     1 
ATOM   3196  O O     . GLY C 1 84  ? -10.868 -34.338 17.240  1.00 32.01  ? 85  GLY C O     1 
ATOM   3197  N N     . LYS C 1 85  ? -10.055 -36.197 16.249  1.00 32.58  ? 86  LYS C N     1 
ATOM   3198  C CA    . LYS C 1 85  ? -8.718  -36.067 16.801  1.00 34.00  ? 86  LYS C CA    1 
ATOM   3199  C C     . LYS C 1 85  ? -7.988  -34.908 16.127  1.00 35.31  ? 86  LYS C C     1 
ATOM   3200  O O     . LYS C 1 85  ? -8.064  -34.742 14.911  1.00 32.45  ? 86  LYS C O     1 
ATOM   3201  C CB    . LYS C 1 85  ? -7.934  -37.368 16.596  1.00 34.29  ? 86  LYS C CB    1 
ATOM   3202  C CG    . LYS C 1 85  ? -8.608  -38.621 17.137  1.00 38.39  ? 86  LYS C CG    1 
ATOM   3203  C CD    . LYS C 1 85  ? -7.838  -39.906 16.857  1.00 40.21  ? 86  LYS C CD    1 
ATOM   3204  C CE    . LYS C 1 85  ? -8.569  -41.132 17.310  1.00 42.37  ? 86  LYS C CE    1 
ATOM   3205  N NZ    . LYS C 1 85  ? -8.802  -41.127 18.756  1.00 42.17  ? 86  LYS C NZ    1 
ATOM   3206  N N     . LYS C 1 86  ? -7.284  -34.112 16.938  1.00 34.34  ? 87  LYS C N     1 
ATOM   3207  C CA    . LYS C 1 86  ? -6.393  -33.085 16.424  1.00 38.62  ? 87  LYS C CA    1 
ATOM   3208  C C     . LYS C 1 86  ? -5.171  -33.775 15.823  1.00 37.89  ? 87  LYS C C     1 
ATOM   3209  O O     . LYS C 1 86  ? -4.224  -34.105 16.534  1.00 32.53  ? 87  LYS C O     1 
ATOM   3210  C CB    . LYS C 1 86  ? -6.022  -32.103 17.542  1.00 40.01  ? 87  LYS C CB    1 
ATOM   3211  C CG    . LYS C 1 86  ? -5.155  -30.927 17.111  1.00 43.12  ? 87  LYS C CG    1 
ATOM   3212  C CD    . LYS C 1 86  ? -4.950  -29.876 18.196  1.00 46.74  ? 87  LYS C CD    1 
ATOM   3213  C CE    . LYS C 1 86  ? -4.283  -30.424 19.418  1.00 47.50  ? 87  LYS C CE    1 
ATOM   3214  N NZ    . LYS C 1 86  ? -4.076  -29.387 20.431  1.00 50.01  ? 87  LYS C NZ    1 
ATOM   3215  N N     . THR C 1 87  ? -5.215  -33.991 14.503  1.00 35.48  ? 88  THR C N     1 
ATOM   3216  C CA    . THR C 1 87  ? -4.287  -34.886 13.832  1.00 33.77  ? 88  THR C CA    1 
ATOM   3217  C C     . THR C 1 87  ? -3.120  -34.096 13.247  1.00 32.46  ? 88  THR C C     1 
ATOM   3218  O O     . THR C 1 87  ? -3.305  -33.012 12.698  1.00 32.76  ? 88  THR C O     1 
ATOM   3219  C CB    . THR C 1 87  ? -5.033  -35.660 12.747  1.00 32.69  ? 88  THR C CB    1 
ATOM   3220  O OG1   . THR C 1 87  ? -6.100  -36.325 13.416  1.00 31.49  ? 88  THR C OG1   1 
ATOM   3221  C CG2   . THR C 1 87  ? -4.148  -36.669 12.038  1.00 33.42  ? 88  THR C CG2   1 
ATOM   3222  N N     . VAL C 1 88  ? -1.921  -34.677 13.355  1.00 32.00  ? 89  VAL C N     1 
ATOM   3223  C CA    . VAL C 1 88  ? -0.724  -34.118 12.750  1.00 34.38  ? 89  VAL C CA    1 
ATOM   3224  C C     . VAL C 1 88  ? -0.090  -35.184 11.862  1.00 34.78  ? 89  VAL C C     1 
ATOM   3225  O O     . VAL C 1 88  ? 0.068   -36.330 12.277  1.00 35.18  ? 89  VAL C O     1 
ATOM   3226  C CB    . VAL C 1 88  ? 0.276   -33.616 13.810  1.00 35.96  ? 89  VAL C CB    1 
ATOM   3227  C CG1   . VAL C 1 88  ? 1.634   -33.289 13.198  1.00 35.60  ? 89  VAL C CG1   1 
ATOM   3228  C CG2   . VAL C 1 88  ? -0.268  -32.422 14.585  1.00 35.88  ? 89  VAL C CG2   1 
ATOM   3229  N N     . CYS C 1 89  ? 0.264   -34.792 10.634  1.00 39.62  ? 90  CYS C N     1 
ATOM   3230  C CA    . CYS C 1 89  ? 0.963   -35.675 9.716   1.00 44.41  ? 90  CYS C CA    1 
ATOM   3231  C C     . CYS C 1 89  ? 2.427   -35.252 9.624   1.00 42.98  ? 90  CYS C C     1 
ATOM   3232  O O     . CYS C 1 89  ? 2.735   -34.178 9.113   1.00 48.22  ? 90  CYS C O     1 
ATOM   3233  C CB    . CYS C 1 89  ? 0.309   -35.669 8.339   1.00 48.43  ? 90  CYS C CB    1 
ATOM   3234  S SG    . CYS C 1 89  ? 1.177   -36.697 7.126   1.00 56.16  ? 90  CYS C SG    1 
ATOM   3235  N N     . ALA C 1 90  ? 3.318   -36.109 10.132  1.00 36.55  ? 91  ALA C N     1 
ATOM   3236  C CA    . ALA C 1 90  ? 4.741   -35.813 10.166  1.00 29.55  ? 91  ALA C CA    1 
ATOM   3237  C C     . ALA C 1 90  ? 5.465   -36.595 9.074   1.00 31.08  ? 91  ALA C C     1 
ATOM   3238  O O     . ALA C 1 90  ? 5.767   -37.775 9.244   1.00 29.51  ? 91  ALA C O     1 
ATOM   3239  C CB    . ALA C 1 90  ? 5.300   -36.131 11.536  1.00 27.92  ? 91  ALA C CB    1 
ATOM   3240  N N     . LEU C 1 91  ? 5.738   -35.918 7.954   1.00 32.36  ? 92  LEU C N     1 
ATOM   3241  C CA    . LEU C 1 91  ? 6.493   -36.504 6.859   1.00 30.39  ? 92  LEU C CA    1 
ATOM   3242  C C     . LEU C 1 91  ? 7.909   -35.939 6.880   1.00 31.23  ? 92  LEU C C     1 
ATOM   3243  O O     . LEU C 1 91  ? 8.126   -34.820 7.341   1.00 28.38  ? 92  LEU C O     1 
ATOM   3244  C CB    . LEU C 1 91  ? 5.798   -36.219 5.529   1.00 30.76  ? 92  LEU C CB    1 
ATOM   3245  C CG    . LEU C 1 91  ? 4.329   -36.644 5.438   1.00 29.91  ? 92  LEU C CG    1 
ATOM   3246  C CD1   . LEU C 1 91  ? 3.821   -36.529 4.012   1.00 29.80  ? 92  LEU C CD1   1 
ATOM   3247  C CD2   . LEU C 1 91  ? 4.137   -38.055 5.967   1.00 27.99  ? 92  LEU C CD2   1 
ATOM   3248  N N     . TYR C 1 92  ? 8.863   -36.726 6.370   1.00 28.43  ? 93  TYR C N     1 
ATOM   3249  C CA    . TYR C 1 92  ? 10.257  -36.319 6.336   1.00 28.76  ? 93  TYR C CA    1 
ATOM   3250  C C     . TYR C 1 92  ? 10.428  -35.236 5.274   1.00 32.10  ? 93  TYR C C     1 
ATOM   3251  O O     . TYR C 1 92  ? 9.664   -35.175 4.313   1.00 31.13  ? 93  TYR C O     1 
ATOM   3252  C CB    . TYR C 1 92  ? 11.175  -37.516 6.064   1.00 27.59  ? 93  TYR C CB    1 
ATOM   3253  C CG    . TYR C 1 92  ? 11.163  -38.019 4.626   1.00 29.71  ? 93  TYR C CG    1 
ATOM   3254  C CD1   . TYR C 1 92  ? 11.937  -37.405 3.648   1.00 30.67  ? 93  TYR C CD1   1 
ATOM   3255  C CD2   . TYR C 1 92  ? 10.401  -39.120 4.253   1.00 34.04  ? 93  TYR C CD2   1 
ATOM   3256  C CE1   . TYR C 1 92  ? 11.938  -37.857 2.339   1.00 31.27  ? 93  TYR C CE1   1 
ATOM   3257  C CE2   . TYR C 1 92  ? 10.397  -39.584 2.947   1.00 33.47  ? 93  TYR C CE2   1 
ATOM   3258  C CZ    . TYR C 1 92  ? 11.168  -38.952 1.988   1.00 32.75  ? 93  TYR C CZ    1 
ATOM   3259  O OH    . TYR C 1 92  ? 11.169  -39.405 0.701   1.00 42.79  ? 93  TYR C OH    1 
ATOM   3260  N N     . GLY C 1 93  ? 11.445  -34.389 5.463   1.00 33.12  ? 94  GLY C N     1 
ATOM   3261  C CA    . GLY C 1 93  ? 11.705  -33.282 4.559   1.00 31.93  ? 94  GLY C CA    1 
ATOM   3262  C C     . GLY C 1 93  ? 10.550  -32.285 4.562   1.00 27.35  ? 94  GLY C C     1 
ATOM   3263  O O     . GLY C 1 93  ? 10.098  -31.855 5.620   1.00 30.68  ? 94  GLY C O     1 
ATOM   3264  N N     . HIS C 1 94  ? 10.083  -31.929 3.361   1.00 26.91  ? 95  HIS C N     1 
ATOM   3265  C CA    . HIS C 1 94  ? 8.971   -31.008 3.198   1.00 30.32  ? 95  HIS C CA    1 
ATOM   3266  C C     . HIS C 1 94  ? 7.721   -31.814 2.853   1.00 33.61  ? 95  HIS C C     1 
ATOM   3267  O O     . HIS C 1 94  ? 7.723   -32.597 1.905   1.00 32.01  ? 95  HIS C O     1 
ATOM   3268  C CB    . HIS C 1 94  ? 9.317   -29.946 2.146   1.00 31.72  ? 95  HIS C CB    1 
ATOM   3269  C CG    . HIS C 1 94  ? 8.291   -28.873 1.987   1.00 28.66  ? 95  HIS C CG    1 
ATOM   3270  N ND1   . HIS C 1 94  ? 6.936   -29.099 2.089   1.00 24.99  ? 95  HIS C ND1   1 
ATOM   3271  C CD2   . HIS C 1 94  ? 8.429   -27.568 1.711   1.00 26.58  ? 95  HIS C CD2   1 
ATOM   3272  C CE1   . HIS C 1 94  ? 6.287   -27.961 1.890   1.00 27.14  ? 95  HIS C CE1   1 
ATOM   3273  N NE2   . HIS C 1 94  ? 7.174   -27.017 1.660   1.00 25.79  ? 95  HIS C NE2   1 
ATOM   3274  N N     . PRO C 1 95  ? 6.614   -31.643 3.611   1.00 30.74  ? 96  PRO C N     1 
ATOM   3275  C CA    . PRO C 1 95  ? 5.447   -32.519 3.479   1.00 31.52  ? 96  PRO C CA    1 
ATOM   3276  C C     . PRO C 1 95  ? 4.800   -32.507 2.096   1.00 29.59  ? 96  PRO C C     1 
ATOM   3277  O O     . PRO C 1 95  ? 4.139   -33.470 1.713   1.00 28.93  ? 96  PRO C O     1 
ATOM   3278  C CB    . PRO C 1 95  ? 4.489   -31.991 4.572   1.00 32.06  ? 96  PRO C CB    1 
ATOM   3279  C CG    . PRO C 1 95  ? 4.924   -30.557 4.794   1.00 30.63  ? 96  PRO C CG    1 
ATOM   3280  C CD    . PRO C 1 95  ? 6.428   -30.586 4.615   1.00 31.57  ? 96  PRO C CD    1 
ATOM   3281  N N     . GLY C 1 96  ? 5.009   -31.420 1.347   1.00 27.24  ? 97  GLY C N     1 
ATOM   3282  C CA    . GLY C 1 96  ? 4.324   -31.227 0.080   1.00 28.28  ? 97  GLY C CA    1 
ATOM   3283  C C     . GLY C 1 96  ? 5.292   -31.166 -1.101  1.00 29.89  ? 97  GLY C C     1 
ATOM   3284  O O     . GLY C 1 96  ? 4.920   -30.715 -2.181  1.00 30.96  ? 97  GLY C O     1 
ATOM   3285  N N     . VAL C 1 97  ? 6.528   -31.630 -0.890  1.00 32.48  ? 98  VAL C N     1 
ATOM   3286  C CA    . VAL C 1 97  ? 7.526   -31.651 -1.950  1.00 33.86  ? 98  VAL C CA    1 
ATOM   3287  C C     . VAL C 1 97  ? 7.677   -33.083 -2.456  1.00 29.87  ? 98  VAL C C     1 
ATOM   3288  O O     . VAL C 1 97  ? 8.234   -33.935 -1.768  1.00 27.69  ? 98  VAL C O     1 
ATOM   3289  C CB    . VAL C 1 97  ? 8.877   -31.078 -1.481  1.00 29.88  ? 98  VAL C CB    1 
ATOM   3290  C CG1   . VAL C 1 97  ? 9.996   -31.379 -2.472  1.00 32.33  ? 98  VAL C CG1   1 
ATOM   3291  C CG2   . VAL C 1 97  ? 8.792   -29.581 -1.205  1.00 27.78  ? 98  VAL C CG2   1 
ATOM   3292  N N     . PHE C 1 98  ? 7.184   -33.328 -3.676  1.00 30.99  ? 99  PHE C N     1 
ATOM   3293  C CA    . PHE C 1 98  ? 7.189   -34.662 -4.254  1.00 31.98  ? 99  PHE C CA    1 
ATOM   3294  C C     . PHE C 1 98  ? 6.518   -35.621 -3.276  1.00 29.99  ? 99  PHE C C     1 
ATOM   3295  O O     . PHE C 1 98  ? 7.018   -36.716 -3.027  1.00 34.00  ? 99  PHE C O     1 
ATOM   3296  C CB    . PHE C 1 98  ? 8.620   -35.089 -4.600  1.00 33.60  ? 99  PHE C CB    1 
ATOM   3297  C CG    . PHE C 1 98  ? 9.196   -34.420 -5.841  1.00 34.60  ? 99  PHE C CG    1 
ATOM   3298  C CD1   . PHE C 1 98  ? 9.764   -33.152 -5.774  1.00 32.73  ? 99  PHE C CD1   1 
ATOM   3299  C CD2   . PHE C 1 98  ? 9.175   -35.066 -7.073  1.00 38.75  ? 99  PHE C CD2   1 
ATOM   3300  C CE1   . PHE C 1 98  ? 10.284  -32.547 -6.908  1.00 35.98  ? 99  PHE C CE1   1 
ATOM   3301  C CE2   . PHE C 1 98  ? 9.701   -34.458 -8.202  1.00 34.51  ? 99  PHE C CE2   1 
ATOM   3302  C CZ    . PHE C 1 98  ? 10.254  -33.201 -8.117  1.00 33.91  ? 99  PHE C CZ    1 
ATOM   3303  N N     . ALA C 1 99  ? 5.384   -35.179 -2.722  1.00 27.79  ? 100 ALA C N     1 
ATOM   3304  C CA    . ALA C 1 99  ? 4.596   -35.982 -1.803  1.00 28.84  ? 100 ALA C CA    1 
ATOM   3305  C C     . ALA C 1 99  ? 3.119   -35.646 -1.988  1.00 30.10  ? 100 ALA C C     1 
ATOM   3306  O O     . ALA C 1 99  ? 2.722   -34.489 -1.868  1.00 38.17  ? 100 ALA C O     1 
ATOM   3307  C CB    . ALA C 1 99  ? 5.054   -35.741 -0.382  1.00 26.99  ? 100 ALA C CB    1 
ATOM   3308  N N     . CYS C 1 100 ? 2.317   -36.674 -2.280  1.00 30.52  ? 101 CYS C N     1 
ATOM   3309  C CA    . CYS C 1 100 ? 0.933   -36.487 -2.679  1.00 32.52  ? 101 CYS C CA    1 
ATOM   3310  C C     . CYS C 1 100 ? -0.008  -36.783 -1.514  1.00 32.23  ? 101 CYS C C     1 
ATOM   3311  O O     . CYS C 1 100 ? -1.184  -36.430 -1.558  1.00 30.32  ? 101 CYS C O     1 
ATOM   3312  C CB    . CYS C 1 100 ? 0.586   -37.389 -3.857  1.00 37.59  ? 101 CYS C CB    1 
ATOM   3313  S SG    . CYS C 1 100 ? 0.869   -39.147 -3.521  1.00 36.56  ? 101 CYS C SG    1 
ATOM   3314  N N     . VAL C 1 101 ? 0.520   -37.443 -0.479  1.00 34.37  ? 102 VAL C N     1 
ATOM   3315  C CA    . VAL C 1 101 ? -0.291  -37.861 0.652   1.00 31.49  ? 102 VAL C CA    1 
ATOM   3316  C C     . VAL C 1 101 ? -0.882  -36.625 1.324   1.00 29.64  ? 102 VAL C C     1 
ATOM   3317  O O     . VAL C 1 101 ? -2.100  -36.500 1.442   1.00 26.48  ? 102 VAL C O     1 
ATOM   3318  C CB    . VAL C 1 101 ? 0.518   -38.712 1.650   1.00 36.48  ? 102 VAL C CB    1 
ATOM   3319  C CG1   . VAL C 1 101 ? -0.245  -38.940 2.950   1.00 41.64  ? 102 VAL C CG1   1 
ATOM   3320  C CG2   . VAL C 1 101 ? 0.946   -40.041 1.040   1.00 38.46  ? 102 VAL C CG2   1 
ATOM   3321  N N     . SER C 1 102 ? -0.004  -35.714 1.755   1.00 25.47  ? 103 SER C N     1 
ATOM   3322  C CA    . SER C 1 102 ? -0.421  -34.524 2.478   1.00 26.28  ? 103 SER C CA    1 
ATOM   3323  C C     . SER C 1 102 ? -1.432  -33.732 1.654   1.00 26.30  ? 103 SER C C     1 
ATOM   3324  O O     . SER C 1 102 ? -2.541  -33.473 2.116   1.00 30.32  ? 103 SER C O     1 
ATOM   3325  C CB    . SER C 1 102 ? 0.761   -33.671 2.860   1.00 28.69  ? 103 SER C CB    1 
ATOM   3326  O OG    . SER C 1 102 ? 1.501   -34.271 3.914   1.00 30.58  ? 103 SER C OG    1 
ATOM   3327  N N     . HIS C 1 103 ? -1.037  -33.354 0.433   1.00 27.95  ? 104 HIS C N     1 
ATOM   3328  C CA    . HIS C 1 103 ? -1.886  -32.550 -0.432  1.00 26.74  ? 104 HIS C CA    1 
ATOM   3329  C C     . HIS C 1 103 ? -3.241  -33.230 -0.605  1.00 29.04  ? 104 HIS C C     1 
ATOM   3330  O O     . HIS C 1 103 ? -4.268  -32.560 -0.687  1.00 33.22  ? 104 HIS C O     1 
ATOM   3331  C CB    . HIS C 1 103 ? -1.213  -32.296 -1.787  1.00 26.23  ? 104 HIS C CB    1 
ATOM   3332  C CG    . HIS C 1 103 ? -0.067  -31.341 -1.733  1.00 23.37  ? 104 HIS C CG    1 
ATOM   3333  N ND1   . HIS C 1 103 ? 1.252   -31.739 -1.782  1.00 21.20  ? 104 HIS C ND1   1 
ATOM   3334  C CD2   . HIS C 1 103 ? -0.047  -30.002 -1.675  1.00 20.96  ? 104 HIS C CD2   1 
ATOM   3335  C CE1   . HIS C 1 103 ? 2.032   -30.668 -1.731  1.00 19.86  ? 104 HIS C CE1   1 
ATOM   3336  N NE2   . HIS C 1 103 ? 1.263   -29.603 -1.662  1.00 18.26  ? 104 HIS C NE2   1 
ATOM   3337  N N     . MET C 1 104 ? -3.229  -34.566 -0.672  1.00 30.60  ? 105 MET C N     1 
ATOM   3338  C CA    . MET C 1 104 ? -4.446  -35.335 -0.875  1.00 32.97  ? 105 MET C CA    1 
ATOM   3339  C C     . MET C 1 104 ? -5.270  -35.340 0.410   1.00 29.25  ? 105 MET C C     1 
ATOM   3340  O O     . MET C 1 104 ? -6.498  -35.315 0.365   1.00 27.03  ? 105 MET C O     1 
ATOM   3341  C CB    . MET C 1 104 ? -4.129  -36.776 -1.292  1.00 35.28  ? 105 MET C CB    1 
ATOM   3342  C CG    . MET C 1 104 ? -3.622  -36.909 -2.714  1.00 39.52  ? 105 MET C CG    1 
ATOM   3343  S SD    . MET C 1 104 ? -3.199  -38.608 -3.148  1.00 42.36  ? 105 MET C SD    1 
ATOM   3344  C CE    . MET C 1 104 ? -4.800  -39.415 -3.008  1.00 52.98  ? 105 MET C CE    1 
ATOM   3345  N N     . ALA C 1 105 ? -4.581  -35.373 1.554   1.00 28.58  ? 106 ALA C N     1 
ATOM   3346  C CA    . ALA C 1 105 ? -5.245  -35.389 2.845   1.00 25.57  ? 106 ALA C CA    1 
ATOM   3347  C C     . ALA C 1 105 ? -5.865  -34.021 3.124   1.00 26.83  ? 106 ALA C C     1 
ATOM   3348  O O     . ALA C 1 105 ? -7.001  -33.933 3.585   1.00 26.66  ? 106 ALA C O     1 
ATOM   3349  C CB    . ALA C 1 105 ? -4.266  -35.789 3.926   1.00 26.37  ? 106 ALA C CB    1 
ATOM   3350  N N     . ILE C 1 106 ? -5.113  -32.958 2.819   1.00 27.29  ? 107 ILE C N     1 
ATOM   3351  C CA    . ILE C 1 106 ? -5.563  -31.601 3.084   1.00 28.08  ? 107 ILE C CA    1 
ATOM   3352  C C     . ILE C 1 106 ? -6.758  -31.279 2.189   1.00 30.65  ? 107 ILE C C     1 
ATOM   3353  O O     . ILE C 1 106 ? -7.735  -30.689 2.645   1.00 36.19  ? 107 ILE C O     1 
ATOM   3354  C CB    . ILE C 1 106 ? -4.421  -30.587 2.889   1.00 25.27  ? 107 ILE C CB    1 
ATOM   3355  C CG1   . ILE C 1 106 ? -3.323  -30.768 3.936   1.00 25.11  ? 107 ILE C CG1   1 
ATOM   3356  C CG2   . ILE C 1 106 ? -4.961  -29.157 2.884   1.00 24.27  ? 107 ILE C CG2   1 
ATOM   3357  C CD1   . ILE C 1 106 ? -2.226  -29.722 3.866   1.00 23.67  ? 107 ILE C CD1   1 
ATOM   3358  N N     . THR C 1 107 ? -6.664  -31.666 0.913   1.00 34.96  ? 108 THR C N     1 
ATOM   3359  C CA    . THR C 1 107 ? -7.711  -31.376 -0.053  1.00 38.17  ? 108 THR C CA    1 
ATOM   3360  C C     . THR C 1 107 ? -9.008  -32.051 0.383   1.00 40.14  ? 108 THR C C     1 
ATOM   3361  O O     . THR C 1 107 ? -10.073 -31.438 0.349   1.00 45.11  ? 108 THR C O     1 
ATOM   3362  C CB    . THR C 1 107 ? -7.279  -31.838 -1.444  1.00 40.36  ? 108 THR C CB    1 
ATOM   3363  O OG1   . THR C 1 107 ? -6.197  -30.986 -1.806  1.00 39.74  ? 108 THR C OG1   1 
ATOM   3364  C CG2   . THR C 1 107 ? -8.394  -31.722 -2.467  1.00 41.69  ? 108 THR C CG2   1 
ATOM   3365  N N     . ARG C 1 108 ? -8.906  -33.322 0.786   1.00 42.55  ? 109 ARG C N     1 
ATOM   3366  C CA    . ARG C 1 108 ? -10.073 -34.106 1.152   1.00 39.44  ? 109 ARG C CA    1 
ATOM   3367  C C     . ARG C 1 108 ? -10.631 -33.594 2.478   1.00 35.64  ? 109 ARG C C     1 
ATOM   3368  O O     . ARG C 1 108 ? -11.839 -33.631 2.704   1.00 31.71  ? 109 ARG C O     1 
ATOM   3369  C CB    . ARG C 1 108 ? -9.716  -35.595 1.227   1.00 43.23  ? 109 ARG C CB    1 
ATOM   3370  C CG    . ARG C 1 108 ? -10.923 -36.516 1.341   1.00 46.25  ? 109 ARG C CG    1 
ATOM   3371  C CD    . ARG C 1 108 ? -10.538 -37.987 1.282   1.00 48.86  ? 109 ARG C CD    1 
ATOM   3372  N NE    . ARG C 1 108 ? -9.817  -38.322 0.049   1.00 49.89  ? 109 ARG C NE    1 
ATOM   3373  C CZ    . ARG C 1 108 ? -9.388  -39.537 -0.270  1.00 51.50  ? 109 ARG C CZ    1 
ATOM   3374  N NH1   . ARG C 1 108 ? -9.627  -40.555 0.537   1.00 52.56  ? 109 ARG C NH1   1 
ATOM   3375  N NH2   . ARG C 1 108 ? -8.727  -39.729 -1.397  1.00 53.56  ? 109 ARG C NH2   1 
ATOM   3376  N N     . ALA C 1 109 ? -9.735  -33.109 3.344   1.00 31.87  ? 110 ALA C N     1 
ATOM   3377  C CA    . ALA C 1 109 ? -10.122 -32.599 4.649   1.00 34.22  ? 110 ALA C CA    1 
ATOM   3378  C C     . ALA C 1 109 ? -11.004 -31.364 4.484   1.00 35.00  ? 110 ALA C C     1 
ATOM   3379  O O     . ALA C 1 109 ? -12.050 -31.253 5.121   1.00 36.40  ? 110 ALA C O     1 
ATOM   3380  C CB    . ALA C 1 109 ? -8.888  -32.296 5.470   1.00 31.73  ? 110 ALA C CB    1 
ATOM   3381  N N     . LYS C 1 110 ? -10.569 -30.441 3.619   1.00 37.67  ? 111 LYS C N     1 
ATOM   3382  C CA    . LYS C 1 110 ? -11.301 -29.209 3.374   1.00 40.83  ? 111 LYS C CA    1 
ATOM   3383  C C     . LYS C 1 110 ? -12.656 -29.535 2.752   1.00 41.47  ? 111 LYS C C     1 
ATOM   3384  O O     . LYS C 1 110 ? -13.668 -28.936 3.111   1.00 38.60  ? 111 LYS C O     1 
ATOM   3385  C CB    . LYS C 1 110 ? -10.500 -28.274 2.459   1.00 45.09  ? 111 LYS C CB    1 
ATOM   3386  C CG    . LYS C 1 110 ? -9.216  -27.718 3.062   1.00 46.60  ? 111 LYS C CG    1 
ATOM   3387  C CD    . LYS C 1 110 ? -8.470  -26.761 2.140   1.00 49.07  ? 111 LYS C CD    1 
ATOM   3388  C CE    . LYS C 1 110 ? -7.239  -26.192 2.774   1.00 50.73  ? 111 LYS C CE    1 
ATOM   3389  N NZ    . LYS C 1 110 ? -7.555  -25.444 3.993   1.00 53.40  ? 111 LYS C NZ    1 
ATOM   3390  N N     . ALA C 1 111 ? -12.658 -30.492 1.819   1.00 41.93  ? 112 ALA C N     1 
ATOM   3391  C CA    . ALA C 1 111 ? -13.863 -30.863 1.095   1.00 44.05  ? 112 ALA C CA    1 
ATOM   3392  C C     . ALA C 1 111 ? -14.927 -31.360 2.071   1.00 40.72  ? 112 ALA C C     1 
ATOM   3393  O O     . ALA C 1 111 ? -16.119 -31.184 1.834   1.00 39.89  ? 112 ALA C O     1 
ATOM   3394  C CB    . ALA C 1 111 ? -13.536 -31.910 0.052   1.00 43.64  ? 112 ALA C CB    1 
ATOM   3395  N N     . GLU C 1 112 ? -14.477 -31.979 3.168   1.00 40.87  ? 113 GLU C N     1 
ATOM   3396  C CA    . GLU C 1 112 ? -15.379 -32.521 4.171   1.00 40.99  ? 113 GLU C CA    1 
ATOM   3397  C C     . GLU C 1 112 ? -15.593 -31.487 5.273   1.00 42.64  ? 113 GLU C C     1 
ATOM   3398  O O     . GLU C 1 112 ? -16.192 -31.788 6.303   1.00 41.62  ? 113 GLU C O     1 
ATOM   3399  C CB    . GLU C 1 112 ? -14.828 -33.835 4.725   1.00 46.19  ? 113 GLU C CB    1 
ATOM   3400  C CG    . GLU C 1 112 ? -14.650 -34.910 3.656   1.00 49.46  ? 113 GLU C CG    1 
ATOM   3401  C CD    . GLU C 1 112 ? -14.139 -36.240 4.181   1.00 55.74  ? 113 GLU C CD    1 
ATOM   3402  O OE1   . GLU C 1 112 ? -13.985 -36.374 5.414   1.00 62.92  ? 113 GLU C OE1   1 
ATOM   3403  O OE2   . GLU C 1 112 ? -13.887 -37.141 3.354   1.00 56.57  ? 113 GLU C OE2   1 
ATOM   3404  N N     . GLY C 1 113 ? -15.079 -30.272 5.045   1.00 39.88  ? 114 GLY C N     1 
ATOM   3405  C CA    . GLY C 1 113 ? -15.355 -29.135 5.908   1.00 40.74  ? 114 GLY C CA    1 
ATOM   3406  C C     . GLY C 1 113 ? -14.517 -29.159 7.184   1.00 40.21  ? 114 GLY C C     1 
ATOM   3407  O O     . GLY C 1 113 ? -14.945 -28.648 8.217   1.00 39.36  ? 114 GLY C O     1 
ATOM   3408  N N     . PHE C 1 114 ? -13.315 -29.739 7.100   1.00 37.37  ? 115 PHE C N     1 
ATOM   3409  C CA    . PHE C 1 114 ? -12.411 -29.778 8.238   1.00 36.95  ? 115 PHE C CA    1 
ATOM   3410  C C     . PHE C 1 114 ? -11.314 -28.734 8.047   1.00 33.82  ? 115 PHE C C     1 
ATOM   3411  O O     . PHE C 1 114 ? -11.013 -28.336 6.925   1.00 35.17  ? 115 PHE C O     1 
ATOM   3412  C CB    . PHE C 1 114 ? -11.808 -31.173 8.435   1.00 36.25  ? 115 PHE C CB    1 
ATOM   3413  C CG    . PHE C 1 114 ? -12.807 -32.239 8.865   1.00 40.80  ? 115 PHE C CG    1 
ATOM   3414  C CD1   . PHE C 1 114 ? -13.346 -32.233 10.147  1.00 39.68  ? 115 PHE C CD1   1 
ATOM   3415  C CD2   . PHE C 1 114 ? -13.179 -33.263 8.001   1.00 38.74  ? 115 PHE C CD2   1 
ATOM   3416  C CE1   . PHE C 1 114 ? -14.251 -33.206 10.540  1.00 40.65  ? 115 PHE C CE1   1 
ATOM   3417  C CE2   . PHE C 1 114 ? -14.082 -34.236 8.402   1.00 38.33  ? 115 PHE C CE2   1 
ATOM   3418  C CZ    . PHE C 1 114 ? -14.615 -34.205 9.668   1.00 37.35  ? 115 PHE C CZ    1 
ATOM   3419  N N     . SER C 1 115 ? -10.734 -28.294 9.168   1.00 31.47  ? 116 SER C N     1 
ATOM   3420  C CA    . SER C 1 115 ? -9.597  -27.391 9.151   1.00 35.13  ? 116 SER C CA    1 
ATOM   3421  C C     . SER C 1 115 ? -8.324  -28.185 8.871   1.00 32.28  ? 116 SER C C     1 
ATOM   3422  O O     . SER C 1 115 ? -7.996  -29.116 9.603   1.00 27.30  ? 116 SER C O     1 
ATOM   3423  C CB    . SER C 1 115 ? -9.490  -26.626 10.448  1.00 32.53  ? 116 SER C CB    1 
ATOM   3424  O OG    . SER C 1 115 ? -8.336  -25.797 10.460  1.00 35.16  ? 116 SER C OG    1 
ATOM   3425  N N     . ALA C 1 116 ? -7.618  -27.808 7.801   1.00 31.64  ? 117 ALA C N     1 
ATOM   3426  C CA    . ALA C 1 116 ? -6.413  -28.511 7.395   1.00 33.13  ? 117 ALA C CA    1 
ATOM   3427  C C     . ALA C 1 116 ? -5.448  -27.542 6.720   1.00 35.32  ? 117 ALA C C     1 
ATOM   3428  O O     . ALA C 1 116 ? -5.831  -26.808 5.812   1.00 36.11  ? 117 ALA C O     1 
ATOM   3429  C CB    . ALA C 1 116 ? -6.774  -29.660 6.480   1.00 35.70  ? 117 ALA C CB    1 
ATOM   3430  N N     . LYS C 1 117 ? -4.191  -27.558 7.176   1.00 35.50  ? 118 LYS C N     1 
ATOM   3431  C CA    . LYS C 1 117 ? -3.153  -26.723 6.598   1.00 32.53  ? 118 LYS C CA    1 
ATOM   3432  C C     . LYS C 1 117 ? -1.852  -27.518 6.515   1.00 29.52  ? 118 LYS C C     1 
ATOM   3433  O O     . LYS C 1 117 ? -1.749  -28.614 7.058   1.00 27.74  ? 118 LYS C O     1 
ATOM   3434  C CB    . LYS C 1 117 ? -2.962  -25.444 7.422   1.00 35.62  ? 118 LYS C CB    1 
ATOM   3435  C CG    . LYS C 1 117 ? -2.461  -25.657 8.845   1.00 37.14  ? 118 LYS C CG    1 
ATOM   3436  C CD    . LYS C 1 117 ? -2.179  -24.359 9.594   1.00 41.89  ? 118 LYS C CD    1 
ATOM   3437  C CE    . LYS C 1 117 ? -1.641  -24.588 10.970  1.00 42.97  ? 118 LYS C CE    1 
ATOM   3438  N NZ    . LYS C 1 117 ? -1.329  -23.324 11.640  1.00 40.84  ? 118 LYS C NZ    1 
ATOM   3439  N N     . MET C 1 118 ? -0.865  -26.945 5.821   1.00 31.63  ? 119 MET C N     1 
ATOM   3440  C CA    . MET C 1 118 ? 0.432   -27.576 5.659   1.00 31.89  ? 119 MET C CA    1 
ATOM   3441  C C     . MET C 1 118 ? 1.525   -26.593 6.064   1.00 30.17  ? 119 MET C C     1 
ATOM   3442  O O     . MET C 1 118 ? 1.566   -25.466 5.575   1.00 27.57  ? 119 MET C O     1 
ATOM   3443  C CB    . MET C 1 118 ? 0.651   -28.013 4.206   1.00 33.66  ? 119 MET C CB    1 
ATOM   3444  C CG    . MET C 1 118 ? 2.059   -28.496 3.907   1.00 36.93  ? 119 MET C CG    1 
ATOM   3445  S SD    . MET C 1 118 ? 2.297   -28.896 2.164   1.00 37.58  ? 119 MET C SD    1 
ATOM   3446  C CE    . MET C 1 118 ? 0.970   -30.085 1.927   1.00 34.89  ? 119 MET C CE    1 
ATOM   3447  N N     . GLU C 1 119 ? 2.394   -27.032 6.980   1.00 30.81  ? 120 GLU C N     1 
ATOM   3448  C CA    . GLU C 1 119 ? 3.557   -26.255 7.372   1.00 34.50  ? 120 GLU C CA    1 
ATOM   3449  C C     . GLU C 1 119 ? 4.741   -26.681 6.511   1.00 33.87  ? 120 GLU C C     1 
ATOM   3450  O O     . GLU C 1 119 ? 4.995   -27.872 6.345   1.00 32.22  ? 120 GLU C O     1 
ATOM   3451  C CB    . GLU C 1 119 ? 3.876   -26.447 8.855   1.00 34.39  ? 120 GLU C CB    1 
ATOM   3452  C CG    . GLU C 1 119 ? 2.830   -25.848 9.790   1.00 38.55  ? 120 GLU C CG    1 
ATOM   3453  C CD    . GLU C 1 119 ? 2.653   -24.347 9.652   1.00 39.67  ? 120 GLU C CD    1 
ATOM   3454  O OE1   . GLU C 1 119 ? 3.663   -23.618 9.760   1.00 47.19  ? 120 GLU C OE1   1 
ATOM   3455  O OE2   . GLU C 1 119 ? 1.503   -23.905 9.446   1.00 42.08  ? 120 GLU C OE2   1 
ATOM   3456  N N     . PRO C 1 120 ? 5.490   -25.721 5.925   1.00 35.21  ? 121 PRO C N     1 
ATOM   3457  C CA    . PRO C 1 120 ? 6.652   -26.053 5.101   1.00 35.15  ? 121 PRO C CA    1 
ATOM   3458  C C     . PRO C 1 120 ? 7.801   -26.606 5.940   1.00 34.85  ? 121 PRO C C     1 
ATOM   3459  O O     . PRO C 1 120 ? 7.974   -26.222 7.095   1.00 35.21  ? 121 PRO C O     1 
ATOM   3460  C CB    . PRO C 1 120 ? 7.000   -24.712 4.430   1.00 37.48  ? 121 PRO C CB    1 
ATOM   3461  C CG    . PRO C 1 120 ? 6.501   -23.668 5.409   1.00 38.79  ? 121 PRO C CG    1 
ATOM   3462  C CD    . PRO C 1 120 ? 5.250   -24.274 6.025   1.00 37.25  ? 121 PRO C CD    1 
ATOM   3463  N N     . GLY C 1 121 ? 8.568   -27.524 5.346   1.00 34.47  ? 122 GLY C N     1 
ATOM   3464  C CA    . GLY C 1 121 ? 9.729   -28.103 5.999   1.00 30.37  ? 122 GLY C CA    1 
ATOM   3465  C C     . GLY C 1 121 ? 10.967  -27.979 5.116   1.00 27.86  ? 122 GLY C C     1 
ATOM   3466  O O     . GLY C 1 121 ? 10.922  -27.341 4.066   1.00 27.37  ? 122 GLY C O     1 
ATOM   3467  N N     . ILE C 1 122 ? 12.068  -28.595 5.556   1.00 26.19  ? 123 ILE C N     1 
ATOM   3468  C CA    . ILE C 1 122 ? 13.318  -28.562 4.816   1.00 27.50  ? 123 ILE C CA    1 
ATOM   3469  C C     . ILE C 1 122 ? 13.412  -29.820 3.955   1.00 27.07  ? 123 ILE C C     1 
ATOM   3470  O O     . ILE C 1 122 ? 13.477  -30.930 4.477   1.00 24.47  ? 123 ILE C O     1 
ATOM   3471  C CB    . ILE C 1 122 ? 14.516  -28.427 5.773   1.00 28.70  ? 123 ILE C CB    1 
ATOM   3472  C CG1   . ILE C 1 122 ? 14.398  -27.172 6.641   1.00 35.84  ? 123 ILE C CG1   1 
ATOM   3473  C CG2   . ILE C 1 122 ? 15.836  -28.459 5.002   1.00 28.64  ? 123 ILE C CG2   1 
ATOM   3474  C CD1   . ILE C 1 122 ? 15.535  -26.991 7.629   1.00 36.70  ? 123 ILE C CD1   1 
ATOM   3475  N N     . SER C 1 123 ? 13.425  -29.622 2.632   1.00 26.52  ? 124 SER C N     1 
ATOM   3476  C CA    . SER C 1 123 ? 13.396  -30.722 1.682   1.00 27.03  ? 124 SER C CA    1 
ATOM   3477  C C     . SER C 1 123 ? 14.815  -31.103 1.267   1.00 27.44  ? 124 SER C C     1 
ATOM   3478  O O     . SER C 1 123 ? 15.762  -30.355 1.500   1.00 25.93  ? 124 SER C O     1 
ATOM   3479  C CB    . SER C 1 123 ? 12.558  -30.372 0.479   1.00 28.86  ? 124 SER C CB    1 
ATOM   3480  O OG    . SER C 1 123 ? 13.074  -29.228 -0.187  1.00 28.70  ? 124 SER C OG    1 
ATOM   3481  N N     . ALA C 1 124 ? 14.939  -32.276 0.637   1.00 27.52  ? 125 ALA C N     1 
ATOM   3482  C CA    . ALA C 1 124 ? 16.222  -32.773 0.169   1.00 29.04  ? 125 ALA C CA    1 
ATOM   3483  C C     . ALA C 1 124 ? 16.852  -31.763 -0.786  1.00 26.75  ? 125 ALA C C     1 
ATOM   3484  O O     . ALA C 1 124 ? 18.070  -31.719 -0.937  1.00 25.55  ? 125 ALA C O     1 
ATOM   3485  C CB    . ALA C 1 124 ? 16.042  -34.122 -0.491  1.00 27.22  ? 125 ALA C CB    1 
ATOM   3486  N N     . GLU C 1 125 ? 16.000  -30.962 -1.433  1.00 28.66  ? 126 GLU C N     1 
ATOM   3487  C CA    . GLU C 1 125 ? 16.455  -29.915 -2.331  1.00 31.76  ? 126 GLU C CA    1 
ATOM   3488  C C     . GLU C 1 125 ? 17.185  -28.844 -1.524  1.00 32.74  ? 126 GLU C C     1 
ATOM   3489  O O     . GLU C 1 125 ? 18.284  -28.428 -1.883  1.00 33.20  ? 126 GLU C O     1 
ATOM   3490  C CB    . GLU C 1 125 ? 15.260  -29.331 -3.083  1.00 36.01  ? 126 GLU C CB    1 
ATOM   3491  C CG    . GLU C 1 125 ? 15.616  -28.141 -3.969  1.00 38.69  ? 126 GLU C CG    1 
ATOM   3492  C CD    . GLU C 1 125 ? 14.455  -27.637 -4.806  1.00 44.55  ? 126 GLU C CD    1 
ATOM   3493  O OE1   . GLU C 1 125 ? 13.949  -28.417 -5.640  1.00 51.90  ? 126 GLU C OE1   1 
ATOM   3494  O OE2   . GLU C 1 125 ? 14.052  -26.470 -4.621  1.00 55.82  ? 126 GLU C OE2   1 
ATOM   3495  N N     . ALA C 1 126 ? 16.559  -28.418 -0.423  1.00 33.40  ? 127 ALA C N     1 
ATOM   3496  C CA    . ALA C 1 126 ? 17.113  -27.381 0.432   1.00 33.12  ? 127 ALA C CA    1 
ATOM   3497  C C     . ALA C 1 126 ? 18.480  -27.813 0.957   1.00 28.28  ? 127 ALA C C     1 
ATOM   3498  O O     . ALA C 1 126 ? 19.389  -26.995 1.076   1.00 29.44  ? 127 ALA C O     1 
ATOM   3499  C CB    . ALA C 1 126 ? 16.154  -27.084 1.565   1.00 30.41  ? 127 ALA C CB    1 
ATOM   3500  N N     . CYS C 1 127 ? 18.607  -29.107 1.271   1.00 25.54  ? 128 CYS C N     1 
ATOM   3501  C CA    . CYS C 1 127 ? 19.843  -29.655 1.803   1.00 26.74  ? 128 CYS C CA    1 
ATOM   3502  C C     . CYS C 1 127 ? 20.923  -29.642 0.724   1.00 30.64  ? 128 CYS C C     1 
ATOM   3503  O O     . CYS C 1 127 ? 22.083  -29.345 1.002   1.00 26.19  ? 128 CYS C O     1 
ATOM   3504  C CB    . CYS C 1 127 ? 19.634  -31.072 2.323   1.00 28.18  ? 128 CYS C CB    1 
ATOM   3505  S SG    . CYS C 1 127 ? 18.425  -31.177 3.668   1.00 33.45  ? 128 CYS C SG    1 
ATOM   3506  N N     . LEU C 1 128 ? 20.517  -29.964 -0.508  1.00 33.89  ? 129 LEU C N     1 
ATOM   3507  C CA    . LEU C 1 128 ? 21.437  -30.072 -1.628  1.00 34.10  ? 129 LEU C CA    1 
ATOM   3508  C C     . LEU C 1 128 ? 22.157  -28.742 -1.836  1.00 31.46  ? 129 LEU C C     1 
ATOM   3509  O O     . LEU C 1 128 ? 23.374  -28.711 -2.004  1.00 27.64  ? 129 LEU C O     1 
ATOM   3510  C CB    . LEU C 1 128 ? 20.659  -30.496 -2.873  1.00 36.42  ? 129 LEU C CB    1 
ATOM   3511  C CG    . LEU C 1 128 ? 21.486  -30.718 -4.143  1.00 37.03  ? 129 LEU C CG    1 
ATOM   3512  C CD1   . LEU C 1 128 ? 20.616  -31.256 -5.266  1.00 38.24  ? 129 LEU C CD1   1 
ATOM   3513  C CD2   . LEU C 1 128 ? 22.179  -29.439 -4.574  1.00 39.09  ? 129 LEU C CD2   1 
ATOM   3514  N N     . TRP C 1 129 ? 21.386  -27.649 -1.826  1.00 31.32  ? 130 TRP C N     1 
ATOM   3515  C CA    . TRP C 1 129 ? 21.924  -26.317 -2.053  1.00 30.91  ? 130 TRP C CA    1 
ATOM   3516  C C     . TRP C 1 129 ? 23.003  -26.001 -1.020  1.00 28.66  ? 130 TRP C C     1 
ATOM   3517  O O     . TRP C 1 129 ? 23.975  -25.312 -1.324  1.00 31.73  ? 130 TRP C O     1 
ATOM   3518  C CB    . TRP C 1 129 ? 20.803  -25.270 -1.993  1.00 31.63  ? 130 TRP C CB    1 
ATOM   3519  C CG    . TRP C 1 129 ? 19.692  -25.490 -2.984  1.00 33.48  ? 130 TRP C CG    1 
ATOM   3520  C CD1   . TRP C 1 129 ? 18.356  -25.335 -2.756  1.00 32.00  ? 130 TRP C CD1   1 
ATOM   3521  C CD2   . TRP C 1 129 ? 19.819  -25.874 -4.371  1.00 33.83  ? 130 TRP C CD2   1 
ATOM   3522  N NE1   . TRP C 1 129 ? 17.643  -25.612 -3.890  1.00 31.35  ? 130 TRP C NE1   1 
ATOM   3523  C CE2   . TRP C 1 129 ? 18.511  -25.941 -4.898  1.00 33.18  ? 130 TRP C CE2   1 
ATOM   3524  C CE3   . TRP C 1 129 ? 20.899  -26.170 -5.211  1.00 31.72  ? 130 TRP C CE3   1 
ATOM   3525  C CZ2   . TRP C 1 129 ? 18.260  -26.291 -6.223  1.00 31.14  ? 130 TRP C CZ2   1 
ATOM   3526  C CZ3   . TRP C 1 129 ? 20.648  -26.514 -6.521  1.00 30.10  ? 130 TRP C CZ3   1 
ATOM   3527  C CH2   . TRP C 1 129 ? 19.347  -26.570 -7.018  1.00 30.64  ? 130 TRP C CH2   1 
ATOM   3528  N N     . ALA C 1 130 ? 22.806  -26.502 0.204   1.00 26.44  ? 131 ALA C N     1 
ATOM   3529  C CA    . ALA C 1 130 ? 23.676  -26.185 1.324   1.00 24.65  ? 131 ALA C CA    1 
ATOM   3530  C C     . ALA C 1 130 ? 24.913  -27.078 1.308   1.00 26.14  ? 131 ALA C C     1 
ATOM   3531  O O     . ALA C 1 130 ? 26.004  -26.635 1.657   1.00 23.95  ? 131 ALA C O     1 
ATOM   3532  C CB    . ALA C 1 130 ? 22.909  -26.330 2.622   1.00 26.48  ? 131 ALA C CB    1 
ATOM   3533  N N     . ASP C 1 131 ? 24.726  -28.340 0.906   1.00 29.63  ? 132 ASP C N     1 
ATOM   3534  C CA    . ASP C 1 131 ? 25.792  -29.329 0.935   1.00 30.20  ? 132 ASP C CA    1 
ATOM   3535  C C     . ASP C 1 131 ? 26.761  -29.088 -0.219  1.00 32.93  ? 132 ASP C C     1 
ATOM   3536  O O     . ASP C 1 131 ? 27.975  -29.172 -0.042  1.00 40.89  ? 132 ASP C O     1 
ATOM   3537  C CB    . ASP C 1 131 ? 25.230  -30.743 0.925   1.00 31.90  ? 132 ASP C CB    1 
ATOM   3538  C CG    . ASP C 1 131 ? 24.767  -31.265 2.278   1.00 30.48  ? 132 ASP C CG    1 
ATOM   3539  O OD1   . ASP C 1 131 ? 25.140  -30.651 3.298   1.00 33.94  ? 132 ASP C OD1   1 
ATOM   3540  O OD2   . ASP C 1 131 ? 24.028  -32.270 2.299   1.00 29.64  ? 132 ASP C OD2   1 
ATOM   3541  N N     . LEU C 1 132 ? 26.213  -28.790 -1.400  1.00 33.23  ? 133 LEU C N     1 
ATOM   3542  C CA    . LEU C 1 132 ? 27.019  -28.629 -2.599  1.00 34.81  ? 133 LEU C CA    1 
ATOM   3543  C C     . LEU C 1 132 ? 27.368  -27.157 -2.800  1.00 38.77  ? 133 LEU C C     1 
ATOM   3544  O O     . LEU C 1 132 ? 28.069  -26.809 -3.748  1.00 46.83  ? 133 LEU C O     1 
ATOM   3545  C CB    . LEU C 1 132 ? 26.271  -29.194 -3.805  1.00 38.57  ? 133 LEU C CB    1 
ATOM   3546  C CG    . LEU C 1 132 ? 26.170  -30.721 -3.876  1.00 36.56  ? 133 LEU C CG    1 
ATOM   3547  C CD1   . LEU C 1 132 ? 25.351  -31.279 -2.725  1.00 39.87  ? 133 LEU C CD1   1 
ATOM   3548  C CD2   . LEU C 1 132 ? 25.588  -31.154 -5.208  1.00 42.25  ? 133 LEU C CD2   1 
ATOM   3549  N N     . GLY C 1 133 ? 26.879  -26.301 -1.898  1.00 36.64  ? 134 GLY C N     1 
ATOM   3550  C CA    . GLY C 1 133 ? 27.105  -24.870 -2.007  1.00 35.95  ? 134 GLY C CA    1 
ATOM   3551  C C     . GLY C 1 133 ? 26.710  -24.358 -3.389  1.00 36.55  ? 134 GLY C C     1 
ATOM   3552  O O     . GLY C 1 133 ? 27.511  -23.731 -4.079  1.00 34.13  ? 134 GLY C O     1 
ATOM   3553  N N     . ILE C 1 134 ? 25.467  -24.650 -3.785  1.00 40.51  ? 135 ILE C N     1 
ATOM   3554  C CA    . ILE C 1 134 ? 24.939  -24.207 -5.065  1.00 38.31  ? 135 ILE C CA    1 
ATOM   3555  C C     . ILE C 1 134 ? 23.717  -23.328 -4.815  1.00 37.43  ? 135 ILE C C     1 
ATOM   3556  O O     . ILE C 1 134 ? 22.852  -23.671 -4.011  1.00 35.72  ? 135 ILE C O     1 
ATOM   3557  C CB    . ILE C 1 134 ? 24.601  -25.407 -5.969  1.00 41.23  ? 135 ILE C CB    1 
ATOM   3558  C CG1   . ILE C 1 134 ? 25.840  -26.247 -6.280  1.00 43.05  ? 135 ILE C CG1   1 
ATOM   3559  C CG2   . ILE C 1 134 ? 23.897  -24.945 -7.246  1.00 44.90  ? 135 ILE C CG2   1 
ATOM   3560  C CD1   . ILE C 1 134 ? 25.569  -27.439 -7.180  1.00 44.40  ? 135 ILE C CD1   1 
ATOM   3561  N N     . ASP C 1 135 ? 23.665  -22.189 -5.513  1.00 32.04  ? 136 ASP C N     1 
ATOM   3562  C CA    . ASP C 1 135 ? 22.538  -21.278 -5.420  1.00 31.98  ? 136 ASP C CA    1 
ATOM   3563  C C     . ASP C 1 135 ? 21.635  -21.488 -6.632  1.00 30.10  ? 136 ASP C C     1 
ATOM   3564  O O     . ASP C 1 135 ? 22.057  -21.287 -7.768  1.00 35.81  ? 136 ASP C O     1 
ATOM   3565  C CB    . ASP C 1 135 ? 23.004  -19.836 -5.286  1.00 28.94  ? 136 ASP C CB    1 
ATOM   3566  C CG    . ASP C 1 135 ? 21.899  -18.792 -5.228  1.00 28.45  ? 136 ASP C CG    1 
ATOM   3567  O OD1   . ASP C 1 135 ? 20.724  -19.168 -5.422  1.00 23.30  ? 136 ASP C OD1   1 
ATOM   3568  O OD2   . ASP C 1 135 ? 22.221  -17.611 -4.979  1.00 31.07  ? 136 ASP C OD2   1 
ATOM   3569  N N     . PRO C 1 136 ? 20.363  -21.896 -6.424  1.00 28.36  ? 137 PRO C N     1 
ATOM   3570  C CA    . PRO C 1 136 ? 19.455  -22.186 -7.535  1.00 31.81  ? 137 PRO C CA    1 
ATOM   3571  C C     . PRO C 1 136 ? 19.232  -20.974 -8.436  1.00 32.69  ? 137 PRO C C     1 
ATOM   3572  O O     . PRO C 1 136 ? 18.819  -21.119 -9.584  1.00 33.12  ? 137 PRO C O     1 
ATOM   3573  C CB    . PRO C 1 136 ? 18.159  -22.639 -6.829  1.00 30.55  ? 137 PRO C CB    1 
ATOM   3574  C CG    . PRO C 1 136 ? 18.254  -22.026 -5.445  1.00 31.29  ? 137 PRO C CG    1 
ATOM   3575  C CD    . PRO C 1 136 ? 19.732  -22.073 -5.108  1.00 28.85  ? 137 PRO C CD    1 
ATOM   3576  N N     . GLY C 1 137 ? 19.517  -19.783 -7.901  1.00 32.19  ? 138 GLY C N     1 
ATOM   3577  C CA    . GLY C 1 137 ? 19.307  -18.542 -8.627  1.00 31.97  ? 138 GLY C CA    1 
ATOM   3578  C C     . GLY C 1 137 ? 20.537  -18.153 -9.443  1.00 32.78  ? 138 GLY C C     1 
ATOM   3579  O O     . GLY C 1 137 ? 20.492  -17.209 -10.228 1.00 32.30  ? 138 GLY C O     1 
ATOM   3580  N N     . ASN C 1 138 ? 21.631  -18.897 -9.253  1.00 32.42  ? 139 ASN C N     1 
ATOM   3581  C CA    . ASN C 1 138 ? 22.884  -18.604 -9.928  1.00 35.07  ? 139 ASN C CA    1 
ATOM   3582  C C     . ASN C 1 138 ? 22.657  -18.591 -11.438 1.00 33.49  ? 139 ASN C C     1 
ATOM   3583  O O     . ASN C 1 138 ? 22.906  -17.585 -12.097 1.00 31.92  ? 139 ASN C O     1 
ATOM   3584  C CB    . ASN C 1 138 ? 23.977  -19.591 -9.538  1.00 38.39  ? 139 ASN C CB    1 
ATOM   3585  C CG    . ASN C 1 138 ? 25.308  -19.235 -10.156 1.00 39.78  ? 139 ASN C CG    1 
ATOM   3586  O OD1   . ASN C 1 138 ? 25.874  -20.028 -10.916 1.00 41.20  ? 139 ASN C OD1   1 
ATOM   3587  N ND2   . ASN C 1 138 ? 25.820  -18.051 -9.849  1.00 40.04  ? 139 ASN C ND2   1 
ATOM   3588  N N     . SER C 1 139 ? 22.187  -19.722 -11.975 1.00 31.58  ? 140 SER C N     1 
ATOM   3589  C CA    . SER C 1 139 ? 21.927  -19.841 -13.400 1.00 33.74  ? 140 SER C CA    1 
ATOM   3590  C C     . SER C 1 139 ? 20.506  -20.346 -13.635 1.00 30.59  ? 140 SER C C     1 
ATOM   3591  O O     . SER C 1 139 ? 20.093  -20.538 -14.776 1.00 34.00  ? 140 SER C O     1 
ATOM   3592  C CB    . SER C 1 139 ? 22.945  -20.737 -14.065 1.00 36.32  ? 140 SER C CB    1 
ATOM   3593  O OG    . SER C 1 139 ? 22.947  -22.033 -13.482 1.00 36.39  ? 140 SER C OG    1 
ATOM   3594  N N     . GLY C 1 140 ? 19.761  -20.540 -12.542 1.00 28.50  ? 141 GLY C N     1 
ATOM   3595  C CA    . GLY C 1 140 ? 18.405  -21.057 -12.615 1.00 28.07  ? 141 GLY C CA    1 
ATOM   3596  C C     . GLY C 1 140 ? 18.337  -22.497 -12.113 1.00 28.42  ? 141 GLY C C     1 
ATOM   3597  O O     . GLY C 1 140 ? 19.363  -23.161 -11.981 1.00 28.29  ? 141 GLY C O     1 
ATOM   3598  N N     . HIS C 1 141 ? 17.113  -22.968 -11.851 1.00 31.92  ? 142 HIS C N     1 
ATOM   3599  C CA    . HIS C 1 141 ? 16.896  -24.286 -11.277 1.00 31.52  ? 142 HIS C CA    1 
ATOM   3600  C C     . HIS C 1 141 ? 15.678  -24.940 -11.925 1.00 28.83  ? 142 HIS C C     1 
ATOM   3601  O O     . HIS C 1 141 ? 14.678  -24.277 -12.189 1.00 31.18  ? 142 HIS C O     1 
ATOM   3602  C CB    . HIS C 1 141 ? 16.737  -24.176 -9.756  1.00 34.60  ? 142 HIS C CB    1 
ATOM   3603  C CG    . HIS C 1 141 ? 16.081  -25.358 -9.125  1.00 34.02  ? 142 HIS C CG    1 
ATOM   3604  N ND1   . HIS C 1 141 ? 15.162  -25.230 -8.107  1.00 38.43  ? 142 HIS C ND1   1 
ATOM   3605  C CD2   . HIS C 1 141 ? 16.175  -26.670 -9.377  1.00 37.70  ? 142 HIS C CD2   1 
ATOM   3606  C CE1   . HIS C 1 141 ? 14.733  -26.432 -7.752  1.00 37.45  ? 142 HIS C CE1   1 
ATOM   3607  N NE2   . HIS C 1 141 ? 15.335  -27.322 -8.509  1.00 38.77  ? 142 HIS C NE2   1 
ATOM   3608  N N     . GLN C 1 142 ? 15.785  -26.250 -12.179 1.00 29.90  ? 143 GLN C N     1 
ATOM   3609  C CA    . GLN C 1 142 ? 14.671  -27.040 -12.678 1.00 30.40  ? 143 GLN C CA    1 
ATOM   3610  C C     . GLN C 1 142 ? 14.631  -28.374 -11.939 1.00 27.42  ? 143 GLN C C     1 
ATOM   3611  O O     . GLN C 1 142 ? 15.664  -29.009 -11.743 1.00 28.67  ? 143 GLN C O     1 
ATOM   3612  C CB    . GLN C 1 142 ? 14.791  -27.335 -14.173 1.00 32.90  ? 143 GLN C CB    1 
ATOM   3613  C CG    . GLN C 1 142 ? 14.869  -26.099 -15.060 1.00 38.99  ? 143 GLN C CG    1 
ATOM   3614  C CD    . GLN C 1 142 ? 14.883  -26.442 -16.533 1.00 40.54  ? 143 GLN C CD    1 
ATOM   3615  O OE1   . GLN C 1 142 ? 14.046  -25.977 -17.314 1.00 43.02  ? 143 GLN C OE1   1 
ATOM   3616  N NE2   . GLN C 1 142 ? 15.836  -27.276 -16.924 1.00 44.75  ? 143 GLN C NE2   1 
ATOM   3617  N N     . SER C 1 143 ? 13.423  -28.795 -11.551 1.00 25.44  ? 144 SER C N     1 
ATOM   3618  C CA    . SER C 1 143 ? 13.228  -30.080 -10.897 1.00 26.70  ? 144 SER C CA    1 
ATOM   3619  C C     . SER C 1 143 ? 12.188  -30.894 -11.662 1.00 23.53  ? 144 SER C C     1 
ATOM   3620  O O     . SER C 1 143 ? 11.180  -30.354 -12.110 1.00 23.93  ? 144 SER C O     1 
ATOM   3621  C CB    . SER C 1 143 ? 12.829  -29.903 -9.455  1.00 26.90  ? 144 SER C CB    1 
ATOM   3622  O OG    . SER C 1 143 ? 13.865  -29.279 -8.709  1.00 31.41  ? 144 SER C OG    1 
ATOM   3623  N N     . PHE C 1 144 ? 12.453  -32.198 -11.806 1.00 23.61  ? 145 PHE C N     1 
ATOM   3624  C CA    . PHE C 1 144 ? 11.537  -33.104 -12.479 1.00 26.64  ? 145 PHE C CA    1 
ATOM   3625  C C     . PHE C 1 144 ? 11.610  -34.481 -11.827 1.00 28.32  ? 145 PHE C C     1 
ATOM   3626  O O     . PHE C 1 144 ? 12.676  -34.915 -11.398 1.00 31.25  ? 145 PHE C O     1 
ATOM   3627  C CB    . PHE C 1 144 ? 11.859  -33.258 -13.968 1.00 30.48  ? 145 PHE C CB    1 
ATOM   3628  C CG    . PHE C 1 144 ? 11.788  -31.977 -14.785 1.00 28.93  ? 145 PHE C CG    1 
ATOM   3629  C CD1   . PHE C 1 144 ? 10.564  -31.467 -15.204 1.00 30.27  ? 145 PHE C CD1   1 
ATOM   3630  C CD2   . PHE C 1 144 ? 12.946  -31.310 -15.166 1.00 30.44  ? 145 PHE C CD2   1 
ATOM   3631  C CE1   . PHE C 1 144 ? 10.503  -30.308 -15.960 1.00 29.98  ? 145 PHE C CE1   1 
ATOM   3632  C CE2   . PHE C 1 144 ? 12.878  -30.151 -15.924 1.00 30.13  ? 145 PHE C CE2   1 
ATOM   3633  C CZ    . PHE C 1 144 ? 11.658  -29.654 -16.319 1.00 29.15  ? 145 PHE C CZ    1 
ATOM   3634  N N     . GLU C 1 145 ? 10.462  -35.162 -11.778 1.00 34.68  ? 146 GLU C N     1 
ATOM   3635  C CA    . GLU C 1 145 ? 10.406  -36.547 -11.344 1.00 33.67  ? 146 GLU C CA    1 
ATOM   3636  C C     . GLU C 1 145 ? 10.939  -37.419 -12.477 1.00 31.42  ? 146 GLU C C     1 
ATOM   3637  O O     . GLU C 1 145 ? 10.342  -37.486 -13.548 1.00 42.34  ? 146 GLU C O     1 
ATOM   3638  C CB    . GLU C 1 145 ? 8.974   -36.907 -10.944 1.00 33.42  ? 146 GLU C CB    1 
ATOM   3639  C CG    . GLU C 1 145 ? 8.883   -38.100 -9.996  1.00 32.89  ? 146 GLU C CG    1 
ATOM   3640  C CD    . GLU C 1 145 ? 8.945   -39.463 -10.659 1.00 31.96  ? 146 GLU C CD    1 
ATOM   3641  O OE1   . GLU C 1 145 ? 8.829   -39.533 -11.902 1.00 26.74  ? 146 GLU C OE1   1 
ATOM   3642  O OE2   . GLU C 1 145 ? 9.112   -40.457 -9.922  1.00 29.70  ? 146 GLU C OE2   1 
ATOM   3643  N N     . ALA C 1 146 ? 12.081  -38.066 -12.227 1.00 28.43  ? 147 ALA C N     1 
ATOM   3644  C CA    . ALA C 1 146 ? 12.803  -38.802 -13.252 1.00 30.12  ? 147 ALA C CA    1 
ATOM   3645  C C     . ALA C 1 146 ? 11.832  -39.429 -14.253 1.00 30.77  ? 147 ALA C C     1 
ATOM   3646  O O     . ALA C 1 146 ? 11.867  -39.109 -15.438 1.00 29.42  ? 147 ALA C O     1 
ATOM   3647  C CB    . ALA C 1 146 ? 13.684  -39.848 -12.606 1.00 30.57  ? 147 ALA C CB    1 
ATOM   3648  N N     . SER C 1 147 ? 10.968  -40.323 -13.759 1.00 29.41  ? 148 SER C N     1 
ATOM   3649  C CA    . SER C 1 147 ? 10.119  -41.134 -14.618 1.00 31.54  ? 148 SER C CA    1 
ATOM   3650  C C     . SER C 1 147 ? 9.186   -40.256 -15.450 1.00 34.96  ? 148 SER C C     1 
ATOM   3651  O O     . SER C 1 147 ? 8.870   -40.595 -16.589 1.00 32.78  ? 148 SER C O     1 
ATOM   3652  C CB    . SER C 1 147 ? 9.343   -42.144 -13.814 1.00 30.23  ? 148 SER C CB    1 
ATOM   3653  O OG    . SER C 1 147 ? 10.206  -43.137 -13.279 1.00 30.48  ? 148 SER C OG    1 
ATOM   3654  N N     . GLN C 1 148 ? 8.741   -39.136 -14.872 1.00 30.77  ? 149 GLN C N     1 
ATOM   3655  C CA    . GLN C 1 148 ? 7.823   -38.243 -15.562 1.00 33.98  ? 149 GLN C CA    1 
ATOM   3656  C C     . GLN C 1 148 ? 8.552   -37.575 -16.725 1.00 34.94  ? 149 GLN C C     1 
ATOM   3657  O O     . GLN C 1 148 ? 7.942   -37.239 -17.738 1.00 33.26  ? 149 GLN C O     1 
ATOM   3658  C CB    . GLN C 1 148 ? 7.247   -37.185 -14.620 1.00 38.04  ? 149 GLN C CB    1 
ATOM   3659  C CG    . GLN C 1 148 ? 6.234   -36.260 -15.286 1.00 39.34  ? 149 GLN C CG    1 
ATOM   3660  C CD    . GLN C 1 148 ? 5.822   -35.096 -14.411 1.00 40.53  ? 149 GLN C CD    1 
ATOM   3661  O OE1   . GLN C 1 148 ? 6.055   -33.928 -14.741 1.00 38.29  ? 149 GLN C OE1   1 
ATOM   3662  N NE2   . GLN C 1 148 ? 5.207   -35.406 -13.279 1.00 46.74  ? 149 GLN C NE2   1 
ATOM   3663  N N     . PHE C 1 149 ? 9.865   -37.388 -16.560 1.00 35.80  ? 150 PHE C N     1 
ATOM   3664  C CA    . PHE C 1 149 ? 10.694  -36.762 -17.576 1.00 39.60  ? 150 PHE C CA    1 
ATOM   3665  C C     . PHE C 1 149 ? 10.844  -37.714 -18.760 1.00 38.81  ? 150 PHE C C     1 
ATOM   3666  O O     . PHE C 1 149 ? 11.079  -37.278 -19.886 1.00 34.99  ? 150 PHE C O     1 
ATOM   3667  C CB    . PHE C 1 149 ? 12.043  -36.389 -16.952 1.00 44.10  ? 150 PHE C CB    1 
ATOM   3668  C CG    . PHE C 1 149 ? 13.046  -35.773 -17.918 1.00 41.72  ? 150 PHE C CG    1 
ATOM   3669  C CD1   . PHE C 1 149 ? 13.841  -36.577 -18.727 1.00 40.95  ? 150 PHE C CD1   1 
ATOM   3670  C CD2   . PHE C 1 149 ? 13.209  -34.394 -17.999 1.00 42.20  ? 150 PHE C CD2   1 
ATOM   3671  C CE1   . PHE C 1 149 ? 14.758  -36.016 -19.602 1.00 37.94  ? 150 PHE C CE1   1 
ATOM   3672  C CE2   . PHE C 1 149 ? 14.129  -33.840 -18.874 1.00 41.42  ? 150 PHE C CE2   1 
ATOM   3673  C CZ    . PHE C 1 149 ? 14.900  -34.651 -19.673 1.00 40.48  ? 150 PHE C CZ    1 
ATOM   3674  N N     . MET C 1 150 ? 10.703  -39.016 -18.487 1.00 37.15  ? 151 MET C N     1 
ATOM   3675  C CA    . MET C 1 150 ? 10.872  -40.043 -19.501 1.00 35.77  ? 151 MET C CA    1 
ATOM   3676  C C     . MET C 1 150 ? 9.542   -40.310 -20.202 1.00 35.98  ? 151 MET C C     1 
ATOM   3677  O O     . MET C 1 150 ? 9.510   -40.547 -21.407 1.00 44.69  ? 151 MET C O     1 
ATOM   3678  C CB    . MET C 1 150 ? 11.383  -41.351 -18.882 1.00 35.21  ? 151 MET C CB    1 
ATOM   3679  C CG    . MET C 1 150 ? 12.804  -41.275 -18.354 1.00 35.52  ? 151 MET C CG    1 
ATOM   3680  S SD    . MET C 1 150 ? 13.367  -42.827 -17.624 1.00 37.09  ? 151 MET C SD    1 
ATOM   3681  C CE    . MET C 1 150 ? 13.463  -43.889 -19.072 1.00 40.85  ? 151 MET C CE    1 
ATOM   3682  N N     . PHE C 1 151 ? 8.449   -40.267 -19.434 1.00 37.48  ? 152 PHE C N     1 
ATOM   3683  C CA    . PHE C 1 151 ? 7.144   -40.670 -19.935 1.00 37.87  ? 152 PHE C CA    1 
ATOM   3684  C C     . PHE C 1 151 ? 6.497   -39.516 -20.696 1.00 38.18  ? 152 PHE C C     1 
ATOM   3685  O O     . PHE C 1 151 ? 5.828   -39.735 -21.703 1.00 42.86  ? 152 PHE C O     1 
ATOM   3686  C CB    . PHE C 1 151 ? 6.267   -41.151 -18.775 1.00 35.54  ? 152 PHE C CB    1 
ATOM   3687  C CG    . PHE C 1 151 ? 6.819   -42.361 -18.035 1.00 34.23  ? 152 PHE C CG    1 
ATOM   3688  C CD1   . PHE C 1 151 ? 7.732   -43.213 -18.647 1.00 35.81  ? 152 PHE C CD1   1 
ATOM   3689  C CD2   . PHE C 1 151 ? 6.413   -42.653 -16.738 1.00 34.63  ? 152 PHE C CD2   1 
ATOM   3690  C CE1   . PHE C 1 151 ? 8.231   -44.317 -17.975 1.00 38.75  ? 152 PHE C CE1   1 
ATOM   3691  C CE2   . PHE C 1 151 ? 6.914   -43.760 -16.072 1.00 37.09  ? 152 PHE C CE2   1 
ATOM   3692  C CZ    . PHE C 1 151 ? 7.821   -44.589 -16.691 1.00 36.74  ? 152 PHE C CZ    1 
ATOM   3693  N N     . PHE C 1 152 ? 6.697   -38.290 -20.203 1.00 38.86  ? 153 PHE C N     1 
ATOM   3694  C CA    . PHE C 1 152 ? 6.068   -37.123 -20.798 1.00 38.49  ? 153 PHE C CA    1 
ATOM   3695  C C     . PHE C 1 152 ? 7.140   -36.218 -21.398 1.00 38.58  ? 153 PHE C C     1 
ATOM   3696  O O     . PHE C 1 152 ? 8.333   -36.441 -21.200 1.00 39.82  ? 153 PHE C O     1 
ATOM   3697  C CB    . PHE C 1 152 ? 5.210   -36.405 -19.752 1.00 37.09  ? 153 PHE C CB    1 
ATOM   3698  C CG    . PHE C 1 152 ? 4.132   -37.282 -19.131 1.00 38.18  ? 153 PHE C CG    1 
ATOM   3699  C CD1   . PHE C 1 152 ? 2.977   -37.599 -19.837 1.00 41.28  ? 153 PHE C CD1   1 
ATOM   3700  C CD2   . PHE C 1 152 ? 4.270   -37.780 -17.840 1.00 37.67  ? 153 PHE C CD2   1 
ATOM   3701  C CE1   . PHE C 1 152 ? 1.997   -38.398 -19.271 1.00 41.10  ? 153 PHE C CE1   1 
ATOM   3702  C CE2   . PHE C 1 152 ? 3.284   -38.576 -17.278 1.00 39.48  ? 153 PHE C CE2   1 
ATOM   3703  C CZ    . PHE C 1 152 ? 2.151   -38.882 -17.994 1.00 40.61  ? 153 PHE C CZ    1 
ATOM   3704  N N     . ASN C 1 153 ? 6.691   -35.193 -22.129 1.00 39.87  ? 154 ASN C N     1 
ATOM   3705  C CA    . ASN C 1 153 ? 7.585   -34.312 -22.859 1.00 38.43  ? 154 ASN C CA    1 
ATOM   3706  C C     . ASN C 1 153 ? 8.014   -33.156 -21.961 1.00 37.43  ? 154 ASN C C     1 
ATOM   3707  O O     . ASN C 1 153 ? 7.226   -32.261 -21.665 1.00 32.16  ? 154 ASN C O     1 
ATOM   3708  C CB    . ASN C 1 153 ? 6.946   -33.819 -24.152 1.00 39.99  ? 154 ASN C CB    1 
ATOM   3709  C CG    . ASN C 1 153 ? 6.713   -34.945 -25.131 1.00 39.29  ? 154 ASN C CG    1 
ATOM   3710  O OD1   . ASN C 1 153 ? 7.651   -35.673 -25.473 1.00 38.07  ? 154 ASN C OD1   1 
ATOM   3711  N ND2   . ASN C 1 153 ? 5.478   -35.115 -25.580 1.00 40.79  ? 154 ASN C ND2   1 
ATOM   3712  N N     . HIS C 1 154 ? 9.280   -33.196 -21.536 1.00 38.22  ? 155 HIS C N     1 
ATOM   3713  C CA    . HIS C 1 154 ? 9.877   -32.123 -20.761 1.00 42.10  ? 155 HIS C CA    1 
ATOM   3714  C C     . HIS C 1 154 ? 11.138  -31.643 -21.470 1.00 41.86  ? 155 HIS C C     1 
ATOM   3715  O O     . HIS C 1 154 ? 11.976  -32.450 -21.866 1.00 43.44  ? 155 HIS C O     1 
ATOM   3716  C CB    . HIS C 1 154 ? 10.173  -32.587 -19.330 1.00 43.01  ? 155 HIS C CB    1 
ATOM   3717  C CG    . HIS C 1 154 ? 8.978   -32.619 -18.437 1.00 46.57  ? 155 HIS C CG    1 
ATOM   3718  N ND1   . HIS C 1 154 ? 8.031   -31.617 -18.420 1.00 46.10  ? 155 HIS C ND1   1 
ATOM   3719  C CD2   . HIS C 1 154 ? 8.596   -33.504 -17.504 1.00 50.04  ? 155 HIS C CD2   1 
ATOM   3720  C CE1   . HIS C 1 154 ? 7.103   -31.908 -17.520 1.00 46.72  ? 155 HIS C CE1   1 
ATOM   3721  N NE2   . HIS C 1 154 ? 7.425   -33.051 -16.954 1.00 46.90  ? 155 HIS C NE2   1 
ATOM   3722  N N     . VAL C 1 155 ? 11.254  -30.322 -21.633 1.00 41.99  ? 156 VAL C N     1 
ATOM   3723  C CA    . VAL C 1 155 ? 12.422  -29.726 -22.258 1.00 38.65  ? 156 VAL C CA    1 
ATOM   3724  C C     . VAL C 1 155 ? 13.214  -28.977 -21.192 1.00 36.71  ? 156 VAL C C     1 
ATOM   3725  O O     . VAL C 1 155 ? 12.791  -27.925 -20.719 1.00 32.07  ? 156 VAL C O     1 
ATOM   3726  C CB    . VAL C 1 155 ? 12.043  -28.794 -23.425 1.00 43.92  ? 156 VAL C CB    1 
ATOM   3727  C CG1   . VAL C 1 155 ? 13.257  -28.052 -23.971 1.00 45.11  ? 156 VAL C CG1   1 
ATOM   3728  C CG2   . VAL C 1 155 ? 11.326  -29.547 -24.540 1.00 46.71  ? 156 VAL C CG2   1 
ATOM   3729  N N     . PRO C 1 156 ? 14.390  -29.501 -20.780 1.00 37.02  ? 157 PRO C N     1 
ATOM   3730  C CA    . PRO C 1 156 ? 15.228  -28.824 -19.792 1.00 34.78  ? 157 PRO C CA    1 
ATOM   3731  C C     . PRO C 1 156 ? 16.012  -27.660 -20.390 1.00 35.89  ? 157 PRO C C     1 
ATOM   3732  O O     . PRO C 1 156 ? 16.225  -27.604 -21.599 1.00 35.83  ? 157 PRO C O     1 
ATOM   3733  C CB    . PRO C 1 156 ? 16.143  -29.961 -19.306 1.00 35.17  ? 157 PRO C CB    1 
ATOM   3734  C CG    . PRO C 1 156 ? 16.302  -30.848 -20.523 1.00 34.84  ? 157 PRO C CG    1 
ATOM   3735  C CD    . PRO C 1 156 ? 14.962  -30.776 -21.241 1.00 35.40  ? 157 PRO C CD    1 
ATOM   3736  N N     . ASP C 1 157 ? 16.417  -26.727 -19.523 1.00 33.70  ? 158 ASP C N     1 
ATOM   3737  C CA    . ASP C 1 157 ? 17.286  -25.629 -19.907 1.00 34.47  ? 158 ASP C CA    1 
ATOM   3738  C C     . ASP C 1 157 ? 18.711  -25.977 -19.488 1.00 35.14  ? 158 ASP C C     1 
ATOM   3739  O O     . ASP C 1 157 ? 19.009  -26.061 -18.298 1.00 35.24  ? 158 ASP C O     1 
ATOM   3740  C CB    . ASP C 1 157 ? 16.801  -24.314 -19.313 1.00 34.00  ? 158 ASP C CB    1 
ATOM   3741  C CG    . ASP C 1 157 ? 17.703  -23.111 -19.553 1.00 34.00  ? 158 ASP C CG    1 
ATOM   3742  O OD1   . ASP C 1 157 ? 18.794  -23.301 -20.130 1.00 36.40  ? 158 ASP C OD1   1 
ATOM   3743  O OD2   . ASP C 1 157 ? 17.304  -21.993 -19.163 1.00 33.80  ? 158 ASP C OD2   1 
ATOM   3744  N N     . PRO C 1 158 ? 19.633  -26.195 -20.452 1.00 32.93  ? 159 PRO C N     1 
ATOM   3745  C CA    . PRO C 1 158 ? 20.973  -26.692 -20.133 1.00 33.52  ? 159 PRO C CA    1 
ATOM   3746  C C     . PRO C 1 158 ? 21.861  -25.682 -19.407 1.00 34.62  ? 159 PRO C C     1 
ATOM   3747  O O     . PRO C 1 158 ? 23.004  -25.990 -19.074 1.00 35.40  ? 159 PRO C O     1 
ATOM   3748  C CB    . PRO C 1 158 ? 21.534  -27.074 -21.519 1.00 36.10  ? 159 PRO C CB    1 
ATOM   3749  C CG    . PRO C 1 158 ? 20.811  -26.152 -22.482 1.00 37.11  ? 159 PRO C CG    1 
ATOM   3750  C CD    . PRO C 1 158 ? 19.425  -25.974 -21.890 1.00 35.30  ? 159 PRO C CD    1 
ATOM   3751  N N     . THR C 1 159 ? 21.322  -24.484 -19.153 1.00 34.02  ? 160 THR C N     1 
ATOM   3752  C CA    . THR C 1 159 ? 22.071  -23.439 -18.474 1.00 34.91  ? 160 THR C CA    1 
ATOM   3753  C C     . THR C 1 159 ? 21.773  -23.488 -16.977 1.00 34.96  ? 160 THR C C     1 
ATOM   3754  O O     . THR C 1 159 ? 22.484  -22.880 -16.180 1.00 37.10  ? 160 THR C O     1 
ATOM   3755  C CB    . THR C 1 159 ? 21.718  -22.076 -19.068 1.00 35.60  ? 160 THR C CB    1 
ATOM   3756  O OG1   . THR C 1 159 ? 20.331  -21.892 -18.802 1.00 40.08  ? 160 THR C OG1   1 
ATOM   3757  C CG2   . THR C 1 159 ? 21.982  -22.002 -20.562 1.00 35.00  ? 160 THR C CG2   1 
ATOM   3758  N N     . THR C 1 160 ? 20.717  -24.220 -16.607 1.00 34.77  ? 161 THR C N     1 
ATOM   3759  C CA    . THR C 1 160 ? 20.260  -24.270 -15.228 1.00 33.59  ? 161 THR C CA    1 
ATOM   3760  C C     . THR C 1 160 ? 20.783  -25.538 -14.564 1.00 30.29  ? 161 THR C C     1 
ATOM   3761  O O     . THR C 1 160 ? 21.193  -26.477 -15.241 1.00 30.08  ? 161 THR C O     1 
ATOM   3762  C CB    . THR C 1 160 ? 18.733  -24.231 -15.187 1.00 34.35  ? 161 THR C CB    1 
ATOM   3763  O OG1   . THR C 1 160 ? 18.311  -25.494 -15.691 1.00 39.19  ? 161 THR C OG1   1 
ATOM   3764  C CG2   . THR C 1 160 ? 18.152  -23.104 -16.021 1.00 36.26  ? 161 THR C CG2   1 
ATOM   3765  N N     . HIS C 1 161 ? 20.750  -25.551 -13.227 1.00 30.43  ? 162 HIS C N     1 
ATOM   3766  C CA    . HIS C 1 161 ? 20.939  -26.775 -12.471 1.00 28.21  ? 162 HIS C CA    1 
ATOM   3767  C C     . HIS C 1 161 ? 19.663  -27.603 -12.578 1.00 29.55  ? 162 HIS C C     1 
ATOM   3768  O O     . HIS C 1 161 ? 18.574  -27.111 -12.290 1.00 31.73  ? 162 HIS C O     1 
ATOM   3769  C CB    . HIS C 1 161 ? 21.332  -26.468 -11.021 1.00 29.37  ? 162 HIS C CB    1 
ATOM   3770  C CG    . HIS C 1 161 ? 22.733  -25.973 -10.878 1.00 27.41  ? 162 HIS C CG    1 
ATOM   3771  N ND1   . HIS C 1 161 ? 23.067  -24.637 -10.908 1.00 26.03  ? 162 HIS C ND1   1 
ATOM   3772  C CD2   . HIS C 1 161 ? 23.884  -26.641 -10.714 1.00 26.41  ? 162 HIS C CD2   1 
ATOM   3773  C CE1   . HIS C 1 161 ? 24.379  -24.512 -10.764 1.00 27.51  ? 162 HIS C CE1   1 
ATOM   3774  N NE2   . HIS C 1 161 ? 24.895  -25.716 -10.645 1.00 28.19  ? 162 HIS C NE2   1 
ATOM   3775  N N     . LEU C 1 162 ? 19.814  -28.853 -13.024 1.00 30.71  ? 163 LEU C N     1 
ATOM   3776  C CA    . LEU C 1 162 ? 18.682  -29.736 -13.247 1.00 30.20  ? 163 LEU C CA    1 
ATOM   3777  C C     . LEU C 1 162 ? 18.703  -30.856 -12.213 1.00 28.53  ? 163 LEU C C     1 
ATOM   3778  O O     . LEU C 1 162 ? 19.715  -31.532 -12.047 1.00 28.24  ? 163 LEU C O     1 
ATOM   3779  C CB    . LEU C 1 162 ? 18.754  -30.283 -14.672 1.00 32.77  ? 163 LEU C CB    1 
ATOM   3780  C CG    . LEU C 1 162 ? 17.647  -31.264 -15.073 1.00 36.94  ? 163 LEU C CG    1 
ATOM   3781  C CD1   . LEU C 1 162 ? 16.300  -30.567 -15.132 1.00 39.85  ? 163 LEU C CD1   1 
ATOM   3782  C CD2   . LEU C 1 162 ? 17.966  -31.930 -16.401 1.00 39.49  ? 163 LEU C CD2   1 
ATOM   3783  N N     . LEU C 1 163 ? 17.571  -31.040 -11.525 1.00 31.78  ? 164 LEU C N     1 
ATOM   3784  C CA    . LEU C 1 163 ? 17.422  -32.116 -10.558 1.00 31.26  ? 164 LEU C CA    1 
ATOM   3785  C C     . LEU C 1 163 ? 16.422  -33.135 -11.096 1.00 30.05  ? 164 LEU C C     1 
ATOM   3786  O O     . LEU C 1 163 ? 15.351  -32.768 -11.574 1.00 30.15  ? 164 LEU C O     1 
ATOM   3787  C CB    . LEU C 1 163 ? 16.970  -31.567 -9.206  1.00 32.40  ? 164 LEU C CB    1 
ATOM   3788  C CG    . LEU C 1 163 ? 17.920  -30.578 -8.522  1.00 33.33  ? 164 LEU C CG    1 
ATOM   3789  C CD1   . LEU C 1 163 ? 17.432  -30.252 -7.119  1.00 33.10  ? 164 LEU C CD1   1 
ATOM   3790  C CD2   . LEU C 1 163 ? 19.338  -31.116 -8.484  1.00 34.54  ? 164 LEU C CD2   1 
ATOM   3791  N N     . LEU C 1 164 ? 16.795  -34.417 -11.022 1.00 31.55  ? 165 LEU C N     1 
ATOM   3792  C CA    . LEU C 1 164 ? 15.875  -35.503 -11.315 1.00 29.56  ? 165 LEU C CA    1 
ATOM   3793  C C     . LEU C 1 164 ? 15.646  -36.301 -10.035 1.00 28.14  ? 165 LEU C C     1 
ATOM   3794  O O     . LEU C 1 164 ? 16.553  -36.969 -9.543  1.00 25.38  ? 165 LEU C O     1 
ATOM   3795  C CB    . LEU C 1 164 ? 16.409  -36.389 -12.440 1.00 32.04  ? 165 LEU C CB    1 
ATOM   3796  C CG    . LEU C 1 164 ? 16.502  -35.741 -13.826 1.00 31.66  ? 165 LEU C CG    1 
ATOM   3797  C CD1   . LEU C 1 164 ? 16.812  -36.790 -14.881 1.00 35.63  ? 165 LEU C CD1   1 
ATOM   3798  C CD2   . LEU C 1 164 ? 15.231  -34.989 -14.180 1.00 31.63  ? 165 LEU C CD2   1 
ATOM   3799  N N     . TRP C 1 165 ? 14.427  -36.208 -9.497  1.00 28.55  ? 166 TRP C N     1 
ATOM   3800  C CA    . TRP C 1 165 ? 14.079  -36.897 -8.266  1.00 28.38  ? 166 TRP C CA    1 
ATOM   3801  C C     . TRP C 1 165 ? 13.666  -38.332 -8.581  1.00 27.48  ? 166 TRP C C     1 
ATOM   3802  O O     . TRP C 1 165 ? 13.309  -38.645 -9.714  1.00 30.07  ? 166 TRP C O     1 
ATOM   3803  C CB    . TRP C 1 165 ? 12.959  -36.152 -7.523  1.00 26.46  ? 166 TRP C CB    1 
ATOM   3804  C CG    . TRP C 1 165 ? 13.277  -34.716 -7.198  1.00 28.86  ? 166 TRP C CG    1 
ATOM   3805  C CD1   . TRP C 1 165 ? 13.719  -33.753 -8.058  1.00 33.08  ? 166 TRP C CD1   1 
ATOM   3806  C CD2   . TRP C 1 165 ? 13.200  -34.087 -5.899  1.00 28.33  ? 166 TRP C CD2   1 
ATOM   3807  N NE1   . TRP C 1 165 ? 13.901  -32.569 -7.393  1.00 33.12  ? 166 TRP C NE1   1 
ATOM   3808  C CE2   . TRP C 1 165 ? 13.597  -32.744 -6.068  1.00 28.50  ? 166 TRP C CE2   1 
ATOM   3809  C CE3   . TRP C 1 165 ? 12.834  -34.525 -4.621  1.00 26.10  ? 166 TRP C CE3   1 
ATOM   3810  C CZ2   . TRP C 1 165 ? 13.638  -31.842 -5.008  1.00 30.76  ? 166 TRP C CZ2   1 
ATOM   3811  C CZ3   . TRP C 1 165 ? 12.876  -33.632 -3.573  1.00 29.34  ? 166 TRP C CZ3   1 
ATOM   3812  C CH2   . TRP C 1 165 ? 13.274  -32.309 -3.766  1.00 26.55  ? 166 TRP C CH2   1 
ATOM   3813  N N     . GLN C 1 166 ? 13.722  -39.195 -7.562  1.00 26.64  ? 167 GLN C N     1 
ATOM   3814  C CA    . GLN C 1 166 ? 13.339  -40.589 -7.711  1.00 31.51  ? 167 GLN C CA    1 
ATOM   3815  C C     . GLN C 1 166 ? 13.985  -41.157 -8.972  1.00 32.59  ? 167 GLN C C     1 
ATOM   3816  O O     . GLN C 1 166 ? 13.312  -41.759 -9.805  1.00 33.82  ? 167 GLN C O     1 
ATOM   3817  C CB    . GLN C 1 166 ? 11.816  -40.719 -7.762  1.00 32.41  ? 167 GLN C CB    1 
ATOM   3818  C CG    . GLN C 1 166 ? 11.115  -40.283 -6.480  1.00 33.80  ? 167 GLN C CG    1 
ATOM   3819  C CD    . GLN C 1 166 ? 9.607   -40.374 -6.565  1.00 37.00  ? 167 GLN C CD    1 
ATOM   3820  O OE1   . GLN C 1 166 ? 9.038   -40.725 -7.605  1.00 35.86  ? 167 GLN C OE1   1 
ATOM   3821  N NE2   . GLN C 1 166 ? 8.942   -40.053 -5.464  1.00 42.93  ? 167 GLN C NE2   1 
ATOM   3822  N N     . ILE C 1 167 ? 15.298  -40.950 -9.096  1.00 31.83  ? 168 ILE C N     1 
ATOM   3823  C CA    . ILE C 1 167 ? 16.056  -41.454 -10.228 1.00 30.19  ? 168 ILE C CA    1 
ATOM   3824  C C     . ILE C 1 167 ? 16.185  -42.970 -10.095 1.00 30.92  ? 168 ILE C C     1 
ATOM   3825  O O     . ILE C 1 167 ? 16.354  -43.673 -11.088 1.00 32.00  ? 168 ILE C O     1 
ATOM   3826  C CB    . ILE C 1 167 ? 17.432  -40.766 -10.309 1.00 28.57  ? 168 ILE C CB    1 
ATOM   3827  C CG1   . ILE C 1 167 ? 18.221  -41.219 -11.537 1.00 30.28  ? 168 ILE C CG1   1 
ATOM   3828  C CG2   . ILE C 1 167 ? 18.225  -40.979 -9.019  1.00 28.75  ? 168 ILE C CG2   1 
ATOM   3829  C CD1   . ILE C 1 167 ? 17.541  -40.911 -12.859 1.00 30.37  ? 168 ILE C CD1   1 
ATOM   3830  N N     . ALA C 1 168 ? 16.078  -43.459 -8.855  1.00 27.98  ? 169 ALA C N     1 
ATOM   3831  C CA    . ALA C 1 168 ? 16.290  -44.864 -8.554  1.00 29.53  ? 169 ALA C CA    1 
ATOM   3832  C C     . ALA C 1 168 ? 15.211  -45.722 -9.212  1.00 27.52  ? 169 ALA C C     1 
ATOM   3833  O O     . ALA C 1 168 ? 15.423  -46.908 -9.450  1.00 30.30  ? 169 ALA C O     1 
ATOM   3834  C CB    . ALA C 1 168 ? 16.320  -45.067 -7.054  1.00 30.20  ? 169 ALA C CB    1 
ATOM   3835  N N     . ILE C 1 169 ? 14.053  -45.115 -9.496  1.00 27.15  ? 170 ILE C N     1 
ATOM   3836  C CA    . ILE C 1 169 ? 12.933  -45.839 -10.075 1.00 28.86  ? 170 ILE C CA    1 
ATOM   3837  C C     . ILE C 1 169 ? 12.561  -45.213 -11.417 1.00 28.70  ? 170 ILE C C     1 
ATOM   3838  O O     . ILE C 1 169 ? 11.420  -45.317 -11.859 1.00 26.77  ? 170 ILE C O     1 
ATOM   3839  C CB    . ILE C 1 169 ? 11.735  -45.864 -9.107  1.00 32.93  ? 170 ILE C CB    1 
ATOM   3840  C CG1   . ILE C 1 169 ? 11.321  -44.454 -8.685  1.00 36.13  ? 170 ILE C CG1   1 
ATOM   3841  C CG2   . ILE C 1 169 ? 12.032  -46.750 -7.897  1.00 37.62  ? 170 ILE C CG2   1 
ATOM   3842  C CD1   . ILE C 1 169 ? 10.119  -44.412 -7.760  1.00 37.09  ? 170 ILE C CD1   1 
ATOM   3843  N N     . ALA C 1 170 ? 13.543  -44.576 -12.064 1.00 29.00  ? 171 ALA C N     1 
ATOM   3844  C CA    . ALA C 1 170 ? 13.324  -43.924 -13.345 1.00 28.14  ? 171 ALA C CA    1 
ATOM   3845  C C     . ALA C 1 170 ? 12.968  -44.964 -14.405 1.00 31.25  ? 171 ALA C C     1 
ATOM   3846  O O     . ALA C 1 170 ? 13.806  -45.776 -14.791 1.00 30.38  ? 171 ALA C O     1 
ATOM   3847  C CB    . ALA C 1 170 ? 14.554  -43.138 -13.738 1.00 27.78  ? 171 ALA C CB    1 
ATOM   3848  N N     . GLY C 1 171 ? 11.716  -44.922 -14.872 1.00 33.14  ? 172 GLY C N     1 
ATOM   3849  C CA    . GLY C 1 171 ? 11.257  -45.814 -15.924 1.00 36.97  ? 172 GLY C CA    1 
ATOM   3850  C C     . GLY C 1 171 ? 10.380  -46.933 -15.369 1.00 42.15  ? 172 GLY C C     1 
ATOM   3851  O O     . GLY C 1 171 ? 9.820   -47.721 -16.128 1.00 48.12  ? 172 GLY C O     1 
ATOM   3852  N N     . GLU C 1 172 ? 10.273  -46.991 -14.037 1.00 39.95  ? 173 GLU C N     1 
ATOM   3853  C CA    . GLU C 1 172 ? 9.446   -47.984 -13.372 1.00 45.37  ? 173 GLU C CA    1 
ATOM   3854  C C     . GLU C 1 172 ? 7.983   -47.571 -13.520 1.00 42.40  ? 173 GLU C C     1 
ATOM   3855  O O     . GLU C 1 172 ? 7.494   -46.725 -12.775 1.00 47.41  ? 173 GLU C O     1 
ATOM   3856  C CB    . GLU C 1 172 ? 9.876   -48.103 -11.909 1.00 46.29  ? 173 GLU C CB    1 
ATOM   3857  C CG    . GLU C 1 172 ? 9.419   -49.394 -11.237 1.00 49.07  ? 173 GLU C CG    1 
ATOM   3858  C CD    . GLU C 1 172 ? 7.914   -49.574 -11.172 1.00 59.58  ? 173 GLU C CD    1 
ATOM   3859  O OE1   . GLU C 1 172 ? 7.378   -49.660 -10.048 1.00 59.63  ? 173 GLU C OE1   1 
ATOM   3860  O OE2   . GLU C 1 172 ? 7.278   -49.633 -12.245 1.00 73.95  ? 173 GLU C OE2   1 
ATOM   3861  N N     . HIS C 1 173 ? 7.295   -48.183 -14.492 1.00 36.44  ? 174 HIS C N     1 
ATOM   3862  C CA    . HIS C 1 173 ? 5.995   -47.705 -14.936 1.00 33.89  ? 174 HIS C CA    1 
ATOM   3863  C C     . HIS C 1 173 ? 4.871   -48.398 -14.171 1.00 36.65  ? 174 HIS C C     1 
ATOM   3864  O O     . HIS C 1 173 ? 3.751   -47.893 -14.126 1.00 36.47  ? 174 HIS C O     1 
ATOM   3865  C CB    . HIS C 1 173 ? 5.837   -47.905 -16.449 1.00 31.79  ? 174 HIS C CB    1 
ATOM   3866  C CG    . HIS C 1 173 ? 5.808   -49.337 -16.871 1.00 30.32  ? 174 HIS C CG    1 
ATOM   3867  N ND1   . HIS C 1 173 ? 6.948   -50.060 -17.150 1.00 30.77  ? 174 HIS C ND1   1 
ATOM   3868  C CD2   . HIS C 1 173 ? 4.782   -50.180 -17.054 1.00 29.67  ? 174 HIS C CD2   1 
ATOM   3869  C CE1   . HIS C 1 173 ? 6.610   -51.295 -17.493 1.00 30.96  ? 174 HIS C CE1   1 
ATOM   3870  N NE2   . HIS C 1 173 ? 5.299   -51.390 -17.442 1.00 30.26  ? 174 HIS C NE2   1 
ATOM   3871  N N     . THR C 1 174 ? 5.172   -49.562 -13.583 1.00 40.12  ? 175 THR C N     1 
ATOM   3872  C CA    . THR C 1 174 ? 4.162   -50.354 -12.898 1.00 43.02  ? 175 THR C CA    1 
ATOM   3873  C C     . THR C 1 174 ? 3.818   -49.700 -11.561 1.00 39.10  ? 175 THR C C     1 
ATOM   3874  O O     . THR C 1 174 ? 2.685   -49.793 -11.095 1.00 39.30  ? 175 THR C O     1 
ATOM   3875  C CB    . THR C 1 174 ? 4.664   -51.786 -12.706 1.00 44.53  ? 175 THR C CB    1 
ATOM   3876  O OG1   . THR C 1 174 ? 5.781   -51.684 -11.829 1.00 49.49  ? 175 THR C OG1   1 
ATOM   3877  C CG2   . THR C 1 174 ? 5.072   -52.443 -14.013 1.00 47.70  ? 175 THR C CG2   1 
ATOM   3878  N N     . LEU C 1 175 ? 4.810   -49.041 -10.953 1.00 41.54  ? 176 LEU C N     1 
ATOM   3879  C CA    . LEU C 1 175 ? 4.642   -48.428 -9.645  1.00 43.86  ? 176 LEU C CA    1 
ATOM   3880  C C     . LEU C 1 175 ? 4.505   -49.527 -8.595  1.00 43.02  ? 176 LEU C C     1 
ATOM   3881  O O     . LEU C 1 175 ? 3.850   -49.335 -7.572  1.00 40.12  ? 176 LEU C O     1 
ATOM   3882  C CB    . LEU C 1 175 ? 3.428   -47.499 -9.630  1.00 41.91  ? 176 LEU C CB    1 
ATOM   3883  C CG    . LEU C 1 175 ? 3.395   -46.400 -10.697 1.00 47.37  ? 176 LEU C CG    1 
ATOM   3884  C CD1   . LEU C 1 175 ? 2.228   -45.459 -10.447 1.00 45.37  ? 176 LEU C CD1   1 
ATOM   3885  C CD2   . LEU C 1 175 ? 4.704   -45.631 -10.754 1.00 50.49  ? 176 LEU C CD2   1 
ATOM   3886  N N     . THR C 1 176 ? 5.124   -50.681 -8.866  1.00 43.37  ? 177 THR C N     1 
ATOM   3887  C CA    . THR C 1 176 ? 5.061   -51.820 -7.967  1.00 39.28  ? 177 THR C CA    1 
ATOM   3888  C C     . THR C 1 176 ? 6.473   -52.183 -7.517  1.00 40.34  ? 177 THR C C     1 
ATOM   3889  O O     . THR C 1 176 ? 6.651   -52.888 -6.526  1.00 41.18  ? 177 THR C O     1 
ATOM   3890  C CB    . THR C 1 176 ? 4.378   -52.995 -8.668  1.00 39.76  ? 177 THR C CB    1 
ATOM   3891  O OG1   . THR C 1 176 ? 5.265   -53.378 -9.716  1.00 38.56  ? 177 THR C OG1   1 
ATOM   3892  C CG2   . THR C 1 176 ? 3.016   -52.629 -9.230  1.00 39.75  ? 177 THR C CG2   1 
ATOM   3893  N N     . GLN C 1 177 ? 7.471   -51.699 -8.264  1.00 36.70  ? 178 GLN C N     1 
ATOM   3894  C CA    . GLN C 1 177 ? 8.865   -51.984 -7.966  1.00 39.68  ? 178 GLN C CA    1 
ATOM   3895  C C     . GLN C 1 177 ? 9.464   -50.814 -7.189  1.00 40.30  ? 178 GLN C C     1 
ATOM   3896  O O     . GLN C 1 177 ? 9.017   -49.678 -7.326  1.00 31.25  ? 178 GLN C O     1 
ATOM   3897  C CB    . GLN C 1 177 ? 9.652   -52.243 -9.251  1.00 38.61  ? 178 GLN C CB    1 
ATOM   3898  C CG    . GLN C 1 177 ? 9.090   -53.370 -10.112 1.00 46.01  ? 178 GLN C CG    1 
ATOM   3899  C CD    . GLN C 1 177 ? 9.030   -54.701 -9.394  1.00 48.75  ? 178 GLN C CD    1 
ATOM   3900  O OE1   . GLN C 1 177 ? 9.287   -54.799 -8.189  1.00 48.29  ? 178 GLN C OE1   1 
ATOM   3901  N NE2   . GLN C 1 177 ? 8.679   -55.744 -10.132 1.00 54.51  ? 178 GLN C NE2   1 
ATOM   3902  N N     . PHE C 1 178 ? 10.491  -51.114 -6.388  1.00 45.50  ? 179 PHE C N     1 
ATOM   3903  C CA    . PHE C 1 178 ? 11.119  -50.128 -5.523  1.00 47.87  ? 179 PHE C CA    1 
ATOM   3904  C C     . PHE C 1 178 ? 12.375  -49.582 -6.197  1.00 50.43  ? 179 PHE C C     1 
ATOM   3905  O O     . PHE C 1 178 ? 12.959  -48.607 -5.729  1.00 46.88  ? 179 PHE C O     1 
ATOM   3906  C CB    . PHE C 1 178 ? 11.432  -50.777 -4.171  1.00 56.05  ? 179 PHE C CB    1 
ATOM   3907  C CG    . PHE C 1 178 ? 10.208  -51.209 -3.374  1.00 65.69  ? 179 PHE C CG    1 
ATOM   3908  C CD1   . PHE C 1 178 ? 9.122   -50.355 -3.213  1.00 64.96  ? 179 PHE C CD1   1 
ATOM   3909  C CD2   . PHE C 1 178 ? 10.135  -52.478 -2.809  1.00 68.33  ? 179 PHE C CD2   1 
ATOM   3910  C CE1   . PHE C 1 178 ? 8.009   -50.753 -2.489  1.00 61.53  ? 179 PHE C CE1   1 
ATOM   3911  C CE2   . PHE C 1 178 ? 9.017   -52.871 -2.090  1.00 68.20  ? 179 PHE C CE2   1 
ATOM   3912  C CZ    . PHE C 1 178 ? 7.958   -52.009 -1.932  1.00 64.39  ? 179 PHE C CZ    1 
ATOM   3913  N N     . HIS C 1 179 ? 12.781  -50.225 -7.297  1.00 49.70  ? 180 HIS C N     1 
ATOM   3914  C CA    . HIS C 1 179 ? 13.973  -49.821 -8.025  1.00 50.79  ? 180 HIS C CA    1 
ATOM   3915  C C     . HIS C 1 179 ? 13.803  -50.150 -9.506  1.00 43.65  ? 180 HIS C C     1 
ATOM   3916  O O     . HIS C 1 179 ? 13.002  -51.008 -9.868  1.00 43.68  ? 180 HIS C O     1 
ATOM   3917  C CB    . HIS C 1 179 ? 15.219  -50.488 -7.430  1.00 52.11  ? 180 HIS C CB    1 
ATOM   3918  C CG    . HIS C 1 179 ? 15.171  -51.980 -7.440  1.00 59.36  ? 180 HIS C CG    1 
ATOM   3919  N ND1   . HIS C 1 179 ? 15.536  -52.731 -8.537  1.00 65.10  ? 180 HIS C ND1   1 
ATOM   3920  C CD2   . HIS C 1 179 ? 14.798  -52.857 -6.499  1.00 58.47  ? 180 HIS C CD2   1 
ATOM   3921  C CE1   . HIS C 1 179 ? 15.389  -54.017 -8.254  1.00 61.28  ? 180 HIS C CE1   1 
ATOM   3922  N NE2   . HIS C 1 179 ? 14.942  -54.117 -7.021  1.00 61.07  ? 180 HIS C NE2   1 
ATOM   3923  N N     . THR C 1 180 ? 14.564  -49.448 -10.353 1.00 43.51  ? 181 THR C N     1 
ATOM   3924  C CA    . THR C 1 180 ? 14.519  -49.664 -11.790 1.00 47.02  ? 181 THR C CA    1 
ATOM   3925  C C     . THR C 1 180 ? 15.660  -50.597 -12.187 1.00 47.54  ? 181 THR C C     1 
ATOM   3926  O O     . THR C 1 180 ? 16.176  -51.343 -11.357 1.00 41.11  ? 181 THR C O     1 
ATOM   3927  C CB    . THR C 1 180 ? 14.604  -48.321 -12.516 1.00 44.93  ? 181 THR C CB    1 
ATOM   3928  O OG1   . THR C 1 180 ? 14.395  -48.614 -13.894 1.00 46.67  ? 181 THR C OG1   1 
ATOM   3929  C CG2   . THR C 1 180 ? 15.945  -47.636 -12.324 1.00 44.29  ? 181 THR C CG2   1 
ATOM   3930  N N     . SER C 1 181 ? 16.043  -50.545 -13.467 1.00 47.20  ? 182 SER C N     1 
ATOM   3931  C CA    . SER C 1 181 ? 17.121  -51.372 -13.982 1.00 49.37  ? 182 SER C CA    1 
ATOM   3932  C C     . SER C 1 181 ? 18.097  -50.511 -14.779 1.00 49.08  ? 182 SER C C     1 
ATOM   3933  O O     . SER C 1 181 ? 17.797  -49.367 -15.111 1.00 46.08  ? 182 SER C O     1 
ATOM   3934  C CB    . SER C 1 181 ? 16.584  -52.509 -14.816 1.00 52.61  ? 182 SER C CB    1 
ATOM   3935  O OG    . SER C 1 181 ? 15.847  -52.024 -15.930 1.00 53.69  ? 182 SER C OG    1 
ATOM   3936  N N     . SER C 1 182 ? 19.266  -51.086 -15.082 1.00 50.32  ? 183 SER C N     1 
ATOM   3937  C CA    . SER C 1 182 ? 20.328  -50.370 -15.769 1.00 52.15  ? 183 SER C CA    1 
ATOM   3938  C C     . SER C 1 182 ? 19.908  -50.040 -17.199 1.00 48.57  ? 183 SER C C     1 
ATOM   3939  O O     . SER C 1 182 ? 20.358  -49.047 -17.766 1.00 47.23  ? 183 SER C O     1 
ATOM   3940  C CB    . SER C 1 182 ? 21.611  -51.163 -15.750 1.00 54.62  ? 183 SER C CB    1 
ATOM   3941  O OG    . SER C 1 182 ? 21.446  -52.414 -16.403 1.00 54.43  ? 183 SER C OG    1 
ATOM   3942  N N     . ASP C 1 183 ? 19.045  -50.886 -17.773 1.00 48.29  ? 184 ASP C N     1 
ATOM   3943  C CA    . ASP C 1 183 ? 18.611  -50.721 -19.151 1.00 50.59  ? 184 ASP C CA    1 
ATOM   3944  C C     . ASP C 1 183 ? 17.704  -49.497 -19.257 1.00 49.72  ? 184 ASP C C     1 
ATOM   3945  O O     . ASP C 1 183 ? 17.709  -48.805 -20.273 1.00 48.13  ? 184 ASP C O     1 
ATOM   3946  C CB    . ASP C 1 183 ? 17.953  -51.987 -19.680 1.00 56.51  ? 184 ASP C CB    1 
ATOM   3947  C CG    . ASP C 1 183 ? 16.842  -52.561 -18.815 1.00 62.04  ? 184 ASP C CG    1 
ATOM   3948  O OD1   . ASP C 1 183 ? 17.136  -52.943 -17.662 1.00 62.47  ? 184 ASP C OD1   1 
ATOM   3949  O OD2   . ASP C 1 183 ? 15.693  -52.627 -19.302 1.00 65.24  ? 184 ASP C OD2   1 
ATOM   3950  N N     . ARG C 1 184 ? 16.928  -49.240 -18.199 1.00 48.17  ? 185 ARG C N     1 
ATOM   3951  C CA    . ARG C 1 184 ? 16.070  -48.068 -18.146 1.00 50.46  ? 185 ARG C CA    1 
ATOM   3952  C C     . ARG C 1 184 ? 16.931  -46.811 -18.059 1.00 44.61  ? 185 ARG C C     1 
ATOM   3953  O O     . ARG C 1 184 ? 16.716  -45.853 -18.798 1.00 40.11  ? 185 ARG C O     1 
ATOM   3954  C CB    . ARG C 1 184 ? 15.103  -48.136 -16.956 1.00 52.32  ? 185 ARG C CB    1 
ATOM   3955  C CG    . ARG C 1 184 ? 13.844  -48.956 -17.200 1.00 56.62  ? 185 ARG C CG    1 
ATOM   3956  C CD    . ARG C 1 184 ? 14.132  -50.421 -17.487 1.00 60.98  ? 185 ARG C CD    1 
ATOM   3957  N NE    . ARG C 1 184 ? 12.902  -51.179 -17.745 1.00 61.59  ? 185 ARG C NE    1 
ATOM   3958  C CZ    . ARG C 1 184 ? 12.087  -50.973 -18.773 1.00 62.75  ? 185 ARG C CZ    1 
ATOM   3959  N NH1   . ARG C 1 184 ? 12.377  -50.052 -19.674 1.00 64.67  ? 185 ARG C NH1   1 
ATOM   3960  N NH2   . ARG C 1 184 ? 10.989  -51.697 -18.903 1.00 63.22  ? 185 ARG C NH2   1 
ATOM   3961  N N     . LEU C 1 185 ? 17.909  -46.834 -17.147 1.00 41.50  ? 186 LEU C N     1 
ATOM   3962  C CA    . LEU C 1 185 ? 18.762  -45.683 -16.902 1.00 40.79  ? 186 LEU C CA    1 
ATOM   3963  C C     . LEU C 1 185 ? 19.590  -45.385 -18.149 1.00 41.42  ? 186 LEU C C     1 
ATOM   3964  O O     . LEU C 1 185 ? 19.968  -44.240 -18.387 1.00 42.69  ? 186 LEU C O     1 
ATOM   3965  C CB    . LEU C 1 185 ? 19.649  -45.946 -15.686 1.00 39.66  ? 186 LEU C CB    1 
ATOM   3966  C CG    . LEU C 1 185 ? 18.920  -46.103 -14.347 1.00 43.10  ? 186 LEU C CG    1 
ATOM   3967  C CD1   . LEU C 1 185 ? 19.906  -46.334 -13.215 1.00 42.70  ? 186 LEU C CD1   1 
ATOM   3968  C CD2   . LEU C 1 185 ? 18.047  -44.894 -14.055 1.00 45.36  ? 186 LEU C CD2   1 
ATOM   3969  N N     . GLN C 1 186 ? 19.865  -46.430 -18.937 1.00 39.97  ? 187 GLN C N     1 
ATOM   3970  C CA    . GLN C 1 186 ? 20.636  -46.291 -20.161 1.00 43.98  ? 187 GLN C CA    1 
ATOM   3971  C C     . GLN C 1 186 ? 19.837  -45.471 -21.171 1.00 45.14  ? 187 GLN C C     1 
ATOM   3972  O O     . GLN C 1 186 ? 20.398  -44.653 -21.898 1.00 45.86  ? 187 GLN C O     1 
ATOM   3973  C CB    . GLN C 1 186 ? 20.997  -47.667 -20.721 1.00 47.41  ? 187 GLN C CB    1 
ATOM   3974  C CG    . GLN C 1 186 ? 21.696  -47.624 -22.076 1.00 51.70  ? 187 GLN C CG    1 
ATOM   3975  C CD    . GLN C 1 186 ? 22.946  -46.770 -22.076 1.00 52.46  ? 187 GLN C CD    1 
ATOM   3976  O OE1   . GLN C 1 186 ? 23.867  -46.974 -21.278 1.00 52.94  ? 187 GLN C OE1   1 
ATOM   3977  N NE2   . GLN C 1 186 ? 22.985  -45.796 -22.974 1.00 49.38  ? 187 GLN C NE2   1 
ATOM   3978  N N     . ILE C 1 187 ? 18.520  -45.700 -21.203 1.00 43.34  ? 188 ILE C N     1 
ATOM   3979  C CA    . ILE C 1 187 ? 17.639  -44.997 -22.121 1.00 42.66  ? 188 ILE C CA    1 
ATOM   3980  C C     . ILE C 1 187 ? 17.532  -43.538 -21.685 1.00 40.59  ? 188 ILE C C     1 
ATOM   3981  O O     . ILE C 1 187 ? 17.380  -42.646 -22.517 1.00 35.08  ? 188 ILE C O     1 
ATOM   3982  C CB    . ILE C 1 187 ? 16.260  -45.679 -22.189 1.00 43.82  ? 188 ILE C CB    1 
ATOM   3983  C CG1   . ILE C 1 187 ? 16.360  -47.086 -22.779 1.00 40.39  ? 188 ILE C CG1   1 
ATOM   3984  C CG2   . ILE C 1 187 ? 15.260  -44.815 -22.957 1.00 44.69  ? 188 ILE C CG2   1 
ATOM   3985  C CD1   . ILE C 1 187 ? 15.037  -47.827 -22.843 1.00 40.82  ? 188 ILE C CD1   1 
ATOM   3986  N N     . LEU C 1 188 ? 17.613  -43.309 -20.371 1.00 36.83  ? 189 LEU C N     1 
ATOM   3987  C CA    . LEU C 1 188 ? 17.565  -41.964 -19.825 1.00 35.89  ? 189 LEU C CA    1 
ATOM   3988  C C     . LEU C 1 188 ? 18.787  -41.189 -20.308 1.00 31.47  ? 189 LEU C C     1 
ATOM   3989  O O     . LEU C 1 188 ? 18.688  -40.015 -20.657 1.00 28.28  ? 189 LEU C O     1 
ATOM   3990  C CB    . LEU C 1 188 ? 17.498  -42.016 -18.299 1.00 33.56  ? 189 LEU C CB    1 
ATOM   3991  C CG    . LEU C 1 188 ? 17.435  -40.663 -17.584 1.00 32.91  ? 189 LEU C CG    1 
ATOM   3992  C CD1   . LEU C 1 188 ? 16.245  -39.848 -18.061 1.00 34.14  ? 189 LEU C CD1   1 
ATOM   3993  C CD2   . LEU C 1 188 ? 17.386  -40.845 -16.077 1.00 30.21  ? 189 LEU C CD2   1 
ATOM   3994  N N     . VAL C 1 189 ? 19.937  -41.871 -20.327 1.00 32.94  ? 190 VAL C N     1 
ATOM   3995  C CA    . VAL C 1 189 ? 21.186  -41.269 -20.760 1.00 34.97  ? 190 VAL C CA    1 
ATOM   3996  C C     . VAL C 1 189 ? 21.036  -40.805 -22.207 1.00 36.00  ? 190 VAL C C     1 
ATOM   3997  O O     . VAL C 1 189 ? 21.355  -39.664 -22.534 1.00 41.93  ? 190 VAL C O     1 
ATOM   3998  C CB    . VAL C 1 189 ? 22.362  -42.253 -20.604 1.00 38.13  ? 190 VAL C CB    1 
ATOM   3999  C CG1   . VAL C 1 189 ? 23.620  -41.754 -21.305 1.00 40.72  ? 190 VAL C CG1   1 
ATOM   4000  C CG2   . VAL C 1 189 ? 22.648  -42.562 -19.139 1.00 38.84  ? 190 VAL C CG2   1 
ATOM   4001  N N     . GLU C 1 190 ? 20.539  -41.704 -23.062 1.00 35.17  ? 191 GLU C N     1 
ATOM   4002  C CA    . GLU C 1 190 ? 20.357  -41.409 -24.474 1.00 38.36  ? 191 GLU C CA    1 
ATOM   4003  C C     . GLU C 1 190 ? 19.416  -40.217 -24.624 1.00 37.16  ? 191 GLU C C     1 
ATOM   4004  O O     . GLU C 1 190 ? 19.602  -39.380 -25.504 1.00 39.58  ? 191 GLU C O     1 
ATOM   4005  C CB    . GLU C 1 190 ? 19.813  -42.635 -25.207 1.00 39.24  ? 191 GLU C CB    1 
ATOM   4006  C CG    . GLU C 1 190 ? 20.750  -43.838 -25.154 1.00 42.11  ? 191 GLU C CG    1 
ATOM   4007  C CD    . GLU C 1 190 ? 20.197  -45.091 -25.807 1.00 45.98  ? 191 GLU C CD    1 
ATOM   4008  O OE1   . GLU C 1 190 ? 19.041  -45.053 -26.280 1.00 48.67  ? 191 GLU C OE1   1 
ATOM   4009  O OE2   . GLU C 1 190 ? 20.923  -46.106 -25.843 1.00 50.45  ? 191 GLU C OE2   1 
ATOM   4010  N N     . GLN C 1 191 ? 18.404  -40.159 -23.753 1.00 36.85  ? 192 GLN C N     1 
ATOM   4011  C CA    . GLN C 1 191 ? 17.430  -39.082 -23.768 1.00 36.44  ? 192 GLN C CA    1 
ATOM   4012  C C     . GLN C 1 191 ? 18.117  -37.771 -23.395 1.00 34.70  ? 192 GLN C C     1 
ATOM   4013  O O     . GLN C 1 191 ? 17.916  -36.750 -24.049 1.00 38.66  ? 192 GLN C O     1 
ATOM   4014  C CB    . GLN C 1 191 ? 16.289  -39.388 -22.797 1.00 36.48  ? 192 GLN C CB    1 
ATOM   4015  C CG    . GLN C 1 191 ? 15.164  -38.358 -22.818 1.00 37.90  ? 192 GLN C CG    1 
ATOM   4016  C CD    . GLN C 1 191 ? 14.106  -38.612 -21.768 1.00 38.36  ? 192 GLN C CD    1 
ATOM   4017  O OE1   . GLN C 1 191 ? 14.238  -39.498 -20.917 1.00 39.27  ? 192 GLN C OE1   1 
ATOM   4018  N NE2   . GLN C 1 191 ? 13.043  -37.821 -21.811 1.00 37.38  ? 192 GLN C NE2   1 
ATOM   4019  N N     . LEU C 1 192 ? 18.929  -37.817 -22.334 1.00 29.90  ? 193 LEU C N     1 
ATOM   4020  C CA    . LEU C 1 192 ? 19.604  -36.634 -21.825 1.00 31.66  ? 193 LEU C CA    1 
ATOM   4021  C C     . LEU C 1 192 ? 20.687  -36.194 -22.806 1.00 33.24  ? 193 LEU C C     1 
ATOM   4022  O O     . LEU C 1 192 ? 21.148  -35.057 -22.756 1.00 32.21  ? 193 LEU C O     1 
ATOM   4023  C CB    . LEU C 1 192 ? 20.192  -36.927 -20.445 1.00 29.04  ? 193 LEU C CB    1 
ATOM   4024  C CG    . LEU C 1 192 ? 19.185  -37.073 -19.299 1.00 31.35  ? 193 LEU C CG    1 
ATOM   4025  C CD1   . LEU C 1 192 ? 19.890  -37.402 -17.993 1.00 32.25  ? 193 LEU C CD1   1 
ATOM   4026  C CD2   . LEU C 1 192 ? 18.353  -35.812 -19.153 1.00 32.59  ? 193 LEU C CD2   1 
ATOM   4027  N N     . ASN C 1 193 ? 21.084  -37.109 -23.696 1.00 38.17  ? 194 ASN C N     1 
ATOM   4028  C CA    . ASN C 1 193 ? 22.201  -36.873 -24.595 1.00 44.81  ? 194 ASN C CA    1 
ATOM   4029  C C     . ASN C 1 193 ? 21.823  -35.806 -25.620 1.00 46.40  ? 194 ASN C C     1 
ATOM   4030  O O     . ASN C 1 193 ? 22.671  -35.346 -26.382 1.00 47.50  ? 194 ASN C O     1 
ATOM   4031  C CB    . ASN C 1 193 ? 22.656  -38.162 -25.270 1.00 46.43  ? 194 ASN C CB    1 
ATOM   4032  C CG    . ASN C 1 193 ? 23.934  -37.975 -26.052 1.00 47.34  ? 194 ASN C CG    1 
ATOM   4033  O OD1   . ASN C 1 193 ? 24.965  -37.605 -25.478 1.00 47.61  ? 194 ASN C OD1   1 
ATOM   4034  N ND2   . ASN C 1 193 ? 23.892  -38.224 -27.352 1.00 48.25  ? 194 ASN C ND2   1 
ATOM   4035  N N     . GLN C 1 194 ? 20.544  -35.420 -25.629 1.00 47.09  ? 195 GLN C N     1 
ATOM   4036  C CA    . GLN C 1 194 ? 20.058  -34.400 -26.543 1.00 48.59  ? 195 GLN C CA    1 
ATOM   4037  C C     . GLN C 1 194 ? 20.631  -33.044 -26.143 1.00 48.85  ? 195 GLN C C     1 
ATOM   4038  O O     . GLN C 1 194 ? 20.833  -32.177 -26.991 1.00 46.74  ? 195 GLN C O     1 
ATOM   4039  C CB    . GLN C 1 194 ? 18.531  -34.333 -26.537 1.00 48.82  ? 195 GLN C CB    1 
ATOM   4040  C CG    . GLN C 1 194 ? 17.845  -35.619 -26.983 1.00 49.29  ? 195 GLN C CG    1 
ATOM   4041  C CD    . GLN C 1 194 ? 16.336  -35.529 -26.933 1.00 49.81  ? 195 GLN C CD    1 
ATOM   4042  O OE1   . GLN C 1 194 ? 15.715  -34.713 -27.623 1.00 43.85  ? 195 GLN C OE1   1 
ATOM   4043  N NE2   . GLN C 1 194 ? 15.729  -36.367 -26.105 1.00 51.48  ? 195 GLN C NE2   1 
ATOM   4044  N N     . TRP C 1 195 ? 20.893  -32.878 -24.842 1.00 43.86  ? 196 TRP C N     1 
ATOM   4045  C CA    . TRP C 1 195 ? 21.279  -31.587 -24.297 1.00 42.43  ? 196 TRP C CA    1 
ATOM   4046  C C     . TRP C 1 195 ? 22.615  -31.690 -23.566 1.00 43.94  ? 196 TRP C C     1 
ATOM   4047  O O     . TRP C 1 195 ? 23.313  -30.691 -23.404 1.00 50.22  ? 196 TRP C O     1 
ATOM   4048  C CB    . TRP C 1 195 ? 20.182  -31.062 -23.360 1.00 41.26  ? 196 TRP C CB    1 
ATOM   4049  C CG    . TRP C 1 195 ? 18.807  -31.059 -23.974 1.00 37.65  ? 196 TRP C CG    1 
ATOM   4050  C CD1   . TRP C 1 195 ? 18.294  -30.127 -24.828 1.00 40.32  ? 196 TRP C CD1   1 
ATOM   4051  C CD2   . TRP C 1 195 ? 17.760  -32.031 -23.765 1.00 36.96  ? 196 TRP C CD2   1 
ATOM   4052  N NE1   . TRP C 1 195 ? 17.010  -30.455 -25.175 1.00 38.09  ? 196 TRP C NE1   1 
ATOM   4053  C CE2   . TRP C 1 195 ? 16.654  -31.614 -24.537 1.00 39.47  ? 196 TRP C CE2   1 
ATOM   4054  C CE3   . TRP C 1 195 ? 17.649  -33.204 -23.009 1.00 33.77  ? 196 TRP C CE3   1 
ATOM   4055  C CZ2   . TRP C 1 195 ? 15.459  -32.330 -24.571 1.00 39.08  ? 196 TRP C CZ2   1 
ATOM   4056  C CZ3   . TRP C 1 195 ? 16.466  -33.909 -23.043 1.00 34.07  ? 196 TRP C CZ3   1 
ATOM   4057  C CH2   . TRP C 1 195 ? 15.388  -33.476 -23.813 1.00 36.09  ? 196 TRP C CH2   1 
ATOM   4058  N N     . TYR C 1 196 ? 22.961  -32.903 -23.122 1.00 42.87  ? 197 TYR C N     1 
ATOM   4059  C CA    . TYR C 1 196 ? 24.150  -33.105 -22.311 1.00 40.73  ? 197 TYR C CA    1 
ATOM   4060  C C     . TYR C 1 196 ? 25.039  -34.166 -22.953 1.00 38.75  ? 197 TYR C C     1 
ATOM   4061  O O     . TYR C 1 196 ? 24.569  -35.242 -23.313 1.00 38.75  ? 197 TYR C O     1 
ATOM   4062  C CB    . TYR C 1 196 ? 23.746  -33.500 -20.888 1.00 37.35  ? 197 TYR C CB    1 
ATOM   4063  C CG    . TYR C 1 196 ? 22.806  -32.512 -20.213 1.00 39.03  ? 197 TYR C CG    1 
ATOM   4064  C CD1   . TYR C 1 196 ? 23.292  -31.361 -19.604 1.00 37.41  ? 197 TYR C CD1   1 
ATOM   4065  C CD2   . TYR C 1 196 ? 21.434  -32.731 -20.183 1.00 37.24  ? 197 TYR C CD2   1 
ATOM   4066  C CE1   . TYR C 1 196 ? 22.442  -30.455 -18.992 1.00 36.22  ? 197 TYR C CE1   1 
ATOM   4067  C CE2   . TYR C 1 196 ? 20.574  -31.834 -19.572 1.00 35.50  ? 197 TYR C CE2   1 
ATOM   4068  C CZ    . TYR C 1 196 ? 21.080  -30.693 -18.975 1.00 35.58  ? 197 TYR C CZ    1 
ATOM   4069  O OH    . TYR C 1 196 ? 20.237  -29.803 -18.372 1.00 35.81  ? 197 TYR C OH    1 
ATOM   4070  N N     . PRO C 1 197 ? 26.351  -33.884 -23.121 1.00 45.92  ? 198 PRO C N     1 
ATOM   4071  C CA    . PRO C 1 197 ? 27.305  -34.890 -23.589 1.00 46.55  ? 198 PRO C CA    1 
ATOM   4072  C C     . PRO C 1 197 ? 27.307  -36.114 -22.676 1.00 50.49  ? 198 PRO C C     1 
ATOM   4073  O O     . PRO C 1 197 ? 26.766  -36.071 -21.573 1.00 48.97  ? 198 PRO C O     1 
ATOM   4074  C CB    . PRO C 1 197 ? 28.656  -34.147 -23.577 1.00 47.40  ? 198 PRO C CB    1 
ATOM   4075  C CG    . PRO C 1 197 ? 28.279  -32.679 -23.660 1.00 48.56  ? 198 PRO C CG    1 
ATOM   4076  C CD    . PRO C 1 197 ? 26.969  -32.568 -22.902 1.00 46.07  ? 198 PRO C CD    1 
ATOM   4077  N N     . LEU C 1 198 ? 27.933  -37.198 -23.146 1.00 51.71  ? 199 LEU C N     1 
ATOM   4078  C CA    . LEU C 1 198 ? 27.978  -38.445 -22.401 1.00 49.88  ? 199 LEU C CA    1 
ATOM   4079  C C     . LEU C 1 198 ? 28.994  -38.328 -21.267 1.00 46.56  ? 199 LEU C C     1 
ATOM   4080  O O     . LEU C 1 198 ? 28.893  -39.031 -20.263 1.00 46.77  ? 199 LEU C O     1 
ATOM   4081  C CB    . LEU C 1 198 ? 28.318  -39.602 -23.340 1.00 50.83  ? 199 LEU C CB    1 
ATOM   4082  C CG    . LEU C 1 198 ? 27.276  -39.923 -24.416 1.00 52.49  ? 199 LEU C CG    1 
ATOM   4083  C CD1   . LEU C 1 198 ? 27.667  -41.169 -25.193 1.00 52.94  ? 199 LEU C CD1   1 
ATOM   4084  C CD2   . LEU C 1 198 ? 25.894  -40.083 -23.805 1.00 53.74  ? 199 LEU C CD2   1 
ATOM   4085  N N     . ASP C 1 199 ? 29.968  -37.429 -21.440 1.00 42.93  ? 200 ASP C N     1 
ATOM   4086  C CA    . ASP C 1 199 ? 31.046  -37.269 -20.480 1.00 44.17  ? 200 ASP C CA    1 
ATOM   4087  C C     . ASP C 1 199 ? 30.735  -36.099 -19.551 1.00 43.25  ? 200 ASP C C     1 
ATOM   4088  O O     . ASP C 1 199 ? 31.621  -35.600 -18.861 1.00 41.56  ? 200 ASP C O     1 
ATOM   4089  C CB    . ASP C 1 199 ? 32.381  -37.066 -21.179 1.00 47.42  ? 200 ASP C CB    1 
ATOM   4090  C CG    . ASP C 1 199 ? 32.471  -35.831 -22.063 1.00 50.85  ? 200 ASP C CG    1 
ATOM   4091  O OD1   . ASP C 1 199 ? 31.462  -35.100 -22.152 1.00 52.61  ? 200 ASP C OD1   1 
ATOM   4092  O OD2   . ASP C 1 199 ? 33.549  -35.610 -22.654 1.00 55.27  ? 200 ASP C OD2   1 
ATOM   4093  N N     . HIS C 1 200 ? 29.471  -35.664 -19.549 1.00 42.29  ? 201 HIS C N     1 
ATOM   4094  C CA    . HIS C 1 200 ? 29.050  -34.555 -18.711 1.00 44.45  ? 201 HIS C CA    1 
ATOM   4095  C C     . HIS C 1 200 ? 28.957  -35.028 -17.263 1.00 39.00  ? 201 HIS C C     1 
ATOM   4096  O O     . HIS C 1 200 ? 28.263  -35.997 -16.964 1.00 39.90  ? 201 HIS C O     1 
ATOM   4097  C CB    . HIS C 1 200 ? 27.730  -33.960 -19.213 1.00 46.41  ? 201 HIS C CB    1 
ATOM   4098  C CG    . HIS C 1 200 ? 27.255  -32.806 -18.396 1.00 45.49  ? 201 HIS C CG    1 
ATOM   4099  N ND1   . HIS C 1 200 ? 27.827  -31.555 -18.478 1.00 46.34  ? 201 HIS C ND1   1 
ATOM   4100  C CD2   . HIS C 1 200 ? 26.304  -32.717 -17.459 1.00 40.32  ? 201 HIS C CD2   1 
ATOM   4101  C CE1   . HIS C 1 200 ? 27.218  -30.740 -17.630 1.00 41.85  ? 201 HIS C CE1   1 
ATOM   4102  N NE2   . HIS C 1 200 ? 26.287  -31.423 -17.004 1.00 42.87  ? 201 HIS C NE2   1 
ATOM   4103  N N     . GLU C 1 201 ? 29.669  -34.327 -16.376 1.00 35.21  ? 202 GLU C N     1 
ATOM   4104  C CA    . GLU C 1 201 ? 29.734  -34.695 -14.972 1.00 39.76  ? 202 GLU C CA    1 
ATOM   4105  C C     . GLU C 1 201 ? 28.384  -34.432 -14.310 1.00 35.73  ? 202 GLU C C     1 
ATOM   4106  O O     . GLU C 1 201 ? 27.910  -33.299 -14.280 1.00 32.49  ? 202 GLU C O     1 
ATOM   4107  C CB    . GLU C 1 201 ? 30.841  -33.911 -14.265 1.00 41.27  ? 202 GLU C CB    1 
ATOM   4108  C CG    . GLU C 1 201 ? 30.910  -34.183 -12.766 1.00 43.72  ? 202 GLU C CG    1 
ATOM   4109  C CD    . GLU C 1 201 ? 31.973  -33.384 -12.035 1.00 45.84  ? 202 GLU C CD    1 
ATOM   4110  O OE1   . GLU C 1 201 ? 33.168  -33.549 -12.357 1.00 54.14  ? 202 GLU C OE1   1 
ATOM   4111  O OE2   . GLU C 1 201 ? 31.603  -32.592 -11.144 1.00 51.55  ? 202 GLU C OE2   1 
ATOM   4112  N N     . VAL C 1 202 ? 27.776  -35.502 -13.788 1.00 34.49  ? 203 VAL C N     1 
ATOM   4113  C CA    . VAL C 1 202 ? 26.560  -35.395 -13.001 1.00 30.96  ? 203 VAL C CA    1 
ATOM   4114  C C     . VAL C 1 202 ? 26.889  -35.820 -11.574 1.00 30.69  ? 203 VAL C C     1 
ATOM   4115  O O     . VAL C 1 202 ? 27.936  -36.416 -11.328 1.00 27.59  ? 203 VAL C O     1 
ATOM   4116  C CB    . VAL C 1 202 ? 25.409  -36.239 -13.581 1.00 30.14  ? 203 VAL C CB    1 
ATOM   4117  C CG1   . VAL C 1 202 ? 25.048  -35.805 -14.996 1.00 31.61  ? 203 VAL C CG1   1 
ATOM   4118  C CG2   . VAL C 1 202 ? 25.720  -37.730 -13.539 1.00 29.83  ? 203 VAL C CG2   1 
ATOM   4119  N N     . VAL C 1 203 ? 25.981  -35.514 -10.642 1.00 29.24  ? 204 VAL C N     1 
ATOM   4120  C CA    . VAL C 1 203 ? 26.214  -35.782 -9.234  1.00 27.98  ? 204 VAL C CA    1 
ATOM   4121  C C     . VAL C 1 203 ? 25.046  -36.586 -8.672  1.00 28.99  ? 204 VAL C C     1 
ATOM   4122  O O     . VAL C 1 203 ? 23.887  -36.203 -8.825  1.00 32.46  ? 204 VAL C O     1 
ATOM   4123  C CB    . VAL C 1 203 ? 26.413  -34.476 -8.441  1.00 28.46  ? 204 VAL C CB    1 
ATOM   4124  C CG1   . VAL C 1 203 ? 26.622  -34.743 -6.955  1.00 28.75  ? 204 VAL C CG1   1 
ATOM   4125  C CG2   . VAL C 1 203 ? 27.556  -33.640 -9.003  1.00 28.76  ? 204 VAL C CG2   1 
ATOM   4126  N N     . ILE C 1 204 ? 25.373  -37.707 -8.023  1.00 28.82  ? 205 ILE C N     1 
ATOM   4127  C CA    . ILE C 1 204 ? 24.405  -38.460 -7.246  1.00 32.28  ? 205 ILE C CA    1 
ATOM   4128  C C     . ILE C 1 204 ? 24.446  -37.939 -5.814  1.00 31.31  ? 205 ILE C C     1 
ATOM   4129  O O     . ILE C 1 204 ? 25.446  -38.105 -5.119  1.00 33.49  ? 205 ILE C O     1 
ATOM   4130  C CB    . ILE C 1 204 ? 24.695  -39.971 -7.312  1.00 31.00  ? 205 ILE C CB    1 
ATOM   4131  C CG1   . ILE C 1 204 ? 24.614  -40.496 -8.745  1.00 31.89  ? 205 ILE C CG1   1 
ATOM   4132  C CG2   . ILE C 1 204 ? 23.768  -40.744 -6.373  1.00 30.88  ? 205 ILE C CG2   1 
ATOM   4133  C CD1   . ILE C 1 204 ? 24.988  -41.960 -8.890  1.00 34.41  ? 205 ILE C CD1   1 
ATOM   4134  N N     . TYR C 1 205 ? 23.353  -37.298 -5.389  1.00 31.53  ? 206 TYR C N     1 
ATOM   4135  C CA    . TYR C 1 205 ? 23.306  -36.657 -4.086  1.00 29.10  ? 206 TYR C CA    1 
ATOM   4136  C C     . TYR C 1 205 ? 22.364  -37.423 -3.163  1.00 27.29  ? 206 TYR C C     1 
ATOM   4137  O O     . TYR C 1 205 ? 21.262  -37.799 -3.557  1.00 30.31  ? 206 TYR C O     1 
ATOM   4138  C CB    . TYR C 1 205 ? 22.872  -35.193 -4.204  1.00 27.01  ? 206 TYR C CB    1 
ATOM   4139  C CG    . TYR C 1 205 ? 22.598  -34.527 -2.863  1.00 29.52  ? 206 TYR C CG    1 
ATOM   4140  C CD1   . TYR C 1 205 ? 23.639  -34.185 -2.008  1.00 29.85  ? 206 TYR C CD1   1 
ATOM   4141  C CD2   . TYR C 1 205 ? 21.302  -34.235 -2.454  1.00 30.25  ? 206 TYR C CD2   1 
ATOM   4142  C CE1   . TYR C 1 205 ? 23.400  -33.582 -0.784  1.00 28.09  ? 206 TYR C CE1   1 
ATOM   4143  C CE2   . TYR C 1 205 ? 21.050  -33.628 -1.234  1.00 31.75  ? 206 TYR C CE2   1 
ATOM   4144  C CZ    . TYR C 1 205 ? 22.102  -33.300 -0.398  1.00 28.58  ? 206 TYR C CZ    1 
ATOM   4145  O OH    . TYR C 1 205 ? 21.862  -32.703 0.804   1.00 31.69  ? 206 TYR C OH    1 
ATOM   4146  N N     . GLU C 1 206 ? 22.826  -37.634 -1.926  1.00 25.35  ? 207 GLU C N     1 
ATOM   4147  C CA    . GLU C 1 206 ? 22.006  -38.192 -0.866  1.00 25.85  ? 207 GLU C CA    1 
ATOM   4148  C C     . GLU C 1 206 ? 22.291  -37.429 0.425   1.00 27.53  ? 207 GLU C C     1 
ATOM   4149  O O     . GLU C 1 206 ? 23.406  -37.471 0.942   1.00 25.87  ? 207 GLU C O     1 
ATOM   4150  C CB    . GLU C 1 206 ? 22.287  -39.684 -0.685  1.00 28.92  ? 207 GLU C CB    1 
ATOM   4151  C CG    . GLU C 1 206 ? 21.908  -40.522 -1.902  1.00 30.55  ? 207 GLU C CG    1 
ATOM   4152  C CD    . GLU C 1 206 ? 22.206  -42.003 -1.755  1.00 34.70  ? 207 GLU C CD    1 
ATOM   4153  O OE1   . GLU C 1 206 ? 22.713  -42.405 -0.685  1.00 36.36  ? 207 GLU C OE1   1 
ATOM   4154  O OE2   . GLU C 1 206 ? 21.933  -42.755 -2.714  1.00 36.82  ? 207 GLU C OE2   1 
ATOM   4155  N N     . ALA C 1 207 ? 21.274  -36.716 0.922   1.00 27.54  ? 208 ALA C N     1 
ATOM   4156  C CA    . ALA C 1 207 ? 21.393  -35.963 2.159   1.00 28.88  ? 208 ALA C CA    1 
ATOM   4157  C C     . ALA C 1 207 ? 21.428  -36.929 3.339   1.00 26.86  ? 208 ALA C C     1 
ATOM   4158  O O     . ALA C 1 207 ? 20.724  -37.936 3.342   1.00 28.43  ? 208 ALA C O     1 
ATOM   4159  C CB    . ALA C 1 207 ? 20.247  -34.981 2.280   1.00 30.57  ? 208 ALA C CB    1 
ATOM   4160  N N     . ALA C 1 208 ? 22.260  -36.611 4.335   1.00 24.67  ? 209 ALA C N     1 
ATOM   4161  C CA    . ALA C 1 208 ? 22.413  -37.462 5.502   1.00 25.74  ? 209 ALA C CA    1 
ATOM   4162  C C     . ALA C 1 208 ? 21.166  -37.363 6.374   1.00 27.48  ? 209 ALA C C     1 
ATOM   4163  O O     . ALA C 1 208 ? 20.489  -36.337 6.388   1.00 28.16  ? 209 ALA C O     1 
ATOM   4164  C CB    . ALA C 1 208 ? 23.660  -37.075 6.266   1.00 26.01  ? 209 ALA C CB    1 
ATOM   4165  N N     . ASN C 1 209 ? 20.867  -38.450 7.090   1.00 26.39  ? 210 ASN C N     1 
ATOM   4166  C CA    . ASN C 1 209 ? 19.709  -38.502 7.964   1.00 25.25  ? 210 ASN C CA    1 
ATOM   4167  C C     . ASN C 1 209 ? 20.179  -38.452 9.415   1.00 23.61  ? 210 ASN C C     1 
ATOM   4168  O O     . ASN C 1 209 ? 19.394  -38.175 10.318  1.00 23.99  ? 210 ASN C O     1 
ATOM   4169  C CB    . ASN C 1 209 ? 18.853  -39.731 7.679   1.00 27.42  ? 210 ASN C CB    1 
ATOM   4170  C CG    . ASN C 1 209 ? 18.321  -39.740 6.265   1.00 28.33  ? 210 ASN C CG    1 
ATOM   4171  O OD1   . ASN C 1 209 ? 17.615  -38.811 5.858   1.00 29.64  ? 210 ASN C OD1   1 
ATOM   4172  N ND2   . ASN C 1 209 ? 18.643  -40.775 5.505   1.00 30.61  ? 210 ASN C ND2   1 
ATOM   4173  N N     . LEU C 1 210 ? 21.474  -38.710 9.622   1.00 23.91  ? 211 LEU C N     1 
ATOM   4174  C CA    . LEU C 1 210 ? 22.050  -38.729 10.956  1.00 26.78  ? 211 LEU C CA    1 
ATOM   4175  C C     . LEU C 1 210 ? 23.126  -37.653 11.061  1.00 27.72  ? 211 LEU C C     1 
ATOM   4176  O O     . LEU C 1 210 ? 23.757  -37.301 10.067  1.00 27.84  ? 211 LEU C O     1 
ATOM   4177  C CB    . LEU C 1 210 ? 22.608  -40.119 11.256  1.00 25.19  ? 211 LEU C CB    1 
ATOM   4178  C CG    . LEU C 1 210 ? 21.587  -41.262 11.248  1.00 27.54  ? 211 LEU C CG    1 
ATOM   4179  C CD1   . LEU C 1 210 ? 22.232  -42.576 11.649  1.00 30.23  ? 211 LEU C CD1   1 
ATOM   4180  C CD2   . LEU C 1 210 ? 20.413  -40.942 12.156  1.00 28.80  ? 211 LEU C CD2   1 
ATOM   4181  N N     . PRO C 1 211 ? 23.367  -37.106 12.275  1.00 30.81  ? 212 PRO C N     1 
ATOM   4182  C CA    . PRO C 1 211 ? 24.332  -36.020 12.460  1.00 34.18  ? 212 PRO C CA    1 
ATOM   4183  C C     . PRO C 1 211 ? 25.787  -36.482 12.443  1.00 37.70  ? 212 PRO C C     1 
ATOM   4184  O O     . PRO C 1 211 ? 26.703  -35.663 12.487  1.00 45.53  ? 212 PRO C O     1 
ATOM   4185  C CB    . PRO C 1 211 ? 23.914  -35.457 13.830  1.00 32.32  ? 212 PRO C CB    1 
ATOM   4186  C CG    . PRO C 1 211 ? 23.415  -36.672 14.585  1.00 33.13  ? 212 PRO C CG    1 
ATOM   4187  C CD    . PRO C 1 211 ? 22.714  -37.512 13.529  1.00 34.33  ? 212 PRO C CD    1 
ATOM   4188  N N     . ILE C 1 212 ? 25.983  -37.804 12.389  1.00 40.34  ? 213 ILE C N     1 
ATOM   4189  C CA    . ILE C 1 212 ? 27.312  -38.389 12.327  1.00 38.87  ? 213 ILE C CA    1 
ATOM   4190  C C     . ILE C 1 212 ? 27.558  -38.895 10.909  1.00 40.72  ? 213 ILE C C     1 
ATOM   4191  O O     . ILE C 1 212 ? 28.614  -39.451 10.617  1.00 39.33  ? 213 ILE C O     1 
ATOM   4192  C CB    . ILE C 1 212 ? 27.464  -39.516 13.365  1.00 38.58  ? 213 ILE C CB    1 
ATOM   4193  C CG1   . ILE C 1 212 ? 26.383  -40.586 13.198  1.00 40.71  ? 213 ILE C CG1   1 
ATOM   4194  C CG2   . ILE C 1 212 ? 27.483  -38.953 14.785  1.00 38.31  ? 213 ILE C CG2   1 
ATOM   4195  C CD1   . ILE C 1 212 ? 26.374  -41.257 11.837  1.00 40.54  ? 213 ILE C CD1   1 
ATOM   4196  N N     . GLN C 1 213 ? 26.566  -38.690 10.038  1.00 42.30  ? 214 GLN C N     1 
ATOM   4197  C CA    . GLN C 1 213 ? 26.606  -39.209 8.683   1.00 40.64  ? 214 GLN C CA    1 
ATOM   4198  C C     . GLN C 1 213 ? 26.953  -38.085 7.713   1.00 39.67  ? 214 GLN C C     1 
ATOM   4199  O O     . GLN C 1 213 ? 26.334  -37.025 7.736   1.00 46.30  ? 214 GLN C O     1 
ATOM   4200  C CB    . GLN C 1 213 ? 25.254  -39.824 8.323   1.00 43.14  ? 214 GLN C CB    1 
ATOM   4201  C CG    . GLN C 1 213 ? 25.176  -40.369 6.902   1.00 49.14  ? 214 GLN C CG    1 
ATOM   4202  C CD    . GLN C 1 213 ? 23.766  -40.711 6.476   1.00 50.37  ? 214 GLN C CD    1 
ATOM   4203  O OE1   . GLN C 1 213 ? 22.798  -40.492 7.215   1.00 54.16  ? 214 GLN C OE1   1 
ATOM   4204  N NE2   . GLN C 1 213 ? 23.634  -41.241 5.269   1.00 53.34  ? 214 GLN C NE2   1 
ATOM   4205  N N     . ALA C 1 214 ? 27.952  -38.337 6.862   1.00 39.89  ? 215 ALA C N     1 
ATOM   4206  C CA    . ALA C 1 214 ? 28.312  -37.415 5.798   1.00 38.53  ? 215 ALA C CA    1 
ATOM   4207  C C     . ALA C 1 214 ? 27.383  -37.633 4.608   1.00 34.27  ? 215 ALA C C     1 
ATOM   4208  O O     . ALA C 1 214 ? 26.939  -38.751 4.359   1.00 32.11  ? 215 ALA C O     1 
ATOM   4209  C CB    . ALA C 1 214 ? 29.762  -37.612 5.413   1.00 42.05  ? 215 ALA C CB    1 
ATOM   4210  N N     . PRO C 1 215 ? 27.053  -36.572 3.840   1.00 37.74  ? 216 PRO C N     1 
ATOM   4211  C CA    . PRO C 1 215 ? 26.195  -36.718 2.665   1.00 37.38  ? 216 PRO C CA    1 
ATOM   4212  C C     . PRO C 1 215 ? 26.897  -37.484 1.547   1.00 33.37  ? 216 PRO C C     1 
ATOM   4213  O O     . PRO C 1 215 ? 28.122  -37.577 1.527   1.00 35.09  ? 216 PRO C O     1 
ATOM   4214  C CB    . PRO C 1 215 ? 25.888  -35.261 2.276   1.00 35.79  ? 216 PRO C CB    1 
ATOM   4215  C CG    . PRO C 1 215 ? 27.094  -34.488 2.772   1.00 36.60  ? 216 PRO C CG    1 
ATOM   4216  C CD    . PRO C 1 215 ? 27.496  -35.187 4.061   1.00 39.50  ? 216 PRO C CD    1 
ATOM   4217  N N     . ARG C 1 216 ? 26.102  -38.039 0.628   1.00 32.75  ? 217 ARG C N     1 
ATOM   4218  C CA    . ARG C 1 216 ? 26.637  -38.701 -0.548  1.00 35.37  ? 217 ARG C CA    1 
ATOM   4219  C C     . ARG C 1 216 ? 26.711  -37.691 -1.688  1.00 31.96  ? 217 ARG C C     1 
ATOM   4220  O O     . ARG C 1 216 ? 25.696  -37.126 -2.090  1.00 27.91  ? 217 ARG C O     1 
ATOM   4221  C CB    . ARG C 1 216 ? 25.781  -39.905 -0.955  1.00 35.56  ? 217 ARG C CB    1 
ATOM   4222  C CG    . ARG C 1 216 ? 26.324  -40.660 -2.161  1.00 41.39  ? 217 ARG C CG    1 
ATOM   4223  C CD    . ARG C 1 216 ? 25.406  -41.787 -2.611  1.00 41.79  ? 217 ARG C CD    1 
ATOM   4224  N NE    . ARG C 1 216 ? 25.987  -42.564 -3.711  1.00 45.30  ? 217 ARG C NE    1 
ATOM   4225  C CZ    . ARG C 1 216 ? 25.389  -43.584 -4.315  1.00 48.55  ? 217 ARG C CZ    1 
ATOM   4226  N NH1   . ARG C 1 216 ? 24.172  -43.948 -3.951  1.00 48.04  ? 217 ARG C NH1   1 
ATOM   4227  N NH2   . ARG C 1 216 ? 26.008  -44.234 -5.285  1.00 45.42  ? 217 ARG C NH2   1 
ATOM   4228  N N     . ILE C 1 217 ? 27.928  -37.462 -2.189  1.00 34.40  ? 218 ILE C N     1 
ATOM   4229  C CA    . ILE C 1 217 ? 28.145  -36.558 -3.305  1.00 39.97  ? 218 ILE C CA    1 
ATOM   4230  C C     . ILE C 1 217 ? 29.088  -37.232 -4.297  1.00 42.38  ? 218 ILE C C     1 
ATOM   4231  O O     . ILE C 1 217 ? 30.280  -36.936 -4.331  1.00 45.85  ? 218 ILE C O     1 
ATOM   4232  C CB    . ILE C 1 217 ? 28.695  -35.203 -2.819  1.00 40.60  ? 218 ILE C CB    1 
ATOM   4233  C CG1   . ILE C 1 217 ? 27.823  -34.605 -1.714  1.00 41.72  ? 218 ILE C CG1   1 
ATOM   4234  C CG2   . ILE C 1 217 ? 28.869  -34.234 -3.989  1.00 41.54  ? 218 ILE C CG2   1 
ATOM   4235  C CD1   . ILE C 1 217 ? 28.316  -33.268 -1.191  1.00 44.20  ? 218 ILE C CD1   1 
ATOM   4236  N N     . GLU C 1 218 ? 28.533  -38.148 -5.097  1.00 42.19  ? 219 GLU C N     1 
ATOM   4237  C CA    . GLU C 1 218 ? 29.316  -38.909 -6.055  1.00 44.19  ? 219 GLU C CA    1 
ATOM   4238  C C     . GLU C 1 218 ? 29.263  -38.221 -7.416  1.00 40.84  ? 219 GLU C C     1 
ATOM   4239  O O     . GLU C 1 218 ? 28.193  -38.072 -8.002  1.00 40.45  ? 219 GLU C O     1 
ATOM   4240  C CB    . GLU C 1 218 ? 28.805  -40.346 -6.152  1.00 47.59  ? 219 GLU C CB    1 
ATOM   4241  C CG    . GLU C 1 218 ? 29.590  -41.198 -7.145  1.00 51.70  ? 219 GLU C CG    1 
ATOM   4242  C CD    . GLU C 1 218 ? 29.144  -42.647 -7.214  1.00 52.13  ? 219 GLU C CD    1 
ATOM   4243  O OE1   . GLU C 1 218 ? 28.201  -43.011 -6.481  1.00 55.34  ? 219 GLU C OE1   1 
ATOM   4244  O OE2   . GLU C 1 218 ? 29.741  -43.412 -8.001  1.00 61.55  ? 219 GLU C OE2   1 
ATOM   4245  N N     . ARG C 1 219 ? 30.435  -37.804 -7.901  1.00 40.11  ? 220 ARG C N     1 
ATOM   4246  C CA    . ARG C 1 219 ? 30.561  -37.217 -9.224  1.00 40.40  ? 220 ARG C CA    1 
ATOM   4247  C C     . ARG C 1 219 ? 30.986  -38.306 -10.205 1.00 40.04  ? 220 ARG C C     1 
ATOM   4248  O O     . ARG C 1 219 ? 31.854  -39.119 -9.896  1.00 42.74  ? 220 ARG C O     1 
ATOM   4249  C CB    . ARG C 1 219 ? 31.578  -36.070 -9.201  1.00 38.84  ? 220 ARG C CB    1 
ATOM   4250  C CG    . ARG C 1 219 ? 31.234  -34.943 -8.238  1.00 40.67  ? 220 ARG C CG    1 
ATOM   4251  C CD    . ARG C 1 219 ? 32.369  -33.938 -8.106  1.00 43.62  ? 220 ARG C CD    1 
ATOM   4252  N NE    . ARG C 1 219 ? 32.056  -32.873 -7.147  1.00 46.09  ? 220 ARG C NE    1 
ATOM   4253  C CZ    . ARG C 1 219 ? 31.122  -31.946 -7.324  1.00 51.18  ? 220 ARG C CZ    1 
ATOM   4254  N NH1   . ARG C 1 219 ? 30.434  -31.905 -8.451  1.00 53.15  ? 220 ARG C NH1   1 
ATOM   4255  N NH2   . ARG C 1 219 ? 30.893  -31.050 -6.380  1.00 47.46  ? 220 ARG C NH2   1 
ATOM   4256  N N     . LEU C 1 220 ? 30.360  -38.314 -11.385 1.00 38.12  ? 221 LEU C N     1 
ATOM   4257  C CA    . LEU C 1 220 ? 30.669  -39.301 -12.405 1.00 36.90  ? 221 LEU C CA    1 
ATOM   4258  C C     . LEU C 1 220 ? 30.114  -38.833 -13.746 1.00 36.52  ? 221 LEU C C     1 
ATOM   4259  O O     . LEU C 1 220 ? 29.212  -38.000 -13.793 1.00 35.21  ? 221 LEU C O     1 
ATOM   4260  C CB    . LEU C 1 220 ? 30.093  -40.661 -12.011 1.00 37.67  ? 221 LEU C CB    1 
ATOM   4261  C CG    . LEU C 1 220 ? 28.567  -40.789 -12.073 1.00 37.62  ? 221 LEU C CG    1 
ATOM   4262  C CD1   . LEU C 1 220 ? 28.130  -42.199 -11.711 1.00 39.43  ? 221 LEU C CD1   1 
ATOM   4263  C CD2   . LEU C 1 220 ? 27.889  -39.771 -11.171 1.00 37.26  ? 221 LEU C CD2   1 
ATOM   4264  N N     . PRO C 1 221 ? 30.642  -39.353 -14.876 1.00 40.21  ? 222 PRO C N     1 
ATOM   4265  C CA    . PRO C 1 221 ? 30.103  -39.026 -16.195 1.00 41.33  ? 222 PRO C CA    1 
ATOM   4266  C C     . PRO C 1 221 ? 28.692  -39.582 -16.363 1.00 41.03  ? 222 PRO C C     1 
ATOM   4267  O O     . PRO C 1 221 ? 28.369  -40.642 -15.831 1.00 43.42  ? 222 PRO C O     1 
ATOM   4268  C CB    . PRO C 1 221 ? 31.115  -39.660 -17.169 1.00 42.33  ? 222 PRO C CB    1 
ATOM   4269  C CG    . PRO C 1 221 ? 31.752  -40.780 -16.368 1.00 42.76  ? 222 PRO C CG    1 
ATOM   4270  C CD    . PRO C 1 221 ? 31.785  -40.276 -14.935 1.00 39.73  ? 222 PRO C CD    1 
ATOM   4271  N N     . LEU C 1 222 ? 27.862  -38.847 -17.109 1.00 41.40  ? 223 LEU C N     1 
ATOM   4272  C CA    . LEU C 1 222 ? 26.468  -39.204 -17.308 1.00 41.85  ? 223 LEU C CA    1 
ATOM   4273  C C     . LEU C 1 222 ? 26.366  -40.629 -17.845 1.00 41.19  ? 223 LEU C C     1 
ATOM   4274  O O     . LEU C 1 222 ? 25.361  -41.305 -17.634 1.00 46.06  ? 223 LEU C O     1 
ATOM   4275  C CB    . LEU C 1 222 ? 25.832  -38.199 -18.266 1.00 44.90  ? 223 LEU C CB    1 
ATOM   4276  C CG    . LEU C 1 222 ? 24.380  -38.478 -18.668 1.00 46.72  ? 223 LEU C CG    1 
ATOM   4277  C CD1   . LEU C 1 222 ? 23.448  -38.346 -17.476 1.00 47.75  ? 223 LEU C CD1   1 
ATOM   4278  C CD2   . LEU C 1 222 ? 23.946  -37.559 -19.796 1.00 47.17  ? 223 LEU C CD2   1 
ATOM   4279  N N     . ALA C 1 223 ? 27.419  -41.074 -18.536 1.00 42.20  ? 224 ALA C N     1 
ATOM   4280  C CA    . ALA C 1 223 ? 27.403  -42.352 -19.230 1.00 38.50  ? 224 ALA C CA    1 
ATOM   4281  C C     . ALA C 1 223 ? 27.437  -43.507 -18.231 1.00 36.37  ? 224 ALA C C     1 
ATOM   4282  O O     . ALA C 1 223 ? 26.928  -44.588 -18.516 1.00 31.84  ? 224 ALA C O     1 
ATOM   4283  C CB    . ALA C 1 223 ? 28.567  -42.424 -20.194 1.00 41.33  ? 224 ALA C CB    1 
ATOM   4284  N N     . ASN C 1 224 ? 28.039  -43.265 -17.060 1.00 34.92  ? 225 ASN C N     1 
ATOM   4285  C CA    . ASN C 1 224 ? 28.261  -44.315 -16.078 1.00 34.19  ? 225 ASN C CA    1 
ATOM   4286  C C     . ASN C 1 224 ? 27.069  -44.410 -15.128 1.00 35.11  ? 225 ASN C C     1 
ATOM   4287  O O     . ASN C 1 224 ? 27.071  -45.223 -14.206 1.00 33.86  ? 225 ASN C O     1 
ATOM   4288  C CB    . ASN C 1 224 ? 29.554  -44.092 -15.302 1.00 35.39  ? 225 ASN C CB    1 
ATOM   4289  C CG    . ASN C 1 224 ? 30.779  -44.256 -16.171 1.00 36.23  ? 225 ASN C CG    1 
ATOM   4290  O OD1   . ASN C 1 224 ? 30.663  -44.578 -17.358 1.00 40.49  ? 225 ASN C OD1   1 
ATOM   4291  N ND2   . ASN C 1 224 ? 31.956  -44.051 -15.599 1.00 35.82  ? 225 ASN C ND2   1 
ATOM   4292  N N     . LEU C 1 225 ? 26.055  -43.573 -15.362 1.00 38.98  ? 226 LEU C N     1 
ATOM   4293  C CA    . LEU C 1 225 ? 24.879  -43.543 -14.509 1.00 38.69  ? 226 LEU C CA    1 
ATOM   4294  C C     . LEU C 1 225 ? 24.299  -44.951 -14.395 1.00 42.46  ? 226 LEU C C     1 
ATOM   4295  O O     . LEU C 1 225 ? 24.042  -45.432 -13.293 1.00 43.75  ? 226 LEU C O     1 
ATOM   4296  C CB    . LEU C 1 225 ? 23.854  -42.559 -15.069 1.00 41.00  ? 226 LEU C CB    1 
ATOM   4297  C CG    . LEU C 1 225 ? 22.542  -42.443 -14.287 1.00 39.38  ? 226 LEU C CG    1 
ATOM   4298  C CD1   . LEU C 1 225 ? 22.789  -41.921 -12.881 1.00 40.68  ? 226 LEU C CD1   1 
ATOM   4299  C CD2   . LEU C 1 225 ? 21.548  -41.560 -15.022 1.00 37.83  ? 226 LEU C CD2   1 
ATOM   4300  N N     . PRO C 1 226 ? 24.078  -45.653 -15.529 1.00 42.57  ? 227 PRO C N     1 
ATOM   4301  C CA    . PRO C 1 226 ? 23.426  -46.965 -15.512 1.00 41.93  ? 227 PRO C CA    1 
ATOM   4302  C C     . PRO C 1 226 ? 24.098  -47.985 -14.594 1.00 41.27  ? 227 PRO C C     1 
ATOM   4303  O O     . PRO C 1 226 ? 23.455  -48.932 -14.145 1.00 43.72  ? 227 PRO C O     1 
ATOM   4304  C CB    . PRO C 1 226 ? 23.480  -47.400 -16.994 1.00 42.07  ? 227 PRO C CB    1 
ATOM   4305  C CG    . PRO C 1 226 ? 23.571  -46.098 -17.762 1.00 42.10  ? 227 PRO C CG    1 
ATOM   4306  C CD    . PRO C 1 226 ? 24.425  -45.203 -16.886 1.00 43.08  ? 227 PRO C CD    1 
ATOM   4307  N N     . GLN C 1 227 ? 25.393  -47.785 -14.327 1.00 45.62  ? 228 GLN C N     1 
ATOM   4308  C CA    . GLN C 1 227 ? 26.166  -48.726 -13.531 1.00 46.37  ? 228 GLN C CA    1 
ATOM   4309  C C     . GLN C 1 227 ? 26.295  -48.220 -12.096 1.00 39.34  ? 228 GLN C C     1 
ATOM   4310  O O     . GLN C 1 227 ? 26.892  -48.886 -11.253 1.00 35.98  ? 228 GLN C O     1 
ATOM   4311  C CB    . GLN C 1 227 ? 27.560  -48.945 -14.123 1.00 49.90  ? 228 GLN C CB    1 
ATOM   4312  C CG    . GLN C 1 227 ? 27.572  -49.704 -15.446 1.00 56.49  ? 228 GLN C CG    1 
ATOM   4313  C CD    . GLN C 1 227 ? 27.070  -48.883 -16.613 1.00 60.93  ? 228 GLN C CD    1 
ATOM   4314  O OE1   . GLN C 1 227 ? 27.606  -47.814 -16.926 1.00 66.09  ? 228 GLN C OE1   1 
ATOM   4315  N NE2   . GLN C 1 227 ? 26.038  -49.382 -17.276 1.00 64.51  ? 228 GLN C NE2   1 
ATOM   4316  N N     . ALA C 1 228 ? 25.732  -47.038 -11.829 1.00 38.49  ? 229 ALA C N     1 
ATOM   4317  C CA    . ALA C 1 228 ? 25.865  -46.403 -10.528 1.00 39.27  ? 229 ALA C CA    1 
ATOM   4318  C C     . ALA C 1 228 ? 24.936  -47.071 -9.518  1.00 38.33  ? 229 ALA C C     1 
ATOM   4319  O O     . ALA C 1 228 ? 23.865  -47.556 -9.875  1.00 37.72  ? 229 ALA C O     1 
ATOM   4320  C CB    . ALA C 1 228 ? 25.580  -44.922 -10.647 1.00 41.94  ? 229 ALA C CB    1 
ATOM   4321  N N     . HIS C 1 229 ? 25.370  -47.085 -8.252  1.00 38.48  ? 230 HIS C N     1 
ATOM   4322  C CA    . HIS C 1 229 ? 24.579  -47.633 -7.162  1.00 41.47  ? 230 HIS C CA    1 
ATOM   4323  C C     . HIS C 1 229 ? 23.582  -46.578 -6.691  1.00 37.65  ? 230 HIS C C     1 
ATOM   4324  O O     . HIS C 1 229 ? 23.968  -45.584 -6.081  1.00 40.78  ? 230 HIS C O     1 
ATOM   4325  C CB    . HIS C 1 229 ? 25.489  -48.085 -6.015  1.00 47.39  ? 230 HIS C CB    1 
ATOM   4326  C CG    . HIS C 1 229 ? 24.765  -48.738 -4.884  1.00 57.15  ? 230 HIS C CG    1 
ATOM   4327  N ND1   . HIS C 1 229 ? 24.697  -50.106 -4.729  1.00 60.31  ? 230 HIS C ND1   1 
ATOM   4328  C CD2   . HIS C 1 229 ? 24.099  -48.216 -3.845  1.00 60.27  ? 230 HIS C CD2   1 
ATOM   4329  C CE1   . HIS C 1 229 ? 24.001  -50.389 -3.637  1.00 64.44  ? 230 HIS C CE1   1 
ATOM   4330  N NE2   . HIS C 1 229 ? 23.626  -49.256 -3.086  1.00 63.70  ? 230 HIS C NE2   1 
ATOM   4331  N N     . LEU C 1 230 ? 22.297  -46.808 -6.980  1.00 34.80  ? 231 LEU C N     1 
ATOM   4332  C CA    . LEU C 1 230 ? 21.253  -45.854 -6.641  1.00 32.89  ? 231 LEU C CA    1 
ATOM   4333  C C     . LEU C 1 230 ? 20.420  -46.397 -5.484  1.00 33.26  ? 231 LEU C C     1 
ATOM   4334  O O     . LEU C 1 230 ? 20.204  -47.601 -5.378  1.00 35.26  ? 231 LEU C O     1 
ATOM   4335  C CB    . LEU C 1 230 ? 20.387  -45.571 -7.868  1.00 31.36  ? 231 LEU C CB    1 
ATOM   4336  C CG    . LEU C 1 230 ? 21.109  -44.966 -9.075  1.00 33.62  ? 231 LEU C CG    1 
ATOM   4337  C CD1   . LEU C 1 230 ? 20.134  -44.696 -10.209 1.00 32.38  ? 231 LEU C CD1   1 
ATOM   4338  C CD2   . LEU C 1 230 ? 21.848  -43.695 -8.689  1.00 31.69  ? 231 LEU C CD2   1 
ATOM   4339  N N     . MET C 1 231 ? 19.964  -45.484 -4.620  1.00 33.71  ? 232 MET C N     1 
ATOM   4340  C CA    . MET C 1 231 ? 19.076  -45.826 -3.522  1.00 35.04  ? 232 MET C CA    1 
ATOM   4341  C C     . MET C 1 231 ? 17.805  -44.989 -3.632  1.00 34.33  ? 232 MET C C     1 
ATOM   4342  O O     . MET C 1 231 ? 17.801  -43.943 -4.277  1.00 33.03  ? 232 MET C O     1 
ATOM   4343  C CB    . MET C 1 231 ? 19.749  -45.576 -2.167  1.00 37.59  ? 232 MET C CB    1 
ATOM   4344  C CG    . MET C 1 231 ? 20.918  -46.500 -1.878  1.00 40.72  ? 232 MET C CG    1 
ATOM   4345  S SD    . MET C 1 231 ? 20.455  -48.243 -1.915  1.00 49.84  ? 232 MET C SD    1 
ATOM   4346  C CE    . MET C 1 231 ? 19.082  -48.244 -0.754  1.00 60.12  ? 232 MET C CE    1 
ATOM   4347  N N     . PRO C 1 232 ? 16.687  -45.426 -3.009  1.00 35.14  ? 233 PRO C N     1 
ATOM   4348  C CA    . PRO C 1 232 ? 15.421  -44.697 -3.095  1.00 35.71  ? 233 PRO C CA    1 
ATOM   4349  C C     . PRO C 1 232 ? 15.553  -43.205 -2.798  1.00 37.25  ? 233 PRO C C     1 
ATOM   4350  O O     . PRO C 1 232 ? 14.804  -42.393 -3.335  1.00 44.91  ? 233 PRO C O     1 
ATOM   4351  C CB    . PRO C 1 232 ? 14.543  -45.416 -2.050  1.00 34.99  ? 233 PRO C CB    1 
ATOM   4352  C CG    . PRO C 1 232 ? 15.096  -46.824 -2.005  1.00 36.06  ? 233 PRO C CG    1 
ATOM   4353  C CD    . PRO C 1 232 ? 16.590  -46.655 -2.207  1.00 36.32  ? 233 PRO C CD    1 
ATOM   4354  N N     . ILE C 1 233 ? 16.519  -42.857 -1.940  1.00 32.36  ? 234 ILE C N     1 
ATOM   4355  C CA    . ILE C 1 233 ? 16.655  -41.497 -1.446  1.00 30.92  ? 234 ILE C CA    1 
ATOM   4356  C C     . ILE C 1 233 ? 17.643  -40.726 -2.319  1.00 30.58  ? 234 ILE C C     1 
ATOM   4357  O O     . ILE C 1 233 ? 18.040  -39.617 -1.971  1.00 29.33  ? 234 ILE C O     1 
ATOM   4358  C CB    . ILE C 1 233 ? 17.094  -41.497 0.030   1.00 29.29  ? 234 ILE C CB    1 
ATOM   4359  C CG1   . ILE C 1 233 ? 18.482  -42.117 0.202   1.00 28.51  ? 234 ILE C CG1   1 
ATOM   4360  C CG2   . ILE C 1 233 ? 16.050  -42.189 0.908   1.00 30.52  ? 234 ILE C CG2   1 
ATOM   4361  C CD1   . ILE C 1 233 ? 19.024  -42.043 1.617   1.00 27.78  ? 234 ILE C CD1   1 
ATOM   4362  N N     . SER C 1 234 ? 18.021  -41.316 -3.457  1.00 28.68  ? 235 SER C N     1 
ATOM   4363  C CA    . SER C 1 234 ? 19.023  -40.723 -4.326  1.00 28.43  ? 235 SER C CA    1 
ATOM   4364  C C     . SER C 1 234 ? 18.386  -39.691 -5.254  1.00 28.13  ? 235 SER C C     1 
ATOM   4365  O O     . SER C 1 234 ? 17.366  -39.956 -5.885  1.00 29.41  ? 235 SER C O     1 
ATOM   4366  C CB    . SER C 1 234 ? 19.757  -41.780 -5.111  1.00 28.00  ? 235 SER C CB    1 
ATOM   4367  O OG    . SER C 1 234 ? 20.593  -42.554 -4.262  1.00 24.19  ? 235 SER C OG    1 
ATOM   4368  N N     . THR C 1 235 ? 19.008  -38.509 -5.318  1.00 28.79  ? 236 THR C N     1 
ATOM   4369  C CA    . THR C 1 235 ? 18.624  -37.476 -6.265  1.00 28.05  ? 236 THR C CA    1 
ATOM   4370  C C     . THR C 1 235 ? 19.772  -37.268 -7.249  1.00 29.36  ? 236 THR C C     1 
ATOM   4371  O O     . THR C 1 235 ? 20.939  -37.362 -6.874  1.00 30.93  ? 236 THR C O     1 
ATOM   4372  C CB    . THR C 1 235 ? 18.278  -36.189 -5.517  1.00 28.72  ? 236 THR C CB    1 
ATOM   4373  O OG1   . THR C 1 235 ? 17.127  -36.490 -4.735  1.00 27.74  ? 236 THR C OG1   1 
ATOM   4374  C CG2   . THR C 1 235 ? 17.969  -35.035 -6.455  1.00 29.03  ? 236 THR C CG2   1 
ATOM   4375  N N     . LEU C 1 236 ? 19.423  -36.987 -8.508  1.00 30.87  ? 237 LEU C N     1 
ATOM   4376  C CA    . LEU C 1 236 ? 20.409  -36.801 -9.560  1.00 32.86  ? 237 LEU C CA    1 
ATOM   4377  C C     . LEU C 1 236 ? 20.521  -35.316 -9.898  1.00 30.77  ? 237 LEU C C     1 
ATOM   4378  O O     . LEU C 1 236 ? 19.547  -34.692 -10.313 1.00 30.25  ? 237 LEU C O     1 
ATOM   4379  C CB    . LEU C 1 236 ? 20.015  -37.620 -10.788 1.00 34.00  ? 237 LEU C CB    1 
ATOM   4380  C CG    . LEU C 1 236 ? 20.915  -37.453 -12.017 1.00 36.77  ? 237 LEU C CG    1 
ATOM   4381  C CD1   . LEU C 1 236 ? 22.288  -38.060 -11.776 1.00 35.62  ? 237 LEU C CD1   1 
ATOM   4382  C CD2   . LEU C 1 236 ? 20.269  -38.054 -13.255 1.00 39.35  ? 237 LEU C CD2   1 
ATOM   4383  N N     . LEU C 1 237 ? 21.728  -34.768 -9.720  1.00 32.02  ? 238 LEU C N     1 
ATOM   4384  C CA    A LEU C 1 237 ? 22.007  -33.380 -10.048 0.70 29.17  ? 238 LEU C CA    1 
ATOM   4385  C CA    B LEU C 1 237 ? 22.000  -33.380 -10.050 0.30 30.42  ? 238 LEU C CA    1 
ATOM   4386  C C     . LEU C 1 237 ? 22.756  -33.324 -11.375 1.00 29.77  ? 238 LEU C C     1 
ATOM   4387  O O     . LEU C 1 237 ? 23.753  -34.018 -11.557 1.00 29.91  ? 238 LEU C O     1 
ATOM   4388  C CB    A LEU C 1 237 ? 22.819  -32.738 -8.925  0.70 29.91  ? 238 LEU C CB    1 
ATOM   4389  C CB    B LEU C 1 237 ? 22.795  -32.722 -8.922  0.30 31.31  ? 238 LEU C CB    1 
ATOM   4390  C CG    A LEU C 1 237 ? 23.388  -31.346 -9.222  0.70 31.13  ? 238 LEU C CG    1 
ATOM   4391  C CG    B LEU C 1 237 ? 22.981  -31.205 -9.028  0.30 32.47  ? 238 LEU C CG    1 
ATOM   4392  C CD1   A LEU C 1 237 ? 22.286  -30.302 -9.295  0.70 31.19  ? 238 LEU C CD1   1 
ATOM   4393  C CD1   B LEU C 1 237 ? 23.922  -30.701 -7.947  0.30 33.91  ? 238 LEU C CD1   1 
ATOM   4394  C CD2   A LEU C 1 237 ? 24.431  -30.958 -8.188  0.70 34.38  ? 238 LEU C CD2   1 
ATOM   4395  C CD2   B LEU C 1 237 ? 23.481  -30.801 -10.403 0.30 32.74  ? 238 LEU C CD2   1 
ATOM   4396  N N     . ILE C 1 238 ? 22.264  -32.488 -12.294 1.00 30.48  ? 239 ILE C N     1 
ATOM   4397  C CA    . ILE C 1 238 ? 22.885  -32.327 -13.598 1.00 29.77  ? 239 ILE C CA    1 
ATOM   4398  C C     . ILE C 1 238 ? 23.285  -30.864 -13.773 1.00 29.82  ? 239 ILE C C     1 
ATOM   4399  O O     . ILE C 1 238 ? 22.476  -30.038 -14.188 1.00 29.32  ? 239 ILE C O     1 
ATOM   4400  C CB    . ILE C 1 238 ? 21.942  -32.804 -14.717 1.00 29.52  ? 239 ILE C CB    1 
ATOM   4401  C CG1   . ILE C 1 238 ? 21.544  -34.268 -14.527 1.00 29.29  ? 239 ILE C CG1   1 
ATOM   4402  C CG2   . ILE C 1 238 ? 22.560  -32.561 -16.094 1.00 31.74  ? 239 ILE C CG2   1 
ATOM   4403  C CD1   . ILE C 1 238 ? 20.627  -34.808 -15.609 1.00 30.90  ? 239 ILE C CD1   1 
ATOM   4404  N N     . PRO C 1 239 ? 24.548  -30.503 -13.455 1.00 30.18  ? 240 PRO C N     1 
ATOM   4405  C CA    . PRO C 1 239 ? 25.007  -29.117 -13.567 1.00 31.75  ? 240 PRO C CA    1 
ATOM   4406  C C     . PRO C 1 239 ? 24.814  -28.545 -14.969 1.00 31.60  ? 240 PRO C C     1 
ATOM   4407  O O     . PRO C 1 239 ? 24.541  -29.281 -15.916 1.00 34.95  ? 240 PRO C O     1 
ATOM   4408  C CB    . PRO C 1 239 ? 26.496  -29.203 -13.171 1.00 34.45  ? 240 PRO C CB    1 
ATOM   4409  C CG    . PRO C 1 239 ? 26.585  -30.458 -12.324 1.00 33.52  ? 240 PRO C CG    1 
ATOM   4410  C CD    . PRO C 1 239 ? 25.588  -31.412 -12.954 1.00 31.69  ? 240 PRO C CD    1 
ATOM   4411  N N     . PRO C 1 240 ? 24.953  -27.211 -15.139 1.00 32.12  ? 241 PRO C N     1 
ATOM   4412  C CA    . PRO C 1 240 ? 24.773  -26.574 -16.444 1.00 35.44  ? 241 PRO C CA    1 
ATOM   4413  C C     . PRO C 1 240 ? 25.730  -27.128 -17.497 1.00 36.75  ? 241 PRO C C     1 
ATOM   4414  O O     . PRO C 1 240 ? 26.922  -27.280 -17.240 1.00 35.21  ? 241 PRO C O     1 
ATOM   4415  C CB    . PRO C 1 240 ? 25.032  -25.079 -16.158 1.00 33.82  ? 241 PRO C CB    1 
ATOM   4416  C CG    . PRO C 1 240 ? 24.807  -24.934 -14.664 1.00 31.73  ? 241 PRO C CG    1 
ATOM   4417  C CD    . PRO C 1 240 ? 25.272  -26.251 -14.073 1.00 33.44  ? 241 PRO C CD    1 
ATOM   4418  N N     . ALA C 1 241 ? 25.187  -27.416 -18.684 1.00 38.85  ? 242 ALA C N     1 
ATOM   4419  C CA    . ALA C 1 241 ? 25.980  -27.902 -19.801 1.00 39.64  ? 242 ALA C CA    1 
ATOM   4420  C C     . ALA C 1 241 ? 26.478  -26.722 -20.630 1.00 41.95  ? 242 ALA C C     1 
ATOM   4421  O O     . ALA C 1 241 ? 27.370  -26.875 -21.462 1.00 39.37  ? 242 ALA C O     1 
ATOM   4422  C CB    . ALA C 1 241 ? 25.159  -28.858 -20.639 1.00 38.49  ? 242 ALA C CB    1 
ATOM   4423  N N     . LYS C 1 242 ? 25.886  -25.547 -20.391 1.00 39.99  ? 243 LYS C N     1 
ATOM   4424  C CA    . LYS C 1 242 ? 26.247  -24.337 -21.110 1.00 44.98  ? 243 LYS C CA    1 
ATOM   4425  C C     . LYS C 1 242 ? 26.231  -23.154 -20.147 1.00 49.00  ? 243 LYS C C     1 
ATOM   4426  O O     . LYS C 1 242 ? 25.509  -23.169 -19.152 1.00 47.55  ? 243 LYS C O     1 
ATOM   4427  C CB    . LYS C 1 242 ? 25.273  -24.094 -22.268 1.00 46.91  ? 243 LYS C CB    1 
ATOM   4428  C CG    . LYS C 1 242 ? 25.124  -25.252 -23.244 1.00 51.56  ? 243 LYS C CG    1 
ATOM   4429  C CD    . LYS C 1 242 ? 24.118  -24.997 -24.359 1.00 57.67  ? 243 LYS C CD    1 
ATOM   4430  C CE    . LYS C 1 242 ? 24.490  -23.828 -25.216 1.00 64.48  ? 243 LYS C CE    1 
ATOM   4431  N NZ    . LYS C 1 242 ? 23.522  -23.618 -26.296 1.00 66.72  ? 243 LYS C NZ    1 
ATOM   4432  N N     . LYS C 1 243 ? 27.033  -22.131 -20.460 1.00 44.83  ? 244 LYS C N     1 
ATOM   4433  C CA    . LYS C 1 243 ? 27.078  -20.917 -19.663 1.00 47.75  ? 244 LYS C CA    1 
ATOM   4434  C C     . LYS C 1 243 ? 26.024  -19.941 -20.177 1.00 47.92  ? 244 LYS C C     1 
ATOM   4435  O O     . LYS C 1 243 ? 25.516  -20.094 -21.285 1.00 41.19  ? 244 LYS C O     1 
ATOM   4436  C CB    . LYS C 1 243 ? 28.472  -20.281 -19.698 1.00 52.51  ? 244 LYS C CB    1 
ATOM   4437  C CG    . LYS C 1 243 ? 29.567  -21.083 -19.006 1.00 55.45  ? 244 LYS C CG    1 
ATOM   4438  C CD    . LYS C 1 243 ? 30.897  -20.348 -18.891 1.00 62.71  ? 244 LYS C CD    1 
ATOM   4439  C CE    . LYS C 1 243 ? 31.490  -19.998 -20.220 1.00 66.64  ? 244 LYS C CE    1 
ATOM   4440  N NZ    . LYS C 1 243 ? 31.809  -21.194 -21.004 1.00 70.12  ? 244 LYS C NZ    1 
ATOM   4441  N N     . LEU C 1 244 ? 25.708  -18.937 -19.351 1.00 50.04  ? 245 LEU C N     1 
ATOM   4442  C CA    . LEU C 1 244 ? 24.699  -17.946 -19.685 1.00 49.69  ? 245 LEU C CA    1 
ATOM   4443  C C     . LEU C 1 244 ? 25.186  -17.106 -20.862 1.00 49.74  ? 245 LEU C C     1 
ATOM   4444  O O     . LEU C 1 244 ? 26.303  -16.594 -20.845 1.00 48.07  ? 245 LEU C O     1 
ATOM   4445  C CB    . LEU C 1 244 ? 24.402  -17.077 -18.464 1.00 49.90  ? 245 LEU C CB    1 
ATOM   4446  C CG    . LEU C 1 244 ? 23.912  -17.814 -17.213 1.00 51.66  ? 245 LEU C CG    1 
ATOM   4447  C CD1   . LEU C 1 244 ? 23.626  -16.832 -16.089 1.00 54.34  ? 245 LEU C CD1   1 
ATOM   4448  C CD2   . LEU C 1 244 ? 22.683  -18.654 -17.515 1.00 50.70  ? 245 LEU C CD2   1 
ATOM   4449  N N     . GLU C 1 245 ? 24.328  -16.975 -21.879 1.00 51.50  ? 246 GLU C N     1 
ATOM   4450  C CA    . GLU C 1 245 ? 24.620  -16.149 -23.039 1.00 51.81  ? 246 GLU C CA    1 
ATOM   4451  C C     . GLU C 1 245 ? 23.635  -14.982 -23.073 1.00 48.57  ? 246 GLU C C     1 
ATOM   4452  O O     . GLU C 1 245 ? 22.455  -15.153 -22.776 1.00 45.04  ? 246 GLU C O     1 
ATOM   4453  C CB    . GLU C 1 245 ? 24.547  -16.982 -24.319 1.00 52.49  ? 246 GLU C CB    1 
ATOM   4454  C CG    . GLU C 1 245 ? 25.558  -18.126 -24.355 1.00 56.02  ? 246 GLU C CG    1 
ATOM   4455  C CD    . GLU C 1 245 ? 25.522  -18.952 -25.629 1.00 56.32  ? 246 GLU C CD    1 
ATOM   4456  O OE1   . GLU C 1 245 ? 25.757  -18.378 -26.714 1.00 59.76  ? 246 GLU C OE1   1 
ATOM   4457  O OE2   . GLU C 1 245 ? 25.261  -20.170 -25.537 1.00 55.80  ? 246 GLU C OE2   1 
ATOM   4458  N N     . TYR C 1 246 ? 24.138  -13.798 -23.437 1.00 48.28  ? 247 TYR C N     1 
ATOM   4459  C CA    . TYR C 1 246 ? 23.343  -12.581 -23.404 1.00 50.35  ? 247 TYR C CA    1 
ATOM   4460  C C     . TYR C 1 246 ? 22.153  -12.723 -24.349 1.00 46.92  ? 247 TYR C C     1 
ATOM   4461  O O     . TYR C 1 246 ? 22.258  -13.347 -25.403 1.00 48.59  ? 247 TYR C O     1 
ATOM   4462  C CB    . TYR C 1 246 ? 24.191  -11.358 -23.768 1.00 51.73  ? 247 TYR C CB    1 
ATOM   4463  C CG    . TYR C 1 246 ? 25.321  -11.057 -22.793 1.00 52.41  ? 247 TYR C CG    1 
ATOM   4464  C CD1   . TYR C 1 246 ? 25.063  -10.499 -21.547 1.00 54.83  ? 247 TYR C CD1   1 
ATOM   4465  C CD2   . TYR C 1 246 ? 26.647  -11.301 -23.131 1.00 56.19  ? 247 TYR C CD2   1 
ATOM   4466  C CE1   . TYR C 1 246 ? 26.085  -10.217 -20.656 1.00 57.63  ? 247 TYR C CE1   1 
ATOM   4467  C CE2   . TYR C 1 246 ? 27.679  -11.020 -22.251 1.00 59.47  ? 247 TYR C CE2   1 
ATOM   4468  C CZ    . TYR C 1 246 ? 27.397  -10.476 -21.011 1.00 61.13  ? 247 TYR C CZ    1 
ATOM   4469  O OH    . TYR C 1 246 ? 28.410  -10.195 -20.139 1.00 65.55  ? 247 TYR C OH    1 
ATOM   4470  N N     . ASN C 1 247 ? 21.026  -12.124 -23.951 1.00 41.05  ? 248 ASN C N     1 
ATOM   4471  C CA    . ASN C 1 247 ? 19.813  -12.131 -24.750 1.00 38.01  ? 248 ASN C CA    1 
ATOM   4472  C C     . ASN C 1 247 ? 19.671  -10.774 -25.435 1.00 37.52  ? 248 ASN C C     1 
ATOM   4473  O O     . ASN C 1 247 ? 18.964  -9.896  -24.946 1.00 35.86  ? 248 ASN C O     1 
ATOM   4474  C CB    . ASN C 1 247 ? 18.601  -12.487 -23.895 1.00 38.75  ? 248 ASN C CB    1 
ATOM   4475  C CG    . ASN C 1 247 ? 17.339  -12.622 -24.712 1.00 38.25  ? 248 ASN C CG    1 
ATOM   4476  O OD1   . ASN C 1 247 ? 17.342  -12.340 -25.916 1.00 43.07  ? 248 ASN C OD1   1 
ATOM   4477  N ND2   . ASN C 1 247 ? 16.254  -13.043 -24.080 1.00 38.55  ? 248 ASN C ND2   1 
ATOM   4478  N N     . TYR C 1 248 ? 20.351  -10.621 -26.578 1.00 36.24  ? 249 TYR C N     1 
ATOM   4479  C CA    . TYR C 1 248 ? 20.439  -9.344  -27.269 1.00 36.62  ? 249 TYR C CA    1 
ATOM   4480  C C     . TYR C 1 248 ? 19.047  -8.874  -27.683 1.00 36.23  ? 249 TYR C C     1 
ATOM   4481  O O     . TYR C 1 248 ? 18.801  -7.674  -27.783 1.00 33.67  ? 249 TYR C O     1 
ATOM   4482  C CB    . TYR C 1 248 ? 21.367  -9.457  -28.483 1.00 36.13  ? 249 TYR C CB    1 
ATOM   4483  C CG    . TYR C 1 248 ? 22.840  -9.627  -28.135 1.00 36.40  ? 249 TYR C CG    1 
ATOM   4484  C CD1   . TYR C 1 248 ? 23.619  -8.534  -27.774 1.00 37.45  ? 249 TYR C CD1   1 
ATOM   4485  C CD2   . TYR C 1 248 ? 23.453  -10.873 -28.181 1.00 36.99  ? 249 TYR C CD2   1 
ATOM   4486  C CE1   . TYR C 1 248 ? 24.959  -8.677  -27.456 1.00 39.23  ? 249 TYR C CE1   1 
ATOM   4487  C CE2   . TYR C 1 248 ? 24.794  -11.028 -27.869 1.00 37.21  ? 249 TYR C CE2   1 
ATOM   4488  C CZ    . TYR C 1 248 ? 25.549  -9.927  -27.506 1.00 41.88  ? 249 TYR C CZ    1 
ATOM   4489  O OH    . TYR C 1 248 ? 26.871  -10.073 -27.197 1.00 45.12  ? 249 TYR C OH    1 
ATOM   4490  N N     . ALA C 1 249 ? 18.148  -9.830  -27.937 1.00 34.93  ? 250 ALA C N     1 
ATOM   4491  C CA    . ALA C 1 249 ? 16.794  -9.516  -28.360 1.00 35.68  ? 250 ALA C CA    1 
ATOM   4492  C C     . ALA C 1 249 ? 16.122  -8.615  -27.327 1.00 35.94  ? 250 ALA C C     1 
ATOM   4493  O O     . ALA C 1 249 ? 15.520  -7.602  -27.677 1.00 38.46  ? 250 ALA C O     1 
ATOM   4494  C CB    . ALA C 1 249 ? 16.010  -10.793 -28.574 1.00 34.80  ? 250 ALA C CB    1 
ATOM   4495  N N     . ILE C 1 250 ? 16.238  -8.997  -26.050 1.00 38.27  ? 251 ILE C N     1 
ATOM   4496  C CA    . ILE C 1 250 ? 15.564  -8.293  -24.972 1.00 39.15  ? 251 ILE C CA    1 
ATOM   4497  C C     . ILE C 1 250 ? 16.382  -7.061  -24.590 1.00 42.60  ? 251 ILE C C     1 
ATOM   4498  O O     . ILE C 1 250 ? 15.822  -5.999  -24.329 1.00 46.11  ? 251 ILE C O     1 
ATOM   4499  C CB    . ILE C 1 250 ? 15.335  -9.228  -23.769 1.00 39.21  ? 251 ILE C CB    1 
ATOM   4500  C CG1   . ILE C 1 250 ? 14.650  -10.528 -24.193 1.00 39.13  ? 251 ILE C CG1   1 
ATOM   4501  C CG2   . ILE C 1 250 ? 14.560  -8.516  -22.660 1.00 38.28  ? 251 ILE C CG2   1 
ATOM   4502  C CD1   . ILE C 1 250 ? 13.321  -10.328 -24.899 1.00 39.57  ? 251 ILE C CD1   1 
ATOM   4503  N N     . LEU C 1 251 ? 17.709  -7.217  -24.563 1.00 41.10  ? 252 LEU C N     1 
ATOM   4504  C CA    . LEU C 1 251 ? 18.603  -6.122  -24.223 1.00 44.77  ? 252 LEU C CA    1 
ATOM   4505  C C     . LEU C 1 251 ? 18.311  -4.934  -25.136 1.00 49.24  ? 252 LEU C C     1 
ATOM   4506  O O     . LEU C 1 251 ? 18.322  -3.787  -24.694 1.00 49.45  ? 252 LEU C O     1 
ATOM   4507  C CB    . LEU C 1 251 ? 20.059  -6.570  -24.339 1.00 46.39  ? 252 LEU C CB    1 
ATOM   4508  C CG    . LEU C 1 251 ? 20.525  -7.617  -23.322 1.00 45.87  ? 252 LEU C CG    1 
ATOM   4509  C CD1   . LEU C 1 251 ? 21.991  -7.956  -23.529 1.00 44.67  ? 252 LEU C CD1   1 
ATOM   4510  C CD2   . LEU C 1 251 ? 20.281  -7.142  -21.899 1.00 48.10  ? 252 LEU C CD2   1 
ATOM   4511  N N     . ALA C 1 252 ? 18.051  -5.229  -26.414 1.00 53.83  ? 253 ALA C N     1 
ATOM   4512  C CA    . ALA C 1 252 ? 17.792  -4.200  -27.407 1.00 53.57  ? 253 ALA C CA    1 
ATOM   4513  C C     . ALA C 1 252 ? 16.506  -3.457  -27.060 1.00 53.81  ? 253 ALA C C     1 
ATOM   4514  O O     . ALA C 1 252 ? 16.438  -2.236  -27.182 1.00 56.32  ? 253 ALA C O     1 
ATOM   4515  C CB    . ALA C 1 252 ? 17.719  -4.820  -28.785 1.00 53.13  ? 253 ALA C CB    1 
ATOM   4516  N N     . LYS C 1 253 ? 15.489  -4.211  -26.629 1.00 52.78  ? 254 LYS C N     1 
ATOM   4517  C CA    . LYS C 1 253 ? 14.207  -3.634  -26.262 1.00 51.19  ? 254 LYS C CA    1 
ATOM   4518  C C     . LYS C 1 253 ? 14.382  -2.772  -25.013 1.00 52.18  ? 254 LYS C C     1 
ATOM   4519  O O     . LYS C 1 253 ? 13.764  -1.717  -24.894 1.00 54.94  ? 254 LYS C O     1 
ATOM   4520  C CB    . LYS C 1 253 ? 13.160  -4.734  -26.050 1.00 50.15  ? 254 LYS C CB    1 
ATOM   4521  C CG    . LYS C 1 253 ? 12.818  -5.538  -27.298 1.00 52.98  ? 254 LYS C CG    1 
ATOM   4522  C CD    . LYS C 1 253 ? 11.721  -6.575  -27.092 1.00 53.64  ? 254 LYS C CD    1 
ATOM   4523  C CE    . LYS C 1 253 ? 11.459  -7.389  -28.321 1.00 54.34  ? 254 LYS C CE    1 
ATOM   4524  N NZ    . LYS C 1 253 ? 11.039  -6.554  -29.450 1.00 53.97  ? 254 LYS C NZ    1 
ATOM   4525  N N     . LEU C 1 254 ? 15.235  -3.235  -24.092 1.00 51.93  ? 255 LEU C N     1 
ATOM   4526  C CA    . LEU C 1 254 ? 15.546  -2.486  -22.886 1.00 52.56  ? 255 LEU C CA    1 
ATOM   4527  C C     . LEU C 1 254 ? 16.450  -1.310  -23.249 1.00 52.63  ? 255 LEU C C     1 
ATOM   4528  O O     . LEU C 1 254 ? 16.687  -0.426  -22.429 1.00 53.95  ? 255 LEU C O     1 
ATOM   4529  C CB    . LEU C 1 254 ? 16.202  -3.395  -21.847 1.00 53.77  ? 255 LEU C CB    1 
ATOM   4530  C CG    . LEU C 1 254 ? 15.330  -4.529  -21.298 1.00 50.64  ? 255 LEU C CG    1 
ATOM   4531  C CD1   . LEU C 1 254 ? 16.061  -5.294  -20.208 1.00 52.59  ? 255 LEU C CD1   1 
ATOM   4532  C CD2   . LEU C 1 254 ? 14.006  -3.998  -20.780 1.00 51.38  ? 255 LEU C CD2   1 
ATOM   4533  N N     . GLY C 1 255 ? 16.953  -1.321  -24.488 1.00 53.78  ? 256 GLY C N     1 
ATOM   4534  C CA    . GLY C 1 255 ? 17.790  -0.246  -24.994 1.00 46.53  ? 256 GLY C CA    1 
ATOM   4535  C C     . GLY C 1 255 ? 19.132  -0.196  -24.271 1.00 43.81  ? 256 GLY C C     1 
ATOM   4536  O O     . GLY C 1 255 ? 19.701  0.877   -24.082 1.00 46.13  ? 256 GLY C O     1 
ATOM   4537  N N     . ILE C 1 256 ? 19.629  -1.372  -23.873 1.00 40.57  ? 257 ILE C N     1 
ATOM   4538  C CA    . ILE C 1 256 ? 20.900  -1.475  -23.176 1.00 40.58  ? 257 ILE C CA    1 
ATOM   4539  C C     . ILE C 1 256 ? 21.755  -2.541  -23.856 1.00 43.71  ? 257 ILE C C     1 
ATOM   4540  O O     . ILE C 1 256 ? 21.290  -3.238  -24.756 1.00 39.61  ? 257 ILE C O     1 
ATOM   4541  C CB    . ILE C 1 256 ? 20.686  -1.793  -21.685 1.00 37.78  ? 257 ILE C CB    1 
ATOM   4542  C CG1   . ILE C 1 256 ? 20.116  -3.198  -21.488 1.00 33.93  ? 257 ILE C CG1   1 
ATOM   4543  C CG2   . ILE C 1 256 ? 19.817  -0.728  -21.016 1.00 39.28  ? 257 ILE C CG2   1 
ATOM   4544  C CD1   . ILE C 1 256 ? 19.959  -3.605  -20.034 1.00 32.08  ? 257 ILE C CD1   1 
ATOM   4545  N N     . GLY C 1 257 ? 23.007  -2.657  -23.401 1.00 48.71  ? 258 GLY C N     1 
ATOM   4546  C CA    . GLY C 1 257 ? 23.928  -3.661  -23.905 1.00 51.38  ? 258 GLY C CA    1 
ATOM   4547  C C     . GLY C 1 257 ? 24.605  -4.409  -22.759 1.00 56.61  ? 258 GLY C C     1 
ATOM   4548  O O     . GLY C 1 257 ? 24.449  -4.042  -21.596 1.00 59.63  ? 258 GLY C O     1 
ATOM   4549  N N     . PRO C 1 258 ? 25.372  -5.482  -23.054 1.00 57.21  ? 259 PRO C N     1 
ATOM   4550  C CA    . PRO C 1 258 ? 26.040  -6.263  -22.010 1.00 60.19  ? 259 PRO C CA    1 
ATOM   4551  C C     . PRO C 1 258 ? 26.880  -5.410  -21.063 1.00 62.66  ? 259 PRO C C     1 
ATOM   4552  O O     . PRO C 1 258 ? 26.929  -5.673  -19.863 1.00 63.23  ? 259 PRO C O     1 
ATOM   4553  C CB    . PRO C 1 258 ? 26.906  -7.253  -22.817 1.00 61.77  ? 259 PRO C CB    1 
ATOM   4554  C CG    . PRO C 1 258 ? 26.184  -7.388  -24.141 1.00 61.76  ? 259 PRO C CG    1 
ATOM   4555  C CD    . PRO C 1 258 ? 25.610  -6.008  -24.406 1.00 61.10  ? 259 PRO C CD    1 
ATOM   4556  N N     . GLU C 1 259 ? 27.541  -4.389  -21.619 1.00 63.04  ? 260 GLU C N     1 
ATOM   4557  C CA    . GLU C 1 259 ? 28.467  -3.564  -20.860 1.00 65.63  ? 260 GLU C CA    1 
ATOM   4558  C C     . GLU C 1 259 ? 27.693  -2.619  -19.944 1.00 61.87  ? 260 GLU C C     1 
ATOM   4559  O O     . GLU C 1 259 ? 28.277  -1.986  -19.067 1.00 58.49  ? 260 GLU C O     1 
ATOM   4560  C CB    . GLU C 1 259 ? 29.389  -2.778  -21.794 1.00 63.92  ? 260 GLU C CB    1 
ATOM   4561  C CG    . GLU C 1 259 ? 28.644  -1.862  -22.762 1.00 67.71  ? 260 GLU C CG    1 
ATOM   4562  C CD    . GLU C 1 259 ? 27.858  -2.587  -23.839 1.00 70.59  ? 260 GLU C CD    1 
ATOM   4563  O OE1   . GLU C 1 259 ? 27.873  -3.836  -23.846 1.00 73.35  ? 260 GLU C OE1   1 
ATOM   4564  O OE2   . GLU C 1 259 ? 27.234  -1.901  -24.675 1.00 68.78  ? 260 GLU C OE2   1 
ATOM   4565  N N     . ASP C 1 260 ? 26.376  -2.532  -20.157 1.00 57.83  ? 261 ASP C N     1 
ATOM   4566  C CA    . ASP C 1 260 ? 25.529  -1.653  -19.369 1.00 53.06  ? 261 ASP C CA    1 
ATOM   4567  C C     . ASP C 1 260 ? 25.064  -2.387  -18.114 1.00 55.30  ? 261 ASP C C     1 
ATOM   4568  O O     . ASP C 1 260 ? 24.595  -1.763  -17.165 1.00 52.87  ? 261 ASP C O     1 
ATOM   4569  C CB    . ASP C 1 260 ? 24.364  -1.124  -20.190 1.00 53.17  ? 261 ASP C CB    1 
ATOM   4570  C CG    . ASP C 1 260 ? 24.748  -0.255  -21.380 1.00 51.09  ? 261 ASP C CG    1 
ATOM   4571  O OD1   . ASP C 1 260 ? 25.472  0.740   -21.168 1.00 49.83  ? 261 ASP C OD1   1 
ATOM   4572  O OD2   . ASP C 1 260 ? 24.316  -0.578  -22.506 1.00 50.65  ? 261 ASP C OD2   1 
ATOM   4573  N N     . LEU C 1 261 ? 25.201  -3.717  -18.123 1.00 55.41  ? 262 LEU C N     1 
ATOM   4574  C CA    . LEU C 1 261 ? 24.815  -4.535  -16.985 1.00 53.72  ? 262 LEU C CA    1 
ATOM   4575  C C     . LEU C 1 261 ? 25.632  -4.111  -15.768 1.00 55.33  ? 262 LEU C C     1 
ATOM   4576  O O     . LEU C 1 261 ? 26.850  -3.965  -15.851 1.00 56.50  ? 262 LEU C O     1 
ATOM   4577  C CB    . LEU C 1 261 ? 25.013  -6.017  -17.303 1.00 56.71  ? 262 LEU C CB    1 
ATOM   4578  C CG    . LEU C 1 261 ? 24.212  -6.565  -18.489 1.00 58.38  ? 262 LEU C CG    1 
ATOM   4579  C CD1   . LEU C 1 261 ? 24.390  -8.069  -18.607 1.00 57.43  ? 262 LEU C CD1   1 
ATOM   4580  C CD2   . LEU C 1 261 ? 22.740  -6.206  -18.374 1.00 57.21  ? 262 LEU C CD2   1 
ATOM   4581  N N     . GLY C 1 262 ? 24.941  -3.912  -14.641 1.00 52.90  ? 263 GLY C N     1 
ATOM   4582  C CA    . GLY C 1 262 ? 25.585  -3.515  -13.400 1.00 52.40  ? 263 GLY C CA    1 
ATOM   4583  C C     . GLY C 1 262 ? 26.410  -4.648  -12.821 1.00 52.39  ? 263 GLY C C     1 
ATOM   4584  O O     . GLY C 1 262 ? 27.345  -4.336  -12.053 1.00 54.05  ? 263 GLY C O     1 
ATOM   4585  O OXT   . GLY C 1 262 ? 26.093  -5.809  -13.153 1.00 52.21  ? 263 GLY C OXT   1 
ATOM   4586  N N     . LEU D 3 2   ? 22.940  -45.059 21.629  1.00 41.58  ? 4   LEU D N     1 
ATOM   4587  C CA    . LEU D 3 2   ? 23.125  -44.485 20.270  1.00 38.71  ? 4   LEU D CA    1 
ATOM   4588  C C     . LEU D 3 2   ? 22.010  -43.485 19.982  1.00 35.68  ? 4   LEU D C     1 
ATOM   4589  O O     . LEU D 3 2   ? 22.274  -42.321 19.693  1.00 40.70  ? 4   LEU D O     1 
ATOM   4590  C CB    . LEU D 3 2   ? 23.153  -45.599 19.224  1.00 37.10  ? 4   LEU D CB    1 
ATOM   4591  C CG    . LEU D 3 2   ? 24.437  -46.432 19.162  1.00 35.81  ? 4   LEU D CG    1 
ATOM   4592  C CD1   . LEU D 3 2   ? 24.399  -47.385 17.979  1.00 36.94  ? 4   LEU D CD1   1 
ATOM   4593  C CD2   . LEU D 3 2   ? 25.660  -45.535 19.093  1.00 35.35  ? 4   LEU D CD2   1 
ATOM   4594  N N     . SER D 3 3   ? 20.764  -43.962 20.060  1.00 34.21  ? 5   SER D N     1 
ATOM   4595  C CA    . SER D 3 3   ? 19.606  -43.152 19.724  1.00 33.62  ? 5   SER D CA    1 
ATOM   4596  C C     . SER D 3 3   ? 19.581  -41.889 20.581  1.00 32.26  ? 5   SER D C     1 
ATOM   4597  O O     . SER D 3 3   ? 19.247  -40.812 20.094  1.00 32.45  ? 5   SER D O     1 
ATOM   4598  C CB    . SER D 3 3   ? 18.331  -43.940 19.878  1.00 31.56  ? 5   SER D CB    1 
ATOM   4599  O OG    . SER D 3 3   ? 17.205  -43.166 19.489  1.00 35.60  ? 5   SER D OG    1 
ATOM   4600  N N     . ASP D 3 4   ? 19.940  -42.040 21.860  1.00 32.97  ? 6   ASP D N     1 
ATOM   4601  C CA    . ASP D 3 4   ? 19.908  -40.936 22.804  1.00 32.95  ? 6   ASP D CA    1 
ATOM   4602  C C     . ASP D 3 4   ? 20.968  -39.907 22.422  1.00 29.36  ? 6   ASP D C     1 
ATOM   4603  O O     . ASP D 3 4   ? 20.748  -38.706 22.557  1.00 27.46  ? 6   ASP D O     1 
ATOM   4604  C CB    . ASP D 3 4   ? 20.094  -41.423 24.233  1.00 38.44  ? 6   ASP D CB    1 
ATOM   4605  C CG    . ASP D 3 4   ? 18.998  -42.337 24.763  1.00 44.86  ? 6   ASP D CG    1 
ATOM   4606  O OD1   . ASP D 3 4   ? 18.047  -42.614 24.003  1.00 52.81  ? 6   ASP D OD1   1 
ATOM   4607  O OD2   . ASP D 3 4   ? 19.105  -42.763 25.932  1.00 51.62  ? 6   ASP D OD2   1 
ATOM   4608  N N     . PHE D 3 5   ? 22.117  -40.392 21.944  1.00 29.72  ? 7   PHE D N     1 
ATOM   4609  C CA    . PHE D 3 5   ? 23.241  -39.525 21.634  1.00 30.32  ? 7   PHE D CA    1 
ATOM   4610  C C     . PHE D 3 5   ? 22.968  -38.770 20.335  1.00 26.66  ? 7   PHE D C     1 
ATOM   4611  O O     . PHE D 3 5   ? 23.244  -37.576 20.242  1.00 25.84  ? 7   PHE D O     1 
ATOM   4612  C CB    . PHE D 3 5   ? 24.540  -40.333 21.556  1.00 32.60  ? 7   PHE D CB    1 
ATOM   4613  C CG    . PHE D 3 5   ? 25.713  -39.556 20.973  1.00 33.39  ? 7   PHE D CG    1 
ATOM   4614  C CD1   . PHE D 3 5   ? 26.311  -38.524 21.688  1.00 37.19  ? 7   PHE D CD1   1 
ATOM   4615  C CD2   . PHE D 3 5   ? 26.222  -39.867 19.717  1.00 32.29  ? 7   PHE D CD2   1 
ATOM   4616  C CE1   . PHE D 3 5   ? 27.375  -37.816 21.154  1.00 32.77  ? 7   PHE D CE1   1 
ATOM   4617  C CE2   . PHE D 3 5   ? 27.290  -39.158 19.191  1.00 35.42  ? 7   PHE D CE2   1 
ATOM   4618  C CZ    . PHE D 3 5   ? 27.863  -38.135 19.909  1.00 32.76  ? 7   PHE D CZ    1 
ATOM   4619  N N     . PHE D 3 6   ? 22.424  -39.474 19.336  1.00 24.24  ? 8   PHE D N     1 
ATOM   4620  C CA    . PHE D 3 6   ? 22.210  -38.891 18.021  1.00 24.55  ? 8   PHE D CA    1 
ATOM   4621  C C     . PHE D 3 6   ? 21.153  -37.793 18.115  1.00 24.77  ? 8   PHE D C     1 
ATOM   4622  O O     . PHE D 3 6   ? 21.267  -36.762 17.456  1.00 22.94  ? 8   PHE D O     1 
ATOM   4623  C CB    . PHE D 3 6   ? 21.812  -39.956 16.994  1.00 22.58  ? 8   PHE D CB    1 
ATOM   4624  C CG    . PHE D 3 6   ? 22.920  -40.938 16.639  1.00 25.93  ? 8   PHE D CG    1 
ATOM   4625  C CD1   . PHE D 3 6   ? 24.256  -40.625 16.870  1.00 27.20  ? 8   PHE D CD1   1 
ATOM   4626  C CD2   . PHE D 3 6   ? 22.625  -42.163 16.050  1.00 27.54  ? 8   PHE D CD2   1 
ATOM   4627  C CE1   . PHE D 3 6   ? 25.261  -41.520 16.538  1.00 26.58  ? 8   PHE D CE1   1 
ATOM   4628  C CE2   . PHE D 3 6   ? 23.636  -43.052 15.718  1.00 29.03  ? 8   PHE D CE2   1 
ATOM   4629  C CZ    . PHE D 3 6   ? 24.950  -42.728 15.962  1.00 30.38  ? 8   PHE D CZ    1 
ATOM   4630  N N     . THR D 3 7   ? 20.126  -38.024 18.938  1.00 26.16  ? 9   THR D N     1 
ATOM   4631  C CA    . THR D 3 7   ? 19.038  -37.071 19.085  1.00 26.88  ? 9   THR D CA    1 
ATOM   4632  C C     . THR D 3 7   ? 19.582  -35.777 19.689  1.00 28.55  ? 9   THR D C     1 
ATOM   4633  O O     . THR D 3 7   ? 19.289  -34.688 19.199  1.00 32.37  ? 9   THR D O     1 
ATOM   4634  C CB    . THR D 3 7   ? 17.931  -37.680 19.943  1.00 28.64  ? 9   THR D CB    1 
ATOM   4635  O OG1   . THR D 3 7   ? 17.554  -38.881 19.278  1.00 27.56  ? 9   THR D OG1   1 
ATOM   4636  C CG2   . THR D 3 7   ? 16.729  -36.761 20.078  1.00 29.07  ? 9   THR D CG2   1 
ATOM   4637  N N     . GLN D 3 8   ? 20.378  -35.910 20.755  1.00 23.83  ? 10  GLN D N     1 
ATOM   4638  C CA    . GLN D 3 8   ? 20.989  -34.762 21.406  1.00 23.62  ? 10  GLN D CA    1 
ATOM   4639  C C     . GLN D 3 8   ? 21.877  -34.025 20.407  1.00 23.32  ? 10  GLN D C     1 
ATOM   4640  O O     . GLN D 3 8   ? 21.708  -32.830 20.179  1.00 27.00  ? 10  GLN D O     1 
ATOM   4641  C CB    . GLN D 3 8   ? 21.820  -35.193 22.615  1.00 23.58  ? 10  GLN D CB    1 
ATOM   4642  C CG    . GLN D 3 8   ? 21.008  -35.821 23.742  1.00 29.61  ? 10  GLN D CG    1 
ATOM   4643  C CD    . GLN D 3 8   ? 21.856  -36.217 24.931  1.00 35.82  ? 10  GLN D CD    1 
ATOM   4644  O OE1   . GLN D 3 8   ? 23.077  -36.024 24.946  1.00 40.61  ? 10  GLN D OE1   1 
ATOM   4645  N NE2   . GLN D 3 8   ? 21.213  -36.775 25.946  1.00 40.15  ? 10  GLN D NE2   1 
ATOM   4646  N N     . LEU D 3 9   ? 22.826  -34.763 19.822  1.00 28.94  ? 11  LEU D N     1 
ATOM   4647  C CA    . LEU D 3 9   ? 23.812  -34.198 18.915  1.00 30.92  ? 11  LEU D CA    1 
ATOM   4648  C C     . LEU D 3 9   ? 23.117  -33.404 17.813  1.00 30.72  ? 11  LEU D C     1 
ATOM   4649  O O     . LEU D 3 9   ? 23.585  -32.336 17.423  1.00 32.15  ? 11  LEU D O     1 
ATOM   4650  C CB    . LEU D 3 9   ? 24.660  -35.331 18.338  1.00 32.02  ? 11  LEU D CB    1 
ATOM   4651  C CG    . LEU D 3 9   ? 25.691  -34.926 17.281  1.00 33.54  ? 11  LEU D CG    1 
ATOM   4652  C CD1   . LEU D 3 9   ? 26.690  -33.930 17.844  1.00 33.55  ? 11  LEU D CD1   1 
ATOM   4653  C CD2   . LEU D 3 9   ? 26.405  -36.151 16.731  1.00 34.80  ? 11  LEU D CD2   1 
ATOM   4654  N N     . GLY D 3 10  ? 22.002  -33.943 17.312  1.00 30.24  ? 12  GLY D N     1 
ATOM   4655  C CA    . GLY D 3 10  ? 21.306  -33.353 16.181  1.00 28.85  ? 12  GLY D CA    1 
ATOM   4656  C C     . GLY D 3 10  ? 20.631  -32.034 16.551  1.00 27.16  ? 12  GLY D C     1 
ATOM   4657  O O     . GLY D 3 10  ? 20.361  -31.210 15.682  1.00 25.80  ? 12  GLY D O     1 
ATOM   4658  N N     . GLN D 3 11  ? 20.367  -31.844 17.848  1.00 28.10  ? 13  GLN D N     1 
ATOM   4659  C CA    . GLN D 3 11  ? 19.584  -30.709 18.312  1.00 33.47  ? 13  GLN D CA    1 
ATOM   4660  C C     . GLN D 3 11  ? 20.492  -29.658 18.949  1.00 34.06  ? 13  GLN D C     1 
ATOM   4661  O O     . GLN D 3 11  ? 20.214  -28.465 18.861  1.00 34.33  ? 13  GLN D O     1 
ATOM   4662  C CB    . GLN D 3 11  ? 18.524  -31.164 19.316  1.00 37.19  ? 13  GLN D CB    1 
ATOM   4663  C CG    . GLN D 3 11  ? 17.436  -32.049 18.716  1.00 39.06  ? 13  GLN D CG    1 
ATOM   4664  C CD    . GLN D 3 11  ? 16.410  -32.499 19.733  1.00 40.78  ? 13  GLN D CD    1 
ATOM   4665  O OE1   . GLN D 3 11  ? 15.221  -32.175 19.637  1.00 47.02  ? 13  GLN D OE1   1 
ATOM   4666  N NE2   . GLN D 3 11  ? 16.864  -33.251 20.726  1.00 41.50  ? 13  GLN D NE2   1 
ATOM   4667  N N     . ASP D 3 12  ? 21.572  -30.116 19.592  1.00 34.29  ? 14  ASP D N     1 
ATOM   4668  C CA    . ASP D 3 12  ? 22.420  -29.246 20.393  1.00 33.67  ? 14  ASP D CA    1 
ATOM   4669  C C     . ASP D 3 12  ? 23.615  -28.786 19.561  1.00 34.65  ? 14  ASP D C     1 
ATOM   4670  O O     . ASP D 3 12  ? 24.490  -29.582 19.229  1.00 36.02  ? 14  ASP D O     1 
ATOM   4671  C CB    . ASP D 3 12  ? 22.843  -29.938 21.680  1.00 35.73  ? 14  ASP D CB    1 
ATOM   4672  C CG    . ASP D 3 12  ? 23.723  -29.119 22.613  1.00 41.63  ? 14  ASP D CG    1 
ATOM   4673  O OD1   . ASP D 3 12  ? 24.076  -27.979 22.241  1.00 39.56  ? 14  ASP D OD1   1 
ATOM   4674  O OD2   . ASP D 3 12  ? 24.046  -29.627 23.708  1.00 47.55  ? 14  ASP D OD2   1 
ATOM   4675  N N     . ALA D 3 13  ? 23.649  -27.484 19.255  1.00 31.24  ? 15  ALA D N     1 
ATOM   4676  C CA    . ALA D 3 13  ? 24.699  -26.910 18.428  1.00 33.79  ? 15  ALA D CA    1 
ATOM   4677  C C     . ALA D 3 13  ? 26.017  -26.893 19.196  1.00 36.28  ? 15  ALA D C     1 
ATOM   4678  O O     . ALA D 3 13  ? 27.088  -27.000 18.601  1.00 31.13  ? 15  ALA D O     1 
ATOM   4679  C CB    . ALA D 3 13  ? 24.304  -25.521 17.979  1.00 33.02  ? 15  ALA D CB    1 
ATOM   4680  N N     . GLN D 3 14  ? 25.922  -26.749 20.521  1.00 37.98  ? 16  GLN D N     1 
ATOM   4681  C CA    . GLN D 3 14  ? 27.093  -26.753 21.382  1.00 42.77  ? 16  GLN D CA    1 
ATOM   4682  C C     . GLN D 3 14  ? 27.764  -28.121 21.302  1.00 38.33  ? 16  GLN D C     1 
ATOM   4683  O O     . GLN D 3 14  ? 28.973  -28.216 21.104  1.00 35.23  ? 16  GLN D O     1 
ATOM   4684  C CB    . GLN D 3 14  ? 26.699  -26.414 22.820  1.00 46.85  ? 16  GLN D CB    1 
ATOM   4685  C CG    . GLN D 3 14  ? 27.864  -26.432 23.803  1.00 54.29  ? 16  GLN D CG    1 
ATOM   4686  C CD    . GLN D 3 14  ? 28.973  -25.473 23.427  1.00 61.36  ? 16  GLN D CD    1 
ATOM   4687  O OE1   . GLN D 3 14  ? 28.765  -24.260 23.309  1.00 66.34  ? 16  GLN D OE1   1 
ATOM   4688  N NE2   . GLN D 3 14  ? 30.167  -26.011 23.231  1.00 61.59  ? 16  GLN D NE2   1 
ATOM   4689  N N     . LEU D 3 15  ? 26.955  -29.175 21.450  1.00 36.83  ? 17  LEU D N     1 
ATOM   4690  C CA    . LEU D 3 15  ? 27.449  -30.540 21.406  1.00 32.70  ? 17  LEU D CA    1 
ATOM   4691  C C     . LEU D 3 15  ? 27.939  -30.856 19.995  1.00 30.52  ? 17  LEU D C     1 
ATOM   4692  O O     . LEU D 3 15  ? 28.917  -31.579 19.821  1.00 30.39  ? 17  LEU D O     1 
ATOM   4693  C CB    . LEU D 3 15  ? 26.344  -31.500 21.844  1.00 36.24  ? 17  LEU D CB    1 
ATOM   4694  C CG    . LEU D 3 15  ? 26.740  -32.976 21.942  1.00 37.91  ? 17  LEU D CG    1 
ATOM   4695  C CD1   . LEU D 3 15  ? 27.771  -33.186 23.039  1.00 39.77  ? 17  LEU D CD1   1 
ATOM   4696  C CD2   . LEU D 3 15  ? 25.522  -33.855 22.173  1.00 35.54  ? 17  LEU D CD2   1 
ATOM   4697  N N     . MET D 3 16  ? 27.248  -30.304 18.993  1.00 29.33  ? 18  MET D N     1 
ATOM   4698  C CA    . MET D 3 16  ? 27.607  -30.525 17.602  1.00 31.64  ? 18  MET D CA    1 
ATOM   4699  C C     . MET D 3 16  ? 29.025  -30.017 17.356  1.00 33.23  ? 18  MET D C     1 
ATOM   4700  O O     . MET D 3 16  ? 29.875  -30.753 16.861  1.00 29.90  ? 18  MET D O     1 
ATOM   4701  C CB    . MET D 3 16  ? 26.637  -29.808 16.655  1.00 32.41  ? 18  MET D CB    1 
ATOM   4702  C CG    . MET D 3 16  ? 27.011  -29.931 15.190  1.00 34.87  ? 18  MET D CG    1 
ATOM   4703  S SD    . MET D 3 16  ? 26.906  -31.623 14.573  1.00 41.99  ? 18  MET D SD    1 
ATOM   4704  C CE    . MET D 3 16  ? 25.124  -31.820 14.436  1.00 34.79  ? 18  MET D CE    1 
ATOM   4705  N N     . GLU D 3 17  ? 29.267  -28.751 17.712  1.00 34.15  ? 19  GLU D N     1 
ATOM   4706  C CA    . GLU D 3 17  ? 30.558  -28.124 17.488  1.00 35.62  ? 19  GLU D CA    1 
ATOM   4707  C C     . GLU D 3 17  ? 31.638  -28.878 18.261  1.00 35.04  ? 19  GLU D C     1 
ATOM   4708  O O     . GLU D 3 17  ? 32.773  -28.980 17.802  1.00 35.22  ? 19  GLU D O     1 
ATOM   4709  C CB    . GLU D 3 17  ? 30.512  -26.645 17.873  1.00 35.12  ? 19  GLU D CB    1 
ATOM   4710  C CG    . GLU D 3 17  ? 29.688  -25.799 16.906  1.00 37.67  ? 19  GLU D CG    1 
ATOM   4711  C CD    . GLU D 3 17  ? 30.184  -25.845 15.471  1.00 40.22  ? 19  GLU D CD    1 
ATOM   4712  O OE1   . GLU D 3 17  ? 31.343  -25.445 15.234  1.00 45.54  ? 19  GLU D OE1   1 
ATOM   4713  O OE2   . GLU D 3 17  ? 29.413  -26.283 14.591  1.00 46.16  ? 19  GLU D OE2   1 
ATOM   4714  N N     . ASP D 3 18  ? 31.272  -29.402 19.436  1.00 35.67  ? 20  ASP D N     1 
ATOM   4715  C CA    . ASP D 3 18  ? 32.186  -30.200 20.236  1.00 37.37  ? 20  ASP D CA    1 
ATOM   4716  C C     . ASP D 3 18  ? 32.535  -31.475 19.475  1.00 34.96  ? 20  ASP D C     1 
ATOM   4717  O O     . ASP D 3 18  ? 33.694  -31.884 19.437  1.00 31.29  ? 20  ASP D O     1 
ATOM   4718  C CB    . ASP D 3 18  ? 31.601  -30.520 21.603  1.00 45.18  ? 20  ASP D CB    1 
ATOM   4719  C CG    . ASP D 3 18  ? 31.440  -29.334 22.543  1.00 53.09  ? 20  ASP D CG    1 
ATOM   4720  O OD1   . ASP D 3 18  ? 31.826  -28.214 22.146  1.00 52.61  ? 20  ASP D OD1   1 
ATOM   4721  O OD2   . ASP D 3 18  ? 30.930  -29.540 23.664  1.00 65.14  ? 20  ASP D OD2   1 
ATOM   4722  N N     . TYR D 3 19  ? 31.515  -32.090 18.868  1.00 35.88  ? 21  TYR D N     1 
ATOM   4723  C CA    . TYR D 3 19  ? 31.677  -33.356 18.172  1.00 34.04  ? 21  TYR D CA    1 
ATOM   4724  C C     . TYR D 3 19  ? 32.648  -33.181 17.008  1.00 36.10  ? 21  TYR D C     1 
ATOM   4725  O O     . TYR D 3 19  ? 33.581  -33.964 16.854  1.00 34.26  ? 21  TYR D O     1 
ATOM   4726  C CB    . TYR D 3 19  ? 30.317  -33.878 17.699  1.00 32.23  ? 21  TYR D CB    1 
ATOM   4727  C CG    . TYR D 3 19  ? 30.398  -35.092 16.783  1.00 31.20  ? 21  TYR D CG    1 
ATOM   4728  C CD1   . TYR D 3 19  ? 30.550  -36.373 17.299  1.00 28.37  ? 21  TYR D CD1   1 
ATOM   4729  C CD2   . TYR D 3 19  ? 30.323  -34.955 15.402  1.00 30.60  ? 21  TYR D CD2   1 
ATOM   4730  C CE1   . TYR D 3 19  ? 30.629  -37.480 16.469  1.00 29.23  ? 21  TYR D CE1   1 
ATOM   4731  C CE2   . TYR D 3 19  ? 30.397  -36.053 14.562  1.00 29.52  ? 21  TYR D CE2   1 
ATOM   4732  C CZ    . TYR D 3 19  ? 30.550  -37.320 15.097  1.00 28.81  ? 21  TYR D CZ    1 
ATOM   4733  O OH    . TYR D 3 19  ? 30.622  -38.408 14.275  1.00 30.02  ? 21  TYR D OH    1 
ATOM   4734  N N     . LYS D 3 20  ? 32.415  -32.149 16.190  1.00 39.07  ? 22  LYS D N     1 
ATOM   4735  C CA    . LYS D 3 20  ? 33.217  -31.929 14.997  1.00 41.83  ? 22  LYS D CA    1 
ATOM   4736  C C     . LYS D 3 20  ? 34.652  -31.593 15.398  1.00 42.41  ? 22  LYS D C     1 
ATOM   4737  O O     . LYS D 3 20  ? 35.577  -31.784 14.613  1.00 41.27  ? 22  LYS D O     1 
ATOM   4738  C CB    . LYS D 3 20  ? 32.620  -30.829 14.113  1.00 43.31  ? 22  LYS D CB    1 
ATOM   4739  C CG    . LYS D 3 20  ? 31.262  -31.154 13.504  1.00 43.64  ? 22  LYS D CG    1 
ATOM   4740  C CD    . LYS D 3 20  ? 30.909  -30.278 12.308  1.00 42.47  ? 22  LYS D CD    1 
ATOM   4741  C CE    . LYS D 3 20  ? 31.043  -28.819 12.604  1.00 45.09  ? 22  LYS D CE    1 
ATOM   4742  N NZ    . LYS D 3 20  ? 30.892  -28.008 11.393  1.00 46.71  ? 22  LYS D NZ    1 
ATOM   4743  N N     . GLN D 3 21  ? 34.823  -31.088 16.624  1.00 43.30  ? 23  GLN D N     1 
ATOM   4744  C CA    . GLN D 3 21  ? 36.144  -30.788 17.150  1.00 41.52  ? 23  GLN D CA    1 
ATOM   4745  C C     . GLN D 3 21  ? 36.902  -32.090 17.388  1.00 36.81  ? 23  GLN D C     1 
ATOM   4746  O O     . GLN D 3 21  ? 38.071  -32.207 17.028  1.00 31.22  ? 23  GLN D O     1 
ATOM   4747  C CB    . GLN D 3 21  ? 36.052  -29.978 18.444  1.00 41.64  ? 23  GLN D CB    1 
ATOM   4748  C CG    . GLN D 3 21  ? 35.665  -28.518 18.237  1.00 47.19  ? 23  GLN D CG    1 
ATOM   4749  C CD    . GLN D 3 21  ? 36.726  -27.720 17.512  1.00 52.51  ? 23  GLN D CD    1 
ATOM   4750  O OE1   . GLN D 3 21  ? 37.112  -28.036 16.381  1.00 59.56  ? 23  GLN D OE1   1 
ATOM   4751  N NE2   . GLN D 3 21  ? 37.213  -26.673 18.161  1.00 51.76  ? 23  GLN D NE2   1 
ATOM   4752  N N     . ASN D 3 22  ? 36.219  -33.065 17.997  1.00 35.55  ? 24  ASN D N     1 
ATOM   4753  C CA    . ASN D 3 22  ? 36.845  -34.324 18.361  1.00 36.42  ? 24  ASN D CA    1 
ATOM   4754  C C     . ASN D 3 22  ? 35.780  -35.418 18.416  1.00 33.35  ? 24  ASN D C     1 
ATOM   4755  O O     . ASN D 3 22  ? 35.307  -35.781 19.489  1.00 39.77  ? 24  ASN D O     1 
ATOM   4756  C CB    . ASN D 3 22  ? 37.617  -34.189 19.669  1.00 34.66  ? 24  ASN D CB    1 
ATOM   4757  C CG    . ASN D 3 22  ? 38.467  -35.401 19.963  1.00 36.80  ? 24  ASN D CG    1 
ATOM   4758  O OD1   . ASN D 3 22  ? 38.356  -36.422 19.274  1.00 42.78  ? 24  ASN D OD1   1 
ATOM   4759  N ND2   . ASN D 3 22  ? 39.311  -35.313 20.981  1.00 37.14  ? 24  ASN D ND2   1 
ATOM   4760  N N     . PRO D 3 23  ? 35.376  -35.975 17.252  1.00 30.33  ? 25  PRO D N     1 
ATOM   4761  C CA    . PRO D 3 23  ? 34.321  -36.990 17.202  1.00 30.20  ? 25  PRO D CA    1 
ATOM   4762  C C     . PRO D 3 23  ? 34.483  -38.126 18.212  1.00 30.75  ? 25  PRO D C     1 
ATOM   4763  O O     . PRO D 3 23  ? 33.586  -38.378 19.012  1.00 28.70  ? 25  PRO D O     1 
ATOM   4764  C CB    . PRO D 3 23  ? 34.414  -37.491 15.747  1.00 29.74  ? 25  PRO D CB    1 
ATOM   4765  C CG    . PRO D 3 23  ? 34.912  -36.286 14.977  1.00 28.70  ? 25  PRO D CG    1 
ATOM   4766  C CD    . PRO D 3 23  ? 35.897  -35.622 15.922  1.00 29.43  ? 25  PRO D CD    1 
ATOM   4767  N N     . GLU D 3 24  ? 35.632  -38.811 18.159  1.00 32.94  ? 26  GLU D N     1 
ATOM   4768  C CA    . GLU D 3 24  ? 35.860  -39.994 18.975  1.00 38.84  ? 26  GLU D CA    1 
ATOM   4769  C C     . GLU D 3 24  ? 35.783  -39.636 20.457  1.00 37.74  ? 26  GLU D C     1 
ATOM   4770  O O     . GLU D 3 24  ? 35.258  -40.408 21.256  1.00 37.30  ? 26  GLU D O     1 
ATOM   4771  C CB    . GLU D 3 24  ? 37.203  -40.652 18.653  1.00 44.97  ? 26  GLU D CB    1 
ATOM   4772  C CG    . GLU D 3 24  ? 37.156  -41.552 17.421  1.00 53.75  ? 26  GLU D CG    1 
ATOM   4773  C CD    . GLU D 3 24  ? 38.388  -42.420 17.241  1.00 60.14  ? 26  GLU D CD    1 
ATOM   4774  O OE1   . GLU D 3 24  ? 39.007  -42.356 16.159  1.00 73.46  ? 26  GLU D OE1   1 
ATOM   4775  O OE2   . GLU D 3 24  ? 38.731  -43.158 18.189  1.00 59.84  ? 26  GLU D OE2   1 
ATOM   4776  N N     . ALA D 3 25  ? 36.321  -38.467 20.815  1.00 36.26  ? 27  ALA D N     1 
ATOM   4777  C CA    . ALA D 3 25  ? 36.339  -38.029 22.201  1.00 36.06  ? 27  ALA D CA    1 
ATOM   4778  C C     . ALA D 3 25  ? 34.909  -37.875 22.712  1.00 31.89  ? 27  ALA D C     1 
ATOM   4779  O O     . ALA D 3 25  ? 34.581  -38.343 23.800  1.00 29.25  ? 27  ALA D O     1 
ATOM   4780  C CB    . ALA D 3 25  ? 37.114  -36.736 22.326  1.00 35.94  ? 27  ALA D CB    1 
ATOM   4781  N N     . VAL D 3 26  ? 34.064  -37.224 21.906  1.00 28.77  ? 28  VAL D N     1 
ATOM   4782  C CA    . VAL D 3 26  ? 32.695  -36.931 22.297  1.00 29.34  ? 28  VAL D CA    1 
ATOM   4783  C C     . VAL D 3 26  ? 31.896  -38.230 22.353  1.00 31.92  ? 28  VAL D C     1 
ATOM   4784  O O     . VAL D 3 26  ? 31.081  -38.420 23.253  1.00 32.35  ? 28  VAL D O     1 
ATOM   4785  C CB    . VAL D 3 26  ? 32.040  -35.914 21.343  1.00 30.40  ? 28  VAL D CB    1 
ATOM   4786  C CG1   . VAL D 3 26  ? 30.536  -35.811 21.572  1.00 31.07  ? 28  VAL D CG1   1 
ATOM   4787  C CG2   . VAL D 3 26  ? 32.696  -34.542 21.443  1.00 32.58  ? 28  VAL D CG2   1 
ATOM   4788  N N     . MET D 3 27  ? 32.132  -39.120 21.382  1.00 29.91  ? 29  MET D N     1 
ATOM   4789  C CA    . MET D 3 27  ? 31.388  -40.366 21.300  1.00 32.06  ? 29  MET D CA    1 
ATOM   4790  C C     . MET D 3 27  ? 31.735  -41.254 22.494  1.00 30.20  ? 29  MET D C     1 
ATOM   4791  O O     . MET D 3 27  ? 30.846  -41.820 23.125  1.00 33.79  ? 29  MET D O     1 
ATOM   4792  C CB    . MET D 3 27  ? 31.665  -41.098 19.982  1.00 28.63  ? 29  MET D CB    1 
ATOM   4793  C CG    . MET D 3 27  ? 30.844  -40.576 18.816  1.00 30.64  ? 29  MET D CG    1 
ATOM   4794  S SD    . MET D 3 27  ? 31.117  -41.486 17.283  1.00 33.32  ? 29  MET D SD    1 
ATOM   4795  C CE    . MET D 3 27  ? 32.844  -41.091 16.980  1.00 35.97  ? 29  MET D CE    1 
ATOM   4796  N N     . ARG D 3 28  ? 33.031  -41.362 22.803  1.00 32.27  ? 30  ARG D N     1 
ATOM   4797  C CA    . ARG D 3 28  ? 33.475  -42.145 23.944  1.00 35.75  ? 30  ARG D CA    1 
ATOM   4798  C C     . ARG D 3 28  ? 32.904  -41.544 25.226  1.00 33.79  ? 30  ARG D C     1 
ATOM   4799  O O     . ARG D 3 28  ? 32.591  -42.268 26.168  1.00 39.26  ? 30  ARG D O     1 
ATOM   4800  C CB    . ARG D 3 28  ? 35.005  -42.215 24.025  1.00 36.62  ? 30  ARG D CB    1 
ATOM   4801  C CG    . ARG D 3 28  ? 35.645  -43.215 23.072  1.00 42.57  ? 30  ARG D CG    1 
ATOM   4802  C CD    . ARG D 3 28  ? 37.125  -43.408 23.370  1.00 47.62  ? 30  ARG D CD    1 
ATOM   4803  N NE    . ARG D 3 28  ? 37.696  -44.560 22.662  1.00 51.73  ? 30  ARG D NE    1 
ATOM   4804  C CZ    . ARG D 3 28  ? 37.817  -44.660 21.345  1.00 59.18  ? 30  ARG D CZ    1 
ATOM   4805  N NH1   . ARG D 3 28  ? 38.314  -45.762 20.811  1.00 57.42  ? 30  ARG D NH1   1 
ATOM   4806  N NH2   . ARG D 3 28  ? 37.434  -43.665 20.565  1.00 61.25  ? 30  ARG D NH2   1 
ATOM   4807  N N     . ALA D 3 29  ? 32.770  -40.214 25.244  1.00 31.98  ? 31  ALA D N     1 
ATOM   4808  C CA    . ALA D 3 29  ? 32.298  -39.502 26.420  1.00 32.80  ? 31  ALA D CA    1 
ATOM   4809  C C     . ALA D 3 29  ? 30.831  -39.834 26.681  1.00 31.82  ? 31  ALA D C     1 
ATOM   4810  O O     . ALA D 3 29  ? 30.357  -39.710 27.808  1.00 33.68  ? 31  ALA D O     1 
ATOM   4811  C CB    . ALA D 3 29  ? 32.504  -38.014 26.239  1.00 33.39  ? 31  ALA D CB    1 
ATOM   4812  N N     . HIS D 3 30  ? 30.122  -40.257 25.630  1.00 31.33  ? 32  HIS D N     1 
ATOM   4813  C CA    . HIS D 3 30  ? 28.709  -40.579 25.741  1.00 30.94  ? 32  HIS D CA    1 
ATOM   4814  C C     . HIS D 3 30  ? 28.529  -42.095 25.795  1.00 30.72  ? 32  HIS D C     1 
ATOM   4815  O O     . HIS D 3 30  ? 27.404  -42.587 25.856  1.00 31.55  ? 32  HIS D O     1 
ATOM   4816  C CB    . HIS D 3 30  ? 27.916  -39.890 24.625  1.00 30.84  ? 32  HIS D CB    1 
ATOM   4817  C CG    . HIS D 3 30  ? 27.734  -38.427 24.859  1.00 30.12  ? 32  HIS D CG    1 
ATOM   4818  N ND1   . HIS D 3 30  ? 28.721  -37.499 24.603  1.00 28.40  ? 32  HIS D ND1   1 
ATOM   4819  C CD2   . HIS D 3 30  ? 26.702  -37.738 25.368  1.00 29.80  ? 32  HIS D CD2   1 
ATOM   4820  C CE1   . HIS D 3 30  ? 28.281  -36.291 24.926  1.00 28.79  ? 32  HIS D CE1   1 
ATOM   4821  N NE2   . HIS D 3 30  ? 27.057  -36.412 25.392  1.00 30.11  ? 32  HIS D NE2   1 
ATOM   4822  N N     . GLY D 3 31  ? 29.652  -42.822 25.769  1.00 31.16  ? 33  GLY D N     1 
ATOM   4823  C CA    . GLY D 3 31  ? 29.668  -44.237 26.104  1.00 34.05  ? 33  GLY D CA    1 
ATOM   4824  C C     . GLY D 3 31  ? 29.388  -45.132 24.898  1.00 34.63  ? 33  GLY D C     1 
ATOM   4825  O O     . GLY D 3 31  ? 28.901  -46.249 25.057  1.00 33.84  ? 33  GLY D O     1 
ATOM   4826  N N     . LEU D 3 32  ? 29.716  -44.644 23.697  1.00 37.55  ? 34  LEU D N     1 
ATOM   4827  C CA    . LEU D 3 32  ? 29.579  -45.448 22.493  1.00 38.33  ? 34  LEU D CA    1 
ATOM   4828  C C     . LEU D 3 32  ? 30.690  -46.496 22.469  1.00 38.71  ? 34  LEU D C     1 
ATOM   4829  O O     . LEU D 3 32  ? 31.833  -46.206 22.815  1.00 35.12  ? 34  LEU D O     1 
ATOM   4830  C CB    . LEU D 3 32  ? 29.606  -44.574 21.240  1.00 40.86  ? 34  LEU D CB    1 
ATOM   4831  C CG    . LEU D 3 32  ? 28.334  -43.768 20.957  1.00 42.05  ? 34  LEU D CG    1 
ATOM   4832  C CD1   . LEU D 3 32  ? 28.152  -42.646 21.964  1.00 42.25  ? 34  LEU D CD1   1 
ATOM   4833  C CD2   . LEU D 3 32  ? 28.343  -43.222 19.538  1.00 41.09  ? 34  LEU D CD2   1 
ATOM   4834  N N     . THR D 3 33  ? 30.332  -47.719 22.061  1.00 39.58  ? 35  THR D N     1 
ATOM   4835  C CA    . THR D 3 33  ? 31.278  -48.821 22.000  1.00 37.91  ? 35  THR D CA    1 
ATOM   4836  C C     . THR D 3 33  ? 32.274  -48.563 20.873  1.00 36.85  ? 35  THR D C     1 
ATOM   4837  O O     . THR D 3 33  ? 32.100  -47.640 20.082  1.00 32.23  ? 35  THR D O     1 
ATOM   4838  C CB    . THR D 3 33  ? 30.525  -50.135 21.798  1.00 36.82  ? 35  THR D CB    1 
ATOM   4839  O OG1   . THR D 3 33  ? 29.841  -49.986 20.559  1.00 36.33  ? 35  THR D OG1   1 
ATOM   4840  C CG2   . THR D 3 33  ? 29.539  -50.422 22.916  1.00 35.66  ? 35  THR D CG2   1 
ATOM   4841  N N     . ASP D 3 34  ? 33.318  -49.397 20.815  1.00 43.56  ? 36  ASP D N     1 
ATOM   4842  C CA    . ASP D 3 34  ? 34.352  -49.273 19.802  1.00 45.91  ? 36  ASP D CA    1 
ATOM   4843  C C     . ASP D 3 34  ? 33.755  -49.589 18.433  1.00 41.06  ? 36  ASP D C     1 
ATOM   4844  O O     . ASP D 3 34  ? 34.015  -48.885 17.460  1.00 36.24  ? 36  ASP D O     1 
ATOM   4845  C CB    . ASP D 3 34  ? 35.542  -50.166 20.118  1.00 50.92  ? 36  ASP D CB    1 
ATOM   4846  C CG    . ASP D 3 34  ? 36.265  -49.849 21.420  1.00 56.34  ? 36  ASP D CG    1 
ATOM   4847  O OD1   . ASP D 3 34  ? 35.864  -48.875 22.091  1.00 62.40  ? 36  ASP D OD1   1 
ATOM   4848  O OD2   . ASP D 3 34  ? 37.222  -50.581 21.751  1.00 60.29  ? 36  ASP D OD2   1 
ATOM   4849  N N     . GLU D 3 35  ? 32.950  -50.655 18.376  1.00 41.90  ? 37  GLU D N     1 
ATOM   4850  C CA    . GLU D 3 35  ? 32.321  -51.076 17.136  1.00 44.20  ? 37  GLU D CA    1 
ATOM   4851  C C     . GLU D 3 35  ? 31.392  -49.969 16.646  1.00 38.47  ? 37  GLU D C     1 
ATOM   4852  O O     . GLU D 3 35  ? 31.366  -49.655 15.459  1.00 37.16  ? 37  GLU D O     1 
ATOM   4853  C CB    . GLU D 3 35  ? 31.569  -52.394 17.332  1.00 49.59  ? 37  GLU D CB    1 
ATOM   4854  C CG    . GLU D 3 35  ? 30.412  -52.297 18.322  1.00 57.06  ? 37  GLU D CG    1 
ATOM   4855  C CD    . GLU D 3 35  ? 29.725  -53.621 18.606  1.00 67.78  ? 37  GLU D CD    1 
ATOM   4856  O OE1   . GLU D 3 35  ? 29.222  -54.246 17.649  1.00 70.05  ? 37  GLU D OE1   1 
ATOM   4857  O OE2   . GLU D 3 35  ? 29.692  -54.027 19.788  1.00 74.35  ? 37  GLU D OE2   1 
ATOM   4858  N N     . GLN D 3 36  ? 30.642  -49.375 17.581  1.00 38.29  ? 38  GLN D N     1 
ATOM   4859  C CA    . GLN D 3 36  ? 29.708  -48.309 17.257  1.00 35.74  ? 38  GLN D CA    1 
ATOM   4860  C C     . GLN D 3 36  ? 30.474  -47.122 16.679  1.00 33.16  ? 38  GLN D C     1 
ATOM   4861  O O     . GLN D 3 36  ? 30.057  -46.533 15.684  1.00 34.78  ? 38  GLN D O     1 
ATOM   4862  C CB    . GLN D 3 36  ? 28.908  -47.908 18.496  1.00 34.05  ? 38  GLN D CB    1 
ATOM   4863  C CG    . GLN D 3 36  ? 27.971  -48.997 19.007  1.00 34.12  ? 38  GLN D CG    1 
ATOM   4864  C CD    . GLN D 3 36  ? 27.279  -48.624 20.300  1.00 34.17  ? 38  GLN D CD    1 
ATOM   4865  O OE1   . GLN D 3 36  ? 27.507  -47.549 20.866  1.00 30.12  ? 38  GLN D OE1   1 
ATOM   4866  N NE2   . GLN D 3 36  ? 26.428  -49.516 20.786  1.00 32.67  ? 38  GLN D NE2   1 
ATOM   4867  N N     . ILE D 3 37  ? 31.604  -46.787 17.310  1.00 32.13  ? 39  ILE D N     1 
ATOM   4868  C CA    . ILE D 3 37  ? 32.432  -45.680 16.863  1.00 33.28  ? 39  ILE D CA    1 
ATOM   4869  C C     . ILE D 3 37  ? 32.994  -46.007 15.482  1.00 33.85  ? 39  ILE D C     1 
ATOM   4870  O O     . ILE D 3 37  ? 32.995  -45.160 14.592  1.00 39.26  ? 39  ILE D O     1 
ATOM   4871  C CB    . ILE D 3 37  ? 33.546  -45.381 17.883  1.00 32.08  ? 39  ILE D CB    1 
ATOM   4872  C CG1   . ILE D 3 37  ? 32.968  -44.929 19.225  1.00 32.34  ? 39  ILE D CG1   1 
ATOM   4873  C CG2   . ILE D 3 37  ? 34.539  -44.361 17.326  1.00 32.74  ? 39  ILE D CG2   1 
ATOM   4874  C CD1   . ILE D 3 37  ? 34.014  -44.557 20.259  1.00 31.94  ? 39  ILE D CD1   1 
ATOM   4875  N N     . ASN D 3 38  ? 33.464  -47.249 15.318  1.00 37.00  ? 40  ASN D N     1 
ATOM   4876  C CA    . ASN D 3 38  ? 34.029  -47.704 14.059  1.00 39.14  ? 40  ASN D CA    1 
ATOM   4877  C C     . ASN D 3 38  ? 32.998  -47.534 12.947  1.00 37.04  ? 40  ASN D C     1 
ATOM   4878  O O     . ASN D 3 38  ? 33.321  -47.056 11.862  1.00 34.98  ? 40  ASN D O     1 
ATOM   4879  C CB    . ASN D 3 38  ? 34.501  -49.152 14.146  1.00 46.74  ? 40  ASN D CB    1 
ATOM   4880  C CG    . ASN D 3 38  ? 34.944  -49.687 12.805  1.00 52.89  ? 40  ASN D CG    1 
ATOM   4881  O OD1   . ASN D 3 38  ? 35.909  -49.181 12.222  1.00 60.53  ? 40  ASN D OD1   1 
ATOM   4882  N ND2   . ASN D 3 38  ? 34.257  -50.701 12.301  1.00 55.82  ? 40  ASN D ND2   1 
ATOM   4883  N N     . ALA D 3 39  ? 31.759  -47.946 13.231  1.00 35.37  ? 41  ALA D N     1 
ATOM   4884  C CA    . ALA D 3 39  ? 30.679  -47.861 12.263  1.00 33.66  ? 41  ALA D CA    1 
ATOM   4885  C C     . ALA D 3 39  ? 30.495  -46.413 11.819  1.00 33.02  ? 41  ALA D C     1 
ATOM   4886  O O     . ALA D 3 39  ? 30.220  -46.147 10.651  1.00 35.03  ? 41  ALA D O     1 
ATOM   4887  C CB    . ALA D 3 39  ? 29.409  -48.425 12.860  1.00 33.27  ? 41  ALA D CB    1 
ATOM   4888  N N     . VAL D 3 40  ? 30.652  -45.484 12.769  1.00 30.74  ? 42  VAL D N     1 
ATOM   4889  C CA    . VAL D 3 40  ? 30.450  -44.069 12.504  1.00 31.34  ? 42  VAL D CA    1 
ATOM   4890  C C     . VAL D 3 40  ? 31.574  -43.559 11.604  1.00 32.26  ? 42  VAL D C     1 
ATOM   4891  O O     . VAL D 3 40  ? 31.327  -42.816 10.657  1.00 30.43  ? 42  VAL D O     1 
ATOM   4892  C CB    . VAL D 3 40  ? 30.377  -43.251 13.807  1.00 31.86  ? 42  VAL D CB    1 
ATOM   4893  C CG1   . VAL D 3 40  ? 30.492  -41.754 13.543  1.00 31.32  ? 42  VAL D CG1   1 
ATOM   4894  C CG2   . VAL D 3 40  ? 29.116  -43.564 14.604  1.00 32.09  ? 42  VAL D CG2   1 
ATOM   4895  N N     . MET D 3 41  ? 32.809  -43.961 11.916  1.00 31.24  ? 43  MET D N     1 
ATOM   4896  C CA    . MET D 3 41  ? 33.977  -43.454 11.216  1.00 36.21  ? 43  MET D CA    1 
ATOM   4897  C C     . MET D 3 41  ? 34.046  -44.057 9.813   1.00 34.34  ? 43  MET D C     1 
ATOM   4898  O O     . MET D 3 41  ? 34.533  -43.415 8.886   1.00 33.26  ? 43  MET D O     1 
ATOM   4899  C CB    . MET D 3 41  ? 35.261  -43.771 11.991  1.00 39.55  ? 43  MET D CB    1 
ATOM   4900  C CG    . MET D 3 41  ? 35.334  -43.111 13.358  1.00 40.94  ? 43  MET D CG    1 
ATOM   4901  S SD    . MET D 3 41  ? 34.984  -41.341 13.304  1.00 50.50  ? 43  MET D SD    1 
ATOM   4902  C CE    . MET D 3 41  ? 36.074  -40.825 11.971  1.00 53.41  ? 43  MET D CE    1 
ATOM   4903  N N     . THR D 3 42  ? 33.547  -45.290 9.669   1.00 32.08  ? 44  THR D N     1 
ATOM   4904  C CA    . THR D 3 42  ? 33.566  -45.980 8.390   1.00 34.79  ? 44  THR D CA    1 
ATOM   4905  C C     . THR D 3 42  ? 32.355  -45.552 7.566   1.00 34.71  ? 44  THR D C     1 
ATOM   4906  O O     . THR D 3 42  ? 32.287  -45.823 6.369   1.00 38.32  ? 44  THR D O     1 
ATOM   4907  C CB    . THR D 3 42  ? 33.585  -47.492 8.613   1.00 37.22  ? 44  THR D CB    1 
ATOM   4908  O OG1   . THR D 3 42  ? 32.404  -47.785 9.353   1.00 36.42  ? 44  THR D OG1   1 
ATOM   4909  C CG2   . THR D 3 42  ? 34.815  -47.955 9.374   1.00 37.60  ? 44  THR D CG2   1 
ATOM   4910  N N     . GLY D 3 43  ? 31.401  -44.887 8.223   1.00 36.89  ? 45  GLY D N     1 
ATOM   4911  C CA    . GLY D 3 43  ? 30.189  -44.430 7.565   1.00 35.40  ? 45  GLY D CA    1 
ATOM   4912  C C     . GLY D 3 43  ? 29.295  -45.605 7.178   1.00 37.21  ? 45  GLY D C     1 
ATOM   4913  O O     . GLY D 3 43  ? 28.702  -45.611 6.101   1.00 40.77  ? 45  GLY D O     1 
ATOM   4914  N N     . ASP D 3 44  ? 29.217  -46.599 8.070   1.00 37.96  ? 46  ASP D N     1 
ATOM   4915  C CA    . ASP D 3 44  ? 28.364  -47.758 7.864   1.00 41.92  ? 46  ASP D CA    1 
ATOM   4916  C C     . ASP D 3 44  ? 27.060  -47.553 8.629   1.00 44.25  ? 46  ASP D C     1 
ATOM   4917  O O     . ASP D 3 44  ? 26.925  -47.997 9.767   1.00 43.94  ? 46  ASP D O     1 
ATOM   4918  C CB    . ASP D 3 44  ? 29.066  -49.042 8.280   1.00 45.63  ? 46  ASP D CB    1 
ATOM   4919  C CG    . ASP D 3 44  ? 28.271  -50.320 8.053   1.00 49.35  ? 46  ASP D CG    1 
ATOM   4920  O OD1   . ASP D 3 44  ? 27.128  -50.221 7.560   1.00 50.16  ? 46  ASP D OD1   1 
ATOM   4921  O OD2   . ASP D 3 44  ? 28.803  -51.405 8.370   1.00 53.15  ? 46  ASP D OD2   1 
ATOM   4922  N N     . MET D 3 45  ? 26.104  -46.877 7.984   1.00 45.83  ? 47  MET D N     1 
ATOM   4923  C CA    . MET D 3 45  ? 24.843  -46.529 8.617   1.00 47.92  ? 47  MET D CA    1 
ATOM   4924  C C     . MET D 3 45  ? 24.066  -47.798 8.961   1.00 50.81  ? 47  MET D C     1 
ATOM   4925  O O     . MET D 3 45  ? 23.369  -47.846 9.972   1.00 55.94  ? 47  MET D O     1 
ATOM   4926  C CB    . MET D 3 45  ? 23.989  -45.646 7.699   1.00 49.30  ? 47  MET D CB    1 
ATOM   4927  C CG    . MET D 3 45  ? 24.604  -44.295 7.374   1.00 47.71  ? 47  MET D CG    1 
ATOM   4928  S SD    . MET D 3 45  ? 25.079  -43.342 8.831   1.00 48.55  ? 47  MET D SD    1 
ATOM   4929  C CE    . MET D 3 45  ? 26.709  -44.011 9.187   1.00 49.29  ? 47  MET D CE    1 
ATOM   4930  N N     . GLU D 3 46  ? 24.197  -48.823 8.112   1.00 53.93  ? 48  GLU D N     1 
ATOM   4931  C CA    . GLU D 3 46  ? 23.416  -50.041 8.252   1.00 57.24  ? 48  GLU D CA    1 
ATOM   4932  C C     . GLU D 3 46  ? 23.743  -50.717 9.582   1.00 57.44  ? 48  GLU D C     1 
ATOM   4933  O O     . GLU D 3 46  ? 22.847  -51.203 10.268  1.00 68.00  ? 48  GLU D O     1 
ATOM   4934  C CB    . GLU D 3 46  ? 23.670  -50.995 7.085   1.00 60.76  ? 48  GLU D CB    1 
ATOM   4935  C CG    . GLU D 3 46  ? 22.778  -52.234 7.114   1.00 66.95  ? 48  GLU D CG    1 
ATOM   4936  C CD    . GLU D 3 46  ? 21.292  -51.931 7.048   1.00 66.38  ? 48  GLU D CD    1 
ATOM   4937  O OE1   . GLU D 3 46  ? 20.857  -51.326 6.045   1.00 76.28  ? 48  GLU D OE1   1 
ATOM   4938  O OE2   . GLU D 3 46  ? 20.569  -52.298 7.998   1.00 66.37  ? 48  GLU D OE2   1 
ATOM   4939  N N     . LYS D 3 47  ? 25.033  -50.748 9.934   1.00 59.99  ? 49  LYS D N     1 
ATOM   4940  C CA    . LYS D 3 47  ? 25.473  -51.413 11.150  1.00 58.18  ? 49  LYS D CA    1 
ATOM   4941  C C     . LYS D 3 47  ? 24.962  -50.637 12.361  1.00 56.04  ? 49  LYS D C     1 
ATOM   4942  O O     . LYS D 3 47  ? 24.573  -51.232 13.364  1.00 57.24  ? 49  LYS D O     1 
ATOM   4943  C CB    . LYS D 3 47  ? 26.999  -51.547 11.201  1.00 58.05  ? 49  LYS D CB    1 
ATOM   4944  C CG    . LYS D 3 47  ? 27.516  -52.472 12.296  1.00 58.07  ? 49  LYS D CG    1 
ATOM   4945  C CD    . LYS D 3 47  ? 27.181  -53.943 12.071  1.00 58.88  ? 49  LYS D CD    1 
ATOM   4946  C CE    . LYS D 3 47  ? 27.593  -54.812 13.217  1.00 59.26  ? 49  LYS D CE    1 
ATOM   4947  N NZ    . LYS D 3 47  ? 28.990  -54.585 13.598  1.00 60.67  ? 49  LYS D NZ    1 
ATOM   4948  N N     . LEU D 3 48  ? 24.973  -49.303 12.256  1.00 50.73  ? 50  LEU D N     1 
ATOM   4949  C CA    . LEU D 3 48  ? 24.489  -48.449 13.328  1.00 49.49  ? 50  LEU D CA    1 
ATOM   4950  C C     . LEU D 3 48  ? 23.061  -48.857 13.681  1.00 50.03  ? 50  LEU D C     1 
ATOM   4951  O O     . LEU D 3 48  ? 22.682  -48.862 14.851  1.00 44.56  ? 50  LEU D O     1 
ATOM   4952  C CB    . LEU D 3 48  ? 24.564  -46.978 12.918  1.00 48.35  ? 50  LEU D CB    1 
ATOM   4953  C CG    . LEU D 3 48  ? 25.970  -46.407 12.706  1.00 48.85  ? 50  LEU D CG    1 
ATOM   4954  C CD1   . LEU D 3 48  ? 25.909  -44.919 12.404  1.00 46.48  ? 50  LEU D CD1   1 
ATOM   4955  C CD2   . LEU D 3 48  ? 26.855  -46.672 13.913  1.00 50.22  ? 50  LEU D CD2   1 
ATOM   4956  N N     . LYS D 3 49  ? 22.282  -49.206 12.653  1.00 51.19  ? 51  LYS D N     1 
ATOM   4957  C CA    . LYS D 3 49  ? 20.887  -49.574 12.829  1.00 57.22  ? 51  LYS D CA    1 
ATOM   4958  C C     . LYS D 3 49  ? 20.801  -50.957 13.470  1.00 57.38  ? 51  LYS D C     1 
ATOM   4959  O O     . LYS D 3 49  ? 20.011  -51.172 14.385  1.00 64.45  ? 51  LYS D O     1 
ATOM   4960  C CB    . LYS D 3 49  ? 20.158  -49.529 11.482  1.00 59.13  ? 51  LYS D CB    1 
ATOM   4961  C CG    . LYS D 3 49  ? 20.137  -48.157 10.822  1.00 60.33  ? 51  LYS D CG    1 
ATOM   4962  C CD    . LYS D 3 49  ? 19.400  -48.114 9.489   1.00 64.63  ? 51  LYS D CD    1 
ATOM   4963  C CE    . LYS D 3 49  ? 19.390  -46.742 8.891   1.00 63.63  ? 51  LYS D CE    1 
ATOM   4964  N NZ    . LYS D 3 49  ? 18.673  -46.710 7.613   1.00 63.09  ? 51  LYS D NZ    1 
ATOM   4965  N N     . THR D 3 50  ? 21.623  -51.887 12.974  1.00 56.33  ? 52  THR D N     1 
ATOM   4966  C CA    . THR D 3 50  ? 21.684  -53.232 13.521  1.00 57.47  ? 52  THR D CA    1 
ATOM   4967  C C     . THR D 3 50  ? 22.008  -53.152 15.010  1.00 55.99  ? 52  THR D C     1 
ATOM   4968  O O     . THR D 3 50  ? 21.457  -53.904 15.811  1.00 54.03  ? 52  THR D O     1 
ATOM   4969  C CB    . THR D 3 50  ? 22.728  -54.049 12.760  1.00 58.72  ? 52  THR D CB    1 
ATOM   4970  O OG1   . THR D 3 50  ? 22.203  -54.197 11.444  1.00 61.70  ? 52  THR D OG1   1 
ATOM   4971  C CG2   . THR D 3 50  ? 22.970  -55.412 13.381  1.00 62.69  ? 52  THR D CG2   1 
ATOM   4972  N N     . LEU D 3 51  ? 22.906  -52.228 15.366  1.00 57.23  ? 53  LEU D N     1 
ATOM   4973  C CA    . LEU D 3 51  ? 23.357  -52.079 16.740  1.00 57.10  ? 53  LEU D CA    1 
ATOM   4974  C C     . LEU D 3 51  ? 22.296  -51.344 17.556  1.00 57.07  ? 53  LEU D C     1 
ATOM   4975  O O     . LEU D 3 51  ? 22.333  -51.365 18.784  1.00 52.10  ? 53  LEU D O     1 
ATOM   4976  C CB    . LEU D 3 51  ? 24.699  -51.349 16.772  1.00 57.52  ? 53  LEU D CB    1 
ATOM   4977  C CG    . LEU D 3 51  ? 25.903  -52.143 16.255  1.00 60.66  ? 53  LEU D CG    1 
ATOM   4978  C CD1   . LEU D 3 51  ? 27.185  -51.335 16.369  1.00 55.19  ? 53  LEU D CD1   1 
ATOM   4979  C CD2   . LEU D 3 51  ? 26.032  -53.462 16.998  1.00 63.30  ? 53  LEU D CD2   1 
ATOM   4980  N N     . SER D 3 52  ? 21.353  -50.701 16.860  1.00 58.40  ? 54  SER D N     1 
ATOM   4981  C CA    . SER D 3 52  ? 20.275  -49.980 17.518  1.00 61.38  ? 54  SER D CA    1 
ATOM   4982  C C     . SER D 3 52  ? 19.001  -50.821 17.496  1.00 61.01  ? 54  SER D C     1 
ATOM   4983  O O     . SER D 3 52  ? 17.974  -50.416 18.038  1.00 59.58  ? 54  SER D O     1 
ATOM   4984  C CB    . SER D 3 52  ? 20.053  -48.631 16.884  1.00 59.16  ? 54  SER D CB    1 
ATOM   4985  O OG    . SER D 3 52  ? 19.102  -47.874 17.619  1.00 61.08  ? 54  SER D OG    1 
ATOM   4986  N N     . GLY D 3 53  ? 19.083  -51.993 16.856  1.00 64.22  ? 55  GLY D N     1 
ATOM   4987  C CA    . GLY D 3 53  ? 17.993  -52.954 16.853  1.00 62.75  ? 55  GLY D CA    1 
ATOM   4988  C C     . GLY D 3 53  ? 16.935  -52.614 15.806  1.00 63.01  ? 55  GLY D C     1 
ATOM   4989  O O     . GLY D 3 53  ? 16.114  -53.458 15.454  1.00 66.71  ? 55  GLY D O     1 
ATOM   4990  N N     . ASP D 3 54  ? 16.965  -51.371 15.314  1.00 62.41  ? 56  ASP D N     1 
ATOM   4991  C CA    . ASP D 3 54  ? 15.968  -50.897 14.369  1.00 66.36  ? 56  ASP D CA    1 
ATOM   4992  C C     . ASP D 3 54  ? 16.484  -51.088 12.946  1.00 64.71  ? 56  ASP D C     1 
ATOM   4993  O O     . ASP D 3 54  ? 17.093  -50.186 12.374  1.00 61.11  ? 56  ASP D O     1 
ATOM   4994  C CB    . ASP D 3 54  ? 15.582  -49.453 14.650  1.00 70.76  ? 56  ASP D CB    1 
ATOM   4995  C CG    . ASP D 3 54  ? 14.967  -49.199 16.019  1.00 74.80  ? 56  ASP D CG    1 
ATOM   4996  O OD1   . ASP D 3 54  ? 14.909  -50.154 16.823  1.00 79.77  ? 56  ASP D OD1   1 
ATOM   4997  O OD2   . ASP D 3 54  ? 14.540  -48.052 16.265  1.00 68.22  ? 56  ASP D OD2   1 
ATOM   4998  N N     . SER D 3 55  ? 16.224  -52.274 12.387  1.00 56.72  ? 57  SER D N     1 
ATOM   4999  C CA    . SER D 3 55  ? 16.607  -52.590 11.022  1.00 56.55  ? 57  SER D CA    1 
ATOM   5000  C C     . SER D 3 55  ? 16.429  -51.351 10.131  1.00 57.75  ? 57  SER D C     1 
ATOM   5001  O O     . SER D 3 55  ? 15.269  -51.088 9.744   1.00 64.63  ? 57  SER D O     1 
ATOM   5002  C CB    . SER D 3 55  ? 15.814  -53.759 10.493  1.00 55.95  ? 57  SER D CB    1 
ATOM   5003  O OG    . SER D 3 55  ? 15.999  -54.911 11.304  1.00 55.88  ? 57  SER D OG    1 
ATOM   5004  N N     . ALA D 3 60  ? 9.900   -47.433 2.986   1.00 63.08  ? 62  ALA D N     1 
ATOM   5005  C CA    . ALA D 3 60  ? 9.726   -46.759 1.677   1.00 61.12  ? 62  ALA D CA    1 
ATOM   5006  C C     . ALA D 3 60  ? 9.531   -45.261 1.889   1.00 59.95  ? 62  ALA D C     1 
ATOM   5007  O O     . ALA D 3 60  ? 8.512   -44.828 2.422   1.00 57.93  ? 62  ALA D O     1 
ATOM   5008  C CB    . ALA D 3 60  ? 8.562   -47.368 0.928   1.00 58.58  ? 62  ALA D CB    1 
ATOM   5009  N N     . LEU D 3 61  ? 10.528  -44.485 1.457   1.00 62.00  ? 63  LEU D N     1 
ATOM   5010  C CA    . LEU D 3 61  ? 10.497  -43.039 1.578   1.00 63.22  ? 63  LEU D CA    1 
ATOM   5011  C C     . LEU D 3 61  ? 9.726   -42.437 0.406   1.00 57.53  ? 63  LEU D C     1 
ATOM   5012  O O     . LEU D 3 61  ? 9.575   -41.221 0.318   1.00 61.72  ? 63  LEU D O     1 
ATOM   5013  C CB    . LEU D 3 61  ? 11.929  -42.512 1.628   1.00 65.06  ? 63  LEU D CB    1 
ATOM   5014  C CG    . LEU D 3 61  ? 12.691  -42.744 2.937   1.00 75.44  ? 63  LEU D CG    1 
ATOM   5015  C CD1   . LEU D 3 61  ? 13.531  -41.515 3.238   1.00 78.93  ? 63  LEU D CD1   1 
ATOM   5016  C CD2   . LEU D 3 61  ? 11.769  -43.076 4.098   1.00 74.45  ? 63  LEU D CD2   1 
ATOM   5017  N N     . VAL D 3 62  ? 9.244   -43.305 -0.489  1.00 54.78  ? 64  VAL D N     1 
ATOM   5018  C CA    . VAL D 3 62  ? 8.598   -42.872 -1.718  1.00 53.36  ? 64  VAL D CA    1 
ATOM   5019  C C     . VAL D 3 62  ? 7.146   -42.502 -1.418  1.00 50.35  ? 64  VAL D C     1 
ATOM   5020  O O     . VAL D 3 62  ? 6.379   -43.337 -0.943  1.00 41.76  ? 64  VAL D O     1 
ATOM   5021  C CB    . VAL D 3 62  ? 8.694   -43.984 -2.781  1.00 54.51  ? 64  VAL D CB    1 
ATOM   5022  C CG1   . VAL D 3 62  ? 8.179   -43.521 -4.138  1.00 55.05  ? 64  VAL D CG1   1 
ATOM   5023  C CG2   . VAL D 3 62  ? 10.114  -44.525 -2.908  1.00 56.38  ? 64  VAL D CG2   1 
ATOM   5024  N N     . ILE D 3 63  ? 6.775   -41.245 -1.704  1.00 52.26  ? 65  ILE D N     1 
ATOM   5025  C CA    . ILE D 3 63  ? 5.430   -40.765 -1.420  1.00 47.71  ? 65  ILE D CA    1 
ATOM   5026  C C     . ILE D 3 63  ? 4.877   -40.029 -2.642  1.00 47.07  ? 65  ILE D C     1 
ATOM   5027  O O     . ILE D 3 63  ? 4.034   -39.147 -2.496  1.00 47.24  ? 65  ILE D O     1 
ATOM   5028  C CB    . ILE D 3 63  ? 5.413   -39.846 -0.181  1.00 43.70  ? 65  ILE D CB    1 
ATOM   5029  C CG1   . ILE D 3 63  ? 6.721   -39.898 0.607   1.00 42.71  ? 65  ILE D CG1   1 
ATOM   5030  C CG2   . ILE D 3 63  ? 4.201   -40.144 0.704   1.00 44.80  ? 65  ILE D CG2   1 
ATOM   5031  C CD1   . ILE D 3 63  ? 6.824   -38.841 1.694   1.00 41.07  ? 65  ILE D CD1   1 
ATOM   5032  N N     . SER D 3 64  ? 5.348   -40.394 -3.842  1.00 48.47  ? 66  SER D N     1 
ATOM   5033  C CA    . SER D 3 64  ? 4.938   -39.702 -5.057  1.00 43.77  ? 66  SER D CA    1 
ATOM   5034  C C     . SER D 3 64  ? 5.198   -40.566 -6.291  1.00 45.78  ? 66  SER D C     1 
ATOM   5035  O O     . SER D 3 64  ? 6.050   -41.451 -6.268  1.00 46.66  ? 66  SER D O     1 
ATOM   5036  C CB    . SER D 3 64  ? 5.637   -38.371 -5.177  1.00 41.62  ? 66  SER D CB    1 
ATOM   5037  O OG    . SER D 3 64  ? 7.048   -38.537 -5.219  1.00 41.58  ? 66  SER D OG    1 
ATOM   5038  N N     . HIS D 3 65  ? 4.450   -40.285 -7.369  1.00 42.68  ? 67  HIS D N     1 
ATOM   5039  C CA    . HIS D 3 65  ? 4.650   -40.940 -8.654  1.00 51.33  ? 67  HIS D CA    1 
ATOM   5040  C C     . HIS D 3 65  ? 4.689   -39.890 -9.763  1.00 50.42  ? 67  HIS D C     1 
ATOM   5041  O O     . HIS D 3 65  ? 4.585   -38.695 -9.496  1.00 49.17  ? 67  HIS D O     1 
ATOM   5042  C CB    . HIS D 3 65  ? 3.569   -41.998 -8.916  1.00 53.81  ? 67  HIS D CB    1 
ATOM   5043  C CG    . HIS D 3 65  ? 2.169   -41.532 -8.680  1.00 58.57  ? 67  HIS D CG    1 
ATOM   5044  N ND1   . HIS D 3 65  ? 1.504   -40.665 -9.522  1.00 61.70  ? 67  HIS D ND1   1 
ATOM   5045  C CD2   . HIS D 3 65  ? 1.313   -41.810 -7.686  1.00 64.49  ? 67  HIS D CD2   1 
ATOM   5046  C CE1   . HIS D 3 65  ? 0.287   -40.441 -9.045  1.00 68.49  ? 67  HIS D CE1   1 
ATOM   5047  N NE2   . HIS D 3 65  ? 0.149   -41.129 -7.933  1.00 65.69  ? 67  HIS D NE2   1 
ATOM   5048  N N     . GLY D 3 66  ? 4.840   -40.355 -11.010 1.00 52.11  ? 68  GLY D N     1 
ATOM   5049  C CA    . GLY D 3 66  ? 4.923   -39.468 -12.160 1.00 49.84  ? 68  GLY D CA    1 
ATOM   5050  C C     . GLY D 3 66  ? 4.340   -40.114 -13.416 1.00 51.40  ? 68  GLY D C     1 
ATOM   5051  O O     . GLY D 3 66  ? 4.813   -39.861 -14.522 1.00 41.68  ? 68  GLY D O     1 
ATOM   5052  N N     . ASN D 3 67  ? 3.308   -40.945 -13.229 1.00 51.33  ? 69  ASN D N     1 
ATOM   5053  C CA    . ASN D 3 67  ? 2.630   -41.592 -14.341 1.00 52.53  ? 69  ASN D CA    1 
ATOM   5054  C C     . ASN D 3 67  ? 1.360   -40.817 -14.682 1.00 50.69  ? 69  ASN D C     1 
ATOM   5055  O O     . ASN D 3 67  ? 0.481   -41.332 -15.368 1.00 48.40  ? 69  ASN D O     1 
ATOM   5056  C CB    . ASN D 3 67  ? 2.308   -43.053 -14.040 1.00 53.01  ? 69  ASN D CB    1 
ATOM   5057  C CG    . ASN D 3 67  ? 3.548   -43.881 -13.806 1.00 53.52  ? 69  ASN D CG    1 
ATOM   5058  O OD1   . ASN D 3 67  ? 4.660   -43.341 -13.766 1.00 58.09  ? 69  ASN D OD1   1 
ATOM   5059  N ND2   . ASN D 3 67  ? 3.382   -45.186 -13.642 1.00 59.21  ? 69  ASN D ND2   1 
ATOM   5060  N N     . GLY D 3 68  ? 1.279   -39.576 -14.191 1.00 52.60  ? 70  GLY D N     1 
ATOM   5061  C CA    . GLY D 3 68  ? 0.112   -38.737 -14.407 1.00 54.18  ? 70  GLY D CA    1 
ATOM   5062  C C     . GLY D 3 68  ? -0.849  -38.819 -13.235 1.00 51.29  ? 70  GLY D C     1 
ATOM   5063  O O     . GLY D 3 68  ? -0.353  -39.010 -12.105 1.00 53.10  ? 70  GLY D O     1 
ATOM   5064  N N     . GLY E 1 1   ? 60.933  -26.250 69.184  1.00 42.54  ? 2   GLY E N     1 
ATOM   5065  C CA    . GLY E 1 1   ? 59.708  -25.671 68.601  1.00 39.77  ? 2   GLY E CA    1 
ATOM   5066  C C     . GLY E 1 1   ? 59.088  -26.611 67.571  1.00 38.34  ? 2   GLY E C     1 
ATOM   5067  O O     . GLY E 1 1   ? 59.797  -27.357 66.898  1.00 39.17  ? 2   GLY E O     1 
ATOM   5068  N N     . SER E 1 2   ? 57.757  -26.564 67.465  1.00 33.02  ? 3   SER E N     1 
ATOM   5069  C CA    . SER E 1 2   ? 57.029  -27.399 66.526  1.00 33.92  ? 3   SER E CA    1 
ATOM   5070  C C     . SER E 1 2   ? 55.790  -26.659 66.039  1.00 33.08  ? 3   SER E C     1 
ATOM   5071  O O     . SER E 1 2   ? 55.447  -25.600 66.560  1.00 28.32  ? 3   SER E O     1 
ATOM   5072  C CB    . SER E 1 2   ? 56.663  -28.725 67.143  1.00 36.39  ? 3   SER E CB    1 
ATOM   5073  O OG    . SER E 1 2   ? 55.786  -28.549 68.248  1.00 37.73  ? 3   SER E OG    1 
ATOM   5074  N N     . LEU E 1 3   ? 55.127  -27.233 65.033  1.00 30.73  ? 4   LEU E N     1 
ATOM   5075  C CA    . LEU E 1 3   ? 53.938  -26.630 64.459  1.00 29.43  ? 4   LEU E CA    1 
ATOM   5076  C C     . LEU E 1 3   ? 52.860  -27.696 64.305  1.00 28.25  ? 4   LEU E C     1 
ATOM   5077  O O     . LEU E 1 3   ? 53.128  -28.796 63.828  1.00 30.62  ? 4   LEU E O     1 
ATOM   5078  C CB    . LEU E 1 3   ? 54.279  -25.980 63.119  1.00 32.48  ? 4   LEU E CB    1 
ATOM   5079  C CG    . LEU E 1 3   ? 53.105  -25.354 62.359  1.00 33.90  ? 4   LEU E CG    1 
ATOM   5080  C CD1   . LEU E 1 3   ? 52.471  -24.225 63.153  1.00 36.48  ? 4   LEU E CD1   1 
ATOM   5081  C CD2   . LEU E 1 3   ? 53.552  -24.863 60.993  1.00 34.02  ? 4   LEU E CD2   1 
ATOM   5082  N N     . VAL E 1 4   ? 51.648  -27.354 64.745  1.00 27.33  ? 5   VAL E N     1 
ATOM   5083  C CA    . VAL E 1 4   ? 50.476  -28.175 64.506  1.00 29.60  ? 5   VAL E CA    1 
ATOM   5084  C C     . VAL E 1 4   ? 49.362  -27.259 64.015  1.00 30.31  ? 5   VAL E C     1 
ATOM   5085  O O     . VAL E 1 4   ? 48.934  -26.356 64.730  1.00 32.88  ? 5   VAL E O     1 
ATOM   5086  C CB    . VAL E 1 4   ? 50.033  -28.965 65.753  1.00 28.89  ? 5   VAL E CB    1 
ATOM   5087  C CG1   . VAL E 1 4   ? 48.730  -29.716 65.509  1.00 31.69  ? 5   VAL E CG1   1 
ATOM   5088  C CG2   . VAL E 1 4   ? 51.119  -29.916 66.239  1.00 29.65  ? 5   VAL E CG2   1 
ATOM   5089  N N     . CYS E 1 5   ? 48.926  -27.486 62.775  1.00 28.20  ? 6   CYS E N     1 
ATOM   5090  C CA    . CYS E 1 5   ? 47.824  -26.738 62.199  1.00 27.75  ? 6   CYS E CA    1 
ATOM   5091  C C     . CYS E 1 5   ? 46.535  -27.531 62.388  1.00 24.27  ? 6   CYS E C     1 
ATOM   5092  O O     . CYS E 1 5   ? 46.474  -28.714 62.060  1.00 21.05  ? 6   CYS E O     1 
ATOM   5093  C CB    . CYS E 1 5   ? 48.082  -26.431 60.728  1.00 31.05  ? 6   CYS E CB    1 
ATOM   5094  S SG    . CYS E 1 5   ? 49.508  -25.344 60.459  1.00 39.63  ? 6   CYS E SG    1 
ATOM   5095  N N     . VAL E 1 6   ? 45.515  -26.866 62.934  1.00 24.32  ? 7   VAL E N     1 
ATOM   5096  C CA    . VAL E 1 6   ? 44.244  -27.511 63.210  1.00 24.81  ? 7   VAL E CA    1 
ATOM   5097  C C     . VAL E 1 6   ? 43.124  -26.669 62.607  1.00 23.91  ? 7   VAL E C     1 
ATOM   5098  O O     . VAL E 1 6   ? 43.333  -25.516 62.234  1.00 20.98  ? 7   VAL E O     1 
ATOM   5099  C CB    . VAL E 1 6   ? 44.029  -27.717 64.722  1.00 26.16  ? 7   VAL E CB    1 
ATOM   5100  C CG1   . VAL E 1 6   ? 45.172  -28.504 65.353  1.00 25.39  ? 7   VAL E CG1   1 
ATOM   5101  C CG2   . VAL E 1 6   ? 43.821  -26.395 65.451  1.00 27.94  ? 7   VAL E CG2   1 
ATOM   5102  N N     . GLY E 1 7   ? 41.940  -27.276 62.499  1.00 21.08  ? 8   GLY E N     1 
ATOM   5103  C CA    . GLY E 1 7   ? 40.740  -26.563 62.099  1.00 22.09  ? 8   GLY E CA    1 
ATOM   5104  C C     . GLY E 1 7   ? 39.757  -26.480 63.261  1.00 22.53  ? 8   GLY E C     1 
ATOM   5105  O O     . GLY E 1 7   ? 39.786  -27.316 64.161  1.00 24.07  ? 8   GLY E O     1 
ATOM   5106  N N     . THR E 1 8   ? 38.895  -25.461 63.235  1.00 23.40  ? 9   THR E N     1 
ATOM   5107  C CA    . THR E 1 8   ? 37.923  -25.260 64.295  1.00 26.55  ? 9   THR E CA    1 
ATOM   5108  C C     . THR E 1 8   ? 36.520  -25.440 63.727  1.00 29.97  ? 9   THR E C     1 
ATOM   5109  O O     . THR E 1 8   ? 35.531  -25.179 64.408  1.00 33.62  ? 9   THR E O     1 
ATOM   5110  C CB    . THR E 1 8   ? 38.109  -23.873 64.906  1.00 25.49  ? 9   THR E CB    1 
ATOM   5111  O OG1   . THR E 1 8   ? 37.867  -22.956 63.844  1.00 21.87  ? 9   THR E OG1   1 
ATOM   5112  C CG2   . THR E 1 8   ? 39.503  -23.673 65.473  1.00 26.37  ? 9   THR E CG2   1 
ATOM   5113  N N     . GLY E 1 9   ? 36.449  -25.899 62.475  1.00 34.88  ? 10  GLY E N     1 
ATOM   5114  C CA    . GLY E 1 9   ? 35.180  -26.030 61.785  1.00 33.06  ? 10  GLY E CA    1 
ATOM   5115  C C     . GLY E 1 9   ? 34.560  -24.659 61.547  1.00 32.80  ? 10  GLY E C     1 
ATOM   5116  O O     . GLY E 1 9   ? 35.243  -23.642 61.648  1.00 35.50  ? 10  GLY E O     1 
ATOM   5117  N N     . LEU E 1 10  ? 33.259  -24.642 61.247  1.00 34.56  ? 11  LEU E N     1 
ATOM   5118  C CA    . LEU E 1 10  ? 32.580  -23.401 60.912  1.00 34.56  ? 11  LEU E CA    1 
ATOM   5119  C C     . LEU E 1 10  ? 31.634  -22.977 62.030  1.00 29.93  ? 11  LEU E C     1 
ATOM   5120  O O     . LEU E 1 10  ? 31.402  -21.785 62.220  1.00 29.55  ? 11  LEU E O     1 
ATOM   5121  C CB    . LEU E 1 10  ? 31.865  -23.534 59.571  1.00 40.10  ? 11  LEU E CB    1 
ATOM   5122  C CG    . LEU E 1 10  ? 32.568  -22.831 58.407  1.00 38.22  ? 11  LEU E CG    1 
ATOM   5123  C CD1   . LEU E 1 10  ? 34.058  -23.123 58.460  1.00 42.43  ? 11  LEU E CD1   1 
ATOM   5124  C CD2   . LEU E 1 10  ? 31.987  -23.219 57.064  1.00 36.39  ? 11  LEU E CD2   1 
ATOM   5125  N N     . GLN E 1 11  ? 31.092  -23.951 62.764  1.00 32.15  ? 12  GLN E N     1 
ATOM   5126  C CA    . GLN E 1 11  ? 30.240  -23.654 63.903  1.00 36.32  ? 12  GLN E CA    1 
ATOM   5127  C C     . GLN E 1 11  ? 31.113  -23.332 65.113  1.00 38.04  ? 12  GLN E C     1 
ATOM   5128  O O     . GLN E 1 11  ? 32.277  -23.722 65.173  1.00 39.50  ? 12  GLN E O     1 
ATOM   5129  C CB    . GLN E 1 11  ? 29.269  -24.801 64.181  1.00 34.91  ? 12  GLN E CB    1 
ATOM   5130  C CG    . GLN E 1 11  ? 27.961  -24.702 63.404  1.00 37.72  ? 12  GLN E CG    1 
ATOM   5131  C CD    . GLN E 1 11  ? 27.051  -23.609 63.921  1.00 38.17  ? 12  GLN E CD    1 
ATOM   5132  O OE1   . GLN E 1 11  ? 27.362  -22.923 64.900  1.00 29.55  ? 12  GLN E OE1   1 
ATOM   5133  N NE2   . GLN E 1 11  ? 25.906  -23.447 63.274  1.00 43.32  ? 12  GLN E NE2   1 
ATOM   5134  N N     . LEU E 1 12  ? 30.523  -22.617 66.074  1.00 40.98  ? 13  LEU E N     1 
ATOM   5135  C CA    . LEU E 1 12  ? 31.249  -22.097 67.220  1.00 36.63  ? 13  LEU E CA    1 
ATOM   5136  C C     . LEU E 1 12  ? 31.447  -23.192 68.267  1.00 31.37  ? 13  LEU E C     1 
ATOM   5137  O O     . LEU E 1 12  ? 30.480  -23.741 68.790  1.00 32.43  ? 13  LEU E O     1 
ATOM   5138  C CB    . LEU E 1 12  ? 30.464  -20.910 67.778  1.00 34.83  ? 13  LEU E CB    1 
ATOM   5139  C CG    . LEU E 1 12  ? 30.885  -20.402 69.160  1.00 29.82  ? 13  LEU E CG    1 
ATOM   5140  C CD1   . LEU E 1 12  ? 32.302  -19.854 69.157  1.00 27.13  ? 13  LEU E CD1   1 
ATOM   5141  C CD2   . LEU E 1 12  ? 29.904  -19.349 69.647  1.00 28.91  ? 13  LEU E CD2   1 
ATOM   5142  N N     . ALA E 1 13  ? 32.718  -23.520 68.529  1.00 29.46  ? 14  ALA E N     1 
ATOM   5143  C CA    . ALA E 1 13  ? 33.115  -24.260 69.718  1.00 31.05  ? 14  ALA E CA    1 
ATOM   5144  C C     . ALA E 1 13  ? 32.822  -25.753 69.576  1.00 31.82  ? 14  ALA E C     1 
ATOM   5145  O O     . ALA E 1 13  ? 33.522  -26.576 70.160  1.00 33.43  ? 14  ALA E O     1 
ATOM   5146  C CB    . ALA E 1 13  ? 32.420  -23.680 70.933  1.00 33.13  ? 14  ALA E CB    1 
ATOM   5147  N N     . GLY E 1 14  ? 31.786  -26.096 68.804  1.00 32.61  ? 15  GLY E N     1 
ATOM   5148  C CA    . GLY E 1 14  ? 31.253  -27.449 68.809  1.00 32.14  ? 15  GLY E CA    1 
ATOM   5149  C C     . GLY E 1 14  ? 31.816  -28.310 67.680  1.00 31.89  ? 15  GLY E C     1 
ATOM   5150  O O     . GLY E 1 14  ? 31.824  -29.534 67.780  1.00 28.81  ? 15  GLY E O     1 
ATOM   5151  N N     . GLN E 1 15  ? 32.298  -27.664 66.615  1.00 32.85  ? 16  GLN E N     1 
ATOM   5152  C CA    . GLN E 1 15  ? 32.579  -28.363 65.372  1.00 31.93  ? 16  GLN E CA    1 
ATOM   5153  C C     . GLN E 1 15  ? 34.076  -28.637 65.235  1.00 33.72  ? 16  GLN E C     1 
ATOM   5154  O O     . GLN E 1 15  ? 34.533  -29.067 64.177  1.00 39.30  ? 16  GLN E O     1 
ATOM   5155  C CB    . GLN E 1 15  ? 32.036  -27.548 64.198  1.00 29.47  ? 16  GLN E CB    1 
ATOM   5156  C CG    . GLN E 1 15  ? 31.835  -28.360 62.924  1.00 32.80  ? 16  GLN E CG    1 
ATOM   5157  C CD    . GLN E 1 15  ? 31.005  -27.637 61.887  1.00 33.05  ? 16  GLN E CD    1 
ATOM   5158  O OE1   . GLN E 1 15  ? 31.400  -26.593 61.356  1.00 38.55  ? 16  GLN E OE1   1 
ATOM   5159  N NE2   . GLN E 1 15  ? 29.838  -28.190 61.588  1.00 33.80  ? 16  GLN E NE2   1 
ATOM   5160  N N     . ILE E 1 16  ? 34.830  -28.397 66.313  1.00 27.47  ? 17  ILE E N     1 
ATOM   5161  C CA    . ILE E 1 16  ? 36.246  -28.730 66.343  1.00 25.67  ? 17  ILE E CA    1 
ATOM   5162  C C     . ILE E 1 16  ? 36.398  -30.149 66.881  1.00 24.41  ? 17  ILE E C     1 
ATOM   5163  O O     . ILE E 1 16  ? 35.596  -30.595 67.700  1.00 22.06  ? 17  ILE E O     1 
ATOM   5164  C CB    . ILE E 1 16  ? 37.040  -27.714 67.186  1.00 26.38  ? 17  ILE E CB    1 
ATOM   5165  C CG1   . ILE E 1 16  ? 38.548  -27.933 67.059  1.00 27.75  ? 17  ILE E CG1   1 
ATOM   5166  C CG2   . ILE E 1 16  ? 36.588  -27.741 68.646  1.00 26.72  ? 17  ILE E CG2   1 
ATOM   5167  C CD1   . ILE E 1 16  ? 39.389  -26.914 67.808  1.00 29.90  ? 17  ILE E CD1   1 
ATOM   5168  N N     A SER E 1 17  ? 37.434  -30.850 66.407  0.50 24.85  ? 18  SER E N     1 
ATOM   5169  N N     B SER E 1 17  ? 37.434  -30.851 66.409  0.50 23.41  ? 18  SER E N     1 
ATOM   5170  C CA    A SER E 1 17  ? 37.718  -32.203 66.855  0.50 26.82  ? 18  SER E CA    1 
ATOM   5171  C CA    B SER E 1 17  ? 37.710  -32.206 66.856  0.50 24.22  ? 18  SER E CA    1 
ATOM   5172  C C     A SER E 1 17  ? 38.171  -32.175 68.311  0.50 25.86  ? 18  SER E C     1 
ATOM   5173  C C     B SER E 1 17  ? 38.174  -32.177 68.309  0.50 24.48  ? 18  SER E C     1 
ATOM   5174  O O     A SER E 1 17  ? 38.676  -31.161 68.789  0.50 25.85  ? 18  SER E O     1 
ATOM   5175  O O     B SER E 1 17  ? 38.687  -31.165 68.781  0.50 24.48  ? 18  SER E O     1 
ATOM   5176  C CB    A SER E 1 17  ? 38.748  -32.862 65.974  0.50 28.98  ? 18  SER E CB    1 
ATOM   5177  C CB    B SER E 1 17  ? 38.729  -32.881 65.970  0.50 24.37  ? 18  SER E CB    1 
ATOM   5178  O OG    A SER E 1 17  ? 38.310  -32.906 64.623  0.50 31.60  ? 18  SER E OG    1 
ATOM   5179  O OG    B SER E 1 17  ? 40.006  -32.271 66.098  0.50 23.43  ? 18  SER E OG    1 
ATOM   5180  N N     . VAL E 1 18  ? 37.985  -33.302 69.006  1.00 24.37  ? 19  VAL E N     1 
ATOM   5181  C CA    . VAL E 1 18  ? 38.354  -33.412 70.407  1.00 25.68  ? 19  VAL E CA    1 
ATOM   5182  C C     . VAL E 1 18  ? 39.862  -33.212 70.539  1.00 28.60  ? 19  VAL E C     1 
ATOM   5183  O O     . VAL E 1 18  ? 40.323  -32.502 71.431  1.00 29.07  ? 19  VAL E O     1 
ATOM   5184  C CB    . VAL E 1 18  ? 37.915  -34.766 70.999  1.00 27.81  ? 19  VAL E CB    1 
ATOM   5185  C CG1   . VAL E 1 18  ? 38.407  -34.945 72.430  1.00 30.60  ? 19  VAL E CG1   1 
ATOM   5186  C CG2   . VAL E 1 18  ? 36.404  -34.953 70.923  1.00 26.47  ? 19  VAL E CG2   1 
ATOM   5187  N N     . LEU E 1 19  ? 40.619  -33.836 69.629  1.00 27.44  ? 20  LEU E N     1 
ATOM   5188  C CA    . LEU E 1 19  ? 42.071  -33.804 69.678  1.00 27.51  ? 20  LEU E CA    1 
ATOM   5189  C C     . LEU E 1 19  ? 42.570  -32.403 69.328  1.00 26.28  ? 20  LEU E C     1 
ATOM   5190  O O     . LEU E 1 19  ? 43.492  -31.894 69.962  1.00 26.93  ? 20  LEU E O     1 
ATOM   5191  C CB    . LEU E 1 19  ? 42.643  -34.855 68.729  1.00 27.58  ? 20  LEU E CB    1 
ATOM   5192  C CG    . LEU E 1 19  ? 44.172  -34.935 68.660  1.00 28.82  ? 20  LEU E CG    1 
ATOM   5193  C CD1   . LEU E 1 19  ? 44.763  -35.324 70.006  1.00 30.88  ? 20  LEU E CD1   1 
ATOM   5194  C CD2   . LEU E 1 19  ? 44.615  -35.905 67.580  1.00 29.61  ? 20  LEU E CD2   1 
ATOM   5195  N N     . SER E 1 20  ? 41.959  -31.794 68.307  1.00 25.36  ? 21  SER E N     1 
ATOM   5196  C CA    . SER E 1 20  ? 42.370  -30.477 67.846  1.00 27.45  ? 21  SER E CA    1 
ATOM   5197  C C     . SER E 1 20  ? 42.155  -29.443 68.948  1.00 29.81  ? 21  SER E C     1 
ATOM   5198  O O     . SER E 1 20  ? 42.955  -28.525 69.105  1.00 30.47  ? 21  SER E O     1 
ATOM   5199  C CB    . SER E 1 20  ? 41.651  -30.088 66.580  1.00 26.27  ? 21  SER E CB    1 
ATOM   5200  O OG    . SER E 1 20  ? 42.156  -30.814 65.468  1.00 28.64  ? 21  SER E OG    1 
ATOM   5201  N N     . ARG E 1 21  ? 41.065  -29.605 69.705  1.00 30.87  ? 22  ARG E N     1 
ATOM   5202  C CA    . ARG E 1 21  ? 40.774  -28.727 70.826  1.00 29.17  ? 22  ARG E CA    1 
ATOM   5203  C C     . ARG E 1 21  ? 41.862  -28.897 71.883  1.00 25.92  ? 22  ARG E C     1 
ATOM   5204  O O     . ARG E 1 21  ? 42.276  -27.931 72.519  1.00 24.25  ? 22  ARG E O     1 
ATOM   5205  C CB    . ARG E 1 21  ? 39.391  -29.044 71.406  1.00 33.43  ? 22  ARG E CB    1 
ATOM   5206  C CG    . ARG E 1 21  ? 38.941  -28.117 72.526  1.00 35.34  ? 22  ARG E CG    1 
ATOM   5207  C CD    . ARG E 1 21  ? 37.540  -28.467 73.012  1.00 39.04  ? 22  ARG E CD    1 
ATOM   5208  N NE    . ARG E 1 21  ? 37.011  -27.510 73.990  1.00 38.79  ? 22  ARG E NE    1 
ATOM   5209  C CZ    . ARG E 1 21  ? 37.478  -27.341 75.221  1.00 45.26  ? 22  ARG E CZ    1 
ATOM   5210  N NH1   . ARG E 1 21  ? 38.489  -28.072 75.654  1.00 43.74  ? 22  ARG E NH1   1 
ATOM   5211  N NH2   . ARG E 1 21  ? 36.922  -26.445 76.018  1.00 48.22  ? 22  ARG E NH2   1 
ATOM   5212  N N     . SER E 1 22  ? 42.322  -30.140 72.046  1.00 25.64  ? 23  SER E N     1 
ATOM   5213  C CA    . SER E 1 22  ? 43.314  -30.477 73.053  1.00 29.34  ? 23  SER E CA    1 
ATOM   5214  C C     . SER E 1 22  ? 44.653  -29.827 72.711  1.00 31.43  ? 23  SER E C     1 
ATOM   5215  O O     . SER E 1 22  ? 45.402  -29.438 73.605  1.00 27.99  ? 23  SER E O     1 
ATOM   5216  C CB    . SER E 1 22  ? 43.450  -31.974 73.192  1.00 32.88  ? 23  SER E CB    1 
ATOM   5217  O OG    . SER E 1 22  ? 44.336  -32.315 74.249  1.00 34.30  ? 23  SER E OG    1 
ATOM   5218  N N     . TYR E 1 23  ? 44.946  -29.722 71.408  1.00 29.80  ? 24  TYR E N     1 
ATOM   5219  C CA    . TYR E 1 23  ? 46.182  -29.109 70.948  1.00 27.84  ? 24  TYR E CA    1 
ATOM   5220  C C     . TYR E 1 23  ? 46.180  -27.628 71.314  1.00 27.96  ? 24  TYR E C     1 
ATOM   5221  O O     . TYR E 1 23  ? 47.171  -27.111 71.824  1.00 28.04  ? 24  TYR E O     1 
ATOM   5222  C CB    . TYR E 1 23  ? 46.381  -29.298 69.440  1.00 28.72  ? 24  TYR E CB    1 
ATOM   5223  C CG    . TYR E 1 23  ? 47.089  -30.589 69.053  1.00 27.52  ? 24  TYR E CG    1 
ATOM   5224  C CD1   . TYR E 1 23  ? 48.454  -30.742 69.260  1.00 27.96  ? 24  TYR E CD1   1 
ATOM   5225  C CD2   . TYR E 1 23  ? 46.403  -31.638 68.457  1.00 28.09  ? 24  TYR E CD2   1 
ATOM   5226  C CE1   . TYR E 1 23  ? 49.111  -31.909 68.909  1.00 30.57  ? 24  TYR E CE1   1 
ATOM   5227  C CE2   . TYR E 1 23  ? 47.049  -32.809 68.095  1.00 31.61  ? 24  TYR E CE2   1 
ATOM   5228  C CZ    . TYR E 1 23  ? 48.407  -32.945 68.322  1.00 32.23  ? 24  TYR E CZ    1 
ATOM   5229  O OH    . TYR E 1 23  ? 49.049  -34.096 67.966  1.00 34.09  ? 24  TYR E OH    1 
ATOM   5230  N N     . ILE E 1 24  ? 45.062  -26.953 71.034  1.00 26.14  ? 25  ILE E N     1 
ATOM   5231  C CA    . ILE E 1 24  ? 44.937  -25.531 71.309  1.00 28.64  ? 25  ILE E CA    1 
ATOM   5232  C C     . ILE E 1 24  ? 45.165  -25.291 72.799  1.00 30.23  ? 25  ILE E C     1 
ATOM   5233  O O     . ILE E 1 24  ? 45.861  -24.354 73.182  1.00 28.65  ? 25  ILE E O     1 
ATOM   5234  C CB    . ILE E 1 24  ? 43.565  -25.004 70.848  1.00 28.95  ? 25  ILE E CB    1 
ATOM   5235  C CG1   . ILE E 1 24  ? 43.412  -25.088 69.329  1.00 28.93  ? 25  ILE E CG1   1 
ATOM   5236  C CG2   . ILE E 1 24  ? 43.326  -23.583 71.360  1.00 30.30  ? 25  ILE E CG2   1 
ATOM   5237  C CD1   . ILE E 1 24  ? 42.096  -24.540 68.807  1.00 28.48  ? 25  ILE E CD1   1 
ATOM   5238  N N     . GLU E 1 25  ? 44.582  -26.162 73.628  1.00 32.35  ? 26  GLU E N     1 
ATOM   5239  C CA    . GLU E 1 25  ? 44.587  -25.987 75.070  1.00 35.10  ? 26  GLU E CA    1 
ATOM   5240  C C     . GLU E 1 25  ? 46.017  -26.018 75.604  1.00 35.04  ? 26  GLU E C     1 
ATOM   5241  O O     . GLU E 1 25  ? 46.363  -25.245 76.494  1.00 34.95  ? 26  GLU E O     1 
ATOM   5242  C CB    . GLU E 1 25  ? 43.739  -27.073 75.734  1.00 37.63  ? 26  GLU E CB    1 
ATOM   5243  C CG    . GLU E 1 25  ? 43.705  -26.969 77.257  1.00 44.68  ? 26  GLU E CG    1 
ATOM   5244  C CD    . GLU E 1 25  ? 42.924  -28.080 77.937  1.00 51.33  ? 26  GLU E CD    1 
ATOM   5245  O OE1   . GLU E 1 25  ? 42.413  -28.967 77.221  1.00 59.78  ? 26  GLU E OE1   1 
ATOM   5246  O OE2   . GLU E 1 25  ? 42.826  -28.058 79.182  1.00 59.68  ? 26  GLU E OE2   1 
ATOM   5247  N N     . HIS E 1 26  ? 46.841  -26.923 75.061  1.00 38.50  ? 27  HIS E N     1 
ATOM   5248  C CA    . HIS E 1 26  ? 48.174  -27.158 75.592  1.00 36.54  ? 27  HIS E CA    1 
ATOM   5249  C C     . HIS E 1 26  ? 49.232  -26.493 74.713  1.00 34.72  ? 27  HIS E C     1 
ATOM   5250  O O     . HIS E 1 26  ? 50.421  -26.763 74.862  1.00 33.08  ? 27  HIS E O     1 
ATOM   5251  C CB    . HIS E 1 26  ? 48.448  -28.660 75.735  1.00 38.03  ? 27  HIS E CB    1 
ATOM   5252  C CG    . HIS E 1 26  ? 47.593  -29.348 76.750  1.00 39.84  ? 27  HIS E CG    1 
ATOM   5253  N ND1   . HIS E 1 26  ? 46.542  -30.173 76.412  1.00 43.40  ? 27  HIS E ND1   1 
ATOM   5254  C CD2   . HIS E 1 26  ? 47.663  -29.368 78.087  1.00 43.76  ? 27  HIS E CD2   1 
ATOM   5255  C CE1   . HIS E 1 26  ? 45.989  -30.651 77.518  1.00 42.85  ? 27  HIS E CE1   1 
ATOM   5256  N NE2   . HIS E 1 26  ? 46.653  -30.173 78.547  1.00 42.22  ? 27  HIS E NE2   1 
ATOM   5257  N N     . ALA E 1 27  ? 48.792  -25.618 73.804  1.00 32.31  ? 28  ALA E N     1 
ATOM   5258  C CA    . ALA E 1 27  ? 49.708  -24.900 72.933  1.00 31.40  ? 28  ALA E CA    1 
ATOM   5259  C C     . ALA E 1 27  ? 50.404  -23.787 73.715  1.00 30.07  ? 28  ALA E C     1 
ATOM   5260  O O     . ALA E 1 27  ? 49.805  -23.177 74.598  1.00 34.09  ? 28  ALA E O     1 
ATOM   5261  C CB    . ALA E 1 27  ? 48.958  -24.349 71.741  1.00 28.60  ? 28  ALA E CB    1 
ATOM   5262  N N     . ASP E 1 28  ? 51.677  -23.541 73.382  1.00 29.04  ? 29  ASP E N     1 
ATOM   5263  C CA    . ASP E 1 28  ? 52.431  -22.439 73.958  1.00 29.12  ? 29  ASP E CA    1 
ATOM   5264  C C     . ASP E 1 28  ? 51.895  -21.123 73.403  1.00 27.93  ? 29  ASP E C     1 
ATOM   5265  O O     . ASP E 1 28  ? 51.821  -20.126 74.118  1.00 29.60  ? 29  ASP E O     1 
ATOM   5266  C CB    . ASP E 1 28  ? 53.920  -22.565 73.673  1.00 30.09  ? 29  ASP E CB    1 
ATOM   5267  C CG    . ASP E 1 28  ? 54.656  -23.647 74.449  1.00 35.80  ? 29  ASP E CG    1 
ATOM   5268  O OD1   . ASP E 1 28  ? 54.039  -24.241 75.358  1.00 38.57  ? 29  ASP E OD1   1 
ATOM   5269  O OD2   . ASP E 1 28  ? 55.841  -23.893 74.132  1.00 40.82  ? 29  ASP E OD2   1 
ATOM   5270  N N     . ILE E 1 29  ? 51.538  -21.137 72.114  1.00 26.89  ? 30  ILE E N     1 
ATOM   5271  C CA    . ILE E 1 29  ? 51.026  -19.959 71.437  1.00 25.19  ? 30  ILE E CA    1 
ATOM   5272  C C     . ILE E 1 29  ? 50.130  -20.409 70.288  1.00 24.93  ? 30  ILE E C     1 
ATOM   5273  O O     . ILE E 1 29  ? 50.385  -21.436 69.663  1.00 24.64  ? 30  ILE E O     1 
ATOM   5274  C CB    . ILE E 1 29  ? 52.179  -19.067 70.939  1.00 28.04  ? 30  ILE E CB    1 
ATOM   5275  C CG1   . ILE E 1 29  ? 51.669  -17.720 70.428  1.00 29.66  ? 30  ILE E CG1   1 
ATOM   5276  C CG2   . ILE E 1 29  ? 53.011  -19.795 69.883  1.00 28.45  ? 30  ILE E CG2   1 
ATOM   5277  C CD1   . ILE E 1 29  ? 52.769  -16.751 70.038  1.00 32.74  ? 30  ILE E CD1   1 
ATOM   5278  N N     . VAL E 1 30  ? 49.087  -19.620 70.014  1.00 25.81  ? 31  VAL E N     1 
ATOM   5279  C CA    . VAL E 1 30  ? 48.125  -19.955 68.980  1.00 27.62  ? 31  VAL E CA    1 
ATOM   5280  C C     . VAL E 1 30  ? 48.020  -18.789 68.002  1.00 29.70  ? 31  VAL E C     1 
ATOM   5281  O O     . VAL E 1 30  ? 47.839  -17.643 68.408  1.00 30.33  ? 31  VAL E O     1 
ATOM   5282  C CB    . VAL E 1 30  ? 46.748  -20.302 69.578  1.00 28.71  ? 31  VAL E CB    1 
ATOM   5283  C CG1   . VAL E 1 30  ? 45.736  -20.662 68.495  1.00 30.87  ? 31  VAL E CG1   1 
ATOM   5284  C CG2   . VAL E 1 30  ? 46.844  -21.417 70.612  1.00 26.91  ? 31  VAL E CG2   1 
ATOM   5285  N N     . PHE E 1 31  ? 48.160  -19.105 66.711  1.00 29.14  ? 32  PHE E N     1 
ATOM   5286  C CA    . PHE E 1 31  ? 47.872  -18.164 65.643  1.00 27.66  ? 32  PHE E CA    1 
ATOM   5287  C C     . PHE E 1 31  ? 46.492  -18.497 65.088  1.00 30.15  ? 32  PHE E C     1 
ATOM   5288  O O     . PHE E 1 31  ? 46.243  -19.624 64.666  1.00 31.05  ? 32  PHE E O     1 
ATOM   5289  C CB    . PHE E 1 31  ? 48.976  -18.225 64.584  1.00 27.39  ? 32  PHE E CB    1 
ATOM   5290  C CG    . PHE E 1 31  ? 50.318  -17.684 65.057  1.00 28.79  ? 32  PHE E CG    1 
ATOM   5291  C CD1   . PHE E 1 31  ? 51.171  -18.465 65.828  1.00 31.30  ? 32  PHE E CD1   1 
ATOM   5292  C CD2   . PHE E 1 31  ? 50.723  -16.394 64.729  1.00 31.15  ? 32  PHE E CD2   1 
ATOM   5293  C CE1   . PHE E 1 31  ? 52.390  -17.968 66.260  1.00 32.82  ? 32  PHE E CE1   1 
ATOM   5294  C CE2   . PHE E 1 31  ? 51.944  -15.903 65.163  1.00 30.44  ? 32  PHE E CE2   1 
ATOM   5295  C CZ    . PHE E 1 31  ? 52.774  -16.690 65.926  1.00 31.18  ? 32  PHE E CZ    1 
ATOM   5296  N N     . SER E 1 32  ? 45.599  -17.505 65.103  1.00 29.76  ? 33  SER E N     1 
ATOM   5297  C CA    . SER E 1 32  ? 44.190  -17.750 64.857  1.00 30.23  ? 33  SER E CA    1 
ATOM   5298  C C     . SER E 1 32  ? 43.721  -17.003 63.612  1.00 28.45  ? 33  SER E C     1 
ATOM   5299  O O     . SER E 1 32  ? 44.236  -15.937 63.283  1.00 29.85  ? 33  SER E O     1 
ATOM   5300  C CB    . SER E 1 32  ? 43.366  -17.368 66.061  1.00 26.47  ? 33  SER E CB    1 
ATOM   5301  O OG    . SER E 1 32  ? 43.545  -15.997 66.388  1.00 28.48  ? 33  SER E OG    1 
ATOM   5302  N N     . LEU E 1 33  ? 42.741  -17.599 62.926  1.00 26.16  ? 34  LEU E N     1 
ATOM   5303  C CA    . LEU E 1 33  ? 42.006  -16.930 61.866  1.00 27.74  ? 34  LEU E CA    1 
ATOM   5304  C C     . LEU E 1 33  ? 40.575  -17.460 61.884  1.00 29.84  ? 34  LEU E C     1 
ATOM   5305  O O     . LEU E 1 33  ? 40.250  -18.414 61.180  1.00 32.25  ? 34  LEU E O     1 
ATOM   5306  C CB    . LEU E 1 33  ? 42.678  -17.158 60.514  1.00 28.15  ? 34  LEU E CB    1 
ATOM   5307  C CG    . LEU E 1 33  ? 42.358  -16.123 59.429  1.00 31.23  ? 34  LEU E CG    1 
ATOM   5308  C CD1   . LEU E 1 33  ? 42.946  -16.543 58.094  1.00 34.62  ? 34  LEU E CD1   1 
ATOM   5309  C CD2   . LEU E 1 33  ? 40.862  -15.887 59.309  1.00 32.88  ? 34  LEU E CD2   1 
ATOM   5310  N N     . LEU E 1 34  ? 39.737  -16.842 62.725  1.00 30.01  ? 35  LEU E N     1 
ATOM   5311  C CA    . LEU E 1 34  ? 38.399  -17.345 62.992  1.00 32.54  ? 35  LEU E CA    1 
ATOM   5312  C C     . LEU E 1 34  ? 37.362  -16.422 62.359  1.00 34.08  ? 35  LEU E C     1 
ATOM   5313  O O     . LEU E 1 34  ? 37.646  -15.263 62.067  1.00 32.22  ? 35  LEU E O     1 
ATOM   5314  C CB    . LEU E 1 34  ? 38.196  -17.478 64.500  1.00 33.69  ? 35  LEU E CB    1 
ATOM   5315  C CG    . LEU E 1 34  ? 38.969  -18.614 65.179  1.00 38.84  ? 35  LEU E CG    1 
ATOM   5316  C CD1   . LEU E 1 34  ? 40.458  -18.511 64.898  1.00 43.66  ? 35  LEU E CD1   1 
ATOM   5317  C CD2   . LEU E 1 34  ? 38.711  -18.632 66.674  1.00 39.03  ? 35  LEU E CD2   1 
ATOM   5318  N N     . PRO E 1 35  ? 36.123  -16.916 62.140  1.00 40.19  ? 36  PRO E N     1 
ATOM   5319  C CA    . PRO E 1 35  ? 35.108  -16.170 61.393  1.00 43.02  ? 36  PRO E CA    1 
ATOM   5320  C C     . PRO E 1 35  ? 34.665  -14.874 62.067  1.00 44.51  ? 36  PRO E C     1 
ATOM   5321  O O     . PRO E 1 35  ? 34.532  -13.845 61.408  1.00 46.27  ? 36  PRO E O     1 
ATOM   5322  C CB    . PRO E 1 35  ? 33.939  -17.179 61.265  1.00 44.16  ? 36  PRO E CB    1 
ATOM   5323  C CG    . PRO E 1 35  ? 34.562  -18.531 61.561  1.00 43.05  ? 36  PRO E CG    1 
ATOM   5324  C CD    . PRO E 1 35  ? 35.652  -18.239 62.572  1.00 38.39  ? 36  PRO E CD    1 
ATOM   5325  N N     . ASP E 1 36  ? 34.431  -14.937 63.383  1.00 44.35  ? 37  ASP E N     1 
ATOM   5326  C CA    . ASP E 1 36  ? 33.822  -13.829 64.101  1.00 46.49  ? 37  ASP E CA    1 
ATOM   5327  C C     . ASP E 1 36  ? 34.481  -13.664 65.468  1.00 41.26  ? 37  ASP E C     1 
ATOM   5328  O O     . ASP E 1 36  ? 35.452  -14.347 65.785  1.00 41.35  ? 37  ASP E O     1 
ATOM   5329  C CB    . ASP E 1 36  ? 32.319  -14.024 64.218  1.00 47.99  ? 37  ASP E CB    1 
ATOM   5330  C CG    . ASP E 1 36  ? 31.881  -15.362 64.798  1.00 52.03  ? 37  ASP E CG    1 
ATOM   5331  O OD1   . ASP E 1 36  ? 32.251  -15.648 65.956  1.00 54.36  ? 37  ASP E OD1   1 
ATOM   5332  O OD2   . ASP E 1 36  ? 31.179  -16.108 64.083  1.00 56.02  ? 37  ASP E OD2   1 
ATOM   5333  N N     . GLY E 1 37  ? 33.927  -12.747 66.269  1.00 42.58  ? 38  GLY E N     1 
ATOM   5334  C CA    . GLY E 1 37  ? 34.470  -12.419 67.577  1.00 39.42  ? 38  GLY E CA    1 
ATOM   5335  C C     . GLY E 1 37  ? 34.029  -13.424 68.637  1.00 37.02  ? 38  GLY E C     1 
ATOM   5336  O O     . GLY E 1 37  ? 34.743  -13.652 69.612  1.00 36.06  ? 38  GLY E O     1 
ATOM   5337  N N     . PHE E 1 38  ? 32.843  -14.011 68.442  1.00 33.95  ? 39  PHE E N     1 
ATOM   5338  C CA    . PHE E 1 38  ? 32.339  -15.030 69.348  1.00 32.10  ? 39  PHE E CA    1 
ATOM   5339  C C     . PHE E 1 38  ? 33.315  -16.200 69.355  1.00 33.19  ? 39  PHE E C     1 
ATOM   5340  O O     . PHE E 1 38  ? 33.570  -16.800 70.397  1.00 32.40  ? 39  PHE E O     1 
ATOM   5341  C CB    . PHE E 1 38  ? 30.935  -15.503 68.956  1.00 33.60  ? 39  PHE E CB    1 
ATOM   5342  C CG    . PHE E 1 38  ? 29.827  -14.478 69.154  1.00 33.98  ? 39  PHE E CG    1 
ATOM   5343  C CD1   . PHE E 1 38  ? 29.341  -14.192 70.425  1.00 32.91  ? 39  PHE E CD1   1 
ATOM   5344  C CD2   . PHE E 1 38  ? 29.242  -13.836 68.067  1.00 35.13  ? 39  PHE E CD2   1 
ATOM   5345  C CE1   . PHE E 1 38  ? 28.325  -13.266 70.603  1.00 35.91  ? 39  PHE E CE1   1 
ATOM   5346  C CE2   . PHE E 1 38  ? 28.222  -12.916 68.253  1.00 35.19  ? 39  PHE E CE2   1 
ATOM   5347  C CZ    . PHE E 1 38  ? 27.768  -12.632 69.518  1.00 33.30  ? 39  PHE E CZ    1 
ATOM   5348  N N     . SER E 1 39  ? 33.856  -16.508 68.172  1.00 32.35  ? 40  SER E N     1 
ATOM   5349  C CA    . SER E 1 39  ? 34.799  -17.601 68.012  1.00 35.18  ? 40  SER E CA    1 
ATOM   5350  C C     . SER E 1 39  ? 36.159  -17.196 68.572  1.00 32.02  ? 40  SER E C     1 
ATOM   5351  O O     . SER E 1 39  ? 36.905  -18.037 69.068  1.00 29.26  ? 40  SER E O     1 
ATOM   5352  C CB    . SER E 1 39  ? 34.903  -18.016 66.564  1.00 36.69  ? 40  SER E CB    1 
ATOM   5353  O OG    . SER E 1 39  ? 35.743  -19.152 66.415  1.00 45.46  ? 40  SER E OG    1 
ATOM   5354  N N     . GLN E 1 40  ? 36.469  -15.898 68.486  1.00 36.19  ? 41  GLN E N     1 
ATOM   5355  C CA    . GLN E 1 40  ? 37.748  -15.386 68.948  1.00 38.39  ? 41  GLN E CA    1 
ATOM   5356  C C     . GLN E 1 40  ? 37.780  -15.431 70.474  1.00 33.74  ? 41  GLN E C     1 
ATOM   5357  O O     . GLN E 1 40  ? 38.800  -15.774 71.067  1.00 39.46  ? 41  GLN E O     1 
ATOM   5358  C CB    . GLN E 1 40  ? 37.987  -13.967 68.429  1.00 44.88  ? 41  GLN E CB    1 
ATOM   5359  C CG    . GLN E 1 40  ? 39.439  -13.512 68.532  1.00 48.38  ? 41  GLN E CG    1 
ATOM   5360  C CD    . GLN E 1 40  ? 40.378  -14.342 67.683  1.00 51.49  ? 41  GLN E CD    1 
ATOM   5361  O OE1   . GLN E 1 40  ? 39.952  -15.184 66.886  1.00 61.53  ? 41  GLN E OE1   1 
ATOM   5362  N NE2   . GLN E 1 40  ? 41.672  -14.103 67.839  1.00 52.02  ? 41  GLN E NE2   1 
ATOM   5363  N N     . ARG E 1 41  ? 36.649  -15.080 71.095  1.00 34.47  ? 42  ARG E N     1 
ATOM   5364  C CA    A ARG E 1 41  ? 36.514  -15.115 72.543  0.50 33.25  ? 42  ARG E CA    1 
ATOM   5365  C CA    B ARG E 1 41  ? 36.529  -15.112 72.543  0.50 32.41  ? 42  ARG E CA    1 
ATOM   5366  C C     . ARG E 1 41  ? 36.651  -16.555 73.029  1.00 31.66  ? 42  ARG E C     1 
ATOM   5367  O O     . ARG E 1 41  ? 37.386  -16.831 73.975  1.00 33.23  ? 42  ARG E O     1 
ATOM   5368  C CB    A ARG E 1 41  ? 35.157  -14.551 72.980  0.50 34.33  ? 42  ARG E CB    1 
ATOM   5369  C CB    B ARG E 1 41  ? 35.226  -14.432 72.982  0.50 32.29  ? 42  ARG E CB    1 
ATOM   5370  C CG    A ARG E 1 41  ? 34.926  -13.080 72.661  0.50 35.46  ? 42  ARG E CG    1 
ATOM   5371  C CG    B ARG E 1 41  ? 35.371  -12.932 73.202  0.50 32.44  ? 42  ARG E CG    1 
ATOM   5372  C CD    A ARG E 1 41  ? 35.905  -12.165 73.379  0.50 38.15  ? 42  ARG E CD    1 
ATOM   5373  C CD    B ARG E 1 41  ? 34.042  -12.214 73.404  0.50 33.41  ? 42  ARG E CD    1 
ATOM   5374  N NE    A ARG E 1 41  ? 35.474  -10.762 73.346  0.50 39.39  ? 42  ARG E NE    1 
ATOM   5375  N NE    B ARG E 1 41  ? 33.432  -11.798 72.136  0.50 35.06  ? 42  ARG E NE    1 
ATOM   5376  C CZ    A ARG E 1 41  ? 34.310  -10.341 72.865  0.50 44.10  ? 42  ARG E CZ    1 
ATOM   5377  C CZ    B ARG E 1 41  ? 32.228  -12.160 71.713  0.50 35.67  ? 42  ARG E CZ    1 
ATOM   5378  N NH1   A ARG E 1 41  ? 33.446  -11.208 72.367  0.50 43.05  ? 42  ARG E NH1   1 
ATOM   5379  N NH1   B ARG E 1 41  ? 31.494  -12.984 72.437  0.50 35.94  ? 42  ARG E NH1   1 
ATOM   5380  N NH2   A ARG E 1 41  ? 34.012  -9.054  72.887  0.50 47.09  ? 42  ARG E NH2   1 
ATOM   5381  N NH2   B ARG E 1 41  ? 31.766  -11.703 70.563  0.50 35.98  ? 42  ARG E NH2   1 
ATOM   5382  N N     . TRP E 1 42  ? 35.931  -17.469 72.368  1.00 29.06  ? 43  TRP E N     1 
ATOM   5383  C CA    . TRP E 1 42  ? 35.970  -18.880 72.717  1.00 26.00  ? 43  TRP E CA    1 
ATOM   5384  C C     . TRP E 1 42  ? 37.411  -19.381 72.741  1.00 25.09  ? 43  TRP E C     1 
ATOM   5385  O O     . TRP E 1 42  ? 37.809  -20.101 73.654  1.00 18.95  ? 43  TRP E O     1 
ATOM   5386  C CB    . TRP E 1 42  ? 35.129  -19.708 71.737  1.00 28.45  ? 43  TRP E CB    1 
ATOM   5387  C CG    . TRP E 1 42  ? 35.470  -21.175 71.748  1.00 27.89  ? 43  TRP E CG    1 
ATOM   5388  C CD1   . TRP E 1 42  ? 35.056  -22.109 72.651  1.00 29.18  ? 43  TRP E CD1   1 
ATOM   5389  C CD2   . TRP E 1 42  ? 36.303  -21.878 70.800  1.00 29.77  ? 43  TRP E CD2   1 
ATOM   5390  N NE1   . TRP E 1 42  ? 35.573  -23.338 72.338  1.00 27.96  ? 43  TRP E NE1   1 
ATOM   5391  C CE2   . TRP E 1 42  ? 36.340  -23.228 71.208  1.00 30.45  ? 43  TRP E CE2   1 
ATOM   5392  C CE3   . TRP E 1 42  ? 37.015  -21.501 69.655  1.00 30.55  ? 43  TRP E CE3   1 
ATOM   5393  C CZ2   . TRP E 1 42  ? 37.060  -24.196 70.510  1.00 30.46  ? 43  TRP E CZ2   1 
ATOM   5394  C CZ3   . TRP E 1 42  ? 37.724  -22.459 68.967  1.00 33.91  ? 43  TRP E CZ3   1 
ATOM   5395  C CH2   . TRP E 1 42  ? 37.746  -23.787 69.391  1.00 30.66  ? 43  TRP E CH2   1 
ATOM   5396  N N     . LEU E 1 43  ? 38.178  -19.006 71.713  1.00 26.47  ? 44  LEU E N     1 
ATOM   5397  C CA    . LEU E 1 43  ? 39.556  -19.447 71.581  1.00 27.27  ? 44  LEU E CA    1 
ATOM   5398  C C     . LEU E 1 43  ? 40.383  -18.904 72.742  1.00 25.80  ? 44  LEU E C     1 
ATOM   5399  O O     . LEU E 1 43  ? 41.186  -19.626 73.327  1.00 23.60  ? 44  LEU E O     1 
ATOM   5400  C CB    . LEU E 1 43  ? 40.118  -18.990 70.236  1.00 29.77  ? 44  LEU E CB    1 
ATOM   5401  C CG    . LEU E 1 43  ? 41.591  -19.322 69.981  1.00 30.69  ? 44  LEU E CG    1 
ATOM   5402  C CD1   . LEU E 1 43  ? 41.823  -20.824 70.017  1.00 31.30  ? 44  LEU E CD1   1 
ATOM   5403  C CD2   . LEU E 1 43  ? 42.059  -18.737 68.660  1.00 31.10  ? 44  LEU E CD2   1 
ATOM   5404  N N     . THR E 1 44  ? 40.172  -17.624 73.065  1.00 28.33  ? 45  THR E N     1 
ATOM   5405  C CA    . THR E 1 44  ? 40.979  -16.935 74.058  1.00 28.71  ? 45  THR E CA    1 
ATOM   5406  C C     . THR E 1 44  ? 40.811  -17.614 75.415  1.00 33.52  ? 45  THR E C     1 
ATOM   5407  O O     . THR E 1 44  ? 41.734  -17.617 76.226  1.00 31.37  ? 45  THR E O     1 
ATOM   5408  C CB    . THR E 1 44  ? 40.574  -15.463 74.109  1.00 31.64  ? 45  THR E CB    1 
ATOM   5409  O OG1   . THR E 1 44  ? 40.736  -14.983 72.778  1.00 36.07  ? 45  THR E OG1   1 
ATOM   5410  C CG2   . THR E 1 44  ? 41.426  -14.657 75.073  1.00 31.96  ? 45  THR E CG2   1 
ATOM   5411  N N     . LYS E 1 45  ? 39.625  -18.187 75.647  1.00 36.69  ? 46  LYS E N     1 
ATOM   5412  C CA    . LYS E 1 45  ? 39.312  -18.824 76.916  1.00 39.72  ? 46  LYS E CA    1 
ATOM   5413  C C     . LYS E 1 45  ? 40.001  -20.184 76.988  1.00 41.65  ? 46  LYS E C     1 
ATOM   5414  O O     . LYS E 1 45  ? 40.360  -20.642 78.072  1.00 34.13  ? 46  LYS E O     1 
ATOM   5415  C CB    . LYS E 1 45  ? 37.797  -18.955 77.106  1.00 46.84  ? 46  LYS E CB    1 
ATOM   5416  C CG    . LYS E 1 45  ? 37.044  -17.634 77.195  1.00 51.46  ? 46  LYS E CG    1 
ATOM   5417  C CD    . LYS E 1 45  ? 35.586  -17.776 77.615  1.00 56.28  ? 46  LYS E CD    1 
ATOM   5418  C CE    . LYS E 1 45  ? 35.440  -18.342 78.994  1.00 63.79  ? 46  LYS E CE    1 
ATOM   5419  N NZ    . LYS E 1 45  ? 34.036  -18.434 79.401  1.00 69.27  ? 46  LYS E NZ    1 
ATOM   5420  N N     . LEU E 1 46  ? 40.171  -20.824 75.825  1.00 38.88  ? 47  LEU E N     1 
ATOM   5421  C CA    . LEU E 1 46  ? 40.906  -22.075 75.740  1.00 38.13  ? 47  LEU E CA    1 
ATOM   5422  C C     . LEU E 1 46  ? 42.381  -21.801 76.016  1.00 38.13  ? 47  LEU E C     1 
ATOM   5423  O O     . LEU E 1 46  ? 43.000  -22.477 76.835  1.00 35.71  ? 47  LEU E O     1 
ATOM   5424  C CB    . LEU E 1 46  ? 40.714  -22.733 74.374  1.00 40.08  ? 47  LEU E CB    1 
ATOM   5425  C CG    . LEU E 1 46  ? 39.436  -23.559 74.198  1.00 40.11  ? 47  LEU E CG    1 
ATOM   5426  C CD1   . LEU E 1 46  ? 39.417  -24.252 72.846  1.00 38.35  ? 47  LEU E CD1   1 
ATOM   5427  C CD2   . LEU E 1 46  ? 39.297  -24.572 75.321  1.00 41.65  ? 47  LEU E CD2   1 
ATOM   5428  N N     . ASN E 1 47  ? 42.925  -20.799 75.318  1.00 36.05  ? 48  ASN E N     1 
ATOM   5429  C CA    . ASN E 1 47  ? 44.325  -20.436 75.445  1.00 34.62  ? 48  ASN E CA    1 
ATOM   5430  C C     . ASN E 1 47  ? 44.449  -18.919 75.332  1.00 35.43  ? 48  ASN E C     1 
ATOM   5431  O O     . ASN E 1 47  ? 44.074  -18.337 74.316  1.00 38.36  ? 48  ASN E O     1 
ATOM   5432  C CB    . ASN E 1 47  ? 45.176  -21.154 74.403  1.00 40.74  ? 48  ASN E CB    1 
ATOM   5433  C CG    . ASN E 1 47  ? 46.652  -21.070 74.711  1.00 38.06  ? 48  ASN E CG    1 
ATOM   5434  O OD1   . ASN E 1 47  ? 47.181  -19.975 74.934  1.00 40.99  ? 48  ASN E OD1   1 
ATOM   5435  N ND2   . ASN E 1 47  ? 47.327  -22.209 74.738  1.00 37.17  ? 48  ASN E ND2   1 
ATOM   5436  N N     . PRO E 1 48  ? 44.976  -18.234 76.372  1.00 35.41  ? 49  PRO E N     1 
ATOM   5437  C CA    . PRO E 1 48  ? 45.032  -16.770 76.380  1.00 37.21  ? 49  PRO E CA    1 
ATOM   5438  C C     . PRO E 1 48  ? 46.108  -16.181 75.471  1.00 37.64  ? 49  PRO E C     1 
ATOM   5439  O O     . PRO E 1 48  ? 46.025  -15.019 75.080  1.00 36.48  ? 49  PRO E O     1 
ATOM   5440  C CB    . PRO E 1 48  ? 45.298  -16.470 77.867  1.00 36.90  ? 49  PRO E CB    1 
ATOM   5441  C CG    . PRO E 1 48  ? 46.120  -17.651 78.335  1.00 36.96  ? 49  PRO E CG    1 
ATOM   5442  C CD    . PRO E 1 48  ? 45.528  -18.838 77.595  1.00 35.93  ? 49  PRO E CD    1 
ATOM   5443  N N     . ASN E 1 49  ? 47.118  -16.995 75.145  1.00 39.15  ? 50  ASN E N     1 
ATOM   5444  C CA    . ASN E 1 49  ? 48.238  -16.543 74.336  1.00 39.17  ? 50  ASN E CA    1 
ATOM   5445  C C     . ASN E 1 49  ? 47.911  -16.742 72.859  1.00 36.00  ? 50  ASN E C     1 
ATOM   5446  O O     . ASN E 1 49  ? 48.408  -17.673 72.230  1.00 32.35  ? 50  ASN E O     1 
ATOM   5447  C CB    . ASN E 1 49  ? 49.527  -17.261 74.716  1.00 40.70  ? 50  ASN E CB    1 
ATOM   5448  C CG    . ASN E 1 49  ? 50.723  -16.708 73.979  1.00 43.41  ? 50  ASN E CG    1 
ATOM   5449  O OD1   . ASN E 1 49  ? 50.601  -15.717 73.250  1.00 46.64  ? 50  ASN E OD1   1 
ATOM   5450  N ND2   . ASN E 1 49  ? 51.883  -17.322 74.161  1.00 39.50  ? 50  ASN E ND2   1 
ATOM   5451  N N     . VAL E 1 50  ? 47.082  -15.845 72.316  1.00 34.73  ? 51  VAL E N     1 
ATOM   5452  C CA    . VAL E 1 50  ? 46.642  -15.941 70.935  1.00 36.39  ? 51  VAL E CA    1 
ATOM   5453  C C     . VAL E 1 50  ? 47.172  -14.743 70.153  1.00 33.96  ? 51  VAL E C     1 
ATOM   5454  O O     . VAL E 1 50  ? 47.256  -13.636 70.679  1.00 37.37  ? 51  VAL E O     1 
ATOM   5455  C CB    . VAL E 1 50  ? 45.106  -16.024 70.847  1.00 39.54  ? 51  VAL E CB    1 
ATOM   5456  C CG1   . VAL E 1 50  ? 44.614  -15.928 69.408  1.00 40.19  ? 51  VAL E CG1   1 
ATOM   5457  C CG2   . VAL E 1 50  ? 44.567  -17.280 71.520  1.00 40.70  ? 51  VAL E CG2   1 
ATOM   5458  N N     . ILE E 1 51  ? 47.534  -14.991 68.890  1.00 33.95  ? 52  ILE E N     1 
ATOM   5459  C CA    . ILE E 1 51  ? 47.875  -13.933 67.954  1.00 31.70  ? 52  ILE E CA    1 
ATOM   5460  C C     . ILE E 1 51  ? 46.948  -14.047 66.747  1.00 30.94  ? 52  ILE E C     1 
ATOM   5461  O O     . ILE E 1 51  ? 46.863  -15.103 66.123  1.00 28.25  ? 52  ILE E O     1 
ATOM   5462  C CB    . ILE E 1 51  ? 49.359  -14.008 67.550  1.00 35.13  ? 52  ILE E CB    1 
ATOM   5463  C CG1   . ILE E 1 51  ? 50.279  -13.775 68.751  1.00 35.31  ? 52  ILE E CG1   1 
ATOM   5464  C CG2   . ILE E 1 51  ? 49.666  -13.038 66.408  1.00 34.96  ? 52  ILE E CG2   1 
ATOM   5465  C CD1   . ILE E 1 51  ? 51.758  -13.777 68.407  1.00 38.66  ? 52  ILE E CD1   1 
ATOM   5466  N N     . ASN E 1 52  ? 46.251  -12.950 66.434  1.00 28.49  ? 53  ASN E N     1 
ATOM   5467  C CA    . ASN E 1 52  ? 45.252  -12.946 65.379  1.00 30.50  ? 53  ASN E CA    1 
ATOM   5468  C C     . ASN E 1 52  ? 45.926  -12.648 64.041  1.00 29.02  ? 53  ASN E C     1 
ATOM   5469  O O     . ASN E 1 52  ? 46.527  -11.590 63.863  1.00 27.10  ? 53  ASN E O     1 
ATOM   5470  C CB    . ASN E 1 52  ? 44.130  -11.960 65.686  1.00 33.28  ? 53  ASN E CB    1 
ATOM   5471  C CG    . ASN E 1 52  ? 42.964  -12.105 64.737  1.00 37.87  ? 53  ASN E CG    1 
ATOM   5472  O OD1   . ASN E 1 52  ? 43.018  -12.912 63.804  1.00 39.74  ? 53  ASN E OD1   1 
ATOM   5473  N ND2   . ASN E 1 52  ? 41.905  -11.339 64.957  1.00 39.63  ? 53  ASN E ND2   1 
ATOM   5474  N N     . LEU E 1 53  ? 45.806  -13.593 63.102  1.00 27.64  ? 54  LEU E N     1 
ATOM   5475  C CA    . LEU E 1 53  ? 46.414  -13.462 61.787  1.00 30.35  ? 54  LEU E CA    1 
ATOM   5476  C C     . LEU E 1 53  ? 45.656  -12.415 60.976  1.00 30.32  ? 54  LEU E C     1 
ATOM   5477  O O     . LEU E 1 53  ? 46.167  -11.901 59.984  1.00 34.49  ? 54  LEU E O     1 
ATOM   5478  C CB    . LEU E 1 53  ? 46.420  -14.818 61.080  1.00 31.00  ? 54  LEU E CB    1 
ATOM   5479  C CG    . LEU E 1 53  ? 47.292  -15.905 61.716  1.00 32.00  ? 54  LEU E CG    1 
ATOM   5480  C CD1   . LEU E 1 53  ? 47.172  -17.213 60.950  1.00 30.75  ? 54  LEU E CD1   1 
ATOM   5481  C CD2   . LEU E 1 53  ? 48.743  -15.462 61.795  1.00 34.12  ? 54  LEU E CD2   1 
ATOM   5482  N N     . GLN E 1 54  ? 44.434  -12.106 61.419  1.00 29.11  ? 55  GLN E N     1 
ATOM   5483  C CA    . GLN E 1 54  ? 43.570  -11.160 60.734  1.00 32.36  ? 55  GLN E CA    1 
ATOM   5484  C C     . GLN E 1 54  ? 44.307  -9.837  60.530  1.00 31.34  ? 55  GLN E C     1 
ATOM   5485  O O     . GLN E 1 54  ? 43.986  -9.075  59.620  1.00 26.69  ? 55  GLN E O     1 
ATOM   5486  C CB    . GLN E 1 54  ? 42.298  -10.958 61.560  1.00 33.49  ? 55  GLN E CB    1 
ATOM   5487  C CG    . GLN E 1 54  ? 41.174  -10.240 60.820  1.00 37.72  ? 55  GLN E CG    1 
ATOM   5488  C CD    . GLN E 1 54  ? 40.553  -11.078 59.724  1.00 50.54  ? 55  GLN E CD    1 
ATOM   5489  O OE1   . GLN E 1 54  ? 40.507  -10.681 58.554  1.00 58.24  ? 55  GLN E OE1   1 
ATOM   5490  N NE2   . GLN E 1 54  ? 40.057  -12.250 60.095  1.00 51.56  ? 55  GLN E NE2   1 
ATOM   5491  N N     . GLN E 1 55  ? 45.310  -9.585  61.377  1.00 33.95  ? 56  GLN E N     1 
ATOM   5492  C CA    . GLN E 1 55  ? 45.963  -8.287  61.442  1.00 34.74  ? 56  GLN E CA    1 
ATOM   5493  C C     . GLN E 1 55  ? 46.839  -8.062  60.212  1.00 37.96  ? 56  GLN E C     1 
ATOM   5494  O O     . GLN E 1 55  ? 47.336  -6.957  60.002  1.00 39.03  ? 56  GLN E O     1 
ATOM   5495  C CB    . GLN E 1 55  ? 46.826  -8.188  62.700  1.00 37.36  ? 56  GLN E CB    1 
ATOM   5496  C CG    . GLN E 1 55  ? 48.074  -9.063  62.661  1.00 36.37  ? 56  GLN E CG    1 
ATOM   5497  C CD    . GLN E 1 55  ? 48.828  -9.082  63.973  1.00 38.08  ? 56  GLN E CD    1 
ATOM   5498  O OE1   . GLN E 1 55  ? 48.308  -9.513  65.008  1.00 37.41  ? 56  GLN E OE1   1 
ATOM   5499  N NE2   . GLN E 1 55  ? 50.069  -8.618  63.941  1.00 37.76  ? 56  GLN E NE2   1 
ATOM   5500  N N     . PHE E 1 56  ? 47.031  -9.115  59.409  1.00 40.46  ? 57  PHE E N     1 
ATOM   5501  C CA    . PHE E 1 56  ? 47.953  -9.050  58.286  1.00 41.32  ? 57  PHE E CA    1 
ATOM   5502  C C     . PHE E 1 56  ? 47.188  -8.743  57.001  1.00 41.55  ? 57  PHE E C     1 
ATOM   5503  O O     . PHE E 1 56  ? 47.793  -8.601  55.941  1.00 35.63  ? 57  PHE E O     1 
ATOM   5504  C CB    . PHE E 1 56  ? 48.765  -10.345 58.170  1.00 40.52  ? 57  PHE E CB    1 
ATOM   5505  C CG    . PHE E 1 56  ? 49.752  -10.565 59.308  1.00 39.96  ? 57  PHE E CG    1 
ATOM   5506  C CD1   . PHE E 1 56  ? 50.897  -9.782  59.418  1.00 43.04  ? 57  PHE E CD1   1 
ATOM   5507  C CD2   . PHE E 1 56  ? 49.546  -11.564 60.253  1.00 41.00  ? 57  PHE E CD2   1 
ATOM   5508  C CE1   . PHE E 1 56  ? 51.794  -9.980  60.456  1.00 40.87  ? 57  PHE E CE1   1 
ATOM   5509  C CE2   . PHE E 1 56  ? 50.450  -11.760 61.285  1.00 42.25  ? 57  PHE E CE2   1 
ATOM   5510  C CZ    . PHE E 1 56  ? 51.571  -10.970 61.383  1.00 41.73  ? 57  PHE E CZ    1 
ATOM   5511  N N     . TYR E 1 57  ? 45.860  -8.632  57.104  1.00 42.28  ? 58  TYR E N     1 
ATOM   5512  C CA    . TYR E 1 57  ? 45.041  -8.277  55.956  1.00 42.66  ? 58  TYR E CA    1 
ATOM   5513  C C     . TYR E 1 57  ? 45.088  -6.766  55.758  1.00 46.80  ? 58  TYR E C     1 
ATOM   5514  O O     . TYR E 1 57  ? 45.305  -6.015  56.708  1.00 42.18  ? 58  TYR E O     1 
ATOM   5515  C CB    . TYR E 1 57  ? 43.593  -8.754  56.104  1.00 41.28  ? 58  TYR E CB    1 
ATOM   5516  C CG    . TYR E 1 57  ? 43.398  -10.243 55.858  1.00 38.89  ? 58  TYR E CG    1 
ATOM   5517  C CD1   . TYR E 1 57  ? 43.358  -10.757 54.567  1.00 33.44  ? 58  TYR E CD1   1 
ATOM   5518  C CD2   . TYR E 1 57  ? 43.236  -11.131 56.913  1.00 38.47  ? 58  TYR E CD2   1 
ATOM   5519  C CE1   . TYR E 1 57  ? 43.180  -12.111 54.335  1.00 37.55  ? 58  TYR E CE1   1 
ATOM   5520  C CE2   . TYR E 1 57  ? 43.052  -12.486 56.694  1.00 38.58  ? 58  TYR E CE2   1 
ATOM   5521  C CZ    . TYR E 1 57  ? 43.026  -12.977 55.402  1.00 36.14  ? 58  TYR E CZ    1 
ATOM   5522  O OH    . TYR E 1 57  ? 42.847  -14.311 55.179  1.00 46.45  ? 58  TYR E OH    1 
ATOM   5523  N N     . ALA E 1 58  ? 44.878  -6.339  54.509  1.00 44.26  ? 59  ALA E N     1 
ATOM   5524  C CA    . ALA E 1 58  ? 44.883  -4.929  54.160  1.00 46.40  ? 59  ALA E CA    1 
ATOM   5525  C C     . ALA E 1 58  ? 44.170  -4.129  55.246  1.00 49.44  ? 59  ALA E C     1 
ATOM   5526  O O     . ALA E 1 58  ? 43.072  -4.486  55.666  1.00 41.08  ? 59  ALA E O     1 
ATOM   5527  C CB    . ALA E 1 58  ? 44.233  -4.733  52.808  1.00 50.72  ? 59  ALA E CB    1 
ATOM   5528  N N     . GLN E 1 59  ? 44.815  -3.047  55.694  1.00 51.79  ? 60  GLN E N     1 
ATOM   5529  C CA    . GLN E 1 59  ? 44.267  -2.198  56.738  1.00 58.71  ? 60  GLN E CA    1 
ATOM   5530  C C     . GLN E 1 59  ? 44.161  -0.764  56.225  1.00 57.79  ? 60  GLN E C     1 
ATOM   5531  O O     . GLN E 1 59  ? 45.167  -0.151  55.874  1.00 60.41  ? 60  GLN E O     1 
ATOM   5532  C CB    . GLN E 1 59  ? 45.151  -2.230  57.985  1.00 64.61  ? 60  GLN E CB    1 
ATOM   5533  C CG    . GLN E 1 59  ? 45.393  -3.625  58.556  1.00 66.35  ? 60  GLN E CG    1 
ATOM   5534  C CD    . GLN E 1 59  ? 44.154  -4.253  59.156  1.00 69.31  ? 60  GLN E CD    1 
ATOM   5535  O OE1   . GLN E 1 59  ? 43.430  -3.631  59.942  1.00 63.00  ? 60  GLN E OE1   1 
ATOM   5536  N NE2   . GLN E 1 59  ? 43.897  -5.501  58.789  1.00 67.28  ? 60  GLN E NE2   1 
ATOM   5537  N N     . ASN E 1 60  ? 42.930  -0.243  56.186  1.00 61.93  ? 61  ASN E N     1 
ATOM   5538  C CA    . ASN E 1 60  ? 42.692  1.156   55.870  1.00 63.78  ? 61  ASN E CA    1 
ATOM   5539  C C     . ASN E 1 60  ? 42.756  1.367   54.359  1.00 56.98  ? 61  ASN E C     1 
ATOM   5540  O O     . ASN E 1 60  ? 43.682  2.001   53.857  1.00 65.20  ? 61  ASN E O     1 
ATOM   5541  C CB    . ASN E 1 60  ? 43.684  2.065   56.589  1.00 68.22  ? 61  ASN E CB    1 
ATOM   5542  C CG    . ASN E 1 60  ? 43.698  1.831   58.081  1.00 76.02  ? 61  ASN E CG    1 
ATOM   5543  O OD1   . ASN E 1 60  ? 42.668  1.990   58.746  1.00 79.75  ? 61  ASN E OD1   1 
ATOM   5544  N ND2   . ASN E 1 60  ? 44.847  1.457   58.624  1.00 81.34  ? 61  ASN E ND2   1 
ATOM   5545  N N     . GLY E 1 61  ? 41.755  0.838   53.646  1.00 45.41  ? 62  GLY E N     1 
ATOM   5546  C CA    . GLY E 1 61  ? 41.642  1.026   52.207  1.00 43.46  ? 62  GLY E CA    1 
ATOM   5547  C C     . GLY E 1 61  ? 42.998  0.901   51.517  1.00 41.13  ? 62  GLY E C     1 
ATOM   5548  O O     . GLY E 1 61  ? 43.256  1.565   50.516  1.00 45.36  ? 62  GLY E O     1 
ATOM   5549  N N     . GLU E 1 62  ? 43.848  0.027   52.064  1.00 43.16  ? 63  GLU E N     1 
ATOM   5550  C CA    . GLU E 1 62  ? 45.195  -0.180  51.561  1.00 42.15  ? 63  GLU E CA    1 
ATOM   5551  C C     . GLU E 1 62  ? 45.172  -1.187  50.415  1.00 41.72  ? 63  GLU E C     1 
ATOM   5552  O O     . GLU E 1 62  ? 44.427  -2.164  50.456  1.00 40.78  ? 63  GLU E O     1 
ATOM   5553  C CB    . GLU E 1 62  ? 46.077  -0.672  52.708  1.00 43.54  ? 63  GLU E CB    1 
ATOM   5554  C CG    . GLU E 1 62  ? 47.345  -1.384  52.246  1.00 45.41  ? 63  GLU E CG    1 
ATOM   5555  C CD    . GLU E 1 62  ? 48.113  -2.055  53.370  1.00 53.63  ? 63  GLU E CD    1 
ATOM   5556  O OE1   . GLU E 1 62  ? 47.634  -2.009  54.524  1.00 58.69  ? 63  GLU E OE1   1 
ATOM   5557  O OE2   . GLU E 1 62  ? 49.188  -2.625  53.092  1.00 61.62  ? 63  GLU E OE2   1 
ATOM   5558  N N     . VAL E 1 63  ? 46.002  -0.933  49.397  1.00 39.46  ? 64  VAL E N     1 
ATOM   5559  C CA    . VAL E 1 63  ? 46.171  -1.857  48.287  1.00 40.39  ? 64  VAL E CA    1 
ATOM   5560  C C     . VAL E 1 63  ? 47.282  -2.837  48.650  1.00 41.92  ? 64  VAL E C     1 
ATOM   5561  O O     . VAL E 1 63  ? 48.459  -2.483  48.628  1.00 42.28  ? 64  VAL E O     1 
ATOM   5562  C CB    . VAL E 1 63  ? 46.484  -1.131  46.964  1.00 43.24  ? 64  VAL E CB    1 
ATOM   5563  C CG1   . VAL E 1 63  ? 46.781  -2.114  45.837  1.00 46.54  ? 64  VAL E CG1   1 
ATOM   5564  C CG2   . VAL E 1 63  ? 45.367  -0.175  46.562  1.00 44.38  ? 64  VAL E CG2   1 
ATOM   5565  N N     . LYS E 1 64  ? 46.890  -4.070  48.982  1.00 40.05  ? 65  LYS E N     1 
ATOM   5566  C CA    . LYS E 1 64  ? 47.834  -5.085  49.418  1.00 41.54  ? 65  LYS E CA    1 
ATOM   5567  C C     . LYS E 1 64  ? 47.473  -6.422  48.778  1.00 40.60  ? 65  LYS E C     1 
ATOM   5568  O O     . LYS E 1 64  ? 46.373  -6.934  48.972  1.00 36.83  ? 65  LYS E O     1 
ATOM   5569  C CB    . LYS E 1 64  ? 47.819  -5.178  50.948  1.00 43.75  ? 65  LYS E CB    1 
ATOM   5570  C CG    . LYS E 1 64  ? 48.822  -6.149  51.554  1.00 43.58  ? 65  LYS E CG    1 
ATOM   5571  C CD    . LYS E 1 64  ? 48.788  -6.178  53.078  1.00 46.20  ? 65  LYS E CD    1 
ATOM   5572  C CE    . LYS E 1 64  ? 49.993  -6.833  53.672  1.00 43.72  ? 65  LYS E CE    1 
ATOM   5573  N NZ    . LYS E 1 64  ? 49.932  -6.841  55.136  1.00 43.27  ? 65  LYS E NZ    1 
ATOM   5574  N N     . ASN E 1 65  ? 48.416  -6.974  48.008  1.00 44.59  ? 66  ASN E N     1 
ATOM   5575  C CA    . ASN E 1 65  ? 48.246  -8.285  47.405  1.00 44.76  ? 66  ASN E CA    1 
ATOM   5576  C C     . ASN E 1 65  ? 48.155  -9.322  48.521  1.00 44.05  ? 66  ASN E C     1 
ATOM   5577  O O     . ASN E 1 65  ? 48.947  -9.297  49.461  1.00 47.18  ? 66  ASN E O     1 
ATOM   5578  C CB    . ASN E 1 65  ? 49.372  -8.595  46.424  1.00 46.20  ? 66  ASN E CB    1 
ATOM   5579  C CG    . ASN E 1 65  ? 49.114  -9.859  45.640  1.00 46.73  ? 66  ASN E CG    1 
ATOM   5580  O OD1   . ASN E 1 65  ? 48.898  -10.924 46.228  1.00 43.83  ? 66  ASN E OD1   1 
ATOM   5581  N ND2   . ASN E 1 65  ? 49.125  -9.764  44.318  1.00 44.78  ? 66  ASN E ND2   1 
ATOM   5582  N N     . ARG E 1 66  ? 47.178  -10.228 48.411  1.00 43.60  ? 67  ARG E N     1 
ATOM   5583  C CA    . ARG E 1 66  ? 46.917  -11.200 49.459  1.00 46.43  ? 67  ARG E CA    1 
ATOM   5584  C C     . ARG E 1 66  ? 48.085  -12.177 49.562  1.00 45.90  ? 67  ARG E C     1 
ATOM   5585  O O     . ARG E 1 66  ? 48.277  -12.810 50.598  1.00 48.41  ? 67  ARG E O     1 
ATOM   5586  C CB    . ARG E 1 66  ? 45.594  -11.934 49.216  1.00 49.63  ? 67  ARG E CB    1 
ATOM   5587  C CG    . ARG E 1 66  ? 44.366  -11.042 49.324  1.00 51.06  ? 67  ARG E CG    1 
ATOM   5588  C CD    . ARG E 1 66  ? 43.125  -11.821 49.735  1.00 48.77  ? 67  ARG E CD    1 
ATOM   5589  N NE    . ARG E 1 66  ? 42.728  -12.830 48.748  1.00 51.34  ? 67  ARG E NE    1 
ATOM   5590  C CZ    . ARG E 1 66  ? 42.187  -12.558 47.567  1.00 51.23  ? 67  ARG E CZ    1 
ATOM   5591  N NH1   . ARG E 1 66  ? 41.927  -11.308 47.231  1.00 49.24  ? 67  ARG E NH1   1 
ATOM   5592  N NH2   . ARG E 1 66  ? 41.889  -13.541 46.735  1.00 53.38  ? 67  ARG E NH2   1 
ATOM   5593  N N     . ARG E 1 67  ? 48.861  -12.290 48.479  1.00 42.78  ? 68  ARG E N     1 
ATOM   5594  C CA    . ARG E 1 67  ? 50.015  -13.173 48.452  1.00 42.19  ? 68  ARG E CA    1 
ATOM   5595  C C     . ARG E 1 67  ? 51.045  -12.675 49.463  1.00 40.62  ? 68  ARG E C     1 
ATOM   5596  O O     . ARG E 1 67  ? 51.784  -13.467 50.045  1.00 36.61  ? 68  ARG E O     1 
ATOM   5597  C CB    . ARG E 1 67  ? 50.600  -13.249 47.036  1.00 45.91  ? 68  ARG E CB    1 
ATOM   5598  C CG    . ARG E 1 67  ? 49.592  -13.676 45.978  1.00 52.01  ? 68  ARG E CG    1 
ATOM   5599  C CD    . ARG E 1 67  ? 50.197  -13.737 44.583  1.00 57.93  ? 68  ARG E CD    1 
ATOM   5600  N NE    . ARG E 1 67  ? 51.162  -14.832 44.433  1.00 59.70  ? 68  ARG E NE    1 
ATOM   5601  C CZ    . ARG E 1 67  ? 51.049  -15.817 43.550  1.00 62.54  ? 68  ARG E CZ    1 
ATOM   5602  N NH1   . ARG E 1 67  ? 50.015  -15.854 42.729  1.00 62.79  ? 68  ARG E NH1   1 
ATOM   5603  N NH2   . ARG E 1 67  ? 51.972  -16.761 43.491  1.00 61.94  ? 68  ARG E NH2   1 
ATOM   5604  N N     . ASP E 1 68  ? 51.075  -11.353 49.666  1.00 36.96  ? 69  ASP E N     1 
ATOM   5605  C CA    . ASP E 1 68  ? 51.956  -10.740 50.646  1.00 36.95  ? 69  ASP E CA    1 
ATOM   5606  C C     . ASP E 1 68  ? 51.398  -10.989 52.045  1.00 40.38  ? 69  ASP E C     1 
ATOM   5607  O O     . ASP E 1 68  ? 52.149  -11.260 52.980  1.00 41.70  ? 69  ASP E O     1 
ATOM   5608  C CB    . ASP E 1 68  ? 52.141  -9.255  50.374  1.00 39.80  ? 69  ASP E CB    1 
ATOM   5609  C CG    . ASP E 1 68  ? 52.874  -8.911  49.085  1.00 39.17  ? 69  ASP E CG    1 
ATOM   5610  O OD1   . ASP E 1 68  ? 54.051  -9.309  48.957  1.00 42.95  ? 69  ASP E OD1   1 
ATOM   5611  O OD2   . ASP E 1 68  ? 52.264  -8.246  48.223  1.00 42.54  ? 69  ASP E OD2   1 
ATOM   5612  N N     . THR E 1 69  ? 50.071  -10.888 52.171  1.00 35.97  ? 70  THR E N     1 
ATOM   5613  C CA    . THR E 1 69  ? 49.391  -11.109 53.436  1.00 34.99  ? 70  THR E CA    1 
ATOM   5614  C C     . THR E 1 69  ? 49.713  -12.513 53.942  1.00 35.28  ? 70  THR E C     1 
ATOM   5615  O O     . THR E 1 69  ? 50.139  -12.687 55.082  1.00 31.25  ? 70  THR E O     1 
ATOM   5616  C CB    . THR E 1 69  ? 47.888  -10.910 53.246  1.00 38.04  ? 70  THR E CB    1 
ATOM   5617  O OG1   . THR E 1 69  ? 47.717  -9.519  52.998  1.00 39.14  ? 70  THR E OG1   1 
ATOM   5618  C CG2   . THR E 1 69  ? 47.084  -11.324 54.466  1.00 40.03  ? 70  THR E CG2   1 
ATOM   5619  N N     . TYR E 1 70  ? 49.501  -13.507 53.073  1.00 33.24  ? 71  TYR E N     1 
ATOM   5620  C CA    . TYR E 1 70  ? 49.717  -14.901 53.421  1.00 33.84  ? 71  TYR E CA    1 
ATOM   5621  C C     . TYR E 1 70  ? 51.175  -15.098 53.830  1.00 33.39  ? 71  TYR E C     1 
ATOM   5622  O O     . TYR E 1 70  ? 51.460  -15.758 54.826  1.00 34.15  ? 71  TYR E O     1 
ATOM   5623  C CB    . TYR E 1 70  ? 49.308  -15.783 52.237  1.00 37.35  ? 71  TYR E CB    1 
ATOM   5624  C CG    . TYR E 1 70  ? 47.853  -15.630 51.808  1.00 40.24  ? 71  TYR E CG    1 
ATOM   5625  C CD1   . TYR E 1 70  ? 46.857  -15.349 52.736  1.00 37.58  ? 71  TYR E CD1   1 
ATOM   5626  C CD2   . TYR E 1 70  ? 47.479  -15.757 50.476  1.00 42.15  ? 71  TYR E CD2   1 
ATOM   5627  C CE1   . TYR E 1 70  ? 45.534  -15.204 52.352  1.00 39.42  ? 71  TYR E CE1   1 
ATOM   5628  C CE2   . TYR E 1 70  ? 46.159  -15.614 50.080  1.00 41.83  ? 71  TYR E CE2   1 
ATOM   5629  C CZ    . TYR E 1 70  ? 45.183  -15.337 51.020  1.00 39.89  ? 71  TYR E CZ    1 
ATOM   5630  O OH    . TYR E 1 70  ? 43.881  -15.196 50.635  1.00 43.06  ? 71  TYR E OH    1 
ATOM   5631  N N     . GLU E 1 71  ? 52.091  -14.513 53.050  1.00 36.05  ? 72  GLU E N     1 
ATOM   5632  C CA    . GLU E 1 71  ? 53.517  -14.631 53.310  1.00 37.83  ? 72  GLU E CA    1 
ATOM   5633  C C     . GLU E 1 71  ? 53.831  -14.118 54.714  1.00 39.61  ? 72  GLU E C     1 
ATOM   5634  O O     . GLU E 1 71  ? 54.624  -14.718 55.437  1.00 35.69  ? 72  GLU E O     1 
ATOM   5635  C CB    . GLU E 1 71  ? 54.323  -13.855 52.268  1.00 38.04  ? 72  GLU E CB    1 
ATOM   5636  C CG    . GLU E 1 71  ? 55.823  -13.848 52.548  1.00 40.17  ? 72  GLU E CG    1 
ATOM   5637  C CD    . GLU E 1 71  ? 56.456  -15.227 52.607  1.00 42.93  ? 72  GLU E CD    1 
ATOM   5638  O OE1   . GLU E 1 71  ? 55.730  -16.222 52.401  1.00 51.67  ? 72  GLU E OE1   1 
ATOM   5639  O OE2   . GLU E 1 71  ? 57.676  -15.304 52.862  1.00 44.59  ? 72  GLU E OE2   1 
ATOM   5640  N N     . GLN E 1 72  ? 53.210  -12.994 55.082  1.00 35.76  ? 73  GLN E N     1 
ATOM   5641  C CA    . GLN E 1 72  ? 53.439  -12.381 56.379  1.00 41.05  ? 73  GLN E CA    1 
ATOM   5642  C C     . GLN E 1 72  ? 52.866  -13.282 57.470  1.00 35.86  ? 73  GLN E C     1 
ATOM   5643  O O     . GLN E 1 72  ? 53.439  -13.396 58.551  1.00 34.58  ? 73  GLN E O     1 
ATOM   5644  C CB    . GLN E 1 72  ? 52.831  -10.979 56.418  1.00 43.68  ? 73  GLN E CB    1 
ATOM   5645  C CG    . GLN E 1 72  ? 53.524  -9.982  55.496  1.00 47.96  ? 73  GLN E CG    1 
ATOM   5646  C CD    . GLN E 1 72  ? 52.897  -8.606  55.526  1.00 53.02  ? 73  GLN E CD    1 
ATOM   5647  O OE1   . GLN E 1 72  ? 51.889  -8.370  56.200  1.00 59.61  ? 73  GLN E OE1   1 
ATOM   5648  N NE2   . GLN E 1 72  ? 53.490  -7.680  54.786  1.00 56.75  ? 73  GLN E NE2   1 
ATOM   5649  N N     . MET E 1 73  ? 51.731  -13.921 57.170  1.00 35.42  ? 74  MET E N     1 
ATOM   5650  C CA    . MET E 1 73  ? 51.116  -14.860 58.091  1.00 31.76  ? 74  MET E CA    1 
ATOM   5651  C C     . MET E 1 73  ? 52.083  -16.012 58.355  1.00 30.64  ? 74  MET E C     1 
ATOM   5652  O O     . MET E 1 73  ? 52.364  -16.341 59.505  1.00 31.68  ? 74  MET E O     1 
ATOM   5653  C CB    . MET E 1 73  ? 49.801  -15.409 57.527  1.00 31.46  ? 74  MET E CB    1 
ATOM   5654  C CG    . MET E 1 73  ? 48.650  -14.420 57.564  1.00 32.20  ? 74  MET E CG    1 
ATOM   5655  S SD    . MET E 1 73  ? 47.131  -15.105 56.874  1.00 31.64  ? 74  MET E SD    1 
ATOM   5656  C CE    . MET E 1 73  ? 46.011  -13.705 57.012  1.00 34.40  ? 74  MET E CE    1 
ATOM   5657  N N     . VAL E 1 74  ? 52.594  -16.605 57.272  1.00 31.50  ? 75  VAL E N     1 
ATOM   5658  C CA    . VAL E 1 74  ? 53.460  -17.769 57.362  1.00 32.14  ? 75  VAL E CA    1 
ATOM   5659  C C     . VAL E 1 74  ? 54.695  -17.411 58.185  1.00 34.50  ? 75  VAL E C     1 
ATOM   5660  O O     . VAL E 1 74  ? 55.113  -18.178 59.050  1.00 35.16  ? 75  VAL E O     1 
ATOM   5661  C CB    . VAL E 1 74  ? 53.846  -18.285 55.961  1.00 29.99  ? 75  VAL E CB    1 
ATOM   5662  C CG1   . VAL E 1 74  ? 54.905  -19.379 56.029  1.00 30.20  ? 75  VAL E CG1   1 
ATOM   5663  C CG2   . VAL E 1 74  ? 52.629  -18.766 55.180  1.00 33.34  ? 75  VAL E CG2   1 
ATOM   5664  N N     . ASN E 1 75  ? 55.266  -16.234 57.909  1.00 36.64  ? 76  ASN E N     1 
ATOM   5665  C CA    . ASN E 1 75  ? 56.492  -15.802 58.559  1.00 36.07  ? 76  ASN E CA    1 
ATOM   5666  C C     . ASN E 1 75  ? 56.260  -15.684 60.063  1.00 33.75  ? 76  ASN E C     1 
ATOM   5667  O O     . ASN E 1 75  ? 57.093  -16.113 60.860  1.00 32.14  ? 76  ASN E O     1 
ATOM   5668  C CB    . ASN E 1 75  ? 57.004  -14.491 57.974  1.00 37.55  ? 76  ASN E CB    1 
ATOM   5669  C CG    . ASN E 1 75  ? 58.243  -13.999 58.682  1.00 42.99  ? 76  ASN E CG    1 
ATOM   5670  O OD1   . ASN E 1 75  ? 58.226  -12.924 59.292  1.00 53.69  ? 76  ASN E OD1   1 
ATOM   5671  N ND2   . ASN E 1 75  ? 59.319  -14.769 58.625  1.00 49.47  ? 76  ASN E ND2   1 
ATOM   5672  N N     . ALA E 1 76  ? 55.123  -15.088 60.436  1.00 30.93  ? 77  ALA E N     1 
ATOM   5673  C CA    . ALA E 1 76  ? 54.786  -14.868 61.832  1.00 30.13  ? 77  ALA E CA    1 
ATOM   5674  C C     . ALA E 1 76  ? 54.691  -16.205 62.565  1.00 28.58  ? 77  ALA E C     1 
ATOM   5675  O O     . ALA E 1 76  ? 55.133  -16.328 63.705  1.00 24.96  ? 77  ALA E O     1 
ATOM   5676  C CB    . ALA E 1 76  ? 53.491  -14.090 61.931  1.00 28.95  ? 77  ALA E CB    1 
ATOM   5677  N N     . ILE E 1 77  ? 54.110  -17.204 61.894  1.00 27.18  ? 78  ILE E N     1 
ATOM   5678  C CA    . ILE E 1 77  ? 53.909  -18.512 62.495  1.00 25.71  ? 78  ILE E CA    1 
ATOM   5679  C C     . ILE E 1 77  ? 55.264  -19.179 62.716  1.00 25.55  ? 78  ILE E C     1 
ATOM   5680  O O     . ILE E 1 77  ? 55.486  -19.807 63.748  1.00 24.38  ? 78  ILE E O     1 
ATOM   5681  C CB    . ILE E 1 77  ? 52.984  -19.382 61.625  1.00 26.22  ? 78  ILE E CB    1 
ATOM   5682  C CG1   . ILE E 1 77  ? 51.599  -18.752 61.475  1.00 24.66  ? 78  ILE E CG1   1 
ATOM   5683  C CG2   . ILE E 1 77  ? 52.900  -20.805 62.177  1.00 27.13  ? 78  ILE E CG2   1 
ATOM   5684  C CD1   . ILE E 1 77  ? 50.662  -19.522 60.563  1.00 21.93  ? 78  ILE E CD1   1 
ATOM   5685  N N     . LEU E 1 78  ? 56.162  -19.041 61.734  1.00 26.44  ? 79  LEU E N     1 
ATOM   5686  C CA    . LEU E 1 78  ? 57.458  -19.696 61.791  1.00 28.20  ? 79  LEU E CA    1 
ATOM   5687  C C     . LEU E 1 78  ? 58.349  -19.007 62.823  1.00 28.64  ? 79  LEU E C     1 
ATOM   5688  O O     . LEU E 1 78  ? 59.173  -19.660 63.459  1.00 32.00  ? 79  LEU E O     1 
ATOM   5689  C CB    . LEU E 1 78  ? 58.117  -19.739 60.412  1.00 30.03  ? 79  LEU E CB    1 
ATOM   5690  C CG    . LEU E 1 78  ? 57.826  -20.991 59.578  1.00 33.14  ? 79  LEU E CG    1 
ATOM   5691  C CD1   . LEU E 1 78  ? 57.945  -22.222 60.462  1.00 34.23  ? 79  LEU E CD1   1 
ATOM   5692  C CD2   . LEU E 1 78  ? 56.469  -20.944 58.898  1.00 34.97  ? 79  LEU E CD2   1 
ATOM   5693  N N     . ASP E 1 79  ? 58.173  -17.691 62.989  1.00 28.26  ? 80  ASP E N     1 
ATOM   5694  C CA    . ASP E 1 79  ? 58.967  -16.933 63.944  1.00 32.41  ? 80  ASP E CA    1 
ATOM   5695  C C     . ASP E 1 79  ? 58.795  -17.526 65.341  1.00 33.04  ? 80  ASP E C     1 
ATOM   5696  O O     . ASP E 1 79  ? 59.748  -17.584 66.115  1.00 32.15  ? 80  ASP E O     1 
ATOM   5697  C CB    . ASP E 1 79  ? 58.626  -15.451 63.912  1.00 36.15  ? 80  ASP E CB    1 
ATOM   5698  C CG    . ASP E 1 79  ? 59.265  -14.659 62.780  1.00 38.43  ? 80  ASP E CG    1 
ATOM   5699  O OD1   . ASP E 1 79  ? 59.983  -15.276 61.967  1.00 48.58  ? 80  ASP E OD1   1 
ATOM   5700  O OD2   . ASP E 1 79  ? 59.051  -13.429 62.732  1.00 45.34  ? 80  ASP E OD2   1 
ATOM   5701  N N     . ALA E 1 80  ? 57.571  -17.963 65.656  1.00 31.17  ? 81  ALA E N     1 
ATOM   5702  C CA    . ALA E 1 80  ? 57.282  -18.537 66.959  1.00 30.03  ? 81  ALA E CA    1 
ATOM   5703  C C     . ALA E 1 80  ? 57.924  -19.917 67.068  1.00 29.32  ? 81  ALA E C     1 
ATOM   5704  O O     . ALA E 1 80  ? 58.498  -20.259 68.099  1.00 25.54  ? 81  ALA E O     1 
ATOM   5705  C CB    . ALA E 1 80  ? 55.787  -18.596 67.182  1.00 30.45  ? 81  ALA E CB    1 
ATOM   5706  N N     . VAL E 1 81  ? 57.830  -20.696 65.984  1.00 31.71  ? 82  VAL E N     1 
ATOM   5707  C CA    . VAL E 1 81  ? 58.383  -22.040 65.949  1.00 30.48  ? 82  VAL E CA    1 
ATOM   5708  C C     . VAL E 1 81  ? 59.898  -21.954 66.116  1.00 29.39  ? 82  VAL E C     1 
ATOM   5709  O O     . VAL E 1 81  ? 60.486  -22.706 66.889  1.00 26.45  ? 82  VAL E O     1 
ATOM   5710  C CB    . VAL E 1 81  ? 58.016  -22.778 64.647  1.00 28.46  ? 82  VAL E CB    1 
ATOM   5711  C CG1   . VAL E 1 81  ? 58.673  -24.151 64.573  1.00 26.63  ? 82  VAL E CG1   1 
ATOM   5712  C CG2   . VAL E 1 81  ? 56.508  -22.895 64.465  1.00 28.63  ? 82  VAL E CG2   1 
ATOM   5713  N N     . ARG E 1 82  ? 60.514  -21.026 65.377  1.00 34.45  ? 83  ARG E N     1 
ATOM   5714  C CA    . ARG E 1 82  ? 61.958  -20.859 65.387  1.00 34.41  ? 83  ARG E CA    1 
ATOM   5715  C C     . ARG E 1 82  ? 62.421  -20.462 66.787  1.00 35.60  ? 83  ARG E C     1 
ATOM   5716  O O     . ARG E 1 82  ? 63.544  -20.767 67.182  1.00 33.10  ? 83  ARG E O     1 
ATOM   5717  C CB    . ARG E 1 82  ? 62.366  -19.809 64.346  1.00 37.10  ? 83  ARG E CB    1 
ATOM   5718  C CG    . ARG E 1 82  ? 62.078  -20.224 62.911  1.00 36.67  ? 83  ARG E CG    1 
ATOM   5719  C CD    . ARG E 1 82  ? 62.137  -19.048 61.950  1.00 39.92  ? 83  ARG E CD    1 
ATOM   5720  N NE    . ARG E 1 82  ? 61.717  -19.425 60.596  1.00 38.77  ? 83  ARG E NE    1 
ATOM   5721  C CZ    . ARG E 1 82  ? 61.434  -18.561 59.630  1.00 41.95  ? 83  ARG E CZ    1 
ATOM   5722  N NH1   . ARG E 1 82  ? 61.491  -17.263 59.868  1.00 46.23  ? 83  ARG E NH1   1 
ATOM   5723  N NH2   . ARG E 1 82  ? 61.078  -18.999 58.434  1.00 43.42  ? 83  ARG E NH2   1 
ATOM   5724  N N     . ALA E 1 83  ? 61.542  -19.779 67.527  1.00 35.91  ? 84  ALA E N     1 
ATOM   5725  C CA    . ALA E 1 83  ? 61.862  -19.317 68.868  1.00 37.52  ? 84  ALA E CA    1 
ATOM   5726  C C     . ALA E 1 83  ? 61.821  -20.489 69.846  1.00 34.02  ? 84  ALA E C     1 
ATOM   5727  O O     . ALA E 1 83  ? 62.395  -20.416 70.931  1.00 35.46  ? 84  ALA E O     1 
ATOM   5728  C CB    . ALA E 1 83  ? 60.909  -18.215 69.278  1.00 40.19  ? 84  ALA E CB    1 
ATOM   5729  N N     . GLY E 1 84  ? 61.126  -21.563 69.452  1.00 31.30  ? 85  GLY E N     1 
ATOM   5730  C CA    . GLY E 1 84  ? 61.112  -22.797 70.221  1.00 32.81  ? 85  GLY E CA    1 
ATOM   5731  C C     . GLY E 1 84  ? 59.776  -23.015 70.929  1.00 32.92  ? 85  GLY E C     1 
ATOM   5732  O O     . GLY E 1 84  ? 59.706  -23.746 71.915  1.00 35.96  ? 85  GLY E O     1 
ATOM   5733  N N     . LYS E 1 85  ? 58.718  -22.390 70.405  1.00 32.80  ? 86  LYS E N     1 
ATOM   5734  C CA    . LYS E 1 85  ? 57.397  -22.480 71.004  1.00 34.14  ? 86  LYS E CA    1 
ATOM   5735  C C     . LYS E 1 85  ? 56.599  -23.598 70.339  1.00 31.49  ? 86  LYS E C     1 
ATOM   5736  O O     . LYS E 1 85  ? 56.564  -23.703 69.113  1.00 25.44  ? 86  LYS E O     1 
ATOM   5737  C CB    . LYS E 1 85  ? 56.634  -21.160 70.850  1.00 36.80  ? 86  LYS E CB    1 
ATOM   5738  C CG    . LYS E 1 85  ? 57.228  -19.965 71.581  1.00 41.46  ? 86  LYS E CG    1 
ATOM   5739  C CD    . LYS E 1 85  ? 56.540  -18.649 71.235  1.00 43.61  ? 86  LYS E CD    1 
ATOM   5740  C CE    . LYS E 1 85  ? 57.317  -17.446 71.668  1.00 46.41  ? 86  LYS E CE    1 
ATOM   5741  N NZ    . LYS E 1 85  ? 57.487  -17.393 73.122  1.00 51.00  ? 86  LYS E NZ    1 
ATOM   5742  N N     . LYS E 1 86  ? 55.953  -24.427 71.164  1.00 30.68  ? 87  LYS E N     1 
ATOM   5743  C CA    . LYS E 1 86  ? 54.977  -25.381 70.668  1.00 30.64  ? 87  LYS E CA    1 
ATOM   5744  C C     . LYS E 1 86  ? 53.813  -24.591 70.079  1.00 30.76  ? 87  LYS E C     1 
ATOM   5745  O O     . LYS E 1 86  ? 52.916  -24.161 70.801  1.00 31.21  ? 87  LYS E O     1 
ATOM   5746  C CB    . LYS E 1 86  ? 54.529  -26.335 71.781  1.00 29.12  ? 87  LYS E CB    1 
ATOM   5747  C CG    . LYS E 1 86  ? 53.474  -27.351 71.366  1.00 30.47  ? 87  LYS E CG    1 
ATOM   5748  C CD    . LYS E 1 86  ? 53.214  -28.437 72.403  1.00 29.56  ? 87  LYS E CD    1 
ATOM   5749  C CE    . LYS E 1 86  ? 52.981  -27.878 73.769  1.00 30.51  ? 87  LYS E CE    1 
ATOM   5750  N NZ    . LYS E 1 86  ? 52.600  -28.922 74.722  1.00 32.17  ? 87  LYS E NZ    1 
ATOM   5751  N N     . THR E 1 87  ? 53.867  -24.380 68.760  1.00 30.32  ? 88  THR E N     1 
ATOM   5752  C CA    . THR E 1 87  ? 52.957  -23.475 68.081  1.00 29.29  ? 88  THR E CA    1 
ATOM   5753  C C     . THR E 1 87  ? 51.804  -24.266 67.473  1.00 28.23  ? 88  THR E C     1 
ATOM   5754  O O     . THR E 1 87  ? 52.011  -25.318 66.874  1.00 30.46  ? 88  THR E O     1 
ATOM   5755  C CB    . THR E 1 87  ? 53.729  -22.701 67.012  1.00 28.25  ? 88  THR E CB    1 
ATOM   5756  O OG1   . THR E 1 87  ? 54.822  -22.096 67.695  1.00 31.83  ? 88  THR E OG1   1 
ATOM   5757  C CG2   . THR E 1 87  ? 52.878  -21.648 66.327  1.00 28.14  ? 88  THR E CG2   1 
ATOM   5758  N N     . VAL E 1 88  ? 50.588  -23.736 67.634  1.00 27.94  ? 89  VAL E N     1 
ATOM   5759  C CA    . VAL E 1 88  ? 49.411  -24.294 66.992  1.00 28.78  ? 89  VAL E CA    1 
ATOM   5760  C C     . VAL E 1 88  ? 48.763  -23.206 66.143  1.00 29.33  ? 89  VAL E C     1 
ATOM   5761  O O     . VAL E 1 88  ? 48.565  -22.085 66.604  1.00 32.96  ? 89  VAL E O     1 
ATOM   5762  C CB    . VAL E 1 88  ? 48.404  -24.873 68.004  1.00 28.75  ? 89  VAL E CB    1 
ATOM   5763  C CG1   . VAL E 1 88  ? 47.018  -25.036 67.390  1.00 30.86  ? 89  VAL E CG1   1 
ATOM   5764  C CG2   . VAL E 1 88  ? 48.889  -26.189 68.598  1.00 29.96  ? 89  VAL E CG2   1 
ATOM   5765  N N     . CYS E 1 89  ? 48.449  -23.556 64.893  1.00 33.49  ? 90  CYS E N     1 
ATOM   5766  C CA    . CYS E 1 89  ? 47.727  -22.669 63.999  1.00 33.63  ? 90  CYS E CA    1 
ATOM   5767  C C     . CYS E 1 89  ? 46.261  -23.092 63.962  1.00 35.23  ? 90  CYS E C     1 
ATOM   5768  O O     . CYS E 1 89  ? 45.950  -24.245 63.674  1.00 30.67  ? 90  CYS E O     1 
ATOM   5769  C CB    . CYS E 1 89  ? 48.347  -22.680 62.606  1.00 38.78  ? 90  CYS E CB    1 
ATOM   5770  S SG    . CYS E 1 89  ? 47.471  -21.634 61.414  1.00 49.17  ? 90  CYS E SG    1 
ATOM   5771  N N     . ALA E 1 90  ? 45.368  -22.150 64.279  1.00 34.45  ? 91  ALA E N     1 
ATOM   5772  C CA    . ALA E 1 90  ? 43.946  -22.442 64.353  1.00 33.80  ? 91  ALA E CA    1 
ATOM   5773  C C     . ALA E 1 90  ? 43.196  -21.665 63.276  1.00 36.54  ? 91  ALA E C     1 
ATOM   5774  O O     . ALA E 1 90  ? 42.906  -20.482 63.444  1.00 36.46  ? 91  ALA E O     1 
ATOM   5775  C CB    . ALA E 1 90  ? 43.426  -22.118 65.735  1.00 33.41  ? 91  ALA E CB    1 
ATOM   5776  N N     . LEU E 1 91  ? 42.888  -22.350 62.170  1.00 37.08  ? 92  LEU E N     1 
ATOM   5777  C CA    . LEU E 1 91  ? 42.121  -21.760 61.086  1.00 37.31  ? 92  LEU E CA    1 
ATOM   5778  C C     . LEU E 1 91  ? 40.717  -22.357 61.097  1.00 35.45  ? 92  LEU E C     1 
ATOM   5779  O O     . LEU E 1 91  ? 40.525  -23.492 61.526  1.00 40.20  ? 92  LEU E O     1 
ATOM   5780  C CB    . LEU E 1 91  ? 42.822  -22.005 59.751  1.00 37.35  ? 92  LEU E CB    1 
ATOM   5781  C CG    . LEU E 1 91  ? 44.299  -21.601 59.683  1.00 42.21  ? 92  LEU E CG    1 
ATOM   5782  C CD1   . LEU E 1 91  ? 44.807  -21.673 58.253  1.00 45.87  ? 92  LEU E CD1   1 
ATOM   5783  C CD2   . LEU E 1 91  ? 44.521  -20.214 60.263  1.00 42.56  ? 92  LEU E CD2   1 
ATOM   5784  N N     . TYR E 1 92  ? 39.742  -21.577 60.621  1.00 32.35  ? 93  TYR E N     1 
ATOM   5785  C CA    . TYR E 1 92  ? 38.357  -22.013 60.601  1.00 34.78  ? 93  TYR E CA    1 
ATOM   5786  C C     . TYR E 1 92  ? 38.200  -23.109 59.551  1.00 41.05  ? 93  TYR E C     1 
ATOM   5787  O O     . TYR E 1 92  ? 38.941  -23.149 58.571  1.00 45.50  ? 93  TYR E O     1 
ATOM   5788  C CB    . TYR E 1 92  ? 37.429  -20.823 60.339  1.00 31.46  ? 93  TYR E CB    1 
ATOM   5789  C CG    . TYR E 1 92  ? 37.458  -20.284 58.915  1.00 30.31  ? 93  TYR E CG    1 
ATOM   5790  C CD1   . TYR E 1 92  ? 38.405  -19.346 58.520  1.00 31.02  ? 93  TYR E CD1   1 
ATOM   5791  C CD2   . TYR E 1 92  ? 36.521  -20.693 57.975  1.00 32.49  ? 93  TYR E CD2   1 
ATOM   5792  C CE1   . TYR E 1 92  ? 38.429  -18.846 57.228  1.00 31.23  ? 93  TYR E CE1   1 
ATOM   5793  C CE2   . TYR E 1 92  ? 36.534  -20.202 56.680  1.00 30.48  ? 93  TYR E CE2   1 
ATOM   5794  C CZ    . TYR E 1 92  ? 37.490  -19.274 56.306  1.00 30.71  ? 93  TYR E CZ    1 
ATOM   5795  O OH    . TYR E 1 92  ? 37.505  -18.781 55.034  1.00 36.91  ? 93  TYR E OH    1 
ATOM   5796  N N     . GLY E 1 93  ? 37.229  -24.000 59.777  1.00 39.86  ? 94  GLY E N     1 
ATOM   5797  C CA    . GLY E 1 93  ? 36.978  -25.114 58.880  1.00 38.21  ? 94  GLY E CA    1 
ATOM   5798  C C     . GLY E 1 93  ? 38.146  -26.097 58.876  1.00 33.39  ? 94  GLY E C     1 
ATOM   5799  O O     . GLY E 1 93  ? 38.629  -26.499 59.932  1.00 33.38  ? 94  GLY E O     1 
ATOM   5800  N N     . HIS E 1 94  ? 38.585  -26.476 57.672  1.00 27.04  ? 95  HIS E N     1 
ATOM   5801  C CA    . HIS E 1 94  ? 39.704  -27.388 57.503  1.00 27.31  ? 95  HIS E CA    1 
ATOM   5802  C C     . HIS E 1 94  ? 40.939  -26.571 57.134  1.00 28.54  ? 95  HIS E C     1 
ATOM   5803  O O     . HIS E 1 94  ? 40.917  -25.802 56.175  1.00 30.90  ? 95  HIS E O     1 
ATOM   5804  C CB    . HIS E 1 94  ? 39.353  -28.470 56.473  1.00 26.62  ? 95  HIS E CB    1 
ATOM   5805  C CG    . HIS E 1 94  ? 40.381  -29.543 56.321  1.00 24.84  ? 95  HIS E CG    1 
ATOM   5806  N ND1   . HIS E 1 94  ? 41.737  -29.301 56.316  1.00 22.94  ? 95  HIS E ND1   1 
ATOM   5807  C CD2   . HIS E 1 94  ? 40.240  -30.865 56.134  1.00 21.76  ? 95  HIS E CD2   1 
ATOM   5808  C CE1   . HIS E 1 94  ? 42.384  -30.446 56.149  1.00 23.28  ? 95  HIS E CE1   1 
ATOM   5809  N NE2   . HIS E 1 94  ? 41.493  -31.409 56.039  1.00 22.35  ? 95  HIS E NE2   1 
ATOM   5810  N N     . PRO E 1 95  ? 42.053  -26.710 57.885  1.00 31.75  ? 96  PRO E N     1 
ATOM   5811  C CA    . PRO E 1 95  ? 43.197  -25.808 57.736  1.00 32.40  ? 96  PRO E CA    1 
ATOM   5812  C C     . PRO E 1 95  ? 43.904  -25.923 56.389  1.00 31.52  ? 96  PRO E C     1 
ATOM   5813  O O     . PRO E 1 95  ? 44.716  -25.069 56.039  1.00 33.57  ? 96  PRO E O     1 
ATOM   5814  C CB    . PRO E 1 95  ? 44.109  -26.222 58.909  1.00 31.03  ? 96  PRO E CB    1 
ATOM   5815  C CG    . PRO E 1 95  ? 43.768  -27.677 59.148  1.00 29.84  ? 96  PRO E CG    1 
ATOM   5816  C CD    . PRO E 1 95  ? 42.275  -27.762 58.889  1.00 31.47  ? 96  PRO E CD    1 
ATOM   5817  N N     . GLY E 1 96  ? 43.577  -26.978 55.635  1.00 28.59  ? 97  GLY E N     1 
ATOM   5818  C CA    . GLY E 1 96  ? 44.279  -27.279 54.399  1.00 29.97  ? 97  GLY E CA    1 
ATOM   5819  C C     . GLY E 1 96  ? 43.387  -27.115 53.171  1.00 29.41  ? 97  GLY E C     1 
ATOM   5820  O O     . GLY E 1 96  ? 43.860  -27.236 52.043  1.00 26.27  ? 97  GLY E O     1 
ATOM   5821  N N     . VAL E 1 97  ? 42.099  -26.833 53.398  1.00 32.52  ? 98  VAL E N     1 
ATOM   5822  C CA    . VAL E 1 97  ? 41.134  -26.735 52.313  1.00 34.57  ? 98  VAL E CA    1 
ATOM   5823  C C     . VAL E 1 97  ? 41.044  -25.281 51.856  1.00 37.42  ? 98  VAL E C     1 
ATOM   5824  O O     . VAL E 1 97  ? 40.621  -24.411 52.614  1.00 40.18  ? 98  VAL E O     1 
ATOM   5825  C CB    . VAL E 1 97  ? 39.756  -27.278 52.736  1.00 38.13  ? 98  VAL E CB    1 
ATOM   5826  C CG1   . VAL E 1 97  ? 38.690  -27.011 51.680  1.00 37.95  ? 98  VAL E CG1   1 
ATOM   5827  C CG2   . VAL E 1 97  ? 39.815  -28.763 53.075  1.00 36.14  ? 98  VAL E CG2   1 
ATOM   5828  N N     . PHE E 1 98  ? 41.443  -25.037 50.601  1.00 37.50  ? 99  PHE E N     1 
ATOM   5829  C CA    . PHE E 1 98  ? 41.457  -23.696 50.039  1.00 33.75  ? 99  PHE E CA    1 
ATOM   5830  C C     . PHE E 1 98  ? 42.149  -22.755 51.021  1.00 33.91  ? 99  PHE E C     1 
ATOM   5831  O O     . PHE E 1 98  ? 41.744  -21.606 51.183  1.00 33.71  ? 99  PHE E O     1 
ATOM   5832  C CB    . PHE E 1 98  ? 40.027  -23.259 49.702  1.00 35.48  ? 99  PHE E CB    1 
ATOM   5833  C CG    . PHE E 1 98  ? 39.447  -23.905 48.450  1.00 31.91  ? 99  PHE E CG    1 
ATOM   5834  C CD1   . PHE E 1 98  ? 38.948  -25.203 48.479  1.00 30.20  ? 99  PHE E CD1   1 
ATOM   5835  C CD2   . PHE E 1 98  ? 39.390  -23.206 47.248  1.00 32.47  ? 99  PHE E CD2   1 
ATOM   5836  C CE1   . PHE E 1 98  ? 38.422  -25.786 47.336  1.00 32.34  ? 99  PHE E CE1   1 
ATOM   5837  C CE2   . PHE E 1 98  ? 38.860  -23.793 46.110  1.00 33.24  ? 99  PHE E CE2   1 
ATOM   5838  C CZ    . PHE E 1 98  ? 38.377  -25.080 46.156  1.00 33.18  ? 99  PHE E CZ    1 
ATOM   5839  N N     . ALA E 1 99  ? 43.200  -23.269 51.669  1.00 36.48  ? 100 ALA E N     1 
ATOM   5840  C CA    . ALA E 1 99  ? 43.985  -22.501 52.621  1.00 36.76  ? 100 ALA E CA    1 
ATOM   5841  C C     . ALA E 1 99  ? 45.462  -22.846 52.451  1.00 38.84  ? 100 ALA E C     1 
ATOM   5842  O O     . ALA E 1 99  ? 45.895  -23.939 52.812  1.00 42.02  ? 100 ALA E O     1 
ATOM   5843  C CB    . ALA E 1 99  ? 43.506  -22.780 54.029  1.00 39.31  ? 100 ALA E CB    1 
ATOM   5844  N N     . CYS E 1 100 ? 46.224  -21.895 51.904  1.00 38.09  ? 101 CYS E N     1 
ATOM   5845  C CA    . CYS E 1 100 ? 47.616  -22.123 51.552  1.00 41.69  ? 101 CYS E CA    1 
ATOM   5846  C C     . CYS E 1 100 ? 48.519  -21.877 52.758  1.00 39.15  ? 101 CYS E C     1 
ATOM   5847  O O     . CYS E 1 100 ? 49.583  -22.481 52.874  1.00 38.58  ? 101 CYS E O     1 
ATOM   5848  C CB    . CYS E 1 100 ? 48.032  -21.226 50.392  1.00 43.36  ? 101 CYS E CB    1 
ATOM   5849  S SG    . CYS E 1 100 ? 47.875  -19.458 50.755  1.00 45.03  ? 101 CYS E SG    1 
ATOM   5850  N N     . VAL E 1 101 ? 48.079  -20.988 53.653  1.00 42.51  ? 102 VAL E N     1 
ATOM   5851  C CA    . VAL E 1 101 ? 48.893  -20.563 54.781  1.00 40.24  ? 102 VAL E CA    1 
ATOM   5852  C C     . VAL E 1 101 ? 49.458  -21.791 55.491  1.00 34.79  ? 102 VAL E C     1 
ATOM   5853  O O     . VAL E 1 101 ? 50.668  -21.900 55.678  1.00 33.04  ? 102 VAL E O     1 
ATOM   5854  C CB    . VAL E 1 101 ? 48.097  -19.674 55.754  1.00 45.90  ? 102 VAL E CB    1 
ATOM   5855  C CG1   . VAL E 1 101 ? 48.873  -19.401 57.038  1.00 50.55  ? 102 VAL E CG1   1 
ATOM   5856  C CG2   . VAL E 1 101 ? 47.665  -18.367 55.100  1.00 49.02  ? 102 VAL E CG2   1 
ATOM   5857  N N     . SER E 1 102 ? 48.569  -22.709 55.882  1.00 31.26  ? 103 SER E N     1 
ATOM   5858  C CA    . SER E 1 102 ? 48.957  -23.869 56.668  1.00 38.48  ? 103 SER E CA    1 
ATOM   5859  C C     . SER E 1 102 ? 49.939  -24.737 55.885  1.00 38.22  ? 103 SER E C     1 
ATOM   5860  O O     . SER E 1 102 ? 50.993  -25.100 56.401  1.00 43.48  ? 103 SER E O     1 
ATOM   5861  C CB    . SER E 1 102 ? 47.750  -24.660 57.102  1.00 42.81  ? 103 SER E CB    1 
ATOM   5862  O OG    . SER E 1 102 ? 46.941  -23.902 57.991  1.00 42.50  ? 103 SER E OG    1 
ATOM   5863  N N     . HIS E 1 103 ? 49.580  -25.067 54.639  1.00 40.50  ? 104 HIS E N     1 
ATOM   5864  C CA    . HIS E 1 103 ? 50.430  -25.886 53.789  1.00 34.20  ? 104 HIS E CA    1 
ATOM   5865  C C     . HIS E 1 103 ? 51.807  -25.239 53.666  1.00 31.32  ? 104 HIS E C     1 
ATOM   5866  O O     . HIS E 1 103 ? 52.827  -25.922 53.733  1.00 26.73  ? 104 HIS E O     1 
ATOM   5867  C CB    . HIS E 1 103 ? 49.795  -26.097 52.409  1.00 34.91  ? 104 HIS E CB    1 
ATOM   5868  C CG    . HIS E 1 103 ? 48.568  -26.949 52.417  1.00 35.29  ? 104 HIS E CG    1 
ATOM   5869  N ND1   . HIS E 1 103 ? 48.616  -28.320 52.556  1.00 32.38  ? 104 HIS E ND1   1 
ATOM   5870  C CD2   . HIS E 1 103 ? 47.271  -26.633 52.318  1.00 34.49  ? 104 HIS E CD2   1 
ATOM   5871  C CE1   . HIS E 1 103 ? 47.383  -28.804 52.532  1.00 30.96  ? 104 HIS E CE1   1 
ATOM   5872  N NE2   . HIS E 1 103 ? 46.551  -27.798 52.386  1.00 33.03  ? 104 HIS E NE2   1 
ATOM   5873  N N     . MET E 1 104 ? 51.820  -23.915 53.477  1.00 29.91  ? 105 MET E N     1 
ATOM   5874  C CA    . MET E 1 104 ? 53.057  -23.175 53.283  1.00 29.19  ? 105 MET E CA    1 
ATOM   5875  C C     . MET E 1 104 ? 53.878  -23.189 54.570  1.00 27.36  ? 105 MET E C     1 
ATOM   5876  O O     . MET E 1 104 ? 55.097  -23.333 54.531  1.00 25.93  ? 105 MET E O     1 
ATOM   5877  C CB    . MET E 1 104 ? 52.776  -21.727 52.870  1.00 32.85  ? 105 MET E CB    1 
ATOM   5878  C CG    . MET E 1 104 ? 52.275  -21.578 51.449  1.00 37.70  ? 105 MET E CG    1 
ATOM   5879  S SD    . MET E 1 104 ? 51.789  -19.885 51.057  1.00 45.56  ? 105 MET E SD    1 
ATOM   5880  C CE    . MET E 1 104 ? 53.350  -19.009 51.221  1.00 49.52  ? 105 MET E CE    1 
ATOM   5881  N N     . ALA E 1 105 ? 53.194  -23.029 55.707  1.00 24.33  ? 106 ALA E N     1 
ATOM   5882  C CA    . ALA E 1 105 ? 53.855  -23.004 57.001  1.00 24.81  ? 106 ALA E CA    1 
ATOM   5883  C C     . ALA E 1 105 ? 54.509  -24.355 57.274  1.00 27.38  ? 106 ALA E C     1 
ATOM   5884  O O     . ALA E 1 105 ? 55.684  -24.419 57.630  1.00 26.61  ? 106 ALA E O     1 
ATOM   5885  C CB    . ALA E 1 105 ? 52.861  -22.640 58.084  1.00 26.12  ? 106 ALA E CB    1 
ATOM   5886  N N     . ILE E 1 106 ? 53.732  -25.430 57.093  1.00 27.92  ? 107 ILE E N     1 
ATOM   5887  C CA    . ILE E 1 106 ? 54.204  -26.778 57.363  1.00 29.21  ? 107 ILE E CA    1 
ATOM   5888  C C     . ILE E 1 106 ? 55.393  -27.086 56.456  1.00 28.67  ? 107 ILE E C     1 
ATOM   5889  O O     . ILE E 1 106 ? 56.402  -27.618 56.912  1.00 30.54  ? 107 ILE E O     1 
ATOM   5890  C CB    . ILE E 1 106 ? 53.072  -27.807 57.186  1.00 29.54  ? 107 ILE E CB    1 
ATOM   5891  C CG1   . ILE E 1 106 ? 51.986  -27.635 58.247  1.00 29.98  ? 107 ILE E CG1   1 
ATOM   5892  C CG2   . ILE E 1 106 ? 53.627  -29.231 57.176  1.00 30.63  ? 107 ILE E CG2   1 
ATOM   5893  C CD1   . ILE E 1 106 ? 50.885  -28.677 58.179  1.00 29.95  ? 107 ILE E CD1   1 
ATOM   5894  N N     . THR E 1 107 ? 55.255  -26.753 55.169  1.00 28.92  ? 108 THR E N     1 
ATOM   5895  C CA    . THR E 1 107 ? 56.309  -26.990 54.197  1.00 29.66  ? 108 THR E CA    1 
ATOM   5896  C C     . THR E 1 107 ? 57.600  -26.345 54.692  1.00 32.18  ? 108 THR E C     1 
ATOM   5897  O O     . THR E 1 107 ? 58.640  -26.997 54.762  1.00 33.68  ? 108 THR E O     1 
ATOM   5898  C CB    . THR E 1 107 ? 55.892  -26.435 52.835  1.00 30.46  ? 108 THR E CB    1 
ATOM   5899  O OG1   . THR E 1 107 ? 54.769  -27.209 52.423  1.00 30.71  ? 108 THR E OG1   1 
ATOM   5900  C CG2   . THR E 1 107 ? 56.995  -26.546 51.797  1.00 32.20  ? 108 THR E CG2   1 
ATOM   5901  N N     . ARG E 1 108 ? 57.513  -25.058 55.043  1.00 31.64  ? 109 ARG E N     1 
ATOM   5902  C CA    . ARG E 1 108 ? 58.683  -24.269 55.387  1.00 31.96  ? 109 ARG E CA    1 
ATOM   5903  C C     . ARG E 1 108 ? 59.275  -24.767 56.704  1.00 33.25  ? 109 ARG E C     1 
ATOM   5904  O O     . ARG E 1 108 ? 60.493  -24.783 56.872  1.00 34.82  ? 109 ARG E O     1 
ATOM   5905  C CB    . ARG E 1 108 ? 58.302  -22.786 55.457  1.00 33.81  ? 109 ARG E CB    1 
ATOM   5906  C CG    . ARG E 1 108 ? 59.490  -21.840 55.552  1.00 36.38  ? 109 ARG E CG    1 
ATOM   5907  C CD    . ARG E 1 108 ? 59.072  -20.382 55.447  1.00 38.24  ? 109 ARG E CD    1 
ATOM   5908  N NE    . ARG E 1 108 ? 58.358  -20.101 54.197  1.00 40.43  ? 109 ARG E NE    1 
ATOM   5909  C CZ    . ARG E 1 108 ? 57.929  -18.901 53.826  1.00 42.83  ? 109 ARG E CZ    1 
ATOM   5910  N NH1   . ARG E 1 108 ? 58.156  -17.852 54.596  1.00 43.82  ? 109 ARG E NH1   1 
ATOM   5911  N NH2   . ARG E 1 108 ? 57.281  -18.753 52.683  1.00 41.42  ? 109 ARG E NH2   1 
ATOM   5912  N N     . ALA E 1 109 ? 58.402  -25.176 57.629  1.00 31.44  ? 110 ALA E N     1 
ATOM   5913  C CA    . ALA E 1 109 ? 58.831  -25.637 58.939  1.00 30.46  ? 110 ALA E CA    1 
ATOM   5914  C C     . ALA E 1 109 ? 59.665  -26.908 58.795  1.00 32.62  ? 110 ALA E C     1 
ATOM   5915  O O     . ALA E 1 109 ? 60.685  -27.065 59.461  1.00 30.80  ? 110 ALA E O     1 
ATOM   5916  C CB    . ALA E 1 109 ? 57.629  -25.860 59.829  1.00 32.40  ? 110 ALA E CB    1 
ATOM   5917  N N     . LYS E 1 110 ? 59.212  -27.809 57.917  1.00 36.49  ? 111 LYS E N     1 
ATOM   5918  C CA    . LYS E 1 110 ? 59.906  -29.062 57.667  1.00 39.56  ? 111 LYS E CA    1 
ATOM   5919  C C     . LYS E 1 110 ? 61.281  -28.775 57.070  1.00 40.31  ? 111 LYS E C     1 
ATOM   5920  O O     . LYS E 1 110 ? 62.274  -29.378 57.469  1.00 39.80  ? 111 LYS E O     1 
ATOM   5921  C CB    . LYS E 1 110 ? 59.093  -29.954 56.721  1.00 40.35  ? 111 LYS E CB    1 
ATOM   5922  C CG    . LYS E 1 110 ? 57.837  -30.569 57.319  1.00 43.24  ? 111 LYS E CG    1 
ATOM   5923  C CD    . LYS E 1 110 ? 57.034  -31.402 56.326  1.00 45.38  ? 111 LYS E CD    1 
ATOM   5924  C CE    . LYS E 1 110 ? 55.913  -32.151 56.973  1.00 50.75  ? 111 LYS E CE    1 
ATOM   5925  N NZ    . LYS E 1 110 ? 56.407  -33.126 57.949  1.00 54.22  ? 111 LYS E NZ    1 
ATOM   5926  N N     . ALA E 1 111 ? 61.318  -27.849 56.106  1.00 42.00  ? 112 ALA E N     1 
ATOM   5927  C CA    . ALA E 1 111 ? 62.543  -27.523 55.395  1.00 39.95  ? 112 ALA E CA    1 
ATOM   5928  C C     . ALA E 1 111 ? 63.601  -27.024 56.375  1.00 40.02  ? 112 ALA E C     1 
ATOM   5929  O O     . ALA E 1 111 ? 64.796  -27.189 56.139  1.00 50.31  ? 112 ALA E O     1 
ATOM   5930  C CB    . ALA E 1 111 ? 62.256  -26.498 54.320  1.00 36.78  ? 112 ALA E CB    1 
ATOM   5931  N N     . GLU E 1 112 ? 63.148  -26.417 57.477  1.00 37.64  ? 113 GLU E N     1 
ATOM   5932  C CA    . GLU E 1 112 ? 64.049  -25.856 58.469  1.00 38.25  ? 113 GLU E CA    1 
ATOM   5933  C C     . GLU E 1 112 ? 64.266  -26.868 59.591  1.00 36.89  ? 113 GLU E C     1 
ATOM   5934  O O     . GLU E 1 112 ? 64.913  -26.564 60.591  1.00 33.21  ? 113 GLU E O     1 
ATOM   5935  C CB    . GLU E 1 112 ? 63.504  -24.526 58.991  1.00 43.75  ? 113 GLU E CB    1 
ATOM   5936  C CG    . GLU E 1 112 ? 63.366  -23.469 57.898  1.00 43.80  ? 113 GLU E CG    1 
ATOM   5937  C CD    . GLU E 1 112 ? 62.979  -22.090 58.400  1.00 45.56  ? 113 GLU E CD    1 
ATOM   5938  O OE1   . GLU E 1 112 ? 62.820  -21.929 59.629  1.00 45.39  ? 113 GLU E OE1   1 
ATOM   5939  O OE2   . GLU E 1 112 ? 62.840  -21.176 57.560  1.00 46.43  ? 113 GLU E OE2   1 
ATOM   5940  N N     . GLY E 1 113 ? 63.709  -28.071 59.412  1.00 35.07  ? 114 GLY E N     1 
ATOM   5941  C CA    . GLY E 1 113 ? 63.979  -29.190 60.299  1.00 34.86  ? 114 GLY E CA    1 
ATOM   5942  C C     . GLY E 1 113 ? 63.151  -29.119 61.580  1.00 36.23  ? 114 GLY E C     1 
ATOM   5943  O O     . GLY E 1 113 ? 63.597  -29.569 62.633  1.00 34.62  ? 114 GLY E O     1 
ATOM   5944  N N     . PHE E 1 114 ? 61.941  -28.562 61.474  1.00 39.20  ? 115 PHE E N     1 
ATOM   5945  C CA    . PHE E 1 114 ? 61.025  -28.508 62.601  1.00 37.33  ? 115 PHE E CA    1 
ATOM   5946  C C     . PHE E 1 114 ? 59.905  -29.519 62.385  1.00 37.74  ? 115 PHE E C     1 
ATOM   5947  O O     . PHE E 1 114 ? 59.504  -29.777 61.251  1.00 39.70  ? 115 PHE E O     1 
ATOM   5948  C CB    . PHE E 1 114 ? 60.432  -27.109 62.796  1.00 34.96  ? 115 PHE E CB    1 
ATOM   5949  C CG    . PHE E 1 114 ? 61.443  -26.035 63.168  1.00 38.43  ? 115 PHE E CG    1 
ATOM   5950  C CD1   . PHE E 1 114 ? 62.045  -26.028 64.421  1.00 37.84  ? 115 PHE E CD1   1 
ATOM   5951  C CD2   . PHE E 1 114 ? 61.757  -25.011 62.281  1.00 36.44  ? 115 PHE E CD2   1 
ATOM   5952  C CE1   . PHE E 1 114 ? 62.960  -25.045 64.761  1.00 37.78  ? 115 PHE E CE1   1 
ATOM   5953  C CE2   . PHE E 1 114 ? 62.669  -24.028 62.630  1.00 35.96  ? 115 PHE E CE2   1 
ATOM   5954  C CZ    . PHE E 1 114 ? 63.268  -24.046 63.867  1.00 35.81  ? 115 PHE E CZ    1 
ATOM   5955  N N     . SER E 1 115 ? 59.409  -30.082 63.491  1.00 35.38  ? 116 SER E N     1 
ATOM   5956  C CA    . SER E 1 115 ? 58.245  -30.948 63.457  1.00 36.95  ? 116 SER E CA    1 
ATOM   5957  C C     . SER E 1 115 ? 57.013  -30.118 63.111  1.00 34.61  ? 116 SER E C     1 
ATOM   5958  O O     . SER E 1 115 ? 56.743  -29.105 63.752  1.00 32.47  ? 116 SER E O     1 
ATOM   5959  C CB    . SER E 1 115 ? 58.065  -31.675 64.765  1.00 35.70  ? 116 SER E CB    1 
ATOM   5960  O OG    . SER E 1 115 ? 56.898  -32.485 64.738  1.00 35.13  ? 116 SER E OG    1 
ATOM   5961  N N     . ALA E 1 116 ? 56.285  -30.551 62.078  1.00 29.48  ? 117 ALA E N     1 
ATOM   5962  C CA    . ALA E 1 116 ? 55.097  -29.848 61.627  1.00 28.19  ? 117 ALA E CA    1 
ATOM   5963  C C     . ALA E 1 116 ? 54.123  -30.841 61.002  1.00 29.88  ? 117 ALA E C     1 
ATOM   5964  O O     . ALA E 1 116 ? 54.521  -31.698 60.217  1.00 28.21  ? 117 ALA E O     1 
ATOM   5965  C CB    . ALA E 1 116 ? 55.481  -28.760 60.649  1.00 31.01  ? 117 ALA E CB    1 
ATOM   5966  N N     . LYS E 1 117 ? 52.843  -30.715 61.364  1.00 29.54  ? 118 LYS E N     1 
ATOM   5967  C CA    . LYS E 1 117 ? 51.810  -31.581 60.825  1.00 29.80  ? 118 LYS E CA    1 
ATOM   5968  C C     . LYS E 1 117 ? 50.490  -30.821 60.770  1.00 29.22  ? 118 LYS E C     1 
ATOM   5969  O O     . LYS E 1 117 ? 50.363  -29.735 61.330  1.00 28.21  ? 118 LYS E O     1 
ATOM   5970  C CB    . LYS E 1 117 ? 51.666  -32.855 61.664  1.00 34.75  ? 118 LYS E CB    1 
ATOM   5971  C CG    . LYS E 1 117 ? 51.216  -32.637 63.102  1.00 37.93  ? 118 LYS E CG    1 
ATOM   5972  C CD    . LYS E 1 117 ? 50.985  -33.931 63.872  1.00 39.64  ? 118 LYS E CD    1 
ATOM   5973  C CE    . LYS E 1 117 ? 50.566  -33.694 65.287  1.00 40.45  ? 118 LYS E CE    1 
ATOM   5974  N NZ    . LYS E 1 117 ? 50.302  -34.952 65.990  1.00 41.89  ? 118 LYS E NZ    1 
ATOM   5975  N N     . MET E 1 118 ? 49.513  -31.416 60.083  1.00 32.22  ? 119 MET E N     1 
ATOM   5976  C CA    . MET E 1 118 ? 48.200  -30.819 59.932  1.00 29.06  ? 119 MET E CA    1 
ATOM   5977  C C     . MET E 1 118 ? 47.142  -31.817 60.391  1.00 27.63  ? 119 MET E C     1 
ATOM   5978  O O     . MET E 1 118 ? 47.155  -32.976 59.982  1.00 26.80  ? 119 MET E O     1 
ATOM   5979  C CB    . MET E 1 118 ? 47.948  -30.428 58.472  1.00 29.01  ? 119 MET E CB    1 
ATOM   5980  C CG    . MET E 1 118 ? 46.530  -29.973 58.188  1.00 33.05  ? 119 MET E CG    1 
ATOM   5981  S SD    . MET E 1 118 ? 46.273  -29.564 56.450  1.00 35.53  ? 119 MET E SD    1 
ATOM   5982  C CE    . MET E 1 118 ? 47.539  -28.311 56.214  1.00 34.23  ? 119 MET E CE    1 
ATOM   5983  N N     . GLU E 1 119 ? 46.242  -31.353 61.262  1.00 29.42  ? 120 GLU E N     1 
ATOM   5984  C CA    . GLU E 1 119 ? 45.110  -32.151 61.697  1.00 27.12  ? 120 GLU E CA    1 
ATOM   5985  C C     . GLU E 1 119 ? 43.890  -31.753 60.875  1.00 23.63  ? 120 GLU E C     1 
ATOM   5986  O O     . GLU E 1 119 ? 43.585  -30.569 60.746  1.00 21.16  ? 120 GLU E O     1 
ATOM   5987  C CB    . GLU E 1 119 ? 44.845  -31.964 63.192  1.00 27.50  ? 120 GLU E CB    1 
ATOM   5988  C CG    . GLU E 1 119 ? 45.903  -32.607 64.084  1.00 31.42  ? 120 GLU E CG    1 
ATOM   5989  C CD    . GLU E 1 119 ? 45.929  -34.124 64.021  1.00 33.39  ? 120 GLU E CD    1 
ATOM   5990  O OE1   . GLU E 1 119 ? 45.118  -34.698 63.265  1.00 43.27  ? 120 GLU E OE1   1 
ATOM   5991  O OE2   . GLU E 1 119 ? 46.754  -34.732 64.733  1.00 36.87  ? 120 GLU E OE2   1 
ATOM   5992  N N     . PRO E 1 120 ? 43.167  -32.728 60.283  1.00 20.22  ? 121 PRO E N     1 
ATOM   5993  C CA    . PRO E 1 120 ? 41.993  -32.423 59.466  1.00 22.36  ? 121 PRO E CA    1 
ATOM   5994  C C     . PRO E 1 120 ? 40.872  -31.796 60.291  1.00 24.33  ? 121 PRO E C     1 
ATOM   5995  O O     . PRO E 1 120 ? 40.760  -32.045 61.489  1.00 26.48  ? 121 PRO E O     1 
ATOM   5996  C CB    . PRO E 1 120 ? 41.598  -33.794 58.877  1.00 20.62  ? 121 PRO E CB    1 
ATOM   5997  C CG    . PRO E 1 120 ? 42.156  -34.798 59.867  1.00 21.28  ? 121 PRO E CG    1 
ATOM   5998  C CD    . PRO E 1 120 ? 43.442  -34.170 60.378  1.00 20.78  ? 121 PRO E CD    1 
ATOM   5999  N N     . GLY E 1 121 ? 40.052  -30.977 59.627  1.00 23.80  ? 122 GLY E N     1 
ATOM   6000  C CA    . GLY E 1 121 ? 38.905  -30.346 60.257  1.00 26.52  ? 122 GLY E CA    1 
ATOM   6001  C C     . GLY E 1 121 ? 37.678  -30.428 59.353  1.00 27.50  ? 122 GLY E C     1 
ATOM   6002  O O     . GLY E 1 121 ? 37.744  -30.990 58.263  1.00 27.91  ? 122 GLY E O     1 
ATOM   6003  N N     . ILE E 1 122 ? 36.561  -29.863 59.823  1.00 29.90  ? 123 ILE E N     1 
ATOM   6004  C CA    . ILE E 1 122 ? 35.317  -29.883 59.073  1.00 28.91  ? 123 ILE E CA    1 
ATOM   6005  C C     . ILE E 1 122 ? 35.248  -28.629 58.207  1.00 30.82  ? 123 ILE E C     1 
ATOM   6006  O O     . ILE E 1 122 ? 35.198  -27.515 58.725  1.00 30.52  ? 123 ILE E O     1 
ATOM   6007  C CB    . ILE E 1 122 ? 34.109  -29.996 60.021  1.00 30.37  ? 123 ILE E CB    1 
ATOM   6008  C CG1   . ILE E 1 122 ? 34.203  -31.244 60.899  1.00 32.37  ? 123 ILE E CG1   1 
ATOM   6009  C CG2   . ILE E 1 122 ? 32.796  -29.954 59.239  1.00 31.78  ? 123 ILE E CG2   1 
ATOM   6010  C CD1   . ILE E 1 122 ? 33.104  -31.354 61.941  1.00 32.81  ? 123 ILE E CD1   1 
ATOM   6011  N N     . SER E 1 123 ? 35.240  -28.830 56.884  1.00 26.10  ? 124 SER E N     1 
ATOM   6012  C CA    . SER E 1 123 ? 35.265  -27.730 55.933  1.00 27.52  ? 124 SER E CA    1 
ATOM   6013  C C     . SER E 1 123 ? 33.842  -27.282 55.610  1.00 25.28  ? 124 SER E C     1 
ATOM   6014  O O     . SER E 1 123 ? 32.876  -27.900 56.051  1.00 24.56  ? 124 SER E O     1 
ATOM   6015  C CB    . SER E 1 123 ? 36.007  -28.114 54.677  1.00 28.87  ? 124 SER E CB    1 
ATOM   6016  O OG    . SER E 1 123 ? 35.298  -29.109 53.952  1.00 31.68  ? 124 SER E OG    1 
ATOM   6017  N N     . ALA E 1 124 ? 33.736  -26.205 54.824  1.00 26.61  ? 125 ALA E N     1 
ATOM   6018  C CA    . ALA E 1 124 ? 32.451  -25.675 54.400  1.00 26.02  ? 125 ALA E CA    1 
ATOM   6019  C C     . ALA E 1 124 ? 31.780  -26.659 53.446  1.00 25.84  ? 125 ALA E C     1 
ATOM   6020  O O     . ALA E 1 124 ? 30.560  -26.660 53.298  1.00 25.89  ? 125 ALA E O     1 
ATOM   6021  C CB    . ALA E 1 124 ? 32.641  -24.321 53.754  1.00 28.38  ? 125 ALA E CB    1 
ATOM   6022  N N     . GLU E 1 125 ? 32.603  -27.485 52.795  1.00 25.43  ? 126 GLU E N     1 
ATOM   6023  C CA    . GLU E 1 125 ? 32.121  -28.514 51.891  1.00 29.05  ? 126 GLU E CA    1 
ATOM   6024  C C     . GLU E 1 125 ? 31.427  -29.604 52.700  1.00 27.97  ? 126 GLU E C     1 
ATOM   6025  O O     . GLU E 1 125 ? 30.350  -30.068 52.333  1.00 34.17  ? 126 GLU E O     1 
ATOM   6026  C CB    . GLU E 1 125 ? 33.297  -29.084 51.098  1.00 34.67  ? 126 GLU E CB    1 
ATOM   6027  C CG    . GLU E 1 125 ? 32.914  -30.246 50.188  1.00 37.35  ? 126 GLU E CG    1 
ATOM   6028  C CD    . GLU E 1 125 ? 34.108  -30.980 49.603  1.00 43.26  ? 126 GLU E CD    1 
ATOM   6029  O OE1   . GLU E 1 125 ? 34.897  -30.343 48.873  1.00 43.45  ? 126 GLU E OE1   1 
ATOM   6030  O OE2   . GLU E 1 125 ? 34.252  -32.188 49.888  1.00 43.78  ? 126 GLU E OE2   1 
ATOM   6031  N N     . ALA E 1 126 ? 32.065  -30.000 53.806  1.00 30.47  ? 127 ALA E N     1 
ATOM   6032  C CA    . ALA E 1 126 ? 31.533  -31.025 54.687  1.00 27.62  ? 127 ALA E CA    1 
ATOM   6033  C C     . ALA E 1 126 ? 30.174  -30.585 55.229  1.00 26.44  ? 127 ALA E C     1 
ATOM   6034  O O     . ALA E 1 126 ? 29.252  -31.390 55.335  1.00 23.77  ? 127 ALA E O     1 
ATOM   6035  C CB    . ALA E 1 126 ? 32.515  -31.298 55.805  1.00 25.94  ? 127 ALA E CB    1 
ATOM   6036  N N     . CYS E 1 127 ? 30.070  -29.295 55.566  1.00 24.08  ? 128 CYS E N     1 
ATOM   6037  C CA    . CYS E 1 127 ? 28.844  -28.730 56.106  1.00 22.12  ? 128 CYS E CA    1 
ATOM   6038  C C     . CYS E 1 127 ? 27.756  -28.735 55.037  1.00 23.88  ? 128 CYS E C     1 
ATOM   6039  O O     . CYS E 1 127 ? 26.589  -28.975 55.334  1.00 27.66  ? 128 CYS E O     1 
ATOM   6040  C CB    . CYS E 1 127 ? 29.070  -27.309 56.609  1.00 22.95  ? 128 CYS E CB    1 
ATOM   6041  S SG    . CYS E 1 127 ? 30.226  -27.205 58.000  1.00 23.19  ? 128 CYS E SG    1 
ATOM   6042  N N     . LEU E 1 128 ? 28.161  -28.468 53.791  1.00 27.67  ? 129 LEU E N     1 
ATOM   6043  C CA    . LEU E 1 128 ? 27.229  -28.347 52.683  1.00 27.72  ? 129 LEU E CA    1 
ATOM   6044  C C     . LEU E 1 128 ? 26.476  -29.663 52.495  1.00 26.83  ? 129 LEU E C     1 
ATOM   6045  O O     . LEU E 1 128 ? 25.247  -29.681 52.479  1.00 27.92  ? 129 LEU E O     1 
ATOM   6046  C CB    . LEU E 1 128 ? 27.999  -27.944 51.426  1.00 28.19  ? 129 LEU E CB    1 
ATOM   6047  C CG    . LEU E 1 128 ? 27.158  -27.692 50.171  1.00 29.99  ? 129 LEU E CG    1 
ATOM   6048  C CD1   . LEU E 1 128 ? 28.016  -27.117 49.058  1.00 34.67  ? 129 LEU E CD1   1 
ATOM   6049  C CD2   . LEU E 1 128 ? 26.468  -28.963 49.707  1.00 34.83  ? 129 LEU E CD2   1 
ATOM   6050  N N     . TRP E 1 129 ? 27.228  -30.759 52.359  1.00 25.54  ? 130 TRP E N     1 
ATOM   6051  C CA    . TRP E 1 129 ? 26.649  -32.069 52.108  1.00 24.37  ? 130 TRP E CA    1 
ATOM   6052  C C     . TRP E 1 129 ? 25.538  -32.359 53.114  1.00 26.61  ? 130 TRP E C     1 
ATOM   6053  O O     . TRP E 1 129 ? 24.497  -32.902 52.752  1.00 23.02  ? 130 TRP E O     1 
ATOM   6054  C CB    . TRP E 1 129 ? 27.733  -33.154 52.169  1.00 24.00  ? 130 TRP E CB    1 
ATOM   6055  C CG    . TRP E 1 129 ? 28.857  -32.959 51.186  1.00 23.20  ? 130 TRP E CG    1 
ATOM   6056  C CD1   . TRP E 1 129 ? 30.186  -33.151 51.420  1.00 23.88  ? 130 TRP E CD1   1 
ATOM   6057  C CD2   . TRP E 1 129 ? 28.747  -32.555 49.803  1.00 23.42  ? 130 TRP E CD2   1 
ATOM   6058  N NE1   . TRP E 1 129 ? 30.913  -32.877 50.292  1.00 24.79  ? 130 TRP E NE1   1 
ATOM   6059  C CE2   . TRP E 1 129 ? 30.059  -32.516 49.283  1.00 25.70  ? 130 TRP E CE2   1 
ATOM   6060  C CE3   . TRP E 1 129 ? 27.680  -32.222 48.962  1.00 22.70  ? 130 TRP E CE3   1 
ATOM   6061  C CZ2   . TRP E 1 129 ? 30.325  -32.158 47.964  1.00 23.56  ? 130 TRP E CZ2   1 
ATOM   6062  C CZ3   . TRP E 1 129 ? 27.945  -31.872 47.656  1.00 23.48  ? 130 TRP E CZ3   1 
ATOM   6063  C CH2   . TRP E 1 129 ? 29.250  -31.842 47.167  1.00 22.18  ? 130 TRP E CH2   1 
ATOM   6064  N N     . ALA E 1 130 ? 25.776  -31.992 54.380  1.00 28.73  ? 131 ALA E N     1 
ATOM   6065  C CA    . ALA E 1 130 ? 24.865  -32.321 55.465  1.00 27.31  ? 131 ALA E CA    1 
ATOM   6066  C C     . ALA E 1 130 ? 23.661  -31.380 55.457  1.00 28.67  ? 131 ALA E C     1 
ATOM   6067  O O     . ALA E 1 130 ? 22.540  -31.806 55.721  1.00 27.91  ? 131 ALA E O     1 
ATOM   6068  C CB    . ALA E 1 130 ? 25.601  -32.265 56.786  1.00 27.73  ? 131 ALA E CB    1 
ATOM   6069  N N     . ASP E 1 131 ? 23.909  -30.101 55.153  1.00 29.94  ? 132 ASP E N     1 
ATOM   6070  C CA    . ASP E 1 131 ? 22.882  -29.073 55.228  1.00 27.22  ? 132 ASP E CA    1 
ATOM   6071  C C     . ASP E 1 131 ? 21.936  -29.186 54.035  1.00 29.80  ? 132 ASP E C     1 
ATOM   6072  O O     . ASP E 1 131 ? 20.761  -28.840 54.138  1.00 33.25  ? 132 ASP E O     1 
ATOM   6073  C CB    . ASP E 1 131 ? 23.494  -27.684 55.329  1.00 26.69  ? 132 ASP E CB    1 
ATOM   6074  C CG    . ASP E 1 131 ? 24.170  -27.363 56.655  1.00 31.00  ? 132 ASP E CG    1 
ATOM   6075  O OD1   . ASP E 1 131 ? 24.092  -28.207 57.571  1.00 41.32  ? 132 ASP E OD1   1 
ATOM   6076  O OD2   . ASP E 1 131 ? 24.771  -26.274 56.759  1.00 33.78  ? 132 ASP E OD2   1 
ATOM   6077  N N     . LEU E 1 132 ? 22.457  -29.653 52.897  1.00 29.40  ? 133 LEU E N     1 
ATOM   6078  C CA    . LEU E 1 132 ? 21.645  -29.804 51.701  1.00 32.16  ? 133 LEU E CA    1 
ATOM   6079  C C     . LEU E 1 132 ? 21.224  -31.263 51.550  1.00 32.20  ? 133 LEU E C     1 
ATOM   6080  O O     . LEU E 1 132 ? 20.380  -31.585 50.718  1.00 32.75  ? 133 LEU E O     1 
ATOM   6081  C CB    . LEU E 1 132 ? 22.403  -29.311 50.469  1.00 33.42  ? 133 LEU E CB    1 
ATOM   6082  C CG    . LEU E 1 132 ? 22.592  -27.795 50.362  1.00 36.82  ? 133 LEU E CG    1 
ATOM   6083  C CD1   . LEU E 1 132 ? 23.548  -27.283 51.426  1.00 42.75  ? 133 LEU E CD1   1 
ATOM   6084  C CD2   . LEU E 1 132 ? 23.071  -27.411 48.974  1.00 37.07  ? 133 LEU E CD2   1 
ATOM   6085  N N     . GLY E 1 133 ? 21.815  -32.134 52.373  1.00 31.96  ? 134 GLY E N     1 
ATOM   6086  C CA    . GLY E 1 133 ? 21.543  -33.559 52.300  1.00 35.13  ? 134 GLY E CA    1 
ATOM   6087  C C     . GLY E 1 133 ? 21.935  -34.119 50.936  1.00 35.29  ? 134 GLY E C     1 
ATOM   6088  O O     . GLY E 1 133 ? 21.146  -34.806 50.289  1.00 39.92  ? 134 GLY E O     1 
ATOM   6089  N N     . ILE E 1 134 ? 23.162  -33.803 50.509  1.00 33.75  ? 135 ILE E N     1 
ATOM   6090  C CA    . ILE E 1 134 ? 23.683  -34.268 49.235  1.00 32.88  ? 135 ILE E CA    1 
ATOM   6091  C C     . ILE E 1 134 ? 24.938  -35.096 49.491  1.00 31.16  ? 135 ILE E C     1 
ATOM   6092  O O     . ILE E 1 134 ? 25.827  -34.673 50.228  1.00 33.46  ? 135 ILE E O     1 
ATOM   6093  C CB    . ILE E 1 134 ? 23.970  -33.087 48.290  1.00 32.81  ? 135 ILE E CB    1 
ATOM   6094  C CG1   . ILE E 1 134 ? 22.720  -32.243 48.041  1.00 34.81  ? 135 ILE E CG1   1 
ATOM   6095  C CG2   . ILE E 1 134 ? 24.592  -33.575 46.980  1.00 33.27  ? 135 ILE E CG2   1 
ATOM   6096  C CD1   . ILE E 1 134 ? 22.952  -31.046 47.137  1.00 40.01  ? 135 ILE E CD1   1 
ATOM   6097  N N     . ASP E 1 135 ? 24.994  -36.276 48.868  1.00 28.41  ? 136 ASP E N     1 
ATOM   6098  C CA    . ASP E 1 135 ? 26.162  -37.136 48.946  1.00 30.48  ? 136 ASP E CA    1 
ATOM   6099  C C     . ASP E 1 135 ? 27.029  -36.894 47.713  1.00 30.75  ? 136 ASP E C     1 
ATOM   6100  O O     . ASP E 1 135 ? 26.571  -37.055 46.584  1.00 30.06  ? 136 ASP E O     1 
ATOM   6101  C CB    . ASP E 1 135 ? 25.756  -38.594 49.099  1.00 32.75  ? 136 ASP E CB    1 
ATOM   6102  C CG    . ASP E 1 135 ? 26.899  -39.579 49.302  1.00 33.87  ? 136 ASP E CG    1 
ATOM   6103  O OD1   . ASP E 1 135 ? 28.069  -39.147 49.222  1.00 37.34  ? 136 ASP E OD1   1 
ATOM   6104  O OD2   . ASP E 1 135 ? 26.609  -40.768 49.552  1.00 32.35  ? 136 ASP E OD2   1 
ATOM   6105  N N     . PRO E 1 136 ? 28.305  -36.488 47.891  1.00 30.50  ? 137 PRO E N     1 
ATOM   6106  C CA    . PRO E 1 136 ? 29.188  -36.205 46.758  1.00 32.12  ? 137 PRO E CA    1 
ATOM   6107  C C     . PRO E 1 136 ? 29.408  -37.432 45.876  1.00 34.98  ? 137 PRO E C     1 
ATOM   6108  O O     . PRO E 1 136 ? 29.759  -37.306 44.705  1.00 40.01  ? 137 PRO E O     1 
ATOM   6109  C CB    . PRO E 1 136 ? 30.491  -35.724 47.427  1.00 30.46  ? 137 PRO E CB    1 
ATOM   6110  C CG    . PRO E 1 136 ? 30.434  -36.310 48.826  1.00 30.19  ? 137 PRO E CG    1 
ATOM   6111  C CD    . PRO E 1 136 ? 28.962  -36.295 49.192  1.00 27.78  ? 137 PRO E CD    1 
ATOM   6112  N N     . GLY E 1 137 ? 29.192  -38.616 46.457  1.00 34.66  ? 138 GLY E N     1 
ATOM   6113  C CA    . GLY E 1 137 ? 29.398  -39.869 45.751  1.00 34.33  ? 138 GLY E CA    1 
ATOM   6114  C C     . GLY E 1 137 ? 28.197  -40.229 44.882  1.00 32.53  ? 138 GLY E C     1 
ATOM   6115  O O     . GLY E 1 137 ? 28.294  -41.096 44.017  1.00 30.93  ? 138 GLY E O     1 
ATOM   6116  N N     . ASN E 1 138 ? 27.070  -39.547 45.118  1.00 29.16  ? 139 ASN E N     1 
ATOM   6117  C CA    . ASN E 1 138 ? 25.824  -39.852 44.434  1.00 29.41  ? 139 ASN E CA    1 
ATOM   6118  C C     . ASN E 1 138 ? 26.039  -39.802 42.923  1.00 27.97  ? 139 ASN E C     1 
ATOM   6119  O O     . ASN E 1 138 ? 25.665  -40.731 42.211  1.00 23.27  ? 139 ASN E O     1 
ATOM   6120  C CB    . ASN E 1 138 ? 24.701  -38.911 44.855  1.00 31.51  ? 139 ASN E CB    1 
ATOM   6121  C CG    . ASN E 1 138 ? 23.366  -39.345 44.296  1.00 36.48  ? 139 ASN E CG    1 
ATOM   6122  O OD1   . ASN E 1 138 ? 22.871  -40.424 44.637  1.00 38.89  ? 139 ASN E OD1   1 
ATOM   6123  N ND2   . ASN E 1 138 ? 22.773  -38.528 43.438  1.00 39.19  ? 139 ASN E ND2   1 
ATOM   6124  N N     . SER E 1 139 ? 26.619  -38.698 42.441  1.00 26.09  ? 140 SER E N     1 
ATOM   6125  C CA    . SER E 1 139 ? 26.903  -38.542 41.024  1.00 26.08  ? 140 SER E CA    1 
ATOM   6126  C C     . SER E 1 139 ? 28.255  -37.860 40.835  1.00 23.77  ? 140 SER E C     1 
ATOM   6127  O O     . SER E 1 139 ? 28.534  -37.311 39.772  1.00 25.43  ? 140 SER E O     1 
ATOM   6128  C CB    . SER E 1 139 ? 25.806  -37.779 40.324  1.00 25.47  ? 140 SER E CB    1 
ATOM   6129  O OG    . SER E 1 139 ? 25.778  -36.421 40.742  1.00 24.91  ? 140 SER E OG    1 
ATOM   6130  N N     . GLY E 1 140 ? 29.083  -37.900 41.883  1.00 22.57  ? 141 GLY E N     1 
ATOM   6131  C CA    . GLY E 1 140 ? 30.424  -37.343 41.822  1.00 25.88  ? 141 GLY E CA    1 
ATOM   6132  C C     . GLY E 1 140 ? 30.448  -35.884 42.269  1.00 26.38  ? 141 GLY E C     1 
ATOM   6133  O O     . GLY E 1 140 ? 29.408  -35.232 42.341  1.00 28.12  ? 141 GLY E O     1 
ATOM   6134  N N     . HIS E 1 141 ? 31.657  -35.383 42.542  1.00 27.82  ? 142 HIS E N     1 
ATOM   6135  C CA    . HIS E 1 141 ? 31.846  -34.060 43.111  1.00 27.36  ? 142 HIS E CA    1 
ATOM   6136  C C     . HIS E 1 141 ? 33.053  -33.386 42.463  1.00 28.46  ? 142 HIS E C     1 
ATOM   6137  O O     . HIS E 1 141 ? 34.094  -34.013 42.278  1.00 27.16  ? 142 HIS E O     1 
ATOM   6138  C CB    . HIS E 1 141 ? 32.005  -34.166 44.632  1.00 28.13  ? 142 HIS E CB    1 
ATOM   6139  C CG    . HIS E 1 141 ? 32.723  -33.018 45.257  1.00 28.24  ? 142 HIS E CG    1 
ATOM   6140  N ND1   . HIS E 1 141 ? 33.576  -33.185 46.326  1.00 30.54  ? 142 HIS E ND1   1 
ATOM   6141  C CD2   . HIS E 1 141 ? 32.741  -31.710 44.969  1.00 28.64  ? 142 HIS E CD2   1 
ATOM   6142  C CE1   . HIS E 1 141 ? 34.079  -32.009 46.671  1.00 30.94  ? 142 HIS E CE1   1 
ATOM   6143  N NE2   . HIS E 1 141 ? 33.585  -31.099 45.861  1.00 30.08  ? 142 HIS E NE2   1 
ATOM   6144  N N     . GLN E 1 142 ? 32.896  -32.099 42.131  1.00 31.00  ? 143 GLN E N     1 
ATOM   6145  C CA    . GLN E 1 142 ? 33.984  -31.296 41.598  1.00 29.86  ? 143 GLN E CA    1 
ATOM   6146  C C     . GLN E 1 142 ? 34.039  -29.967 42.343  1.00 27.66  ? 143 GLN E C     1 
ATOM   6147  O O     . GLN E 1 142 ? 33.008  -29.339 42.573  1.00 28.17  ? 143 GLN E O     1 
ATOM   6148  C CB    . GLN E 1 142 ? 33.801  -31.017 40.106  1.00 30.70  ? 143 GLN E CB    1 
ATOM   6149  C CG    . GLN E 1 142 ? 33.769  -32.267 39.235  1.00 33.12  ? 143 GLN E CG    1 
ATOM   6150  C CD    . GLN E 1 142 ? 33.606  -31.953 37.764  1.00 36.22  ? 143 GLN E CD    1 
ATOM   6151  O OE1   . GLN E 1 142 ? 34.430  -32.336 36.925  1.00 34.09  ? 143 GLN E OE1   1 
ATOM   6152  N NE2   . GLN E 1 142 ? 32.535  -31.246 37.436  1.00 39.49  ? 143 GLN E NE2   1 
ATOM   6153  N N     . SER E 1 143 ? 35.256  -29.543 42.697  1.00 25.98  ? 144 SER E N     1 
ATOM   6154  C CA    . SER E 1 143 ? 35.466  -28.273 43.371  1.00 28.79  ? 144 SER E CA    1 
ATOM   6155  C C     . SER E 1 143 ? 36.531  -27.467 42.634  1.00 27.57  ? 144 SER E C     1 
ATOM   6156  O O     . SER E 1 143 ? 37.599  -27.985 42.320  1.00 31.19  ? 144 SER E O     1 
ATOM   6157  C CB    . SER E 1 143 ? 35.844  -28.474 44.817  1.00 28.13  ? 144 SER E CB    1 
ATOM   6158  O OG    . SER E 1 143 ? 34.769  -29.041 45.553  1.00 34.25  ? 144 SER E OG    1 
ATOM   6159  N N     . PHE E 1 144 ? 36.219  -26.195 42.367  1.00 28.47  ? 145 PHE E N     1 
ATOM   6160  C CA    . PHE E 1 144 ? 37.168  -25.276 41.763  1.00 27.23  ? 145 PHE E CA    1 
ATOM   6161  C C     . PHE E 1 144 ? 37.073  -23.929 42.466  1.00 26.18  ? 145 PHE E C     1 
ATOM   6162  O O     . PHE E 1 144 ? 35.996  -23.527 42.901  1.00 30.85  ? 145 PHE E O     1 
ATOM   6163  C CB    . PHE E 1 144 ? 36.907  -25.057 40.269  1.00 26.19  ? 145 PHE E CB    1 
ATOM   6164  C CG    . PHE E 1 144 ? 36.952  -26.312 39.409  1.00 26.04  ? 145 PHE E CG    1 
ATOM   6165  C CD1   . PHE E 1 144 ? 38.166  -26.851 38.997  1.00 26.03  ? 145 PHE E CD1   1 
ATOM   6166  C CD2   . PHE E 1 144 ? 35.780  -26.930 38.988  1.00 27.00  ? 145 PHE E CD2   1 
ATOM   6167  C CE1   . PHE E 1 144 ? 38.204  -27.989 38.210  1.00 27.61  ? 145 PHE E CE1   1 
ATOM   6168  C CE2   . PHE E 1 144 ? 35.825  -28.067 38.196  1.00 27.22  ? 145 PHE E CE2   1 
ATOM   6169  C CZ    . PHE E 1 144 ? 37.035  -28.593 37.810  1.00 28.19  ? 145 PHE E CZ    1 
ATOM   6170  N N     . GLU E 1 145 ? 38.213  -23.239 42.562  1.00 27.66  ? 146 GLU E N     1 
ATOM   6171  C CA    . GLU E 1 145 ? 38.228  -21.841 42.955  1.00 28.45  ? 146 GLU E CA    1 
ATOM   6172  C C     . GLU E 1 145 ? 37.650  -21.038 41.793  1.00 28.54  ? 146 GLU E C     1 
ATOM   6173  O O     . GLU E 1 145 ? 38.046  -21.230 40.644  1.00 28.66  ? 146 GLU E O     1 
ATOM   6174  C CB    . GLU E 1 145 ? 39.652  -21.433 43.339  1.00 31.34  ? 146 GLU E CB    1 
ATOM   6175  C CG    . GLU E 1 145 ? 39.725  -20.149 44.162  1.00 35.16  ? 146 GLU E CG    1 
ATOM   6176  C CD    . GLU E 1 145 ? 39.516  -18.874 43.368  1.00 39.96  ? 146 GLU E CD    1 
ATOM   6177  O OE1   . GLU E 1 145 ? 39.360  -18.965 42.133  1.00 42.58  ? 146 GLU E OE1   1 
ATOM   6178  O OE2   . GLU E 1 145 ? 39.516  -17.788 43.987  1.00 45.38  ? 146 GLU E OE2   1 
ATOM   6179  N N     . ALA E 1 146 ? 36.684  -20.167 42.101  1.00 28.65  ? 147 ALA E N     1 
ATOM   6180  C CA    . ALA E 1 146 ? 35.880  -19.508 41.084  1.00 28.93  ? 147 ALA E CA    1 
ATOM   6181  C C     . ALA E 1 146 ? 36.772  -18.795 40.069  1.00 27.69  ? 147 ALA E C     1 
ATOM   6182  O O     . ALA E 1 146 ? 36.575  -18.931 38.863  1.00 26.36  ? 147 ALA E O     1 
ATOM   6183  C CB    . ALA E 1 146 ? 34.911  -18.549 41.738  1.00 29.51  ? 147 ALA E CB    1 
ATOM   6184  N N     . SER E 1 147 ? 37.744  -18.026 40.572  1.00 27.41  ? 148 SER E N     1 
ATOM   6185  C CA    . SER E 1 147 ? 38.588  -17.200 39.723  1.00 28.23  ? 148 SER E CA    1 
ATOM   6186  C C     . SER E 1 147 ? 39.489  -18.078 38.858  1.00 26.74  ? 148 SER E C     1 
ATOM   6187  O O     . SER E 1 147 ? 39.716  -17.777 37.688  1.00 24.30  ? 148 SER E O     1 
ATOM   6188  C CB    . SER E 1 147 ? 39.397  -16.226 40.543  1.00 30.00  ? 148 SER E CB    1 
ATOM   6189  O OG    . SER E 1 147 ? 38.551  -15.305 41.219  1.00 29.71  ? 148 SER E OG    1 
ATOM   6190  N N     . GLN E 1 148 ? 39.997  -19.164 39.448  1.00 26.17  ? 149 GLN E N     1 
ATOM   6191  C CA    . GLN E 1 148 ? 40.883  -20.075 38.742  1.00 29.48  ? 149 GLN E CA    1 
ATOM   6192  C C     . GLN E 1 148 ? 40.118  -20.740 37.601  1.00 30.61  ? 149 GLN E C     1 
ATOM   6193  O O     . GLN E 1 148 ? 40.700  -21.079 36.573  1.00 33.65  ? 149 GLN E O     1 
ATOM   6194  C CB    . GLN E 1 148 ? 41.460  -21.129 39.688  1.00 28.43  ? 149 GLN E CB    1 
ATOM   6195  C CG    . GLN E 1 148 ? 42.439  -22.087 39.018  1.00 30.08  ? 149 GLN E CG    1 
ATOM   6196  C CD    . GLN E 1 148 ? 42.870  -23.226 39.915  1.00 30.67  ? 149 GLN E CD    1 
ATOM   6197  O OE1   . GLN E 1 148 ? 42.530  -24.392 39.683  1.00 27.59  ? 149 GLN E OE1   1 
ATOM   6198  N NE2   . GLN E 1 148 ? 43.615  -22.896 40.961  1.00 30.60  ? 149 GLN E NE2   1 
ATOM   6199  N N     . PHE E 1 149 ? 38.807  -20.916 37.796  1.00 26.73  ? 150 PHE E N     1 
ATOM   6200  C CA    . PHE E 1 149 ? 37.961  -21.568 36.810  1.00 27.32  ? 150 PHE E CA    1 
ATOM   6201  C C     . PHE E 1 149 ? 37.762  -20.637 35.617  1.00 31.71  ? 150 PHE E C     1 
ATOM   6202  O O     . PHE E 1 149 ? 37.351  -21.076 34.547  1.00 27.48  ? 150 PHE E O     1 
ATOM   6203  C CB    . PHE E 1 149 ? 36.623  -21.969 37.441  1.00 28.85  ? 150 PHE E CB    1 
ATOM   6204  C CG    . PHE E 1 149 ? 35.664  -22.675 36.491  1.00 30.88  ? 150 PHE E CG    1 
ATOM   6205  C CD1   . PHE E 1 149 ? 34.753  -21.954 35.728  1.00 29.74  ? 150 PHE E CD1   1 
ATOM   6206  C CD2   . PHE E 1 149 ? 35.679  -24.060 36.361  1.00 32.46  ? 150 PHE E CD2   1 
ATOM   6207  C CE1   . PHE E 1 149 ? 33.885  -22.600 34.862  1.00 32.48  ? 150 PHE E CE1   1 
ATOM   6208  C CE2   . PHE E 1 149 ? 34.808  -24.700 35.493  1.00 32.38  ? 150 PHE E CE2   1 
ATOM   6209  C CZ    . PHE E 1 149 ? 33.913  -23.970 34.747  1.00 31.15  ? 150 PHE E CZ    1 
ATOM   6210  N N     . MET E 1 150 ? 38.065  -19.348 35.813  1.00 34.44  ? 151 MET E N     1 
ATOM   6211  C CA    . MET E 1 150 ? 37.850  -18.343 34.784  1.00 33.36  ? 151 MET E CA    1 
ATOM   6212  C C     . MET E 1 150 ? 39.166  -18.021 34.078  1.00 32.52  ? 151 MET E C     1 
ATOM   6213  O O     . MET E 1 150 ? 39.176  -17.753 32.879  1.00 31.66  ? 151 MET E O     1 
ATOM   6214  C CB    . MET E 1 150 ? 37.270  -17.054 35.379  1.00 36.02  ? 151 MET E CB    1 
ATOM   6215  C CG    . MET E 1 150 ? 35.827  -17.176 35.841  1.00 36.46  ? 151 MET E CG    1 
ATOM   6216  S SD    . MET E 1 150 ? 35.158  -15.635 36.502  1.00 38.97  ? 151 MET E SD    1 
ATOM   6217  C CE    . MET E 1 150 ? 35.117  -14.583 35.045  1.00 38.28  ? 151 MET E CE    1 
ATOM   6218  N N     . PHE E 1 151 ? 40.270  -18.046 34.832  1.00 34.17  ? 152 PHE E N     1 
ATOM   6219  C CA    . PHE E 1 151 ? 41.557  -17.605 34.319  1.00 36.35  ? 152 PHE E CA    1 
ATOM   6220  C C     . PHE E 1 151 ? 42.253  -18.753 33.590  1.00 36.60  ? 152 PHE E C     1 
ATOM   6221  O O     . PHE E 1 151 ? 43.069  -18.518 32.702  1.00 34.58  ? 152 PHE E O     1 
ATOM   6222  C CB    . PHE E 1 151 ? 42.444  -17.072 35.448  1.00 38.93  ? 152 PHE E CB    1 
ATOM   6223  C CG    . PHE E 1 151 ? 41.895  -15.856 36.181  1.00 40.10  ? 152 PHE E CG    1 
ATOM   6224  C CD1   . PHE E 1 151 ? 40.997  -14.992 35.565  1.00 40.79  ? 152 PHE E CD1   1 
ATOM   6225  C CD2   . PHE E 1 151 ? 42.296  -15.569 37.482  1.00 40.70  ? 152 PHE E CD2   1 
ATOM   6226  C CE1   . PHE E 1 151 ? 40.506  -13.883 36.238  1.00 41.40  ? 152 PHE E CE1   1 
ATOM   6227  C CE2   . PHE E 1 151 ? 41.803  -14.459 38.147  1.00 39.19  ? 152 PHE E CE2   1 
ATOM   6228  C CZ    . PHE E 1 151 ? 40.911  -13.619 37.525  1.00 40.11  ? 152 PHE E CZ    1 
ATOM   6229  N N     . PHE E 1 152 ? 41.933  -19.991 33.980  1.00 32.46  ? 153 PHE E N     1 
ATOM   6230  C CA    . PHE E 1 152 ? 42.600  -21.157 33.424  1.00 32.19  ? 153 PHE E CA    1 
ATOM   6231  C C     . PHE E 1 152 ? 41.564  -22.086 32.799  1.00 33.30  ? 153 PHE E C     1 
ATOM   6232  O O     . PHE E 1 152 ? 40.365  -21.820 32.855  1.00 31.03  ? 153 PHE E O     1 
ATOM   6233  C CB    . PHE E 1 152 ? 43.435  -21.845 34.508  1.00 34.66  ? 153 PHE E CB    1 
ATOM   6234  C CG    . PHE E 1 152 ? 44.463  -20.936 35.168  1.00 38.79  ? 153 PHE E CG    1 
ATOM   6235  C CD1   . PHE E 1 152 ? 45.644  -20.603 34.515  1.00 43.26  ? 153 PHE E CD1   1 
ATOM   6236  C CD2   . PHE E 1 152 ? 44.249  -20.423 36.443  1.00 42.22  ? 153 PHE E CD2   1 
ATOM   6237  C CE1   . PHE E 1 152 ? 46.577  -19.772 35.117  1.00 43.73  ? 153 PHE E CE1   1 
ATOM   6238  C CE2   . PHE E 1 152 ? 45.188  -19.598 37.042  1.00 42.39  ? 153 PHE E CE2   1 
ATOM   6239  C CZ    . PHE E 1 152 ? 46.348  -19.275 36.378  1.00 44.73  ? 153 PHE E CZ    1 
ATOM   6240  N N     . ASN E 1 153 ? 42.050  -23.180 32.206  1.00 35.94  ? 154 ASN E N     1 
ATOM   6241  C CA    . ASN E 1 153 ? 41.208  -24.081 31.437  1.00 39.22  ? 154 ASN E CA    1 
ATOM   6242  C C     . ASN E 1 153 ? 40.756  -25.240 32.320  1.00 36.70  ? 154 ASN E C     1 
ATOM   6243  O O     . ASN E 1 153 ? 41.522  -26.161 32.594  1.00 35.96  ? 154 ASN E O     1 
ATOM   6244  C CB    . ASN E 1 153 ? 41.922  -24.555 30.175  1.00 42.17  ? 154 ASN E CB    1 
ATOM   6245  C CG    . ASN E 1 153 ? 42.087  -23.439 29.172  1.00 48.51  ? 154 ASN E CG    1 
ATOM   6246  O OD1   . ASN E 1 153 ? 41.112  -23.030 28.531  1.00 53.95  ? 154 ASN E OD1   1 
ATOM   6247  N ND2   . ASN E 1 153 ? 43.305  -22.940 29.015  1.00 46.79  ? 154 ASN E ND2   1 
ATOM   6248  N N     . HIS E 1 154 ? 39.495  -25.170 32.753  1.00 32.55  ? 155 HIS E N     1 
ATOM   6249  C CA    . HIS E 1 154 ? 38.869  -26.231 33.523  1.00 35.02  ? 155 HIS E CA    1 
ATOM   6250  C C     . HIS E 1 154 ? 37.581  -26.650 32.823  1.00 32.95  ? 155 HIS E C     1 
ATOM   6251  O O     . HIS E 1 154 ? 36.758  -25.807 32.477  1.00 33.02  ? 155 HIS E O     1 
ATOM   6252  C CB    . HIS E 1 154 ? 38.601  -25.765 34.960  1.00 36.21  ? 155 HIS E CB    1 
ATOM   6253  C CG    . HIS E 1 154 ? 39.816  -25.719 35.825  1.00 36.78  ? 155 HIS E CG    1 
ATOM   6254  N ND1   . HIS E 1 154 ? 40.700  -26.771 35.927  1.00 38.38  ? 155 HIS E ND1   1 
ATOM   6255  C CD2   . HIS E 1 154 ? 40.266  -24.776 36.664  1.00 37.51  ? 155 HIS E CD2   1 
ATOM   6256  C CE1   . HIS E 1 154 ? 41.663  -26.452 36.780  1.00 37.54  ? 155 HIS E CE1   1 
ATOM   6257  N NE2   . HIS E 1 154 ? 41.421  -25.243 37.236  1.00 34.25  ? 155 HIS E NE2   1 
ATOM   6258  N N     . VAL E 1 155 ? 37.422  -27.961 32.617  1.00 38.07  ? 156 VAL E N     1 
ATOM   6259  C CA    . VAL E 1 155 ? 36.228  -28.499 31.986  1.00 38.88  ? 156 VAL E CA    1 
ATOM   6260  C C     . VAL E 1 155 ? 35.472  -29.341 33.011  1.00 41.53  ? 156 VAL E C     1 
ATOM   6261  O O     . VAL E 1 155 ? 35.933  -30.410 33.404  1.00 35.46  ? 156 VAL E O     1 
ATOM   6262  C CB    . VAL E 1 155 ? 36.564  -29.323 30.728  1.00 41.65  ? 156 VAL E CB    1 
ATOM   6263  C CG1   . VAL E 1 155 ? 35.326  -29.994 30.146  1.00 43.93  ? 156 VAL E CG1   1 
ATOM   6264  C CG2   . VAL E 1 155 ? 37.267  -28.481 29.670  1.00 39.71  ? 156 VAL E CG2   1 
ATOM   6265  N N     . PRO E 1 156 ? 34.284  -28.884 33.466  1.00 39.26  ? 157 PRO E N     1 
ATOM   6266  C CA    . PRO E 1 156 ? 33.514  -29.611 34.476  1.00 35.14  ? 157 PRO E CA    1 
ATOM   6267  C C     . PRO E 1 156 ? 32.688  -30.758 33.901  1.00 37.15  ? 157 PRO E C     1 
ATOM   6268  O O     . PRO E 1 156 ? 32.291  -30.723 32.738  1.00 39.30  ? 157 PRO E O     1 
ATOM   6269  C CB    . PRO E 1 156 ? 32.632  -28.490 35.046  1.00 36.02  ? 157 PRO E CB    1 
ATOM   6270  C CG    . PRO E 1 156 ? 32.338  -27.619 33.842  1.00 39.72  ? 157 PRO E CG    1 
ATOM   6271  C CD    . PRO E 1 156 ? 33.627  -27.641 33.031  1.00 38.74  ? 157 PRO E CD    1 
ATOM   6272  N N     . ASP E 1 157 ? 32.444  -31.775 34.735  1.00 34.10  ? 158 ASP E N     1 
ATOM   6273  C CA    . ASP E 1 157 ? 31.561  -32.873 34.383  1.00 35.87  ? 158 ASP E CA    1 
ATOM   6274  C C     . ASP E 1 157 ? 30.140  -32.500 34.795  1.00 33.41  ? 158 ASP E C     1 
ATOM   6275  O O     . ASP E 1 157 ? 29.819  -32.472 35.982  1.00 31.69  ? 158 ASP E O     1 
ATOM   6276  C CB    . ASP E 1 157 ? 32.026  -34.179 35.011  1.00 34.32  ? 158 ASP E CB    1 
ATOM   6277  C CG    . ASP E 1 157 ? 31.183  -35.402 34.680  1.00 35.83  ? 158 ASP E CG    1 
ATOM   6278  O OD1   . ASP E 1 157 ? 30.142  -35.234 34.011  1.00 45.53  ? 158 ASP E OD1   1 
ATOM   6279  O OD2   . ASP E 1 157 ? 31.582  -36.515 35.085  1.00 33.64  ? 158 ASP E OD2   1 
ATOM   6280  N N     . PRO E 1 158 ? 29.244  -32.211 33.825  1.00 30.36  ? 159 PRO E N     1 
ATOM   6281  C CA    . PRO E 1 158 ? 27.915  -31.681 34.138  1.00 31.52  ? 159 PRO E CA    1 
ATOM   6282  C C     . PRO E 1 158 ? 26.984  -32.678 34.824  1.00 34.53  ? 159 PRO E C     1 
ATOM   6283  O O     . PRO E 1 158 ? 25.825  -32.366 35.084  1.00 33.75  ? 159 PRO E O     1 
ATOM   6284  C CB    . PRO E 1 158 ? 27.389  -31.251 32.751  1.00 34.69  ? 159 PRO E CB    1 
ATOM   6285  C CG    . PRO E 1 158 ? 28.098  -32.174 31.780  1.00 31.80  ? 159 PRO E CG    1 
ATOM   6286  C CD    . PRO E 1 158 ? 29.473  -32.385 32.383  1.00 31.19  ? 159 PRO E CD    1 
ATOM   6287  N N     . THR E 1 159 ? 27.506  -33.872 35.129  1.00 33.58  ? 160 THR E N     1 
ATOM   6288  C CA    . THR E 1 159 ? 26.712  -34.908 35.769  1.00 32.57  ? 160 THR E CA    1 
ATOM   6289  C C     . THR E 1 159 ? 26.966  -34.894 37.274  1.00 30.58  ? 160 THR E C     1 
ATOM   6290  O O     . THR E 1 159 ? 26.257  -35.555 38.029  1.00 31.79  ? 160 THR E O     1 
ATOM   6291  C CB    . THR E 1 159 ? 27.047  -36.270 35.160  1.00 35.76  ? 160 THR E CB    1 
ATOM   6292  O OG1   . THR E 1 159 ? 28.433  -36.479 35.410  1.00 33.18  ? 160 THR E OG1   1 
ATOM   6293  C CG2   . THR E 1 159 ? 26.770  -36.327 33.669  1.00 35.08  ? 160 THR E CG2   1 
ATOM   6294  N N     . THR E 1 160 ? 27.980  -34.133 37.699  1.00 28.33  ? 161 THR E N     1 
ATOM   6295  C CA    . THR E 1 160 ? 28.402  -34.134 39.089  1.00 30.01  ? 161 THR E CA    1 
ATOM   6296  C C     . THR E 1 160 ? 27.846  -32.902 39.794  1.00 30.79  ? 161 THR E C     1 
ATOM   6297  O O     . THR E 1 160 ? 27.157  -32.083 39.191  1.00 37.13  ? 161 THR E O     1 
ATOM   6298  C CB    . THR E 1 160 ? 29.928  -34.169 39.174  1.00 30.19  ? 161 THR E CB    1 
ATOM   6299  O OG1   . THR E 1 160 ? 30.369  -32.870 38.794  1.00 30.54  ? 161 THR E OG1   1 
ATOM   6300  C CG2   . THR E 1 160 ? 30.538  -35.224 38.271  1.00 32.21  ? 161 THR E CG2   1 
ATOM   6301  N N     . HIS E 1 161 ? 28.162  -32.799 41.086  1.00 30.96  ? 162 HIS E N     1 
ATOM   6302  C CA    . HIS E 1 161 ? 27.857  -31.621 41.874  1.00 29.53  ? 162 HIS E CA    1 
ATOM   6303  C C     . HIS E 1 161 ? 29.075  -30.707 41.850  1.00 27.62  ? 162 HIS E C     1 
ATOM   6304  O O     . HIS E 1 161 ? 30.131  -31.063 42.367  1.00 23.52  ? 162 HIS E O     1 
ATOM   6305  C CB    . HIS E 1 161 ? 27.456  -32.012 43.300  1.00 28.91  ? 162 HIS E CB    1 
ATOM   6306  C CG    . HIS E 1 161 ? 26.005  -32.326 43.454  1.00 30.76  ? 162 HIS E CG    1 
ATOM   6307  N ND1   . HIS E 1 161 ? 25.500  -33.608 43.464  1.00 28.93  ? 162 HIS E ND1   1 
ATOM   6308  C CD2   . HIS E 1 161 ? 24.955  -31.511 43.622  1.00 28.68  ? 162 HIS E CD2   1 
ATOM   6309  C CE1   . HIS E 1 161 ? 24.185  -33.557 43.621  1.00 28.14  ? 162 HIS E CE1   1 
ATOM   6310  N NE2   . HIS E 1 161 ? 23.833  -32.293 43.717  1.00 29.08  ? 162 HIS E NE2   1 
ATOM   6311  N N     . LEU E 1 162 ? 28.917  -29.538 41.225  1.00 28.06  ? 163 LEU E N     1 
ATOM   6312  C CA    . LEU E 1 162 ? 30.025  -28.621 41.030  1.00 27.41  ? 163 LEU E CA    1 
ATOM   6313  C C     . LEU E 1 162 ? 29.994  -27.539 42.105  1.00 26.26  ? 163 LEU E C     1 
ATOM   6314  O O     . LEU E 1 162 ? 28.962  -26.910 42.330  1.00 28.08  ? 163 LEU E O     1 
ATOM   6315  C CB    . LEU E 1 162 ? 29.944  -28.017 39.630  1.00 26.05  ? 163 LEU E CB    1 
ATOM   6316  C CG    . LEU E 1 162 ? 30.970  -26.925 39.315  1.00 26.83  ? 163 LEU E CG    1 
ATOM   6317  C CD1   . LEU E 1 162 ? 32.380  -27.491 39.317  1.00 29.00  ? 163 LEU E CD1   1 
ATOM   6318  C CD2   . LEU E 1 162 ? 30.660  -26.254 37.990  1.00 27.69  ? 163 LEU E CD2   1 
ATOM   6319  N N     . LEU E 1 163 ? 31.145  -27.330 42.752  1.00 30.00  ? 164 LEU E N     1 
ATOM   6320  C CA    . LEU E 1 163 ? 31.307  -26.259 43.721  1.00 29.55  ? 164 LEU E CA    1 
ATOM   6321  C C     . LEU E 1 163 ? 32.297  -25.237 43.171  1.00 26.81  ? 164 LEU E C     1 
ATOM   6322  O O     . LEU E 1 163 ? 33.386  -25.597 42.732  1.00 26.36  ? 164 LEU E O     1 
ATOM   6323  C CB    . LEU E 1 163 ? 31.784  -26.811 45.063  1.00 30.26  ? 164 LEU E CB    1 
ATOM   6324  C CG    . LEU E 1 163 ? 30.818  -27.743 45.799  1.00 34.10  ? 164 LEU E CG    1 
ATOM   6325  C CD1   . LEU E 1 163 ? 31.360  -28.085 47.177  1.00 35.01  ? 164 LEU E CD1   1 
ATOM   6326  C CD2   . LEU E 1 163 ? 29.434  -27.129 45.902  1.00 39.59  ? 164 LEU E CD2   1 
ATOM   6327  N N     . LEU E 1 164 ? 31.899  -23.962 43.199  1.00 27.01  ? 165 LEU E N     1 
ATOM   6328  C CA    . LEU E 1 164 ? 32.796  -22.866 42.877  1.00 27.43  ? 165 LEU E CA    1 
ATOM   6329  C C     . LEU E 1 164 ? 33.029  -22.048 44.142  1.00 25.34  ? 165 LEU E C     1 
ATOM   6330  O O     . LEU E 1 164 ? 32.152  -21.302 44.573  1.00 27.62  ? 165 LEU E O     1 
ATOM   6331  C CB    . LEU E 1 164 ? 32.224  -22.001 41.755  1.00 29.01  ? 165 LEU E CB    1 
ATOM   6332  C CG    . LEU E 1 164 ? 32.005  -22.700 40.410  1.00 30.66  ? 165 LEU E CG    1 
ATOM   6333  C CD1   . LEU E 1 164 ? 31.673  -21.684 39.329  1.00 35.14  ? 165 LEU E CD1   1 
ATOM   6334  C CD2   . LEU E 1 164 ? 33.216  -23.528 40.016  1.00 30.72  ? 165 LEU E CD2   1 
ATOM   6335  N N     . TRP E 1 165 ? 34.214  -22.211 44.738  1.00 23.90  ? 166 TRP E N     1 
ATOM   6336  C CA    . TRP E 1 165 ? 34.545  -21.529 45.977  1.00 25.81  ? 166 TRP E CA    1 
ATOM   6337  C C     . TRP E 1 165 ? 34.935  -20.084 45.681  1.00 26.58  ? 166 TRP E C     1 
ATOM   6338  O O     . TRP E 1 165 ? 35.250  -19.742 44.543  1.00 27.38  ? 166 TRP E O     1 
ATOM   6339  C CB    . TRP E 1 165 ? 35.667  -22.268 46.719  1.00 24.89  ? 166 TRP E CB    1 
ATOM   6340  C CG    . TRP E 1 165 ? 35.336  -23.698 47.053  1.00 24.53  ? 166 TRP E CG    1 
ATOM   6341  C CD1   . TRP E 1 165 ? 34.856  -24.653 46.205  1.00 25.73  ? 166 TRP E CD1   1 
ATOM   6342  C CD2   . TRP E 1 165 ? 35.424  -24.324 48.352  1.00 25.03  ? 166 TRP E CD2   1 
ATOM   6343  N NE1   . TRP E 1 165 ? 34.663  -25.831 46.874  1.00 24.18  ? 166 TRP E NE1   1 
ATOM   6344  C CE2   . TRP E 1 165 ? 34.996  -25.660 48.193  1.00 25.40  ? 166 TRP E CE2   1 
ATOM   6345  C CE3   . TRP E 1 165 ? 35.823  -23.890 49.621  1.00 24.99  ? 166 TRP E CE3   1 
ATOM   6346  C CZ2   . TRP E 1 165 ? 34.961  -26.559 49.256  1.00 24.72  ? 166 TRP E CZ2   1 
ATOM   6347  C CZ3   . TRP E 1 165 ? 35.786  -24.781 50.671  1.00 24.16  ? 166 TRP E CZ3   1 
ATOM   6348  C CH2   . TRP E 1 165 ? 35.359  -26.096 50.489  1.00 25.38  ? 166 TRP E CH2   1 
ATOM   6349  N N     . GLN E 1 166 ? 34.890  -19.245 46.721  1.00 25.78  ? 167 GLN E N     1 
ATOM   6350  C CA    . GLN E 1 166 ? 35.256  -17.842 46.606  1.00 26.06  ? 167 GLN E CA    1 
ATOM   6351  C C     . GLN E 1 166 ? 34.598  -17.245 45.364  1.00 26.01  ? 167 GLN E C     1 
ATOM   6352  O O     . GLN E 1 166 ? 35.270  -16.661 44.518  1.00 25.14  ? 167 GLN E O     1 
ATOM   6353  C CB    . GLN E 1 166 ? 36.778  -17.699 46.574  1.00 28.72  ? 167 GLN E CB    1 
ATOM   6354  C CG    . GLN E 1 166 ? 37.465  -18.135 47.864  1.00 30.92  ? 167 GLN E CG    1 
ATOM   6355  C CD    . GLN E 1 166 ? 38.969  -17.977 47.824  1.00 34.77  ? 167 GLN E CD    1 
ATOM   6356  O OE1   . GLN E 1 166 ? 39.556  -17.629 46.794  1.00 44.82  ? 167 GLN E OE1   1 
ATOM   6357  N NE2   . GLN E 1 166 ? 39.612  -18.244 48.952  1.00 36.73  ? 167 GLN E NE2   1 
ATOM   6358  N N     . ILE E 1 167 ? 33.272  -17.385 45.281  1.00 26.18  ? 168 ILE E N     1 
ATOM   6359  C CA    . ILE E 1 167 ? 32.507  -16.853 44.165  1.00 25.41  ? 168 ILE E CA    1 
ATOM   6360  C C     . ILE E 1 167 ? 32.420  -15.334 44.299  1.00 28.93  ? 168 ILE E C     1 
ATOM   6361  O O     . ILE E 1 167 ? 32.182  -14.632 43.317  1.00 25.66  ? 168 ILE E O     1 
ATOM   6362  C CB    . ILE E 1 167 ? 31.111  -17.502 44.104  1.00 24.40  ? 168 ILE E CB    1 
ATOM   6363  C CG1   . ILE E 1 167 ? 30.332  -17.053 42.867  1.00 23.65  ? 168 ILE E CG1   1 
ATOM   6364  C CG2   . ILE E 1 167 ? 30.328  -17.241 45.391  1.00 23.78  ? 168 ILE E CG2   1 
ATOM   6365  C CD1   . ILE E 1 167 ? 30.948  -17.497 41.552  1.00 24.72  ? 168 ILE E CD1   1 
ATOM   6366  N N     . ALA E 1 168 ? 32.638  -14.837 45.523  1.00 27.26  ? 169 ALA E N     1 
ATOM   6367  C CA    . ALA E 1 168 ? 32.461  -13.427 45.832  1.00 30.49  ? 169 ALA E CA    1 
ATOM   6368  C C     . ALA E 1 168 ? 33.501  -12.580 45.102  1.00 29.05  ? 169 ALA E C     1 
ATOM   6369  O O     . ALA E 1 168 ? 33.245  -11.421 44.783  1.00 29.05  ? 169 ALA E O     1 
ATOM   6370  C CB    . ALA E 1 168 ? 32.534  -13.218 47.330  1.00 34.15  ? 169 ALA E CB    1 
ATOM   6371  N N     . ILE E 1 169 ? 34.679  -13.165 44.856  1.00 30.64  ? 170 ILE E N     1 
ATOM   6372  C CA    . ILE E 1 169 ? 35.770  -12.453 44.209  1.00 31.98  ? 170 ILE E CA    1 
ATOM   6373  C C     . ILE E 1 169 ? 36.092  -13.128 42.879  1.00 30.74  ? 170 ILE E C     1 
ATOM   6374  O O     . ILE E 1 169 ? 37.245  -13.159 42.454  1.00 29.21  ? 170 ILE E O     1 
ATOM   6375  C CB    . ILE E 1 169 ? 37.004  -12.390 45.128  1.00 35.08  ? 170 ILE E CB    1 
ATOM   6376  C CG1   . ILE E 1 169 ? 37.454  -13.785 45.560  1.00 36.49  ? 170 ILE E CG1   1 
ATOM   6377  C CG2   . ILE E 1 169 ? 36.741  -11.484 46.332  1.00 33.93  ? 170 ILE E CG2   1 
ATOM   6378  C CD1   . ILE E 1 169 ? 38.682  -13.791 46.452  1.00 38.55  ? 170 ILE E CD1   1 
ATOM   6379  N N     . ALA E 1 170 ? 35.052  -13.654 42.224  1.00 28.18  ? 171 ALA E N     1 
ATOM   6380  C CA    . ALA E 1 170 ? 35.207  -14.342 40.953  1.00 27.84  ? 171 ALA E CA    1 
ATOM   6381  C C     . ALA E 1 170 ? 35.641  -13.351 39.875  1.00 27.98  ? 171 ALA E C     1 
ATOM   6382  O O     . ALA E 1 170 ? 34.895  -12.440 39.524  1.00 27.32  ? 171 ALA E O     1 
ATOM   6383  C CB    . ALA E 1 170 ? 33.912  -15.031 40.583  1.00 27.11  ? 171 ALA E CB    1 
ATOM   6384  N N     . GLY E 1 171 ? 36.857  -13.545 39.356  1.00 28.23  ? 172 GLY E N     1 
ATOM   6385  C CA    . GLY E 1 171 ? 37.365  -12.734 38.262  1.00 28.82  ? 172 GLY E CA    1 
ATOM   6386  C C     . GLY E 1 171 ? 38.216  -11.572 38.768  1.00 29.93  ? 172 GLY E C     1 
ATOM   6387  O O     . GLY E 1 171 ? 38.710  -10.772 37.977  1.00 25.22  ? 172 GLY E O     1 
ATOM   6388  N N     . GLU E 1 172 ? 38.374  -11.490 40.094  1.00 32.36  ? 173 GLU E N     1 
ATOM   6389  C CA    . GLU E 1 172 ? 39.179  -10.447 40.708  1.00 36.05  ? 173 GLU E CA    1 
ATOM   6390  C C     . GLU E 1 172 ? 40.649  -10.849 40.606  1.00 37.80  ? 173 GLU E C     1 
ATOM   6391  O O     . GLU E 1 172 ? 41.127  -11.679 41.376  1.00 39.28  ? 173 GLU E O     1 
ATOM   6392  C CB    . GLU E 1 172 ? 38.742  -10.228 42.157  1.00 38.73  ? 173 GLU E CB    1 
ATOM   6393  C CG    . GLU E 1 172 ? 39.117  -8.852  42.700  1.00 43.93  ? 173 GLU E CG    1 
ATOM   6394  C CD    . GLU E 1 172 ? 40.595  -8.523  42.605  1.00 49.38  ? 173 GLU E CD    1 
ATOM   6395  O OE1   . GLU E 1 172 ? 41.399  -9.211  43.268  1.00 54.04  ? 173 GLU E OE1   1 
ATOM   6396  O OE2   . GLU E 1 172 ? 40.941  -7.584  41.857  1.00 45.30  ? 173 GLU E OE2   1 
ATOM   6397  N N     . HIS E 1 173 ? 41.355  -10.238 39.648  1.00 37.19  ? 174 HIS E N     1 
ATOM   6398  C CA    . HIS E 1 173 ? 42.656  -10.723 39.215  1.00 35.88  ? 174 HIS E CA    1 
ATOM   6399  C C     . HIS E 1 173 ? 43.776  -10.104 40.048  1.00 34.44  ? 174 HIS E C     1 
ATOM   6400  O O     . HIS E 1 173 ? 44.848  -10.691 40.175  1.00 38.71  ? 174 HIS E O     1 
ATOM   6401  C CB    . HIS E 1 173 ? 42.858  -10.432 37.723  1.00 37.36  ? 174 HIS E CB    1 
ATOM   6402  C CG    . HIS E 1 173 ? 42.804  -8.979  37.383  1.00 37.92  ? 174 HIS E CG    1 
ATOM   6403  N ND1   . HIS E 1 173 ? 41.632  -8.325  37.066  1.00 39.33  ? 174 HIS E ND1   1 
ATOM   6404  C CD2   . HIS E 1 173 ? 43.771  -8.054  37.321  1.00 36.99  ? 174 HIS E CD2   1 
ATOM   6405  C CE1   . HIS E 1 173 ? 41.896  -7.051  36.818  1.00 39.80  ? 174 HIS E CE1   1 
ATOM   6406  N NE2   . HIS E 1 173 ? 43.189  -6.864  36.966  1.00 37.49  ? 174 HIS E NE2   1 
ATOM   6407  N N     . THR E 1 174 ? 43.525  -8.915  40.606  1.00 39.16  ? 175 THR E N     1 
ATOM   6408  C CA    . THR E 1 174 ? 44.567  -8.146  41.268  1.00 39.72  ? 175 THR E CA    1 
ATOM   6409  C C     . THR E 1 174 ? 44.871  -8.751  42.638  1.00 34.87  ? 175 THR E C     1 
ATOM   6410  O O     . THR E 1 174 ? 45.993  -8.648  43.127  1.00 36.86  ? 175 THR E O     1 
ATOM   6411  C CB    . THR E 1 174 ? 44.137  -6.684  41.385  1.00 43.74  ? 175 THR E CB    1 
ATOM   6412  O OG1   . THR E 1 174 ? 43.026  -6.681  42.276  1.00 40.52  ? 175 THR E OG1   1 
ATOM   6413  C CG2   . THR E 1 174 ? 43.752  -6.081  40.045  1.00 45.22  ? 175 THR E CG2   1 
ATOM   6414  N N     . LEU E 1 175 ? 43.859  -9.372  43.250  1.00 37.95  ? 176 LEU E N     1 
ATOM   6415  C CA    . LEU E 1 175 ? 44.003  -9.957  44.575  1.00 38.54  ? 176 LEU E CA    1 
ATOM   6416  C C     . LEU E 1 175 ? 44.136  -8.843  45.611  1.00 37.13  ? 176 LEU E C     1 
ATOM   6417  O O     . LEU E 1 175 ? 44.775  -9.031  46.644  1.00 34.99  ? 176 LEU E O     1 
ATOM   6418  C CB    . LEU E 1 175 ? 45.213  -10.890 44.621  1.00 43.11  ? 176 LEU E CB    1 
ATOM   6419  C CG    . LEU E 1 175 ? 45.190  -12.085 43.663  1.00 46.04  ? 176 LEU E CG    1 
ATOM   6420  C CD1   . LEU E 1 175 ? 46.409  -12.966 43.889  1.00 46.14  ? 176 LEU E CD1   1 
ATOM   6421  C CD2   . LEU E 1 175 ? 43.911  -12.892 43.808  1.00 48.96  ? 176 LEU E CD2   1 
ATOM   6422  N N     . THR E 1 176 ? 43.532  -7.684  45.321  1.00 36.91  ? 177 THR E N     1 
ATOM   6423  C CA    . THR E 1 176 ? 43.580  -6.548  46.230  1.00 37.06  ? 177 THR E CA    1 
ATOM   6424  C C     . THR E 1 176 ? 42.158  -6.128  46.592  1.00 38.60  ? 177 THR E C     1 
ATOM   6425  O O     . THR E 1 176 ? 41.963  -5.245  47.424  1.00 42.19  ? 177 THR E O     1 
ATOM   6426  C CB    . THR E 1 176 ? 44.359  -5.398  45.592  1.00 35.66  ? 177 THR E CB    1 
ATOM   6427  O OG1   . THR E 1 176 ? 43.557  -4.938  44.508  1.00 36.09  ? 177 THR E OG1   1 
ATOM   6428  C CG2   . THR E 1 176 ? 45.731  -5.823  45.101  1.00 35.30  ? 177 THR E CG2   1 
ATOM   6429  N N     . GLN E 1 177 ? 41.171  -6.764  45.951  1.00 41.57  ? 178 GLN E N     1 
ATOM   6430  C CA    . GLN E 1 177 ? 39.771  -6.488  46.227  1.00 42.77  ? 178 GLN E CA    1 
ATOM   6431  C C     . GLN E 1 177 ? 39.203  -7.603  47.101  1.00 44.24  ? 178 GLN E C     1 
ATOM   6432  O O     . GLN E 1 177 ? 39.747  -8.704  47.143  1.00 43.65  ? 178 GLN E O     1 
ATOM   6433  C CB    . GLN E 1 177 ? 38.978  -6.347  44.927  1.00 41.47  ? 178 GLN E CB    1 
ATOM   6434  C CG    . GLN E 1 177 ? 39.426  -5.186  44.046  1.00 43.69  ? 178 GLN E CG    1 
ATOM   6435  C CD    . GLN E 1 177 ? 39.287  -3.838  44.720  1.00 48.26  ? 178 GLN E CD    1 
ATOM   6436  O OE1   . GLN E 1 177 ? 38.882  -3.736  45.883  1.00 55.99  ? 178 GLN E OE1   1 
ATOM   6437  N NE2   . GLN E 1 177 ? 39.628  -2.783  43.994  1.00 45.95  ? 178 GLN E NE2   1 
ATOM   6438  N N     . PHE E 1 178 ? 38.103  -7.297  47.797  1.00 47.85  ? 179 PHE E N     1 
ATOM   6439  C CA    . PHE E 1 178 ? 37.462  -8.244  48.694  1.00 49.89  ? 179 PHE E CA    1 
ATOM   6440  C C     . PHE E 1 178 ? 36.184  -8.763  48.044  1.00 43.39  ? 179 PHE E C     1 
ATOM   6441  O O     . PHE E 1 178 ? 35.535  -9.663  48.572  1.00 43.84  ? 179 PHE E O     1 
ATOM   6442  C CB    . PHE E 1 178 ? 37.180  -7.566  50.038  1.00 57.35  ? 179 PHE E CB    1 
ATOM   6443  C CG    . PHE E 1 178 ? 38.418  -7.057  50.765  1.00 65.00  ? 179 PHE E CG    1 
ATOM   6444  C CD1   . PHE E 1 178 ? 39.546  -7.858  50.905  1.00 67.18  ? 179 PHE E CD1   1 
ATOM   6445  C CD2   . PHE E 1 178 ? 38.460  -5.765  51.279  1.00 75.18  ? 179 PHE E CD2   1 
ATOM   6446  C CE1   . PHE E 1 178 ? 40.672  -7.387  51.564  1.00 70.48  ? 179 PHE E CE1   1 
ATOM   6447  C CE2   . PHE E 1 178 ? 39.591  -5.299  51.932  1.00 77.63  ? 179 PHE E CE2   1 
ATOM   6448  C CZ    . PHE E 1 178 ? 40.692  -6.110  52.073  1.00 73.43  ? 179 PHE E CZ    1 
ATOM   6449  N N     . HIS E 1 179 ? 35.832  -8.173  46.897  1.00 40.24  ? 180 HIS E N     1 
ATOM   6450  C CA    . HIS E 1 179 ? 34.663  -8.589  46.140  1.00 40.38  ? 180 HIS E CA    1 
ATOM   6451  C C     . HIS E 1 179 ? 34.870  -8.233  44.671  1.00 39.22  ? 180 HIS E C     1 
ATOM   6452  O O     . HIS E 1 179 ? 35.744  -7.437  44.336  1.00 39.34  ? 180 HIS E O     1 
ATOM   6453  C CB    . HIS E 1 179 ? 33.392  -7.949  46.710  1.00 40.68  ? 180 HIS E CB    1 
ATOM   6454  C CG    . HIS E 1 179 ? 33.369  -6.460  46.607  1.00 44.28  ? 180 HIS E CG    1 
ATOM   6455  N ND1   . HIS E 1 179 ? 32.930  -5.800  45.479  1.00 51.81  ? 180 HIS E ND1   1 
ATOM   6456  C CD2   . HIS E 1 179 ? 33.735  -5.508  47.475  1.00 41.99  ? 180 HIS E CD2   1 
ATOM   6457  C CE1   . HIS E 1 179 ? 33.026  -4.493  45.674  1.00 52.76  ? 180 HIS E CE1   1 
ATOM   6458  N NE2   . HIS E 1 179 ? 33.511  -4.294  46.880  1.00 51.11  ? 180 HIS E NE2   1 
ATOM   6459  N N     . THR E 1 180 ? 34.055  -8.838  43.802  1.00 42.80  ? 181 THR E N     1 
ATOM   6460  C CA    . THR E 1 180 ? 34.136  -8.594  42.371  1.00 48.43  ? 181 THR E CA    1 
ATOM   6461  C C     . THR E 1 180 ? 32.973  -7.697  41.957  1.00 50.69  ? 181 THR E C     1 
ATOM   6462  O O     . THR E 1 180 ? 32.388  -7.008  42.789  1.00 46.82  ? 181 THR E O     1 
ATOM   6463  C CB    . THR E 1 180 ? 34.123  -9.927  41.624  1.00 47.11  ? 181 THR E CB    1 
ATOM   6464  O OG1   . THR E 1 180 ? 34.369  -9.609  40.258  1.00 47.83  ? 181 THR E OG1   1 
ATOM   6465  C CG2   . THR E 1 180 ? 32.802  -10.661 41.761  1.00 47.30  ? 181 THR E CG2   1 
ATOM   6466  N N     . SER E 1 181 ? 32.650  -7.715  40.659  1.00 57.92  ? 182 SER E N     1 
ATOM   6467  C CA    . SER E 1 181 ? 31.553  -6.925  40.126  1.00 56.89  ? 182 SER E CA    1 
ATOM   6468  C C     . SER E 1 181 ? 30.570  -7.835  39.395  1.00 58.33  ? 182 SER E C     1 
ATOM   6469  O O     . SER E 1 181 ? 30.876  -8.992  39.118  1.00 52.04  ? 182 SER E O     1 
ATOM   6470  C CB    . SER E 1 181 ? 32.061  -5.830  39.224  1.00 63.74  ? 182 SER E CB    1 
ATOM   6471  O OG    . SER E 1 181 ? 32.780  -6.367  38.123  1.00 67.27  ? 182 SER E OG    1 
ATOM   6472  N N     . SER E 1 182 ? 29.390  -7.289  39.085  1.00 54.59  ? 183 SER E N     1 
ATOM   6473  C CA    . SER E 1 182 ? 28.339  -8.042  38.421  1.00 56.40  ? 183 SER E CA    1 
ATOM   6474  C C     . SER E 1 182 ? 28.766  -8.397  36.999  1.00 51.97  ? 183 SER E C     1 
ATOM   6475  O O     . SER E 1 182 ? 28.370  -9.432  36.469  1.00 49.33  ? 183 SER E O     1 
ATOM   6476  C CB    . SER E 1 182 ? 27.041  -7.276  38.423  1.00 56.81  ? 183 SER E CB    1 
ATOM   6477  O OG    . SER E 1 182 ? 27.167  -6.060  37.699  1.00 57.04  ? 183 SER E OG    1 
ATOM   6478  N N     . ASP E 1 183 ? 29.573  -7.521  36.392  1.00 46.69  ? 184 ASP E N     1 
ATOM   6479  C CA    . ASP E 1 183 ? 30.021  -7.710  35.022  1.00 48.55  ? 184 ASP E CA    1 
ATOM   6480  C C     . ASP E 1 183 ? 30.936  -8.931  34.953  1.00 43.90  ? 184 ASP E C     1 
ATOM   6481  O O     . ASP E 1 183 ? 30.894  -9.687  33.986  1.00 37.29  ? 184 ASP E O     1 
ATOM   6482  C CB    . ASP E 1 183 ? 30.687  -6.454  34.479  1.00 55.65  ? 184 ASP E CB    1 
ATOM   6483  C CG    . ASP E 1 183 ? 31.879  -5.946  35.276  1.00 64.99  ? 184 ASP E CG    1 
ATOM   6484  O OD1   . ASP E 1 183 ? 31.691  -5.617  36.466  1.00 70.51  ? 184 ASP E OD1   1 
ATOM   6485  O OD2   . ASP E 1 183 ? 32.985  -5.880  34.698  1.00 71.07  ? 184 ASP E OD2   1 
ATOM   6486  N N     . ARG E 1 184 ? 31.760  -9.109  35.991  1.00 39.88  ? 185 ARG E N     1 
ATOM   6487  C CA    . ARG E 1 184 ? 32.658  -10.249 36.075  1.00 42.67  ? 185 ARG E CA    1 
ATOM   6488  C C     . ARG E 1 184 ? 31.835  -11.528 36.207  1.00 41.82  ? 185 ARG E C     1 
ATOM   6489  O O     . ARG E 1 184 ? 32.156  -12.545 35.595  1.00 35.23  ? 185 ARG E O     1 
ATOM   6490  C CB    . ARG E 1 184 ? 33.616  -10.099 37.262  1.00 47.47  ? 185 ARG E CB    1 
ATOM   6491  C CG    . ARG E 1 184 ? 34.600  -8.943  37.148  1.00 54.99  ? 185 ARG E CG    1 
ATOM   6492  C CD    . ARG E 1 184 ? 35.602  -9.144  36.020  1.00 61.49  ? 185 ARG E CD    1 
ATOM   6493  N NE    . ARG E 1 184 ? 36.634  -8.101  36.000  1.00 64.67  ? 185 ARG E NE    1 
ATOM   6494  C CZ    . ARG E 1 184 ? 36.903  -7.316  34.963  1.00 71.53  ? 185 ARG E CZ    1 
ATOM   6495  N NH1   . ARG E 1 184 ? 36.218  -7.442  33.840  1.00 72.66  ? 185 ARG E NH1   1 
ATOM   6496  N NH2   . ARG E 1 184 ? 37.858  -6.408  35.053  1.00 72.27  ? 185 ARG E NH2   1 
ATOM   6497  N N     . LEU E 1 185 ? 30.771  -11.456 37.015  1.00 42.74  ? 186 LEU E N     1 
ATOM   6498  C CA    . LEU E 1 185 ? 29.916  -12.602 37.274  1.00 40.34  ? 186 LEU E CA    1 
ATOM   6499  C C     . LEU E 1 185 ? 29.132  -12.948 36.011  1.00 36.69  ? 186 LEU E C     1 
ATOM   6500  O O     . LEU E 1 185 ? 28.823  -14.112 35.768  1.00 34.29  ? 186 LEU E O     1 
ATOM   6501  C CB    . LEU E 1 185 ? 28.987  -12.296 38.448  1.00 42.66  ? 186 LEU E CB    1 
ATOM   6502  C CG    . LEU E 1 185 ? 29.666  -12.050 39.799  1.00 41.27  ? 186 LEU E CG    1 
ATOM   6503  C CD1   . LEU E 1 185 ? 28.638  -11.733 40.872  1.00 38.89  ? 186 LEU E CD1   1 
ATOM   6504  C CD2   . LEU E 1 185 ? 30.517  -13.239 40.212  1.00 40.13  ? 186 LEU E CD2   1 
ATOM   6505  N N     . GLN E 1 186 ? 28.817  -11.922 35.214  1.00 35.76  ? 187 GLN E N     1 
ATOM   6506  C CA    . GLN E 1 186 ? 28.069  -12.106 33.981  1.00 38.21  ? 187 GLN E CA    1 
ATOM   6507  C C     . GLN E 1 186 ? 28.913  -12.900 32.987  1.00 39.08  ? 187 GLN E C     1 
ATOM   6508  O O     . GLN E 1 186 ? 28.385  -13.705 32.224  1.00 38.50  ? 187 GLN E O     1 
ATOM   6509  C CB    . GLN E 1 186 ? 27.656  -10.755 33.398  1.00 39.90  ? 187 GLN E CB    1 
ATOM   6510  C CG    . GLN E 1 186 ? 26.974  -10.847 32.037  1.00 43.26  ? 187 GLN E CG    1 
ATOM   6511  C CD    . GLN E 1 186 ? 25.756  -11.745 32.038  1.00 46.57  ? 187 GLN E CD    1 
ATOM   6512  O OE1   . GLN E 1 186 ? 24.816  -11.557 32.819  1.00 48.79  ? 187 GLN E OE1   1 
ATOM   6513  N NE2   . GLN E 1 186 ? 25.764  -12.738 31.161  1.00 48.15  ? 187 GLN E NE2   1 
ATOM   6514  N N     . ILE E 1 187 ? 30.228  -12.659 33.008  1.00 39.81  ? 188 ILE E N     1 
ATOM   6515  C CA    . ILE E 1 187 ? 31.153  -13.351 32.125  1.00 39.62  ? 188 ILE E CA    1 
ATOM   6516  C C     . ILE E 1 187 ? 31.247  -14.813 32.554  1.00 36.33  ? 188 ILE E C     1 
ATOM   6517  O O     . ILE E 1 187 ? 31.331  -15.707 31.713  1.00 33.86  ? 188 ILE E O     1 
ATOM   6518  C CB    . ILE E 1 187 ? 32.528  -12.657 32.125  1.00 40.41  ? 188 ILE E CB    1 
ATOM   6519  C CG1   . ILE E 1 187 ? 32.447  -11.258 31.507  1.00 41.04  ? 188 ILE E CG1   1 
ATOM   6520  C CG2   . ILE E 1 187 ? 33.579  -13.522 31.428  1.00 40.02  ? 188 ILE E CG2   1 
ATOM   6521  C CD1   . ILE E 1 187 ? 33.755  -10.488 31.537  1.00 41.94  ? 188 ILE E CD1   1 
ATOM   6522  N N     . LEU E 1 188 ? 31.228  -15.043 33.872  1.00 32.05  ? 189 LEU E N     1 
ATOM   6523  C CA    . LEU E 1 188 ? 31.275  -16.388 34.420  1.00 31.96  ? 189 LEU E CA    1 
ATOM   6524  C C     . LEU E 1 188 ? 30.027  -17.152 33.985  1.00 30.32  ? 189 LEU E C     1 
ATOM   6525  O O     . LEU E 1 188 ? 30.100  -18.329 33.640  1.00 29.02  ? 189 LEU E O     1 
ATOM   6526  C CB    . LEU E 1 188 ? 31.390  -16.323 35.943  1.00 31.15  ? 189 LEU E CB    1 
ATOM   6527  C CG    . LEU E 1 188 ? 31.369  -17.669 36.676  1.00 32.43  ? 189 LEU E CG    1 
ATOM   6528  C CD1   . LEU E 1 188 ? 32.540  -18.542 36.258  1.00 33.40  ? 189 LEU E CD1   1 
ATOM   6529  C CD2   . LEU E 1 188 ? 31.365  -17.464 38.182  1.00 34.67  ? 189 LEU E CD2   1 
ATOM   6530  N N     . VAL E 1 189 ? 28.883  -16.462 34.010  1.00 30.23  ? 190 VAL E N     1 
ATOM   6531  C CA    . VAL E 1 189 ? 27.615  -17.057 33.626  1.00 33.02  ? 190 VAL E CA    1 
ATOM   6532  C C     . VAL E 1 189 ? 27.698  -17.498 32.167  1.00 37.30  ? 190 VAL E C     1 
ATOM   6533  O O     . VAL E 1 189 ? 27.254  -18.590 31.818  1.00 36.23  ? 190 VAL E O     1 
ATOM   6534  C CB    . VAL E 1 189 ? 26.443  -16.082 33.849  1.00 31.98  ? 190 VAL E CB    1 
ATOM   6535  C CG1   . VAL E 1 189 ? 25.178  -16.541 33.134  1.00 32.78  ? 190 VAL E CG1   1 
ATOM   6536  C CG2   . VAL E 1 189 ? 26.172  -15.853 35.332  1.00 31.23  ? 190 VAL E CG2   1 
ATOM   6537  N N     . GLU E 1 190 ? 28.270  -16.633 31.322  1.00 36.54  ? 191 GLU E N     1 
ATOM   6538  C CA    . GLU E 1 190 ? 28.404  -16.923 29.904  1.00 42.11  ? 191 GLU E CA    1 
ATOM   6539  C C     . GLU E 1 190 ? 29.306  -18.140 29.720  1.00 36.55  ? 191 GLU E C     1 
ATOM   6540  O O     . GLU E 1 190 ? 29.051  -18.981 28.861  1.00 34.06  ? 191 GLU E O     1 
ATOM   6541  C CB    . GLU E 1 190 ? 28.957  -15.713 29.152  1.00 48.33  ? 191 GLU E CB    1 
ATOM   6542  C CG    . GLU E 1 190 ? 28.014  -14.513 29.159  1.00 55.30  ? 191 GLU E CG    1 
ATOM   6543  C CD    . GLU E 1 190 ? 28.514  -13.321 28.364  1.00 59.65  ? 191 GLU E CD    1 
ATOM   6544  O OE1   . GLU E 1 190 ? 29.635  -13.400 27.817  1.00 64.83  ? 191 GLU E OE1   1 
ATOM   6545  O OE2   . GLU E 1 190 ? 27.779  -12.314 28.287  1.00 62.18  ? 191 GLU E OE2   1 
ATOM   6546  N N     . GLN E 1 191 ? 30.357  -18.221 30.543  1.00 32.81  ? 192 GLN E N     1 
ATOM   6547  C CA    . GLN E 1 191 ? 31.315  -19.311 30.471  1.00 33.62  ? 192 GLN E CA    1 
ATOM   6548  C C     . GLN E 1 191 ? 30.628  -20.622 30.845  1.00 35.62  ? 192 GLN E C     1 
ATOM   6549  O O     . GLN E 1 191 ? 30.811  -21.636 30.175  1.00 35.33  ? 192 GLN E O     1 
ATOM   6550  C CB    . GLN E 1 191 ? 32.498  -19.037 31.400  1.00 34.87  ? 192 GLN E CB    1 
ATOM   6551  C CG    . GLN E 1 191 ? 33.561  -20.130 31.391  1.00 36.24  ? 192 GLN E CG    1 
ATOM   6552  C CD    . GLN E 1 191 ? 34.637  -19.914 32.433  1.00 35.97  ? 192 GLN E CD    1 
ATOM   6553  O OE1   . GLN E 1 191 ? 34.590  -18.962 33.220  1.00 37.43  ? 192 GLN E OE1   1 
ATOM   6554  N NE2   . GLN E 1 191 ? 35.619  -20.805 32.451  1.00 32.77  ? 192 GLN E NE2   1 
ATOM   6555  N N     . LEU E 1 192 ? 29.842  -20.588 31.927  1.00 34.44  ? 193 LEU E N     1 
ATOM   6556  C CA    . LEU E 1 192 ? 29.174  -21.775 32.434  1.00 32.06  ? 193 LEU E CA    1 
ATOM   6557  C C     . LEU E 1 192 ? 28.092  -22.218 31.451  1.00 30.93  ? 193 LEU E C     1 
ATOM   6558  O O     . LEU E 1 192 ? 27.672  -23.373 31.465  1.00 25.70  ? 193 LEU E O     1 
ATOM   6559  C CB    . LEU E 1 192 ? 28.583  -21.496 33.816  1.00 33.20  ? 193 LEU E CB    1 
ATOM   6560  C CG    . LEU E 1 192 ? 29.588  -21.294 34.954  1.00 34.52  ? 193 LEU E CG    1 
ATOM   6561  C CD1   . LEU E 1 192 ? 28.868  -21.022 36.263  1.00 32.25  ? 193 LEU E CD1   1 
ATOM   6562  C CD2   . LEU E 1 192 ? 30.509  -22.494 35.093  1.00 36.52  ? 193 LEU E CD2   1 
ATOM   6563  N N     . ASN E 1 193 ? 27.651  -21.288 30.599  1.00 32.54  ? 194 ASN E N     1 
ATOM   6564  C CA    . ASN E 1 193 ? 26.540  -21.540 29.695  1.00 35.87  ? 194 ASN E CA    1 
ATOM   6565  C C     . ASN E 1 193 ? 26.948  -22.587 28.660  1.00 37.96  ? 194 ASN E C     1 
ATOM   6566  O O     . ASN E 1 193 ? 26.117  -23.046 27.880  1.00 33.73  ? 194 ASN E O     1 
ATOM   6567  C CB    . ASN E 1 193 ? 26.053  -20.254 29.037  1.00 38.31  ? 194 ASN E CB    1 
ATOM   6568  C CG    . ASN E 1 193 ? 24.804  -20.473 28.217  1.00 41.42  ? 194 ASN E CG    1 
ATOM   6569  O OD1   . ASN E 1 193 ? 23.811  -21.003 28.725  1.00 46.30  ? 194 ASN E OD1   1 
ATOM   6570  N ND2   . ASN E 1 193 ? 24.834  -20.081 26.951  1.00 43.46  ? 194 ASN E ND2   1 
ATOM   6571  N N     . GLN E 1 194 ? 28.233  -22.956 28.666  1.00 37.72  ? 195 GLN E N     1 
ATOM   6572  C CA    . GLN E 1 194 ? 28.745  -23.972 27.762  1.00 39.68  ? 195 GLN E CA    1 
ATOM   6573  C C     . GLN E 1 194 ? 28.190  -25.335 28.162  1.00 42.84  ? 195 GLN E C     1 
ATOM   6574  O O     . GLN E 1 194 ? 28.054  -26.224 27.324  1.00 43.30  ? 195 GLN E O     1 
ATOM   6575  C CB    . GLN E 1 194 ? 30.273  -24.017 27.791  1.00 41.73  ? 195 GLN E CB    1 
ATOM   6576  C CG    . GLN E 1 194 ? 30.947  -22.734 27.318  1.00 40.51  ? 195 GLN E CG    1 
ATOM   6577  C CD    . GLN E 1 194 ? 32.457  -22.796 27.402  1.00 38.96  ? 195 GLN E CD    1 
ATOM   6578  O OE1   . GLN E 1 194 ? 33.102  -23.660 26.797  1.00 41.17  ? 195 GLN E OE1   1 
ATOM   6579  N NE2   . GLN E 1 194 ? 33.036  -21.879 28.163  1.00 37.65  ? 195 GLN E NE2   1 
ATOM   6580  N N     . TRP E 1 195 ? 27.874  -25.485 29.453  1.00 41.37  ? 196 TRP E N     1 
ATOM   6581  C CA    . TRP E 1 195 ? 27.478  -26.772 30.000  1.00 38.61  ? 196 TRP E CA    1 
ATOM   6582  C C     . TRP E 1 195 ? 26.104  -26.674 30.660  1.00 34.63  ? 196 TRP E C     1 
ATOM   6583  O O     . TRP E 1 195 ? 25.353  -27.646 30.677  1.00 31.98  ? 196 TRP E O     1 
ATOM   6584  C CB    . TRP E 1 195 ? 28.533  -27.267 30.999  1.00 41.09  ? 196 TRP E CB    1 
ATOM   6585  C CG    . TRP E 1 195 ? 29.921  -27.373 30.422  1.00 38.62  ? 196 TRP E CG    1 
ATOM   6586  C CD1   . TRP E 1 195 ? 30.441  -28.425 29.728  1.00 40.22  ? 196 TRP E CD1   1 
ATOM   6587  C CD2   . TRP E 1 195 ? 30.975  -26.388 30.507  1.00 36.95  ? 196 TRP E CD2   1 
ATOM   6588  N NE1   . TRP E 1 195 ? 31.736  -28.164 29.366  1.00 41.58  ? 196 TRP E NE1   1 
ATOM   6589  C CE2   . TRP E 1 195 ? 32.092  -26.925 29.831  1.00 36.74  ? 196 TRP E CE2   1 
ATOM   6590  C CE3   . TRP E 1 195 ? 31.083  -25.116 31.081  1.00 38.98  ? 196 TRP E CE3   1 
ATOM   6591  C CZ2   . TRP E 1 195 ? 33.295  -26.232 29.716  1.00 35.49  ? 196 TRP E CZ2   1 
ATOM   6592  C CZ3   . TRP E 1 195 ? 32.275  -24.434 30.967  1.00 34.30  ? 196 TRP E CZ3   1 
ATOM   6593  C CH2   . TRP E 1 195 ? 33.364  -24.986 30.295  1.00 33.59  ? 196 TRP E CH2   1 
ATOM   6594  N N     . TYR E 1 196 ? 25.782  -25.491 31.195  1.00 31.91  ? 197 TYR E N     1 
ATOM   6595  C CA    . TYR E 1 196 ? 24.578  -25.315 31.991  1.00 31.93  ? 197 TYR E CA    1 
ATOM   6596  C C     . TYR E 1 196 ? 23.668  -24.276 31.344  1.00 32.41  ? 197 TYR E C     1 
ATOM   6597  O O     . TYR E 1 196 ? 24.115  -23.189 30.983  1.00 34.27  ? 197 TYR E O     1 
ATOM   6598  C CB    . TYR E 1 196 ? 24.962  -24.903 33.416  1.00 28.58  ? 197 TYR E CB    1 
ATOM   6599  C CG    . TYR E 1 196 ? 25.914  -25.867 34.107  1.00 29.18  ? 197 TYR E CG    1 
ATOM   6600  C CD1   . TYR E 1 196 ? 25.440  -26.994 34.766  1.00 29.66  ? 197 TYR E CD1   1 
ATOM   6601  C CD2   . TYR E 1 196 ? 27.287  -25.651 34.098  1.00 28.79  ? 197 TYR E CD2   1 
ATOM   6602  C CE1   . TYR E 1 196 ? 26.301  -27.879 35.393  1.00 30.37  ? 197 TYR E CE1   1 
ATOM   6603  C CE2   . TYR E 1 196 ? 28.159  -26.528 34.723  1.00 30.05  ? 197 TYR E CE2   1 
ATOM   6604  C CZ    . TYR E 1 196 ? 27.664  -27.645 35.371  1.00 29.07  ? 197 TYR E CZ    1 
ATOM   6605  O OH    . TYR E 1 196 ? 28.517  -28.512 35.990  1.00 36.55  ? 197 TYR E OH    1 
ATOM   6606  N N     . PRO E 1 197 ? 22.360  -24.581 31.183  1.00 33.90  ? 198 PRO E N     1 
ATOM   6607  C CA    . PRO E 1 197 ? 21.390  -23.593 30.712  1.00 36.51  ? 198 PRO E CA    1 
ATOM   6608  C C     . PRO E 1 197 ? 21.363  -22.372 31.628  1.00 37.10  ? 198 PRO E C     1 
ATOM   6609  O O     . PRO E 1 197 ? 21.840  -22.431 32.759  1.00 39.57  ? 198 PRO E O     1 
ATOM   6610  C CB    . PRO E 1 197 ? 20.053  -24.362 30.714  1.00 39.59  ? 198 PRO E CB    1 
ATOM   6611  C CG    . PRO E 1 197 ? 20.460  -25.823 30.638  1.00 40.31  ? 198 PRO E CG    1 
ATOM   6612  C CD    . PRO E 1 197 ? 21.764  -25.905 31.412  1.00 36.10  ? 198 PRO E CD    1 
ATOM   6613  N N     . LEU E 1 198 ? 20.797  -21.269 31.128  1.00 40.18  ? 199 LEU E N     1 
ATOM   6614  C CA    . LEU E 1 198 ? 20.760  -20.020 31.870  1.00 42.37  ? 199 LEU E CA    1 
ATOM   6615  C C     . LEU E 1 198 ? 19.705  -20.106 32.969  1.00 44.97  ? 199 LEU E C     1 
ATOM   6616  O O     . LEU E 1 198 ? 19.777  -19.382 33.960  1.00 44.90  ? 199 LEU E O     1 
ATOM   6617  C CB    . LEU E 1 198 ? 20.486  -18.853 30.921  1.00 44.58  ? 199 LEU E CB    1 
ATOM   6618  C CG    . LEU E 1 198 ? 21.567  -18.576 29.871  1.00 45.96  ? 199 LEU E CG    1 
ATOM   6619  C CD1   . LEU E 1 198 ? 21.251  -17.316 29.082  1.00 42.38  ? 199 LEU E CD1   1 
ATOM   6620  C CD2   . LEU E 1 198 ? 22.938  -18.476 30.517  1.00 47.47  ? 199 LEU E CD2   1 
ATOM   6621  N N     . ASP E 1 199 ? 18.732  -21.006 32.786  1.00 45.52  ? 200 ASP E N     1 
ATOM   6622  C CA    . ASP E 1 199 ? 17.641  -21.157 33.733  1.00 47.72  ? 200 ASP E CA    1 
ATOM   6623  C C     . ASP E 1 199 ? 17.938  -22.323 34.673  1.00 46.70  ? 200 ASP E C     1 
ATOM   6624  O O     . ASP E 1 199 ? 17.062  -22.764 35.414  1.00 43.30  ? 200 ASP E O     1 
ATOM   6625  C CB    . ASP E 1 199 ? 16.310  -21.338 33.020  1.00 48.57  ? 200 ASP E CB    1 
ATOM   6626  C CG    . ASP E 1 199 ? 16.183  -22.607 32.189  1.00 50.45  ? 200 ASP E CG    1 
ATOM   6627  O OD1   . ASP E 1 199 ? 17.132  -23.419 32.209  1.00 51.81  ? 200 ASP E OD1   1 
ATOM   6628  O OD2   . ASP E 1 199 ? 15.137  -22.770 31.526  1.00 54.69  ? 200 ASP E OD2   1 
ATOM   6629  N N     . HIS E 1 200 ? 19.180  -22.816 34.629  1.00 41.75  ? 201 HIS E N     1 
ATOM   6630  C CA    . HIS E 1 200 ? 19.606  -23.896 35.503  1.00 40.83  ? 201 HIS E CA    1 
ATOM   6631  C C     . HIS E 1 200 ? 19.664  -23.378 36.937  1.00 37.23  ? 201 HIS E C     1 
ATOM   6632  O O     . HIS E 1 200 ? 20.299  -22.363 37.209  1.00 35.23  ? 201 HIS E O     1 
ATOM   6633  C CB    . HIS E 1 200 ? 20.948  -24.474 35.041  1.00 42.01  ? 201 HIS E CB    1 
ATOM   6634  C CG    . HIS E 1 200 ? 21.434  -25.607 35.885  1.00 40.05  ? 201 HIS E CG    1 
ATOM   6635  N ND1   . HIS E 1 200 ? 20.949  -26.890 35.757  1.00 40.00  ? 201 HIS E ND1   1 
ATOM   6636  C CD2   . HIS E 1 200 ? 22.333  -25.648 36.878  1.00 39.03  ? 201 HIS E CD2   1 
ATOM   6637  C CE1   . HIS E 1 200 ? 21.553  -27.675 36.638  1.00 41.79  ? 201 HIS E CE1   1 
ATOM   6638  N NE2   . HIS E 1 200 ? 22.398  -26.942 37.328  1.00 40.37  ? 201 HIS E NE2   1 
ATOM   6639  N N     . GLU E 1 201 ? 18.984  -24.088 37.843  1.00 34.55  ? 202 GLU E N     1 
ATOM   6640  C CA    . GLU E 1 201 ? 18.898  -23.677 39.234  1.00 35.95  ? 202 GLU E CA    1 
ATOM   6641  C C     . GLU E 1 201 ? 20.233  -23.938 39.925  1.00 29.34  ? 202 GLU E C     1 
ATOM   6642  O O     . GLU E 1 201 ? 20.709  -25.070 39.953  1.00 24.27  ? 202 GLU E O     1 
ATOM   6643  C CB    . GLU E 1 201 ? 17.770  -24.423 39.948  1.00 36.03  ? 202 GLU E CB    1 
ATOM   6644  C CG    . GLU E 1 201 ? 17.599  -24.005 41.406  1.00 42.38  ? 202 GLU E CG    1 
ATOM   6645  C CD    . GLU E 1 201 ? 16.542  -24.790 42.161  1.00 45.31  ? 202 GLU E CD    1 
ATOM   6646  O OE1   . GLU E 1 201 ? 15.553  -24.173 42.608  1.00 46.76  ? 202 GLU E OE1   1 
ATOM   6647  O OE2   . GLU E 1 201 ? 16.713  -26.019 42.308  1.00 44.45  ? 202 GLU E OE2   1 
ATOM   6648  N N     . VAL E 1 202 ? 20.824  -22.871 40.476  1.00 30.00  ? 203 VAL E N     1 
ATOM   6649  C CA    . VAL E 1 202 ? 22.047  -22.977 41.256  1.00 28.65  ? 203 VAL E CA    1 
ATOM   6650  C C     . VAL E 1 202 ? 21.726  -22.611 42.703  1.00 28.06  ? 203 VAL E C     1 
ATOM   6651  O O     . VAL E 1 202 ? 20.627  -22.148 42.999  1.00 28.94  ? 203 VAL E O     1 
ATOM   6652  C CB    . VAL E 1 202 ? 23.173  -22.091 40.689  1.00 32.23  ? 203 VAL E CB    1 
ATOM   6653  C CG1   . VAL E 1 202 ? 23.661  -22.598 39.336  1.00 36.26  ? 203 VAL E CG1   1 
ATOM   6654  C CG2   . VAL E 1 202 ? 22.757  -20.628 40.598  1.00 32.32  ? 203 VAL E CG2   1 
ATOM   6655  N N     . VAL E 1 203 ? 22.698  -22.822 43.598  1.00 25.29  ? 204 VAL E N     1 
ATOM   6656  C CA    . VAL E 1 203 ? 22.475  -22.640 45.022  1.00 22.80  ? 204 VAL E CA    1 
ATOM   6657  C C     . VAL E 1 203 ? 23.636  -21.852 45.622  1.00 23.57  ? 204 VAL E C     1 
ATOM   6658  O O     . VAL E 1 203 ? 24.789  -22.264 45.527  1.00 24.85  ? 204 VAL E O     1 
ATOM   6659  C CB    . VAL E 1 203 ? 22.304  -23.997 45.733  1.00 23.77  ? 204 VAL E CB    1 
ATOM   6660  C CG1   . VAL E 1 203 ? 22.141  -23.833 47.239  1.00 25.97  ? 204 VAL E CG1   1 
ATOM   6661  C CG2   . VAL E 1 203 ? 21.147  -24.801 45.152  1.00 23.27  ? 204 VAL E CG2   1 
ATOM   6662  N N     . ILE E 1 204 ? 23.310  -20.711 46.240  1.00 23.97  ? 205 ILE E N     1 
ATOM   6663  C CA    . ILE E 1 204 ? 24.272  -19.966 47.033  1.00 24.15  ? 205 ILE E CA    1 
ATOM   6664  C C     . ILE E 1 204 ? 24.187  -20.467 48.471  1.00 24.56  ? 205 ILE E C     1 
ATOM   6665  O O     . ILE E 1 204 ? 23.178  -20.265 49.141  1.00 28.79  ? 205 ILE E O     1 
ATOM   6666  C CB    . ILE E 1 204 ? 24.018  -18.450 46.944  1.00 22.69  ? 205 ILE E CB    1 
ATOM   6667  C CG1   . ILE E 1 204 ? 24.142  -17.942 45.509  1.00 22.36  ? 205 ILE E CG1   1 
ATOM   6668  C CG2   . ILE E 1 204 ? 24.942  -17.690 47.895  1.00 22.47  ? 205 ILE E CG2   1 
ATOM   6669  C CD1   . ILE E 1 204 ? 23.812  -16.469 45.342  1.00 24.64  ? 205 ILE E CD1   1 
ATOM   6670  N N     . TYR E 1 205 ? 25.252  -21.133 48.926  1.00 25.56  ? 206 TYR E N     1 
ATOM   6671  C CA    . TYR E 1 205 ? 25.258  -21.751 50.241  1.00 25.56  ? 206 TYR E CA    1 
ATOM   6672  C C     . TYR E 1 205 ? 26.192  -20.979 51.167  1.00 25.78  ? 206 TYR E C     1 
ATOM   6673  O O     . TYR E 1 205 ? 27.273  -20.561 50.761  1.00 28.38  ? 206 TYR E O     1 
ATOM   6674  C CB    . TYR E 1 205 ? 25.674  -23.223 50.150  1.00 24.45  ? 206 TYR E CB    1 
ATOM   6675  C CG    . TYR E 1 205 ? 25.962  -23.870 51.499  1.00 26.50  ? 206 TYR E CG    1 
ATOM   6676  C CD1   . TYR E 1 205 ? 24.931  -24.231 52.357  1.00 28.84  ? 206 TYR E CD1   1 
ATOM   6677  C CD2   . TYR E 1 205 ? 27.265  -24.130 51.908  1.00 25.80  ? 206 TYR E CD2   1 
ATOM   6678  C CE1   . TYR E 1 205 ? 25.186  -24.820 53.586  1.00 27.59  ? 206 TYR E CE1   1 
ATOM   6679  C CE2   . TYR E 1 205 ? 27.533  -24.721 53.132  1.00 26.27  ? 206 TYR E CE2   1 
ATOM   6680  C CZ    . TYR E 1 205 ? 26.491  -25.067 53.973  1.00 28.59  ? 206 TYR E CZ    1 
ATOM   6681  O OH    . TYR E 1 205 ? 26.753  -25.647 55.181  1.00 34.85  ? 206 TYR E OH    1 
ATOM   6682  N N     . GLU E 1 206 ? 25.752  -20.813 52.419  1.00 25.85  ? 207 GLU E N     1 
ATOM   6683  C CA    . GLU E 1 206 ? 26.574  -20.229 53.464  1.00 25.31  ? 207 GLU E CA    1 
ATOM   6684  C C     . GLU E 1 206 ? 26.331  -20.986 54.766  1.00 26.63  ? 207 GLU E C     1 
ATOM   6685  O O     . GLU E 1 206 ? 25.280  -20.841 55.386  1.00 27.65  ? 207 GLU E O     1 
ATOM   6686  C CB    . GLU E 1 206 ? 26.258  -18.745 53.655  1.00 26.04  ? 207 GLU E CB    1 
ATOM   6687  C CG    . GLU E 1 206 ? 26.556  -17.894 52.425  1.00 29.23  ? 207 GLU E CG    1 
ATOM   6688  C CD    . GLU E 1 206 ? 26.270  -16.417 52.618  1.00 31.86  ? 207 GLU E CD    1 
ATOM   6689  O OE1   . GLU E 1 206 ? 25.832  -16.037 53.727  1.00 31.16  ? 207 GLU E OE1   1 
ATOM   6690  O OE2   . GLU E 1 206 ? 26.482  -15.645 51.660  1.00 30.12  ? 207 GLU E OE2   1 
ATOM   6691  N N     . ALA E 1 207 ? 27.310  -21.804 55.163  1.00 28.72  ? 208 ALA E N     1 
ATOM   6692  C CA    . ALA E 1 207 ? 27.242  -22.522 56.424  1.00 31.91  ? 208 ALA E CA    1 
ATOM   6693  C C     . ALA E 1 207 ? 27.117  -21.520 57.567  1.00 28.19  ? 208 ALA E C     1 
ATOM   6694  O O     . ALA E 1 207 ? 27.697  -20.438 57.515  1.00 30.57  ? 208 ALA E O     1 
ATOM   6695  C CB    . ALA E 1 207 ? 28.463  -23.399 56.590  1.00 30.99  ? 208 ALA E CB    1 
ATOM   6696  N N     . ALA E 1 208 ? 26.340  -21.890 58.589  1.00 27.55  ? 209 ALA E N     1 
ATOM   6697  C CA    . ALA E 1 208 ? 26.155  -21.046 59.757  1.00 27.59  ? 209 ALA E CA    1 
ATOM   6698  C C     . ALA E 1 208 ? 27.419  -21.075 60.610  1.00 25.23  ? 209 ALA E C     1 
ATOM   6699  O O     . ALA E 1 208 ? 28.095  -22.097 60.692  1.00 27.64  ? 209 ALA E O     1 
ATOM   6700  C CB    . ALA E 1 208 ? 24.945  -21.506 60.539  1.00 28.46  ? 209 ALA E CB    1 
ATOM   6701  N N     . ASN E 1 209 ? 27.733  -19.935 61.231  1.00 23.70  ? 210 ASN E N     1 
ATOM   6702  C CA    . ASN E 1 209 ? 28.889  -19.829 62.104  1.00 25.55  ? 210 ASN E CA    1 
ATOM   6703  C C     . ASN E 1 209 ? 28.435  -19.895 63.560  1.00 24.32  ? 210 ASN E C     1 
ATOM   6704  O O     . ASN E 1 209 ? 29.234  -20.180 64.449  1.00 27.83  ? 210 ASN E O     1 
ATOM   6705  C CB    . ASN E 1 209 ? 29.689  -18.562 61.820  1.00 24.97  ? 210 ASN E CB    1 
ATOM   6706  C CG    . ASN E 1 209 ? 30.337  -18.592 60.456  1.00 24.63  ? 210 ASN E CG    1 
ATOM   6707  O OD1   . ASN E 1 209 ? 31.153  -19.477 60.174  1.00 26.20  ? 210 ASN E OD1   1 
ATOM   6708  N ND2   . ASN E 1 209 ? 29.993  -17.642 59.601  1.00 26.75  ? 210 ASN E ND2   1 
ATOM   6709  N N     . LEU E 1 210 ? 27.141  -19.638 63.788  1.00 24.65  ? 211 LEU E N     1 
ATOM   6710  C CA    . LEU E 1 210 ? 26.583  -19.614 65.131  1.00 26.98  ? 211 LEU E CA    1 
ATOM   6711  C C     . LEU E 1 210 ? 25.550  -20.728 65.282  1.00 24.29  ? 211 LEU E C     1 
ATOM   6712  O O     . LEU E 1 210 ? 24.900  -21.115 64.312  1.00 22.00  ? 211 LEU E O     1 
ATOM   6713  C CB    . LEU E 1 210 ? 25.972  -18.241 65.408  1.00 30.20  ? 211 LEU E CB    1 
ATOM   6714  C CG    . LEU E 1 210 ? 26.960  -17.071 65.475  1.00 32.69  ? 211 LEU E CG    1 
ATOM   6715  C CD1   . LEU E 1 210 ? 26.250  -15.777 65.836  1.00 35.15  ? 211 LEU E CD1   1 
ATOM   6716  C CD2   . LEU E 1 210 ? 28.074  -17.364 66.464  1.00 37.39  ? 211 LEU E CD2   1 
ATOM   6717  N N     . PRO E 1 211 ? 25.362  -21.264 66.511  1.00 20.98  ? 212 PRO E N     1 
ATOM   6718  C CA    . PRO E 1 211 ? 24.427  -22.367 66.746  1.00 22.45  ? 212 PRO E CA    1 
ATOM   6719  C C     . PRO E 1 211 ? 22.954  -21.962 66.693  1.00 26.06  ? 212 PRO E C     1 
ATOM   6720  O O     . PRO E 1 211 ? 22.073  -22.819 66.635  1.00 27.44  ? 212 PRO E O     1 
ATOM   6721  C CB    . PRO E 1 211 ? 24.844  -22.855 68.148  1.00 23.07  ? 212 PRO E CB    1 
ATOM   6722  C CG    . PRO E 1 211 ? 25.356  -21.606 68.834  1.00 22.39  ? 212 PRO E CG    1 
ATOM   6723  C CD    . PRO E 1 211 ? 26.060  -20.834 67.733  1.00 23.20  ? 212 PRO E CD    1 
ATOM   6724  N N     . ILE E 1 212 ? 22.699  -20.651 66.722  1.00 27.73  ? 213 ILE E N     1 
ATOM   6725  C CA    . ILE E 1 212 ? 21.344  -20.130 66.654  1.00 28.57  ? 213 ILE E CA    1 
ATOM   6726  C C     . ILE E 1 212 ? 21.088  -19.611 65.243  1.00 26.80  ? 213 ILE E C     1 
ATOM   6727  O O     . ILE E 1 212 ? 20.026  -19.062 64.958  1.00 26.68  ? 213 ILE E O     1 
ATOM   6728  C CB    . ILE E 1 212 ? 21.124  -19.036 67.716  1.00 31.44  ? 213 ILE E CB    1 
ATOM   6729  C CG1   . ILE E 1 212 ? 22.111  -17.879 67.550  1.00 32.84  ? 213 ILE E CG1   1 
ATOM   6730  C CG2   . ILE E 1 212 ? 21.181  -19.625 69.126  1.00 35.58  ? 213 ILE E CG2   1 
ATOM   6731  C CD1   . ILE E 1 212 ? 21.994  -17.147 66.225  1.00 34.45  ? 213 ILE E CD1   1 
ATOM   6732  N N     . GLN E 1 213 ? 22.074  -19.804 64.363  1.00 29.37  ? 214 GLN E N     1 
ATOM   6733  C CA    . GLN E 1 213 ? 22.009  -19.289 63.007  1.00 30.28  ? 214 GLN E CA    1 
ATOM   6734  C C     . GLN E 1 213 ? 21.611  -20.410 62.053  1.00 33.03  ? 214 GLN E C     1 
ATOM   6735  O O     . GLN E 1 213 ? 22.105  -21.530 62.160  1.00 40.43  ? 214 GLN E O     1 
ATOM   6736  C CB    . GLN E 1 213 ? 23.360  -18.694 62.615  1.00 34.09  ? 214 GLN E CB    1 
ATOM   6737  C CG    . GLN E 1 213 ? 23.408  -18.138 61.197  1.00 36.37  ? 214 GLN E CG    1 
ATOM   6738  C CD    . GLN E 1 213 ? 24.798  -17.714 60.777  1.00 35.38  ? 214 GLN E CD    1 
ATOM   6739  O OE1   . GLN E 1 213 ? 25.774  -17.878 61.517  1.00 34.36  ? 214 GLN E OE1   1 
ATOM   6740  N NE2   . GLN E 1 213 ? 24.903  -17.171 59.572  1.00 36.97  ? 214 GLN E NE2   1 
ATOM   6741  N N     . ALA E 1 214 ? 20.705  -20.089 61.124  1.00 37.70  ? 215 ALA E N     1 
ATOM   6742  C CA    . ALA E 1 214 ? 20.315  -21.011 60.072  1.00 36.92  ? 215 ALA E CA    1 
ATOM   6743  C C     . ALA E 1 214 ? 21.216  -20.800 58.859  1.00 34.90  ? 215 ALA E C     1 
ATOM   6744  O O     . ALA E 1 214 ? 21.614  -19.675 58.565  1.00 32.27  ? 215 ALA E O     1 
ATOM   6745  C CB    . ALA E 1 214 ? 18.857  -20.810 59.722  1.00 41.09  ? 215 ALA E CB    1 
ATOM   6746  N N     . PRO E 1 215 ? 21.570  -21.873 58.119  1.00 33.13  ? 216 PRO E N     1 
ATOM   6747  C CA    . PRO E 1 215 ? 22.402  -21.735 56.925  1.00 35.33  ? 216 PRO E CA    1 
ATOM   6748  C C     . PRO E 1 215 ? 21.658  -21.013 55.806  1.00 31.05  ? 216 PRO E C     1 
ATOM   6749  O O     . PRO E 1 215 ? 20.430  -21.034 55.756  1.00 32.46  ? 216 PRO E O     1 
ATOM   6750  C CB    . PRO E 1 215 ? 22.737  -23.193 56.564  1.00 32.75  ? 216 PRO E CB    1 
ATOM   6751  C CG    . PRO E 1 215 ? 21.564  -23.984 57.109  1.00 32.73  ? 216 PRO E CG    1 
ATOM   6752  C CD    . PRO E 1 215 ? 21.180  -23.265 58.392  1.00 31.36  ? 216 PRO E CD    1 
ATOM   6753  N N     . ARG E 1 216 ? 22.420  -20.367 54.919  1.00 31.09  ? 217 ARG E N     1 
ATOM   6754  C CA    . ARG E 1 216 ? 21.854  -19.727 53.745  1.00 28.50  ? 217 ARG E CA    1 
ATOM   6755  C C     . ARG E 1 216 ? 21.820  -20.738 52.604  1.00 27.54  ? 217 ARG E C     1 
ATOM   6756  O O     . ARG E 1 216 ? 22.855  -21.267 52.207  1.00 23.38  ? 217 ARG E O     1 
ATOM   6757  C CB    . ARG E 1 216 ? 22.670  -18.495 53.341  1.00 27.32  ? 217 ARG E CB    1 
ATOM   6758  C CG    . ARG E 1 216 ? 22.120  -17.765 52.124  1.00 28.79  ? 217 ARG E CG    1 
ATOM   6759  C CD    . ARG E 1 216 ? 23.072  -16.695 51.614  1.00 28.45  ? 217 ARG E CD    1 
ATOM   6760  N NE    . ARG E 1 216 ? 22.500  -15.922 50.505  1.00 29.92  ? 217 ARG E NE    1 
ATOM   6761  C CZ    . ARG E 1 216 ? 23.144  -14.973 49.835  1.00 30.54  ? 217 ARG E CZ    1 
ATOM   6762  N NH1   . ARG E 1 216 ? 24.406  -14.704 50.118  1.00 31.46  ? 217 ARG E NH1   1 
ATOM   6763  N NH2   . ARG E 1 216 ? 22.528  -14.306 48.876  1.00 29.82  ? 217 ARG E NH2   1 
ATOM   6764  N N     . ILE E 1 217 ? 20.613  -21.013 52.101  1.00 31.09  ? 218 ILE E N     1 
ATOM   6765  C CA    . ILE E 1 217 ? 20.436  -21.887 50.955  1.00 34.26  ? 218 ILE E CA    1 
ATOM   6766  C C     . ILE E 1 217 ? 19.526  -21.183 49.954  1.00 36.60  ? 218 ILE E C     1 
ATOM   6767  O O     . ILE E 1 217 ? 18.327  -21.446 49.906  1.00 39.23  ? 218 ILE E O     1 
ATOM   6768  C CB    . ILE E 1 217 ? 19.872  -23.256 51.381  1.00 36.91  ? 218 ILE E CB    1 
ATOM   6769  C CG1   . ILE E 1 217 ? 20.718  -23.896 52.480  1.00 38.62  ? 218 ILE E CG1   1 
ATOM   6770  C CG2   . ILE E 1 217 ? 19.717  -24.182 50.174  1.00 38.61  ? 218 ILE E CG2   1 
ATOM   6771  C CD1   . ILE E 1 217 ? 20.213  -25.253 52.938  1.00 42.74  ? 218 ILE E CD1   1 
ATOM   6772  N N     . GLU E 1 218 ? 20.117  -20.278 49.166  1.00 37.78  ? 219 GLU E N     1 
ATOM   6773  C CA    . GLU E 1 218 ? 19.363  -19.469 48.224  1.00 39.24  ? 219 GLU E CA    1 
ATOM   6774  C C     . GLU E 1 218 ? 19.421  -20.110 46.841  1.00 37.57  ? 219 GLU E C     1 
ATOM   6775  O O     . GLU E 1 218 ? 20.490  -20.216 46.242  1.00 35.73  ? 219 GLU E O     1 
ATOM   6776  C CB    . GLU E 1 218 ? 19.909  -18.041 48.192  1.00 44.60  ? 219 GLU E CB    1 
ATOM   6777  C CG    . GLU E 1 218 ? 19.145  -17.124 47.242  1.00 47.30  ? 219 GLU E CG    1 
ATOM   6778  C CD    . GLU E 1 218 ? 19.646  -15.692 47.221  1.00 54.39  ? 219 GLU E CD    1 
ATOM   6779  O OE1   . GLU E 1 218 ? 20.569  -15.377 48.001  1.00 56.71  ? 219 GLU E OE1   1 
ATOM   6780  O OE2   . GLU E 1 218 ? 19.118  -14.893 46.419  1.00 62.69  ? 219 GLU E OE2   1 
ATOM   6781  N N     . ARG E 1 219 ? 18.252  -20.529 46.348  1.00 32.85  ? 220 ARG E N     1 
ATOM   6782  C CA    . ARG E 1 219 ? 18.135  -21.121 45.027  1.00 33.35  ? 220 ARG E CA    1 
ATOM   6783  C C     . ARG E 1 219 ? 17.704  -20.044 44.037  1.00 34.26  ? 220 ARG E C     1 
ATOM   6784  O O     . ARG E 1 219 ? 16.832  -19.231 44.337  1.00 35.39  ? 220 ARG E O     1 
ATOM   6785  C CB    . ARG E 1 219 ? 17.131  -22.280 45.055  1.00 35.91  ? 220 ARG E CB    1 
ATOM   6786  C CG    . ARG E 1 219 ? 17.492  -23.394 46.027  1.00 38.11  ? 220 ARG E CG    1 
ATOM   6787  C CD    . ARG E 1 219 ? 16.381  -24.425 46.157  1.00 44.53  ? 220 ARG E CD    1 
ATOM   6788  N NE    . ARG E 1 219 ? 16.693  -25.463 47.146  1.00 43.50  ? 220 ARG E NE    1 
ATOM   6789  C CZ    . ARG E 1 219 ? 17.649  -26.375 47.012  1.00 49.80  ? 220 ARG E CZ    1 
ATOM   6790  N NH1   . ARG E 1 219 ? 18.371  -26.424 45.907  1.00 48.72  ? 220 ARG E NH1   1 
ATOM   6791  N NH2   . ARG E 1 219 ? 17.869  -27.247 47.980  1.00 53.61  ? 220 ARG E NH2   1 
ATOM   6792  N N     . LEU E 1 220 ? 18.332  -20.047 42.856  1.00 31.84  ? 221 LEU E N     1 
ATOM   6793  C CA    . LEU E 1 220 ? 18.033  -19.070 41.824  1.00 33.40  ? 221 LEU E CA    1 
ATOM   6794  C C     . LEU E 1 220 ? 18.583  -19.566 40.492  1.00 35.22  ? 221 LEU E C     1 
ATOM   6795  O O     . LEU E 1 220 ? 19.509  -20.374 40.461  1.00 36.44  ? 221 LEU E O     1 
ATOM   6796  C CB    . LEU E 1 220 ? 18.631  -17.714 42.198  1.00 35.75  ? 221 LEU E CB    1 
ATOM   6797  C CG    . LEU E 1 220 ? 20.162  -17.631 42.194  1.00 36.54  ? 221 LEU E CG    1 
ATOM   6798  C CD1   . LEU E 1 220 ? 20.627  -16.234 42.571  1.00 42.46  ? 221 LEU E CD1   1 
ATOM   6799  C CD2   . LEU E 1 220 ? 20.776  -18.666 43.120  1.00 37.24  ? 221 LEU E CD2   1 
ATOM   6800  N N     . PRO E 1 221 ? 18.029  -19.096 39.353  1.00 37.25  ? 222 PRO E N     1 
ATOM   6801  C CA    . PRO E 1 221 ? 18.575  -19.432 38.039  1.00 36.61  ? 222 PRO E CA    1 
ATOM   6802  C C     . PRO E 1 221 ? 19.980  -18.863 37.865  1.00 36.95  ? 222 PRO E C     1 
ATOM   6803  O O     . PRO E 1 221 ? 20.278  -17.768 38.341  1.00 36.38  ? 222 PRO E O     1 
ATOM   6804  C CB    . PRO E 1 221 ? 17.560  -18.823 37.052  1.00 38.31  ? 222 PRO E CB    1 
ATOM   6805  C CG    . PRO E 1 221 ? 16.885  -17.719 37.844  1.00 40.79  ? 222 PRO E CG    1 
ATOM   6806  C CD    . PRO E 1 221 ? 16.847  -18.225 39.277  1.00 38.34  ? 222 PRO E CD    1 
ATOM   6807  N N     . LEU E 1 222 ? 20.834  -19.627 37.178  1.00 33.97  ? 223 LEU E N     1 
ATOM   6808  C CA    . LEU E 1 222 ? 22.221  -19.249 36.966  1.00 36.16  ? 223 LEU E CA    1 
ATOM   6809  C C     . LEU E 1 222 ? 22.296  -17.814 36.450  1.00 36.50  ? 223 LEU E C     1 
ATOM   6810  O O     . LEU E 1 222 ? 23.257  -17.100 36.728  1.00 38.15  ? 223 LEU E O     1 
ATOM   6811  C CB    . LEU E 1 222 ? 22.851  -20.233 35.980  1.00 36.31  ? 223 LEU E CB    1 
ATOM   6812  C CG    . LEU E 1 222 ? 24.316  -19.978 35.614  1.00 38.77  ? 223 LEU E CG    1 
ATOM   6813  C CD1   . LEU E 1 222 ? 25.228  -20.210 36.806  1.00 39.02  ? 223 LEU E CD1   1 
ATOM   6814  C CD2   . LEU E 1 222 ? 24.735  -20.844 34.439  1.00 39.59  ? 223 LEU E CD2   1 
ATOM   6815  N N     . ALA E 1 223 ? 21.264  -17.403 35.707  1.00 38.37  ? 224 ALA E N     1 
ATOM   6816  C CA    . ALA E 1 223 ? 21.276  -16.138 34.990  1.00 38.39  ? 224 ALA E CA    1 
ATOM   6817  C C     . ALA E 1 223 ? 21.219  -14.959 35.960  1.00 39.27  ? 224 ALA E C     1 
ATOM   6818  O O     . ALA E 1 223 ? 21.625  -13.853 35.614  1.00 35.40  ? 224 ALA E O     1 
ATOM   6819  C CB    . ALA E 1 223 ? 20.122  -16.096 34.013  1.00 42.05  ? 224 ALA E CB    1 
ATOM   6820  N N     . ASN E 1 224 ? 20.709  -15.204 37.172  1.00 37.73  ? 225 ASN E N     1 
ATOM   6821  C CA    . ASN E 1 224 ? 20.472  -14.136 38.130  1.00 37.40  ? 225 ASN E CA    1 
ATOM   6822  C C     . ASN E 1 224 ? 21.664  -14.001 39.074  1.00 36.14  ? 225 ASN E C     1 
ATOM   6823  O O     . ASN E 1 224 ? 21.675  -13.130 39.941  1.00 39.85  ? 225 ASN E O     1 
ATOM   6824  C CB    . ASN E 1 224 ? 19.178  -14.358 38.906  1.00 39.09  ? 225 ASN E CB    1 
ATOM   6825  C CG    . ASN E 1 224 ? 17.958  -14.255 38.022  1.00 40.86  ? 225 ASN E CG    1 
ATOM   6826  O OD1   . ASN E 1 224 ? 18.081  -14.001 36.819  1.00 46.33  ? 225 ASN E OD1   1 
ATOM   6827  N ND2   . ASN E 1 224 ? 16.778  -14.442 38.595  1.00 46.93  ? 225 ASN E ND2   1 
ATOM   6828  N N     . LEU E 1 225 ? 22.670  -14.861 38.887  1.00 31.65  ? 226 LEU E N     1 
ATOM   6829  C CA    . LEU E 1 225 ? 23.829  -14.882 39.764  1.00 30.71  ? 226 LEU E CA    1 
ATOM   6830  C C     . LEU E 1 225 ? 24.427  -13.480 39.862  1.00 30.98  ? 226 LEU E C     1 
ATOM   6831  O O     . LEU E 1 225 ? 24.728  -13.007 40.956  1.00 32.72  ? 226 LEU E O     1 
ATOM   6832  C CB    . LEU E 1 225 ? 24.860  -15.886 39.255  1.00 30.73  ? 226 LEU E CB    1 
ATOM   6833  C CG    . LEU E 1 225 ? 26.168  -15.952 40.050  1.00 28.02  ? 226 LEU E CG    1 
ATOM   6834  C CD1   . LEU E 1 225 ? 25.926  -16.512 41.443  1.00 28.81  ? 226 LEU E CD1   1 
ATOM   6835  C CD2   . LEU E 1 225 ? 27.221  -16.763 39.315  1.00 27.78  ? 226 LEU E CD2   1 
ATOM   6836  N N     . PRO E 1 226 ? 24.636  -12.782 38.722  1.00 31.49  ? 227 PRO E N     1 
ATOM   6837  C CA    . PRO E 1 226 ? 25.295  -11.473 38.727  1.00 34.21  ? 227 PRO E CA    1 
ATOM   6838  C C     . PRO E 1 226 ? 24.606  -10.428 39.603  1.00 35.22  ? 227 PRO E C     1 
ATOM   6839  O O     . PRO E 1 226 ? 25.237  -9.465  40.032  1.00 40.21  ? 227 PRO E O     1 
ATOM   6840  C CB    . PRO E 1 226 ? 25.284  -11.069 37.234  1.00 32.86  ? 227 PRO E CB    1 
ATOM   6841  C CG    . PRO E 1 226 ? 25.162  -12.383 36.489  1.00 32.03  ? 227 PRO E CG    1 
ATOM   6842  C CD    . PRO E 1 226 ? 24.276  -13.237 37.371  1.00 31.88  ? 227 PRO E CD    1 
ATOM   6843  N N     . GLN E 1 227 ? 23.305  -10.623 39.852  1.00 39.30  ? 228 GLN E N     1 
ATOM   6844  C CA    . GLN E 1 227 ? 22.514  -9.661  40.602  1.00 42.39  ? 228 GLN E CA    1 
ATOM   6845  C C     . GLN E 1 227 ? 22.303  -10.157 42.031  1.00 41.86  ? 228 GLN E C     1 
ATOM   6846  O O     . GLN E 1 227 ? 21.598  -9.522  42.812  1.00 42.77  ? 228 GLN E O     1 
ATOM   6847  C CB    . GLN E 1 227 ? 21.158  -9.419  39.937  1.00 47.24  ? 228 GLN E CB    1 
ATOM   6848  C CG    . GLN E 1 227 ? 21.229  -8.641  38.627  1.00 52.47  ? 228 GLN E CG    1 
ATOM   6849  C CD    . GLN E 1 227 ? 21.831  -9.435  37.488  1.00 53.45  ? 228 GLN E CD    1 
ATOM   6850  O OE1   . GLN E 1 227 ? 21.329  -10.499 37.107  1.00 56.47  ? 228 GLN E OE1   1 
ATOM   6851  N NE2   . GLN E 1 227 ? 22.914  -8.919  36.926  1.00 58.43  ? 228 GLN E NE2   1 
ATOM   6852  N N     . ALA E 1 228 ? 22.925  -11.293 42.362  1.00 37.35  ? 229 ALA E N     1 
ATOM   6853  C CA    . ALA E 1 228 ? 22.754  -11.911 43.667  1.00 36.26  ? 229 ALA E CA    1 
ATOM   6854  C C     . ALA E 1 228 ? 23.645  -11.220 44.696  1.00 35.39  ? 229 ALA E C     1 
ATOM   6855  O O     . ALA E 1 228 ? 24.660  -10.623 44.346  1.00 34.72  ? 229 ALA E O     1 
ATOM   6856  C CB    . ALA E 1 228 ? 23.061  -13.389 43.578  1.00 37.27  ? 229 ALA E CB    1 
ATOM   6857  N N     . HIS E 1 229 ? 23.247  -11.319 45.969  1.00 34.63  ? 230 HIS E N     1 
ATOM   6858  C CA    . HIS E 1 229 ? 24.019  -10.765 47.069  1.00 34.77  ? 230 HIS E CA    1 
ATOM   6859  C C     . HIS E 1 229 ? 25.015  -11.814 47.555  1.00 32.44  ? 230 HIS E C     1 
ATOM   6860  O O     . HIS E 1 229 ? 24.626  -12.819 48.145  1.00 35.83  ? 230 HIS E O     1 
ATOM   6861  C CB    . HIS E 1 229 ? 23.089  -10.288 48.191  1.00 41.99  ? 230 HIS E CB    1 
ATOM   6862  C CG    . HIS E 1 229 ? 23.803  -9.729  49.378  1.00 45.18  ? 230 HIS E CG    1 
ATOM   6863  N ND1   . HIS E 1 229 ? 24.275  -8.435  49.424  1.00 46.46  ? 230 HIS E ND1   1 
ATOM   6864  C CD2   . HIS E 1 229 ? 24.135  -10.285 50.552  1.00 42.93  ? 230 HIS E CD2   1 
ATOM   6865  C CE1   . HIS E 1 229 ? 24.864  -8.225  50.593  1.00 45.76  ? 230 HIS E CE1   1 
ATOM   6866  N NE2   . HIS E 1 229 ? 24.789  -9.335  51.294  1.00 41.86  ? 230 HIS E NE2   1 
ATOM   6867  N N     . LEU E 1 230 ? 26.303  -11.564 47.294  1.00 30.12  ? 231 LEU E N     1 
ATOM   6868  C CA    . LEU E 1 230 ? 27.354  -12.510 47.626  1.00 29.28  ? 231 LEU E CA    1 
ATOM   6869  C C     . LEU E 1 230 ? 28.204  -11.956 48.766  1.00 34.42  ? 231 LEU E C     1 
ATOM   6870  O O     . LEU E 1 230 ? 28.445  -10.753 48.844  1.00 36.66  ? 231 LEU E O     1 
ATOM   6871  C CB    . LEU E 1 230 ? 28.207  -12.794 46.390  1.00 28.38  ? 231 LEU E CB    1 
ATOM   6872  C CG    . LEU E 1 230 ? 27.492  -13.472 45.217  1.00 27.64  ? 231 LEU E CG    1 
ATOM   6873  C CD1   . LEU E 1 230 ? 28.468  -13.749 44.086  1.00 28.80  ? 231 LEU E CD1   1 
ATOM   6874  C CD2   . LEU E 1 230 ? 26.805  -14.752 45.661  1.00 26.74  ? 231 LEU E CD2   1 
ATOM   6875  N N     . MET E 1 231 ? 28.655  -12.859 49.642  1.00 31.81  ? 232 MET E N     1 
ATOM   6876  C CA    . MET E 1 231 ? 29.574  -12.510 50.711  1.00 34.18  ? 232 MET E CA    1 
ATOM   6877  C C     . MET E 1 231 ? 30.827  -13.371 50.581  1.00 32.95  ? 232 MET E C     1 
ATOM   6878  O O     . MET E 1 231 ? 30.812  -14.397 49.904  1.00 28.71  ? 232 MET E O     1 
ATOM   6879  C CB    . MET E 1 231 ? 28.930  -12.723 52.086  1.00 39.76  ? 232 MET E CB    1 
ATOM   6880  C CG    . MET E 1 231 ? 27.774  -11.782 52.384  1.00 46.61  ? 232 MET E CG    1 
ATOM   6881  S SD    . MET E 1 231 ? 28.254  -10.043 52.359  1.00 60.34  ? 232 MET E SD    1 
ATOM   6882  C CE    . MET E 1 231 ? 29.619  -10.046 53.530  1.00 66.01  ? 232 MET E CE    1 
ATOM   6883  N N     . PRO E 1 232 ? 31.952  -12.974 51.218  1.00 33.01  ? 233 PRO E N     1 
ATOM   6884  C CA    . PRO E 1 232 ? 33.202  -13.730 51.118  1.00 32.75  ? 233 PRO E CA    1 
ATOM   6885  C C     . PRO E 1 232 ? 33.031  -15.217 51.422  1.00 35.21  ? 233 PRO E C     1 
ATOM   6886  O O     . PRO E 1 232 ? 33.724  -16.054 50.848  1.00 37.09  ? 233 PRO E O     1 
ATOM   6887  C CB    . PRO E 1 232 ? 34.115  -13.033 52.146  1.00 31.30  ? 233 PRO E CB    1 
ATOM   6888  C CG    . PRO E 1 232 ? 33.575  -11.620 52.226  1.00 32.56  ? 233 PRO E CG    1 
ATOM   6889  C CD    . PRO E 1 232 ? 32.075  -11.766 52.047  1.00 32.90  ? 233 PRO E CD    1 
ATOM   6890  N N     . ILE E 1 233 ? 32.098  -15.531 52.327  1.00 32.14  ? 234 ILE E N     1 
ATOM   6891  C CA    . ILE E 1 233 ? 31.928  -16.891 52.815  1.00 34.28  ? 234 ILE E CA    1 
ATOM   6892  C C     . ILE E 1 233 ? 30.935  -17.637 51.926  1.00 34.61  ? 234 ILE E C     1 
ATOM   6893  O O     . ILE E 1 233 ? 30.532  -18.752 52.250  1.00 39.55  ? 234 ILE E O     1 
ATOM   6894  C CB    . ILE E 1 233 ? 31.475  -16.892 54.286  1.00 36.58  ? 234 ILE E CB    1 
ATOM   6895  C CG1   . ILE E 1 233 ? 30.103  -16.237 54.454  1.00 35.08  ? 234 ILE E CG1   1 
ATOM   6896  C CG2   . ILE E 1 233 ? 32.527  -16.239 55.183  1.00 39.26  ? 234 ILE E CG2   1 
ATOM   6897  C CD1   . ILE E 1 233 ? 29.562  -16.286 55.871  1.00 36.49  ? 234 ILE E CD1   1 
ATOM   6898  N N     . SER E 1 234 ? 30.550  -17.018 50.805  1.00 32.24  ? 235 SER E N     1 
ATOM   6899  C CA    . SER E 1 234 ? 29.577  -17.611 49.902  1.00 31.90  ? 235 SER E CA    1 
ATOM   6900  C C     . SER E 1 234 ? 30.239  -18.675 49.030  1.00 29.76  ? 235 SER E C     1 
ATOM   6901  O O     . SER E 1 234 ? 31.334  -18.472 48.510  1.00 27.83  ? 235 SER E O     1 
ATOM   6902  C CB    . SER E 1 234 ? 28.905  -16.560 49.057  1.00 31.82  ? 235 SER E CB    1 
ATOM   6903  O OG    . SER E 1 234 ? 28.043  -15.747 49.842  1.00 30.03  ? 235 SER E OG    1 
ATOM   6904  N N     . THR E 1 235 ? 29.552  -19.813 48.882  1.00 32.90  ? 236 THR E N     1 
ATOM   6905  C CA    . THR E 1 235 ? 29.972  -20.862 47.968  1.00 31.38  ? 236 THR E CA    1 
ATOM   6906  C C     . THR E 1 235 ? 28.839  -21.125 46.980  1.00 27.93  ? 236 THR E C     1 
ATOM   6907  O O     . THR E 1 235 ? 27.669  -21.112 47.356  1.00 26.21  ? 236 THR E O     1 
ATOM   6908  C CB    . THR E 1 235 ? 30.343  -22.118 48.757  1.00 37.89  ? 236 THR E CB    1 
ATOM   6909  O OG1   . THR E 1 235 ? 31.408  -21.729 49.619  1.00 38.15  ? 236 THR E OG1   1 
ATOM   6910  C CG2   . THR E 1 235 ? 30.797  -23.257 47.862  1.00 37.47  ? 236 THR E CG2   1 
ATOM   6911  N N     . LEU E 1 236 ? 29.201  -21.352 45.712  1.00 26.38  ? 237 LEU E N     1 
ATOM   6912  C CA    . LEU E 1 236 ? 28.219  -21.582 44.664  1.00 24.79  ? 237 LEU E CA    1 
ATOM   6913  C C     . LEU E 1 236 ? 28.162  -23.071 44.335  1.00 26.49  ? 237 LEU E C     1 
ATOM   6914  O O     . LEU E 1 236 ? 29.147  -23.656 43.886  1.00 23.32  ? 237 LEU E O     1 
ATOM   6915  C CB    . LEU E 1 236 ? 28.557  -20.756 43.425  1.00 25.35  ? 237 LEU E CB    1 
ATOM   6916  C CG    . LEU E 1 236 ? 27.637  -20.962 42.217  1.00 26.70  ? 237 LEU E CG    1 
ATOM   6917  C CD1   . LEU E 1 236 ? 26.215  -20.526 42.531  1.00 26.42  ? 237 LEU E CD1   1 
ATOM   6918  C CD2   . LEU E 1 236 ? 28.163  -20.230 40.995  1.00 29.83  ? 237 LEU E CD2   1 
ATOM   6919  N N     . LEU E 1 237 ? 26.987  -23.669 44.556  1.00 28.12  ? 238 LEU E N     1 
ATOM   6920  C CA    . LEU E 1 237 ? 26.752  -25.063 44.219  1.00 27.40  ? 238 LEU E CA    1 
ATOM   6921  C C     . LEU E 1 237 ? 25.987  -25.137 42.902  1.00 26.80  ? 238 LEU E C     1 
ATOM   6922  O O     . LEU E 1 237 ? 24.896  -24.586 42.780  1.00 27.37  ? 238 LEU E O     1 
ATOM   6923  C CB    . LEU E 1 237 ? 25.980  -25.752 45.342  1.00 27.35  ? 238 LEU E CB    1 
ATOM   6924  C CG    . LEU E 1 237 ? 25.450  -27.153 45.022  1.00 28.01  ? 238 LEU E CG    1 
ATOM   6925  C CD1   . LEU E 1 237 ? 26.577  -28.170 44.959  1.00 30.71  ? 238 LEU E CD1   1 
ATOM   6926  C CD2   . LEU E 1 237 ? 24.399  -27.578 46.027  1.00 26.65  ? 238 LEU E CD2   1 
ATOM   6927  N N     . ILE E 1 238 ? 26.572  -25.832 41.923  1.00 30.51  ? 239 ILE E N     1 
ATOM   6928  C CA    . ILE E 1 238 ? 25.930  -26.023 40.635  1.00 27.46  ? 239 ILE E CA    1 
ATOM   6929  C C     . ILE E 1 238 ? 25.539  -27.493 40.501  1.00 28.45  ? 239 ILE E C     1 
ATOM   6930  O O     . ILE E 1 238 ? 26.373  -28.341 40.195  1.00 28.37  ? 239 ILE E O     1 
ATOM   6931  C CB    . ILE E 1 238 ? 26.847  -25.553 39.492  1.00 27.83  ? 239 ILE E CB    1 
ATOM   6932  C CG1   . ILE E 1 238 ? 27.235  -24.080 39.660  1.00 27.18  ? 239 ILE E CG1   1 
ATOM   6933  C CG2   . ILE E 1 238 ? 26.203  -25.817 38.131  1.00 28.48  ? 239 ILE E CG2   1 
ATOM   6934  C CD1   . ILE E 1 238 ? 28.177  -23.558 38.591  1.00 29.11  ? 239 ILE E CD1   1 
ATOM   6935  N N     . PRO E 1 239 ? 24.256  -27.835 40.753  1.00 27.53  ? 240 PRO E N     1 
ATOM   6936  C CA    . PRO E 1 239 ? 23.794  -29.222 40.677  1.00 26.89  ? 240 PRO E CA    1 
ATOM   6937  C C     . PRO E 1 239 ? 23.913  -29.797 39.268  1.00 24.98  ? 240 PRO E C     1 
ATOM   6938  O O     . PRO E 1 239 ? 24.026  -29.056 38.295  1.00 26.34  ? 240 PRO E O     1 
ATOM   6939  C CB    . PRO E 1 239 ? 22.324  -29.147 41.150  1.00 25.74  ? 240 PRO E CB    1 
ATOM   6940  C CG    . PRO E 1 239 ? 22.220  -27.815 41.871  1.00 26.91  ? 240 PRO E CG    1 
ATOM   6941  C CD    . PRO E 1 239 ? 23.194  -26.903 41.154  1.00 26.58  ? 240 PRO E CD    1 
ATOM   6942  N N     . PRO E 1 240 ? 23.876  -31.139 39.123  1.00 22.52  ? 241 PRO E N     1 
ATOM   6943  C CA    . PRO E 1 240 ? 23.986  -31.777 37.810  1.00 24.10  ? 241 PRO E CA    1 
ATOM   6944  C C     . PRO E 1 240 ? 23.039  -31.168 36.781  1.00 25.18  ? 241 PRO E C     1 
ATOM   6945  O O     . PRO E 1 240 ? 21.893  -30.850 37.094  1.00 28.38  ? 241 PRO E O     1 
ATOM   6946  C CB    . PRO E 1 240 ? 23.648  -33.253 38.106  1.00 23.40  ? 241 PRO E CB    1 
ATOM   6947  C CG    . PRO E 1 240 ? 24.021  -33.440 39.562  1.00 23.93  ? 241 PRO E CG    1 
ATOM   6948  C CD    . PRO E 1 240 ? 23.727  -32.105 40.221  1.00 23.86  ? 241 PRO E CD    1 
ATOM   6949  N N     . ALA E 1 241 ? 23.533  -31.018 35.548  1.00 28.72  ? 242 ALA E N     1 
ATOM   6950  C CA    . ALA E 1 241 ? 22.716  -30.554 34.440  1.00 30.30  ? 242 ALA E CA    1 
ATOM   6951  C C     . ALA E 1 241 ? 22.238  -31.753 33.624  1.00 35.35  ? 242 ALA E C     1 
ATOM   6952  O O     . ALA E 1 241 ? 21.316  -31.637 32.820  1.00 38.63  ? 242 ALA E O     1 
ATOM   6953  C CB    . ALA E 1 241 ? 23.501  -29.576 33.593  1.00 30.14  ? 242 ALA E CB    1 
ATOM   6954  N N     . LYS E 1 242 ? 22.879  -32.906 33.855  1.00 39.84  ? 243 LYS E N     1 
ATOM   6955  C CA    . LYS E 1 242 ? 22.529  -34.147 33.183  1.00 44.09  ? 243 LYS E CA    1 
ATOM   6956  C C     . LYS E 1 242 ? 22.448  -35.277 34.204  1.00 42.80  ? 243 LYS E C     1 
ATOM   6957  O O     . LYS E 1 242 ? 23.112  -35.235 35.237  1.00 44.83  ? 243 LYS E O     1 
ATOM   6958  C CB    . LYS E 1 242 ? 23.569  -34.548 32.129  1.00 47.45  ? 243 LYS E CB    1 
ATOM   6959  C CG    . LYS E 1 242 ? 23.390  -33.958 30.739  1.00 51.27  ? 243 LYS E CG    1 
ATOM   6960  C CD    . LYS E 1 242 ? 24.292  -34.592 29.683  1.00 53.11  ? 243 LYS E CD    1 
ATOM   6961  C CE    . LYS E 1 242 ? 25.587  -35.110 30.234  1.00 54.62  ? 243 LYS E CE    1 
ATOM   6962  N NZ    . LYS E 1 242 ? 25.472  -36.506 30.670  1.00 55.87  ? 243 LYS E NZ    1 
ATOM   6963  N N     . LYS E 1 243 ? 21.637  -36.292 33.890  1.00 43.19  ? 244 LYS E N     1 
ATOM   6964  C CA    . LYS E 1 243 ? 21.620  -37.525 34.661  1.00 48.12  ? 244 LYS E CA    1 
ATOM   6965  C C     . LYS E 1 243 ? 22.656  -38.488 34.092  1.00 38.95  ? 244 LYS E C     1 
ATOM   6966  O O     . LYS E 1 243 ? 23.122  -38.320 32.968  1.00 47.09  ? 244 LYS E O     1 
ATOM   6967  C CB    . LYS E 1 243 ? 20.225  -38.161 34.714  1.00 54.76  ? 244 LYS E CB    1 
ATOM   6968  C CG    . LYS E 1 243 ? 19.155  -37.515 33.844  1.00 61.08  ? 244 LYS E CG    1 
ATOM   6969  C CD    . LYS E 1 243 ? 17.936  -38.395 33.586  1.00 63.61  ? 244 LYS E CD    1 
ATOM   6970  C CE    . LYS E 1 243 ? 17.929  -39.663 34.382  1.00 66.41  ? 244 LYS E CE    1 
ATOM   6971  N NZ    . LYS E 1 243 ? 18.619  -40.735 33.658  1.00 67.89  ? 244 LYS E NZ    1 
ATOM   6972  N N     . LEU E 1 244 ? 23.005  -39.495 34.897  1.00 37.84  ? 245 LEU E N     1 
ATOM   6973  C CA    . LEU E 1 244 ? 24.055  -40.441 34.561  1.00 38.60  ? 245 LEU E CA    1 
ATOM   6974  C C     . LEU E 1 244 ? 23.633  -41.287 33.362  1.00 39.95  ? 245 LEU E C     1 
ATOM   6975  O O     . LEU E 1 244 ? 22.566  -41.898 33.372  1.00 43.33  ? 245 LEU E O     1 
ATOM   6976  C CB    . LEU E 1 244 ? 24.339  -41.298 35.793  1.00 34.01  ? 245 LEU E CB    1 
ATOM   6977  C CG    . LEU E 1 244 ? 24.885  -40.545 37.011  1.00 32.92  ? 245 LEU E CG    1 
ATOM   6978  C CD1   . LEU E 1 244 ? 25.047  -41.459 38.213  1.00 32.50  ? 245 LEU E CD1   1 
ATOM   6979  C CD2   . LEU E 1 244 ? 26.204  -39.874 36.667  1.00 31.33  ? 245 LEU E CD2   1 
ATOM   6980  N N     . GLU E 1 245 ? 24.488  -41.306 32.332  1.00 42.57  ? 246 GLU E N     1 
ATOM   6981  C CA    . GLU E 1 245 ? 24.272  -42.128 31.152  1.00 44.88  ? 246 GLU E CA    1 
ATOM   6982  C C     . GLU E 1 245 ? 25.206  -43.334 31.212  1.00 42.60  ? 246 GLU E C     1 
ATOM   6983  O O     . GLU E 1 245 ? 26.294  -43.254 31.777  1.00 38.72  ? 246 GLU E O     1 
ATOM   6984  C CB    . GLU E 1 245 ? 24.508  -41.319 29.875  1.00 49.14  ? 246 GLU E CB    1 
ATOM   6985  C CG    . GLU E 1 245 ? 23.532  -40.159 29.699  1.00 53.61  ? 246 GLU E CG    1 
ATOM   6986  C CD    . GLU E 1 245 ? 23.735  -39.364 28.420  1.00 57.42  ? 246 GLU E CD    1 
ATOM   6987  O OE1   . GLU E 1 245 ? 23.616  -39.960 27.329  1.00 61.61  ? 246 GLU E OE1   1 
ATOM   6988  O OE2   . GLU E 1 245 ? 24.013  -38.151 28.516  1.00 60.03  ? 246 GLU E OE2   1 
ATOM   6989  N N     . TYR E 1 246 ? 24.769  -44.449 30.615  1.00 43.97  ? 247 TYR E N     1 
ATOM   6990  C CA    . TYR E 1 246 ? 25.507  -45.700 30.688  1.00 41.76  ? 247 TYR E CA    1 
ATOM   6991  C C     . TYR E 1 246 ? 26.726  -45.635 29.773  1.00 39.78  ? 247 TYR E C     1 
ATOM   6992  O O     . TYR E 1 246 ? 26.663  -45.079 28.678  1.00 40.48  ? 247 TYR E O     1 
ATOM   6993  C CB    . TYR E 1 246 ? 24.615  -46.891 30.322  1.00 40.82  ? 247 TYR E CB    1 
ATOM   6994  C CG    . TYR E 1 246 ? 23.525  -47.195 31.339  1.00 38.68  ? 247 TYR E CG    1 
ATOM   6995  C CD1   . TYR E 1 246 ? 23.830  -47.790 32.557  1.00 37.97  ? 247 TYR E CD1   1 
ATOM   6996  C CD2   . TYR E 1 246 ? 22.191  -46.911 31.073  1.00 38.53  ? 247 TYR E CD2   1 
ATOM   6997  C CE1   . TYR E 1 246 ? 22.846  -48.072 33.489  1.00 39.86  ? 247 TYR E CE1   1 
ATOM   6998  C CE2   . TYR E 1 246 ? 21.196  -47.193 31.995  1.00 39.59  ? 247 TYR E CE2   1 
ATOM   6999  C CZ    . TYR E 1 246 ? 21.526  -47.775 33.207  1.00 40.09  ? 247 TYR E CZ    1 
ATOM   7000  O OH    . TYR E 1 246 ? 20.557  -48.057 34.126  1.00 38.48  ? 247 TYR E OH    1 
ATOM   7001  N N     . ASN E 1 247 ? 27.828  -46.230 30.242  1.00 40.90  ? 248 ASN E N     1 
ATOM   7002  C CA    . ASN E 1 247 ? 29.060  -46.317 29.478  1.00 41.44  ? 248 ASN E CA    1 
ATOM   7003  C C     . ASN E 1 247 ? 29.160  -47.716 28.875  1.00 39.24  ? 248 ASN E C     1 
ATOM   7004  O O     . ASN E 1 247 ? 29.740  -48.616 29.478  1.00 35.74  ? 248 ASN E O     1 
ATOM   7005  C CB    . ASN E 1 247 ? 30.266  -45.976 30.347  1.00 42.38  ? 248 ASN E CB    1 
ATOM   7006  C CG    . ASN E 1 247 ? 31.533  -45.822 29.542  1.00 45.64  ? 248 ASN E CG    1 
ATOM   7007  O OD1   . ASN E 1 247 ? 31.511  -45.955 28.314  1.00 49.19  ? 248 ASN E OD1   1 
ATOM   7008  N ND2   . ASN E 1 247 ? 32.641  -45.533 30.209  1.00 53.95  ? 248 ASN E ND2   1 
ATOM   7009  N N     . TYR E 1 248 ? 28.583  -47.884 27.680  1.00 39.82  ? 249 TYR E N     1 
ATOM   7010  C CA    . TYR E 1 248 ? 28.474  -49.191 27.050  1.00 41.75  ? 249 TYR E CA    1 
ATOM   7011  C C     . TYR E 1 248 ? 29.866  -49.728 26.729  1.00 41.05  ? 249 TYR E C     1 
ATOM   7012  O O     . TYR E 1 248 ? 30.114  -50.926 26.853  1.00 38.31  ? 249 TYR E O     1 
ATOM   7013  C CB    . TYR E 1 248 ? 27.605  -49.105 25.791  1.00 44.34  ? 249 TYR E CB    1 
ATOM   7014  C CG    . TYR E 1 248 ? 26.167  -48.683 26.054  1.00 46.99  ? 249 TYR E CG    1 
ATOM   7015  C CD1   . TYR E 1 248 ? 25.244  -49.577 26.580  1.00 48.88  ? 249 TYR E CD1   1 
ATOM   7016  C CD2   . TYR E 1 248 ? 25.729  -47.397 25.762  1.00 50.19  ? 249 TYR E CD2   1 
ATOM   7017  C CE1   . TYR E 1 248 ? 23.933  -49.203 26.822  1.00 49.57  ? 249 TYR E CE1   1 
ATOM   7018  C CE2   . TYR E 1 248 ? 24.419  -47.011 25.996  1.00 49.54  ? 249 TYR E CE2   1 
ATOM   7019  C CZ    . TYR E 1 248 ? 23.519  -47.917 26.528  1.00 51.98  ? 249 TYR E CZ    1 
ATOM   7020  O OH    . TYR E 1 248 ? 22.227  -47.545 26.763  1.00 49.40  ? 249 TYR E OH    1 
ATOM   7021  N N     . ALA E 1 249 ? 30.762  -48.831 26.309  1.00 41.17  ? 250 ALA E N     1 
ATOM   7022  C CA    . ALA E 1 249 ? 32.110  -49.215 25.925  1.00 39.61  ? 250 ALA E CA    1 
ATOM   7023  C C     . ALA E 1 249 ? 32.728  -50.091 27.011  1.00 36.84  ? 250 ALA E C     1 
ATOM   7024  O O     . ALA E 1 249 ? 33.219  -51.182 26.730  1.00 40.87  ? 250 ALA E O     1 
ATOM   7025  C CB    . ALA E 1 249 ? 32.945  -47.980 25.666  1.00 41.92  ? 250 ALA E CB    1 
ATOM   7026  N N     . ILE E 1 250 ? 32.684  -49.602 28.254  1.00 38.19  ? 251 ILE E N     1 
ATOM   7027  C CA    . ILE E 1 250 ? 33.324  -50.275 29.371  1.00 37.76  ? 251 ILE E CA    1 
ATOM   7028  C C     . ILE E 1 250 ? 32.479  -51.478 29.785  1.00 36.13  ? 251 ILE E C     1 
ATOM   7029  O O     . ILE E 1 250 ? 33.015  -52.545 30.071  1.00 33.82  ? 251 ILE E O     1 
ATOM   7030  C CB    . ILE E 1 250 ? 33.550  -49.299 30.541  1.00 39.56  ? 251 ILE E CB    1 
ATOM   7031  C CG1   . ILE E 1 250 ? 34.387  -48.093 30.110  1.00 42.83  ? 251 ILE E CG1   1 
ATOM   7032  C CG2   . ILE E 1 250 ? 34.171  -50.014 31.740  1.00 40.84  ? 251 ILE E CG2   1 
ATOM   7033  C CD1   . ILE E 1 250 ? 35.755  -48.454 29.559  1.00 45.52  ? 251 ILE E CD1   1 
ATOM   7034  N N     . LEU E 1 251 ? 31.155  -51.291 29.813  1.00 38.29  ? 252 LEU E N     1 
ATOM   7035  C CA    . LEU E 1 251 ? 30.240  -52.355 30.194  1.00 40.24  ? 252 LEU E CA    1 
ATOM   7036  C C     . LEU E 1 251 ? 30.494  -53.577 29.313  1.00 38.73  ? 252 LEU E C     1 
ATOM   7037  O O     . LEU E 1 251 ? 30.455  -54.709 29.790  1.00 36.99  ? 252 LEU E O     1 
ATOM   7038  C CB    . LEU E 1 251 ? 28.793  -51.877 30.083  1.00 42.50  ? 252 LEU E CB    1 
ATOM   7039  C CG    . LEU E 1 251 ? 28.365  -50.786 31.071  1.00 43.05  ? 252 LEU E CG    1 
ATOM   7040  C CD1   . LEU E 1 251 ? 26.910  -50.404 30.856  1.00 40.15  ? 252 LEU E CD1   1 
ATOM   7041  C CD2   . LEU E 1 251 ? 28.595  -51.221 32.508  1.00 43.92  ? 252 LEU E CD2   1 
ATOM   7042  N N     . ALA E 1 252 ? 30.761  -53.328 28.027  1.00 37.51  ? 253 ALA E N     1 
ATOM   7043  C CA    . ALA E 1 252 ? 30.975  -54.393 27.061  1.00 38.16  ? 253 ALA E CA    1 
ATOM   7044  C C     . ALA E 1 252 ? 32.267  -55.138 27.385  1.00 39.62  ? 253 ALA E C     1 
ATOM   7045  O O     . ALA E 1 252 ? 32.333  -56.358 27.257  1.00 43.17  ? 253 ALA E O     1 
ATOM   7046  C CB    . ALA E 1 252 ? 31.000  -53.822 25.660  1.00 37.61  ? 253 ALA E CB    1 
ATOM   7047  N N     . LYS E 1 253 ? 33.293  -54.385 27.797  1.00 38.28  ? 254 LYS E N     1 
ATOM   7048  C CA    . LYS E 1 253 ? 34.563  -54.969 28.196  1.00 40.05  ? 254 LYS E CA    1 
ATOM   7049  C C     . LYS E 1 253 ? 34.366  -55.767 29.482  1.00 41.47  ? 254 LYS E C     1 
ATOM   7050  O O     . LYS E 1 253 ? 35.001  -56.801 29.680  1.00 40.02  ? 254 LYS E O     1 
ATOM   7051  C CB    . LYS E 1 253 ? 35.631  -53.883 28.371  1.00 40.76  ? 254 LYS E CB    1 
ATOM   7052  C CG    . LYS E 1 253 ? 36.171  -53.297 27.073  1.00 41.23  ? 254 LYS E CG    1 
ATOM   7053  C CD    . LYS E 1 253 ? 37.185  -52.178 27.273  1.00 43.65  ? 254 LYS E CD    1 
ATOM   7054  C CE    . LYS E 1 253 ? 37.848  -51.762 25.997  1.00 44.56  ? 254 LYS E CE    1 
ATOM   7055  N NZ    . LYS E 1 253 ? 36.879  -51.319 24.992  1.00 43.46  ? 254 LYS E NZ    1 
ATOM   7056  N N     . LEU E 1 254 ? 33.479  -55.268 30.351  1.00 39.87  ? 255 LEU E N     1 
ATOM   7057  C CA    . LEU E 1 254 ? 33.131  -55.962 31.580  1.00 39.38  ? 255 LEU E CA    1 
ATOM   7058  C C     . LEU E 1 254 ? 32.214  -57.135 31.245  1.00 40.57  ? 255 LEU E C     1 
ATOM   7059  O O     . LEU E 1 254 ? 31.983  -58.008 32.079  1.00 34.73  ? 255 LEU E O     1 
ATOM   7060  C CB    . LEU E 1 254 ? 32.473  -54.991 32.561  1.00 36.95  ? 255 LEU E CB    1 
ATOM   7061  C CG    . LEU E 1 254 ? 33.370  -53.875 33.107  1.00 35.19  ? 255 LEU E CG    1 
ATOM   7062  C CD1   . LEU E 1 254 ? 32.595  -52.953 34.032  1.00 33.01  ? 255 LEU E CD1   1 
ATOM   7063  C CD2   . LEU E 1 254 ? 34.579  -54.449 33.824  1.00 35.06  ? 255 LEU E CD2   1 
ATOM   7064  N N     . GLY E 1 255 ? 31.694  -57.135 30.012  1.00 40.21  ? 256 GLY E N     1 
ATOM   7065  C CA    . GLY E 1 255 ? 30.848  -58.212 29.525  1.00 41.50  ? 256 GLY E CA    1 
ATOM   7066  C C     . GLY E 1 255 ? 29.474  -58.191 30.188  1.00 44.82  ? 256 GLY E C     1 
ATOM   7067  O O     . GLY E 1 255 ? 28.812  -59.222 30.285  1.00 45.90  ? 256 GLY E O     1 
ATOM   7068  N N     . ILE E 1 256 ? 29.055  -57.002 30.635  1.00 46.11  ? 257 ILE E N     1 
ATOM   7069  C CA    . ILE E 1 256 ? 27.781  -56.843 31.316  1.00 46.64  ? 257 ILE E CA    1 
ATOM   7070  C C     . ILE E 1 256 ? 26.965  -55.773 30.596  1.00 48.55  ? 257 ILE E C     1 
ATOM   7071  O O     . ILE E 1 256 ? 27.385  -55.250 29.567  1.00 49.36  ? 257 ILE E O     1 
ATOM   7072  C CB    . ILE E 1 256 ? 27.995  -56.497 32.802  1.00 47.19  ? 257 ILE E CB    1 
ATOM   7073  C CG1   . ILE E 1 256 ? 28.594  -55.101 32.978  1.00 46.19  ? 257 ILE E CG1   1 
ATOM   7074  C CG2   . ILE E 1 256 ? 28.839  -57.567 33.494  1.00 50.61  ? 257 ILE E CG2   1 
ATOM   7075  C CD1   . ILE E 1 256 ? 28.836  -54.709 34.425  1.00 46.61  ? 257 ILE E CD1   1 
ATOM   7076  N N     . GLY E 1 257 ? 25.788  -55.466 31.153  1.00 51.44  ? 258 GLY E N     1 
ATOM   7077  C CA    . GLY E 1 257 ? 24.912  -54.444 30.606  1.00 49.02  ? 258 GLY E CA    1 
ATOM   7078  C C     . GLY E 1 257 ? 24.057  -53.814 31.702  1.00 46.66  ? 258 GLY E C     1 
ATOM   7079  O O     . GLY E 1 257 ? 24.076  -54.266 32.845  1.00 42.25  ? 258 GLY E O     1 
ATOM   7080  N N     . PRO E 1 258 ? 23.276  -52.756 31.386  1.00 44.89  ? 259 PRO E N     1 
ATOM   7081  C CA    . PRO E 1 258 ? 22.463  -52.072 32.393  1.00 49.22  ? 259 PRO E CA    1 
ATOM   7082  C C     . PRO E 1 258 ? 21.673  -53.036 33.274  1.00 49.47  ? 259 PRO E C     1 
ATOM   7083  O O     . PRO E 1 258 ? 21.650  -52.894 34.494  1.00 45.61  ? 259 PRO E O     1 
ATOM   7084  C CB    . PRO E 1 258 ? 21.546  -51.177 31.536  1.00 48.40  ? 259 PRO E CB    1 
ATOM   7085  C CG    . PRO E 1 258 ? 22.369  -50.886 30.299  1.00 46.59  ? 259 PRO E CG    1 
ATOM   7086  C CD    . PRO E 1 258 ? 23.142  -52.169 30.044  1.00 46.86  ? 259 PRO E CD    1 
ATOM   7087  N N     . GLU E 1 259 ? 21.038  -54.025 32.636  1.00 54.98  ? 260 GLU E N     1 
ATOM   7088  C CA    . GLU E 1 259 ? 20.140  -54.939 33.321  1.00 58.00  ? 260 GLU E CA    1 
ATOM   7089  C C     . GLU E 1 259 ? 20.925  -55.820 34.291  1.00 52.36  ? 260 GLU E C     1 
ATOM   7090  O O     . GLU E 1 259 ? 20.341  -56.445 35.173  1.00 48.03  ? 260 GLU E O     1 
ATOM   7091  C CB    . GLU E 1 259 ? 19.375  -55.793 32.309  1.00 64.59  ? 260 GLU E CB    1 
ATOM   7092  C CG    . GLU E 1 259 ? 20.275  -56.676 31.450  1.00 76.01  ? 260 GLU E CG    1 
ATOM   7093  C CD    . GLU E 1 259 ? 21.174  -55.917 30.490  1.00 84.30  ? 260 GLU E CD    1 
ATOM   7094  O OE1   . GLU E 1 259 ? 21.094  -54.670 30.461  1.00 86.42  ? 260 GLU E OE1   1 
ATOM   7095  O OE2   . GLU E 1 259 ? 21.956  -56.574 29.770  1.00 88.12  ? 260 GLU E OE2   1 
ATOM   7096  N N     . ASP E 1 260 ? 22.251  -55.865 34.117  1.00 47.13  ? 261 ASP E N     1 
ATOM   7097  C CA    . ASP E 1 260 ? 23.104  -56.706 34.941  1.00 46.00  ? 261 ASP E CA    1 
ATOM   7098  C C     . ASP E 1 260 ? 23.522  -55.945 36.197  1.00 46.78  ? 261 ASP E C     1 
ATOM   7099  O O     . ASP E 1 260 ? 24.043  -56.538 37.138  1.00 46.22  ? 261 ASP E O     1 
ATOM   7100  C CB    . ASP E 1 260 ? 24.314  -57.204 34.166  1.00 48.51  ? 261 ASP E CB    1 
ATOM   7101  C CG    . ASP E 1 260 ? 24.008  -58.139 33.005  1.00 48.60  ? 261 ASP E CG    1 
ATOM   7102  O OD1   . ASP E 1 260 ? 23.388  -59.196 33.252  1.00 51.62  ? 261 ASP E OD1   1 
ATOM   7103  O OD2   . ASP E 1 260 ? 24.396  -57.806 31.867  1.00 50.53  ? 261 ASP E OD2   1 
ATOM   7104  N N     . LEU E 1 261 ? 23.294  -54.627 36.196  1.00 46.91  ? 262 LEU E N     1 
ATOM   7105  C CA    . LEU E 1 261 ? 23.644  -53.791 37.332  1.00 48.08  ? 262 LEU E CA    1 
ATOM   7106  C C     . LEU E 1 261 ? 22.815  -54.217 38.539  1.00 48.00  ? 262 LEU E C     1 
ATOM   7107  O O     . LEU E 1 261 ? 21.595  -54.344 38.448  1.00 50.77  ? 262 LEU E O     1 
ATOM   7108  C CB    . LEU E 1 261 ? 23.427  -52.316 36.992  1.00 48.43  ? 262 LEU E CB    1 
ATOM   7109  C CG    . LEU E 1 261 ? 24.199  -51.786 35.779  1.00 51.89  ? 262 LEU E CG    1 
ATOM   7110  C CD1   . LEU E 1 261 ? 24.079  -50.275 35.676  1.00 52.82  ? 262 LEU E CD1   1 
ATOM   7111  C CD2   . LEU E 1 261 ? 25.658  -52.207 35.830  1.00 50.51  ? 262 LEU E CD2   1 
ATOM   7112  N N     . GLY E 1 262 ? 23.497  -54.444 39.666  1.00 47.64  ? 263 GLY E N     1 
ATOM   7113  C CA    . GLY E 1 262 ? 22.843  -54.853 40.898  1.00 51.18  ? 263 GLY E CA    1 
ATOM   7114  C C     . GLY E 1 262 ? 22.168  -53.678 41.581  1.00 53.56  ? 263 GLY E C     1 
ATOM   7115  O O     . GLY E 1 262 ? 22.563  -52.535 41.267  1.00 46.38  ? 263 GLY E O     1 
ATOM   7116  O OXT   . GLY E 1 262 ? 21.269  -53.941 42.407  1.00 57.58  ? 263 GLY E OXT   1 
ATOM   7117  N N     . GLY F 2 1   ? 27.639  -13.263 78.795  1.00 51.46  ? 3   GLY F N     1 
ATOM   7118  C CA    . GLY F 2 1   ? 26.181  -13.482 78.724  1.00 46.03  ? 3   GLY F CA    1 
ATOM   7119  C C     . GLY F 2 1   ? 25.778  -14.095 77.386  1.00 44.68  ? 3   GLY F C     1 
ATOM   7120  O O     . GLY F 2 1   ? 25.468  -15.282 77.309  1.00 42.10  ? 3   GLY F O     1 
ATOM   7121  N N     . LEU F 2 2   ? 25.791  -13.267 76.337  1.00 40.85  ? 4   LEU F N     1 
ATOM   7122  C CA    . LEU F 2 2   ? 25.414  -13.700 75.003  1.00 38.85  ? 4   LEU F CA    1 
ATOM   7123  C C     . LEU F 2 2   ? 26.468  -14.666 74.471  1.00 36.00  ? 4   LEU F C     1 
ATOM   7124  O O     . LEU F 2 2   ? 26.138  -15.708 73.908  1.00 34.77  ? 4   LEU F O     1 
ATOM   7125  C CB    . LEU F 2 2   ? 25.269  -12.475 74.100  1.00 39.59  ? 4   LEU F CB    1 
ATOM   7126  C CG    . LEU F 2 2   ? 24.706  -12.735 72.699  1.00 43.57  ? 4   LEU F CG    1 
ATOM   7127  C CD1   . LEU F 2 2   ? 23.245  -13.143 72.773  1.00 42.59  ? 4   LEU F CD1   1 
ATOM   7128  C CD2   . LEU F 2 2   ? 24.880  -11.520 71.803  1.00 45.47  ? 4   LEU F CD2   1 
ATOM   7129  N N     . SER F 2 3   ? 27.739  -14.303 74.670  1.00 28.68  ? 5   SER F N     1 
ATOM   7130  C CA    . SER F 2 3   ? 28.859  -15.072 74.154  1.00 28.98  ? 5   SER F CA    1 
ATOM   7131  C C     . SER F 2 3   ? 28.947  -16.419 74.865  1.00 28.57  ? 5   SER F C     1 
ATOM   7132  O O     . SER F 2 3   ? 29.189  -17.444 74.232  1.00 30.17  ? 5   SER F O     1 
ATOM   7133  C CB    . SER F 2 3   ? 30.146  -14.299 74.291  1.00 30.72  ? 5   SER F CB    1 
ATOM   7134  O OG    . SER F 2 3   ? 31.237  -15.011 73.723  1.00 30.63  ? 5   SER F OG    1 
ATOM   7135  N N     . ASP F 2 4   ? 28.746  -16.400 76.187  1.00 27.79  ? 6   ASP F N     1 
ATOM   7136  C CA    . ASP F 2 4   ? 28.881  -17.593 77.005  1.00 27.44  ? 6   ASP F CA    1 
ATOM   7137  C C     . ASP F 2 4   ? 27.774  -18.583 76.654  1.00 25.25  ? 6   ASP F C     1 
ATOM   7138  O O     . ASP F 2 4   ? 27.970  -19.793 76.740  1.00 26.91  ? 6   ASP F O     1 
ATOM   7139  C CB    . ASP F 2 4   ? 28.879  -17.251 78.487  1.00 31.51  ? 6   ASP F CB    1 
ATOM   7140  C CG    . ASP F 2 4   ? 30.016  -16.352 78.951  1.00 37.70  ? 6   ASP F CG    1 
ATOM   7141  O OD1   . ASP F 2 4   ? 30.843  -15.964 78.099  1.00 41.98  ? 6   ASP F OD1   1 
ATOM   7142  O OD2   . ASP F 2 4   ? 30.065  -16.047 80.162  1.00 42.61  ? 6   ASP F OD2   1 
ATOM   7143  N N     . PHE F 2 5   ? 26.611  -18.052 76.261  1.00 25.45  ? 7   PHE F N     1 
ATOM   7144  C CA    . PHE F 2 5   ? 25.458  -18.880 75.949  1.00 24.94  ? 7   PHE F CA    1 
ATOM   7145  C C     . PHE F 2 5   ? 25.701  -19.612 74.632  1.00 23.70  ? 7   PHE F C     1 
ATOM   7146  O O     . PHE F 2 5   ? 25.524  -20.826 74.555  1.00 25.57  ? 7   PHE F O     1 
ATOM   7147  C CB    . PHE F 2 5   ? 24.180  -18.034 75.913  1.00 23.65  ? 7   PHE F CB    1 
ATOM   7148  C CG    . PHE F 2 5   ? 22.974  -18.762 75.334  1.00 25.06  ? 7   PHE F CG    1 
ATOM   7149  C CD1   . PHE F 2 5   ? 22.378  -19.813 76.022  1.00 25.26  ? 7   PHE F CD1   1 
ATOM   7150  C CD2   . PHE F 2 5   ? 22.430  -18.385 74.111  1.00 26.04  ? 7   PHE F CD2   1 
ATOM   7151  C CE1   . PHE F 2 5   ? 21.283  -20.477 75.492  1.00 26.65  ? 7   PHE F CE1   1 
ATOM   7152  C CE2   . PHE F 2 5   ? 21.331  -19.049 73.589  1.00 27.15  ? 7   PHE F CE2   1 
ATOM   7153  C CZ    . PHE F 2 5   ? 20.761  -20.093 74.279  1.00 26.47  ? 7   PHE F CZ    1 
ATOM   7154  N N     . PHE F 2 6   ? 26.110  -18.862 73.602  1.00 26.95  ? 8   PHE F N     1 
ATOM   7155  C CA    . PHE F 2 6   ? 26.343  -19.428 72.283  1.00 28.00  ? 8   PHE F CA    1 
ATOM   7156  C C     . PHE F 2 6   ? 27.424  -20.502 72.367  1.00 26.92  ? 8   PHE F C     1 
ATOM   7157  O O     . PHE F 2 6   ? 27.340  -21.524 71.689  1.00 21.93  ? 8   PHE F O     1 
ATOM   7158  C CB    . PHE F 2 6   ? 26.745  -18.348 71.272  1.00 30.01  ? 8   PHE F CB    1 
ATOM   7159  C CG    . PHE F 2 6   ? 25.634  -17.382 70.886  1.00 34.21  ? 8   PHE F CG    1 
ATOM   7160  C CD1   . PHE F 2 6   ? 24.300  -17.694 71.123  1.00 35.98  ? 8   PHE F CD1   1 
ATOM   7161  C CD2   . PHE F 2 6   ? 25.924  -16.180 70.250  1.00 37.80  ? 8   PHE F CD2   1 
ATOM   7162  C CE1   . PHE F 2 6   ? 23.291  -16.816 70.760  1.00 35.75  ? 8   PHE F CE1   1 
ATOM   7163  C CE2   . PHE F 2 6   ? 24.910  -15.307 69.887  1.00 38.99  ? 8   PHE F CE2   1 
ATOM   7164  C CZ    . PHE F 2 6   ? 23.598  -15.627 70.143  1.00 36.71  ? 8   PHE F CZ    1 
ATOM   7165  N N     . THR F 2 7   ? 28.446  -20.249 73.192  1.00 28.89  ? 9   THR F N     1 
ATOM   7166  C CA    . THR F 2 7   ? 29.580  -21.152 73.312  1.00 28.60  ? 9   THR F CA    1 
ATOM   7167  C C     . THR F 2 7   ? 29.109  -22.486 73.885  1.00 32.83  ? 9   THR F C     1 
ATOM   7168  O O     . THR F 2 7   ? 29.508  -23.546 73.408  1.00 33.86  ? 9   THR F O     1 
ATOM   7169  C CB    . THR F 2 7   ? 30.657  -20.511 74.188  1.00 29.02  ? 9   THR F CB    1 
ATOM   7170  O OG1   . THR F 2 7   ? 31.121  -19.385 73.451  1.00 31.31  ? 9   THR F OG1   1 
ATOM   7171  C CG2   . THR F 2 7   ? 31.813  -21.453 74.474  1.00 28.75  ? 9   THR F CG2   1 
ATOM   7172  N N     . GLN F 2 8   ? 28.259  -22.416 74.913  1.00 38.09  ? 10  GLN F N     1 
ATOM   7173  C CA    . GLN F 2 8   ? 27.789  -23.605 75.604  1.00 41.04  ? 10  GLN F CA    1 
ATOM   7174  C C     . GLN F 2 8   ? 26.789  -24.347 74.720  1.00 38.39  ? 10  GLN F C     1 
ATOM   7175  O O     . GLN F 2 8   ? 26.799  -25.574 74.659  1.00 42.93  ? 10  GLN F O     1 
ATOM   7176  C CB    . GLN F 2 8   ? 27.165  -23.224 76.947  1.00 50.64  ? 10  GLN F CB    1 
ATOM   7177  C CG    . GLN F 2 8   ? 26.737  -24.419 77.792  1.00 62.57  ? 10  GLN F CG    1 
ATOM   7178  C CD    . GLN F 2 8   ? 26.232  -24.027 79.164  1.00 72.72  ? 10  GLN F CD    1 
ATOM   7179  O OE1   . GLN F 2 8   ? 26.943  -23.402 79.959  1.00 79.57  ? 10  GLN F OE1   1 
ATOM   7180  N NE2   . GLN F 2 8   ? 24.993  -24.393 79.456  1.00 76.65  ? 10  GLN F NE2   1 
ATOM   7181  N N     . LEU F 2 9   ? 25.932  -23.583 74.033  1.00 34.35  ? 11  LEU F N     1 
ATOM   7182  C CA    . LEU F 2 9   ? 24.886  -24.153 73.201  1.00 39.08  ? 11  LEU F CA    1 
ATOM   7183  C C     . LEU F 2 9   ? 25.510  -24.984 72.084  1.00 40.78  ? 11  LEU F C     1 
ATOM   7184  O O     . LEU F 2 9   ? 25.005  -26.051 71.741  1.00 45.04  ? 11  LEU F O     1 
ATOM   7185  C CB    . LEU F 2 9   ? 24.011  -23.033 72.639  1.00 40.44  ? 11  LEU F CB    1 
ATOM   7186  C CG    . LEU F 2 9   ? 22.920  -23.467 71.655  1.00 39.84  ? 11  LEU F CG    1 
ATOM   7187  C CD1   . LEU F 2 9   ? 21.902  -24.371 72.329  1.00 40.32  ? 11  LEU F CD1   1 
ATOM   7188  C CD2   . LEU F 2 9   ? 22.238  -22.260 71.035  1.00 39.16  ? 11  LEU F CD2   1 
ATOM   7189  N N     . GLY F 2 10  ? 26.613  -24.479 71.522  1.00 41.66  ? 12  GLY F N     1 
ATOM   7190  C CA    . GLY F 2 10  ? 27.249  -25.102 70.374  1.00 39.12  ? 12  GLY F CA    1 
ATOM   7191  C C     . GLY F 2 10  ? 28.031  -26.355 70.761  1.00 39.45  ? 12  GLY F C     1 
ATOM   7192  O O     . GLY F 2 10  ? 28.430  -27.129 69.894  1.00 44.17  ? 12  GLY F O     1 
ATOM   7193  N N     . GLN F 2 11  ? 28.238  -26.549 72.069  1.00 38.59  ? 13  GLN F N     1 
ATOM   7194  C CA    . GLN F 2 11  ? 29.061  -27.642 72.561  1.00 40.44  ? 13  GLN F CA    1 
ATOM   7195  C C     . GLN F 2 11  ? 28.190  -28.714 73.213  1.00 36.86  ? 13  GLN F C     1 
ATOM   7196  O O     . GLN F 2 11  ? 28.507  -29.899 73.141  1.00 38.28  ? 13  GLN F O     1 
ATOM   7197  C CB    . GLN F 2 11  ? 30.093  -27.142 73.572  1.00 45.45  ? 13  GLN F CB    1 
ATOM   7198  C CG    . GLN F 2 11  ? 31.113  -26.167 72.996  1.00 47.67  ? 13  GLN F CG    1 
ATOM   7199  C CD    . GLN F 2 11  ? 32.183  -25.774 73.991  1.00 52.56  ? 13  GLN F CD    1 
ATOM   7200  O OE1   . GLN F 2 11  ? 32.966  -26.608 74.459  1.00 55.83  ? 13  GLN F OE1   1 
ATOM   7201  N NE2   . GLN F 2 11  ? 32.227  -24.493 74.326  1.00 60.02  ? 13  GLN F NE2   1 
ATOM   7202  N N     . ASP F 2 12  ? 27.102  -28.284 73.860  1.00 33.40  ? 14  ASP F N     1 
ATOM   7203  C CA    . ASP F 2 12  ? 26.282  -29.176 74.665  1.00 34.39  ? 14  ASP F CA    1 
ATOM   7204  C C     . ASP F 2 12  ? 25.065  -29.618 73.857  1.00 31.31  ? 14  ASP F C     1 
ATOM   7205  O O     . ASP F 2 12  ? 24.178  -28.817 73.574  1.00 34.64  ? 14  ASP F O     1 
ATOM   7206  C CB    . ASP F 2 12  ? 25.894  -28.517 75.981  1.00 36.74  ? 14  ASP F CB    1 
ATOM   7207  C CG    . ASP F 2 12  ? 25.105  -29.388 76.949  1.00 40.69  ? 14  ASP F CG    1 
ATOM   7208  O OD1   . ASP F 2 12  ? 24.815  -30.550 76.594  1.00 37.20  ? 14  ASP F OD1   1 
ATOM   7209  O OD2   . ASP F 2 12  ? 24.790  -28.896 78.054  1.00 49.39  ? 14  ASP F OD2   1 
ATOM   7210  N N     . ALA F 2 13  ? 25.033  -30.910 73.509  1.00 32.36  ? 15  ALA F N     1 
ATOM   7211  C CA    . ALA F 2 13  ? 23.956  -31.474 72.711  1.00 34.42  ? 15  ALA F CA    1 
ATOM   7212  C C     . ALA F 2 13  ? 22.648  -31.430 73.496  1.00 37.64  ? 15  ALA F C     1 
ATOM   7213  O O     . ALA F 2 13  ? 21.576  -31.262 72.917  1.00 42.06  ? 15  ALA F O     1 
ATOM   7214  C CB    . ALA F 2 13  ? 24.304  -32.888 72.300  1.00 35.28  ? 15  ALA F CB    1 
ATOM   7215  N N     . GLN F 2 14  ? 22.754  -31.592 74.818  1.00 35.79  ? 16  GLN F N     1 
ATOM   7216  C CA    . GLN F 2 14  ? 21.595  -31.581 75.693  1.00 37.82  ? 16  GLN F CA    1 
ATOM   7217  C C     . GLN F 2 14  ? 20.890  -30.233 75.575  1.00 32.83  ? 16  GLN F C     1 
ATOM   7218  O O     . GLN F 2 14  ? 19.702  -30.172 75.266  1.00 33.20  ? 16  GLN F O     1 
ATOM   7219  C CB    . GLN F 2 14  ? 22.026  -31.858 77.135  1.00 44.20  ? 16  GLN F CB    1 
ATOM   7220  C CG    . GLN F 2 14  ? 20.865  -32.019 78.110  1.00 49.20  ? 16  GLN F CG    1 
ATOM   7221  C CD    . GLN F 2 14  ? 19.975  -33.199 77.787  1.00 56.26  ? 16  GLN F CD    1 
ATOM   7222  O OE1   . GLN F 2 14  ? 20.208  -33.940 76.825  1.00 62.16  ? 16  GLN F OE1   1 
ATOM   7223  N NE2   . GLN F 2 14  ? 18.942  -33.387 78.595  1.00 61.94  ? 16  GLN F NE2   1 
ATOM   7224  N N     . LEU F 2 15  ? 21.645  -29.157 75.819  1.00 29.63  ? 17  LEU F N     1 
ATOM   7225  C CA    . LEU F 2 15  ? 21.112  -27.806 75.758  1.00 29.33  ? 17  LEU F CA    1 
ATOM   7226  C C     . LEU F 2 15  ? 20.638  -27.508 74.337  1.00 28.00  ? 17  LEU F C     1 
ATOM   7227  O O     . LEU F 2 15  ? 19.644  -26.814 74.143  1.00 25.99  ? 17  LEU F O     1 
ATOM   7228  C CB    . LEU F 2 15  ? 22.186  -26.819 76.214  1.00 31.74  ? 17  LEU F CB    1 
ATOM   7229  C CG    . LEU F 2 15  ? 21.786  -25.340 76.215  1.00 33.31  ? 17  LEU F CG    1 
ATOM   7230  C CD1   . LEU F 2 15  ? 20.624  -25.087 77.161  1.00 35.42  ? 17  LEU F CD1   1 
ATOM   7231  C CD2   . LEU F 2 15  ? 22.971  -24.462 76.578  1.00 32.52  ? 17  LEU F CD2   1 
ATOM   7232  N N     . MET F 2 16  ? 21.362  -28.043 73.349  1.00 29.74  ? 18  MET F N     1 
ATOM   7233  C CA    . MET F 2 16  ? 21.036  -27.819 71.950  1.00 32.07  ? 18  MET F CA    1 
ATOM   7234  C C     . MET F 2 16  ? 19.642  -28.367 71.652  1.00 33.46  ? 18  MET F C     1 
ATOM   7235  O O     . MET F 2 16  ? 18.828  -27.698 71.019  1.00 25.94  ? 18  MET F O     1 
ATOM   7236  C CB    . MET F 2 16  ? 22.057  -28.494 71.028  1.00 34.45  ? 18  MET F CB    1 
ATOM   7237  C CG    . MET F 2 16  ? 21.702  -28.401 69.558  1.00 37.76  ? 18  MET F CG    1 
ATOM   7238  S SD    . MET F 2 16  ? 21.680  -26.704 68.946  1.00 48.20  ? 18  MET F SD    1 
ATOM   7239  C CE    . MET F 2 16  ? 23.441  -26.393 68.753  1.00 40.64  ? 18  MET F CE    1 
ATOM   7240  N N     . GLU F 2 17  ? 19.382  -29.595 72.115  1.00 34.82  ? 19  GLU F N     1 
ATOM   7241  C CA    . GLU F 2 17  ? 18.100  -30.244 71.894  1.00 39.78  ? 19  GLU F CA    1 
ATOM   7242  C C     . GLU F 2 17  ? 17.013  -29.510 72.675  1.00 39.81  ? 19  GLU F C     1 
ATOM   7243  O O     . GLU F 2 17  ? 15.852  -29.502 72.271  1.00 34.52  ? 19  GLU F O     1 
ATOM   7244  C CB    . GLU F 2 17  ? 18.170  -31.719 72.290  1.00 44.14  ? 19  GLU F CB    1 
ATOM   7245  C CG    . GLU F 2 17  ? 19.016  -32.559 71.338  1.00 49.59  ? 19  GLU F CG    1 
ATOM   7246  C CD    . GLU F 2 17  ? 18.476  -32.615 69.919  1.00 57.68  ? 19  GLU F CD    1 
ATOM   7247  O OE1   . GLU F 2 17  ? 17.362  -33.148 69.731  1.00 65.45  ? 19  GLU F OE1   1 
ATOM   7248  O OE2   . GLU F 2 17  ? 19.166  -32.119 69.003  1.00 65.56  ? 19  GLU F OE2   1 
ATOM   7249  N N     . ASP F 2 18  ? 17.404  -28.903 73.801  1.00 42.51  ? 20  ASP F N     1 
ATOM   7250  C CA    . ASP F 2 18  ? 16.488  -28.110 74.602  1.00 40.45  ? 20  ASP F CA    1 
ATOM   7251  C C     . ASP F 2 18  ? 16.133  -26.841 73.833  1.00 32.58  ? 20  ASP F C     1 
ATOM   7252  O O     . ASP F 2 18  ? 14.979  -26.420 73.818  1.00 27.16  ? 20  ASP F O     1 
ATOM   7253  C CB    . ASP F 2 18  ? 17.072  -27.801 75.972  1.00 44.68  ? 20  ASP F CB    1 
ATOM   7254  C CG    . ASP F 2 18  ? 17.340  -29.012 76.855  1.00 52.60  ? 20  ASP F CG    1 
ATOM   7255  O OD1   . ASP F 2 18  ? 17.041  -30.140 76.410  1.00 57.57  ? 20  ASP F OD1   1 
ATOM   7256  O OD2   . ASP F 2 18  ? 17.846  -28.816 77.980  1.00 60.39  ? 20  ASP F OD2   1 
ATOM   7257  N N     . TYR F 2 19  ? 17.143  -26.247 73.188  1.00 34.56  ? 21  TYR F N     1 
ATOM   7258  C CA    . TYR F 2 19  ? 16.958  -25.026 72.422  1.00 32.83  ? 21  TYR F CA    1 
ATOM   7259  C C     . TYR F 2 19  ? 16.014  -25.302 71.255  1.00 36.66  ? 21  TYR F C     1 
ATOM   7260  O O     . TYR F 2 19  ? 15.121  -24.506 70.972  1.00 31.96  ? 21  TYR F O     1 
ATOM   7261  C CB    . TYR F 2 19  ? 18.305  -24.485 71.934  1.00 33.48  ? 21  TYR F CB    1 
ATOM   7262  C CG    . TYR F 2 19  ? 18.185  -23.274 71.018  1.00 29.56  ? 21  TYR F CG    1 
ATOM   7263  C CD1   . TYR F 2 19  ? 18.052  -21.993 71.537  1.00 28.60  ? 21  TYR F CD1   1 
ATOM   7264  C CD2   . TYR F 2 19  ? 18.185  -23.417 69.636  1.00 30.16  ? 21  TYR F CD2   1 
ATOM   7265  C CE1   . TYR F 2 19  ? 17.929  -20.889 70.710  1.00 28.68  ? 21  TYR F CE1   1 
ATOM   7266  C CE2   . TYR F 2 19  ? 18.063  -22.321 68.798  1.00 28.67  ? 21  TYR F CE2   1 
ATOM   7267  C CZ    . TYR F 2 19  ? 17.935  -21.054 69.337  1.00 28.28  ? 21  TYR F CZ    1 
ATOM   7268  O OH    . TYR F 2 19  ? 17.816  -19.970 68.517  1.00 28.93  ? 21  TYR F OH    1 
ATOM   7269  N N     . LYS F 2 20  ? 16.227  -26.440 70.586  1.00 43.64  ? 22  LYS F N     1 
ATOM   7270  C CA    . LYS F 2 20  ? 15.436  -26.817 69.426  1.00 46.31  ? 22  LYS F CA    1 
ATOM   7271  C C     . LYS F 2 20  ? 13.956  -26.846 69.797  1.00 41.77  ? 22  LYS F C     1 
ATOM   7272  O O     . LYS F 2 20  ? 13.108  -26.438 69.008  1.00 44.72  ? 22  LYS F O     1 
ATOM   7273  C CB    . LYS F 2 20  ? 15.880  -28.184 68.892  1.00 50.60  ? 22  LYS F CB    1 
ATOM   7274  C CG    . LYS F 2 20  ? 17.267  -28.220 68.262  1.00 56.21  ? 22  LYS F CG    1 
ATOM   7275  C CD    . LYS F 2 20  ? 17.400  -27.370 67.003  1.00 54.35  ? 22  LYS F CD    1 
ATOM   7276  C CE    . LYS F 2 20  ? 18.750  -27.488 66.369  1.00 62.80  ? 22  LYS F CE    1 
ATOM   7277  N NZ    . LYS F 2 20  ? 18.846  -26.695 65.141  1.00 61.19  ? 22  LYS F NZ    1 
ATOM   7278  N N     . GLN F 2 21  ? 13.662  -27.338 71.006  1.00 42.66  ? 23  GLN F N     1 
ATOM   7279  C CA    . GLN F 2 21  ? 12.290  -27.508 71.456  1.00 42.99  ? 23  GLN F CA    1 
ATOM   7280  C C     . GLN F 2 21  ? 11.637  -26.147 71.673  1.00 37.17  ? 23  GLN F C     1 
ATOM   7281  O O     . GLN F 2 21  ? 10.508  -25.924 71.240  1.00 29.91  ? 23  GLN F O     1 
ATOM   7282  C CB    . GLN F 2 21  ? 12.237  -28.336 72.740  1.00 50.69  ? 23  GLN F CB    1 
ATOM   7283  C CG    . GLN F 2 21  ? 12.503  -29.822 72.529  1.00 57.18  ? 23  GLN F CG    1 
ATOM   7284  C CD    . GLN F 2 21  ? 11.463  -30.490 71.656  1.00 69.42  ? 23  GLN F CD    1 
ATOM   7285  O OE1   . GLN F 2 21  ? 11.765  -31.017 70.580  1.00 80.31  ? 23  GLN F OE1   1 
ATOM   7286  N NE2   . GLN F 2 21  ? 10.219  -30.469 72.113  1.00 72.83  ? 23  GLN F NE2   1 
ATOM   7287  N N     . ASN F 2 22  ? 12.356  -25.247 72.354  1.00 30.55  ? 24  ASN F N     1 
ATOM   7288  C CA    . ASN F 2 22  ? 11.797  -23.965 72.746  1.00 30.13  ? 24  ASN F CA    1 
ATOM   7289  C C     . ASN F 2 22  ? 12.896  -22.905 72.748  1.00 27.84  ? 24  ASN F C     1 
ATOM   7290  O O     . ASN F 2 22  ? 13.464  -22.596 73.792  1.00 28.80  ? 24  ASN F O     1 
ATOM   7291  C CB    . ASN F 2 22  ? 11.114  -24.060 74.105  1.00 32.31  ? 24  ASN F CB    1 
ATOM   7292  C CG    . ASN F 2 22  ? 10.134  -22.935 74.328  1.00 33.26  ? 24  ASN F CG    1 
ATOM   7293  O OD1   . ASN F 2 22  ? 10.481  -21.761 74.151  1.00 38.37  ? 24  ASN F OD1   1 
ATOM   7294  N ND2   . ASN F 2 22  ? 8.906   -23.270 74.692  1.00 31.85  ? 24  ASN F ND2   1 
ATOM   7295  N N     . PRO F 2 23  ? 13.222  -22.314 71.576  1.00 26.66  ? 25  PRO F N     1 
ATOM   7296  C CA    . PRO F 2 23  ? 14.294  -21.320 71.481  1.00 29.26  ? 25  PRO F CA    1 
ATOM   7297  C C     . PRO F 2 23  ? 14.161  -20.167 72.473  1.00 29.96  ? 25  PRO F C     1 
ATOM   7298  O O     . PRO F 2 23  ? 15.094  -19.881 73.221  1.00 32.43  ? 25  PRO F O     1 
ATOM   7299  C CB    . PRO F 2 23  ? 14.187  -20.840 70.017  1.00 27.98  ? 25  PRO F CB    1 
ATOM   7300  C CG    . PRO F 2 23  ? 13.583  -22.020 69.286  1.00 27.42  ? 25  PRO F CG    1 
ATOM   7301  C CD    . PRO F 2 23  ? 12.595  -22.606 70.278  1.00 27.88  ? 25  PRO F CD    1 
ATOM   7302  N N     . GLU F 2 24  ? 12.999  -19.505 72.462  1.00 32.67  ? 26  GLU F N     1 
ATOM   7303  C CA    . GLU F 2 24  ? 12.784  -18.323 73.282  1.00 39.76  ? 26  GLU F CA    1 
ATOM   7304  C C     . GLU F 2 24  ? 12.921  -18.687 74.758  1.00 39.89  ? 26  GLU F C     1 
ATOM   7305  O O     . GLU F 2 24  ? 13.587  -17.982 75.514  1.00 39.58  ? 26  GLU F O     1 
ATOM   7306  C CB    . GLU F 2 24  ? 11.421  -17.686 73.008  1.00 46.01  ? 26  GLU F CB    1 
ATOM   7307  C CG    . GLU F 2 24  ? 11.342  -16.979 71.658  1.00 53.78  ? 26  GLU F CG    1 
ATOM   7308  C CD    . GLU F 2 24  ? 10.153  -16.044 71.516  1.00 59.17  ? 26  GLU F CD    1 
ATOM   7309  O OE1   . GLU F 2 24  ? 9.007   -16.513 71.677  1.00 70.37  ? 26  GLU F OE1   1 
ATOM   7310  O OE2   . GLU F 2 24  ? 10.376  -14.845 71.244  1.00 61.62  ? 26  GLU F OE2   1 
ATOM   7311  N N     . ALA F 2 25  ? 12.284  -19.793 75.156  1.00 36.10  ? 27  ALA F N     1 
ATOM   7312  C CA    . ALA F 2 25  ? 12.284  -20.222 76.545  1.00 39.26  ? 27  ALA F CA    1 
ATOM   7313  C C     . ALA F 2 25  ? 13.717  -20.404 77.038  1.00 40.09  ? 27  ALA F C     1 
ATOM   7314  O O     . ALA F 2 25  ? 14.061  -19.972 78.136  1.00 36.18  ? 27  ALA F O     1 
ATOM   7315  C CB    . ALA F 2 25  ? 11.483  -21.497 76.692  1.00 40.44  ? 27  ALA F CB    1 
ATOM   7316  N N     . VAL F 2 26  ? 14.545  -21.052 76.212  1.00 39.33  ? 28  VAL F N     1 
ATOM   7317  C CA    . VAL F 2 26  ? 15.918  -21.356 76.580  1.00 35.80  ? 28  VAL F CA    1 
ATOM   7318  C C     . VAL F 2 26  ? 16.715  -20.056 76.656  1.00 35.40  ? 28  VAL F C     1 
ATOM   7319  O O     . VAL F 2 26  ? 17.494  -19.855 77.584  1.00 36.82  ? 28  VAL F O     1 
ATOM   7320  C CB    . VAL F 2 26  ? 16.560  -22.347 75.590  1.00 37.32  ? 28  VAL F CB    1 
ATOM   7321  C CG1   . VAL F 2 26  ? 18.049  -22.530 75.857  1.00 35.08  ? 28  VAL F CG1   1 
ATOM   7322  C CG2   . VAL F 2 26  ? 15.844  -23.693 75.593  1.00 37.50  ? 28  VAL F CG2   1 
ATOM   7323  N N     . MET F 2 27  ? 16.507  -19.178 75.670  1.00 33.89  ? 29  MET F N     1 
ATOM   7324  C CA    . MET F 2 27  ? 17.261  -17.939 75.576  1.00 32.83  ? 29  MET F CA    1 
ATOM   7325  C C     . MET F 2 27  ? 16.915  -17.027 76.751  1.00 34.43  ? 29  MET F C     1 
ATOM   7326  O O     . MET F 2 27  ? 17.806  -16.455 77.375  1.00 33.74  ? 29  MET F O     1 
ATOM   7327  C CB    . MET F 2 27  ? 16.985  -17.227 74.246  1.00 30.26  ? 29  MET F CB    1 
ATOM   7328  C CG    . MET F 2 27  ? 17.724  -17.839 73.069  1.00 29.82  ? 29  MET F CG    1 
ATOM   7329  S SD    . MET F 2 27  ? 17.446  -16.972 71.512  1.00 27.49  ? 29  MET F SD    1 
ATOM   7330  C CE    . MET F 2 27  ? 15.712  -17.333 71.203  1.00 30.25  ? 29  MET F CE    1 
ATOM   7331  N N     . ARG F 2 28  ? 15.617  -16.906 77.050  1.00 35.14  ? 30  ARG F N     1 
ATOM   7332  C CA    . ARG F 2 28  ? 15.158  -16.030 78.116  1.00 38.87  ? 30  ARG F CA    1 
ATOM   7333  C C     . ARG F 2 28  ? 15.663  -16.560 79.456  1.00 36.20  ? 30  ARG F C     1 
ATOM   7334  O O     . ARG F 2 28  ? 15.830  -15.800 80.407  1.00 36.55  ? 30  ARG F O     1 
ATOM   7335  C CB    . ARG F 2 28  ? 13.628  -15.921 78.121  1.00 43.80  ? 30  ARG F CB    1 
ATOM   7336  C CG    . ARG F 2 28  ? 13.011  -15.798 76.735  1.00 52.25  ? 30  ARG F CG    1 
ATOM   7337  C CD    . ARG F 2 28  ? 11.550  -15.375 76.772  1.00 55.68  ? 30  ARG F CD    1 
ATOM   7338  N NE    . ARG F 2 28  ? 11.400  -13.941 77.043  1.00 60.50  ? 30  ARG F NE    1 
ATOM   7339  C CZ    . ARG F 2 28  ? 10.907  -13.061 76.179  1.00 69.00  ? 30  ARG F CZ    1 
ATOM   7340  N NH1   . ARG F 2 28  ? 10.508  -13.458 74.984  1.00 63.43  ? 30  ARG F NH1   1 
ATOM   7341  N NH2   . ARG F 2 28  ? 10.819  -11.785 76.511  1.00 77.95  ? 30  ARG F NH2   1 
ATOM   7342  N N     . ALA F 2 29  ? 15.909  -17.873 79.512  1.00 30.74  ? 31  ALA F N     1 
ATOM   7343  C CA    . ALA F 2 29  ? 16.361  -18.524 80.730  1.00 32.60  ? 31  ALA F CA    1 
ATOM   7344  C C     . ALA F 2 29  ? 17.860  -18.306 80.918  1.00 30.28  ? 31  ALA F C     1 
ATOM   7345  O O     . ALA F 2 29  ? 18.393  -18.539 82.002  1.00 29.71  ? 31  ALA F O     1 
ATOM   7346  C CB    . ALA F 2 29  ? 16.019  -19.996 80.685  1.00 32.59  ? 31  ALA F CB    1 
ATOM   7347  N N     . HIS F 2 30  ? 18.531  -17.859 79.850  1.00 28.85  ? 32  HIS F N     1 
ATOM   7348  C CA    . HIS F 2 30  ? 19.958  -17.583 79.896  1.00 31.54  ? 32  HIS F CA    1 
ATOM   7349  C C     . HIS F 2 30  ? 20.188  -16.073 79.882  1.00 31.35  ? 32  HIS F C     1 
ATOM   7350  O O     . HIS F 2 30  ? 21.311  -15.613 79.692  1.00 33.17  ? 32  HIS F O     1 
ATOM   7351  C CB    . HIS F 2 30  ? 20.685  -18.319 78.764  1.00 33.23  ? 32  HIS F CB    1 
ATOM   7352  C CG    . HIS F 2 30  ? 20.801  -19.790 78.990  1.00 33.47  ? 32  HIS F CG    1 
ATOM   7353  N ND1   . HIS F 2 30  ? 19.762  -20.668 78.767  1.00 33.29  ? 32  HIS F ND1   1 
ATOM   7354  C CD2   . HIS F 2 30  ? 21.819  -20.532 79.451  1.00 34.48  ? 32  HIS F CD2   1 
ATOM   7355  C CE1   . HIS F 2 30  ? 20.155  -21.897 79.070  1.00 33.68  ? 32  HIS F CE1   1 
ATOM   7356  N NE2   . HIS F 2 30  ? 21.401  -21.838 79.486  1.00 35.34  ? 32  HIS F NE2   1 
ATOM   7357  N N     . GLY F 2 31  ? 19.102  -15.315 80.071  1.00 32.62  ? 33  GLY F N     1 
ATOM   7358  C CA    . GLY F 2 31  ? 19.187  -13.892 80.361  1.00 31.96  ? 33  GLY F CA    1 
ATOM   7359  C C     . GLY F 2 31  ? 19.413  -13.048 79.109  1.00 32.43  ? 33  GLY F C     1 
ATOM   7360  O O     . GLY F 2 31  ? 19.931  -11.938 79.201  1.00 32.26  ? 33  GLY F O     1 
ATOM   7361  N N     . LEU F 2 32  ? 19.009  -13.571 77.946  1.00 33.84  ? 34  LEU F N     1 
ATOM   7362  C CA    . LEU F 2 32  ? 19.108  -12.818 76.705  1.00 34.36  ? 34  LEU F CA    1 
ATOM   7363  C C     . LEU F 2 32  ? 17.971  -11.801 76.646  1.00 35.73  ? 34  LEU F C     1 
ATOM   7364  O O     . LEU F 2 32  ? 16.820  -12.134 76.923  1.00 31.76  ? 34  LEU F O     1 
ATOM   7365  C CB    . LEU F 2 32  ? 19.092  -13.744 75.490  1.00 33.87  ? 34  LEU F CB    1 
ATOM   7366  C CG    . LEU F 2 32  ? 20.403  -14.475 75.183  1.00 34.10  ? 34  LEU F CG    1 
ATOM   7367  C CD1   . LEU F 2 32  ? 20.720  -15.520 76.238  1.00 36.04  ? 34  LEU F CD1   1 
ATOM   7368  C CD2   . LEU F 2 32  ? 20.356  -15.103 73.800  1.00 33.90  ? 34  LEU F CD2   1 
ATOM   7369  N N     . THR F 2 33  ? 18.313  -10.561 76.277  1.00 39.65  ? 35  THR F N     1 
ATOM   7370  C CA    . THR F 2 33  ? 17.346  -9.478  76.212  1.00 41.44  ? 35  THR F CA    1 
ATOM   7371  C C     . THR F 2 33  ? 16.385  -9.731  75.054  1.00 41.21  ? 35  THR F C     1 
ATOM   7372  O O     . THR F 2 33  ? 16.614  -10.615 74.231  1.00 38.41  ? 35  THR F O     1 
ATOM   7373  C CB    . THR F 2 33  ? 18.070  -8.141  76.053  1.00 42.52  ? 35  THR F CB    1 
ATOM   7374  O OG1   . THR F 2 33  ? 18.742  -8.226  74.800  1.00 44.94  ? 35  THR F OG1   1 
ATOM   7375  C CG2   . THR F 2 33  ? 19.058  -7.874  77.174  1.00 40.71  ? 35  THR F CG2   1 
ATOM   7376  N N     . ASP F 2 34  ? 15.318  -8.927  75.001  1.00 40.10  ? 36  ASP F N     1 
ATOM   7377  C CA    . ASP F 2 34  ? 14.281  -9.072  73.993  1.00 46.34  ? 36  ASP F CA    1 
ATOM   7378  C C     . ASP F 2 34  ? 14.844  -8.708  72.622  1.00 44.27  ? 36  ASP F C     1 
ATOM   7379  O O     . ASP F 2 34  ? 14.453  -9.289  71.613  1.00 39.39  ? 36  ASP F O     1 
ATOM   7380  C CB    . ASP F 2 34  ? 13.063  -8.226  74.333  1.00 50.64  ? 36  ASP F CB    1 
ATOM   7381  C CG    . ASP F 2 34  ? 12.394  -8.546  75.662  1.00 57.66  ? 36  ASP F CG    1 
ATOM   7382  O OD1   . ASP F 2 34  ? 11.913  -9.688  75.816  1.00 62.49  ? 36  ASP F OD1   1 
ATOM   7383  O OD2   . ASP F 2 34  ? 12.361  -7.651  76.532  1.00 61.27  ? 36  ASP F OD2   1 
ATOM   7384  N N     . GLU F 2 35  ? 15.756  -7.730  72.602  1.00 46.28  ? 37  GLU F N     1 
ATOM   7385  C CA    . GLU F 2 35  ? 16.359  -7.261  71.365  1.00 47.60  ? 37  GLU F CA    1 
ATOM   7386  C C     . GLU F 2 35  ? 17.334  -8.315  70.847  1.00 46.28  ? 37  GLU F C     1 
ATOM   7387  O O     . GLU F 2 35  ? 17.485  -8.487  69.639  1.00 46.25  ? 37  GLU F O     1 
ATOM   7388  C CB    . GLU F 2 35  ? 17.070  -5.925  71.586  1.00 50.30  ? 37  GLU F CB    1 
ATOM   7389  C CG    . GLU F 2 35  ? 18.201  -6.002  72.608  1.00 55.82  ? 37  GLU F CG    1 
ATOM   7390  C CD    . GLU F 2 35  ? 18.905  -4.681  72.859  1.00 58.75  ? 37  GLU F CD    1 
ATOM   7391  O OE1   . GLU F 2 35  ? 19.451  -4.108  71.894  1.00 68.75  ? 37  GLU F OE1   1 
ATOM   7392  O OE2   . GLU F 2 35  ? 18.909  -4.225  74.022  1.00 60.80  ? 37  GLU F OE2   1 
ATOM   7393  N N     . GLN F 2 36  ? 17.997  -9.008  71.779  1.00 44.86  ? 38  GLN F N     1 
ATOM   7394  C CA    . GLN F 2 36  ? 18.941  -10.058 71.437  1.00 41.04  ? 38  GLN F CA    1 
ATOM   7395  C C     . GLN F 2 36  ? 18.179  -11.261 70.886  1.00 39.80  ? 38  GLN F C     1 
ATOM   7396  O O     . GLN F 2 36  ? 18.649  -11.934 69.971  1.00 41.06  ? 38  GLN F O     1 
ATOM   7397  C CB    . GLN F 2 36  ? 19.767  -10.453 72.661  1.00 39.70  ? 38  GLN F CB    1 
ATOM   7398  C CG    . GLN F 2 36  ? 20.676  -9.344  73.180  1.00 42.80  ? 38  GLN F CG    1 
ATOM   7399  C CD    . GLN F 2 36  ? 21.395  -9.716  74.459  1.00 44.76  ? 38  GLN F CD    1 
ATOM   7400  O OE1   . GLN F 2 36  ? 21.156  -10.776 75.049  1.00 44.14  ? 38  GLN F OE1   1 
ATOM   7401  N NE2   . GLN F 2 36  ? 22.279  -8.837  74.907  1.00 44.88  ? 38  GLN F NE2   1 
ATOM   7402  N N     . ILE F 2 37  ? 16.999  -11.516 71.459  1.00 36.39  ? 39  ILE F N     1 
ATOM   7403  C CA    . ILE F 2 37  ? 16.170  -12.637 71.050  1.00 35.52  ? 39  ILE F CA    1 
ATOM   7404  C C     . ILE F 2 37  ? 15.564  -12.333 69.683  1.00 34.85  ? 39  ILE F C     1 
ATOM   7405  O O     . ILE F 2 37  ? 15.488  -13.209 68.826  1.00 35.23  ? 39  ILE F O     1 
ATOM   7406  C CB    . ILE F 2 37  ? 15.087  -12.932 72.103  1.00 34.57  ? 39  ILE F CB    1 
ATOM   7407  C CG1   . ILE F 2 37  ? 15.703  -13.375 73.430  1.00 35.82  ? 39  ILE F CG1   1 
ATOM   7408  C CG2   . ILE F 2 37  ? 14.080  -13.957 71.580  1.00 34.76  ? 39  ILE F CG2   1 
ATOM   7409  C CD1   . ILE F 2 37  ? 14.686  -13.699 74.508  1.00 38.04  ? 39  ILE F CD1   1 
ATOM   7410  N N     . ASN F 2 38  ? 15.137  -11.080 69.496  1.00 39.84  ? 40  ASN F N     1 
ATOM   7411  C CA    . ASN F 2 38  ? 14.533  -10.651 68.246  1.00 43.10  ? 40  ASN F CA    1 
ATOM   7412  C C     . ASN F 2 38  ? 15.540  -10.822 67.113  1.00 41.92  ? 40  ASN F C     1 
ATOM   7413  O O     . ASN F 2 38  ? 15.197  -11.314 66.040  1.00 43.88  ? 40  ASN F O     1 
ATOM   7414  C CB    . ASN F 2 38  ? 14.036  -9.212  68.326  1.00 43.80  ? 40  ASN F CB    1 
ATOM   7415  C CG    . ASN F 2 38  ? 13.451  -8.743  67.016  1.00 46.46  ? 40  ASN F CG    1 
ATOM   7416  O OD1   . ASN F 2 38  ? 12.454  -9.301  66.545  1.00 46.58  ? 40  ASN F OD1   1 
ATOM   7417  N ND2   . ASN F 2 38  ? 14.053  -7.728  66.412  1.00 41.85  ? 40  ASN F ND2   1 
ATOM   7418  N N     . ALA F 2 39  ? 16.783  -10.402 67.367  1.00 38.70  ? 41  ALA F N     1 
ATOM   7419  C CA    . ALA F 2 39  ? 17.846  -10.505 66.382  1.00 39.83  ? 41  ALA F CA    1 
ATOM   7420  C C     . ALA F 2 39  ? 18.023  -11.962 65.966  1.00 34.90  ? 41  ALA F C     1 
ATOM   7421  O O     . ALA F 2 39  ? 18.208  -12.258 64.788  1.00 39.40  ? 41  ALA F O     1 
ATOM   7422  C CB    . ALA F 2 39  ? 19.127  -9.930  66.945  1.00 39.33  ? 41  ALA F CB    1 
ATOM   7423  N N     . VAL F 2 40  ? 17.956  -12.864 66.950  1.00 33.16  ? 42  VAL F N     1 
ATOM   7424  C CA    . VAL F 2 40  ? 18.137  -14.285 66.707  1.00 33.22  ? 42  VAL F CA    1 
ATOM   7425  C C     . VAL F 2 40  ? 16.982  -14.797 65.850  1.00 31.00  ? 42  VAL F C     1 
ATOM   7426  O O     . VAL F 2 40  ? 17.195  -15.554 64.908  1.00 28.69  ? 42  VAL F O     1 
ATOM   7427  C CB    . VAL F 2 40  ? 18.243  -15.077 68.025  1.00 32.50  ? 42  VAL F CB    1 
ATOM   7428  C CG1   . VAL F 2 40  ? 18.137  -16.580 67.795  1.00 31.71  ? 42  VAL F CG1   1 
ATOM   7429  C CG2   . VAL F 2 40  ? 19.517  -14.737 68.789  1.00 33.40  ? 42  VAL F CG2   1 
ATOM   7430  N N     . MET F 2 41  ? 15.762  -14.368 66.187  1.00 32.76  ? 43  MET F N     1 
ATOM   7431  C CA    . MET F 2 41  ? 14.565  -14.873 65.534  1.00 35.12  ? 43  MET F CA    1 
ATOM   7432  C C     . MET F 2 41  ? 14.472  -14.321 64.112  1.00 34.73  ? 43  MET F C     1 
ATOM   7433  O O     . MET F 2 41  ? 13.950  -14.986 63.221  1.00 33.85  ? 43  MET F O     1 
ATOM   7434  C CB    . MET F 2 41  ? 13.307  -14.501 66.326  1.00 37.72  ? 43  MET F CB    1 
ATOM   7435  C CG    . MET F 2 41  ? 13.201  -15.197 67.672  1.00 40.56  ? 43  MET F CG    1 
ATOM   7436  S SD    . MET F 2 41  ? 13.415  -16.984 67.550  1.00 49.19  ? 43  MET F SD    1 
ATOM   7437  C CE    . MET F 2 41  ? 12.279  -17.357 66.208  1.00 50.62  ? 43  MET F CE    1 
ATOM   7438  N N     . THR F 2 42  ? 14.979  -13.100 63.910  1.00 37.80  ? 44  THR F N     1 
ATOM   7439  C CA    . THR F 2 42  ? 14.973  -12.482 62.594  1.00 39.66  ? 44  THR F CA    1 
ATOM   7440  C C     . THR F 2 42  ? 16.255  -12.864 61.860  1.00 39.52  ? 44  THR F C     1 
ATOM   7441  O O     . THR F 2 42  ? 16.374  -12.653 60.655  1.00 44.06  ? 44  THR F O     1 
ATOM   7442  C CB    . THR F 2 42  ? 14.824  -10.967 62.727  1.00 42.15  ? 44  THR F CB    1 
ATOM   7443  O OG1   . THR F 2 42  ? 15.917  -10.544 63.538  1.00 43.95  ? 44  THR F OG1   1 
ATOM   7444  C CG2   . THR F 2 42  ? 13.505  -10.566 63.363  1.00 43.46  ? 44  THR F CG2   1 
ATOM   7445  N N     . GLY F 2 43  ? 17.210  -13.429 62.606  1.00 39.06  ? 45  GLY F N     1 
ATOM   7446  C CA    . GLY F 2 43  ? 18.457  -13.906 62.035  1.00 40.77  ? 45  GLY F CA    1 
ATOM   7447  C C     . GLY F 2 43  ? 19.349  -12.752 61.585  1.00 45.90  ? 45  GLY F C     1 
ATOM   7448  O O     . GLY F 2 43  ? 20.064  -12.866 60.592  1.00 38.24  ? 45  GLY F O     1 
ATOM   7449  N N     . ASP F 2 44  ? 19.294  -11.641 62.328  1.00 45.47  ? 46  ASP F N     1 
ATOM   7450  C CA    . ASP F 2 44  ? 20.142  -10.492 62.057  1.00 46.90  ? 46  ASP F CA    1 
ATOM   7451  C C     . ASP F 2 44  ? 21.471  -10.678 62.783  1.00 48.76  ? 46  ASP F C     1 
ATOM   7452  O O     . ASP F 2 44  ? 21.638  -10.217 63.909  1.00 49.13  ? 46  ASP F O     1 
ATOM   7453  C CB    . ASP F 2 44  ? 19.456  -9.192  62.447  1.00 53.81  ? 46  ASP F CB    1 
ATOM   7454  C CG    . ASP F 2 44  ? 20.261  -7.927  62.187  1.00 57.81  ? 46  ASP F CG    1 
ATOM   7455  O OD1   . ASP F 2 44  ? 21.409  -8.050  61.711  1.00 56.24  ? 46  ASP F OD1   1 
ATOM   7456  O OD2   . ASP F 2 44  ? 19.733  -6.828  62.459  1.00 59.58  ? 46  ASP F OD2   1 
ATOM   7457  N N     . MET F 2 45  ? 22.409  -11.363 62.119  1.00 46.43  ? 47  MET F N     1 
ATOM   7458  C CA    . MET F 2 45  ? 23.701  -11.674 62.708  1.00 45.95  ? 47  MET F CA    1 
ATOM   7459  C C     . MET F 2 45  ? 24.446  -10.379 63.029  1.00 48.85  ? 47  MET F C     1 
ATOM   7460  O O     . MET F 2 45  ? 25.131  -10.290 64.045  1.00 45.53  ? 47  MET F O     1 
ATOM   7461  C CB    . MET F 2 45  ? 24.549  -12.528 61.758  1.00 46.99  ? 47  MET F CB    1 
ATOM   7462  C CG    . MET F 2 45  ? 23.982  -13.911 61.477  1.00 46.26  ? 47  MET F CG    1 
ATOM   7463  S SD    . MET F 2 45  ? 23.730  -14.908 62.959  1.00 48.00  ? 47  MET F SD    1 
ATOM   7464  C CE    . MET F 2 45  ? 22.088  -14.385 63.473  1.00 47.15  ? 47  MET F CE    1 
ATOM   7465  N N     . GLU F 2 46  ? 24.302  -9.382  62.149  1.00 53.34  ? 48  GLU F N     1 
ATOM   7466  C CA    . GLU F 2 46  ? 24.996  -8.114  62.298  1.00 57.80  ? 48  GLU F CA    1 
ATOM   7467  C C     . GLU F 2 46  ? 24.745  -7.546  63.693  1.00 55.80  ? 48  GLU F C     1 
ATOM   7468  O O     . GLU F 2 46  ? 25.685  -7.198  64.404  1.00 58.14  ? 48  GLU F O     1 
ATOM   7469  C CB    . GLU F 2 46  ? 24.543  -7.122  61.226  1.00 65.02  ? 48  GLU F CB    1 
ATOM   7470  C CG    . GLU F 2 46  ? 24.990  -7.508  59.820  1.00 70.10  ? 48  GLU F CG    1 
ATOM   7471  C CD    . GLU F 2 46  ? 26.495  -7.620  59.665  1.00 76.74  ? 48  GLU F CD    1 
ATOM   7472  O OE1   . GLU F 2 46  ? 26.947  -7.986  58.560  1.00 85.24  ? 48  GLU F OE1   1 
ATOM   7473  O OE2   . GLU F 2 46  ? 27.213  -7.342  60.650  1.00 81.24  ? 48  GLU F OE2   1 
ATOM   7474  N N     . LYS F 2 47  ? 23.466  -7.455  64.067  1.00 56.31  ? 49  LYS F N     1 
ATOM   7475  C CA    . LYS F 2 47  ? 23.071  -6.846  65.326  1.00 52.88  ? 49  LYS F CA    1 
ATOM   7476  C C     . LYS F 2 47  ? 23.652  -7.642  66.492  1.00 48.90  ? 49  LYS F C     1 
ATOM   7477  O O     . LYS F 2 47  ? 24.050  -7.066  67.502  1.00 49.75  ? 49  LYS F O     1 
ATOM   7478  C CB    . LYS F 2 47  ? 21.544  -6.765  65.427  1.00 58.98  ? 49  LYS F CB    1 
ATOM   7479  C CG    . LYS F 2 47  ? 21.020  -6.108  66.698  1.00 66.70  ? 49  LYS F CG    1 
ATOM   7480  C CD    . LYS F 2 47  ? 19.499  -6.060  66.794  1.00 74.35  ? 49  LYS F CD    1 
ATOM   7481  C CE    . LYS F 2 47  ? 18.871  -5.266  65.693  1.00 78.44  ? 49  LYS F CE    1 
ATOM   7482  N NZ    . LYS F 2 47  ? 19.308  -3.868  65.711  1.00 80.64  ? 49  LYS F NZ    1 
ATOM   7483  N N     . LEU F 2 48  ? 23.689  -8.971  66.344  1.00 45.49  ? 50  LEU F N     1 
ATOM   7484  C CA    . LEU F 2 48  ? 24.185  -9.845  67.394  1.00 45.86  ? 50  LEU F CA    1 
ATOM   7485  C C     . LEU F 2 48  ? 25.614  -9.447  67.753  1.00 47.65  ? 50  LEU F C     1 
ATOM   7486  O O     . LEU F 2 48  ? 25.989  -9.449  68.923  1.00 44.02  ? 50  LEU F O     1 
ATOM   7487  C CB    . LEU F 2 48  ? 24.108  -11.307 66.957  1.00 47.74  ? 50  LEU F CB    1 
ATOM   7488  C CG    . LEU F 2 48  ? 22.700  -11.890 66.803  1.00 50.11  ? 50  LEU F CG    1 
ATOM   7489  C CD1   . LEU F 2 48  ? 22.761  -13.390 66.567  1.00 50.94  ? 50  LEU F CD1   1 
ATOM   7490  C CD2   . LEU F 2 48  ? 21.843  -11.571 68.015  1.00 50.75  ? 50  LEU F CD2   1 
ATOM   7491  N N     . LYS F 2 49  ? 26.403  -9.107  66.729  1.00 53.04  ? 51  LYS F N     1 
ATOM   7492  C CA    . LYS F 2 49  ? 27.797  -8.745  66.920  1.00 62.99  ? 51  LYS F CA    1 
ATOM   7493  C C     . LYS F 2 49  ? 27.877  -7.397  67.633  1.00 62.84  ? 51  LYS F C     1 
ATOM   7494  O O     . LYS F 2 49  ? 28.662  -7.228  68.563  1.00 68.98  ? 51  LYS F O     1 
ATOM   7495  C CB    . LYS F 2 49  ? 28.524  -8.731  65.570  1.00 67.16  ? 51  LYS F CB    1 
ATOM   7496  C CG    . LYS F 2 49  ? 28.546  -10.075 64.852  1.00 70.11  ? 51  LYS F CG    1 
ATOM   7497  C CD    . LYS F 2 49  ? 29.298  -10.072 63.527  1.00 77.07  ? 51  LYS F CD    1 
ATOM   7498  C CE    . LYS F 2 49  ? 29.317  -11.421 62.880  1.00 79.52  ? 51  LYS F CE    1 
ATOM   7499  N NZ    . LYS F 2 49  ? 30.050  -11.408 61.612  1.00 83.05  ? 51  LYS F NZ    1 
ATOM   7500  N N     . THR F 2 50  ? 27.046  -6.447  67.190  1.00 57.07  ? 52  THR F N     1 
ATOM   7501  C CA    . THR F 2 50  ? 26.998  -5.124  67.789  1.00 60.96  ? 52  THR F CA    1 
ATOM   7502  C C     . THR F 2 50  ? 26.676  -5.255  69.275  1.00 59.83  ? 52  THR F C     1 
ATOM   7503  O O     . THR F 2 50  ? 27.310  -4.617  70.113  1.00 60.12  ? 52  THR F O     1 
ATOM   7504  C CB    . THR F 2 50  ? 25.957  -4.271  67.065  1.00 61.64  ? 52  THR F CB    1 
ATOM   7505  O OG1   . THR F 2 50  ? 26.419  -4.167  65.723  1.00 69.04  ? 52  THR F OG1   1 
ATOM   7506  C CG2   . THR F 2 50  ? 25.807  -2.889  67.675  1.00 65.60  ? 52  THR F CG2   1 
ATOM   7507  N N     . LEU F 2 51  ? 25.683  -6.094  69.585  1.00 57.46  ? 53  LEU F N     1 
ATOM   7508  C CA    . LEU F 2 51  ? 25.182  -6.237  70.941  1.00 56.16  ? 53  LEU F CA    1 
ATOM   7509  C C     . LEU F 2 51  ? 26.213  -6.956  71.808  1.00 60.08  ? 53  LEU F C     1 
ATOM   7510  O O     . LEU F 2 51  ? 26.050  -7.043  73.023  1.00 61.91  ? 53  LEU F O     1 
ATOM   7511  C CB    . LEU F 2 51  ? 23.850  -6.985  70.915  1.00 51.59  ? 53  LEU F CB    1 
ATOM   7512  C CG    . LEU F 2 51  ? 22.703  -6.283  70.179  1.00 49.57  ? 53  LEU F CG    1 
ATOM   7513  C CD1   . LEU F 2 51  ? 21.402  -7.056  70.321  1.00 44.86  ? 53  LEU F CD1   1 
ATOM   7514  C CD2   . LEU F 2 51  ? 22.537  -4.859  70.678  1.00 51.91  ? 53  LEU F CD2   1 
ATOM   7515  N N     . SER F 2 52  ? 27.276  -7.462  71.174  1.00 65.01  ? 54  SER F N     1 
ATOM   7516  C CA    . SER F 2 52  ? 28.305  -8.208  71.881  1.00 65.90  ? 54  SER F CA    1 
ATOM   7517  C C     . SER F 2 52  ? 29.613  -7.422  71.889  1.00 70.40  ? 54  SER F C     1 
ATOM   7518  O O     . SER F 2 52  ? 30.530  -7.745  72.641  1.00 72.11  ? 54  SER F O     1 
ATOM   7519  C CB    . SER F 2 52  ? 28.497  -9.574  71.273  1.00 64.36  ? 54  SER F CB    1 
ATOM   7520  O OG    . SER F 2 52  ? 29.366  -10.370 72.068  1.00 65.53  ? 54  SER F OG    1 
ATOM   7521  N N     . GLY F 2 53  ? 29.682  -6.387  71.046  1.00 74.39  ? 55  GLY F N     1 
ATOM   7522  C CA    . GLY F 2 53  ? 30.903  -5.621  70.860  1.00 78.18  ? 55  GLY F CA    1 
ATOM   7523  C C     . GLY F 2 53  ? 31.614  -6.046  69.578  1.00 74.31  ? 55  GLY F C     1 
ATOM   7524  O O     . GLY F 2 53  ? 32.042  -5.209  68.787  1.00 68.08  ? 55  GLY F O     1 
ATOM   7525  N N     . ASP F 2 54  ? 31.730  -7.366  69.397  1.00 76.51  ? 56  ASP F N     1 
ATOM   7526  C CA    . ASP F 2 54  ? 32.248  -7.945  68.171  1.00 81.75  ? 56  ASP F CA    1 
ATOM   7527  C C     . ASP F 2 54  ? 32.186  -6.898  67.052  1.00 83.89  ? 56  ASP F C     1 
ATOM   7528  O O     . ASP F 2 54  ? 31.083  -6.732  66.485  1.00 85.17  ? 56  ASP F O     1 
ATOM   7529  C CB    . ASP F 2 54  ? 31.487  -9.213  67.813  1.00 89.47  ? 56  ASP F CB    1 
ATOM   7530  C CG    . ASP F 2 54  ? 31.919  -9.903  66.528  1.00 103.20 ? 56  ASP F CG    1 
ATOM   7531  O OD1   . ASP F 2 54  ? 32.817  -9.364  65.846  1.00 121.99 ? 56  ASP F OD1   1 
ATOM   7532  O OD2   . ASP F 2 54  ? 31.357  -10.975 66.221  1.00 105.85 ? 56  ASP F OD2   1 
ATOM   7533  N N     . LEU F 2 61  ? 38.115  -13.512 55.422  1.00 53.81  ? 63  LEU F N     1 
ATOM   7534  C CA    . LEU F 2 61  ? 38.108  -14.990 55.591  1.00 53.86  ? 63  LEU F CA    1 
ATOM   7535  C C     . LEU F 2 61  ? 38.848  -15.649 54.429  1.00 47.78  ? 63  LEU F C     1 
ATOM   7536  O O     . LEU F 2 61  ? 38.918  -16.873 54.354  1.00 49.43  ? 63  LEU F O     1 
ATOM   7537  C CB    . LEU F 2 61  ? 36.679  -15.525 55.692  1.00 48.45  ? 63  LEU F CB    1 
ATOM   7538  C CG    . LEU F 2 61  ? 35.948  -15.279 57.015  1.00 58.58  ? 63  LEU F CG    1 
ATOM   7539  C CD1   . LEU F 2 61  ? 35.201  -16.543 57.413  1.00 58.46  ? 63  LEU F CD1   1 
ATOM   7540  C CD2   . LEU F 2 61  ? 36.881  -14.824 58.123  1.00 56.13  ? 63  LEU F CD2   1 
ATOM   7541  N N     . VAL F 2 62  ? 39.397  -14.829 53.528  1.00 49.02  ? 64  VAL F N     1 
ATOM   7542  C CA    . VAL F 2 62  ? 40.030  -15.341 52.325  1.00 51.61  ? 64  VAL F CA    1 
ATOM   7543  C C     . VAL F 2 62  ? 41.454  -15.813 52.609  1.00 47.75  ? 64  VAL F C     1 
ATOM   7544  O O     . VAL F 2 62  ? 42.308  -15.002 52.972  1.00 47.20  ? 64  VAL F O     1 
ATOM   7545  C CB    . VAL F 2 62  ? 40.014  -14.272 51.217  1.00 54.31  ? 64  VAL F CB    1 
ATOM   7546  C CG1   . VAL F 2 62  ? 40.334  -14.873 49.854  1.00 55.56  ? 64  VAL F CG1   1 
ATOM   7547  C CG2   . VAL F 2 62  ? 38.687  -13.525 51.170  1.00 56.05  ? 64  VAL F CG2   1 
HETATM 7548  N N     . IML F 2 63  ? 41.751  -17.128 52.459  1.00 44.60  ? 65  IML F N     1 
HETATM 7549  C CA    . IML F 2 63  ? 43.106  -17.641 52.717  1.00 41.87  ? 65  IML F CA    1 
HETATM 7550  C C     . IML F 2 63  ? 43.721  -18.337 51.503  1.00 45.55  ? 65  IML F C     1 
HETATM 7551  O O     . IML F 2 63  ? 44.622  -19.161 51.651  1.00 41.05  ? 65  IML F O     1 
HETATM 7552  C CB    . IML F 2 63  ? 43.093  -18.593 53.934  1.00 37.69  ? 65  IML F CB    1 
HETATM 7553  C CN    . IML F 2 63  ? 40.727  -18.084 52.080  1.00 43.98  ? 65  IML F CN    1 
HETATM 7554  C CG2   . IML F 2 63  ? 44.491  -18.781 54.504  1.00 39.10  ? 65  IML F CG2   1 
HETATM 7555  C CG1   . IML F 2 63  ? 42.104  -18.126 55.006  1.00 37.35  ? 65  IML F CG1   1 
HETATM 7556  C CD1   . IML F 2 63  ? 42.078  -19.003 56.238  1.00 34.76  ? 65  IML F CD1   1 
ATOM   7557  N N     . SER F 2 64  ? 43.239  -17.993 50.302  1.00 47.52  ? 66  SER F N     1 
ATOM   7558  C CA    . SER F 2 64  ? 43.769  -18.571 49.077  1.00 48.76  ? 66  SER F CA    1 
ATOM   7559  C C     . SER F 2 64  ? 43.412  -17.693 47.881  1.00 50.45  ? 66  SER F C     1 
ATOM   7560  O O     . SER F 2 64  ? 42.607  -16.771 47.998  1.00 59.13  ? 66  SER F O     1 
ATOM   7561  C CB    . SER F 2 64  ? 43.272  -19.982 48.880  1.00 49.05  ? 66  SER F CB    1 
ATOM   7562  O OG    . SER F 2 64  ? 41.864  -20.007 48.688  1.00 47.96  ? 66  SER F OG    1 
ATOM   7563  N N     . HIS F 2 65  ? 44.024  -17.999 46.731  1.00 53.10  ? 67  HIS F N     1 
ATOM   7564  C CA    . HIS F 2 65  ? 43.765  -17.278 45.496  1.00 58.23  ? 67  HIS F CA    1 
ATOM   7565  C C     . HIS F 2 65  ? 43.644  -18.274 44.346  1.00 58.75  ? 67  HIS F C     1 
ATOM   7566  O O     . HIS F 2 65  ? 43.763  -19.481 44.549  1.00 54.39  ? 67  HIS F O     1 
ATOM   7567  C CB    . HIS F 2 65  ? 44.859  -16.236 45.234  1.00 62.62  ? 67  HIS F CB    1 
ATOM   7568  C CG    . HIS F 2 65  ? 46.244  -16.795 45.239  1.00 67.85  ? 67  HIS F CG    1 
ATOM   7569  N ND1   . HIS F 2 65  ? 46.773  -17.496 44.177  1.00 66.13  ? 67  HIS F ND1   1 
ATOM   7570  C CD2   . HIS F 2 65  ? 47.197  -16.774 46.180  1.00 71.45  ? 67  HIS F CD2   1 
ATOM   7571  C CE1   . HIS F 2 65  ? 48.009  -17.870 44.474  1.00 73.24  ? 67  HIS F CE1   1 
ATOM   7572  N NE2   . HIS F 2 65  ? 48.288  -17.441 45.684  1.00 73.53  ? 67  HIS F NE2   1 
ATOM   7573  N N     . GLY F 2 66  ? 43.407  -17.750 43.138  1.00 67.06  ? 68  GLY F N     1 
ATOM   7574  C CA    . GLY F 2 66  ? 43.244  -18.577 41.954  1.00 68.43  ? 68  GLY F CA    1 
ATOM   7575  C C     . GLY F 2 66  ? 44.080  -18.058 40.788  1.00 71.00  ? 68  GLY F C     1 
ATOM   7576  O O     . GLY F 2 66  ? 43.738  -18.276 39.628  1.00 68.20  ? 68  GLY F O     1 
ATOM   7577  N N     . ASN F 2 67  ? 45.181  -17.371 41.114  1.00 68.89  ? 69  ASN F N     1 
ATOM   7578  C CA    . ASN F 2 67  ? 46.083  -16.835 40.108  1.00 66.15  ? 69  ASN F CA    1 
ATOM   7579  C C     . ASN F 2 67  ? 47.271  -17.779 39.944  1.00 66.88  ? 69  ASN F C     1 
ATOM   7580  O O     . ASN F 2 67  ? 48.199  -17.492 39.191  1.00 60.12  ? 69  ASN F O     1 
ATOM   7581  C CB    . ASN F 2 67  ? 46.531  -15.420 40.457  1.00 63.34  ? 69  ASN F CB    1 
ATOM   7582  C CG    . ASN F 2 67  ? 45.384  -14.439 40.435  1.00 63.28  ? 69  ASN F CG    1 
ATOM   7583  O OD1   . ASN F 2 67  ? 44.241  -14.823 40.161  1.00 61.64  ? 69  ASN F OD1   1 
ATOM   7584  N ND2   . ASN F 2 67  ? 45.664  -13.175 40.714  1.00 64.70  ? 69  ASN F ND2   1 
ATOM   7585  N N     . GLY F 2 68  ? 47.225  -18.908 40.659  1.00 68.45  ? 70  GLY F N     1 
ATOM   7586  C CA    . GLY F 2 68  ? 48.281  -19.905 40.599  1.00 69.93  ? 70  GLY F CA    1 
ATOM   7587  C C     . GLY F 2 68  ? 49.468  -19.505 41.456  1.00 65.45  ? 70  GLY F C     1 
ATOM   7588  O O     . GLY F 2 68  ? 49.669  -18.283 41.616  1.00 62.86  ? 70  GLY F O     1 
ATOM   7589  N N     . GLY G 1 1   ? 10.252  -39.131 69.168  1.00 39.31  ? 2   GLY G N     1 
ATOM   7590  C CA    . GLY G 1 1   ? 11.490  -39.690 68.591  1.00 37.52  ? 2   GLY G CA    1 
ATOM   7591  C C     . GLY G 1 1   ? 12.175  -38.684 67.670  1.00 40.71  ? 2   GLY G C     1 
ATOM   7592  O O     . GLY G 1 1   ? 11.532  -37.775 67.148  1.00 40.13  ? 2   GLY G O     1 
ATOM   7593  N N     . SER G 1 2   ? 13.488  -38.861 67.487  1.00 37.07  ? 3   SER G N     1 
ATOM   7594  C CA    . SER G 1 2   ? 14.274  -37.992 66.627  1.00 35.74  ? 3   SER G CA    1 
ATOM   7595  C C     . SER G 1 2   ? 15.517  -38.734 66.145  1.00 34.47  ? 3   SER G C     1 
ATOM   7596  O O     . SER G 1 2   ? 15.914  -39.736 66.736  1.00 29.05  ? 3   SER G O     1 
ATOM   7597  C CB    . SER G 1 2   ? 14.641  -36.713 67.339  1.00 37.69  ? 3   SER G CB    1 
ATOM   7598  O OG    . SER G 1 2   ? 15.466  -36.975 68.466  1.00 40.86  ? 3   SER G OG    1 
ATOM   7599  N N     . LEU G 1 3   ? 16.123  -38.229 65.066  1.00 33.44  ? 4   LEU G N     1 
ATOM   7600  C CA    . LEU G 1 3   ? 17.308  -38.846 64.495  1.00 33.39  ? 4   LEU G CA    1 
ATOM   7601  C C     . LEU G 1 3   ? 18.393  -37.793 64.294  1.00 32.45  ? 4   LEU G C     1 
ATOM   7602  O O     . LEU G 1 3   ? 18.135  -36.715 63.762  1.00 30.76  ? 4   LEU G O     1 
ATOM   7603  C CB    . LEU G 1 3   ? 16.963  -39.535 63.176  1.00 34.58  ? 4   LEU G CB    1 
ATOM   7604  C CG    . LEU G 1 3   ? 18.150  -40.124 62.407  1.00 32.74  ? 4   LEU G CG    1 
ATOM   7605  C CD1   . LEU G 1 3   ? 18.795  -41.251 63.194  1.00 33.15  ? 4   LEU G CD1   1 
ATOM   7606  C CD2   . LEU G 1 3   ? 17.732  -40.601 61.026  1.00 35.57  ? 4   LEU G CD2   1 
ATOM   7607  N N     . VAL G 1 4   ? 19.614  -38.133 64.714  1.00 31.44  ? 5   VAL G N     1 
ATOM   7608  C CA    . VAL G 1 4   ? 20.778  -37.306 64.450  1.00 31.05  ? 5   VAL G CA    1 
ATOM   7609  C C     . VAL G 1 4   ? 21.913  -38.211 63.982  1.00 30.00  ? 5   VAL G C     1 
ATOM   7610  O O     . VAL G 1 4   ? 22.354  -39.094 64.713  1.00 28.31  ? 5   VAL G O     1 
ATOM   7611  C CB    . VAL G 1 4   ? 21.200  -36.475 65.676  1.00 29.54  ? 5   VAL G CB    1 
ATOM   7612  C CG1   . VAL G 1 4   ? 22.527  -35.762 65.442  1.00 30.61  ? 5   VAL G CG1   1 
ATOM   7613  C CG2   . VAL G 1 4   ? 20.120  -35.482 66.084  1.00 30.02  ? 5   VAL G CG2   1 
ATOM   7614  N N     . CYS G 1 5   ? 22.369  -37.979 62.748  1.00 31.83  ? 6   CYS G N     1 
ATOM   7615  C CA    . CYS G 1 5   ? 23.466  -38.738 62.175  1.00 29.84  ? 6   CYS G CA    1 
ATOM   7616  C C     . CYS G 1 5   ? 24.759  -37.946 62.333  1.00 28.79  ? 6   CYS G C     1 
ATOM   7617  O O     . CYS G 1 5   ? 24.843  -36.796 61.909  1.00 29.47  ? 6   CYS G O     1 
ATOM   7618  C CB    . CYS G 1 5   ? 23.195  -39.062 60.711  1.00 32.08  ? 6   CYS G CB    1 
ATOM   7619  S SG    . CYS G 1 5   ? 21.646  -39.967 60.452  1.00 36.41  ? 6   CYS G SG    1 
ATOM   7620  N N     . VAL G 1 6   ? 25.760  -38.579 62.953  1.00 28.96  ? 7   VAL G N     1 
ATOM   7621  C CA    . VAL G 1 6   ? 27.026  -37.925 63.235  1.00 29.84  ? 7   VAL G CA    1 
ATOM   7622  C C     . VAL G 1 6   ? 28.159  -38.766 62.655  1.00 33.73  ? 7   VAL G C     1 
ATOM   7623  O O     . VAL G 1 6   ? 27.981  -39.949 62.372  1.00 39.34  ? 7   VAL G O     1 
ATOM   7624  C CB    . VAL G 1 6   ? 27.224  -37.705 64.747  1.00 28.92  ? 7   VAL G CB    1 
ATOM   7625  C CG1   . VAL G 1 6   ? 26.055  -36.950 65.367  1.00 25.85  ? 7   VAL G CG1   1 
ATOM   7626  C CG2   . VAL G 1 6   ? 27.463  -39.019 65.483  1.00 27.70  ? 7   VAL G CG2   1 
ATOM   7627  N N     . GLY G 1 7   ? 29.321  -38.129 62.481  1.00 36.60  ? 8   GLY G N     1 
ATOM   7628  C CA    . GLY G 1 7   ? 30.526  -38.811 62.043  1.00 35.59  ? 8   GLY G CA    1 
ATOM   7629  C C     . GLY G 1 7   ? 31.559  -38.856 63.165  1.00 34.76  ? 8   GLY G C     1 
ATOM   7630  O O     . GLY G 1 7   ? 31.681  -37.910 63.939  1.00 32.26  ? 8   GLY G O     1 
ATOM   7631  N N     . THR G 1 8   ? 32.298  -39.966 63.241  1.00 35.35  ? 9   THR G N     1 
ATOM   7632  C CA    . THR G 1 8   ? 33.265  -40.173 64.306  1.00 40.84  ? 9   THR G CA    1 
ATOM   7633  C C     . THR G 1 8   ? 34.675  -39.991 63.751  1.00 32.86  ? 9   THR G C     1 
ATOM   7634  O O     . THR G 1 8   ? 35.657  -40.232 64.451  1.00 31.88  ? 9   THR G O     1 
ATOM   7635  C CB    . THR G 1 8   ? 33.072  -41.564 64.909  1.00 41.84  ? 9   THR G CB    1 
ATOM   7636  O OG1   . THR G 1 8   ? 33.323  -42.479 63.846  1.00 45.42  ? 9   THR G OG1   1 
ATOM   7637  C CG2   . THR G 1 8   ? 31.674  -41.771 65.462  1.00 44.22  ? 9   THR G CG2   1 
ATOM   7638  N N     . GLY G 1 9   ? 34.757  -39.556 62.489  1.00 29.50  ? 10  GLY G N     1 
ATOM   7639  C CA    . GLY G 1 9   ? 36.031  -39.393 61.812  1.00 24.72  ? 10  GLY G CA    1 
ATOM   7640  C C     . GLY G 1 9   ? 36.648  -40.747 61.475  1.00 25.09  ? 10  GLY G C     1 
ATOM   7641  O O     . GLY G 1 9   ? 35.960  -41.765 61.480  1.00 25.77  ? 10  GLY G O     1 
ATOM   7642  N N     . LEU G 1 10  ? 37.952  -40.743 61.181  1.00 26.44  ? 11  LEU G N     1 
ATOM   7643  C CA    . LEU G 1 10  ? 38.672  -41.965 60.861  1.00 24.67  ? 11  LEU G CA    1 
ATOM   7644  C C     . LEU G 1 10  ? 39.487  -42.412 62.072  1.00 25.31  ? 11  LEU G C     1 
ATOM   7645  O O     . LEU G 1 10  ? 39.570  -43.604 62.357  1.00 24.77  ? 11  LEU G O     1 
ATOM   7646  C CB    . LEU G 1 10  ? 39.560  -41.751 59.635  1.00 23.77  ? 11  LEU G CB    1 
ATOM   7647  C CG    . LEU G 1 10  ? 38.856  -41.811 58.275  1.00 23.09  ? 11  LEU G CG    1 
ATOM   7648  C CD1   . LEU G 1 10  ? 38.054  -43.096 58.155  1.00 24.97  ? 11  LEU G CD1   1 
ATOM   7649  C CD2   . LEU G 1 10  ? 37.970  -40.602 58.039  1.00 23.60  ? 11  LEU G CD2   1 
ATOM   7650  N N     . GLN G 1 11  ? 40.082  -41.441 62.776  1.00 25.18  ? 12  GLN G N     1 
ATOM   7651  C CA    . GLN G 1 11  ? 40.946  -41.725 63.912  1.00 27.38  ? 12  GLN G CA    1 
ATOM   7652  C C     . GLN G 1 11  ? 40.105  -42.014 65.154  1.00 25.83  ? 12  GLN G C     1 
ATOM   7653  O O     . GLN G 1 11  ? 39.033  -41.443 65.340  1.00 29.67  ? 12  GLN G O     1 
ATOM   7654  C CB    . GLN G 1 11  ? 41.909  -40.568 64.180  1.00 27.92  ? 12  GLN G CB    1 
ATOM   7655  C CG    . GLN G 1 11  ? 43.198  -40.625 63.366  1.00 31.22  ? 12  GLN G CG    1 
ATOM   7656  C CD    . GLN G 1 11  ? 44.137  -41.724 63.816  1.00 30.55  ? 12  GLN G CD    1 
ATOM   7657  O OE1   . GLN G 1 11  ? 43.786  -42.581 64.634  1.00 29.33  ? 12  GLN G OE1   1 
ATOM   7658  N NE2   . GLN G 1 11  ? 45.348  -41.712 63.279  1.00 33.17  ? 12  GLN G NE2   1 
ATOM   7659  N N     . LEU G 1 12  ? 40.641  -42.886 66.013  1.00 25.81  ? 13  LEU G N     1 
ATOM   7660  C CA    . LEU G 1 12  ? 39.959  -43.343 67.211  1.00 25.54  ? 13  LEU G CA    1 
ATOM   7661  C C     . LEU G 1 12  ? 39.806  -42.199 68.213  1.00 25.55  ? 13  LEU G C     1 
ATOM   7662  O O     . LEU G 1 12  ? 40.795  -41.685 68.732  1.00 25.02  ? 13  LEU G O     1 
ATOM   7663  C CB    . LEU G 1 12  ? 40.773  -44.496 67.796  1.00 26.28  ? 13  LEU G CB    1 
ATOM   7664  C CG    . LEU G 1 12  ? 40.352  -44.996 69.182  1.00 27.82  ? 13  LEU G CG    1 
ATOM   7665  C CD1   . LEU G 1 12  ? 39.010  -45.705 69.137  1.00 27.17  ? 13  LEU G CD1   1 
ATOM   7666  C CD2   . LEU G 1 12  ? 41.421  -45.907 69.764  1.00 27.71  ? 13  LEU G CD2   1 
ATOM   7667  N N     . ALA G 1 13  ? 38.551  -41.791 68.443  1.00 26.41  ? 14  ALA G N     1 
ATOM   7668  C CA    . ALA G 1 13  ? 38.170  -41.048 69.635  1.00 27.85  ? 14  ALA G CA    1 
ATOM   7669  C C     . ALA G 1 13  ? 38.354  -39.542 69.450  1.00 28.15  ? 14  ALA G C     1 
ATOM   7670  O O     . ALA G 1 13  ? 37.470  -38.764 69.802  1.00 32.38  ? 14  ALA G O     1 
ATOM   7671  C CB    . ALA G 1 13  ? 38.961  -41.557 70.824  1.00 30.68  ? 14  ALA G CB    1 
ATOM   7672  N N     . GLY G 1 14  ? 39.508  -39.136 68.913  1.00 25.56  ? 15  GLY G N     1 
ATOM   7673  C CA    . GLY G 1 14  ? 39.916  -37.741 68.957  1.00 25.33  ? 15  GLY G CA    1 
ATOM   7674  C C     . GLY G 1 14  ? 39.511  -36.966 67.705  1.00 29.30  ? 15  GLY G C     1 
ATOM   7675  O O     . GLY G 1 14  ? 39.755  -35.765 67.621  1.00 27.54  ? 15  GLY G O     1 
ATOM   7676  N N     . GLN G 1 15  ? 38.884  -37.651 66.741  1.00 29.39  ? 16  GLN G N     1 
ATOM   7677  C CA    . GLN G 1 15  ? 38.611  -37.041 65.448  1.00 31.98  ? 16  GLN G CA    1 
ATOM   7678  C C     . GLN G 1 15  ? 37.112  -36.786 65.290  1.00 32.50  ? 16  GLN G C     1 
ATOM   7679  O O     . GLN G 1 15  ? 36.667  -36.342 64.234  1.00 31.21  ? 16  GLN G O     1 
ATOM   7680  C CB    . GLN G 1 15  ? 39.158  -37.913 64.318  1.00 34.20  ? 16  GLN G CB    1 
ATOM   7681  C CG    . GLN G 1 15  ? 39.545  -37.129 63.069  1.00 38.09  ? 16  GLN G CG    1 
ATOM   7682  C CD    . GLN G 1 15  ? 40.414  -37.922 62.117  1.00 39.52  ? 16  GLN G CD    1 
ATOM   7683  O OE1   . GLN G 1 15  ? 39.979  -38.913 61.521  1.00 39.09  ? 16  GLN G OE1   1 
ATOM   7684  N NE2   . GLN G 1 15  ? 41.656  -37.487 61.964  1.00 41.97  ? 16  GLN G NE2   1 
ATOM   7685  N N     . ILE G 1 16  ? 36.340  -37.064 66.346  1.00 27.75  ? 17  ILE G N     1 
ATOM   7686  C CA    . ILE G 1 16  ? 34.931  -36.705 66.361  1.00 25.99  ? 17  ILE G CA    1 
ATOM   7687  C C     . ILE G 1 16  ? 34.812  -35.249 66.803  1.00 23.48  ? 17  ILE G C     1 
ATOM   7688  O O     . ILE G 1 16  ? 35.679  -34.740 67.509  1.00 23.60  ? 17  ILE G O     1 
ATOM   7689  C CB    . ILE G 1 16  ? 34.118  -37.649 67.266  1.00 27.24  ? 17  ILE G CB    1 
ATOM   7690  C CG1   . ILE G 1 16  ? 32.617  -37.359 67.170  1.00 26.14  ? 17  ILE G CG1   1 
ATOM   7691  C CG2   . ILE G 1 16  ? 34.616  -37.586 68.711  1.00 27.64  ? 17  ILE G CG2   1 
ATOM   7692  C CD1   . ILE G 1 16  ? 31.730  -38.500 67.635  1.00 24.50  ? 17  ILE G CD1   1 
ATOM   7693  N N     . SER G 1 17  ? 33.743  -34.582 66.360  1.00 24.91  ? 18  SER G N     1 
ATOM   7694  C CA    . SER G 1 17  ? 33.476  -33.215 66.774  1.00 27.90  ? 18  SER G CA    1 
ATOM   7695  C C     . SER G 1 17  ? 33.060  -33.214 68.243  1.00 27.89  ? 18  SER G C     1 
ATOM   7696  O O     . SER G 1 17  ? 32.596  -34.229 68.758  1.00 23.98  ? 18  SER G O     1 
ATOM   7697  C CB    . SER G 1 17  ? 32.428  -32.564 65.899  1.00 27.39  ? 18  SER G CB    1 
ATOM   7698  O OG    . SER G 1 17  ? 31.119  -32.993 66.246  1.00 29.60  ? 18  SER G OG    1 
ATOM   7699  N N     . VAL G 1 18  ? 33.254  -32.073 68.914  1.00 28.73  ? 19  VAL G N     1 
ATOM   7700  C CA    . VAL G 1 18  ? 32.918  -31.948 70.323  1.00 30.66  ? 19  VAL G CA    1 
ATOM   7701  C C     . VAL G 1 18  ? 31.410  -32.123 70.479  1.00 31.68  ? 19  VAL G C     1 
ATOM   7702  O O     . VAL G 1 18  ? 30.948  -32.789 71.403  1.00 33.56  ? 19  VAL G O     1 
ATOM   7703  C CB    . VAL G 1 18  ? 33.381  -30.603 70.917  1.00 35.51  ? 19  VAL G CB    1 
ATOM   7704  C CG1   . VAL G 1 18  ? 32.827  -30.383 72.320  1.00 37.56  ? 19  VAL G CG1   1 
ATOM   7705  C CG2   . VAL G 1 18  ? 34.899  -30.471 70.912  1.00 33.19  ? 19  VAL G CG2   1 
ATOM   7706  N N     . LEU G 1 19  ? 30.656  -31.516 69.559  1.00 28.41  ? 20  LEU G N     1 
ATOM   7707  C CA    . LEU G 1 19  ? 29.205  -31.551 69.610  1.00 31.60  ? 20  LEU G CA    1 
ATOM   7708  C C     . LEU G 1 19  ? 28.720  -32.971 69.329  1.00 30.01  ? 20  LEU G C     1 
ATOM   7709  O O     . LEU G 1 19  ? 27.899  -33.507 70.069  1.00 30.52  ? 20  LEU G O     1 
ATOM   7710  C CB    . LEU G 1 19  ? 28.629  -30.552 68.609  1.00 32.26  ? 20  LEU G CB    1 
ATOM   7711  C CG    . LEU G 1 19  ? 27.102  -30.432 68.587  1.00 32.88  ? 20  LEU G CG    1 
ATOM   7712  C CD1   . LEU G 1 19  ? 26.579  -29.931 69.923  1.00 36.23  ? 20  LEU G CD1   1 
ATOM   7713  C CD2   . LEU G 1 19  ? 26.643  -29.529 67.455  1.00 35.38  ? 20  LEU G CD2   1 
ATOM   7714  N N     . SER G 1 20  ? 29.245  -33.573 68.256  1.00 28.47  ? 21  SER G N     1 
ATOM   7715  C CA    . SER G 1 20  ? 28.816  -34.896 67.832  1.00 29.76  ? 21  SER G CA    1 
ATOM   7716  C C     . SER G 1 20  ? 29.009  -35.901 68.965  1.00 26.87  ? 21  SER G C     1 
ATOM   7717  O O     . SER G 1 20  ? 28.146  -36.741 69.206  1.00 27.26  ? 21  SER G O     1 
ATOM   7718  C CB    . SER G 1 20  ? 29.537  -35.329 66.584  1.00 27.83  ? 21  SER G CB    1 
ATOM   7719  O OG    . SER G 1 20  ? 29.171  -34.514 65.480  1.00 31.16  ? 21  SER G OG    1 
ATOM   7720  N N     . ARG G 1 21  ? 30.151  -35.805 69.653  1.00 24.43  ? 22  ARG G N     1 
ATOM   7721  C CA    . ARG G 1 21  ? 30.439  -36.669 70.786  1.00 26.10  ? 22  ARG G CA    1 
ATOM   7722  C C     . ARG G 1 21  ? 29.334  -36.503 71.826  1.00 27.47  ? 22  ARG G C     1 
ATOM   7723  O O     . ARG G 1 21  ? 28.826  -37.485 72.365  1.00 27.09  ? 22  ARG G O     1 
ATOM   7724  C CB    . ARG G 1 21  ? 31.814  -36.337 71.378  1.00 28.80  ? 22  ARG G CB    1 
ATOM   7725  C CG    . ARG G 1 21  ? 32.259  -37.260 72.504  1.00 31.14  ? 22  ARG G CG    1 
ATOM   7726  C CD    . ARG G 1 21  ? 33.633  -36.884 73.042  1.00 34.76  ? 22  ARG G CD    1 
ATOM   7727  N NE    . ARG G 1 21  ? 34.168  -37.883 73.974  1.00 36.10  ? 22  ARG G NE    1 
ATOM   7728  C CZ    . ARG G 1 21  ? 33.663  -38.159 75.171  1.00 40.91  ? 22  ARG G CZ    1 
ATOM   7729  N NH1   . ARG G 1 21  ? 32.628  -37.477 75.627  1.00 46.94  ? 22  ARG G NH1   1 
ATOM   7730  N NH2   . ARG G 1 21  ? 34.207  -39.107 75.914  1.00 40.87  ? 22  ARG G NH2   1 
ATOM   7731  N N     . SER G 1 22  ? 28.959  -35.245 72.077  1.00 29.91  ? 23  SER G N     1 
ATOM   7732  C CA    . SER G 1 22  ? 27.932  -34.917 73.052  1.00 28.59  ? 23  SER G CA    1 
ATOM   7733  C C     . SER G 1 22  ? 26.620  -35.611 72.693  1.00 29.93  ? 23  SER G C     1 
ATOM   7734  O O     . SER G 1 22  ? 25.932  -36.132 73.568  1.00 34.09  ? 23  SER G O     1 
ATOM   7735  C CB    . SER G 1 22  ? 27.751  -33.422 73.161  1.00 27.31  ? 23  SER G CB    1 
ATOM   7736  O OG    . SER G 1 22  ? 26.758  -33.093 74.123  1.00 27.17  ? 23  SER G OG    1 
ATOM   7737  N N     . TYR G 1 23  ? 26.281  -35.611 71.397  1.00 27.67  ? 24  TYR G N     1 
ATOM   7738  C CA    . TYR G 1 23  ? 25.047  -36.223 70.925  1.00 27.19  ? 24  TYR G CA    1 
ATOM   7739  C C     . TYR G 1 23  ? 25.041  -37.708 71.280  1.00 25.81  ? 24  TYR G C     1 
ATOM   7740  O O     . TYR G 1 23  ? 24.044  -38.226 71.777  1.00 27.66  ? 24  TYR G O     1 
ATOM   7741  C CB    . TYR G 1 23  ? 24.857  -36.044 69.415  1.00 26.76  ? 24  TYR G CB    1 
ATOM   7742  C CG    . TYR G 1 23  ? 24.167  -34.751 69.000  1.00 29.56  ? 24  TYR G CG    1 
ATOM   7743  C CD1   . TYR G 1 23  ? 22.804  -34.572 69.206  1.00 33.19  ? 24  TYR G CD1   1 
ATOM   7744  C CD2   . TYR G 1 23  ? 24.864  -33.734 68.362  1.00 34.48  ? 24  TYR G CD2   1 
ATOM   7745  C CE1   . TYR G 1 23  ? 22.163  -33.407 68.821  1.00 33.67  ? 24  TYR G CE1   1 
ATOM   7746  C CE2   . TYR G 1 23  ? 24.233  -32.565 67.967  1.00 33.58  ? 24  TYR G CE2   1 
ATOM   7747  C CZ    . TYR G 1 23  ? 22.880  -32.401 68.197  1.00 35.12  ? 24  TYR G CZ    1 
ATOM   7748  O OH    . TYR G 1 23  ? 22.255  -31.252 67.810  1.00 35.87  ? 24  TYR G OH    1 
ATOM   7749  N N     . ILE G 1 24  ? 26.158  -38.386 70.999  1.00 25.62  ? 25  ILE G N     1 
ATOM   7750  C CA    . ILE G 1 24  ? 26.280  -39.811 71.255  1.00 27.05  ? 25  ILE G CA    1 
ATOM   7751  C C     . ILE G 1 24  ? 26.092  -40.071 72.747  1.00 29.57  ? 25  ILE G C     1 
ATOM   7752  O O     . ILE G 1 24  ? 25.542  -41.097 73.138  1.00 29.41  ? 25  ILE G O     1 
ATOM   7753  C CB    . ILE G 1 24  ? 27.637  -40.344 70.757  1.00 26.73  ? 25  ILE G CB    1 
ATOM   7754  C CG1   . ILE G 1 24  ? 27.754  -40.255 69.234  1.00 24.07  ? 25  ILE G CG1   1 
ATOM   7755  C CG2   . ILE G 1 24  ? 27.882  -41.767 71.259  1.00 28.10  ? 25  ILE G CG2   1 
ATOM   7756  C CD1   . ILE G 1 24  ? 29.067  -40.781 68.683  1.00 22.28  ? 25  ILE G CD1   1 
ATOM   7757  N N     . GLU G 1 25  ? 26.555  -39.126 73.570  1.00 31.13  ? 26  GLU G N     1 
ATOM   7758  C CA    . GLU G 1 25  ? 26.585  -39.304 75.012  1.00 35.74  ? 26  GLU G CA    1 
ATOM   7759  C C     . GLU G 1 25  ? 25.164  -39.265 75.571  1.00 34.66  ? 26  GLU G C     1 
ATOM   7760  O O     . GLU G 1 25  ? 24.833  -40.028 76.475  1.00 36.30  ? 26  GLU G O     1 
ATOM   7761  C CB    . GLU G 1 25  ? 27.461  -38.226 75.652  1.00 36.57  ? 26  GLU G CB    1 
ATOM   7762  C CG    . GLU G 1 25  ? 27.609  -38.380 77.163  1.00 39.17  ? 26  GLU G CG    1 
ATOM   7763  C CD    . GLU G 1 25  ? 28.473  -37.314 77.813  1.00 43.92  ? 26  GLU G CD    1 
ATOM   7764  O OE1   . GLU G 1 25  ? 29.016  -36.461 77.079  1.00 39.07  ? 26  GLU G OE1   1 
ATOM   7765  O OE2   . GLU G 1 25  ? 28.598  -37.334 79.056  1.00 48.53  ? 26  GLU G OE2   1 
ATOM   7766  N N     . HIS G 1 26  ? 24.330  -38.376 75.021  1.00 33.16  ? 27  HIS G N     1 
ATOM   7767  C CA    . HIS G 1 26  ? 23.002  -38.137 75.563  1.00 35.17  ? 27  HIS G CA    1 
ATOM   7768  C C     . HIS G 1 26  ? 21.944  -38.865 74.738  1.00 33.63  ? 27  HIS G C     1 
ATOM   7769  O O     . HIS G 1 26  ? 20.751  -38.632 74.920  1.00 35.51  ? 27  HIS G O     1 
ATOM   7770  C CB    . HIS G 1 26  ? 22.704  -36.634 75.631  1.00 37.07  ? 27  HIS G CB    1 
ATOM   7771  C CG    . HIS G 1 26  ? 23.546  -35.894 76.615  1.00 39.25  ? 27  HIS G CG    1 
ATOM   7772  N ND1   . HIS G 1 26  ? 24.615  -35.105 76.250  1.00 40.60  ? 27  HIS G ND1   1 
ATOM   7773  C CD2   . HIS G 1 26  ? 23.456  -35.802 77.948  1.00 41.34  ? 27  HIS G CD2   1 
ATOM   7774  C CE1   . HIS G 1 26  ? 25.155  -34.572 77.337  1.00 44.49  ? 27  HIS G CE1   1 
ATOM   7775  N NE2   . HIS G 1 26  ? 24.467  -34.984 78.380  1.00 44.20  ? 27  HIS G NE2   1 
ATOM   7776  N N     . ALA G 1 27  ? 22.386  -39.750 73.841  1.00 36.68  ? 28  ALA G N     1 
ATOM   7777  C CA    . ALA G 1 27  ? 21.472  -40.491 72.987  1.00 33.37  ? 28  ALA G CA    1 
ATOM   7778  C C     . ALA G 1 27  ? 20.832  -41.631 73.777  1.00 32.38  ? 28  ALA G C     1 
ATOM   7779  O O     . ALA G 1 27  ? 21.483  -42.263 74.606  1.00 28.79  ? 28  ALA G O     1 
ATOM   7780  C CB    . ALA G 1 27  ? 22.204  -41.008 71.768  1.00 34.70  ? 28  ALA G CB    1 
ATOM   7781  N N     . ASP G 1 28  ? 19.544  -41.876 73.510  1.00 31.80  ? 29  ASP G N     1 
ATOM   7782  C CA    . ASP G 1 28  ? 18.836  -43.002 74.094  1.00 33.63  ? 29  ASP G CA    1 
ATOM   7783  C C     . ASP G 1 28  ? 19.418  -44.296 73.535  1.00 34.30  ? 29  ASP G C     1 
ATOM   7784  O O     . ASP G 1 28  ? 19.596  -45.271 74.262  1.00 32.02  ? 29  ASP G O     1 
ATOM   7785  C CB    . ASP G 1 28  ? 17.342  -42.933 73.816  1.00 36.42  ? 29  ASP G CB    1 
ATOM   7786  C CG    . ASP G 1 28  ? 16.600  -41.776 74.469  1.00 37.49  ? 29  ASP G CG    1 
ATOM   7787  O OD1   . ASP G 1 28  ? 17.221  -41.065 75.288  1.00 43.67  ? 29  ASP G OD1   1 
ATOM   7788  O OD2   . ASP G 1 28  ? 15.409  -41.588 74.143  1.00 39.78  ? 29  ASP G OD2   1 
ATOM   7789  N N     . ILE G 1 29  ? 19.711  -44.282 72.230  1.00 31.36  ? 30  ILE G N     1 
ATOM   7790  C CA    . ILE G 1 29  ? 20.188  -45.460 71.527  1.00 33.42  ? 30  ILE G CA    1 
ATOM   7791  C C     . ILE G 1 29  ? 21.089  -45.010 70.380  1.00 32.66  ? 30  ILE G C     1 
ATOM   7792  O O     . ILE G 1 29  ? 20.826  -43.992 69.743  1.00 32.24  ? 30  ILE G O     1 
ATOM   7793  C CB    . ILE G 1 29  ? 19.000  -46.303 71.028  1.00 32.05  ? 30  ILE G CB    1 
ATOM   7794  C CG1   . ILE G 1 29  ? 19.441  -47.689 70.562  1.00 34.93  ? 30  ILE G CG1   1 
ATOM   7795  C CG2   . ILE G 1 29  ? 18.225  -45.560 69.939  1.00 30.96  ? 30  ILE G CG2   1 
ATOM   7796  C CD1   . ILE G 1 29  ? 18.294  -48.595 70.151  1.00 35.27  ? 30  ILE G CD1   1 
ATOM   7797  N N     . VAL G 1 30  ? 22.150  -45.783 70.127  1.00 32.90  ? 31  VAL G N     1 
ATOM   7798  C CA    . VAL G 1 30  ? 23.111  -45.450 69.089  1.00 31.59  ? 31  VAL G CA    1 
ATOM   7799  C C     . VAL G 1 30  ? 23.219  -46.620 68.114  1.00 32.02  ? 31  VAL G C     1 
ATOM   7800  O O     . VAL G 1 30  ? 23.382  -47.766 68.528  1.00 30.96  ? 31  VAL G O     1 
ATOM   7801  C CB    . VAL G 1 30  ? 24.486  -45.101 69.690  1.00 32.72  ? 31  VAL G CB    1 
ATOM   7802  C CG1   . VAL G 1 30  ? 25.505  -44.753 68.611  1.00 32.07  ? 31  VAL G CG1   1 
ATOM   7803  C CG2   . VAL G 1 30  ? 24.387  -43.978 70.716  1.00 33.26  ? 31  VAL G CG2   1 
ATOM   7804  N N     . PHE G 1 31  ? 23.111  -46.308 66.817  1.00 31.55  ? 32  PHE G N     1 
ATOM   7805  C CA    . PHE G 1 31  ? 23.363  -47.275 65.760  1.00 29.71  ? 32  PHE G CA    1 
ATOM   7806  C C     . PHE G 1 31  ? 24.732  -46.974 65.158  1.00 31.46  ? 32  PHE G C     1 
ATOM   7807  O O     . PHE G 1 31  ? 24.957  -45.887 64.632  1.00 37.81  ? 32  PHE G O     1 
ATOM   7808  C CB    . PHE G 1 31  ? 22.247  -47.228 64.712  1.00 29.20  ? 32  PHE G CB    1 
ATOM   7809  C CG    . PHE G 1 31  ? 20.902  -47.749 65.200  1.00 29.07  ? 32  PHE G CG    1 
ATOM   7810  C CD1   . PHE G 1 31  ? 20.025  -46.922 65.892  1.00 29.74  ? 32  PHE G CD1   1 
ATOM   7811  C CD2   . PHE G 1 31  ? 20.515  -49.062 64.958  1.00 27.42  ? 32  PHE G CD2   1 
ATOM   7812  C CE1   . PHE G 1 31  ? 18.801  -47.400 66.335  1.00 29.54  ? 32  PHE G CE1   1 
ATOM   7813  C CE2   . PHE G 1 31  ? 19.289  -49.533 65.402  1.00 27.41  ? 32  PHE G CE2   1 
ATOM   7814  C CZ    . PHE G 1 31  ? 18.437  -48.702 66.089  1.00 28.50  ? 32  PHE G CZ    1 
ATOM   7815  N N     . SER G 1 32  ? 25.637  -47.954 65.239  1.00 31.05  ? 33  SER G N     1 
ATOM   7816  C CA    . SER G 1 32  ? 27.040  -47.723 64.944  1.00 31.76  ? 33  SER G CA    1 
ATOM   7817  C C     . SER G 1 32  ? 27.450  -48.430 63.656  1.00 31.43  ? 33  SER G C     1 
ATOM   7818  O O     . SER G 1 32  ? 26.865  -49.440 63.272  1.00 30.98  ? 33  SER G O     1 
ATOM   7819  C CB    . SER G 1 32  ? 27.905  -48.165 66.094  1.00 28.78  ? 33  SER G CB    1 
ATOM   7820  O OG    . SER G 1 32  ? 27.850  -49.576 66.253  1.00 29.27  ? 33  SER G OG    1 
ATOM   7821  N N     . LEU G 1 33  ? 28.468  -47.868 62.998  1.00 34.16  ? 34  LEU G N     1 
ATOM   7822  C CA    . LEU G 1 33  ? 29.150  -48.525 61.897  1.00 36.41  ? 34  LEU G CA    1 
ATOM   7823  C C     . LEU G 1 33  ? 30.602  -48.056 61.901  1.00 36.28  ? 34  LEU G C     1 
ATOM   7824  O O     . LEU G 1 33  ? 30.970  -47.151 61.155  1.00 41.19  ? 34  LEU G O     1 
ATOM   7825  C CB    . LEU G 1 33  ? 28.459  -48.217 60.570  1.00 38.91  ? 34  LEU G CB    1 
ATOM   7826  C CG    . LEU G 1 33  ? 28.771  -49.177 59.417  1.00 43.84  ? 34  LEU G CG    1 
ATOM   7827  C CD1   . LEU G 1 33  ? 28.198  -48.662 58.108  1.00 46.81  ? 34  LEU G CD1   1 
ATOM   7828  C CD2   . LEU G 1 33  ? 30.265  -49.423 59.288  1.00 43.92  ? 34  LEU G CD2   1 
ATOM   7829  N N     . LEU G 1 34  ? 31.413  -48.675 62.766  1.00 36.59  ? 35  LEU G N     1 
ATOM   7830  C CA    . LEU G 1 34  ? 32.757  -48.196 63.042  1.00 38.87  ? 35  LEU G CA    1 
ATOM   7831  C C     . LEU G 1 34  ? 33.785  -49.105 62.373  1.00 39.97  ? 35  LEU G C     1 
ATOM   7832  O O     . LEU G 1 34  ? 33.487  -50.246 62.030  1.00 42.56  ? 35  LEU G O     1 
ATOM   7833  C CB    . LEU G 1 34  ? 32.959  -48.124 64.555  1.00 41.87  ? 35  LEU G CB    1 
ATOM   7834  C CG    . LEU G 1 34  ? 31.940  -47.274 65.321  1.00 43.61  ? 35  LEU G CG    1 
ATOM   7835  C CD1   . LEU G 1 34  ? 32.302  -47.184 66.793  1.00 44.01  ? 35  LEU G CD1   1 
ATOM   7836  C CD2   . LEU G 1 34  ? 31.817  -45.886 64.712  1.00 43.64  ? 35  LEU G CD2   1 
ATOM   7837  N N     . PRO G 1 35  ? 35.030  -48.615 62.173  1.00 43.47  ? 36  PRO G N     1 
ATOM   7838  C CA    . PRO G 1 35  ? 36.042  -49.345 61.406  1.00 43.81  ? 36  PRO G CA    1 
ATOM   7839  C C     . PRO G 1 35  ? 36.601  -50.588 62.096  1.00 42.35  ? 36  PRO G C     1 
ATOM   7840  O O     . PRO G 1 35  ? 37.017  -51.531 61.427  1.00 43.32  ? 36  PRO G O     1 
ATOM   7841  C CB    . PRO G 1 35  ? 37.148  -48.284 61.172  1.00 44.64  ? 36  PRO G CB    1 
ATOM   7842  C CG    . PRO G 1 35  ? 36.504  -46.958 61.543  1.00 45.05  ? 36  PRO G CG    1 
ATOM   7843  C CD    . PRO G 1 35  ? 35.504  -47.302 62.625  1.00 43.57  ? 36  PRO G CD    1 
ATOM   7844  N N     . ASP G 1 36  ? 36.628  -50.574 63.433  1.00 38.91  ? 37  ASP G N     1 
ATOM   7845  C CA    . ASP G 1 36  ? 37.288  -51.629 64.185  1.00 40.43  ? 37  ASP G CA    1 
ATOM   7846  C C     . ASP G 1 36  ? 36.659  -51.763 65.569  1.00 36.23  ? 37  ASP G C     1 
ATOM   7847  O O     . ASP G 1 36  ? 35.697  -51.071 65.893  1.00 36.97  ? 37  ASP G O     1 
ATOM   7848  C CB    . ASP G 1 36  ? 38.785  -51.375 64.274  1.00 45.11  ? 37  ASP G CB    1 
ATOM   7849  C CG    . ASP G 1 36  ? 39.180  -50.019 64.840  1.00 49.77  ? 37  ASP G CG    1 
ATOM   7850  O OD1   . ASP G 1 36  ? 38.794  -49.731 65.992  1.00 52.26  ? 37  ASP G OD1   1 
ATOM   7851  O OD2   . ASP G 1 36  ? 39.865  -49.261 64.123  1.00 61.29  ? 37  ASP G OD2   1 
ATOM   7852  N N     . GLY G 1 37  ? 37.235  -52.660 66.378  1.00 35.80  ? 38  GLY G N     1 
ATOM   7853  C CA    . GLY G 1 37  ? 36.712  -52.976 67.696  1.00 36.47  ? 38  GLY G CA    1 
ATOM   7854  C C     . GLY G 1 37  ? 37.211  -51.996 68.755  1.00 36.88  ? 38  GLY G C     1 
ATOM   7855  O O     . GLY G 1 37  ? 36.606  -51.867 69.816  1.00 33.20  ? 38  GLY G O     1 
ATOM   7856  N N     . PHE G 1 38  ? 38.331  -51.325 68.465  1.00 38.00  ? 39  PHE G N     1 
ATOM   7857  C CA    . PHE G 1 38  ? 38.853  -50.300 69.354  1.00 36.96  ? 39  PHE G CA    1 
ATOM   7858  C C     . PHE G 1 38  ? 37.879  -49.127 69.363  1.00 33.99  ? 39  PHE G C     1 
ATOM   7859  O O     . PHE G 1 38  ? 37.570  -48.576 70.417  1.00 32.56  ? 39  PHE G O     1 
ATOM   7860  C CB    . PHE G 1 38  ? 40.257  -49.850 68.939  1.00 37.34  ? 39  PHE G CB    1 
ATOM   7861  C CG    . PHE G 1 38  ? 41.347  -50.891 69.147  1.00 36.60  ? 39  PHE G CG    1 
ATOM   7862  C CD1   . PHE G 1 38  ? 41.834  -51.168 70.420  1.00 38.75  ? 39  PHE G CD1   1 
ATOM   7863  C CD2   . PHE G 1 38  ? 41.909  -51.564 68.067  1.00 35.84  ? 39  PHE G CD2   1 
ATOM   7864  C CE1   . PHE G 1 38  ? 42.833  -52.109 70.607  1.00 39.64  ? 39  PHE G CE1   1 
ATOM   7865  C CE2   . PHE G 1 38  ? 42.909  -52.503 68.262  1.00 38.23  ? 39  PHE G CE2   1 
ATOM   7866  C CZ    . PHE G 1 38  ? 43.369  -52.772 69.529  1.00 40.22  ? 39  PHE G CZ    1 
ATOM   7867  N N     . SER G 1 39  ? 37.403  -48.761 68.169  1.00 33.50  ? 40  SER G N     1 
ATOM   7868  C CA    . SER G 1 39  ? 36.427  -47.696 68.018  1.00 32.68  ? 40  SER G CA    1 
ATOM   7869  C C     . SER G 1 39  ? 35.091  -48.136 68.610  1.00 31.02  ? 40  SER G C     1 
ATOM   7870  O O     . SER G 1 39  ? 34.309  -47.309 69.075  1.00 27.96  ? 40  SER G O     1 
ATOM   7871  C CB    . SER G 1 39  ? 36.279  -47.303 66.569  1.00 31.54  ? 40  SER G CB    1 
ATOM   7872  O OG    . SER G 1 39  ? 35.255  -46.332 66.405  1.00 35.98  ? 40  SER G OG    1 
ATOM   7873  N N     . GLN G 1 40  ? 34.851  -49.452 68.593  1.00 32.20  ? 41  GLN G N     1 
ATOM   7874  C CA    . GLN G 1 40  ? 33.594  -50.013 69.059  1.00 33.59  ? 41  GLN G CA    1 
ATOM   7875  C C     . GLN G 1 40  ? 33.540  -49.936 70.583  1.00 34.19  ? 41  GLN G C     1 
ATOM   7876  O O     . GLN G 1 40  ? 32.514  -49.571 71.152  1.00 36.26  ? 41  GLN G O     1 
ATOM   7877  C CB    . GLN G 1 40  ? 33.437  -51.455 68.576  1.00 36.01  ? 41  GLN G CB    1 
ATOM   7878  C CG    . GLN G 1 40  ? 32.000  -51.964 68.619  1.00 34.55  ? 41  GLN G CG    1 
ATOM   7879  C CD    . GLN G 1 40  ? 31.068  -51.163 67.736  1.00 34.26  ? 41  GLN G CD    1 
ATOM   7880  O OE1   . GLN G 1 40  ? 31.297  -51.008 66.531  1.00 35.51  ? 41  GLN G OE1   1 
ATOM   7881  N NE2   . GLN G 1 40  ? 30.011  -50.631 68.333  1.00 34.28  ? 41  GLN G NE2   1 
ATOM   7882  N N     A ARG G 1 41  ? 34.655  -50.293 71.230  0.50 34.72  ? 42  ARG G N     1 
ATOM   7883  N N     B ARG G 1 41  ? 34.657  -50.282 71.232  0.50 34.44  ? 42  ARG G N     1 
ATOM   7884  C CA    A ARG G 1 41  ? 34.759  -50.226 72.678  0.50 38.85  ? 42  ARG G CA    1 
ATOM   7885  C CA    B ARG G 1 41  ? 34.748  -50.227 72.682  0.50 38.32  ? 42  ARG G CA    1 
ATOM   7886  C C     A ARG G 1 41  ? 34.600  -48.777 73.128  0.50 35.45  ? 42  ARG G C     1 
ATOM   7887  C C     B ARG G 1 41  ? 34.614  -48.778 73.143  0.50 35.17  ? 42  ARG G C     1 
ATOM   7888  O O     A ARG G 1 41  ? 33.827  -48.486 74.037  0.50 33.19  ? 42  ARG G O     1 
ATOM   7889  O O     B ARG G 1 41  ? 33.869  -48.487 74.076  0.50 33.01  ? 42  ARG G O     1 
ATOM   7890  C CB    A ARG G 1 41  ? 36.093  -50.796 73.174  0.50 42.10  ? 42  ARG G CB    1 
ATOM   7891  C CB    B ARG G 1 41  ? 36.055  -50.854 73.182  0.50 41.03  ? 42  ARG G CB    1 
ATOM   7892  C CG    A ARG G 1 41  ? 36.176  -52.315 73.164  0.50 47.12  ? 42  ARG G CG    1 
ATOM   7893  C CG    B ARG G 1 41  ? 36.025  -52.374 73.248  0.50 45.50  ? 42  ARG G CG    1 
ATOM   7894  C CD    A ARG G 1 41  ? 37.404  -52.819 73.910  0.50 50.65  ? 42  ARG G CD    1 
ATOM   7895  C CD    B ARG G 1 41  ? 37.262  -52.953 73.919  0.50 48.22  ? 42  ARG G CD    1 
ATOM   7896  N NE    A ARG G 1 41  ? 37.396  -54.277 74.073  0.50 51.41  ? 42  ARG G NE    1 
ATOM   7897  N NE    B ARG G 1 41  ? 38.460  -52.846 73.080  0.50 47.63  ? 42  ARG G NE    1 
ATOM   7898  C CZ    A ARG G 1 41  ? 38.375  -55.088 73.693  0.50 53.55  ? 42  ARG G CZ    1 
ATOM   7899  C CZ    B ARG G 1 41  ? 38.600  -53.429 71.896  0.50 47.62  ? 42  ARG G CZ    1 
ATOM   7900  N NH1   A ARG G 1 41  ? 39.465  -54.592 73.134  0.50 54.71  ? 42  ARG G NH1   1 
ATOM   7901  N NH1   B ARG G 1 41  ? 39.725  -53.292 71.219  0.50 46.21  ? 42  ARG G NH1   1 
ATOM   7902  N NH2   A ARG G 1 41  ? 38.264  -56.391 73.879  0.50 53.53  ? 42  ARG G NH2   1 
ATOM   7903  N NH2   B ARG G 1 41  ? 37.615  -54.156 71.398  0.50 48.49  ? 42  ARG G NH2   1 
ATOM   7904  N N     . TRP G 1 42  ? 35.344  -47.877 72.477  1.00 34.47  ? 43  TRP G N     1 
ATOM   7905  C CA    . TRP G 1 42  ? 35.298  -46.461 72.799  1.00 32.37  ? 43  TRP G CA    1 
ATOM   7906  C C     . TRP G 1 42  ? 33.849  -45.981 72.843  1.00 32.84  ? 43  TRP G C     1 
ATOM   7907  O O     . TRP G 1 42  ? 33.443  -45.307 73.787  1.00 35.22  ? 43  TRP G O     1 
ATOM   7908  C CB    . TRP G 1 42  ? 36.115  -45.654 71.782  1.00 31.22  ? 43  TRP G CB    1 
ATOM   7909  C CG    . TRP G 1 42  ? 35.800  -44.182 71.783  1.00 28.62  ? 43  TRP G CG    1 
ATOM   7910  C CD1   . TRP G 1 42  ? 36.256  -43.244 72.661  1.00 27.88  ? 43  TRP G CD1   1 
ATOM   7911  C CD2   . TRP G 1 42  ? 34.963  -43.476 70.840  1.00 28.22  ? 43  TRP G CD2   1 
ATOM   7912  N NE1   . TRP G 1 42  ? 35.755  -42.009 72.342  1.00 27.98  ? 43  TRP G NE1   1 
ATOM   7913  C CE2   . TRP G 1 42  ? 34.963  -42.119 71.229  1.00 27.67  ? 43  TRP G CE2   1 
ATOM   7914  C CE3   . TRP G 1 42  ? 34.218  -43.855 69.718  1.00 26.57  ? 43  TRP G CE3   1 
ATOM   7915  C CZ2   . TRP G 1 42  ? 34.248  -41.147 70.533  1.00 27.83  ? 43  TRP G CZ2   1 
ATOM   7916  C CZ3   . TRP G 1 42  ? 33.512  -42.892 69.032  1.00 28.94  ? 43  TRP G CZ3   1 
ATOM   7917  C CH2   . TRP G 1 42  ? 33.530  -41.557 69.434  1.00 28.41  ? 43  TRP G CH2   1 
ATOM   7918  N N     . LEU G 1 43  ? 33.081  -46.341 71.810  1.00 30.94  ? 44  LEU G N     1 
ATOM   7919  C CA    . LEU G 1 43  ? 31.700  -45.906 71.685  1.00 31.42  ? 44  LEU G CA    1 
ATOM   7920  C C     . LEU G 1 43  ? 30.870  -46.481 72.829  1.00 30.46  ? 44  LEU G C     1 
ATOM   7921  O O     . LEU G 1 43  ? 30.048  -45.782 73.415  1.00 25.72  ? 44  LEU G O     1 
ATOM   7922  C CB    . LEU G 1 43  ? 31.143  -46.337 70.329  1.00 31.80  ? 44  LEU G CB    1 
ATOM   7923  C CG    . LEU G 1 43  ? 29.666  -46.014 70.083  1.00 33.26  ? 44  LEU G CG    1 
ATOM   7924  C CD1   . LEU G 1 43  ? 29.445  -44.512 70.004  1.00 35.39  ? 44  LEU G CD1   1 
ATOM   7925  C CD2   . LEU G 1 43  ? 29.159  -46.700 68.827  1.00 34.45  ? 44  LEU G CD2   1 
ATOM   7926  N N     . THR G 1 44  ? 31.093  -47.765 73.128  1.00 33.13  ? 45  THR G N     1 
ATOM   7927  C CA    . THR G 1 44  ? 30.301  -48.481 74.117  1.00 38.17  ? 45  THR G CA    1 
ATOM   7928  C C     . THR G 1 44  ? 30.464  -47.823 75.485  1.00 36.83  ? 45  THR G C     1 
ATOM   7929  O O     . THR G 1 44  ? 29.506  -47.737 76.249  1.00 37.53  ? 45  THR G O     1 
ATOM   7930  C CB    . THR G 1 44  ? 30.720  -49.950 74.144  1.00 39.30  ? 45  THR G CB    1 
ATOM   7931  O OG1   . THR G 1 44  ? 30.317  -50.473 72.882  1.00 41.62  ? 45  THR G OG1   1 
ATOM   7932  C CG2   . THR G 1 44  ? 30.051  -50.727 75.263  1.00 40.51  ? 45  THR G CG2   1 
ATOM   7933  N N     . LYS G 1 45  ? 31.687  -47.374 75.787  1.00 39.57  ? 46  LYS G N     1 
ATOM   7934  C CA    . LYS G 1 45  ? 31.975  -46.745 77.066  1.00 40.13  ? 46  LYS G CA    1 
ATOM   7935  C C     . LYS G 1 45  ? 31.341  -45.356 77.101  1.00 36.36  ? 46  LYS G C     1 
ATOM   7936  O O     . LYS G 1 45  ? 31.030  -44.839 78.173  1.00 36.97  ? 46  LYS G O     1 
ATOM   7937  C CB    . LYS G 1 45  ? 33.486  -46.671 77.314  1.00 46.11  ? 46  LYS G CB    1 
ATOM   7938  C CG    . LYS G 1 45  ? 34.187  -48.019 77.422  1.00 53.87  ? 46  LYS G CG    1 
ATOM   7939  C CD    . LYS G 1 45  ? 35.657  -47.926 77.815  1.00 62.43  ? 46  LYS G CD    1 
ATOM   7940  C CE    . LYS G 1 45  ? 35.853  -47.326 79.173  1.00 68.57  ? 46  LYS G CE    1 
ATOM   7941  N NZ    . LYS G 1 45  ? 37.270  -47.269 79.543  1.00 71.57  ? 46  LYS G NZ    1 
ATOM   7942  N N     . LEU G 1 46  ? 31.147  -44.767 75.917  1.00 33.74  ? 47  LEU G N     1 
ATOM   7943  C CA    . LEU G 1 46  ? 30.563  -43.442 75.803  1.00 35.22  ? 47  LEU G CA    1 
ATOM   7944  C C     . LEU G 1 46  ? 29.051  -43.550 75.980  1.00 38.16  ? 47  LEU G C     1 
ATOM   7945  O O     . LEU G 1 46  ? 28.432  -42.705 76.622  1.00 42.06  ? 47  LEU G O     1 
ATOM   7946  C CB    . LEU G 1 46  ? 30.930  -42.834 74.450  1.00 38.56  ? 47  LEU G CB    1 
ATOM   7947  C CG    . LEU G 1 46  ? 30.919  -41.303 74.371  1.00 39.29  ? 47  LEU G CG    1 
ATOM   7948  C CD1   . LEU G 1 46  ? 31.055  -40.842 72.931  1.00 39.73  ? 47  LEU G CD1   1 
ATOM   7949  C CD2   . LEU G 1 46  ? 29.674  -40.712 75.008  1.00 43.26  ? 47  LEU G CD2   1 
ATOM   7950  N N     . ASN G 1 47  ? 28.471  -44.607 75.399  1.00 38.90  ? 48  ASN G N     1 
ATOM   7951  C CA    . ASN G 1 47  ? 27.047  -44.876 75.509  1.00 36.04  ? 48  ASN G CA    1 
ATOM   7952  C C     . ASN G 1 47  ? 26.819  -46.376 75.336  1.00 41.87  ? 48  ASN G C     1 
ATOM   7953  O O     . ASN G 1 47  ? 27.087  -46.928 74.271  1.00 39.70  ? 48  ASN G O     1 
ATOM   7954  C CB    . ASN G 1 47  ? 26.244  -44.063 74.499  1.00 34.38  ? 48  ASN G CB    1 
ATOM   7955  C CG    . ASN G 1 47  ? 24.756  -44.167 74.734  1.00 31.34  ? 48  ASN G CG    1 
ATOM   7956  O OD1   . ASN G 1 47  ? 24.222  -45.273 74.872  1.00 31.11  ? 48  ASN G OD1   1 
ATOM   7957  N ND2   . ASN G 1 47  ? 24.075  -43.032 74.798  1.00 27.18  ? 48  ASN G ND2   1 
ATOM   7958  N N     . PRO G 1 48  ? 26.315  -47.078 76.376  1.00 44.75  ? 49  PRO G N     1 
ATOM   7959  C CA    . PRO G 1 48  ? 26.202  -48.538 76.339  1.00 47.11  ? 49  PRO G CA    1 
ATOM   7960  C C     . PRO G 1 48  ? 25.118  -49.069 75.403  1.00 48.28  ? 49  PRO G C     1 
ATOM   7961  O O     . PRO G 1 48  ? 25.230  -50.180 74.890  1.00 46.19  ? 49  PRO G O     1 
ATOM   7962  C CB    . PRO G 1 48  ? 25.913  -48.882 77.814  1.00 48.88  ? 49  PRO G CB    1 
ATOM   7963  C CG    . PRO G 1 48  ? 25.173  -47.670 78.336  1.00 48.78  ? 49  PRO G CG    1 
ATOM   7964  C CD    . PRO G 1 48  ? 25.834  -46.495 77.638  1.00 50.28  ? 49  PRO G CD    1 
ATOM   7965  N N     . ASN G 1 49  ? 24.068  -48.268 75.194  1.00 45.13  ? 50  ASN G N     1 
ATOM   7966  C CA    . ASN G 1 49  ? 22.938  -48.681 74.378  1.00 47.03  ? 50  ASN G CA    1 
ATOM   7967  C C     . ASN G 1 49  ? 23.298  -48.520 72.903  1.00 42.66  ? 50  ASN G C     1 
ATOM   7968  O O     . ASN G 1 49  ? 22.923  -47.534 72.274  1.00 37.64  ? 50  ASN G O     1 
ATOM   7969  C CB    . ASN G 1 49  ? 21.679  -47.899 74.735  1.00 52.46  ? 50  ASN G CB    1 
ATOM   7970  C CG    . ASN G 1 49  ? 20.442  -48.479 74.092  1.00 58.04  ? 50  ASN G CG    1 
ATOM   7971  O OD1   . ASN G 1 49  ? 20.504  -49.550 73.478  1.00 61.99  ? 50  ASN G OD1   1 
ATOM   7972  N ND2   . ASN G 1 49  ? 19.312  -47.802 74.232  1.00 59.53  ? 50  ASN G ND2   1 
ATOM   7973  N N     . VAL G 1 50  ? 24.014  -49.512 72.358  1.00 43.68  ? 51  VAL G N     1 
ATOM   7974  C CA    . VAL G 1 50  ? 24.508  -49.443 70.992  1.00 39.97  ? 51  VAL G CA    1 
ATOM   7975  C C     . VAL G 1 50  ? 24.059  -50.682 70.223  1.00 38.53  ? 51  VAL G C     1 
ATOM   7976  O O     . VAL G 1 50  ? 24.160  -51.802 70.720  1.00 38.64  ? 51  VAL G O     1 
ATOM   7977  C CB    . VAL G 1 50  ? 26.043  -49.306 70.960  1.00 42.00  ? 51  VAL G CB    1 
ATOM   7978  C CG1   . VAL G 1 50  ? 26.594  -49.420 69.543  1.00 43.43  ? 51  VAL G CG1   1 
ATOM   7979  C CG2   . VAL G 1 50  ? 26.510  -48.013 71.617  1.00 41.82  ? 51  VAL G CG2   1 
ATOM   7980  N N     . ILE G 1 51  ? 23.561  -50.457 69.002  1.00 39.47  ? 52  ILE G N     1 
ATOM   7981  C CA    . ILE G 1 51  ? 23.303  -51.529 68.054  1.00 38.06  ? 52  ILE G CA    1 
ATOM   7982  C C     . ILE G 1 51  ? 24.238  -51.344 66.863  1.00 35.17  ? 52  ILE G C     1 
ATOM   7983  O O     . ILE G 1 51  ? 24.278  -50.273 66.262  1.00 30.83  ? 52  ILE G O     1 
ATOM   7984  C CB    . ILE G 1 51  ? 21.826  -51.552 67.618  1.00 41.18  ? 52  ILE G CB    1 
ATOM   7985  C CG1   . ILE G 1 51  ? 20.888  -51.818 68.798  1.00 43.65  ? 52  ILE G CG1   1 
ATOM   7986  C CG2   . ILE G 1 51  ? 21.608  -52.561 66.489  1.00 38.95  ? 52  ILE G CG2   1 
ATOM   7987  C CD1   . ILE G 1 51  ? 20.851  -50.702 69.825  1.00 48.39  ? 52  ILE G CD1   1 
ATOM   7988  N N     . ASN G 1 52  ? 24.990  -52.401 66.539  1.00 32.25  ? 53  ASN G N     1 
ATOM   7989  C CA    . ASN G 1 52  ? 25.974  -52.353 65.471  1.00 32.40  ? 53  ASN G CA    1 
ATOM   7990  C C     . ASN G 1 52  ? 25.295  -52.712 64.151  1.00 33.61  ? 53  ASN G C     1 
ATOM   7991  O O     . ASN G 1 52  ? 24.692  -53.775 64.025  1.00 34.77  ? 53  ASN G O     1 
ATOM   7992  C CB    . ASN G 1 52  ? 27.163  -53.254 65.784  1.00 33.10  ? 53  ASN G CB    1 
ATOM   7993  C CG    . ASN G 1 52  ? 28.262  -53.138 64.756  1.00 31.92  ? 53  ASN G CG    1 
ATOM   7994  O OD1   . ASN G 1 52  ? 28.070  -52.518 63.704  1.00 33.34  ? 53  ASN G OD1   1 
ATOM   7995  N ND2   . ASN G 1 52  ? 29.411  -53.736 65.032  1.00 36.04  ? 53  ASN G ND2   1 
ATOM   7996  N N     . LEU G 1 53  ? 25.401  -51.806 63.172  1.00 33.11  ? 54  LEU G N     1 
ATOM   7997  C CA    . LEU G 1 53  ? 24.763  -51.987 61.877  1.00 34.33  ? 54  LEU G CA    1 
ATOM   7998  C C     . LEU G 1 53  ? 25.533  -53.028 61.070  1.00 35.93  ? 54  LEU G C     1 
ATOM   7999  O O     . LEU G 1 53  ? 25.055  -53.503 60.043  1.00 33.03  ? 54  LEU G O     1 
ATOM   8000  C CB    . LEU G 1 53  ? 24.698  -50.648 61.143  1.00 33.86  ? 54  LEU G CB    1 
ATOM   8001  C CG    . LEU G 1 53  ? 23.845  -49.559 61.801  1.00 35.42  ? 54  LEU G CG    1 
ATOM   8002  C CD1   . LEU G 1 53  ? 23.888  -48.270 60.997  1.00 35.38  ? 54  LEU G CD1   1 
ATOM   8003  C CD2   . LEU G 1 53  ? 22.413  -50.028 61.982  1.00 35.41  ? 54  LEU G CD2   1 
ATOM   8004  N N     . GLN G 1 54  ? 26.726  -53.381 61.560  1.00 38.06  ? 55  GLN G N     1 
ATOM   8005  C CA    . GLN G 1 54  ? 27.622  -54.279 60.852  1.00 47.94  ? 55  GLN G CA    1 
ATOM   8006  C C     . GLN G 1 54  ? 26.942  -55.631 60.647  1.00 44.85  ? 55  GLN G C     1 
ATOM   8007  O O     . GLN G 1 54  ? 27.341  -56.406 59.781  1.00 48.72  ? 55  GLN G O     1 
ATOM   8008  C CB    . GLN G 1 54  ? 28.916  -54.445 61.651  1.00 56.22  ? 55  GLN G CB    1 
ATOM   8009  C CG    . GLN G 1 54  ? 30.087  -54.986 60.839  1.00 61.16  ? 55  GLN G CG    1 
ATOM   8010  C CD    . GLN G 1 54  ? 30.639  -53.979 59.853  1.00 66.63  ? 55  GLN G CD    1 
ATOM   8011  O OE1   . GLN G 1 54  ? 30.655  -54.205 58.638  1.00 68.95  ? 55  GLN G OE1   1 
ATOM   8012  N NE2   . GLN G 1 54  ? 31.102  -52.851 60.372  1.00 71.21  ? 55  GLN G NE2   1 
ATOM   8013  N N     . GLN G 1 55  ? 25.906  -55.892 61.450  1.00 41.34  ? 56  GLN G N     1 
ATOM   8014  C CA    . GLN G 1 55  ? 25.269  -57.198 61.500  1.00 40.87  ? 56  GLN G CA    1 
ATOM   8015  C C     . GLN G 1 55  ? 24.411  -57.426 60.258  1.00 39.40  ? 56  GLN G C     1 
ATOM   8016  O O     . GLN G 1 55  ? 24.031  -58.559 59.967  1.00 32.75  ? 56  GLN G O     1 
ATOM   8017  C CB    . GLN G 1 55  ? 24.402  -57.308 62.754  1.00 44.24  ? 56  GLN G CB    1 
ATOM   8018  C CG    . GLN G 1 55  ? 23.310  -56.247 62.842  1.00 45.93  ? 56  GLN G CG    1 
ATOM   8019  C CD    . GLN G 1 55  ? 22.448  -56.380 64.078  1.00 50.88  ? 56  GLN G CD    1 
ATOM   8020  O OE1   . GLN G 1 55  ? 21.706  -57.354 64.246  1.00 48.89  ? 56  GLN G OE1   1 
ATOM   8021  N NE2   . GLN G 1 55  ? 22.531  -55.391 64.956  1.00 52.76  ? 56  GLN G NE2   1 
ATOM   8022  N N     . PHE G 1 56  ? 24.102  -56.344 59.536  1.00 34.56  ? 57  PHE G N     1 
ATOM   8023  C CA    . PHE G 1 56  ? 23.165  -56.417 58.427  1.00 36.31  ? 57  PHE G CA    1 
ATOM   8024  C C     . PHE G 1 56  ? 23.918  -56.693 57.128  1.00 36.01  ? 57  PHE G C     1 
ATOM   8025  O O     . PHE G 1 56  ? 23.310  -56.773 56.062  1.00 32.44  ? 57  PHE G O     1 
ATOM   8026  C CB    . PHE G 1 56  ? 22.331  -55.134 58.349  1.00 37.47  ? 57  PHE G CB    1 
ATOM   8027  C CG    . PHE G 1 56  ? 21.384  -54.935 59.525  1.00 38.96  ? 57  PHE G CG    1 
ATOM   8028  C CD1   . PHE G 1 56  ? 20.237  -55.712 59.654  1.00 40.88  ? 57  PHE G CD1   1 
ATOM   8029  C CD2   . PHE G 1 56  ? 21.628  -53.960 60.486  1.00 41.99  ? 57  PHE G CD2   1 
ATOM   8030  C CE1   . PHE G 1 56  ? 19.375  -55.531 60.724  1.00 40.87  ? 57  PHE G CE1   1 
ATOM   8031  C CE2   . PHE G 1 56  ? 20.759  -53.780 61.550  1.00 41.16  ? 57  PHE G CE2   1 
ATOM   8032  C CZ    . PHE G 1 56  ? 19.635  -54.564 61.666  1.00 41.46  ? 57  PHE G CZ    1 
ATOM   8033  N N     . TYR G 1 57  ? 25.241  -56.853 57.231  1.00 36.76  ? 58  TYR G N     1 
ATOM   8034  C CA    . TYR G 1 57  ? 26.068  -57.150 56.073  1.00 36.72  ? 58  TYR G CA    1 
ATOM   8035  C C     . TYR G 1 57  ? 26.016  -58.645 55.779  1.00 39.70  ? 58  TYR G C     1 
ATOM   8036  O O     . TYR G 1 57  ? 25.605  -59.437 56.624  1.00 38.51  ? 58  TYR G O     1 
ATOM   8037  C CB    . TYR G 1 57  ? 27.515  -56.698 56.282  1.00 36.57  ? 58  TYR G CB    1 
ATOM   8038  C CG    . TYR G 1 57  ? 27.751  -55.217 56.023  1.00 36.38  ? 58  TYR G CG    1 
ATOM   8039  C CD1   . TYR G 1 57  ? 27.822  -54.724 54.726  1.00 35.97  ? 58  TYR G CD1   1 
ATOM   8040  C CD2   . TYR G 1 57  ? 27.923  -54.320 57.068  1.00 36.57  ? 58  TYR G CD2   1 
ATOM   8041  C CE1   . TYR G 1 57  ? 28.038  -53.379 54.476  1.00 39.32  ? 58  TYR G CE1   1 
ATOM   8042  C CE2   . TYR G 1 57  ? 28.145  -52.973 56.832  1.00 40.61  ? 58  TYR G CE2   1 
ATOM   8043  C CZ    . TYR G 1 57  ? 28.203  -52.502 55.532  1.00 39.64  ? 58  TYR G CZ    1 
ATOM   8044  O OH    . TYR G 1 57  ? 28.419  -51.177 55.292  1.00 40.82  ? 58  TYR G OH    1 
ATOM   8045  N N     . ALA G 1 58  ? 26.444  -59.010 54.565  1.00 41.34  ? 59  ALA G N     1 
ATOM   8046  C CA    . ALA G 1 58  ? 26.508  -60.401 54.153  1.00 44.60  ? 59  ALA G CA    1 
ATOM   8047  C C     . ALA G 1 58  ? 27.039  -61.246 55.306  1.00 43.53  ? 59  ALA G C     1 
ATOM   8048  O O     . ALA G 1 58  ? 28.123  -60.991 55.826  1.00 36.32  ? 59  ALA G O     1 
ATOM   8049  C CB    . ALA G 1 58  ? 27.368  -60.540 52.917  1.00 46.03  ? 59  ALA G CB    1 
ATOM   8050  N N     . GLN G 1 59  ? 26.252  -62.253 55.688  1.00 47.65  ? 60  GLN G N     1 
ATOM   8051  C CA    . GLN G 1 59  ? 26.532  -63.067 56.856  1.00 57.70  ? 60  GLN G CA    1 
ATOM   8052  C C     . GLN G 1 59  ? 27.838  -63.833 56.652  1.00 65.02  ? 60  GLN G C     1 
ATOM   8053  O O     . GLN G 1 59  ? 28.889  -63.412 57.131  1.00 70.35  ? 60  GLN G O     1 
ATOM   8054  C CB    . GLN G 1 59  ? 25.336  -63.994 57.065  1.00 64.37  ? 60  GLN G CB    1 
ATOM   8055  C CG    . GLN G 1 59  ? 25.317  -64.705 58.412  1.00 66.80  ? 60  GLN G CG    1 
ATOM   8056  C CD    . GLN G 1 59  ? 24.217  -65.737 58.504  1.00 67.68  ? 60  GLN G CD    1 
ATOM   8057  O OE1   . GLN G 1 59  ? 23.329  -65.660 59.360  1.00 72.28  ? 60  GLN G OE1   1 
ATOM   8058  N NE2   . GLN G 1 59  ? 24.258  -66.709 57.604  1.00 68.07  ? 60  GLN G NE2   1 
ATOM   8059  N N     . ASN G 1 60  ? 27.754  -64.961 55.939  1.00 66.65  ? 61  ASN G N     1 
ATOM   8060  C CA    . ASN G 1 60  ? 28.906  -65.818 55.710  1.00 67.42  ? 61  ASN G CA    1 
ATOM   8061  C C     . ASN G 1 60  ? 28.782  -66.470 54.335  1.00 61.08  ? 61  ASN G C     1 
ATOM   8062  O O     . ASN G 1 60  ? 27.913  -67.310 54.114  1.00 66.11  ? 61  ASN G O     1 
ATOM   8063  C CB    . ASN G 1 60  ? 29.070  -66.832 56.838  1.00 70.91  ? 61  ASN G CB    1 
ATOM   8064  C CG    . ASN G 1 60  ? 27.744  -67.337 57.356  1.00 73.20  ? 61  ASN G CG    1 
ATOM   8065  O OD1   . ASN G 1 60  ? 26.701  -67.098 56.738  1.00 76.24  ? 61  ASN G OD1   1 
ATOM   8066  N ND2   . ASN G 1 60  ? 27.761  -68.035 58.483  1.00 68.53  ? 61  ASN G ND2   1 
ATOM   8067  N N     . GLY G 1 61  ? 29.669  -66.065 53.418  1.00 49.61  ? 62  GLY G N     1 
ATOM   8068  C CA    . GLY G 1 61  ? 29.647  -66.551 52.048  1.00 46.38  ? 62  GLY G CA    1 
ATOM   8069  C C     . GLY G 1 61  ? 28.254  -66.421 51.440  1.00 40.95  ? 62  GLY G C     1 
ATOM   8070  O O     . GLY G 1 61  ? 27.938  -67.074 50.449  1.00 42.71  ? 62  GLY G O     1 
ATOM   8071  N N     . GLU G 1 62  ? 27.430  -65.561 52.048  1.00 43.62  ? 63  GLU G N     1 
ATOM   8072  C CA    . GLU G 1 62  ? 26.058  -65.365 51.615  1.00 42.10  ? 63  GLU G CA    1 
ATOM   8073  C C     . GLU G 1 62  ? 26.022  -64.369 50.460  1.00 37.26  ? 63  GLU G C     1 
ATOM   8074  O O     . GLU G 1 62  ? 26.711  -63.352 50.492  1.00 32.90  ? 63  GLU G O     1 
ATOM   8075  C CB    . GLU G 1 62  ? 25.203  -64.847 52.770  1.00 46.23  ? 63  GLU G CB    1 
ATOM   8076  C CG    . GLU G 1 62  ? 23.748  -64.606 52.380  1.00 51.49  ? 63  GLU G CG    1 
ATOM   8077  C CD    . GLU G 1 62  ? 22.968  -63.768 53.376  1.00 57.90  ? 63  GLU G CD    1 
ATOM   8078  O OE1   . GLU G 1 62  ? 23.549  -63.388 54.415  1.00 59.25  ? 63  GLU G OE1   1 
ATOM   8079  O OE2   . GLU G 1 62  ? 21.780  -63.489 53.109  1.00 61.86  ? 63  GLU G OE2   1 
ATOM   8080  N N     . VAL G 1 63  ? 25.201  -64.673 49.449  1.00 35.52  ? 64  VAL G N     1 
ATOM   8081  C CA    . VAL G 1 63  ? 24.992  -63.771 48.329  1.00 34.97  ? 64  VAL G CA    1 
ATOM   8082  C C     . VAL G 1 63  ? 23.879  -62.795 48.701  1.00 33.80  ? 64  VAL G C     1 
ATOM   8083  O O     . VAL G 1 63  ? 22.707  -63.165 48.733  1.00 29.95  ? 64  VAL G O     1 
ATOM   8084  C CB    . VAL G 1 63  ? 24.661  -64.525 47.026  1.00 36.22  ? 64  VAL G CB    1 
ATOM   8085  C CG1   . VAL G 1 63  ? 24.270  -63.571 45.904  1.00 36.61  ? 64  VAL G CG1   1 
ATOM   8086  C CG2   . VAL G 1 63  ? 25.809  -65.426 46.587  1.00 34.82  ? 64  VAL G CG2   1 
ATOM   8087  N N     . LYS G 1 64  ? 24.270  -61.547 48.977  1.00 32.82  ? 65  LYS G N     1 
ATOM   8088  C CA    . LYS G 1 64  ? 23.346  -60.529 49.445  1.00 34.14  ? 65  LYS G CA    1 
ATOM   8089  C C     . LYS G 1 64  ? 23.681  -59.195 48.784  1.00 34.66  ? 65  LYS G C     1 
ATOM   8090  O O     . LYS G 1 64  ? 24.833  -58.767 48.788  1.00 30.13  ? 65  LYS G O     1 
ATOM   8091  C CB    . LYS G 1 64  ? 23.432  -60.423 50.972  1.00 36.10  ? 65  LYS G CB    1 
ATOM   8092  C CG    . LYS G 1 64  ? 22.458  -59.444 51.613  1.00 37.40  ? 65  LYS G CG    1 
ATOM   8093  C CD    . LYS G 1 64  ? 22.497  -59.451 53.137  1.00 37.23  ? 65  LYS G CD    1 
ATOM   8094  C CE    . LYS G 1 64  ? 21.398  -58.638 53.743  1.00 37.11  ? 65  LYS G CE    1 
ATOM   8095  N NZ    . LYS G 1 64  ? 21.395  -58.734 55.205  1.00 38.62  ? 65  LYS G NZ    1 
ATOM   8096  N N     . ASN G 1 65  ? 22.654  -58.549 48.222  1.00 36.55  ? 66  ASN G N     1 
ATOM   8097  C CA    . ASN G 1 65  ? 22.807  -57.252 47.584  1.00 40.71  ? 66  ASN G CA    1 
ATOM   8098  C C     . ASN G 1 65  ? 22.914  -56.183 48.670  1.00 40.13  ? 66  ASN G C     1 
ATOM   8099  O O     . ASN G 1 65  ? 22.136  -56.185 49.620  1.00 42.90  ? 66  ASN G O     1 
ATOM   8100  C CB    . ASN G 1 65  ? 21.659  -56.976 46.620  1.00 41.65  ? 66  ASN G CB    1 
ATOM   8101  C CG    . ASN G 1 65  ? 21.928  -55.788 45.728  1.00 42.39  ? 66  ASN G CG    1 
ATOM   8102  O OD1   . ASN G 1 65  ? 22.165  -54.680 46.221  1.00 46.09  ? 66  ASN G OD1   1 
ATOM   8103  N ND2   . ASN G 1 65  ? 21.895  -55.994 44.420  1.00 44.21  ? 66  ASN G ND2   1 
ATOM   8104  N N     . ARG G 1 66  ? 23.886  -55.275 48.518  1.00 41.04  ? 67  ARG G N     1 
ATOM   8105  C CA    . ARG G 1 66  ? 24.139  -54.253 49.522  1.00 43.66  ? 67  ARG G CA    1 
ATOM   8106  C C     . ARG G 1 66  ? 22.960  -53.285 49.584  1.00 39.71  ? 67  ARG G C     1 
ATOM   8107  O O     . ARG G 1 66  ? 22.789  -52.578 50.573  1.00 38.49  ? 67  ARG G O     1 
ATOM   8108  C CB    . ARG G 1 66  ? 25.449  -53.502 49.256  1.00 44.64  ? 67  ARG G CB    1 
ATOM   8109  C CG    . ARG G 1 66  ? 26.703  -54.343 49.448  1.00 47.68  ? 67  ARG G CG    1 
ATOM   8110  C CD    . ARG G 1 66  ? 27.922  -53.483 49.758  1.00 49.29  ? 67  ARG G CD    1 
ATOM   8111  N NE    . ARG G 1 66  ? 28.182  -52.469 48.731  1.00 51.99  ? 67  ARG G NE    1 
ATOM   8112  C CZ    . ARG G 1 66  ? 28.582  -52.728 47.494  1.00 52.01  ? 67  ARG G CZ    1 
ATOM   8113  N NH1   . ARG G 1 66  ? 28.796  -53.975 47.114  1.00 54.56  ? 67  ARG G NH1   1 
ATOM   8114  N NH2   . ARG G 1 66  ? 28.780  -51.736 46.643  1.00 53.12  ? 67  ARG G NH2   1 
ATOM   8115  N N     . ARG G 1 67  ? 22.155  -53.258 48.517  1.00 41.58  ? 68  ARG G N     1 
ATOM   8116  C CA    . ARG G 1 67  ? 20.946  -52.452 48.501  1.00 43.99  ? 68  ARG G CA    1 
ATOM   8117  C C     . ARG G 1 67  ? 20.046  -52.890 49.653  1.00 39.86  ? 68  ARG G C     1 
ATOM   8118  O O     . ARG G 1 67  ? 19.453  -52.056 50.335  1.00 37.98  ? 68  ARG G O     1 
ATOM   8119  C CB    . ARG G 1 67  ? 20.209  -52.575 47.162  1.00 47.96  ? 68  ARG G CB    1 
ATOM   8120  C CG    . ARG G 1 67  ? 20.898  -51.889 45.991  1.00 49.32  ? 68  ARG G CG    1 
ATOM   8121  C CD    . ARG G 1 67  ? 20.112  -52.060 44.698  1.00 53.59  ? 68  ARG G CD    1 
ATOM   8122  N NE    . ARG G 1 67  ? 20.716  -51.347 43.566  1.00 54.79  ? 68  ARG G NE    1 
ATOM   8123  C CZ    . ARG G 1 67  ? 20.819  -50.027 43.468  1.00 61.20  ? 68  ARG G CZ    1 
ATOM   8124  N NH1   . ARG G 1 67  ? 20.351  -49.251 44.430  1.00 60.15  ? 68  ARG G NH1   1 
ATOM   8125  N NH2   . ARG G 1 67  ? 21.383  -49.486 42.403  1.00 63.83  ? 68  ARG G NH2   1 
ATOM   8126  N N     . ASP G 1 68  ? 19.968  -54.209 49.864  1.00 37.58  ? 69  ASP G N     1 
ATOM   8127  C CA    . ASP G 1 68  ? 19.128  -54.781 50.902  1.00 37.61  ? 69  ASP G CA    1 
ATOM   8128  C C     . ASP G 1 68  ? 19.753  -54.510 52.268  1.00 31.71  ? 69  ASP G C     1 
ATOM   8129  O O     . ASP G 1 68  ? 19.050  -54.194 53.224  1.00 31.89  ? 69  ASP G O     1 
ATOM   8130  C CB    . ASP G 1 68  ? 18.897  -56.267 50.668  1.00 43.23  ? 69  ASP G CB    1 
ATOM   8131  C CG    . ASP G 1 68  ? 18.222  -56.621 49.351  1.00 48.16  ? 69  ASP G CG    1 
ATOM   8132  O OD1   . ASP G 1 68  ? 17.114  -56.101 49.100  1.00 45.90  ? 69  ASP G OD1   1 
ATOM   8133  O OD2   . ASP G 1 68  ? 18.809  -57.418 48.588  1.00 55.28  ? 69  ASP G OD2   1 
ATOM   8134  N N     . THR G 1 69  ? 21.081  -54.640 52.347  1.00 29.97  ? 70  THR G N     1 
ATOM   8135  C CA    . THR G 1 69  ? 21.805  -54.391 53.582  1.00 31.63  ? 70  THR G CA    1 
ATOM   8136  C C     . THR G 1 69  ? 21.506  -52.974 54.066  1.00 30.17  ? 70  THR G C     1 
ATOM   8137  O O     . THR G 1 69  ? 21.230  -52.761 55.244  1.00 30.27  ? 70  THR G O     1 
ATOM   8138  C CB    . THR G 1 69  ? 23.301  -54.601 53.354  1.00 30.23  ? 70  THR G CB    1 
ATOM   8139  O OG1   . THR G 1 69  ? 23.454  -55.994 53.105  1.00 30.28  ? 70  THR G OG1   1 
ATOM   8140  C CG2   . THR G 1 69  ? 24.138  -54.197 54.555  1.00 30.26  ? 70  THR G CG2   1 
ATOM   8141  N N     . TYR G 1 70  ? 21.566  -52.012 53.140  1.00 26.67  ? 71  TYR G N     1 
ATOM   8142  C CA    . TYR G 1 70  ? 21.384  -50.609 53.473  1.00 27.69  ? 71  TYR G CA    1 
ATOM   8143  C C     . TYR G 1 70  ? 19.925  -50.363 53.847  1.00 30.74  ? 71  TYR G C     1 
ATOM   8144  O O     . TYR G 1 70  ? 19.631  -49.528 54.699  1.00 32.02  ? 71  TYR G O     1 
ATOM   8145  C CB    . TYR G 1 70  ? 21.833  -49.736 52.298  1.00 25.69  ? 71  TYR G CB    1 
ATOM   8146  C CG    . TYR G 1 70  ? 23.286  -49.936 51.887  1.00 24.51  ? 71  TYR G CG    1 
ATOM   8147  C CD1   . TYR G 1 70  ? 24.245  -50.335 52.810  1.00 24.48  ? 71  TYR G CD1   1 
ATOM   8148  C CD2   . TYR G 1 70  ? 23.697  -49.728 50.577  1.00 24.56  ? 71  TYR G CD2   1 
ATOM   8149  C CE1   . TYR G 1 70  ? 25.568  -50.520 52.444  1.00 24.06  ? 71  TYR G CE1   1 
ATOM   8150  C CE2   . TYR G 1 70  ? 25.017  -49.909 50.197  1.00 25.18  ? 71  TYR G CE2   1 
ATOM   8151  C CZ    . TYR G 1 70  ? 25.955  -50.306 51.133  1.00 24.47  ? 71  TYR G CZ    1 
ATOM   8152  O OH    . TYR G 1 70  ? 27.256  -50.488 50.767  1.00 25.49  ? 71  TYR G OH    1 
ATOM   8153  N N     . GLU G 1 71  ? 19.020  -51.102 53.196  1.00 32.54  ? 72  GLU G N     1 
ATOM   8154  C CA    . GLU G 1 71  ? 17.594  -50.976 53.446  1.00 33.96  ? 72  GLU G CA    1 
ATOM   8155  C C     . GLU G 1 71  ? 17.278  -51.459 54.858  1.00 31.69  ? 72  GLU G C     1 
ATOM   8156  O O     . GLU G 1 71  ? 16.460  -50.862 55.553  1.00 33.77  ? 72  GLU G O     1 
ATOM   8157  C CB    . GLU G 1 71  ? 16.798  -51.772 52.412  1.00 35.25  ? 72  GLU G CB    1 
ATOM   8158  C CG    . GLU G 1 71  ? 15.299  -51.799 52.694  1.00 38.43  ? 72  GLU G CG    1 
ATOM   8159  C CD    . GLU G 1 71  ? 14.666  -50.426 52.830  1.00 41.86  ? 72  GLU G CD    1 
ATOM   8160  O OE1   . GLU G 1 71  ? 14.750  -49.637 51.866  1.00 44.69  ? 72  GLU G OE1   1 
ATOM   8161  O OE2   . GLU G 1 71  ? 14.087  -50.146 53.901  1.00 46.00  ? 72  GLU G OE2   1 
ATOM   8162  N N     . GLN G 1 72  ? 17.929  -52.553 55.263  1.00 31.17  ? 73  GLN G N     1 
ATOM   8163  C CA    . GLN G 1 72  ? 17.723  -53.130 56.581  1.00 32.32  ? 73  GLN G CA    1 
ATOM   8164  C C     . GLN G 1 72  ? 18.339  -52.217 57.636  1.00 31.62  ? 73  GLN G C     1 
ATOM   8165  O O     . GLN G 1 72  ? 17.813  -52.094 58.740  1.00 29.25  ? 73  GLN G O     1 
ATOM   8166  C CB    . GLN G 1 72  ? 18.315  -54.538 56.643  1.00 33.47  ? 73  GLN G CB    1 
ATOM   8167  C CG    . GLN G 1 72  ? 17.595  -55.550 55.759  1.00 32.57  ? 73  GLN G CG    1 
ATOM   8168  C CD    . GLN G 1 72  ? 18.252  -56.913 55.762  1.00 35.04  ? 73  GLN G CD    1 
ATOM   8169  O OE1   . GLN G 1 72  ? 19.342  -57.101 56.314  1.00 34.90  ? 73  GLN G OE1   1 
ATOM   8170  N NE2   . GLN G 1 72  ? 17.599  -57.877 55.129  1.00 34.27  ? 73  GLN G NE2   1 
ATOM   8171  N N     . MET G 1 73  ? 19.465  -51.585 57.288  1.00 33.16  ? 74  MET G N     1 
ATOM   8172  C CA    . MET G 1 73  ? 20.108  -50.632 58.175  1.00 34.02  ? 74  MET G CA    1 
ATOM   8173  C C     . MET G 1 73  ? 19.146  -49.480 58.452  1.00 31.61  ? 74  MET G C     1 
ATOM   8174  O O     . MET G 1 73  ? 18.882  -49.150 59.606  1.00 30.75  ? 74  MET G O     1 
ATOM   8175  C CB    . MET G 1 73  ? 21.408  -50.094 57.566  1.00 38.08  ? 74  MET G CB    1 
ATOM   8176  C CG    . MET G 1 73  ? 22.554  -51.088 57.577  1.00 40.68  ? 74  MET G CG    1 
ATOM   8177  S SD    . MET G 1 73  ? 24.058  -50.433 56.825  1.00 47.35  ? 74  MET G SD    1 
ATOM   8178  C CE    . MET G 1 73  ? 25.150  -51.854 56.965  1.00 46.17  ? 74  MET G CE    1 
ATOM   8179  N N     . VAL G 1 74  ? 18.610  -48.894 57.377  1.00 29.97  ? 75  VAL G N     1 
ATOM   8180  C CA    . VAL G 1 74  ? 17.737  -47.735 57.480  1.00 32.17  ? 75  VAL G CA    1 
ATOM   8181  C C     . VAL G 1 74  ? 16.519  -48.094 58.326  1.00 31.61  ? 75  VAL G C     1 
ATOM   8182  O O     . VAL G 1 74  ? 16.059  -47.287 59.131  1.00 27.92  ? 75  VAL G O     1 
ATOM   8183  C CB    . VAL G 1 74  ? 17.312  -47.226 56.089  1.00 29.28  ? 75  VAL G CB    1 
ATOM   8184  C CG1   . VAL G 1 74  ? 16.223  -46.165 56.182  1.00 27.91  ? 75  VAL G CG1   1 
ATOM   8185  C CG2   . VAL G 1 74  ? 18.499  -46.711 55.285  1.00 30.58  ? 75  VAL G CG2   1 
ATOM   8186  N N     . ASN G 1 75  ? 16.002  -49.311 58.127  1.00 33.19  ? 76  ASN G N     1 
ATOM   8187  C CA    . ASN G 1 75  ? 14.772  -49.744 58.771  1.00 36.43  ? 76  ASN G CA    1 
ATOM   8188  C C     . ASN G 1 75  ? 15.005  -49.897 60.272  1.00 37.18  ? 76  ASN G C     1 
ATOM   8189  O O     . ASN G 1 75  ? 14.129  -49.581 61.074  1.00 42.94  ? 76  ASN G O     1 
ATOM   8190  C CB    . ASN G 1 75  ? 14.244  -51.032 58.149  1.00 39.97  ? 76  ASN G CB    1 
ATOM   8191  C CG    . ASN G 1 75  ? 12.923  -51.452 58.749  1.00 39.59  ? 76  ASN G CG    1 
ATOM   8192  O OD1   . ASN G 1 75  ? 11.944  -50.702 58.684  1.00 44.30  ? 76  ASN G OD1   1 
ATOM   8193  N ND2   . ASN G 1 75  ? 12.875  -52.640 59.334  1.00 46.45  ? 76  ASN G ND2   1 
ATOM   8194  N N     . ALA G 1 76  ? 16.190  -50.396 60.636  1.00 39.40  ? 77  ALA G N     1 
ATOM   8195  C CA    . ALA G 1 76  ? 16.549  -50.592 62.030  1.00 41.87  ? 77  ALA G CA    1 
ATOM   8196  C C     . ALA G 1 76  ? 16.599  -49.245 62.746  1.00 39.30  ? 77  ALA G C     1 
ATOM   8197  O O     . ALA G 1 76  ? 16.167  -49.129 63.891  1.00 33.95  ? 77  ALA G O     1 
ATOM   8198  C CB    . ALA G 1 76  ? 17.874  -51.318 62.122  1.00 42.22  ? 77  ALA G CB    1 
ATOM   8199  N N     . ILE G 1 77  ? 17.129  -48.231 62.052  1.00 39.01  ? 78  ILE G N     1 
ATOM   8200  C CA    . ILE G 1 77  ? 17.296  -46.904 62.621  1.00 36.28  ? 78  ILE G CA    1 
ATOM   8201  C C     . ILE G 1 77  ? 15.923  -46.263 62.819  1.00 38.89  ? 78  ILE G C     1 
ATOM   8202  O O     . ILE G 1 77  ? 15.666  -45.649 63.851  1.00 39.35  ? 78  ILE G O     1 
ATOM   8203  C CB    . ILE G 1 77  ? 18.204  -46.036 61.730  1.00 38.91  ? 78  ILE G CB    1 
ATOM   8204  C CG1   . ILE G 1 77  ? 19.596  -46.650 61.573  1.00 40.22  ? 78  ILE G CG1   1 
ATOM   8205  C CG2   . ILE G 1 77  ? 18.278  -44.603 62.259  1.00 37.97  ? 78  ILE G CG2   1 
ATOM   8206  C CD1   . ILE G 1 77  ? 20.517  -45.868 60.652  1.00 39.05  ? 78  ILE G CD1   1 
ATOM   8207  N N     . LEU G 1 78  ? 15.051  -46.412 61.816  1.00 37.08  ? 79  LEU G N     1 
ATOM   8208  C CA    . LEU G 1 78  ? 13.739  -45.784 61.838  1.00 37.64  ? 79  LEU G CA    1 
ATOM   8209  C C     . LEU G 1 78  ? 12.869  -46.422 62.918  1.00 37.78  ? 79  LEU G C     1 
ATOM   8210  O O     . LEU G 1 78  ? 12.061  -45.740 63.545  1.00 41.98  ? 79  LEU G O     1 
ATOM   8211  C CB    . LEU G 1 78  ? 13.082  -45.875 60.461  1.00 40.51  ? 79  LEU G CB    1 
ATOM   8212  C CG    . LEU G 1 78  ? 13.458  -44.773 59.465  1.00 43.33  ? 79  LEU G CG    1 
ATOM   8213  C CD1   . LEU G 1 78  ? 13.072  -43.412 60.016  1.00 45.70  ? 79  LEU G CD1   1 
ATOM   8214  C CD2   . LEU G 1 78  ? 14.935  -44.808 59.117  1.00 46.99  ? 79  LEU G CD2   1 
ATOM   8215  N N     . ASP G 1 79  ? 13.029  -47.734 63.122  1.00 34.95  ? 80  ASP G N     1 
ATOM   8216  C CA    . ASP G 1 79  ? 12.256  -48.446 64.126  1.00 35.70  ? 80  ASP G CA    1 
ATOM   8217  C C     . ASP G 1 79  ? 12.472  -47.793 65.489  1.00 34.49  ? 80  ASP G C     1 
ATOM   8218  O O     . ASP G 1 79  ? 11.529  -47.631 66.260  1.00 35.67  ? 80  ASP G O     1 
ATOM   8219  C CB    . ASP G 1 79  ? 12.581  -49.932 64.139  1.00 34.40  ? 80  ASP G CB    1 
ATOM   8220  C CG    . ASP G 1 79  ? 11.895  -50.758 63.059  1.00 38.20  ? 80  ASP G CG    1 
ATOM   8221  O OD1   . ASP G 1 79  ? 11.152  -50.164 62.249  1.00 38.25  ? 80  ASP G OD1   1 
ATOM   8222  O OD2   . ASP G 1 79  ? 12.095  -51.992 63.047  1.00 38.41  ? 80  ASP G OD2   1 
ATOM   8223  N N     . ALA G 1 80  ? 13.724  -47.417 65.768  1.00 30.84  ? 81  ALA G N     1 
ATOM   8224  C CA    . ALA G 1 80  ? 14.073  -46.785 67.029  1.00 32.05  ? 81  ALA G CA    1 
ATOM   8225  C C     . ALA G 1 80  ? 13.409  -45.413 67.123  1.00 30.90  ? 81  ALA G C     1 
ATOM   8226  O O     . ALA G 1 80  ? 12.949  -45.013 68.191  1.00 31.79  ? 81  ALA G O     1 
ATOM   8227  C CB    . ALA G 1 80  ? 15.577  -46.683 67.155  1.00 33.68  ? 81  ALA G CB    1 
ATOM   8228  N N     . VAL G 1 81  ? 13.359  -44.706 65.989  1.00 27.53  ? 82  VAL G N     1 
ATOM   8229  C CA    . VAL G 1 81  ? 12.821  -43.356 65.938  1.00 29.42  ? 82  VAL G CA    1 
ATOM   8230  C C     . VAL G 1 81  ? 11.303  -43.413 66.096  1.00 29.66  ? 82  VAL G C     1 
ATOM   8231  O O     . VAL G 1 81  ? 10.719  -42.597 66.805  1.00 31.65  ? 82  VAL G O     1 
ATOM   8232  C CB    . VAL G 1 81  ? 13.222  -42.644 64.632  1.00 29.29  ? 82  VAL G CB    1 
ATOM   8233  C CG1   . VAL G 1 81  ? 12.564  -41.274 64.506  1.00 28.30  ? 82  VAL G CG1   1 
ATOM   8234  C CG2   . VAL G 1 81  ? 14.736  -42.525 64.495  1.00 27.65  ? 82  VAL G CG2   1 
ATOM   8235  N N     . ARG G 1 82  ? 10.675  -44.384 65.424  1.00 31.84  ? 83  ARG G N     1 
ATOM   8236  C CA    . ARG G 1 82  ? 9.230   -44.543 65.475  1.00 34.35  ? 83  ARG G CA    1 
ATOM   8237  C C     . ARG G 1 82  ? 8.819   -45.044 66.857  1.00 36.09  ? 83  ARG G C     1 
ATOM   8238  O O     . ARG G 1 82  ? 7.693   -44.817 67.292  1.00 38.43  ? 83  ARG G O     1 
ATOM   8239  C CB    . ARG G 1 82  ? 8.743   -45.491 64.372  1.00 37.33  ? 83  ARG G CB    1 
ATOM   8240  C CG    . ARG G 1 82  ? 8.778   -44.879 62.979  1.00 39.31  ? 83  ARG G CG    1 
ATOM   8241  C CD    . ARG G 1 82  ? 8.253   -45.828 61.911  1.00 44.32  ? 83  ARG G CD    1 
ATOM   8242  N NE    . ARG G 1 82  ? 9.135   -46.980 61.697  1.00 46.41  ? 83  ARG G NE    1 
ATOM   8243  C CZ    . ARG G 1 82  ? 9.723   -47.276 60.543  1.00 48.67  ? 83  ARG G CZ    1 
ATOM   8244  N NH1   . ARG G 1 82  ? 9.540   -46.502 59.487  1.00 48.08  ? 83  ARG G NH1   1 
ATOM   8245  N NH2   . ARG G 1 82  ? 10.495  -48.345 60.449  1.00 46.94  ? 83  ARG G NH2   1 
ATOM   8246  N N     . ALA G 1 83  ? 9.747   -45.725 67.538  1.00 39.78  ? 84  ALA G N     1 
ATOM   8247  C CA    . ALA G 1 83  ? 9.507   -46.219 68.883  1.00 40.59  ? 84  ALA G CA    1 
ATOM   8248  C C     . ALA G 1 83  ? 9.424   -45.045 69.856  1.00 38.55  ? 84  ALA G C     1 
ATOM   8249  O O     . ALA G 1 83  ? 8.735   -45.123 70.870  1.00 42.01  ? 84  ALA G O     1 
ATOM   8250  C CB    . ALA G 1 83  ? 10.595  -47.193 69.279  1.00 41.28  ? 84  ALA G CB    1 
ATOM   8251  N N     . GLY G 1 84  ? 10.143  -43.963 69.533  1.00 37.88  ? 85  GLY G N     1 
ATOM   8252  C CA    . GLY G 1 84  ? 10.112  -42.747 70.329  1.00 33.73  ? 85  GLY G CA    1 
ATOM   8253  C C     . GLY G 1 84  ? 11.463  -42.469 70.983  1.00 34.12  ? 85  GLY G C     1 
ATOM   8254  O O     . GLY G 1 84  ? 11.571  -41.601 71.846  1.00 30.65  ? 85  GLY G O     1 
ATOM   8255  N N     . LYS G 1 85  ? 12.490  -43.208 70.548  1.00 35.49  ? 86  LYS G N     1 
ATOM   8256  C CA    . LYS G 1 85  ? 13.822  -43.096 71.118  1.00 35.92  ? 86  LYS G CA    1 
ATOM   8257  C C     . LYS G 1 85  ? 14.569  -41.936 70.465  1.00 35.28  ? 86  LYS G C     1 
ATOM   8258  O O     . LYS G 1 85  ? 14.463  -41.723 69.258  1.00 32.31  ? 86  LYS G O     1 
ATOM   8259  C CB    . LYS G 1 85  ? 14.603  -44.400 70.911  1.00 37.92  ? 86  LYS G CB    1 
ATOM   8260  C CG    . LYS G 1 85  ? 13.938  -45.654 71.462  1.00 40.06  ? 86  LYS G CG    1 
ATOM   8261  C CD    . LYS G 1 85  ? 14.723  -46.933 71.197  1.00 43.52  ? 86  LYS G CD    1 
ATOM   8262  C CE    . LYS G 1 85  ? 14.008  -48.161 71.668  1.00 46.07  ? 86  LYS G CE    1 
ATOM   8263  N NZ    . LYS G 1 85  ? 13.760  -48.129 73.111  1.00 48.03  ? 86  LYS G NZ    1 
ATOM   8264  N N     . LYS G 1 86  ? 15.323  -41.190 71.280  1.00 34.51  ? 87  LYS G N     1 
ATOM   8265  C CA    . LYS G 1 86  ? 16.225  -40.171 70.772  1.00 37.51  ? 87  LYS G CA    1 
ATOM   8266  C C     . LYS G 1 86  ? 17.431  -40.874 70.155  1.00 36.17  ? 87  LYS G C     1 
ATOM   8267  O O     . LYS G 1 86  ? 18.373  -41.239 70.858  1.00 30.71  ? 87  LYS G O     1 
ATOM   8268  C CB    . LYS G 1 86  ? 16.619  -39.199 71.892  1.00 39.41  ? 87  LYS G CB    1 
ATOM   8269  C CG    . LYS G 1 86  ? 17.475  -38.017 71.452  1.00 45.27  ? 87  LYS G CG    1 
ATOM   8270  C CD    . LYS G 1 86  ? 17.682  -36.959 72.530  1.00 49.69  ? 87  LYS G CD    1 
ATOM   8271  C CE    . LYS G 1 86  ? 18.350  -37.499 73.755  1.00 53.67  ? 87  LYS G CE    1 
ATOM   8272  N NZ    . LYS G 1 86  ? 18.560  -36.456 74.763  1.00 57.95  ? 87  LYS G NZ    1 
ATOM   8273  N N     . THR G 1 87  ? 17.377  -41.069 68.833  1.00 33.31  ? 88  THR G N     1 
ATOM   8274  C CA    . THR G 1 87  ? 18.280  -41.978 68.148  1.00 33.28  ? 88  THR G CA    1 
ATOM   8275  C C     . THR G 1 87  ? 19.428  -41.202 67.513  1.00 32.62  ? 88  THR G C     1 
ATOM   8276  O O     . THR G 1 87  ? 19.218  -40.167 66.884  1.00 34.81  ? 88  THR G O     1 
ATOM   8277  C CB    . THR G 1 87  ? 17.498  -42.767 67.099  1.00 33.71  ? 88  THR G CB    1 
ATOM   8278  O OG1   . THR G 1 87  ? 16.443  -43.405 67.812  1.00 30.61  ? 88  THR G OG1   1 
ATOM   8279  C CG2   . THR G 1 87  ? 18.359  -43.795 66.387  1.00 33.30  ? 88  THR G CG2   1 
ATOM   8280  N N     . VAL G 1 88  ? 20.641  -41.742 67.669  1.00 34.78  ? 89  VAL G N     1 
ATOM   8281  C CA    . VAL G 1 88  ? 21.830  -41.191 67.044  1.00 36.42  ? 89  VAL G CA    1 
ATOM   8282  C C     . VAL G 1 88  ? 22.449  -42.262 66.151  1.00 37.47  ? 89  VAL G C     1 
ATOM   8283  O O     . VAL G 1 88  ? 22.569  -43.418 66.551  1.00 42.57  ? 89  VAL G O     1 
ATOM   8284  C CB    . VAL G 1 88  ? 22.839  -40.692 68.097  1.00 40.40  ? 89  VAL G CB    1 
ATOM   8285  C CG1   . VAL G 1 88  ? 24.191  -40.357 67.477  1.00 40.89  ? 89  VAL G CG1   1 
ATOM   8286  C CG2   . VAL G 1 88  ? 22.297  -39.504 68.884  1.00 40.81  ? 89  VAL G CG2   1 
ATOM   8287  N N     . CYS G 1 89  ? 22.830  -41.864 64.933  1.00 41.19  ? 90  CYS G N     1 
ATOM   8288  C CA    . CYS G 1 89  ? 23.503  -42.757 64.005  1.00 44.50  ? 90  CYS G CA    1 
ATOM   8289  C C     . CYS G 1 89  ? 24.968  -42.345 63.881  1.00 42.14  ? 90  CYS G C     1 
ATOM   8290  O O     . CYS G 1 89  ? 25.277  -41.313 63.289  1.00 51.04  ? 90  CYS G O     1 
ATOM   8291  C CB    . CYS G 1 89  ? 22.822  -42.749 62.642  1.00 49.06  ? 90  CYS G CB    1 
ATOM   8292  S SG    . CYS G 1 89  ? 23.622  -43.831 61.428  1.00 55.77  ? 90  CYS G SG    1 
ATOM   8293  N N     . ALA G 1 90  ? 25.858  -43.163 64.451  1.00 36.23  ? 91  ALA G N     1 
ATOM   8294  C CA    . ALA G 1 90  ? 27.282  -42.871 64.456  1.00 34.60  ? 91  ALA G CA    1 
ATOM   8295  C C     . ALA G 1 90  ? 27.983  -43.672 63.361  1.00 34.38  ? 91  ALA G C     1 
ATOM   8296  O O     . ALA G 1 90  ? 28.197  -44.873 63.504  1.00 29.84  ? 91  ALA G O     1 
ATOM   8297  C CB    . ALA G 1 90  ? 27.866  -43.173 65.819  1.00 35.02  ? 91  ALA G CB    1 
ATOM   8298  N N     . LEU G 1 91  ? 28.333  -42.984 62.269  1.00 38.39  ? 92  LEU G N     1 
ATOM   8299  C CA    . LEU G 1 91  ? 29.078  -43.587 61.177  1.00 38.55  ? 92  LEU G CA    1 
ATOM   8300  C C     . LEU G 1 91  ? 30.499  -43.031 61.187  1.00 41.66  ? 92  LEU G C     1 
ATOM   8301  O O     . LEU G 1 91  ? 30.732  -41.922 61.666  1.00 36.34  ? 92  LEU G O     1 
ATOM   8302  C CB    . LEU G 1 91  ? 28.379  -43.313 59.847  1.00 39.94  ? 92  LEU G CB    1 
ATOM   8303  C CG    . LEU G 1 91  ? 26.909  -43.736 59.759  1.00 43.41  ? 92  LEU G CG    1 
ATOM   8304  C CD1   . LEU G 1 91  ? 26.404  -43.632 58.329  1.00 43.27  ? 92  LEU G CD1   1 
ATOM   8305  C CD2   . LEU G 1 91  ? 26.705  -45.141 60.301  1.00 42.53  ? 92  LEU G CD2   1 
ATOM   8306  N N     . TYR G 1 92  ? 31.443  -43.813 60.651  1.00 37.10  ? 93  TYR G N     1 
ATOM   8307  C CA    . TYR G 1 92  ? 32.840  -43.412 60.625  1.00 34.32  ? 93  TYR G CA    1 
ATOM   8308  C C     . TYR G 1 92  ? 33.022  -42.329 59.565  1.00 36.07  ? 93  TYR G C     1 
ATOM   8309  O O     . TYR G 1 92  ? 32.295  -42.294 58.574  1.00 30.01  ? 93  TYR G O     1 
ATOM   8310  C CB    . TYR G 1 92  ? 33.760  -44.610 60.364  1.00 37.89  ? 93  TYR G CB    1 
ATOM   8311  C CG    . TYR G 1 92  ? 33.757  -45.132 58.933  1.00 37.80  ? 93  TYR G CG    1 
ATOM   8312  C CD1   . TYR G 1 92  ? 34.543  -44.537 57.954  1.00 39.46  ? 93  TYR G CD1   1 
ATOM   8313  C CD2   . TYR G 1 92  ? 32.994  -46.234 58.569  1.00 37.89  ? 93  TYR G CD2   1 
ATOM   8314  C CE1   . TYR G 1 92  ? 34.554  -45.009 56.652  1.00 41.42  ? 93  TYR G CE1   1 
ATOM   8315  C CE2   . TYR G 1 92  ? 32.998  -46.717 57.271  1.00 39.94  ? 93  TYR G CE2   1 
ATOM   8316  C CZ    . TYR G 1 92  ? 33.781  -46.103 56.310  1.00 40.32  ? 93  TYR G CZ    1 
ATOM   8317  O OH    . TYR G 1 92  ? 33.792  -46.573 55.029  1.00 45.00  ? 93  TYR G OH    1 
ATOM   8318  N N     . GLY G 1 93  ? 34.002  -41.448 59.794  1.00 30.95  ? 94  GLY G N     1 
ATOM   8319  C CA    . GLY G 1 93  ? 34.266  -40.339 58.895  1.00 32.18  ? 94  GLY G CA    1 
ATOM   8320  C C     . GLY G 1 93  ? 33.110  -39.342 58.899  1.00 31.40  ? 94  GLY G C     1 
ATOM   8321  O O     . GLY G 1 93  ? 32.627  -38.949 59.958  1.00 29.75  ? 94  GLY G O     1 
ATOM   8322  N N     . HIS G 1 94  ? 32.682  -38.944 57.696  1.00 27.12  ? 95  HIS G N     1 
ATOM   8323  C CA    . HIS G 1 94  ? 31.565  -38.031 57.524  1.00 26.87  ? 95  HIS G CA    1 
ATOM   8324  C C     . HIS G 1 94  ? 30.325  -38.843 57.154  1.00 28.33  ? 95  HIS G C     1 
ATOM   8325  O O     . HIS G 1 94  ? 30.345  -39.607 56.192  1.00 27.76  ? 95  HIS G O     1 
ATOM   8326  C CB    . HIS G 1 94  ? 31.915  -36.965 56.480  1.00 23.14  ? 95  HIS G CB    1 
ATOM   8327  C CG    . HIS G 1 94  ? 30.855  -35.940 56.262  1.00 21.15  ? 95  HIS G CG    1 
ATOM   8328  N ND1   . HIS G 1 94  ? 29.507  -36.223 56.289  1.00 19.44  ? 95  HIS G ND1   1 
ATOM   8329  C CD2   . HIS G 1 94  ? 30.953  -34.634 55.982  1.00 19.03  ? 95  HIS G CD2   1 
ATOM   8330  C CE1   . HIS G 1 94  ? 28.824  -35.114 56.048  1.00 19.09  ? 95  HIS G CE1   1 
ATOM   8331  N NE2   . HIS G 1 94  ? 29.682  -34.138 55.857  1.00 19.73  ? 95  HIS G NE2   1 
ATOM   8332  N N     . PRO G 1 95  ? 29.204  -38.682 57.893  1.00 27.09  ? 96  PRO G N     1 
ATOM   8333  C CA    . PRO G 1 95  ? 28.059  -39.590 57.770  1.00 27.41  ? 96  PRO G CA    1 
ATOM   8334  C C     . PRO G 1 95  ? 27.352  -39.547 56.417  1.00 25.37  ? 96  PRO G C     1 
ATOM   8335  O O     . PRO G 1 95  ? 26.600  -40.460 56.083  1.00 27.50  ? 96  PRO G O     1 
ATOM   8336  C CB    . PRO G 1 95  ? 27.138  -39.122 58.916  1.00 27.82  ? 96  PRO G CB    1 
ATOM   8337  C CG    . PRO G 1 95  ? 27.479  -37.657 59.088  1.00 26.97  ? 96  PRO G CG    1 
ATOM   8338  C CD    . PRO G 1 95  ? 28.975  -37.596 58.858  1.00 27.70  ? 96  PRO G CD    1 
ATOM   8339  N N     . GLY G 1 96  ? 27.603  -38.484 55.647  1.00 22.35  ? 97  GLY G N     1 
ATOM   8340  C CA    . GLY G 1 96  ? 26.897  -38.268 54.395  1.00 26.48  ? 97  GLY G CA    1 
ATOM   8341  C C     . GLY G 1 96  ? 27.845  -38.243 53.199  1.00 23.98  ? 97  GLY G C     1 
ATOM   8342  O O     . GLY G 1 96  ? 27.477  -37.775 52.126  1.00 30.02  ? 97  GLY G O     1 
ATOM   8343  N N     . VAL G 1 97  ? 29.061  -38.764 53.392  1.00 24.46  ? 98  VAL G N     1 
ATOM   8344  C CA    . VAL G 1 97  ? 30.048  -38.814 52.326  1.00 27.31  ? 98  VAL G CA    1 
ATOM   8345  C C     . VAL G 1 97  ? 30.184  -40.258 51.851  1.00 28.70  ? 98  VAL G C     1 
ATOM   8346  O O     . VAL G 1 97  ? 30.661  -41.118 52.587  1.00 24.10  ? 98  VAL G O     1 
ATOM   8347  C CB    . VAL G 1 97  ? 31.401  -38.235 52.782  1.00 27.19  ? 98  VAL G CB    1 
ATOM   8348  C CG1   . VAL G 1 97  ? 32.511  -38.523 51.779  1.00 30.49  ? 98  VAL G CG1   1 
ATOM   8349  C CG2   . VAL G 1 97  ? 31.306  -36.739 53.063  1.00 24.15  ? 98  VAL G CG2   1 
ATOM   8350  N N     . PHE G 1 98  ? 29.747  -40.507 50.611  1.00 32.08  ? 99  PHE G N     1 
ATOM   8351  C CA    . PHE G 1 98  ? 29.738  -41.848 50.051  1.00 31.95  ? 99  PHE G CA    1 
ATOM   8352  C C     . PHE G 1 98  ? 29.084  -42.798 51.051  1.00 32.42  ? 99  PHE G C     1 
ATOM   8353  O O     . PHE G 1 98  ? 29.597  -43.883 51.316  1.00 32.57  ? 99  PHE G O     1 
ATOM   8354  C CB    . PHE G 1 98  ? 31.164  -42.266 49.679  1.00 34.23  ? 99  PHE G CB    1 
ATOM   8355  C CG    . PHE G 1 98  ? 31.701  -41.585 48.427  1.00 35.39  ? 99  PHE G CG    1 
ATOM   8356  C CD1   . PHE G 1 98  ? 32.244  -40.306 48.485  1.00 33.92  ? 99  PHE G CD1   1 
ATOM   8357  C CD2   . PHE G 1 98  ? 31.659  -42.227 47.193  1.00 36.92  ? 99  PHE G CD2   1 
ATOM   8358  C CE1   . PHE G 1 98  ? 32.726  -39.689 47.341  1.00 36.39  ? 99  PHE G CE1   1 
ATOM   8359  C CE2   . PHE G 1 98  ? 32.145  -41.605 46.054  1.00 33.96  ? 99  PHE G CE2   1 
ATOM   8360  C CZ    . PHE G 1 98  ? 32.675  -40.339 46.130  1.00 33.23  ? 99  PHE G CZ    1 
ATOM   8361  N N     . ALA G 1 99  ? 27.947  -42.361 51.600  1.00 36.77  ? 100 ALA G N     1 
ATOM   8362  C CA    . ALA G 1 99  ? 27.158  -43.165 52.518  1.00 32.84  ? 100 ALA G CA    1 
ATOM   8363  C C     . ALA G 1 99  ? 25.686  -42.800 52.355  1.00 33.67  ? 100 ALA G C     1 
ATOM   8364  O O     . ALA G 1 99  ? 25.300  -41.652 52.567  1.00 38.44  ? 100 ALA G O     1 
ATOM   8365  C CB    . ALA G 1 99  ? 27.635  -42.951 53.938  1.00 32.00  ? 100 ALA G CB    1 
ATOM   8366  N N     . CYS G 1 100 ? 24.875  -43.790 51.969  1.00 32.33  ? 101 CYS G N     1 
ATOM   8367  C CA    . CYS G 1 100 ? 23.487  -43.554 51.608  1.00 33.25  ? 101 CYS G CA    1 
ATOM   8368  C C     . CYS G 1 100 ? 22.578  -43.756 52.818  1.00 32.94  ? 101 CYS G C     1 
ATOM   8369  O O     . CYS G 1 100 ? 21.488  -43.191 52.878  1.00 36.18  ? 101 CYS G O     1 
ATOM   8370  C CB    . CYS G 1 100 ? 23.065  -44.468 50.463  1.00 35.74  ? 101 CYS G CB    1 
ATOM   8371  S SG    . CYS G 1 100 ? 23.357  -46.224 50.798  1.00 36.59  ? 101 CYS G SG    1 
ATOM   8372  N N     . VAL G 1 101 ? 23.041  -44.563 53.778  1.00 31.85  ? 102 VAL G N     1 
ATOM   8373  C CA    . VAL G 1 101 ? 22.231  -44.943 54.924  1.00 31.02  ? 102 VAL G CA    1 
ATOM   8374  C C     . VAL G 1 101 ? 21.669  -43.687 55.588  1.00 27.93  ? 102 VAL G C     1 
ATOM   8375  O O     . VAL G 1 101 ? 20.455  -43.527 55.692  1.00 25.11  ? 102 VAL G O     1 
ATOM   8376  C CB    . VAL G 1 101 ? 23.035  -45.793 55.928  1.00 32.21  ? 102 VAL G CB    1 
ATOM   8377  C CG1   . VAL G 1 101 ? 22.262  -46.026 57.220  1.00 33.23  ? 102 VAL G CG1   1 
ATOM   8378  C CG2   . VAL G 1 101 ? 23.476  -47.119 55.320  1.00 32.26  ? 102 VAL G CG2   1 
ATOM   8379  N N     . SER G 1 102 ? 22.567  -42.802 56.032  1.00 27.90  ? 103 SER G N     1 
ATOM   8380  C CA    . SER G 1 102 ? 22.181  -41.623 56.790  1.00 27.96  ? 103 SER G CA    1 
ATOM   8381  C C     . SER G 1 102 ? 21.200  -40.769 55.990  1.00 23.45  ? 103 SER G C     1 
ATOM   8382  O O     . SER G 1 102 ? 20.153  -40.382 56.502  1.00 25.95  ? 103 SER G O     1 
ATOM   8383  C CB    . SER G 1 102 ? 23.390  -40.825 57.205  1.00 33.55  ? 103 SER G CB    1 
ATOM   8384  O OG    . SER G 1 102 ? 24.192  -41.560 58.118  1.00 41.07  ? 103 SER G OG    1 
ATOM   8385  N N     . HIS G 1 103 ? 21.550  -40.476 54.734  1.00 22.52  ? 104 HIS G N     1 
ATOM   8386  C CA    . HIS G 1 103 ? 20.701  -39.661 53.881  1.00 21.23  ? 104 HIS G CA    1 
ATOM   8387  C C     . HIS G 1 103 ? 19.330  -40.320 53.745  1.00 22.43  ? 104 HIS G C     1 
ATOM   8388  O O     . HIS G 1 103 ? 18.304  -39.648 53.822  1.00 22.09  ? 104 HIS G O     1 
ATOM   8389  C CB    . HIS G 1 103 ? 21.364  -39.412 52.521  1.00 21.16  ? 104 HIS G CB    1 
ATOM   8390  C CG    . HIS G 1 103 ? 22.487  -38.427 52.567  1.00 20.49  ? 104 HIS G CG    1 
ATOM   8391  N ND1   . HIS G 1 103 ? 23.816  -38.790 52.537  1.00 21.62  ? 104 HIS G ND1   1 
ATOM   8392  C CD2   . HIS G 1 103 ? 22.470  -37.089 52.609  1.00 19.04  ? 104 HIS G CD2   1 
ATOM   8393  C CE1   . HIS G 1 103 ? 24.567  -37.699 52.581  1.00 23.43  ? 104 HIS G CE1   1 
ATOM   8394  N NE2   . HIS G 1 103 ? 23.769  -36.655 52.628  1.00 20.36  ? 104 HIS G NE2   1 
ATOM   8395  N N     . MET G 1 104 ? 19.326  -41.641 53.542  1.00 24.24  ? 105 MET G N     1 
ATOM   8396  C CA    . MET G 1 104 ? 18.087  -42.385 53.383  1.00 27.54  ? 105 MET G CA    1 
ATOM   8397  C C     . MET G 1 104 ? 17.274  -42.300 54.673  1.00 27.52  ? 105 MET G C     1 
ATOM   8398  O O     . MET G 1 104 ? 16.068  -42.069 54.634  1.00 28.42  ? 105 MET G O     1 
ATOM   8399  C CB    . MET G 1 104 ? 18.365  -43.852 53.031  1.00 29.98  ? 105 MET G CB    1 
ATOM   8400  C CG    . MET G 1 104 ? 18.879  -44.058 51.618  1.00 36.29  ? 105 MET G CG    1 
ATOM   8401  S SD    . MET G 1 104 ? 19.326  -45.770 51.264  1.00 48.53  ? 105 MET G SD    1 
ATOM   8402  C CE    . MET G 1 104 ? 17.727  -46.589 51.356  1.00 49.04  ? 105 MET G CE    1 
ATOM   8403  N N     . ALA G 1 105 ? 17.953  -42.475 55.812  1.00 27.89  ? 106 ALA G N     1 
ATOM   8404  C CA    . ALA G 1 105 ? 17.294  -42.482 57.108  1.00 27.01  ? 106 ALA G CA    1 
ATOM   8405  C C     . ALA G 1 105 ? 16.662  -41.119 57.379  1.00 26.30  ? 106 ALA G C     1 
ATOM   8406  O O     . ALA G 1 105 ? 15.503  -41.038 57.776  1.00 24.79  ? 106 ALA G O     1 
ATOM   8407  C CB    . ALA G 1 105 ? 18.284  -42.859 58.188  1.00 27.67  ? 106 ALA G CB    1 
ATOM   8408  N N     . ILE G 1 106 ? 17.439  -40.054 57.155  1.00 28.22  ? 107 ILE G N     1 
ATOM   8409  C CA    . ILE G 1 106 ? 16.982  -38.699 57.415  1.00 29.39  ? 107 ILE G CA    1 
ATOM   8410  C C     . ILE G 1 106 ? 15.791  -38.387 56.512  1.00 31.89  ? 107 ILE G C     1 
ATOM   8411  O O     . ILE G 1 106 ? 14.801  -37.813 56.963  1.00 31.69  ? 107 ILE G O     1 
ATOM   8412  C CB    . ILE G 1 106 ? 18.124  -37.684 57.224  1.00 29.03  ? 107 ILE G CB    1 
ATOM   8413  C CG1   . ILE G 1 106 ? 19.216  -37.860 58.281  1.00 30.89  ? 107 ILE G CG1   1 
ATOM   8414  C CG2   . ILE G 1 106 ? 17.584  -36.254 57.207  1.00 28.84  ? 107 ILE G CG2   1 
ATOM   8415  C CD1   . ILE G 1 106 ? 20.345  -36.850 58.181  1.00 30.02  ? 107 ILE G CD1   1 
ATOM   8416  N N     . THR G 1 107 ? 15.899  -38.767 55.235  1.00 30.93  ? 108 THR G N     1 
ATOM   8417  C CA    . THR G 1 107 ? 14.855  -38.488 54.263  1.00 35.05  ? 108 THR G CA    1 
ATOM   8418  C C     . THR G 1 107 ? 13.555  -39.149 54.713  1.00 35.39  ? 108 THR G C     1 
ATOM   8419  O O     . THR G 1 107 ? 12.498  -38.521 54.703  1.00 37.17  ? 108 THR G O     1 
ATOM   8420  C CB    . THR G 1 107 ? 15.279  -38.985 52.882  1.00 36.76  ? 108 THR G CB    1 
ATOM   8421  O OG1   . THR G 1 107 ? 16.394  -38.181 52.510  1.00 38.39  ? 108 THR G OG1   1 
ATOM   8422  C CG2   . THR G 1 107 ? 14.173  -38.844 51.852  1.00 38.75  ? 108 THR G CG2   1 
ATOM   8423  N N     . ARG G 1 108 ? 13.649  -40.424 55.100  1.00 36.03  ? 109 ARG G N     1 
ATOM   8424  C CA    . ARG G 1 108 ? 12.480  -41.208 55.462  1.00 36.49  ? 109 ARG G CA    1 
ATOM   8425  C C     . ARG G 1 108 ? 11.914  -40.701 56.786  1.00 33.97  ? 109 ARG G C     1 
ATOM   8426  O O     . ARG G 1 108 ? 10.705  -40.741 57.004  1.00 35.28  ? 109 ARG G O     1 
ATOM   8427  C CB    . ARG G 1 108 ? 12.844  -42.694 55.544  1.00 37.01  ? 109 ARG G CB    1 
ATOM   8428  C CG    . ARG G 1 108 ? 11.644  -43.617 55.701  1.00 38.80  ? 109 ARG G CG    1 
ATOM   8429  C CD    . ARG G 1 108 ? 12.038  -45.082 55.632  1.00 40.49  ? 109 ARG G CD    1 
ATOM   8430  N NE    . ARG G 1 108 ? 12.749  -45.396 54.388  1.00 40.01  ? 109 ARG G NE    1 
ATOM   8431  C CZ    . ARG G 1 108 ? 13.173  -46.606 54.047  1.00 42.48  ? 109 ARG G CZ    1 
ATOM   8432  N NH1   . ARG G 1 108 ? 12.943  -47.636 54.843  1.00 39.93  ? 109 ARG G NH1   1 
ATOM   8433  N NH2   . ARG G 1 108 ? 13.817  -46.782 52.907  1.00 39.86  ? 109 ARG G NH2   1 
ATOM   8434  N N     . ALA G 1 109 ? 12.805  -40.225 57.663  1.00 32.64  ? 110 ALA G N     1 
ATOM   8435  C CA    . ALA G 1 109 ? 12.407  -39.718 58.967  1.00 34.81  ? 110 ALA G CA    1 
ATOM   8436  C C     . ALA G 1 109 ? 11.522  -38.486 58.796  1.00 34.84  ? 110 ALA G C     1 
ATOM   8437  O O     . ALA G 1 109 ? 10.470  -38.381 59.422  1.00 41.40  ? 110 ALA G O     1 
ATOM   8438  C CB    . ALA G 1 109 ? 13.634  -39.408 59.797  1.00 34.36  ? 110 ALA G CB    1 
ATOM   8439  N N     . LYS G 1 110 ? 11.963  -37.559 57.938  1.00 38.49  ? 111 LYS G N     1 
ATOM   8440  C CA    . LYS G 1 110 ? 11.235  -36.325 57.694  1.00 40.81  ? 111 LYS G CA    1 
ATOM   8441  C C     . LYS G 1 110 ? 9.877   -36.646 57.075  1.00 43.25  ? 111 LYS G C     1 
ATOM   8442  O O     . LYS G 1 110 ? 8.873   -36.024 57.414  1.00 44.00  ? 111 LYS G O     1 
ATOM   8443  C CB    . LYS G 1 110 ? 12.033  -35.393 56.775  1.00 43.05  ? 111 LYS G CB    1 
ATOM   8444  C CG    . LYS G 1 110 ? 13.318  -34.836 57.371  1.00 45.95  ? 111 LYS G CG    1 
ATOM   8445  C CD    . LYS G 1 110 ? 14.054  -33.870 56.450  1.00 47.63  ? 111 LYS G CD    1 
ATOM   8446  C CE    . LYS G 1 110 ? 15.294  -33.313 57.072  1.00 50.33  ? 111 LYS G CE    1 
ATOM   8447  N NZ    . LYS G 1 110 ? 14.999  -32.581 58.307  1.00 54.42  ? 111 LYS G NZ    1 
ATOM   8448  N N     . ALA G 1 111 ? 9.866   -37.624 56.162  1.00 43.71  ? 112 ALA G N     1 
ATOM   8449  C CA    . ALA G 1 111 ? 8.658   -37.999 55.446  1.00 43.83  ? 112 ALA G CA    1 
ATOM   8450  C C     . ALA G 1 111 ? 7.599   -38.497 56.427  1.00 42.86  ? 112 ALA G C     1 
ATOM   8451  O O     . ALA G 1 111 ? 6.405   -38.350 56.181  1.00 41.86  ? 112 ALA G O     1 
ATOM   8452  C CB    . ALA G 1 111 ? 8.981   -39.046 54.404  1.00 43.87  ? 112 ALA G CB    1 
ATOM   8453  N N     . GLU G 1 112 ? 8.053   -39.090 57.536  1.00 44.40  ? 113 GLU G N     1 
ATOM   8454  C CA    . GLU G 1 112 ? 7.153   -39.632 58.540  1.00 46.22  ? 113 GLU G CA    1 
ATOM   8455  C C     . GLU G 1 112 ? 6.930   -38.593 59.637  1.00 48.87  ? 113 GLU G C     1 
ATOM   8456  O O     . GLU G 1 112 ? 6.324   -38.887 60.664  1.00 50.43  ? 113 GLU G O     1 
ATOM   8457  C CB    . GLU G 1 112 ? 7.707   -40.945 59.094  1.00 47.14  ? 113 GLU G CB    1 
ATOM   8458  C CG    . GLU G 1 112 ? 7.904   -42.011 58.019  1.00 47.10  ? 113 GLU G CG    1 
ATOM   8459  C CD    . GLU G 1 112 ? 8.412   -43.344 58.536  1.00 50.49  ? 113 GLU G CD    1 
ATOM   8460  O OE1   . GLU G 1 112 ? 8.539   -43.495 59.769  1.00 56.05  ? 113 GLU G OE1   1 
ATOM   8461  O OE2   . GLU G 1 112 ? 8.690   -44.230 57.701  1.00 49.27  ? 113 GLU G OE2   1 
ATOM   8462  N N     . GLY G 1 113 ? 7.435   -37.377 59.400  1.00 49.24  ? 114 GLY G N     1 
ATOM   8463  C CA    . GLY G 1 113 ? 7.170   -36.243 60.270  1.00 50.10  ? 114 GLY G CA    1 
ATOM   8464  C C     . GLY G 1 113 ? 7.995   -36.299 61.553  1.00 47.28  ? 114 GLY G C     1 
ATOM   8465  O O     . GLY G 1 113 ? 7.546   -35.840 62.600  1.00 52.31  ? 114 GLY G O     1 
ATOM   8466  N N     . PHE G 1 114 ? 9.206   -36.857 61.458  1.00 44.58  ? 115 PHE G N     1 
ATOM   8467  C CA    . PHE G 1 114 ? 10.117  -36.893 62.590  1.00 44.10  ? 115 PHE G CA    1 
ATOM   8468  C C     . PHE G 1 114 ? 11.211  -35.852 62.381  1.00 43.27  ? 115 PHE G C     1 
ATOM   8469  O O     . PHE G 1 114 ? 11.502  -35.465 61.251  1.00 46.96  ? 115 PHE G O     1 
ATOM   8470  C CB    . PHE G 1 114 ? 10.736  -38.280 62.788  1.00 44.09  ? 115 PHE G CB    1 
ATOM   8471  C CG    . PHE G 1 114 ? 9.755   -39.354 63.235  1.00 44.47  ? 115 PHE G CG    1 
ATOM   8472  C CD1   . PHE G 1 114 ? 9.233   -39.347 64.524  1.00 46.16  ? 115 PHE G CD1   1 
ATOM   8473  C CD2   . PHE G 1 114 ? 9.385   -40.386 62.380  1.00 43.48  ? 115 PHE G CD2   1 
ATOM   8474  C CE1   . PHE G 1 114 ? 8.343   -40.328 64.932  1.00 43.41  ? 115 PHE G CE1   1 
ATOM   8475  C CE2   . PHE G 1 114 ? 8.499   -41.366 62.796  1.00 41.72  ? 115 PHE G CE2   1 
ATOM   8476  C CZ    . PHE G 1 114 ? 7.981   -41.336 64.069  1.00 41.30  ? 115 PHE G CZ    1 
ATOM   8477  N N     . SER G 1 115 ? 11.800  -35.402 63.491  1.00 38.04  ? 116 SER G N     1 
ATOM   8478  C CA    . SER G 1 115 ? 12.946  -34.513 63.447  1.00 40.20  ? 116 SER G CA    1 
ATOM   8479  C C     . SER G 1 115 ? 14.200  -35.327 63.143  1.00 38.06  ? 116 SER G C     1 
ATOM   8480  O O     . SER G 1 115 ? 14.482  -36.315 63.817  1.00 30.70  ? 116 SER G O     1 
ATOM   8481  C CB    . SER G 1 115 ? 13.090  -33.744 64.735  1.00 43.15  ? 116 SER G CB    1 
ATOM   8482  O OG    . SER G 1 115 ? 14.189  -32.845 64.671  1.00 45.23  ? 116 SER G OG    1 
ATOM   8483  N N     . ALA G 1 116 ? 14.936  -34.905 62.112  1.00 36.84  ? 117 ALA G N     1 
ATOM   8484  C CA    . ALA G 1 116 ? 16.147  -35.594 61.703  1.00 34.97  ? 117 ALA G CA    1 
ATOM   8485  C C     . ALA G 1 116 ? 17.105  -34.604 61.050  1.00 35.87  ? 117 ALA G C     1 
ATOM   8486  O O     . ALA G 1 116 ? 16.703  -33.806 60.206  1.00 35.45  ? 117 ALA G O     1 
ATOM   8487  C CB    . ALA G 1 116 ? 15.805  -36.731 60.766  1.00 34.59  ? 117 ALA G CB    1 
ATOM   8488  N N     . LYS G 1 117 ? 18.375  -34.668 61.458  1.00 32.05  ? 118 LYS G N     1 
ATOM   8489  C CA    . LYS G 1 117 ? 19.405  -33.825 60.881  1.00 36.71  ? 118 LYS G CA    1 
ATOM   8490  C C     . LYS G 1 117 ? 20.701  -34.621 60.773  1.00 31.42  ? 118 LYS G C     1 
ATOM   8491  O O     . LYS G 1 117 ? 20.798  -35.740 61.273  1.00 31.51  ? 118 LYS G O     1 
ATOM   8492  C CB    . LYS G 1 117 ? 19.603  -32.552 61.713  1.00 39.84  ? 118 LYS G CB    1 
ATOM   8493  C CG    . LYS G 1 117 ? 20.078  -32.770 63.142  1.00 42.53  ? 118 LYS G CG    1 
ATOM   8494  C CD    . LYS G 1 117 ? 20.357  -31.473 63.892  1.00 48.90  ? 118 LYS G CD    1 
ATOM   8495  C CE    . LYS G 1 117 ? 20.870  -31.701 65.279  1.00 52.14  ? 118 LYS G CE    1 
ATOM   8496  N NZ    . LYS G 1 117 ? 21.163  -30.437 65.958  1.00 52.34  ? 118 LYS G NZ    1 
ATOM   8497  N N     . MET G 1 118 ? 21.684  -34.028 60.098  1.00 29.00  ? 119 MET G N     1 
ATOM   8498  C CA    . MET G 1 118 ? 22.982  -34.649 59.920  1.00 29.62  ? 119 MET G CA    1 
ATOM   8499  C C     . MET G 1 118 ? 24.065  -33.653 60.305  1.00 33.80  ? 119 MET G C     1 
ATOM   8500  O O     . MET G 1 118 ? 24.123  -32.551 59.765  1.00 29.39  ? 119 MET G O     1 
ATOM   8501  C CB    . MET G 1 118 ? 23.197  -35.073 58.465  1.00 27.92  ? 119 MET G CB    1 
ATOM   8502  C CG    . MET G 1 118 ? 24.607  -35.539 58.163  1.00 29.44  ? 119 MET G CG    1 
ATOM   8503  S SD    . MET G 1 118 ? 24.836  -35.919 56.415  1.00 35.71  ? 119 MET G SD    1 
ATOM   8504  C CE    . MET G 1 118 ? 23.546  -37.152 56.193  1.00 35.72  ? 119 MET G CE    1 
ATOM   8505  N N     . GLU G 1 119 ? 24.912  -34.056 61.250  1.00 36.26  ? 120 GLU G N     1 
ATOM   8506  C CA    . GLU G 1 119 ? 26.079  -33.275 61.601  1.00 35.01  ? 120 GLU G CA    1 
ATOM   8507  C C     . GLU G 1 119 ? 27.239  -33.719 60.718  1.00 34.53  ? 120 GLU G C     1 
ATOM   8508  O O     . GLU G 1 119 ? 27.416  -34.908 60.464  1.00 37.05  ? 120 GLU G O     1 
ATOM   8509  C CB    . GLU G 1 119 ? 26.395  -33.458 63.082  1.00 38.13  ? 120 GLU G CB    1 
ATOM   8510  C CG    . GLU G 1 119 ? 25.220  -33.108 63.991  1.00 44.88  ? 120 GLU G CG    1 
ATOM   8511  C CD    . GLU G 1 119 ? 24.788  -31.656 63.898  1.00 51.25  ? 120 GLU G CD    1 
ATOM   8512  O OE1   . GLU G 1 119 ? 25.647  -30.774 64.107  1.00 51.22  ? 120 GLU G OE1   1 
ATOM   8513  O OE2   . GLU G 1 119 ? 23.595  -31.407 63.620  1.00 63.27  ? 120 GLU G OE2   1 
ATOM   8514  N N     . PRO G 1 120 ? 28.045  -32.769 60.201  1.00 30.09  ? 121 PRO G N     1 
ATOM   8515  C CA    . PRO G 1 120 ? 29.213  -33.112 59.390  1.00 32.01  ? 121 PRO G CA    1 
ATOM   8516  C C     . PRO G 1 120 ? 30.358  -33.685 60.223  1.00 33.76  ? 121 PRO G C     1 
ATOM   8517  O O     . PRO G 1 120 ? 30.527  -33.327 61.386  1.00 32.36  ? 121 PRO G O     1 
ATOM   8518  C CB    . PRO G 1 120 ? 29.576  -31.769 58.733  1.00 33.03  ? 121 PRO G CB    1 
ATOM   8519  C CG    . PRO G 1 120 ? 29.091  -30.727 59.724  1.00 33.22  ? 121 PRO G CG    1 
ATOM   8520  C CD    . PRO G 1 120 ? 27.839  -31.321 60.341  1.00 30.74  ? 121 PRO G CD    1 
ATOM   8521  N N     . GLY G 1 121 ? 31.128  -34.588 59.609  1.00 35.90  ? 122 GLY G N     1 
ATOM   8522  C CA    . GLY G 1 121 ? 32.289  -35.184 60.247  1.00 30.21  ? 122 GLY G CA    1 
ATOM   8523  C C     . GLY G 1 121 ? 33.509  -35.111 59.334  1.00 27.75  ? 122 GLY G C     1 
ATOM   8524  O O     . GLY G 1 121 ? 33.429  -34.586 58.227  1.00 27.25  ? 122 GLY G O     1 
ATOM   8525  N N     . ILE G 1 122 ? 34.635  -35.647 59.813  1.00 25.90  ? 123 ILE G N     1 
ATOM   8526  C CA    . ILE G 1 122 ? 35.876  -35.626 59.058  1.00 28.33  ? 123 ILE G CA    1 
ATOM   8527  C C     . ILE G 1 122 ? 35.955  -36.892 58.208  1.00 27.69  ? 123 ILE G C     1 
ATOM   8528  O O     . ILE G 1 122 ? 36.029  -37.998 58.738  1.00 28.00  ? 123 ILE G O     1 
ATOM   8529  C CB    . ILE G 1 122 ? 37.083  -35.483 60.003  1.00 30.38  ? 123 ILE G CB    1 
ATOM   8530  C CG1   . ILE G 1 122 ? 36.964  -34.224 60.867  1.00 31.02  ? 123 ILE G CG1   1 
ATOM   8531  C CG2   . ILE G 1 122 ? 38.397  -35.514 59.221  1.00 30.39  ? 123 ILE G CG2   1 
ATOM   8532  C CD1   . ILE G 1 122 ? 38.049  -34.084 61.919  1.00 32.12  ? 123 ILE G CD1   1 
ATOM   8533  N N     . SER G 1 123 ? 35.929  -36.706 56.883  1.00 24.89  ? 124 SER G N     1 
ATOM   8534  C CA    . SER G 1 123 ? 35.913  -37.817 55.947  1.00 24.35  ? 124 SER G CA    1 
ATOM   8535  C C     . SER G 1 123 ? 37.338  -38.191 55.550  1.00 26.56  ? 124 SER G C     1 
ATOM   8536  O O     . SER G 1 123 ? 38.278  -37.435 55.791  1.00 25.60  ? 124 SER G O     1 
ATOM   8537  C CB    . SER G 1 123 ? 35.075  -37.491 54.736  1.00 25.00  ? 124 SER G CB    1 
ATOM   8538  O OG    . SER G 1 123 ? 35.594  -36.367 54.038  1.00 27.41  ? 124 SER G OG    1 
ATOM   8539  N N     . ALA G 1 124 ? 37.478  -39.373 54.941  1.00 26.43  ? 125 ALA G N     1 
ATOM   8540  C CA    . ALA G 1 124 ? 38.766  -39.858 54.475  1.00 29.51  ? 125 ALA G CA    1 
ATOM   8541  C C     . ALA G 1 124 ? 39.395  -38.829 53.540  1.00 31.02  ? 125 ALA G C     1 
ATOM   8542  O O     . ALA G 1 124 ? 40.616  -38.742 53.435  1.00 28.75  ? 125 ALA G O     1 
ATOM   8543  C CB    . ALA G 1 124 ? 38.594  -41.197 53.791  1.00 29.11  ? 125 ALA G CB    1 
ATOM   8544  N N     . GLU G 1 125 ? 38.540  -38.057 52.862  1.00 35.54  ? 126 GLU G N     1 
ATOM   8545  C CA    . GLU G 1 125 ? 38.990  -37.016 51.954  1.00 37.91  ? 126 GLU G CA    1 
ATOM   8546  C C     . GLU G 1 125 ? 39.713  -35.930 52.747  1.00 34.09  ? 126 GLU G C     1 
ATOM   8547  O O     . GLU G 1 125 ? 40.767  -35.450 52.335  1.00 28.93  ? 126 GLU G O     1 
ATOM   8548  C CB    . GLU G 1 125 ? 37.798  -36.444 51.186  1.00 40.60  ? 126 GLU G CB    1 
ATOM   8549  C CG    . GLU G 1 125 ? 38.163  -35.269 50.284  1.00 42.68  ? 126 GLU G CG    1 
ATOM   8550  C CD    . GLU G 1 125 ? 36.998  -34.732 49.474  1.00 47.29  ? 126 GLU G CD    1 
ATOM   8551  O OE1   . GLU G 1 125 ? 36.421  -35.509 48.685  1.00 59.46  ? 126 GLU G OE1   1 
ATOM   8552  O OE2   . GLU G 1 125 ? 36.668  -33.538 49.632  1.00 56.36  ? 126 GLU G OE2   1 
ATOM   8553  N N     . ALA G 1 126 ? 39.134  -35.558 53.893  1.00 34.81  ? 127 ALA G N     1 
ATOM   8554  C CA    . ALA G 1 126 ? 39.685  -34.505 54.731  1.00 32.08  ? 127 ALA G CA    1 
ATOM   8555  C C     . ALA G 1 126 ? 41.040  -34.933 55.289  1.00 26.96  ? 127 ALA G C     1 
ATOM   8556  O O     . ALA G 1 126 ? 41.892  -34.093 55.564  1.00 26.88  ? 127 ALA G O     1 
ATOM   8557  C CB    . ALA G 1 126 ? 38.715  -34.167 55.841  1.00 29.27  ? 127 ALA G CB    1 
ATOM   8558  N N     . CYS G 1 127 ? 41.219  -36.247 55.462  1.00 25.26  ? 128 CYS G N     1 
ATOM   8559  C CA    . CYS G 1 127 ? 42.455  -36.792 56.001  1.00 28.46  ? 128 CYS G CA    1 
ATOM   8560  C C     . CYS G 1 127 ? 43.537  -36.792 54.924  1.00 29.92  ? 128 CYS G C     1 
ATOM   8561  O O     . CYS G 1 127 ? 44.712  -36.579 55.216  1.00 26.62  ? 128 CYS G O     1 
ATOM   8562  C CB    . CYS G 1 127 ? 42.246  -38.205 56.533  1.00 30.15  ? 128 CYS G CB    1 
ATOM   8563  S SG    . CYS G 1 127 ? 41.135  -38.282 57.961  1.00 32.60  ? 128 CYS G SG    1 
ATOM   8564  N N     . LEU G 1 128 ? 43.118  -37.035 53.679  1.00 30.19  ? 129 LEU G N     1 
ATOM   8565  C CA    . LEU G 1 128 ? 44.033  -37.125 52.555  1.00 29.60  ? 129 LEU G CA    1 
ATOM   8566  C C     . LEU G 1 128 ? 44.744  -35.789 52.365  1.00 28.35  ? 129 LEU G C     1 
ATOM   8567  O O     . LEU G 1 128 ? 45.970  -35.738 52.310  1.00 24.46  ? 129 LEU G O     1 
ATOM   8568  C CB    . LEU G 1 128 ? 43.245  -37.539 51.313  1.00 30.81  ? 129 LEU G CB    1 
ATOM   8569  C CG    . LEU G 1 128 ? 44.059  -37.769 50.036  1.00 31.99  ? 129 LEU G CG    1 
ATOM   8570  C CD1   . LEU G 1 128 ? 43.349  -38.761 49.132  1.00 34.03  ? 129 LEU G CD1   1 
ATOM   8571  C CD2   . LEU G 1 128 ? 44.309  -36.468 49.295  1.00 33.90  ? 129 LEU G CD2   1 
ATOM   8572  N N     . TRP G 1 129 ? 43.958  -34.711 52.278  1.00 29.82  ? 130 TRP G N     1 
ATOM   8573  C CA    . TRP G 1 129 ? 44.502  -33.377 52.085  1.00 29.61  ? 130 TRP G CA    1 
ATOM   8574  C C     . TRP G 1 129 ? 45.585  -33.104 53.126  1.00 26.45  ? 130 TRP G C     1 
ATOM   8575  O O     . TRP G 1 129 ? 46.614  -32.508 52.815  1.00 29.40  ? 130 TRP G O     1 
ATOM   8576  C CB    . TRP G 1 129 ? 43.388  -32.323 52.170  1.00 30.16  ? 130 TRP G CB    1 
ATOM   8577  C CG    . TRP G 1 129 ? 42.257  -32.515 51.193  1.00 32.81  ? 130 TRP G CG    1 
ATOM   8578  C CD1   . TRP G 1 129 ? 40.930  -32.344 51.456  1.00 33.16  ? 130 TRP G CD1   1 
ATOM   8579  C CD2   . TRP G 1 129 ? 42.344  -32.870 49.793  1.00 32.51  ? 130 TRP G CD2   1 
ATOM   8580  N NE1   . TRP G 1 129 ? 40.185  -32.590 50.335  1.00 35.90  ? 130 TRP G NE1   1 
ATOM   8581  C CE2   . TRP G 1 129 ? 41.021  -32.909 49.299  1.00 33.60  ? 130 TRP G CE2   1 
ATOM   8582  C CE3   . TRP G 1 129 ? 43.396  -33.164 48.918  1.00 32.61  ? 130 TRP G CE3   1 
ATOM   8583  C CZ2   . TRP G 1 129 ? 40.730  -33.227 47.974  1.00 33.34  ? 130 TRP G CZ2   1 
ATOM   8584  C CZ3   . TRP G 1 129 ? 43.105  -33.476 47.608  1.00 33.32  ? 130 TRP G CZ3   1 
ATOM   8585  C CH2   . TRP G 1 129 ? 41.791  -33.504 47.144  1.00 31.62  ? 130 TRP G CH2   1 
ATOM   8586  N N     . ALA G 1 130 ? 45.340  -33.556 54.362  1.00 26.74  ? 131 ALA G N     1 
ATOM   8587  C CA    . ALA G 1 130 ? 46.215  -33.266 55.486  1.00 25.73  ? 131 ALA G CA    1 
ATOM   8588  C C     . ALA G 1 130 ? 47.446  -34.170 55.455  1.00 26.89  ? 131 ALA G C     1 
ATOM   8589  O O     . ALA G 1 130 ? 48.550  -33.726 55.759  1.00 28.26  ? 131 ALA G O     1 
ATOM   8590  C CB    . ALA G 1 130 ? 45.448  -33.424 56.784  1.00 26.10  ? 131 ALA G CB    1 
ATOM   8591  N N     . ASP G 1 131 ? 47.239  -35.440 55.090  1.00 27.72  ? 132 ASP G N     1 
ATOM   8592  C CA    . ASP G 1 131 ? 48.297  -36.439 55.131  1.00 27.31  ? 132 ASP G CA    1 
ATOM   8593  C C     . ASP G 1 131 ? 49.272  -36.225 53.976  1.00 27.75  ? 132 ASP G C     1 
ATOM   8594  O O     . ASP G 1 131 ? 50.482  -36.356 54.150  1.00 29.87  ? 132 ASP G O     1 
ATOM   8595  C CB    . ASP G 1 131 ? 47.725  -37.848 55.133  1.00 28.40  ? 132 ASP G CB    1 
ATOM   8596  C CG    . ASP G 1 131 ? 47.297  -38.370 56.497  1.00 29.04  ? 132 ASP G CG    1 
ATOM   8597  O OD1   . ASP G 1 131 ? 47.691  -37.750 57.508  1.00 29.63  ? 132 ASP G OD1   1 
ATOM   8598  O OD2   . ASP G 1 131 ? 46.569  -39.384 56.537  1.00 29.18  ? 132 ASP G OD2   1 
ATOM   8599  N N     . LEU G 1 132 ? 48.733  -35.909 52.795  1.00 28.65  ? 133 LEU G N     1 
ATOM   8600  C CA    . LEU G 1 132 ? 49.547  -35.760 51.600  1.00 31.71  ? 133 LEU G CA    1 
ATOM   8601  C C     . LEU G 1 132 ? 49.918  -34.292 51.403  1.00 36.12  ? 133 LEU G C     1 
ATOM   8602  O O     . LEU G 1 132 ? 50.635  -33.952 50.465  1.00 35.65  ? 133 LEU G O     1 
ATOM   8603  C CB    . LEU G 1 132 ? 48.799  -36.317 50.389  1.00 33.33  ? 133 LEU G CB    1 
ATOM   8604  C CG    . LEU G 1 132 ? 48.670  -37.843 50.326  1.00 33.43  ? 133 LEU G CG    1 
ATOM   8605  C CD1   . LEU G 1 132 ? 47.839  -38.378 51.478  1.00 32.87  ? 133 LEU G CD1   1 
ATOM   8606  C CD2   . LEU G 1 132 ? 48.083  -38.277 48.997  1.00 38.33  ? 133 LEU G CD2   1 
ATOM   8607  N N     . GLY G 1 133 ? 49.421  -33.431 52.296  1.00 37.01  ? 134 GLY G N     1 
ATOM   8608  C CA    . GLY G 1 133 ? 49.680  -32.004 52.209  1.00 36.67  ? 134 GLY G CA    1 
ATOM   8609  C C     . GLY G 1 133 ? 49.284  -31.454 50.842  1.00 34.87  ? 134 GLY G C     1 
ATOM   8610  O O     . GLY G 1 133 ? 50.074  -30.781 50.184  1.00 33.20  ? 134 GLY G O     1 
ATOM   8611  N N     . ILE G 1 134 ? 48.052  -31.763 50.425  1.00 37.04  ? 135 ILE G N     1 
ATOM   8612  C CA    . ILE G 1 134 ? 47.516  -31.291 49.161  1.00 32.72  ? 135 ILE G CA    1 
ATOM   8613  C C     . ILE G 1 134 ? 46.315  -30.393 49.446  1.00 33.22  ? 135 ILE G C     1 
ATOM   8614  O O     . ILE G 1 134 ? 45.536  -30.663 50.357  1.00 31.01  ? 135 ILE G O     1 
ATOM   8615  C CB    . ILE G 1 134 ? 47.137  -32.475 48.252  1.00 33.26  ? 135 ILE G CB    1 
ATOM   8616  C CG1   . ILE G 1 134 ? 48.355  -33.337 47.913  1.00 36.55  ? 135 ILE G CG1   1 
ATOM   8617  C CG2   . ILE G 1 134 ? 46.419  -31.991 46.992  1.00 35.45  ? 135 ILE G CG2   1 
ATOM   8618  C CD1   . ILE G 1 134 ? 48.039  -34.544 47.047  1.00 36.13  ? 135 ILE G CD1   1 
ATOM   8619  N N     . ASP G 1 135 ? 46.185  -29.319 48.661  1.00 32.82  ? 136 ASP G N     1 
ATOM   8620  C CA    . ASP G 1 135 ? 45.043  -28.426 48.763  1.00 34.96  ? 136 ASP G CA    1 
ATOM   8621  C C     . ASP G 1 135 ? 44.132  -28.651 47.560  1.00 33.11  ? 136 ASP G C     1 
ATOM   8622  O O     . ASP G 1 135 ? 44.552  -28.479 46.419  1.00 33.94  ? 136 ASP G O     1 
ATOM   8623  C CB    . ASP G 1 135 ? 45.479  -26.974 48.882  1.00 35.57  ? 136 ASP G CB    1 
ATOM   8624  C CG    . ASP G 1 135 ? 44.346  -25.957 48.928  1.00 34.85  ? 136 ASP G CG    1 
ATOM   8625  O OD1   . ASP G 1 135 ? 43.175  -26.380 48.828  1.00 32.44  ? 136 ASP G OD1   1 
ATOM   8626  O OD2   . ASP G 1 135 ? 44.643  -24.752 49.067  1.00 40.11  ? 136 ASP G OD2   1 
ATOM   8627  N N     . PRO G 1 136 ? 42.855  -29.035 47.780  1.00 35.24  ? 137 PRO G N     1 
ATOM   8628  C CA    . PRO G 1 136 ? 41.938  -29.325 46.677  1.00 34.62  ? 137 PRO G CA    1 
ATOM   8629  C C     . PRO G 1 136 ? 41.718  -28.121 45.765  1.00 36.91  ? 137 PRO G C     1 
ATOM   8630  O O     . PRO G 1 136 ? 41.314  -28.276 44.614  1.00 42.36  ? 137 PRO G O     1 
ATOM   8631  C CB    . PRO G 1 136 ? 40.644  -29.762 47.394  1.00 35.76  ? 137 PRO G CB    1 
ATOM   8632  C CG    . PRO G 1 136 ? 40.750  -29.137 48.771  1.00 34.56  ? 137 PRO G CG    1 
ATOM   8633  C CD    . PRO G 1 136 ? 42.228  -29.188 49.101  1.00 33.76  ? 137 PRO G CD    1 
ATOM   8634  N N     . GLY G 1 137 ? 41.999  -26.925 46.291  1.00 34.51  ? 138 GLY G N     1 
ATOM   8635  C CA    . GLY G 1 137 ? 41.798  -25.691 45.550  1.00 34.54  ? 138 GLY G CA    1 
ATOM   8636  C C     . GLY G 1 137 ? 43.016  -25.341 44.698  1.00 33.22  ? 138 GLY G C     1 
ATOM   8637  O O     . GLY G 1 137 ? 42.944  -24.471 43.833  1.00 38.26  ? 138 GLY G O     1 
ATOM   8638  N N     . ASN G 1 138 ? 44.130  -26.037 44.948  1.00 32.34  ? 139 ASN G N     1 
ATOM   8639  C CA    . ASN G 1 138 ? 45.383  -25.756 44.266  1.00 34.68  ? 139 ASN G CA    1 
ATOM   8640  C C     . ASN G 1 138 ? 45.150  -25.754 42.757  1.00 32.57  ? 139 ASN G C     1 
ATOM   8641  O O     . ASN G 1 138 ? 45.446  -24.772 42.081  1.00 33.42  ? 139 ASN G O     1 
ATOM   8642  C CB    . ASN G 1 138 ? 46.471  -26.748 44.660  1.00 38.01  ? 139 ASN G CB    1 
ATOM   8643  C CG    . ASN G 1 138 ? 47.823  -26.354 44.114  1.00 38.79  ? 139 ASN G CG    1 
ATOM   8644  O OD1   . ASN G 1 138 ? 48.431  -27.112 43.350  1.00 38.92  ? 139 ASN G OD1   1 
ATOM   8645  N ND2   . ASN G 1 138 ? 48.312  -25.183 44.494  1.00 39.94  ? 139 ASN G ND2   1 
ATOM   8646  N N     . SER G 1 139 ? 44.625  -26.871 42.242  1.00 33.50  ? 140 SER G N     1 
ATOM   8647  C CA    . SER G 1 139 ? 44.339  -27.002 40.823  1.00 35.58  ? 140 SER G CA    1 
ATOM   8648  C C     . SER G 1 139 ? 42.945  -27.592 40.624  1.00 33.03  ? 140 SER G C     1 
ATOM   8649  O O     . SER G 1 139 ? 42.559  -27.923 39.506  1.00 30.71  ? 140 SER G O     1 
ATOM   8650  C CB    . SER G 1 139 ? 45.394  -27.831 40.129  1.00 36.31  ? 140 SER G CB    1 
ATOM   8651  O OG    . SER G 1 139 ? 45.553  -29.093 40.761  1.00 37.28  ? 140 SER G OG    1 
ATOM   8652  N N     . GLY G 1 140 ? 42.194  -27.709 41.724  1.00 33.33  ? 141 GLY G N     1 
ATOM   8653  C CA    . GLY G 1 140 ? 40.839  -28.234 41.675  1.00 29.96  ? 141 GLY G CA    1 
ATOM   8654  C C     . GLY G 1 140 ? 40.786  -29.681 42.156  1.00 28.47  ? 141 GLY G C     1 
ATOM   8655  O O     . GLY G 1 140 ? 41.817  -30.337 42.283  1.00 23.60  ? 141 GLY G O     1 
ATOM   8656  N N     . HIS G 1 141 ? 39.564  -30.170 42.396  1.00 29.17  ? 142 HIS G N     1 
ATOM   8657  C CA    . HIS G 1 141 ? 39.355  -31.480 42.987  1.00 26.91  ? 142 HIS G CA    1 
ATOM   8658  C C     . HIS G 1 141 ? 38.128  -32.141 42.366  1.00 25.50  ? 142 HIS G C     1 
ATOM   8659  O O     . HIS G 1 141 ? 37.114  -31.487 42.139  1.00 27.97  ? 142 HIS G O     1 
ATOM   8660  C CB    . HIS G 1 141 ? 39.214  -31.346 44.508  1.00 31.44  ? 142 HIS G CB    1 
ATOM   8661  C CG    . HIS G 1 141 ? 38.583  -32.523 45.170  1.00 31.85  ? 142 HIS G CG    1 
ATOM   8662  N ND1   . HIS G 1 141 ? 37.690  -32.384 46.211  1.00 36.20  ? 142 HIS G ND1   1 
ATOM   8663  C CD2   . HIS G 1 141 ? 38.683  -33.838 44.940  1.00 35.39  ? 142 HIS G CD2   1 
ATOM   8664  C CE1   . HIS G 1 141 ? 37.280  -33.583 46.596  1.00 35.78  ? 142 HIS G CE1   1 
ATOM   8665  N NE2   . HIS G 1 141 ? 37.872  -34.481 45.840  1.00 36.67  ? 142 HIS G NE2   1 
ATOM   8666  N N     . GLN G 1 142 ? 38.242  -33.446 42.097  1.00 27.44  ? 143 GLN G N     1 
ATOM   8667  C CA    . GLN G 1 142 ? 37.125  -34.242 41.613  1.00 30.97  ? 143 GLN G CA    1 
ATOM   8668  C C     . GLN G 1 142 ? 37.063  -35.547 42.401  1.00 30.74  ? 143 GLN G C     1 
ATOM   8669  O O     . GLN G 1 142 ? 38.096  -36.131 42.722  1.00 39.08  ? 143 GLN G O     1 
ATOM   8670  C CB    . GLN G 1 142 ? 37.261  -34.571 40.126  1.00 31.81  ? 143 GLN G CB    1 
ATOM   8671  C CG    . GLN G 1 142 ? 37.311  -33.353 39.212  1.00 38.22  ? 143 GLN G CG    1 
ATOM   8672  C CD    . GLN G 1 142 ? 37.334  -33.728 37.746  1.00 37.27  ? 143 GLN G CD    1 
ATOM   8673  O OE1   . GLN G 1 142 ? 36.462  -33.335 36.965  1.00 36.07  ? 143 GLN G OE1   1 
ATOM   8674  N NE2   . GLN G 1 142 ? 38.332  -34.510 37.364  1.00 39.40  ? 143 GLN G NE2   1 
ATOM   8675  N N     . SER G 1 143 ? 35.840  -35.997 42.700  1.00 27.87  ? 144 SER G N     1 
ATOM   8676  C CA    . SER G 1 143 ? 35.634  -37.261 43.387  1.00 28.61  ? 144 SER G CA    1 
ATOM   8677  C C     . SER G 1 143 ? 34.578  -38.083 42.653  1.00 28.45  ? 144 SER G C     1 
ATOM   8678  O O     . SER G 1 143 ? 33.515  -37.572 42.307  1.00 26.87  ? 144 SER G O     1 
ATOM   8679  C CB    . SER G 1 143 ? 35.251  -37.046 44.830  1.00 28.63  ? 144 SER G CB    1 
ATOM   8680  O OG    . SER G 1 143 ? 36.333  -36.503 45.573  1.00 35.89  ? 144 SER G OG    1 
ATOM   8681  N N     . PHE G 1 144 ? 34.893  -39.362 42.418  1.00 25.28  ? 145 PHE G N     1 
ATOM   8682  C CA    . PHE G 1 144 ? 33.964  -40.286 41.790  1.00 28.96  ? 145 PHE G CA    1 
ATOM   8683  C C     . PHE G 1 144 ? 34.034  -41.632 42.504  1.00 30.06  ? 145 PHE G C     1 
ATOM   8684  O O     . PHE G 1 144 ? 35.073  -42.002 43.045  1.00 30.55  ? 145 PHE G O     1 
ATOM   8685  C CB    . PHE G 1 144 ? 34.271  -40.490 40.303  1.00 32.26  ? 145 PHE G CB    1 
ATOM   8686  C CG    . PHE G 1 144 ? 34.215  -39.233 39.448  1.00 29.20  ? 145 PHE G CG    1 
ATOM   8687  C CD1   . PHE G 1 144 ? 33.001  -38.736 38.990  1.00 30.08  ? 145 PHE G CD1   1 
ATOM   8688  C CD2   . PHE G 1 144 ? 35.380  -38.571 39.076  1.00 33.90  ? 145 PHE G CD2   1 
ATOM   8689  C CE1   . PHE G 1 144 ? 32.954  -37.598 38.201  1.00 31.89  ? 145 PHE G CE1   1 
ATOM   8690  C CE2   . PHE G 1 144 ? 35.327  -37.433 38.286  1.00 35.55  ? 145 PHE G CE2   1 
ATOM   8691  C CZ    . PHE G 1 144 ? 34.115  -36.951 37.850  1.00 35.48  ? 145 PHE G CZ    1 
ATOM   8692  N N     . GLU G 1 145 ? 32.911  -42.355 42.491  1.00 33.85  ? 146 GLU G N     1 
ATOM   8693  C CA    . GLU G 1 145 ? 32.878  -43.731 42.957  1.00 33.29  ? 146 GLU G CA    1 
ATOM   8694  C C     . GLU G 1 145 ? 33.406  -44.621 41.835  1.00 32.46  ? 146 GLU G C     1 
ATOM   8695  O O     . GLU G 1 145 ? 32.822  -44.682 40.755  1.00 31.18  ? 146 GLU G O     1 
ATOM   8696  C CB    . GLU G 1 145 ? 31.459  -44.094 43.397  1.00 35.84  ? 146 GLU G CB    1 
ATOM   8697  C CG    . GLU G 1 145 ? 31.386  -45.341 44.275  1.00 34.04  ? 146 GLU G CG    1 
ATOM   8698  C CD    . GLU G 1 145 ? 31.362  -46.664 43.529  1.00 38.22  ? 146 GLU G CD    1 
ATOM   8699  O OE1   . GLU G 1 145 ? 31.298  -46.652 42.281  1.00 37.52  ? 146 GLU G OE1   1 
ATOM   8700  O OE2   . GLU G 1 145 ? 31.395  -47.713 44.206  1.00 36.57  ? 146 GLU G OE2   1 
ATOM   8701  N N     . ALA G 1 146 ? 34.531  -45.289 42.104  1.00 33.63  ? 147 ALA G N     1 
ATOM   8702  C CA    . ALA G 1 146 ? 35.281  -46.005 41.084  1.00 32.33  ? 147 ALA G CA    1 
ATOM   8703  C C     . ALA G 1 146 ? 34.337  -46.662 40.078  1.00 31.48  ? 147 ALA G C     1 
ATOM   8704  O O     . ALA G 1 146 ? 34.438  -46.415 38.878  1.00 32.92  ? 147 ALA G O     1 
ATOM   8705  C CB    . ALA G 1 146 ? 36.190  -47.021 41.738  1.00 33.81  ? 147 ALA G CB    1 
ATOM   8706  N N     . SER G 1 147 ? 33.428  -47.504 40.579  1.00 29.01  ? 148 SER G N     1 
ATOM   8707  C CA    . SER G 1 147 ? 32.570  -48.310 39.724  1.00 29.26  ? 148 SER G CA    1 
ATOM   8708  C C     . SER G 1 147 ? 31.674  -47.421 38.866  1.00 30.49  ? 148 SER G C     1 
ATOM   8709  O O     . SER G 1 147 ? 31.441  -47.718 37.696  1.00 30.78  ? 148 SER G O     1 
ATOM   8710  C CB    . SER G 1 147 ? 31.753  -49.284 40.533  1.00 28.68  ? 148 SER G CB    1 
ATOM   8711  O OG    . SER G 1 147 ? 32.579  -50.284 41.112  1.00 28.06  ? 148 SER G OG    1 
ATOM   8712  N N     . GLN G 1 148 ? 31.163  -46.338 39.461  1.00 28.70  ? 149 GLN G N     1 
ATOM   8713  C CA    . GLN G 1 148 ? 30.260  -45.440 38.760  1.00 29.48  ? 149 GLN G CA    1 
ATOM   8714  C C     . GLN G 1 148 ? 30.994  -44.808 37.581  1.00 28.95  ? 149 GLN G C     1 
ATOM   8715  O O     . GLN G 1 148 ? 30.400  -44.554 36.536  1.00 28.24  ? 149 GLN G O     1 
ATOM   8716  C CB    . GLN G 1 148 ? 29.713  -44.360 39.694  1.00 32.37  ? 149 GLN G CB    1 
ATOM   8717  C CG    . GLN G 1 148 ? 28.700  -43.433 39.031  1.00 35.50  ? 149 GLN G CG    1 
ATOM   8718  C CD    . GLN G 1 148 ? 28.265  -42.290 39.921  1.00 37.88  ? 149 GLN G CD    1 
ATOM   8719  O OE1   . GLN G 1 148 ? 28.477  -41.113 39.608  1.00 33.00  ? 149 GLN G OE1   1 
ATOM   8720  N NE2   . GLN G 1 148 ? 27.649  -42.629 41.045  1.00 39.09  ? 149 GLN G NE2   1 
ATOM   8721  N N     . PHE G 1 149 ? 32.294  -44.562 37.769  1.00 29.38  ? 150 PHE G N     1 
ATOM   8722  C CA    . PHE G 1 149 ? 33.124  -43.952 36.745  1.00 29.45  ? 150 PHE G CA    1 
ATOM   8723  C C     . PHE G 1 149 ? 33.228  -44.900 35.551  1.00 31.16  ? 150 PHE G C     1 
ATOM   8724  O O     . PHE G 1 149 ? 33.361  -44.458 34.412  1.00 27.18  ? 150 PHE G O     1 
ATOM   8725  C CB    . PHE G 1 149 ? 34.490  -43.612 37.349  1.00 32.45  ? 150 PHE G CB    1 
ATOM   8726  C CG    . PHE G 1 149 ? 35.478  -42.979 36.378  1.00 33.19  ? 150 PHE G CG    1 
ATOM   8727  C CD1   . PHE G 1 149 ? 36.269  -43.770 35.553  1.00 33.14  ? 150 PHE G CD1   1 
ATOM   8728  C CD2   . PHE G 1 149 ? 35.624  -41.598 36.302  1.00 35.83  ? 150 PHE G CD2   1 
ATOM   8729  C CE1   . PHE G 1 149 ? 37.169  -43.195 34.670  1.00 32.68  ? 150 PHE G CE1   1 
ATOM   8730  C CE2   . PHE G 1 149 ? 36.528  -41.029 35.418  1.00 35.10  ? 150 PHE G CE2   1 
ATOM   8731  C CZ    . PHE G 1 149 ? 37.297  -41.827 34.606  1.00 32.78  ? 150 PHE G CZ    1 
ATOM   8732  N N     . MET G 1 150 ? 33.151  -46.206 35.829  1.00 33.24  ? 151 MET G N     1 
ATOM   8733  C CA    . MET G 1 150 ? 33.297  -47.224 34.801  1.00 34.61  ? 151 MET G CA    1 
ATOM   8734  C C     . MET G 1 150 ? 31.950  -47.486 34.128  1.00 34.37  ? 151 MET G C     1 
ATOM   8735  O O     . MET G 1 150 ? 31.887  -47.668 32.915  1.00 40.05  ? 151 MET G O     1 
ATOM   8736  C CB    . MET G 1 150 ? 33.837  -48.531 35.394  1.00 35.66  ? 151 MET G CB    1 
ATOM   8737  C CG    . MET G 1 150 ? 35.277  -48.444 35.871  1.00 36.00  ? 151 MET G CG    1 
ATOM   8738  S SD    . MET G 1 150 ? 35.873  -49.975 36.617  1.00 43.86  ? 151 MET G SD    1 
ATOM   8739  C CE    . MET G 1 150 ? 35.958  -51.062 35.188  1.00 43.73  ? 151 MET G CE    1 
ATOM   8740  N N     . PHE G 1 151 ? 30.877  -47.496 34.925  1.00 35.27  ? 152 PHE G N     1 
ATOM   8741  C CA    . PHE G 1 151 ? 29.567  -47.901 34.440  1.00 31.69  ? 152 PHE G CA    1 
ATOM   8742  C C     . PHE G 1 151 ? 28.909  -46.753 33.680  1.00 33.43  ? 152 PHE G C     1 
ATOM   8743  O O     . PHE G 1 151 ? 28.201  -46.984 32.701  1.00 34.17  ? 152 PHE G O     1 
ATOM   8744  C CB    . PHE G 1 151 ? 28.693  -48.376 35.605  1.00 30.42  ? 152 PHE G CB    1 
ATOM   8745  C CG    . PHE G 1 151 ? 29.233  -49.601 36.331  1.00 29.41  ? 152 PHE G CG    1 
ATOM   8746  C CD1   . PHE G 1 151 ? 30.127  -50.463 35.706  1.00 31.50  ? 152 PHE G CD1   1 
ATOM   8747  C CD2   . PHE G 1 151 ? 28.837  -49.893 37.631  1.00 27.79  ? 152 PHE G CD2   1 
ATOM   8748  C CE1   . PHE G 1 151 ? 30.617  -51.577 36.369  1.00 33.13  ? 152 PHE G CE1   1 
ATOM   8749  C CE2   . PHE G 1 151 ? 29.330  -51.010 38.287  1.00 28.09  ? 152 PHE G CE2   1 
ATOM   8750  C CZ    . PHE G 1 151 ? 30.217  -51.848 37.656  1.00 29.07  ? 152 PHE G CZ    1 
ATOM   8751  N N     . PHE G 1 152 ? 29.143  -45.519 34.138  1.00 32.22  ? 153 PHE G N     1 
ATOM   8752  C CA    . PHE G 1 152 ? 28.508  -44.354 33.543  1.00 33.29  ? 153 PHE G CA    1 
ATOM   8753  C C     . PHE G 1 152 ? 29.573  -43.455 32.920  1.00 33.20  ? 153 PHE G C     1 
ATOM   8754  O O     . PHE G 1 152 ? 30.768  -43.685 33.090  1.00 32.95  ? 153 PHE G O     1 
ATOM   8755  C CB    . PHE G 1 152 ? 27.668  -43.629 34.599  1.00 35.16  ? 153 PHE G CB    1 
ATOM   8756  C CG    . PHE G 1 152 ? 26.585  -44.496 35.226  1.00 35.63  ? 153 PHE G CG    1 
ATOM   8757  C CD1   . PHE G 1 152 ? 25.410  -44.776 34.538  1.00 39.85  ? 153 PHE G CD1   1 
ATOM   8758  C CD2   . PHE G 1 152 ? 26.743  -45.026 36.502  1.00 36.11  ? 153 PHE G CD2   1 
ATOM   8759  C CE1   . PHE G 1 152 ? 24.427  -45.569 35.108  1.00 37.19  ? 153 PHE G CE1   1 
ATOM   8760  C CE2   . PHE G 1 152 ? 25.754  -45.816 37.067  1.00 37.06  ? 153 PHE G CE2   1 
ATOM   8761  C CZ    . PHE G 1 152 ? 24.600  -46.084 36.371  1.00 37.27  ? 153 PHE G CZ    1 
ATOM   8762  N N     . ASN G 1 153 ? 29.113  -42.426 32.199  1.00 35.09  ? 154 ASN G N     1 
ATOM   8763  C CA    . ASN G 1 153 ? 29.995  -41.552 31.446  1.00 34.17  ? 154 ASN G CA    1 
ATOM   8764  C C     . ASN G 1 153 ? 30.414  -40.368 32.313  1.00 32.95  ? 154 ASN G C     1 
ATOM   8765  O O     . ASN G 1 153 ? 29.627  -39.455 32.556  1.00 30.64  ? 154 ASN G O     1 
ATOM   8766  C CB    . ASN G 1 153 ? 29.347  -41.103 30.141  1.00 32.50  ? 154 ASN G CB    1 
ATOM   8767  C CG    . ASN G 1 153 ? 29.077  -42.267 29.217  1.00 33.39  ? 154 ASN G CG    1 
ATOM   8768  O OD1   . ASN G 1 153 ? 29.992  -43.037 28.903  1.00 34.60  ? 154 ASN G OD1   1 
ATOM   8769  N ND2   . ASN G 1 153 ? 27.836  -42.421 28.781  1.00 30.46  ? 154 ASN G ND2   1 
ATOM   8770  N N     . HIS G 1 154 ? 31.668  -40.409 32.771  1.00 36.51  ? 155 HIS G N     1 
ATOM   8771  C CA    . HIS G 1 154 ? 32.268  -39.321 33.524  1.00 34.37  ? 155 HIS G CA    1 
ATOM   8772  C C     . HIS G 1 154 ? 33.541  -38.874 32.816  1.00 35.71  ? 155 HIS G C     1 
ATOM   8773  O O     . HIS G 1 154 ? 34.367  -39.702 32.439  1.00 35.98  ? 155 HIS G O     1 
ATOM   8774  C CB    . HIS G 1 154 ? 32.575  -39.758 34.961  1.00 34.41  ? 155 HIS G CB    1 
ATOM   8775  C CG    . HIS G 1 154 ? 31.386  -39.805 35.859  1.00 35.71  ? 155 HIS G CG    1 
ATOM   8776  N ND1   . HIS G 1 154 ? 30.432  -38.810 35.891  1.00 35.51  ? 155 HIS G ND1   1 
ATOM   8777  C CD2   . HIS G 1 154 ? 31.019  -40.700 36.786  1.00 35.63  ? 155 HIS G CD2   1 
ATOM   8778  C CE1   . HIS G 1 154 ? 29.515  -39.116 36.796  1.00 36.34  ? 155 HIS G CE1   1 
ATOM   8779  N NE2   . HIS G 1 154 ? 29.850  -40.261 37.349  1.00 35.54  ? 155 HIS G NE2   1 
ATOM   8780  N N     . VAL G 1 155 ? 33.684  -37.556 32.643  1.00 34.89  ? 156 VAL G N     1 
ATOM   8781  C CA    . VAL G 1 155 ? 34.860  -36.985 32.011  1.00 33.78  ? 156 VAL G CA    1 
ATOM   8782  C C     . VAL G 1 155 ? 35.654  -36.223 33.066  1.00 34.03  ? 156 VAL G C     1 
ATOM   8783  O O     . VAL G 1 155 ? 35.212  -35.184 33.550  1.00 31.29  ? 156 VAL G O     1 
ATOM   8784  C CB    . VAL G 1 155 ? 34.485  -36.070 30.829  1.00 35.68  ? 156 VAL G CB    1 
ATOM   8785  C CG1   . VAL G 1 155 ? 35.703  -35.353 30.260  1.00 36.36  ? 156 VAL G CG1   1 
ATOM   8786  C CG2   . VAL G 1 155 ? 33.749  -36.835 29.735  1.00 37.96  ? 156 VAL G CG2   1 
ATOM   8787  N N     . PRO G 1 156 ? 36.841  -36.728 33.467  1.00 35.31  ? 157 PRO G N     1 
ATOM   8788  C CA    . PRO G 1 156 ? 37.670  -36.040 34.454  1.00 36.20  ? 157 PRO G CA    1 
ATOM   8789  C C     . PRO G 1 156 ? 38.417  -34.847 33.865  1.00 35.11  ? 157 PRO G C     1 
ATOM   8790  O O     . PRO G 1 156 ? 38.569  -34.738 32.650  1.00 33.36  ? 157 PRO G O     1 
ATOM   8791  C CB    . PRO G 1 156 ? 38.622  -37.154 34.921  1.00 36.23  ? 157 PRO G CB    1 
ATOM   8792  C CG    . PRO G 1 156 ? 38.783  -38.034 33.699  1.00 36.12  ? 157 PRO G CG    1 
ATOM   8793  C CD    . PRO G 1 156 ? 37.430  -37.994 33.004  1.00 36.31  ? 157 PRO G CD    1 
ATOM   8794  N N     . ASP G 1 157 ? 38.854  -33.947 34.749  1.00 32.19  ? 158 ASP G N     1 
ATOM   8795  C CA    . ASP G 1 157 ? 39.705  -32.833 34.372  1.00 30.83  ? 158 ASP G CA    1 
ATOM   8796  C C     . ASP G 1 157 ? 41.138  -33.182 34.762  1.00 32.79  ? 158 ASP G C     1 
ATOM   8797  O O     . ASP G 1 157 ? 41.457  -33.272 35.945  1.00 29.50  ? 158 ASP G O     1 
ATOM   8798  C CB    . ASP G 1 157 ? 39.218  -31.538 35.004  1.00 30.71  ? 158 ASP G CB    1 
ATOM   8799  C CG    . ASP G 1 157 ? 40.082  -30.313 34.741  1.00 28.19  ? 158 ASP G CG    1 
ATOM   8800  O OD1   . ASP G 1 157 ? 41.146  -30.472 34.112  1.00 26.72  ? 158 ASP G OD1   1 
ATOM   8801  O OD2   . ASP G 1 157 ? 39.678  -29.211 35.162  1.00 33.77  ? 158 ASP G OD2   1 
ATOM   8802  N N     . PRO G 1 158 ? 42.040  -33.404 33.781  1.00 36.82  ? 159 PRO G N     1 
ATOM   8803  C CA    . PRO G 1 158 ? 43.386  -33.899 34.076  1.00 38.19  ? 159 PRO G CA    1 
ATOM   8804  C C     . PRO G 1 158 ? 44.285  -32.879 34.774  1.00 36.91  ? 159 PRO G C     1 
ATOM   8805  O O     . PRO G 1 158 ? 45.450  -33.163 35.045  1.00 35.82  ? 159 PRO G O     1 
ATOM   8806  C CB    . PRO G 1 158 ? 43.917  -34.287 32.681  1.00 43.09  ? 159 PRO G CB    1 
ATOM   8807  C CG    . PRO G 1 158 ? 43.189  -33.355 31.734  1.00 44.55  ? 159 PRO G CG    1 
ATOM   8808  C CD    . PRO G 1 158 ? 41.809  -33.180 32.345  1.00 41.97  ? 159 PRO G CD    1 
ATOM   8809  N N     . THR G 1 159 ? 43.728  -31.700 35.078  1.00 33.62  ? 160 THR G N     1 
ATOM   8810  C CA    . THR G 1 159 ? 44.483  -30.647 35.739  1.00 32.23  ? 160 THR G CA    1 
ATOM   8811  C C     . THR G 1 159 ? 44.209  -30.687 37.241  1.00 29.96  ? 160 THR G C     1 
ATOM   8812  O O     . THR G 1 159 ? 44.930  -30.070 38.021  1.00 29.46  ? 160 THR G O     1 
ATOM   8813  C CB    . THR G 1 159 ? 44.118  -29.289 35.140  1.00 31.17  ? 160 THR G CB    1 
ATOM   8814  O OG1   . THR G 1 159 ? 42.731  -29.106 35.407  1.00 31.53  ? 160 THR G OG1   1 
ATOM   8815  C CG2   . THR G 1 159 ? 44.378  -29.220 33.646  1.00 33.51  ? 160 THR G CG2   1 
ATOM   8816  N N     . THR G 1 160 ? 43.167  -31.425 37.638  1.00 29.71  ? 161 THR G N     1 
ATOM   8817  C CA    . THR G 1 160 ? 42.730  -31.448 39.025  1.00 26.16  ? 161 THR G CA    1 
ATOM   8818  C C     . THR G 1 160 ? 43.261  -32.705 39.706  1.00 24.32  ? 161 THR G C     1 
ATOM   8819  O O     . THR G 1 160 ? 43.711  -33.634 39.042  1.00 25.19  ? 161 THR G O     1 
ATOM   8820  C CB    . THR G 1 160 ? 41.204  -31.396 39.087  1.00 26.30  ? 161 THR G CB    1 
ATOM   8821  O OG1   . THR G 1 160 ? 40.759  -32.661 38.607  1.00 30.71  ? 161 THR G OG1   1 
ATOM   8822  C CG2   . THR G 1 160 ? 40.620  -30.274 38.248  1.00 27.27  ? 161 THR G CG2   1 
ATOM   8823  N N     . HIS G 1 161 ? 43.203  -32.713 41.043  1.00 24.59  ? 162 HIS G N     1 
ATOM   8824  C CA    . HIS G 1 161 ? 43.403  -33.931 41.808  1.00 23.47  ? 162 HIS G CA    1 
ATOM   8825  C C     . HIS G 1 161 ? 42.136  -34.774 41.699  1.00 24.23  ? 162 HIS G C     1 
ATOM   8826  O O     . HIS G 1 161 ? 41.045  -34.303 42.014  1.00 24.02  ? 162 HIS G O     1 
ATOM   8827  C CB    . HIS G 1 161 ? 43.772  -33.613 43.262  1.00 24.18  ? 162 HIS G CB    1 
ATOM   8828  C CG    . HIS G 1 161 ? 45.177  -33.145 43.435  1.00 22.59  ? 162 HIS G CG    1 
ATOM   8829  N ND1   . HIS G 1 161 ? 45.539  -31.815 43.403  1.00 20.67  ? 162 HIS G ND1   1 
ATOM   8830  C CD2   . HIS G 1 161 ? 46.309  -33.833 43.640  1.00 22.18  ? 162 HIS G CD2   1 
ATOM   8831  C CE1   . HIS G 1 161 ? 46.848  -31.715 43.582  1.00 22.20  ? 162 HIS G CE1   1 
ATOM   8832  N NE2   . HIS G 1 161 ? 47.336  -32.928 43.728  1.00 23.30  ? 162 HIS G NE2   1 
ATOM   8833  N N     A LEU G 1 162 ? 42.296  -36.015 41.228  0.60 22.82  ? 163 LEU G N     1 
ATOM   8834  N N     B LEU G 1 162 ? 42.301  -36.024 41.257  0.40 24.20  ? 163 LEU G N     1 
ATOM   8835  C CA    A LEU G 1 162 ? 41.172  -36.911 41.010  0.60 22.09  ? 163 LEU G CA    1 
ATOM   8836  C CA    B LEU G 1 162 ? 41.174  -36.907 41.016  0.40 24.29  ? 163 LEU G CA    1 
ATOM   8837  C C     A LEU G 1 162 ? 41.199  -38.024 42.054  0.60 22.69  ? 163 LEU G C     1 
ATOM   8838  C C     B LEU G 1 162 ? 41.190  -38.045 42.033  0.40 23.99  ? 163 LEU G C     1 
ATOM   8839  O O     A LEU G 1 162 ? 42.218  -38.687 42.237  0.60 23.95  ? 163 LEU G O     1 
ATOM   8840  O O     B LEU G 1 162 ? 42.192  -38.741 42.179  0.40 24.87  ? 163 LEU G O     1 
ATOM   8841  C CB    A LEU G 1 162 ? 41.231  -37.476 39.592  0.60 20.90  ? 163 LEU G CB    1 
ATOM   8842  C CB    B LEU G 1 162 ? 41.242  -37.422 39.580  0.40 24.65  ? 163 LEU G CB    1 
ATOM   8843  C CG    A LEU G 1 162 ? 40.125  -38.471 39.221  0.60 21.33  ? 163 LEU G CG    1 
ATOM   8844  C CG    B LEU G 1 162 ? 40.065  -38.285 39.116  0.40 26.43  ? 163 LEU G CG    1 
ATOM   8845  C CD1   A LEU G 1 162 ? 38.770  -37.788 39.188  0.60 21.14  ? 163 LEU G CD1   1 
ATOM   8846  C CD1   B LEU G 1 162 ? 39.895  -38.180 37.612  0.40 28.03  ? 163 LEU G CD1   1 
ATOM   8847  C CD2   A LEU G 1 162 ? 40.416  -39.148 37.891  0.60 21.05  ? 163 LEU G CD2   1 
ATOM   8848  C CD2   B LEU G 1 162 ? 40.247  -39.735 39.527  0.40 26.35  ? 163 LEU G CD2   1 
ATOM   8849  N N     . LEU G 1 163 ? 40.062  -38.218 42.731  1.00 24.02  ? 164 LEU G N     1 
ATOM   8850  C CA    . LEU G 1 163 ? 39.914  -39.281 43.711  1.00 22.91  ? 164 LEU G CA    1 
ATOM   8851  C C     . LEU G 1 163 ? 38.904  -40.299 43.192  1.00 20.79  ? 164 LEU G C     1 
ATOM   8852  O O     . LEU G 1 163 ? 37.812  -39.933 42.768  1.00 20.20  ? 164 LEU G O     1 
ATOM   8853  C CB    . LEU G 1 163 ? 39.471  -38.712 45.059  1.00 25.28  ? 164 LEU G CB    1 
ATOM   8854  C CG    . LEU G 1 163 ? 40.428  -37.722 45.728  1.00 27.64  ? 164 LEU G CG    1 
ATOM   8855  C CD1   . LEU G 1 163 ? 39.952  -37.400 47.134  1.00 26.33  ? 164 LEU G CD1   1 
ATOM   8856  C CD2   . LEU G 1 163 ? 41.848  -38.255 45.751  1.00 30.40  ? 164 LEU G CD2   1 
ATOM   8857  N N     . LEU G 1 164 ? 39.288  -41.579 43.226  1.00 20.66  ? 165 LEU G N     1 
ATOM   8858  C CA    . LEU G 1 164 ? 38.360  -42.665 42.954  1.00 20.66  ? 165 LEU G CA    1 
ATOM   8859  C C     . LEU G 1 164 ? 38.130  -43.447 44.245  1.00 20.37  ? 165 LEU G C     1 
ATOM   8860  O O     . LEU G 1 164 ? 39.036  -44.111 44.745  1.00 19.04  ? 165 LEU G O     1 
ATOM   8861  C CB    . LEU G 1 164 ? 38.885  -43.564 41.836  1.00 21.39  ? 165 LEU G CB    1 
ATOM   8862  C CG    . LEU G 1 164 ? 39.007  -42.916 40.452  1.00 22.26  ? 165 LEU G CG    1 
ATOM   8863  C CD1   . LEU G 1 164 ? 39.371  -43.953 39.402  1.00 21.97  ? 165 LEU G CD1   1 
ATOM   8864  C CD2   . LEU G 1 164 ? 37.729  -42.190 40.065  1.00 22.13  ? 165 LEU G CD2   1 
ATOM   8865  N N     . TRP G 1 165 ? 36.910  -43.343 44.780  1.00 20.87  ? 166 TRP G N     1 
ATOM   8866  C CA    . TRP G 1 165 ? 36.548  -44.022 46.012  1.00 23.42  ? 166 TRP G CA    1 
ATOM   8867  C C     . TRP G 1 165 ? 36.113  -45.453 45.708  1.00 23.32  ? 166 TRP G C     1 
ATOM   8868  O O     . TRP G 1 165 ? 35.660  -45.748 44.604  1.00 23.33  ? 166 TRP G O     1 
ATOM   8869  C CB    . TRP G 1 165 ? 35.433  -43.263 46.743  1.00 25.29  ? 166 TRP G CB    1 
ATOM   8870  C CG    . TRP G 1 165 ? 35.760  -41.829 47.063  1.00 28.30  ? 166 TRP G CG    1 
ATOM   8871  C CD1   . TRP G 1 165 ? 36.196  -40.865 46.203  1.00 31.56  ? 166 TRP G CD1   1 
ATOM   8872  C CD2   . TRP G 1 165 ? 35.700  -41.207 48.365  1.00 29.29  ? 166 TRP G CD2   1 
ATOM   8873  N NE1   . TRP G 1 165 ? 36.390  -39.685 46.870  1.00 29.29  ? 166 TRP G NE1   1 
ATOM   8874  C CE2   . TRP G 1 165 ? 36.101  -39.864 48.197  1.00 31.68  ? 166 TRP G CE2   1 
ATOM   8875  C CE3   . TRP G 1 165 ? 35.347  -41.650 49.644  1.00 28.40  ? 166 TRP G CE3   1 
ATOM   8876  C CZ2   . TRP G 1 165 ? 36.156  -38.968 49.261  1.00 31.89  ? 166 TRP G CZ2   1 
ATOM   8877  C CZ3   . TRP G 1 165 ? 35.407  -40.763 50.695  1.00 31.54  ? 166 TRP G CZ3   1 
ATOM   8878  C CH2   . TRP G 1 165 ? 35.806  -39.441 50.504  1.00 28.17  ? 166 TRP G CH2   1 
ATOM   8879  N N     . GLN G 1 166 ? 36.239  -46.328 46.712  1.00 23.53  ? 167 GLN G N     1 
ATOM   8880  C CA    . GLN G 1 166 ? 35.848  -47.722 46.580  1.00 28.99  ? 167 GLN G CA    1 
ATOM   8881  C C     . GLN G 1 166 ? 36.494  -48.312 45.329  1.00 29.96  ? 167 GLN G C     1 
ATOM   8882  O O     . GLN G 1 166 ? 35.818  -48.919 44.501  1.00 32.37  ? 167 GLN G O     1 
ATOM   8883  C CB    . GLN G 1 166 ? 34.324  -47.851 46.533  1.00 29.65  ? 167 GLN G CB    1 
ATOM   8884  C CG    . GLN G 1 166 ? 33.627  -47.419 47.819  1.00 30.81  ? 167 GLN G CG    1 
ATOM   8885  C CD    . GLN G 1 166 ? 32.123  -47.581 47.769  1.00 34.72  ? 167 GLN G CD    1 
ATOM   8886  O OE1   . GLN G 1 166 ? 31.548  -47.966 46.744  1.00 35.67  ? 167 GLN G OE1   1 
ATOM   8887  N NE2   . GLN G 1 166 ? 31.469  -47.283 48.881  1.00 37.99  ? 167 GLN G NE2   1 
ATOM   8888  N N     . ILE G 1 167 ? 37.811  -48.123 45.210  1.00 28.59  ? 168 ILE G N     1 
ATOM   8889  C CA    . ILE G 1 167 ? 38.570  -48.639 44.084  1.00 29.52  ? 168 ILE G CA    1 
ATOM   8890  C C     . ILE G 1 167 ? 38.691  -50.155 44.227  1.00 32.77  ? 168 ILE G C     1 
ATOM   8891  O O     . ILE G 1 167 ? 38.860  -50.864 43.238  1.00 34.48  ? 168 ILE G O     1 
ATOM   8892  C CB    . ILE G 1 167 ? 39.949  -47.958 43.997  1.00 28.16  ? 168 ILE G CB    1 
ATOM   8893  C CG1   . ILE G 1 167 ? 40.730  -48.407 42.760  1.00 29.21  ? 168 ILE G CG1   1 
ATOM   8894  C CG2   . ILE G 1 167 ? 40.752  -48.181 45.279  1.00 26.81  ? 168 ILE G CG2   1 
ATOM   8895  C CD1   . ILE G 1 167 ? 40.051  -48.076 41.443  1.00 27.94  ? 168 ILE G CD1   1 
ATOM   8896  N N     . ALA G 1 168 ? 38.577  -50.637 45.469  1.00 31.21  ? 169 ALA G N     1 
ATOM   8897  C CA    . ALA G 1 168 ? 38.788  -52.042 45.780  1.00 32.72  ? 169 ALA G CA    1 
ATOM   8898  C C     . ALA G 1 168 ? 37.697  -52.903 45.146  1.00 31.46  ? 169 ALA G C     1 
ATOM   8899  O O     . ALA G 1 168 ? 37.888  -54.102 44.953  1.00 36.16  ? 169 ALA G O     1 
ATOM   8900  C CB    . ALA G 1 168 ? 38.837  -52.234 47.280  1.00 32.67  ? 169 ALA G CB    1 
ATOM   8901  N N     . ILE G 1 169 ? 36.553  -52.286 44.831  1.00 28.24  ? 170 ILE G N     1 
ATOM   8902  C CA    . ILE G 1 169 ? 35.430  -53.011 44.259  1.00 28.10  ? 170 ILE G CA    1 
ATOM   8903  C C     . ILE G 1 169 ? 35.059  -52.389 42.916  1.00 28.27  ? 170 ILE G C     1 
ATOM   8904  O O     . ILE G 1 169 ? 33.915  -52.484 42.478  1.00 29.67  ? 170 ILE G O     1 
ATOM   8905  C CB    . ILE G 1 169 ? 34.233  -53.028 45.227  1.00 30.08  ? 170 ILE G CB    1 
ATOM   8906  C CG1   . ILE G 1 169 ? 33.812  -51.613 45.629  1.00 34.15  ? 170 ILE G CG1   1 
ATOM   8907  C CG2   . ILE G 1 169 ? 34.532  -53.896 46.449  1.00 32.01  ? 170 ILE G CG2   1 
ATOM   8908  C CD1   . ILE G 1 169 ? 32.618  -51.563 46.564  1.00 33.79  ? 170 ILE G CD1   1 
ATOM   8909  N N     . ALA G 1 170 ? 36.041  -51.762 42.264  1.00 28.23  ? 171 ALA G N     1 
ATOM   8910  C CA    . ALA G 1 170 ? 35.826  -51.160 40.961  1.00 26.71  ? 171 ALA G CA    1 
ATOM   8911  C C     . ALA G 1 170 ? 35.428  -52.240 39.958  1.00 29.00  ? 171 ALA G C     1 
ATOM   8912  O O     . ALA G 1 170 ? 36.209  -53.145 39.670  1.00 28.59  ? 171 ALA G O     1 
ATOM   8913  C CB    . ALA G 1 170 ? 37.072  -50.426 40.521  1.00 26.90  ? 171 ALA G CB    1 
ATOM   8914  N N     . GLY G 1 171 ? 34.195  -52.145 39.451  1.00 29.36  ? 172 GLY G N     1 
ATOM   8915  C CA    . GLY G 1 171 ? 33.725  -53.036 38.403  1.00 33.57  ? 172 GLY G CA    1 
ATOM   8916  C C     . GLY G 1 171 ? 32.864  -54.166 38.962  1.00 37.11  ? 172 GLY G C     1 
ATOM   8917  O O     . GLY G 1 171 ? 32.343  -54.983 38.207  1.00 39.16  ? 172 GLY G O     1 
ATOM   8918  N N     . GLU G 1 172 ? 32.724  -54.200 40.292  1.00 37.93  ? 173 GLU G N     1 
ATOM   8919  C CA    . GLU G 1 172 ? 31.901  -55.198 40.954  1.00 36.56  ? 173 GLU G CA    1 
ATOM   8920  C C     . GLU G 1 172 ? 30.435  -54.800 40.794  1.00 34.41  ? 173 GLU G C     1 
ATOM   8921  O O     . GLU G 1 172 ? 29.915  -54.001 41.569  1.00 37.89  ? 173 GLU G O     1 
ATOM   8922  C CB    . GLU G 1 172 ? 32.311  -55.310 42.423  1.00 38.22  ? 173 GLU G CB    1 
ATOM   8923  C CG    . GLU G 1 172 ? 31.902  -56.628 43.075  1.00 42.74  ? 173 GLU G CG    1 
ATOM   8924  C CD    . GLU G 1 172 ? 30.417  -56.940 43.009  1.00 46.08  ? 173 GLU G CD    1 
ATOM   8925  O OE1   . GLU G 1 172 ? 29.786  -57.041 44.082  1.00 39.12  ? 173 GLU G OE1   1 
ATOM   8926  O OE2   . GLU G 1 172 ? 29.895  -57.095 41.884  1.00 49.99  ? 173 GLU G OE2   1 
ATOM   8927  N N     . HIS G 1 173 ? 29.777  -55.378 39.783  1.00 32.48  ? 174 HIS G N     1 
ATOM   8928  C CA    . HIS G 1 173 ? 28.487  -54.889 39.323  1.00 28.89  ? 174 HIS G CA    1 
ATOM   8929  C C     . HIS G 1 173 ? 27.345  -55.578 40.068  1.00 29.29  ? 174 HIS G C     1 
ATOM   8930  O O     . HIS G 1 173 ? 26.208  -55.115 40.014  1.00 27.59  ? 174 HIS G O     1 
ATOM   8931  C CB    . HIS G 1 173 ? 28.351  -55.085 37.809  1.00 28.99  ? 174 HIS G CB    1 
ATOM   8932  C CG    . HIS G 1 173 ? 28.289  -56.516 37.388  1.00 28.58  ? 174 HIS G CG    1 
ATOM   8933  N ND1   . HIS G 1 173 ? 29.408  -57.260 37.081  1.00 27.97  ? 174 HIS G ND1   1 
ATOM   8934  C CD2   . HIS G 1 173 ? 27.243  -57.339 37.229  1.00 26.64  ? 174 HIS G CD2   1 
ATOM   8935  C CE1   . HIS G 1 173 ? 29.038  -58.488 36.746  1.00 28.31  ? 174 HIS G CE1   1 
ATOM   8936  N NE2   . HIS G 1 173 ? 27.728  -58.558 36.829  1.00 27.92  ? 174 HIS G NE2   1 
ATOM   8937  N N     . THR G 1 174 ? 27.654  -56.681 40.759  1.00 30.94  ? 175 THR G N     1 
ATOM   8938  C CA    . THR G 1 174 ? 26.633  -57.473 41.430  1.00 36.00  ? 175 THR G CA    1 
ATOM   8939  C C     . THR G 1 174 ? 26.293  -56.838 42.777  1.00 36.77  ? 175 THR G C     1 
ATOM   8940  O O     . THR G 1 174 ? 25.165  -56.949 43.250  1.00 32.82  ? 175 THR G O     1 
ATOM   8941  C CB    . THR G 1 174 ? 27.118  -58.912 41.601  1.00 34.64  ? 175 THR G CB    1 
ATOM   8942  O OG1   . THR G 1 174 ? 28.228  -58.837 42.490  1.00 36.40  ? 175 THR G OG1   1 
ATOM   8943  C CG2   . THR G 1 174 ? 27.530  -59.552 40.287  1.00 35.67  ? 175 THR G CG2   1 
ATOM   8944  N N     . LEU G 1 175 ? 27.287  -56.186 43.390  1.00 36.60  ? 176 LEU G N     1 
ATOM   8945  C CA    . LEU G 1 175 ? 27.127  -55.596 44.709  1.00 34.71  ? 176 LEU G CA    1 
ATOM   8946  C C     . LEU G 1 175 ? 26.975  -56.713 45.739  1.00 36.55  ? 176 LEU G C     1 
ATOM   8947  O O     . LEU G 1 175 ? 26.280  -56.549 46.739  1.00 33.13  ? 176 LEU G O     1 
ATOM   8948  C CB    . LEU G 1 175 ? 25.925  -54.653 44.731  1.00 32.59  ? 176 LEU G CB    1 
ATOM   8949  C CG    . LEU G 1 175 ? 25.907  -53.556 43.662  1.00 33.99  ? 176 LEU G CG    1 
ATOM   8950  C CD1   . LEU G 1 175 ? 24.743  -52.606 43.889  1.00 33.48  ? 176 LEU G CD1   1 
ATOM   8951  C CD2   . LEU G 1 175 ? 27.222  -52.796 43.626  1.00 35.48  ? 176 LEU G CD2   1 
ATOM   8952  N N     . THR G 1 176 ? 27.631  -57.848 45.475  1.00 36.86  ? 177 THR G N     1 
ATOM   8953  C CA    . THR G 1 176 ? 27.563  -59.001 46.358  1.00 35.32  ? 177 THR G CA    1 
ATOM   8954  C C     . THR G 1 176 ? 28.975  -59.397 46.780  1.00 38.56  ? 177 THR G C     1 
ATOM   8955  O O     . THR G 1 176 ? 29.150  -60.195 47.698  1.00 40.76  ? 177 THR G O     1 
ATOM   8956  C CB    . THR G 1 176 ? 26.845  -60.150 45.651  1.00 35.36  ? 177 THR G CB    1 
ATOM   8957  O OG1   . THR G 1 176 ? 27.653  -60.464 44.520  1.00 38.08  ? 177 THR G OG1   1 
ATOM   8958  C CG2   . THR G 1 176 ? 25.442  -59.779 45.206  1.00 34.02  ? 177 THR G CG2   1 
ATOM   8959  N N     . GLN G 1 177 ? 29.975  -58.834 46.093  1.00 39.50  ? 178 GLN G N     1 
ATOM   8960  C CA    . GLN G 1 177 ? 31.369  -59.116 46.393  1.00 44.77  ? 178 GLN G CA    1 
ATOM   8961  C C     . GLN G 1 177 ? 31.958  -57.950 47.182  1.00 42.75  ? 178 GLN G C     1 
ATOM   8962  O O     . GLN G 1 177 ? 31.483  -56.821 47.078  1.00 41.09  ? 178 GLN G O     1 
ATOM   8963  C CB    . GLN G 1 177 ? 32.161  -59.362 45.108  1.00 48.34  ? 178 GLN G CB    1 
ATOM   8964  C CG    . GLN G 1 177 ? 31.643  -60.525 44.269  1.00 59.01  ? 178 GLN G CG    1 
ATOM   8965  C CD    . GLN G 1 177 ? 31.702  -61.855 44.989  1.00 65.83  ? 178 GLN G CD    1 
ATOM   8966  O OE1   . GLN G 1 177 ? 32.062  -61.936 46.168  1.00 64.26  ? 178 GLN G OE1   1 
ATOM   8967  N NE2   . GLN G 1 177 ? 31.344  -62.916 44.281  1.00 74.22  ? 178 GLN G NE2   1 
ATOM   8968  N N     . PHE G 1 178 ? 33.003  -58.244 47.961  1.00 44.02  ? 179 PHE G N     1 
ATOM   8969  C CA    . PHE G 1 178 ? 33.640  -57.256 48.816  1.00 50.72  ? 179 PHE G CA    1 
ATOM   8970  C C     . PHE G 1 178 ? 34.896  -56.722 48.133  1.00 46.37  ? 179 PHE G C     1 
ATOM   8971  O O     . PHE G 1 178 ? 35.495  -55.755 48.597  1.00 50.23  ? 179 PHE G O     1 
ATOM   8972  C CB    . PHE G 1 178 ? 33.958  -57.896 50.171  1.00 53.21  ? 179 PHE G CB    1 
ATOM   8973  C CG    . PHE G 1 178 ? 32.738  -58.325 50.975  1.00 61.50  ? 179 PHE G CG    1 
ATOM   8974  C CD1   . PHE G 1 178 ? 31.646  -57.476 51.123  1.00 65.26  ? 179 PHE G CD1   1 
ATOM   8975  C CD2   . PHE G 1 178 ? 32.675  -59.586 51.560  1.00 66.77  ? 179 PHE G CD2   1 
ATOM   8976  C CE1   . PHE G 1 178 ? 30.536  -57.871 51.853  1.00 65.49  ? 179 PHE G CE1   1 
ATOM   8977  C CE2   . PHE G 1 178 ? 31.560  -59.975 52.285  1.00 66.05  ? 179 PHE G CE2   1 
ATOM   8978  C CZ    . PHE G 1 178 ? 30.494  -59.119 52.430  1.00 62.73  ? 179 PHE G CZ    1 
ATOM   8979  N N     . HIS G 1 179 ? 35.286  -57.366 47.028  1.00 44.61  ? 180 HIS G N     1 
ATOM   8980  C CA    . HIS G 1 179 ? 36.481  -56.983 46.295  1.00 46.35  ? 180 HIS G CA    1 
ATOM   8981  C C     . HIS G 1 179 ? 36.311  -57.335 44.820  1.00 42.03  ? 180 HIS G C     1 
ATOM   8982  O O     . HIS G 1 179 ? 35.515  -58.205 44.473  1.00 42.23  ? 180 HIS G O     1 
ATOM   8983  C CB    . HIS G 1 179 ? 37.720  -57.659 46.892  1.00 48.21  ? 180 HIS G CB    1 
ATOM   8984  C CG    . HIS G 1 179 ? 37.660  -59.151 46.869  1.00 55.01  ? 180 HIS G CG    1 
ATOM   8985  N ND1   . HIS G 1 179 ? 37.983  -59.894 45.753  1.00 57.39  ? 180 HIS G ND1   1 
ATOM   8986  C CD2   . HIS G 1 179 ? 37.303  -60.035 47.811  1.00 52.66  ? 180 HIS G CD2   1 
ATOM   8987  C CE1   . HIS G 1 179 ? 37.832  -61.181 46.027  1.00 58.83  ? 180 HIS G CE1   1 
ATOM   8988  N NE2   . HIS G 1 179 ? 37.421  -61.290 47.271  1.00 59.69  ? 180 HIS G NE2   1 
ATOM   8989  N N     . THR G 1 180 ? 37.077  -56.651 43.963  1.00 41.58  ? 181 THR G N     1 
ATOM   8990  C CA    . THR G 1 180 ? 37.019  -56.872 42.527  1.00 42.58  ? 181 THR G CA    1 
ATOM   8991  C C     . THR G 1 180 ? 38.182  -57.772 42.115  1.00 43.56  ? 181 THR G C     1 
ATOM   8992  O O     . THR G 1 180 ? 38.747  -58.481 42.943  1.00 42.92  ? 181 THR G O     1 
ATOM   8993  C CB    . THR G 1 180 ? 37.052  -55.530 41.797  1.00 47.04  ? 181 THR G CB    1 
ATOM   8994  O OG1   . THR G 1 180 ? 36.823  -55.841 40.427  1.00 53.33  ? 181 THR G OG1   1 
ATOM   8995  C CG2   . THR G 1 180 ? 38.378  -54.808 41.959  1.00 46.95  ? 181 THR G CG2   1 
ATOM   8996  N N     . SER G 1 181 ? 38.529  -57.731 40.824  1.00 44.60  ? 182 SER G N     1 
ATOM   8997  C CA    . SER G 1 181 ? 39.607  -58.550 40.293  1.00 46.79  ? 182 SER G CA    1 
ATOM   8998  C C     . SER G 1 181 ? 40.560  -57.690 39.468  1.00 44.59  ? 182 SER G C     1 
ATOM   8999  O O     . SER G 1 181 ? 40.216  -56.582 39.061  1.00 39.04  ? 182 SER G O     1 
ATOM   9000  C CB    . SER G 1 181 ? 39.066  -59.697 39.481  1.00 54.30  ? 182 SER G CB    1 
ATOM   9001  O OG    . SER G 1 181 ? 38.352  -59.226 38.347  1.00 60.19  ? 182 SER G OG    1 
ATOM   9002  N N     . SER G 1 182 ? 41.757  -58.230 39.216  1.00 44.02  ? 183 SER G N     1 
ATOM   9003  C CA    . SER G 1 182 ? 42.809  -57.505 38.523  1.00 44.72  ? 183 SER G CA    1 
ATOM   9004  C C     . SER G 1 182 ? 42.386  -57.203 37.087  1.00 44.60  ? 183 SER G C     1 
ATOM   9005  O O     . SER G 1 182 ? 42.854  -56.237 36.490  1.00 46.49  ? 183 SER G O     1 
ATOM   9006  C CB    . SER G 1 182 ? 44.107  -58.272 38.557  1.00 44.28  ? 183 SER G CB    1 
ATOM   9007  O OG    . SER G 1 182 ? 43.986  -59.513 37.875  1.00 49.95  ? 183 SER G OG    1 
ATOM   9008  N N     . ASP G 1 183 ? 41.497  -58.042 36.544  1.00 46.26  ? 184 ASP G N     1 
ATOM   9009  C CA    . ASP G 1 183 ? 41.046  -57.900 35.169  1.00 45.69  ? 184 ASP G CA    1 
ATOM   9010  C C     . ASP G 1 183 ? 40.119  -56.692 35.060  1.00 41.95  ? 184 ASP G C     1 
ATOM   9011  O O     . ASP G 1 183 ? 40.065  -56.040 34.019  1.00 35.25  ? 184 ASP G O     1 
ATOM   9012  C CB    . ASP G 1 183 ? 40.388  -59.177 34.670  1.00 54.85  ? 184 ASP G CB    1 
ATOM   9013  C CG    . ASP G 1 183 ? 39.206  -59.668 35.493  1.00 67.23  ? 184 ASP G CG    1 
ATOM   9014  O OD1   . ASP G 1 183 ? 39.409  -59.965 36.689  1.00 76.55  ? 184 ASP G OD1   1 
ATOM   9015  O OD2   . ASP G 1 183 ? 38.093  -59.747 34.933  1.00 76.85  ? 184 ASP G OD2   1 
ATOM   9016  N N     . ARG G 1 184 ? 39.386  -56.408 36.142  1.00 38.36  ? 185 ARG G N     1 
ATOM   9017  C CA    . ARG G 1 184 ? 38.517  -55.245 36.194  1.00 41.11  ? 185 ARG G CA    1 
ATOM   9018  C C     . ARG G 1 184 ? 39.369  -53.981 36.279  1.00 34.15  ? 185 ARG G C     1 
ATOM   9019  O O     . ARG G 1 184 ? 39.122  -53.013 35.565  1.00 31.82  ? 185 ARG G O     1 
ATOM   9020  C CB    . ARG G 1 184 ? 37.549  -55.320 37.381  1.00 42.74  ? 185 ARG G CB    1 
ATOM   9021  C CG    . ARG G 1 184 ? 36.286  -56.130 37.129  1.00 51.98  ? 185 ARG G CG    1 
ATOM   9022  C CD    . ARG G 1 184 ? 36.563  -57.597 36.841  1.00 57.97  ? 185 ARG G CD    1 
ATOM   9023  N NE    . ARG G 1 184 ? 35.324  -58.344 36.595  1.00 63.88  ? 185 ARG G NE    1 
ATOM   9024  C CZ    . ARG G 1 184 ? 34.499  -58.126 35.577  1.00 68.42  ? 185 ARG G CZ    1 
ATOM   9025  N NH1   . ARG G 1 184 ? 34.790  -57.207 34.674  1.00 74.35  ? 185 ARG G NH1   1 
ATOM   9026  N NH2   . ARG G 1 184 ? 33.392  -58.838 35.459  1.00 68.56  ? 185 ARG G NH2   1 
ATOM   9027  N N     . LEU G 1 185 ? 40.374  -54.013 37.159  1.00 35.39  ? 186 LEU G N     1 
ATOM   9028  C CA    . LEU G 1 185 ? 41.238  -52.867 37.389  1.00 40.11  ? 186 LEU G CA    1 
ATOM   9029  C C     . LEU G 1 185 ? 42.056  -52.581 36.133  1.00 41.03  ? 186 LEU G C     1 
ATOM   9030  O O     . LEU G 1 185 ? 42.457  -51.444 35.896  1.00 44.20  ? 186 LEU G O     1 
ATOM   9031  C CB    . LEU G 1 185 ? 42.135  -53.137 38.597  1.00 43.11  ? 186 LEU G CB    1 
ATOM   9032  C CG    . LEU G 1 185 ? 41.415  -53.307 39.939  1.00 46.99  ? 186 LEU G CG    1 
ATOM   9033  C CD1   . LEU G 1 185 ? 42.407  -53.551 41.063  1.00 47.58  ? 186 LEU G CD1   1 
ATOM   9034  C CD2   . LEU G 1 185 ? 40.547  -52.097 40.244  1.00 50.85  ? 186 LEU G CD2   1 
ATOM   9035  N N     . GLN G 1 186 ? 42.299  -53.627 35.336  1.00 41.58  ? 187 GLN G N     1 
ATOM   9036  C CA    . GLN G 1 186 ? 43.062  -53.496 34.106  1.00 43.31  ? 187 GLN G CA    1 
ATOM   9037  C C     . GLN G 1 186 ? 42.249  -52.695 33.092  1.00 40.87  ? 187 GLN G C     1 
ATOM   9038  O O     . GLN G 1 186 ? 42.800  -51.898 32.336  1.00 35.57  ? 187 GLN G O     1 
ATOM   9039  C CB    . GLN G 1 186 ? 43.428  -54.876 33.559  1.00 45.71  ? 187 GLN G CB    1 
ATOM   9040  C CG    . GLN G 1 186 ? 44.135  -54.844 32.208  1.00 47.90  ? 187 GLN G CG    1 
ATOM   9041  C CD    . GLN G 1 186 ? 45.390  -53.999 32.212  1.00 47.05  ? 187 GLN G CD    1 
ATOM   9042  O OE1   . GLN G 1 186 ? 46.283  -54.175 33.048  1.00 49.93  ? 187 GLN G OE1   1 
ATOM   9043  N NE2   . GLN G 1 186 ? 45.467  -53.063 31.277  1.00 47.83  ? 187 GLN G NE2   1 
ATOM   9044  N N     . ILE G 1 187 ? 40.931  -52.917 33.093  1.00 39.19  ? 188 ILE G N     1 
ATOM   9045  C CA    . ILE G 1 187 ? 40.034  -52.226 32.183  1.00 37.64  ? 188 ILE G CA    1 
ATOM   9046  C C     . ILE G 1 187 ? 39.906  -50.771 32.622  1.00 33.94  ? 188 ILE G C     1 
ATOM   9047  O O     . ILE G 1 187 ? 39.696  -49.885 31.796  1.00 30.34  ? 188 ILE G O     1 
ATOM   9048  C CB    . ILE G 1 187 ? 38.665  -52.927 32.126  1.00 36.04  ? 188 ILE G CB    1 
ATOM   9049  C CG1   . ILE G 1 187 ? 38.782  -54.331 31.534  1.00 37.64  ? 188 ILE G CG1   1 
ATOM   9050  C CG2   . ILE G 1 187 ? 37.648  -52.076 31.366  1.00 35.13  ? 188 ILE G CG2   1 
ATOM   9051  C CD1   . ILE G 1 187 ? 37.469  -55.091 31.481  1.00 39.95  ? 188 ILE G CD1   1 
ATOM   9052  N N     . LEU G 1 188 ? 40.024  -50.540 33.933  1.00 32.38  ? 189 LEU G N     1 
ATOM   9053  C CA    . LEU G 1 188 ? 39.977  -49.194 34.477  1.00 34.74  ? 189 LEU G CA    1 
ATOM   9054  C C     . LEU G 1 188 ? 41.199  -48.421 33.991  1.00 27.95  ? 189 LEU G C     1 
ATOM   9055  O O     . LEU G 1 188 ? 41.097  -47.247 33.644  1.00 26.46  ? 189 LEU G O     1 
ATOM   9056  C CB    . LEU G 1 188 ? 39.914  -49.244 36.003  1.00 36.34  ? 189 LEU G CB    1 
ATOM   9057  C CG    . LEU G 1 188 ? 39.844  -47.888 36.713  1.00 37.30  ? 189 LEU G CG    1 
ATOM   9058  C CD1   . LEU G 1 188 ? 38.637  -47.090 36.250  1.00 37.15  ? 189 LEU G CD1   1 
ATOM   9059  C CD2   . LEU G 1 188 ? 39.821  -48.064 38.221  1.00 35.55  ? 189 LEU G CD2   1 
ATOM   9060  N N     . VAL G 1 189 ? 42.350  -49.102 33.962  1.00 27.62  ? 190 VAL G N     1 
ATOM   9061  C CA    . VAL G 1 189 ? 43.600  -48.492 33.541  1.00 30.94  ? 190 VAL G CA    1 
ATOM   9062  C C     . VAL G 1 189 ? 43.459  -48.025 32.095  1.00 32.30  ? 190 VAL G C     1 
ATOM   9063  O O     . VAL G 1 189 ? 43.798  -46.889 31.770  1.00 35.46  ? 190 VAL G O     1 
ATOM   9064  C CB    . VAL G 1 189 ? 44.789  -49.459 33.700  1.00 32.19  ? 190 VAL G CB    1 
ATOM   9065  C CG1   . VAL G 1 189 ? 46.040  -48.941 32.999  1.00 32.95  ? 190 VAL G CG1   1 
ATOM   9066  C CG2   . VAL G 1 189 ? 45.080  -49.762 35.165  1.00 31.87  ? 190 VAL G CG2   1 
ATOM   9067  N N     . GLU G 1 190 ? 42.954  -48.917 31.237  1.00 28.05  ? 191 GLU G N     1 
ATOM   9068  C CA    . GLU G 1 190 ? 42.781  -48.616 29.826  1.00 32.94  ? 191 GLU G CA    1 
ATOM   9069  C C     . GLU G 1 190 ? 41.836  -47.427 29.675  1.00 30.94  ? 191 GLU G C     1 
ATOM   9070  O O     . GLU G 1 190 ? 42.007  -46.602 28.781  1.00 30.26  ? 191 GLU G O     1 
ATOM   9071  C CB    . GLU G 1 190 ? 42.255  -49.846 29.084  1.00 35.77  ? 191 GLU G CB    1 
ATOM   9072  C CG    . GLU G 1 190 ? 43.209  -51.037 29.135  1.00 38.04  ? 191 GLU G CG    1 
ATOM   9073  C CD    . GLU G 1 190 ? 42.648  -52.311 28.528  1.00 42.30  ? 191 GLU G CD    1 
ATOM   9074  O OE1   . GLU G 1 190 ? 41.484  -52.288 28.077  1.00 45.73  ? 191 GLU G OE1   1 
ATOM   9075  O OE2   . GLU G 1 190 ? 43.376  -53.326 28.506  1.00 44.66  ? 191 GLU G OE2   1 
ATOM   9076  N N     . GLN G 1 191 ? 40.844  -47.350 30.568  1.00 30.36  ? 192 GLN G N     1 
ATOM   9077  C CA    . GLN G 1 191 ? 39.844  -46.295 30.527  1.00 31.76  ? 192 GLN G CA    1 
ATOM   9078  C C     . GLN G 1 191 ? 40.480  -44.967 30.928  1.00 31.04  ? 192 GLN G C     1 
ATOM   9079  O O     . GLN G 1 191 ? 40.173  -43.926 30.352  1.00 31.63  ? 192 GLN G O     1 
ATOM   9080  C CB    . GLN G 1 191 ? 38.678  -46.626 31.459  1.00 33.86  ? 192 GLN G CB    1 
ATOM   9081  C CG    . GLN G 1 191 ? 37.559  -45.590 31.439  1.00 35.52  ? 192 GLN G CG    1 
ATOM   9082  C CD    . GLN G 1 191 ? 36.440  -45.903 32.408  1.00 34.94  ? 192 GLN G CD    1 
ATOM   9083  O OE1   . GLN G 1 191 ? 36.526  -46.836 33.214  1.00 31.57  ? 192 GLN G OE1   1 
ATOM   9084  N NE2   . GLN G 1 191 ? 35.379  -45.113 32.345  1.00 37.29  ? 192 GLN G NE2   1 
ATOM   9085  N N     . LEU G 1 192 ? 41.360  -45.020 31.934  1.00 30.40  ? 193 LEU G N     1 
ATOM   9086  C CA    . LEU G 1 192 ? 42.030  -43.831 32.434  1.00 28.60  ? 193 LEU G CA    1 
ATOM   9087  C C     . LEU G 1 192 ? 43.097  -43.388 31.438  1.00 29.25  ? 193 LEU G C     1 
ATOM   9088  O O     . LEU G 1 192 ? 43.518  -42.233 31.445  1.00 27.93  ? 193 LEU G O     1 
ATOM   9089  C CB    . LEU G 1 192 ? 42.638  -44.123 33.806  1.00 27.57  ? 193 LEU G CB    1 
ATOM   9090  C CG    . LEU G 1 192 ? 41.646  -44.257 34.965  1.00 25.39  ? 193 LEU G CG    1 
ATOM   9091  C CD1   . LEU G 1 192 ? 42.366  -44.580 36.263  1.00 24.06  ? 193 LEU G CD1   1 
ATOM   9092  C CD2   . LEU G 1 192 ? 40.822  -42.990 35.109  1.00 27.16  ? 193 LEU G CD2   1 
ATOM   9093  N N     . ASN G 1 193 ? 43.518  -44.320 30.578  1.00 32.20  ? 194 ASN G N     1 
ATOM   9094  C CA    . ASN G 1 193 ? 44.621  -44.084 29.661  1.00 34.87  ? 194 ASN G CA    1 
ATOM   9095  C C     . ASN G 1 193 ? 44.212  -43.039 28.625  1.00 33.42  ? 194 ASN G C     1 
ATOM   9096  O O     . ASN G 1 193 ? 45.028  -42.626 27.805  1.00 35.71  ? 194 ASN G O     1 
ATOM   9097  C CB    . ASN G 1 193 ? 45.083  -45.382 29.006  1.00 36.53  ? 194 ASN G CB    1 
ATOM   9098  C CG    . ASN G 1 193 ? 46.352  -45.200 28.207  1.00 39.89  ? 194 ASN G CG    1 
ATOM   9099  O OD1   . ASN G 1 193 ? 47.379  -44.784 28.755  1.00 43.06  ? 194 ASN G OD1   1 
ATOM   9100  N ND2   . ASN G 1 193 ? 46.304  -45.505 26.919  1.00 41.35  ? 194 ASN G ND2   1 
ATOM   9101  N N     . GLN G 1 194 ? 42.944  -42.616 28.677  1.00 36.40  ? 195 GLN G N     1 
ATOM   9102  C CA    . GLN G 1 194 ? 42.432  -41.613 27.757  1.00 35.25  ? 195 GLN G CA    1 
ATOM   9103  C C     . GLN G 1 194 ? 42.953  -40.237 28.159  1.00 34.44  ? 195 GLN G C     1 
ATOM   9104  O O     . GLN G 1 194 ? 43.030  -39.334 27.329  1.00 29.85  ? 195 GLN G O     1 
ATOM   9105  C CB    . GLN G 1 194 ? 40.903  -41.584 27.750  1.00 35.02  ? 195 GLN G CB    1 
ATOM   9106  C CG    . GLN G 1 194 ? 40.252  -42.894 27.320  1.00 35.44  ? 195 GLN G CG    1 
ATOM   9107  C CD    . GLN G 1 194 ? 38.740  -42.848 27.384  1.00 36.75  ? 195 GLN G CD    1 
ATOM   9108  O OE1   . GLN G 1 194 ? 38.083  -42.133 26.621  1.00 34.52  ? 195 GLN G OE1   1 
ATOM   9109  N NE2   . GLN G 1 194 ? 38.172  -43.615 28.303  1.00 39.48  ? 195 GLN G NE2   1 
ATOM   9110  N N     . TRP G 1 195 ? 43.301  -40.089 29.442  1.00 32.51  ? 196 TRP G N     1 
ATOM   9111  C CA    . TRP G 1 195 ? 43.686  -38.797 29.985  1.00 33.41  ? 196 TRP G CA    1 
ATOM   9112  C C     . TRP G 1 195 ? 45.028  -38.894 30.707  1.00 34.46  ? 196 TRP G C     1 
ATOM   9113  O O     . TRP G 1 195 ? 45.720  -37.891 30.866  1.00 31.36  ? 196 TRP G O     1 
ATOM   9114  C CB    . TRP G 1 195 ? 42.594  -38.273 30.929  1.00 33.26  ? 196 TRP G CB    1 
ATOM   9115  C CG    . TRP G 1 195 ? 41.215  -38.260 30.324  1.00 30.78  ? 196 TRP G CG    1 
ATOM   9116  C CD1   . TRP G 1 195 ? 40.686  -37.303 29.510  1.00 31.48  ? 196 TRP G CD1   1 
ATOM   9117  C CD2   . TRP G 1 195 ? 40.179  -39.251 30.504  1.00 27.64  ? 196 TRP G CD2   1 
ATOM   9118  N NE1   . TRP G 1 195 ? 39.403  -37.630 29.162  1.00 33.20  ? 196 TRP G NE1   1 
ATOM   9119  C CE2   . TRP G 1 195 ? 39.063  -38.816 29.758  1.00 30.31  ? 196 TRP G CE2   1 
ATOM   9120  C CE3   . TRP G 1 195 ? 40.087  -40.452 31.215  1.00 26.78  ? 196 TRP G CE3   1 
ATOM   9121  C CZ2   . TRP G 1 195 ? 37.875  -39.542 29.706  1.00 29.45  ? 196 TRP G CZ2   1 
ATOM   9122  C CZ3   . TRP G 1 195 ? 38.911  -41.168 31.164  1.00 28.53  ? 196 TRP G CZ3   1 
ATOM   9123  C CH2   . TRP G 1 195 ? 37.822  -40.718 30.418  1.00 27.46  ? 196 TRP G CH2   1 
ATOM   9124  N N     . TYR G 1 196 ? 45.385  -40.106 31.147  1.00 33.78  ? 197 TYR G N     1 
ATOM   9125  C CA    . TYR G 1 196 ? 46.586  -40.300 31.941  1.00 32.51  ? 197 TYR G CA    1 
ATOM   9126  C C     . TYR G 1 196 ? 47.471  -41.357 31.287  1.00 31.88  ? 197 TYR G C     1 
ATOM   9127  O O     . TYR G 1 196 ? 46.999  -42.431 30.922  1.00 31.24  ? 197 TYR G O     1 
ATOM   9128  C CB    . TYR G 1 196 ? 46.209  -40.696 33.373  1.00 29.14  ? 197 TYR G CB    1 
ATOM   9129  C CG    . TYR G 1 196 ? 45.257  -39.728 34.061  1.00 30.38  ? 197 TYR G CG    1 
ATOM   9130  C CD1   . TYR G 1 196 ? 45.729  -38.592 34.709  1.00 30.75  ? 197 TYR G CD1   1 
ATOM   9131  C CD2   . TYR G 1 196 ? 43.886  -39.951 34.064  1.00 29.66  ? 197 TYR G CD2   1 
ATOM   9132  C CE1   . TYR G 1 196 ? 44.867  -37.706 35.332  1.00 27.17  ? 197 TYR G CE1   1 
ATOM   9133  C CE2   . TYR G 1 196 ? 43.013  -39.073 34.684  1.00 27.05  ? 197 TYR G CE2   1 
ATOM   9134  C CZ    . TYR G 1 196 ? 43.504  -37.947 35.319  1.00 26.01  ? 197 TYR G CZ    1 
ATOM   9135  O OH    . TYR G 1 196 ? 42.644  -37.081 35.929  1.00 24.52  ? 197 TYR G OH    1 
ATOM   9136  N N     . PRO G 1 197 ? 48.783  -41.077 31.115  1.00 34.44  ? 198 PRO G N     1 
ATOM   9137  C CA    . PRO G 1 197 ? 49.729  -42.086 30.639  1.00 37.36  ? 198 PRO G CA    1 
ATOM   9138  C C     . PRO G 1 197 ? 49.712  -43.311 31.549  1.00 38.81  ? 198 PRO G C     1 
ATOM   9139  O O     . PRO G 1 197 ? 49.140  -43.271 32.635  1.00 44.79  ? 198 PRO G O     1 
ATOM   9140  C CB    . PRO G 1 197 ? 51.086  -41.353 30.658  1.00 36.86  ? 198 PRO G CB    1 
ATOM   9141  C CG    . PRO G 1 197 ? 50.720  -39.882 30.583  1.00 37.12  ? 198 PRO G CG    1 
ATOM   9142  C CD    . PRO G 1 197 ? 49.408  -39.765 31.338  1.00 36.16  ? 198 PRO G CD    1 
ATOM   9143  N N     . LEU G 1 198 ? 50.352  -44.393 31.094  1.00 40.12  ? 199 LEU G N     1 
ATOM   9144  C CA    . LEU G 1 198 ? 50.394  -45.632 31.852  1.00 39.77  ? 199 LEU G CA    1 
ATOM   9145  C C     . LEU G 1 198 ? 51.399  -45.497 32.994  1.00 37.43  ? 199 LEU G C     1 
ATOM   9146  O O     . LEU G 1 198 ? 51.257  -46.141 34.032  1.00 33.31  ? 199 LEU G O     1 
ATOM   9147  C CB    . LEU G 1 198 ? 50.746  -46.797 30.927  1.00 42.01  ? 199 LEU G CB    1 
ATOM   9148  C CG    . LEU G 1 198 ? 49.713  -47.128 29.845  1.00 45.85  ? 199 LEU G CG    1 
ATOM   9149  C CD1   . LEU G 1 198 ? 50.109  -48.377 29.074  1.00 47.21  ? 199 LEU G CD1   1 
ATOM   9150  C CD2   . LEU G 1 198 ? 48.329  -47.287 30.449  1.00 46.41  ? 199 LEU G CD2   1 
ATOM   9151  N N     . ASP G 1 199 ? 52.405  -44.640 32.793  1.00 35.94  ? 200 ASP G N     1 
ATOM   9152  C CA    . ASP G 1 199 ? 53.479  -44.469 33.756  1.00 38.22  ? 200 ASP G CA    1 
ATOM   9153  C C     . ASP G 1 199 ? 53.159  -43.303 34.687  1.00 37.52  ? 200 ASP G C     1 
ATOM   9154  O O     . ASP G 1 199 ? 54.040  -42.805 35.383  1.00 36.97  ? 200 ASP G O     1 
ATOM   9155  C CB    . ASP G 1 199 ? 54.812  -44.250 33.060  1.00 41.44  ? 200 ASP G CB    1 
ATOM   9156  C CG    . ASP G 1 199 ? 54.869  -43.039 32.140  1.00 45.63  ? 200 ASP G CG    1 
ATOM   9157  O OD1   . ASP G 1 199 ? 53.826  -42.368 31.991  1.00 48.32  ? 200 ASP G OD1   1 
ATOM   9158  O OD2   . ASP G 1 199 ? 55.956  -42.774 31.584  1.00 46.43  ? 200 ASP G OD2   1 
ATOM   9159  N N     . HIS G 1 200 ? 51.894  -42.870 34.687  1.00 35.86  ? 201 HIS G N     1 
ATOM   9160  C CA    . HIS G 1 200 ? 51.471  -41.757 35.521  1.00 36.23  ? 201 HIS G CA    1 
ATOM   9161  C C     . HIS G 1 200 ? 51.404  -42.216 36.975  1.00 33.22  ? 201 HIS G C     1 
ATOM   9162  O O     . HIS G 1 200 ? 50.701  -43.171 37.300  1.00 28.76  ? 201 HIS G O     1 
ATOM   9163  C CB    . HIS G 1 200 ? 50.141  -41.178 35.025  1.00 39.08  ? 201 HIS G CB    1 
ATOM   9164  C CG    . HIS G 1 200 ? 49.668  -40.003 35.815  1.00 38.11  ? 201 HIS G CG    1 
ATOM   9165  N ND1   . HIS G 1 200 ? 50.225  -38.749 35.686  1.00 39.51  ? 201 HIS G ND1   1 
ATOM   9166  C CD2   . HIS G 1 200 ? 48.725  -39.892 36.759  1.00 36.65  ? 201 HIS G CD2   1 
ATOM   9167  C CE1   . HIS G 1 200 ? 49.619  -37.913 36.516  1.00 36.34  ? 201 HIS G CE1   1 
ATOM   9168  N NE2   . HIS G 1 200 ? 48.702  -38.585 37.175  1.00 37.16  ? 201 HIS G NE2   1 
ATOM   9169  N N     . GLU G 1 201 ? 52.150  -41.520 37.839  1.00 29.28  ? 202 GLU G N     1 
ATOM   9170  C CA    . GLU G 1 201 ? 52.230  -41.867 39.247  1.00 31.85  ? 202 GLU G CA    1 
ATOM   9171  C C     . GLU G 1 201 ? 50.886  -41.596 39.917  1.00 30.21  ? 202 GLU G C     1 
ATOM   9172  O O     . GLU G 1 201 ? 50.426  -40.457 39.957  1.00 30.03  ? 202 GLU G O     1 
ATOM   9173  C CB    . GLU G 1 201 ? 53.351  -41.074 39.922  1.00 35.05  ? 202 GLU G CB    1 
ATOM   9174  C CG    . GLU G 1 201 ? 53.437  -41.302 41.429  1.00 40.10  ? 202 GLU G CG    1 
ATOM   9175  C CD    . GLU G 1 201 ? 54.544  -40.519 42.113  1.00 45.75  ? 202 GLU G CD    1 
ATOM   9176  O OE1   . GLU G 1 201 ? 55.726  -40.751 41.783  1.00 56.51  ? 202 GLU G OE1   1 
ATOM   9177  O OE2   . GLU G 1 201 ? 54.225  -39.671 42.972  1.00 56.29  ? 202 GLU G OE2   1 
ATOM   9178  N N     . VAL G 1 202 ? 50.263  -42.664 40.428  1.00 27.36  ? 203 VAL G N     1 
ATOM   9179  C CA    . VAL G 1 202 ? 49.054  -42.548 41.228  1.00 24.63  ? 203 VAL G CA    1 
ATOM   9180  C C     . VAL G 1 202 ? 49.403  -42.937 42.661  1.00 24.21  ? 203 VAL G C     1 
ATOM   9181  O O     . VAL G 1 202 ? 50.494  -43.439 42.922  1.00 22.77  ? 203 VAL G O     1 
ATOM   9182  C CB    . VAL G 1 202 ? 47.901  -43.410 40.678  1.00 23.79  ? 203 VAL G CB    1 
ATOM   9183  C CG1   . VAL G 1 202 ? 47.485  -42.974 39.279  1.00 23.99  ? 203 VAL G CG1   1 
ATOM   9184  C CG2   . VAL G 1 202 ? 48.241  -44.895 40.700  1.00 23.79  ? 203 VAL G CG2   1 
ATOM   9185  N N     . VAL G 1 203 ? 48.466  -42.702 43.585  1.00 24.75  ? 204 VAL G N     1 
ATOM   9186  C CA    . VAL G 1 203 ? 48.719  -42.929 44.997  1.00 25.99  ? 204 VAL G CA    1 
ATOM   9187  C C     . VAL G 1 203 ? 47.561  -43.720 45.597  1.00 25.63  ? 204 VAL G C     1 
ATOM   9188  O O     . VAL G 1 203 ? 46.405  -43.311 45.498  1.00 30.68  ? 204 VAL G O     1 
ATOM   9189  C CB    . VAL G 1 203 ? 48.923  -41.599 45.747  1.00 26.59  ? 204 VAL G CB    1 
ATOM   9190  C CG1   . VAL G 1 203 ? 49.147  -41.820 47.238  1.00 27.53  ? 204 VAL G CG1   1 
ATOM   9191  C CG2   . VAL G 1 203 ? 50.058  -40.778 45.149  1.00 27.14  ? 204 VAL G CG2   1 
ATOM   9192  N N     . ILE G 1 204 ? 47.892  -44.851 46.227  1.00 25.48  ? 205 ILE G N     1 
ATOM   9193  C CA    . ILE G 1 204 ? 46.930  -45.600 47.018  1.00 24.48  ? 205 ILE G CA    1 
ATOM   9194  C C     . ILE G 1 204 ? 46.973  -45.067 48.446  1.00 24.95  ? 205 ILE G C     1 
ATOM   9195  O O     . ILE G 1 204 ? 47.974  -45.224 49.142  1.00 24.74  ? 205 ILE G O     1 
ATOM   9196  C CB    . ILE G 1 204 ? 47.217  -47.112 46.964  1.00 23.49  ? 205 ILE G CB    1 
ATOM   9197  C CG1   . ILE G 1 204 ? 47.099  -47.658 45.541  1.00 24.50  ? 205 ILE G CG1   1 
ATOM   9198  C CG2   . ILE G 1 204 ? 46.311  -47.870 47.936  1.00 22.06  ? 205 ILE G CG2   1 
ATOM   9199  C CD1   . ILE G 1 204 ? 47.415  -49.139 45.417  1.00 25.23  ? 205 ILE G CD1   1 
ATOM   9200  N N     . TYR G 1 205 ? 45.876  -44.430 48.869  1.00 27.08  ? 206 TYR G N     1 
ATOM   9201  C CA    . TYR G 1 205 ? 45.826  -43.786 50.170  1.00 28.60  ? 206 TYR G CA    1 
ATOM   9202  C C     . TYR G 1 205 ? 44.907  -44.568 51.102  1.00 30.74  ? 206 TYR G C     1 
ATOM   9203  O O     . TYR G 1 205 ? 43.830  -45.011 50.705  1.00 30.55  ? 206 TYR G O     1 
ATOM   9204  C CB    . TYR G 1 205 ? 45.363  -42.332 50.047  1.00 27.99  ? 206 TYR G CB    1 
ATOM   9205  C CG    . TYR G 1 205 ? 45.104  -41.661 51.389  1.00 29.27  ? 206 TYR G CG    1 
ATOM   9206  C CD1   . TYR G 1 205 ? 46.155  -41.291 52.219  1.00 29.79  ? 206 TYR G CD1   1 
ATOM   9207  C CD2   . TYR G 1 205 ? 43.811  -41.395 51.822  1.00 29.20  ? 206 TYR G CD2   1 
ATOM   9208  C CE1   . TYR G 1 205 ? 45.929  -40.685 53.443  1.00 30.16  ? 206 TYR G CE1   1 
ATOM   9209  C CE2   . TYR G 1 205 ? 43.571  -40.786 53.043  1.00 31.51  ? 206 TYR G CE2   1 
ATOM   9210  C CZ    . TYR G 1 205 ? 44.633  -40.429 53.855  1.00 31.41  ? 206 TYR G CZ    1 
ATOM   9211  O OH    . TYR G 1 205 ? 44.405  -39.829 55.058  1.00 28.82  ? 206 TYR G OH    1 
ATOM   9212  N N     . GLU G 1 206 ? 45.361  -44.724 52.350  1.00 28.19  ? 207 GLU G N     1 
ATOM   9213  C CA    . GLU G 1 206 ? 44.552  -45.296 53.411  1.00 29.37  ? 207 GLU G CA    1 
ATOM   9214  C C     . GLU G 1 206 ? 44.830  -44.533 54.702  1.00 26.44  ? 207 GLU G C     1 
ATOM   9215  O O     . GLU G 1 206 ? 45.928  -44.610 55.248  1.00 27.32  ? 207 GLU G O     1 
ATOM   9216  C CB    . GLU G 1 206 ? 44.848  -46.785 53.597  1.00 32.46  ? 207 GLU G CB    1 
ATOM   9217  C CG    . GLU G 1 206 ? 44.456  -47.639 52.395  1.00 34.97  ? 207 GLU G CG    1 
ATOM   9218  C CD    . GLU G 1 206 ? 44.785  -49.112 52.553  1.00 37.41  ? 207 GLU G CD    1 
ATOM   9219  O OE1   . GLU G 1 206 ? 45.304  -49.489 53.626  1.00 39.60  ? 207 GLU G OE1   1 
ATOM   9220  O OE2   . GLU G 1 206 ? 44.528  -49.881 51.603  1.00 40.26  ? 207 GLU G OE2   1 
ATOM   9221  N N     . ALA G 1 207 ? 43.823  -43.787 55.167  1.00 23.39  ? 208 ALA G N     1 
ATOM   9222  C CA    . ALA G 1 207 ? 43.927  -43.036 56.406  1.00 24.50  ? 208 ALA G CA    1 
ATOM   9223  C C     . ALA G 1 207 ? 43.964  -44.002 57.586  1.00 23.90  ? 208 ALA G C     1 
ATOM   9224  O O     . ALA G 1 207 ? 43.260  -45.010 57.591  1.00 24.54  ? 208 ALA G O     1 
ATOM   9225  C CB    . ALA G 1 207 ? 42.771  -42.067 56.519  1.00 25.01  ? 208 ALA G CB    1 
ATOM   9226  N N     . ALA G 1 208 ? 44.792  -43.676 58.582  1.00 23.64  ? 209 ALA G N     1 
ATOM   9227  C CA    . ALA G 1 208 ? 44.955  -44.517 59.756  1.00 26.96  ? 209 ALA G CA    1 
ATOM   9228  C C     . ALA G 1 208 ? 43.704  -44.439 60.625  1.00 29.81  ? 209 ALA G C     1 
ATOM   9229  O O     . ALA G 1 208 ? 43.012  -43.423 60.638  1.00 33.24  ? 209 ALA G O     1 
ATOM   9230  C CB    . ALA G 1 208 ? 46.190  -44.098 60.522  1.00 30.04  ? 209 ALA G CB    1 
ATOM   9231  N N     . ASN G 1 209 ? 43.427  -45.531 61.346  1.00 32.18  ? 210 ASN G N     1 
ATOM   9232  C CA    . ASN G 1 209 ? 42.272  -45.607 62.223  1.00 31.09  ? 210 ASN G CA    1 
ATOM   9233  C C     . ASN G 1 209 ? 42.740  -45.606 63.676  1.00 32.37  ? 210 ASN G C     1 
ATOM   9234  O O     . ASN G 1 209 ? 41.930  -45.482 64.592  1.00 33.87  ? 210 ASN G O     1 
ATOM   9235  C CB    . ASN G 1 209 ? 41.418  -46.833 61.917  1.00 31.42  ? 210 ASN G CB    1 
ATOM   9236  C CG    . ASN G 1 209 ? 40.898  -46.831 60.498  1.00 33.52  ? 210 ASN G CG    1 
ATOM   9237  O OD1   . ASN G 1 209 ? 40.168  -45.916 60.103  1.00 37.81  ? 210 ASN G OD1   1 
ATOM   9238  N ND2   . ASN G 1 209 ? 41.252  -47.845 59.723  1.00 35.34  ? 210 ASN G ND2   1 
ATOM   9239  N N     . LEU G 1 210 ? 44.055  -45.748 63.873  1.00 30.56  ? 211 LEU G N     1 
ATOM   9240  C CA    . LEU G 1 210 ? 44.632  -45.778 65.208  1.00 32.18  ? 211 LEU G CA    1 
ATOM   9241  C C     . LEU G 1 210 ? 45.697  -44.690 65.324  1.00 32.47  ? 211 LEU G C     1 
ATOM   9242  O O     . LEU G 1 210 ? 46.320  -44.315 64.334  1.00 31.59  ? 211 LEU G O     1 
ATOM   9243  C CB    . LEU G 1 210 ? 45.207  -47.164 65.499  1.00 32.00  ? 211 LEU G CB    1 
ATOM   9244  C CG    . LEU G 1 210 ? 44.199  -48.318 65.521  1.00 35.52  ? 211 LEU G CG    1 
ATOM   9245  C CD1   . LEU G 1 210 ? 44.871  -49.620 65.922  1.00 37.21  ? 211 LEU G CD1   1 
ATOM   9246  C CD2   . LEU G 1 210 ? 43.036  -48.008 66.448  1.00 38.75  ? 211 LEU G CD2   1 
ATOM   9247  N N     . PRO G 1 211 ? 45.938  -44.158 66.544  1.00 31.69  ? 212 PRO G N     1 
ATOM   9248  C CA    . PRO G 1 211 ? 46.905  -43.075 66.741  1.00 34.75  ? 212 PRO G CA    1 
ATOM   9249  C C     . PRO G 1 211 ? 48.362  -43.531 66.729  1.00 38.10  ? 212 PRO G C     1 
ATOM   9250  O O     . PRO G 1 211 ? 49.273  -42.709 66.799  1.00 42.83  ? 212 PRO G O     1 
ATOM   9251  C CB    . PRO G 1 211 ? 46.482  -42.527 68.114  1.00 34.93  ? 212 PRO G CB    1 
ATOM   9252  C CG    . PRO G 1 211 ? 46.000  -43.755 68.856  1.00 31.08  ? 212 PRO G CG    1 
ATOM   9253  C CD    . PRO G 1 211 ? 45.280  -44.571 67.794  1.00 33.45  ? 212 PRO G CD    1 
ATOM   9254  N N     . ILE G 1 212 ? 48.567  -44.850 66.656  1.00 38.18  ? 213 ILE G N     1 
ATOM   9255  C CA    . ILE G 1 212 ? 49.903  -45.420 66.586  1.00 37.05  ? 213 ILE G CA    1 
ATOM   9256  C C     . ILE G 1 212 ? 50.156  -45.910 65.164  1.00 37.93  ? 213 ILE G C     1 
ATOM   9257  O O     . ILE G 1 212 ? 51.239  -46.400 64.855  1.00 38.84  ? 213 ILE G O     1 
ATOM   9258  C CB    . ILE G 1 212 ? 50.072  -46.552 67.616  1.00 40.02  ? 213 ILE G CB    1 
ATOM   9259  C CG1   . ILE G 1 212 ? 48.983  -47.619 67.469  1.00 44.14  ? 213 ILE G CG1   1 
ATOM   9260  C CG2   . ILE G 1 212 ? 50.122  -45.993 69.038  1.00 41.71  ? 213 ILE G CG2   1 
ATOM   9261  C CD1   . ILE G 1 212 ? 48.951  -48.294 66.110  1.00 44.92  ? 213 ILE G CD1   1 
ATOM   9262  N N     . GLN G 1 213 ? 49.142  -45.757 64.306  1.00 39.06  ? 214 GLN G N     1 
ATOM   9263  C CA    . GLN G 1 213 ? 49.192  -46.267 62.947  1.00 40.56  ? 214 GLN G CA    1 
ATOM   9264  C C     . GLN G 1 213 ? 49.577  -45.141 61.993  1.00 40.63  ? 214 GLN G C     1 
ATOM   9265  O O     . GLN G 1 213 ? 49.048  -44.036 62.082  1.00 40.98  ? 214 GLN G O     1 
ATOM   9266  C CB    . GLN G 1 213 ? 47.831  -46.857 62.572  1.00 42.34  ? 214 GLN G CB    1 
ATOM   9267  C CG    . GLN G 1 213 ? 47.767  -47.435 61.163  1.00 42.99  ? 214 GLN G CG    1 
ATOM   9268  C CD    . GLN G 1 213 ? 46.363  -47.806 60.740  1.00 39.75  ? 214 GLN G CD    1 
ATOM   9269  O OE1   . GLN G 1 213 ? 45.397  -47.639 61.493  1.00 40.44  ? 214 GLN G OE1   1 
ATOM   9270  N NE2   . GLN G 1 213 ? 46.234  -48.306 59.520  1.00 37.15  ? 214 GLN G NE2   1 
ATOM   9271  N N     . ALA G 1 214 ? 50.513  -45.439 61.086  1.00 38.47  ? 215 ALA G N     1 
ATOM   9272  C CA    . ALA G 1 214 ? 50.881  -44.515 60.028  1.00 41.47  ? 215 ALA G CA    1 
ATOM   9273  C C     . ALA G 1 214 ? 49.964  -44.738 58.829  1.00 36.76  ? 215 ALA G C     1 
ATOM   9274  O O     . ALA G 1 214 ? 49.559  -45.865 58.555  1.00 37.68  ? 215 ALA G O     1 
ATOM   9275  C CB    . ALA G 1 214 ? 52.336  -44.704 59.656  1.00 47.87  ? 215 ALA G CB    1 
ATOM   9276  N N     . PRO G 1 215 ? 49.605  -43.673 58.079  1.00 37.30  ? 216 PRO G N     1 
ATOM   9277  C CA    . PRO G 1 215 ? 48.739  -43.821 56.910  1.00 36.93  ? 216 PRO G CA    1 
ATOM   9278  C C     . PRO G 1 215 ? 49.443  -44.587 55.795  1.00 34.61  ? 216 PRO G C     1 
ATOM   9279  O O     . PRO G 1 215 ? 50.667  -44.695 55.786  1.00 32.82  ? 216 PRO G O     1 
ATOM   9280  C CB    . PRO G 1 215 ? 48.423  -42.366 56.521  1.00 37.24  ? 216 PRO G CB    1 
ATOM   9281  C CG    . PRO G 1 215 ? 49.622  -41.584 57.021  1.00 38.29  ? 216 PRO G CG    1 
ATOM   9282  C CD    . PRO G 1 215 ? 50.031  -42.284 58.307  1.00 39.98  ? 216 PRO G CD    1 
ATOM   9283  N N     . ARG G 1 216 ? 48.649  -45.133 54.868  1.00 34.38  ? 217 ARG G N     1 
ATOM   9284  C CA    . ARG G 1 216 ? 49.188  -45.805 53.699  1.00 33.08  ? 217 ARG G CA    1 
ATOM   9285  C C     . ARG G 1 216 ? 49.249  -44.812 52.544  1.00 29.54  ? 217 ARG G C     1 
ATOM   9286  O O     . ARG G 1 216 ? 48.227  -44.271 52.131  1.00 26.69  ? 217 ARG G O     1 
ATOM   9287  C CB    . ARG G 1 216 ? 48.342  -47.018 53.301  1.00 32.49  ? 217 ARG G CB    1 
ATOM   9288  C CG    . ARG G 1 216 ? 48.893  -47.761 52.092  1.00 35.76  ? 217 ARG G CG    1 
ATOM   9289  C CD    . ARG G 1 216 ? 47.963  -48.857 51.602  1.00 35.67  ? 217 ARG G CD    1 
ATOM   9290  N NE    . ARG G 1 216 ? 48.579  -49.672 50.549  1.00 34.80  ? 217 ARG G NE    1 
ATOM   9291  C CZ    . ARG G 1 216 ? 47.965  -50.656 49.903  1.00 31.99  ? 217 ARG G CZ    1 
ATOM   9292  N NH1   . ARG G 1 216 ? 46.696  -50.919 50.156  1.00 26.40  ? 217 ARG G NH1   1 
ATOM   9293  N NH2   . ARG G 1 216 ? 48.619  -51.363 48.998  1.00 29.75  ? 217 ARG G NH2   1 
ATOM   9294  N N     . ILE G 1 217 ? 50.464  -44.576 52.040  1.00 32.75  ? 218 ILE G N     1 
ATOM   9295  C CA    . ILE G 1 217 ? 50.674  -43.680 50.916  1.00 35.86  ? 218 ILE G CA    1 
ATOM   9296  C C     . ILE G 1 217 ? 51.611  -44.363 49.924  1.00 39.40  ? 218 ILE G C     1 
ATOM   9297  O O     . ILE G 1 217 ? 52.803  -44.066 49.881  1.00 45.87  ? 218 ILE G O     1 
ATOM   9298  C CB    . ILE G 1 217 ? 51.224  -42.322 51.392  1.00 33.65  ? 218 ILE G CB    1 
ATOM   9299  C CG1   . ILE G 1 217 ? 50.363  -41.723 52.505  1.00 30.51  ? 218 ILE G CG1   1 
ATOM   9300  C CG2   . ILE G 1 217 ? 51.383  -41.355 50.218  1.00 32.16  ? 218 ILE G CG2   1 
ATOM   9301  C CD1   . ILE G 1 217 ? 50.856  -40.381 53.016  1.00 31.35  ? 218 ILE G CD1   1 
ATOM   9302  N N     . GLU G 1 218 ? 51.050  -45.283 49.132  1.00 38.61  ? 219 GLU G N     1 
ATOM   9303  C CA    . GLU G 1 218 ? 51.827  -46.073 48.193  1.00 38.61  ? 219 GLU G CA    1 
ATOM   9304  C C     . GLU G 1 218 ? 51.760  -45.437 46.808  1.00 34.15  ? 219 GLU G C     1 
ATOM   9305  O O     . GLU G 1 218 ? 50.696  -45.381 46.196  1.00 31.40  ? 219 GLU G O     1 
ATOM   9306  C CB    . GLU G 1 218 ? 51.310  -47.512 48.155  1.00 42.61  ? 219 GLU G CB    1 
ATOM   9307  C CG    . GLU G 1 218 ? 52.025  -48.386 47.130  1.00 47.79  ? 219 GLU G CG    1 
ATOM   9308  C CD    . GLU G 1 218 ? 51.582  -49.839 47.137  1.00 50.88  ? 219 GLU G CD    1 
ATOM   9309  O OE1   . GLU G 1 218 ? 50.742  -50.196 47.989  1.00 59.37  ? 219 GLU G OE1   1 
ATOM   9310  O OE2   . GLU G 1 218 ? 52.075  -50.612 46.290  1.00 64.85  ? 219 GLU G OE2   1 
ATOM   9311  N N     . ARG G 1 219 ? 52.918  -44.971 46.327  1.00 33.12  ? 220 ARG G N     1 
ATOM   9312  C CA    . ARG G 1 219 ? 53.032  -44.385 45.002  1.00 34.06  ? 220 ARG G CA    1 
ATOM   9313  C C     . ARG G 1 219 ? 53.463  -45.466 44.016  1.00 33.33  ? 220 ARG G C     1 
ATOM   9314  O O     . ARG G 1 219 ? 54.352  -46.262 44.312  1.00 36.08  ? 220 ARG G O     1 
ATOM   9315  C CB    . ARG G 1 219 ? 54.043  -43.232 45.017  1.00 33.66  ? 220 ARG G CB    1 
ATOM   9316  C CG    . ARG G 1 219 ? 53.699  -42.105 45.981  1.00 37.13  ? 220 ARG G CG    1 
ATOM   9317  C CD    . ARG G 1 219 ? 54.825  -41.089 46.103  1.00 38.98  ? 220 ARG G CD    1 
ATOM   9318  N NE    . ARG G 1 219 ? 54.509  -40.030 47.068  1.00 43.37  ? 220 ARG G NE    1 
ATOM   9319  C CZ    . ARG G 1 219 ? 53.587  -39.092 46.887  1.00 47.98  ? 220 ARG G CZ    1 
ATOM   9320  N NH1   . ARG G 1 219 ? 52.926  -39.025 45.745  1.00 56.21  ? 220 ARG G NH1   1 
ATOM   9321  N NH2   . ARG G 1 219 ? 53.346  -38.211 47.840  1.00 45.18  ? 220 ARG G NH2   1 
ATOM   9322  N N     . LEU G 1 220 ? 52.827  -45.481 42.841  1.00 31.48  ? 221 LEU G N     1 
ATOM   9323  C CA    . LEU G 1 220 ? 53.134  -46.467 41.819  1.00 31.32  ? 221 LEU G CA    1 
ATOM   9324  C C     . LEU G 1 220 ? 52.577  -46.000 40.479  1.00 31.45  ? 221 LEU G C     1 
ATOM   9325  O O     . LEU G 1 220 ? 51.660  -45.184 40.432  1.00 35.40  ? 221 LEU G O     1 
ATOM   9326  C CB    . LEU G 1 220 ? 52.552  -47.823 42.216  1.00 34.32  ? 221 LEU G CB    1 
ATOM   9327  C CG    . LEU G 1 220 ? 51.025  -47.936 42.166  1.00 33.40  ? 221 LEU G CG    1 
ATOM   9328  C CD1   . LEU G 1 220 ? 50.572  -49.333 42.550  1.00 35.24  ? 221 LEU G CD1   1 
ATOM   9329  C CD2   . LEU G 1 220 ? 50.368  -46.897 43.058  1.00 35.91  ? 221 LEU G CD2   1 
ATOM   9330  N N     . PRO G 1 221 ? 53.116  -46.509 39.349  1.00 30.36  ? 222 PRO G N     1 
ATOM   9331  C CA    . PRO G 1 221 ? 52.576  -46.187 38.029  1.00 30.89  ? 222 PRO G CA    1 
ATOM   9332  C C     . PRO G 1 221 ? 51.169  -46.753 37.853  1.00 31.67  ? 222 PRO G C     1 
ATOM   9333  O O     . PRO G 1 221 ? 50.865  -47.839 38.340  1.00 31.80  ? 222 PRO G O     1 
ATOM   9334  C CB    . PRO G 1 221 ? 53.594  -46.815 37.058  1.00 31.93  ? 222 PRO G CB    1 
ATOM   9335  C CG    . PRO G 1 221 ? 54.242  -47.925 37.863  1.00 32.50  ? 222 PRO G CG    1 
ATOM   9336  C CD    . PRO G 1 221 ? 54.277  -47.409 39.291  1.00 30.88  ? 222 PRO G CD    1 
ATOM   9337  N N     . LEU G 1 222 ? 50.323  -45.997 37.147  1.00 30.15  ? 223 LEU G N     1 
ATOM   9338  C CA    . LEU G 1 222 ? 48.929  -46.359 36.953  1.00 32.63  ? 223 LEU G CA    1 
ATOM   9339  C C     . LEU G 1 222 ? 48.830  -47.781 36.407  1.00 33.25  ? 223 LEU G C     1 
ATOM   9340  O O     . LEU G 1 222 ? 47.820  -48.454 36.601  1.00 34.47  ? 223 LEU G O     1 
ATOM   9341  C CB    . LEU G 1 222 ? 48.282  -45.351 36.006  1.00 36.28  ? 223 LEU G CB    1 
ATOM   9342  C CG    . LEU G 1 222 ? 46.834  -45.645 35.600  1.00 40.28  ? 223 LEU G CG    1 
ATOM   9343  C CD1   . LEU G 1 222 ? 45.900  -45.528 36.790  1.00 43.10  ? 223 LEU G CD1   1 
ATOM   9344  C CD2   . LEU G 1 222 ? 46.390  -44.729 34.474  1.00 43.40  ? 223 LEU G CD2   1 
ATOM   9345  N N     . ALA G 1 223 ? 49.890  -48.227 35.727  1.00 35.52  ? 224 ALA G N     1 
ATOM   9346  C CA    . ALA G 1 223 ? 49.870  -49.493 35.012  1.00 38.36  ? 224 ALA G CA    1 
ATOM   9347  C C     . ALA G 1 223 ? 49.906  -50.664 35.992  1.00 34.54  ? 224 ALA G C     1 
ATOM   9348  O O     . ALA G 1 223 ? 49.419  -51.748 35.679  1.00 38.69  ? 224 ALA G O     1 
ATOM   9349  C CB    . ALA G 1 223 ? 51.031  -49.551 34.043  1.00 43.11  ? 224 ALA G CB    1 
ATOM   9350  N N     . ASN G 1 224 ? 50.486  -50.434 37.175  1.00 34.35  ? 225 ASN G N     1 
ATOM   9351  C CA    . ASN G 1 224 ? 50.706  -51.497 38.144  1.00 33.88  ? 225 ASN G CA    1 
ATOM   9352  C C     . ASN G 1 224 ? 49.500  -51.625 39.072  1.00 32.81  ? 225 ASN G C     1 
ATOM   9353  O O     . ASN G 1 224 ? 49.457  -52.516 39.916  1.00 32.57  ? 225 ASN G O     1 
ATOM   9354  C CB    . ASN G 1 224 ? 51.982  -51.268 38.947  1.00 36.83  ? 225 ASN G CB    1 
ATOM   9355  C CG    . ASN G 1 224 ? 53.219  -51.324 38.084  1.00 36.73  ? 225 ASN G CG    1 
ATOM   9356  O OD1   . ASN G 1 224 ? 53.122  -51.532 36.870  1.00 40.90  ? 225 ASN G OD1   1 
ATOM   9357  N ND2   . ASN G 1 224 ? 54.386  -51.143 38.686  1.00 40.10  ? 225 ASN G ND2   1 
ATOM   9358  N N     . LEU G 1 225 ? 48.522  -50.730 38.904  1.00 33.92  ? 226 LEU G N     1 
ATOM   9359  C CA    . LEU G 1 225 ? 47.352  -50.708 39.767  1.00 31.65  ? 226 LEU G CA    1 
ATOM   9360  C C     . LEU G 1 225 ? 46.781  -52.119 39.889  1.00 34.69  ? 226 LEU G C     1 
ATOM   9361  O O     . LEU G 1 225 ? 46.547  -52.604 40.994  1.00 31.85  ? 226 LEU G O     1 
ATOM   9362  C CB    . LEU G 1 225 ? 46.315  -49.730 39.216  1.00 33.51  ? 226 LEU G CB    1 
ATOM   9363  C CG    . LEU G 1 225 ? 45.010  -49.620 40.012  1.00 34.61  ? 226 LEU G CG    1 
ATOM   9364  C CD1   . LEU G 1 225 ? 45.264  -49.090 41.413  1.00 37.53  ? 226 LEU G CD1   1 
ATOM   9365  C CD2   . LEU G 1 225 ? 44.003  -48.747 39.283  1.00 34.46  ? 226 LEU G CD2   1 
ATOM   9366  N N     . PRO G 1 226 ? 46.540  -52.820 38.758  1.00 35.55  ? 227 PRO G N     1 
ATOM   9367  C CA    . PRO G 1 226 ? 45.877  -54.127 38.787  1.00 36.52  ? 227 PRO G CA    1 
ATOM   9368  C C     . PRO G 1 226 ? 46.557  -55.160 39.685  1.00 35.57  ? 227 PRO G C     1 
ATOM   9369  O O     . PRO G 1 226 ? 45.915  -56.106 40.133  1.00 39.43  ? 227 PRO G O     1 
ATOM   9370  C CB    . PRO G 1 226 ? 45.892  -54.554 37.303  1.00 35.23  ? 227 PRO G CB    1 
ATOM   9371  C CG    . PRO G 1 226 ? 45.977  -53.249 36.540  1.00 35.35  ? 227 PRO G CG    1 
ATOM   9372  C CD    . PRO G 1 226 ? 46.869  -52.374 37.397  1.00 35.08  ? 227 PRO G CD    1 
ATOM   9373  N N     . GLN G 1 227 ? 47.858  -54.973 39.935  1.00 39.90  ? 228 GLN G N     1 
ATOM   9374  C CA    . GLN G 1 227 ? 48.632  -55.923 40.721  1.00 42.02  ? 228 GLN G CA    1 
ATOM   9375  C C     . GLN G 1 227 ? 48.726  -55.452 42.170  1.00 42.96  ? 228 GLN G C     1 
ATOM   9376  O O     . GLN G 1 227 ? 49.168  -56.200 43.040  1.00 39.81  ? 228 GLN G O     1 
ATOM   9377  C CB    . GLN G 1 227 ? 50.036  -56.113 40.145  1.00 45.84  ? 228 GLN G CB    1 
ATOM   9378  C CG    . GLN G 1 227 ? 50.078  -56.878 38.826  1.00 49.09  ? 228 GLN G CG    1 
ATOM   9379  C CD    . GLN G 1 227 ? 49.570  -56.075 37.649  1.00 49.55  ? 228 GLN G CD    1 
ATOM   9380  O OE1   . GLN G 1 227 ? 50.121  -55.026 37.297  1.00 53.19  ? 228 GLN G OE1   1 
ATOM   9381  N NE2   . GLN G 1 227 ? 48.517  -56.571 37.015  1.00 55.39  ? 228 GLN G NE2   1 
ATOM   9382  N N     . ALA G 1 228 ? 48.302  -54.209 42.419  1.00 41.51  ? 229 ALA G N     1 
ATOM   9383  C CA    . ALA G 1 228 ? 48.429  -53.598 43.732  1.00 39.69  ? 229 ALA G CA    1 
ATOM   9384  C C     . ALA G 1 228 ? 47.520  -54.304 44.735  1.00 36.03  ? 229 ALA G C     1 
ATOM   9385  O O     . ALA G 1 228 ? 46.516  -54.904 44.359  1.00 36.24  ? 229 ALA G O     1 
ATOM   9386  C CB    . ALA G 1 228 ? 48.111  -52.122 43.646  1.00 43.51  ? 229 ALA G CB    1 
ATOM   9387  N N     . HIS G 1 229 ? 47.893  -54.217 46.017  1.00 38.66  ? 230 HIS G N     1 
ATOM   9388  C CA    . HIS G 1 229 ? 47.099  -54.767 47.103  1.00 42.98  ? 230 HIS G CA    1 
ATOM   9389  C C     . HIS G 1 229 ? 46.098  -53.715 47.575  1.00 43.86  ? 230 HIS G C     1 
ATOM   9390  O O     . HIS G 1 229 ? 46.483  -52.720 48.185  1.00 48.96  ? 230 HIS G O     1 
ATOM   9391  C CB    . HIS G 1 229 ? 48.005  -55.211 48.257  1.00 45.71  ? 230 HIS G CB    1 
ATOM   9392  C CG    . HIS G 1 229 ? 47.277  -55.872 49.380  1.00 54.40  ? 230 HIS G CG    1 
ATOM   9393  N ND1   . HIS G 1 229 ? 47.241  -57.240 49.545  1.00 59.28  ? 230 HIS G ND1   1 
ATOM   9394  C CD2   . HIS G 1 229 ? 46.580  -55.358 50.402  1.00 57.37  ? 230 HIS G CD2   1 
ATOM   9395  C CE1   . HIS G 1 229 ? 46.533  -57.531 50.627  1.00 61.04  ? 230 HIS G CE1   1 
ATOM   9396  N NE2   . HIS G 1 229 ? 46.120  -56.403 51.161  1.00 62.67  ? 230 HIS G NE2   1 
ATOM   9397  N N     . LEU G 1 230 ? 44.813  -53.949 47.292  1.00 36.73  ? 231 LEU G N     1 
ATOM   9398  C CA    . LEU G 1 230 ? 43.769  -52.999 47.640  1.00 34.70  ? 231 LEU G CA    1 
ATOM   9399  C C     . LEU G 1 230 ? 42.942  -53.546 48.799  1.00 32.76  ? 231 LEU G C     1 
ATOM   9400  O O     . LEU G 1 230 ? 42.733  -54.752 48.908  1.00 33.79  ? 231 LEU G O     1 
ATOM   9401  C CB    . LEU G 1 230 ? 42.895  -52.710 46.420  1.00 31.99  ? 231 LEU G CB    1 
ATOM   9402  C CG    . LEU G 1 230 ? 43.614  -52.096 45.215  1.00 32.64  ? 231 LEU G CG    1 
ATOM   9403  C CD1   . LEU G 1 230 ? 42.636  -51.803 44.088  1.00 32.92  ? 231 LEU G CD1   1 
ATOM   9404  C CD2   . LEU G 1 230 ? 44.365  -50.839 45.618  1.00 29.55  ? 231 LEU G CD2   1 
ATOM   9405  N N     . MET G 1 231 ? 42.488  -52.634 49.664  1.00 32.79  ? 232 MET G N     1 
ATOM   9406  C CA    . MET G 1 231 ? 41.598  -52.970 50.762  1.00 30.32  ? 232 MET G CA    1 
ATOM   9407  C C     . MET G 1 231 ? 40.330  -52.129 50.644  1.00 31.70  ? 232 MET G C     1 
ATOM   9408  O O     . MET G 1 231 ? 40.328  -51.093 49.985  1.00 34.09  ? 232 MET G O     1 
ATOM   9409  C CB    . MET G 1 231 ? 42.270  -52.709 52.115  1.00 33.60  ? 232 MET G CB    1 
ATOM   9410  C CG    . MET G 1 231 ? 43.447  -53.619 52.403  1.00 38.62  ? 232 MET G CG    1 
ATOM   9411  S SD    . MET G 1 231 ? 42.995  -55.364 52.345  1.00 50.78  ? 232 MET G SD    1 
ATOM   9412  C CE    . MET G 1 231 ? 41.643  -55.385 53.531  1.00 55.99  ? 232 MET G CE    1 
ATOM   9413  N N     . PRO G 1 232 ? 39.211  -52.554 51.274  1.00 31.56  ? 233 PRO G N     1 
ATOM   9414  C CA    . PRO G 1 232 ? 37.954  -51.809 51.194  1.00 33.01  ? 233 PRO G CA    1 
ATOM   9415  C C     . PRO G 1 232 ? 38.109  -50.315 51.472  1.00 33.25  ? 233 PRO G C     1 
ATOM   9416  O O     . PRO G 1 232 ? 37.388  -49.498 50.905  1.00 35.84  ? 233 PRO G O     1 
ATOM   9417  C CB    . PRO G 1 232 ? 37.082  -52.505 52.256  1.00 32.13  ? 233 PRO G CB    1 
ATOM   9418  C CG    . PRO G 1 232 ? 37.608  -53.924 52.293  1.00 31.95  ? 233 PRO G CG    1 
ATOM   9419  C CD    . PRO G 1 232 ? 39.102  -53.783 52.074  1.00 31.40  ? 233 PRO G CD    1 
ATOM   9420  N N     . ILE G 1 233 ? 39.058  -49.973 52.350  1.00 31.90  ? 234 ILE G N     1 
ATOM   9421  C CA    . ILE G 1 233 ? 39.206  -48.608 52.830  1.00 32.63  ? 234 ILE G CA    1 
ATOM   9422  C C     . ILE G 1 233 ? 40.200  -47.855 51.948  1.00 32.19  ? 234 ILE G C     1 
ATOM   9423  O O     . ILE G 1 233 ? 40.593  -46.737 52.272  1.00 33.16  ? 234 ILE G O     1 
ATOM   9424  C CB    . ILE G 1 233 ? 39.641  -48.594 54.307  1.00 34.59  ? 234 ILE G CB    1 
ATOM   9425  C CG1   . ILE G 1 233 ? 41.017  -49.230 54.495  1.00 34.65  ? 234 ILE G CG1   1 
ATOM   9426  C CG2   . ILE G 1 233 ? 38.585  -49.255 55.193  1.00 37.83  ? 234 ILE G CG2   1 
ATOM   9427  C CD1   . ILE G 1 233 ? 41.536  -49.175 55.920  1.00 34.42  ? 234 ILE G CD1   1 
ATOM   9428  N N     . SER G 1 234 ? 40.595  -48.473 50.831  1.00 29.59  ? 235 SER G N     1 
ATOM   9429  C CA    . SER G 1 234 ? 41.566  -47.873 49.931  1.00 28.94  ? 235 SER G CA    1 
ATOM   9430  C C     . SER G 1 234 ? 40.895  -46.809 49.066  1.00 25.95  ? 235 SER G C     1 
ATOM   9431  O O     . SER G 1 234 ? 39.794  -47.013 48.559  1.00 20.57  ? 235 SER G O     1 
ATOM   9432  C CB    . SER G 1 234 ? 42.244  -48.917 49.080  1.00 31.23  ? 235 SER G CB    1 
ATOM   9433  O OG    . SER G 1 234 ? 43.076  -49.760 49.865  1.00 29.42  ? 235 SER G OG    1 
ATOM   9434  N N     . THR G 1 235 ? 41.573  -45.665 48.927  1.00 26.01  ? 236 THR G N     1 
ATOM   9435  C CA    . THR G 1 235 ? 41.159  -44.620 48.007  1.00 25.02  ? 236 THR G CA    1 
ATOM   9436  C C     . THR G 1 235 ? 42.291  -44.378 47.014  1.00 23.54  ? 236 THR G C     1 
ATOM   9437  O O     . THR G 1 235 ? 43.461  -44.402 47.388  1.00 26.22  ? 236 THR G O     1 
ATOM   9438  C CB    . THR G 1 235 ? 40.806  -43.353 48.786  1.00 28.05  ? 236 THR G CB    1 
ATOM   9439  O OG1   . THR G 1 235 ? 39.686  -43.703 49.594  1.00 28.91  ? 236 THR G OG1   1 
ATOM   9440  C CG2   . THR G 1 235 ? 40.452  -42.188 47.879  1.00 28.45  ? 236 THR G CG2   1 
ATOM   9441  N N     . LEU G 1 236 ? 41.928  -44.157 45.746  1.00 22.35  ? 237 LEU G N     1 
ATOM   9442  C CA    . LEU G 1 236 ? 42.907  -43.946 44.693  1.00 21.40  ? 237 LEU G CA    1 
ATOM   9443  C C     . LEU G 1 236 ? 43.012  -42.456 44.379  1.00 21.70  ? 237 LEU G C     1 
ATOM   9444  O O     . LEU G 1 236 ? 42.027  -41.827 44.002  1.00 24.20  ? 237 LEU G O     1 
ATOM   9445  C CB    . LEU G 1 236 ? 42.516  -44.743 43.451  1.00 20.83  ? 237 LEU G CB    1 
ATOM   9446  C CG    . LEU G 1 236 ? 43.428  -44.563 42.233  1.00 21.53  ? 237 LEU G CG    1 
ATOM   9447  C CD1   . LEU G 1 236 ? 44.802  -45.156 42.500  1.00 20.02  ? 237 LEU G CD1   1 
ATOM   9448  C CD2   . LEU G 1 236 ? 42.807  -45.169 40.984  1.00 23.13  ? 237 LEU G CD2   1 
ATOM   9449  N N     . LEU G 1 237 ? 44.223  -41.910 44.530  1.00 22.45  ? 238 LEU G N     1 
ATOM   9450  C CA    A LEU G 1 237 ? 44.491  -40.517 44.210  0.70 21.04  ? 238 LEU G CA    1 
ATOM   9451  C CA    B LEU G 1 237 ? 44.485  -40.517 44.207  0.30 21.24  ? 238 LEU G CA    1 
ATOM   9452  C C     . LEU G 1 237 ? 45.252  -40.446 42.890  1.00 20.52  ? 238 LEU G C     1 
ATOM   9453  O O     . LEU G 1 237 ? 46.328  -41.024 42.757  1.00 21.08  ? 238 LEU G O     1 
ATOM   9454  C CB    A LEU G 1 237 ? 45.288  -39.863 45.336  0.70 21.47  ? 238 LEU G CB    1 
ATOM   9455  C CB    B LEU G 1 237 ? 45.261  -39.848 45.340  0.30 21.49  ? 238 LEU G CB    1 
ATOM   9456  C CG    A LEU G 1 237 ? 45.838  -38.464 45.037  0.70 21.50  ? 238 LEU G CG    1 
ATOM   9457  C CG    B LEU G 1 237 ? 45.454  -38.333 45.212  0.30 21.45  ? 238 LEU G CG    1 
ATOM   9458  C CD1   A LEU G 1 237 ? 44.725  -37.431 44.998  0.70 20.63  ? 238 LEU G CD1   1 
ATOM   9459  C CD1   B LEU G 1 237 ? 46.403  -37.817 46.280  0.30 22.25  ? 238 LEU G CD1   1 
ATOM   9460  C CD2   A LEU G 1 237 ? 46.904  -38.073 46.045  0.70 22.93  ? 238 LEU G CD2   1 
ATOM   9461  C CD2   B LEU G 1 237 ? 45.948  -37.954 43.826  0.30 20.96  ? 238 LEU G CD2   1 
ATOM   9462  N N     . ILE G 1 238 ? 44.683  -39.722 41.924  1.00 20.05  ? 239 ILE G N     1 
ATOM   9463  C CA    . ILE G 1 238 ? 45.299  -39.558 40.620  1.00 20.80  ? 239 ILE G CA    1 
ATOM   9464  C C     . ILE G 1 238 ? 45.680  -38.091 40.445  1.00 21.85  ? 239 ILE G C     1 
ATOM   9465  O O     . ILE G 1 238 ? 44.848  -37.271 40.064  1.00 24.50  ? 239 ILE G O     1 
ATOM   9466  C CB    . ILE G 1 238 ? 44.350  -40.051 39.513  1.00 20.33  ? 239 ILE G CB    1 
ATOM   9467  C CG1   . ILE G 1 238 ? 43.974  -41.520 39.719  1.00 21.99  ? 239 ILE G CG1   1 
ATOM   9468  C CG2   . ILE G 1 238 ? 44.945  -39.806 38.127  1.00 20.94  ? 239 ILE G CG2   1 
ATOM   9469  C CD1   . ILE G 1 238 ? 43.040  -42.078 38.660  1.00 22.58  ? 239 ILE G CD1   1 
ATOM   9470  N N     . PRO G 1 239 ? 46.945  -37.715 40.744  1.00 23.64  ? 240 PRO G N     1 
ATOM   9471  C CA    . PRO G 1 239 ? 47.375  -36.319 40.652  1.00 23.12  ? 240 PRO G CA    1 
ATOM   9472  C C     . PRO G 1 239 ? 47.188  -35.755 39.247  1.00 24.80  ? 240 PRO G C     1 
ATOM   9473  O O     . PRO G 1 239 ? 46.889  -36.493 38.310  1.00 26.29  ? 240 PRO G O     1 
ATOM   9474  C CB    . PRO G 1 239 ? 48.860  -36.368 41.073  1.00 25.28  ? 240 PRO G CB    1 
ATOM   9475  C CG    . PRO G 1 239 ? 48.984  -37.652 41.870  1.00 25.00  ? 240 PRO G CG    1 
ATOM   9476  C CD    . PRO G 1 239 ? 48.015  -38.612 41.203  1.00 23.35  ? 240 PRO G CD    1 
ATOM   9477  N N     . PRO G 1 240 ? 47.352  -34.425 39.062  1.00 25.92  ? 241 PRO G N     1 
ATOM   9478  C CA    . PRO G 1 240 ? 47.178  -33.799 37.751  1.00 27.74  ? 241 PRO G CA    1 
ATOM   9479  C C     . PRO G 1 240 ? 48.126  -34.379 36.705  1.00 27.95  ? 241 PRO G C     1 
ATOM   9480  O O     . PRO G 1 240 ? 49.303  -34.599 36.982  1.00 28.03  ? 241 PRO G O     1 
ATOM   9481  C CB    . PRO G 1 240 ? 47.457  -32.304 38.020  1.00 26.55  ? 241 PRO G CB    1 
ATOM   9482  C CG    . PRO G 1 240 ? 47.240  -32.141 39.512  1.00 26.20  ? 241 PRO G CG    1 
ATOM   9483  C CD    . PRO G 1 240 ? 47.690  -33.458 40.116  1.00 28.14  ? 241 PRO G CD    1 
ATOM   9484  N N     . ALA G 1 241 ? 47.596  -34.608 35.499  1.00 31.79  ? 242 ALA G N     1 
ATOM   9485  C CA    . ALA G 1 241 ? 48.392  -35.100 34.387  1.00 32.42  ? 242 ALA G CA    1 
ATOM   9486  C C     . ALA G 1 241 ? 48.890  -33.925 33.551  1.00 35.57  ? 242 ALA G C     1 
ATOM   9487  O O     . ALA G 1 241 ? 49.775  -34.085 32.712  1.00 38.99  ? 242 ALA G O     1 
ATOM   9488  C CB    . ALA G 1 241 ? 47.576  -36.065 33.556  1.00 35.03  ? 242 ALA G CB    1 
ATOM   9489  N N     . LYS G 1 242 ? 48.304  -32.746 33.788  1.00 33.77  ? 243 LYS G N     1 
ATOM   9490  C CA    . LYS G 1 242 ? 48.680  -31.538 33.073  1.00 41.29  ? 243 LYS G CA    1 
ATOM   9491  C C     . LYS G 1 242 ? 48.675  -30.358 34.041  1.00 48.27  ? 243 LYS G C     1 
ATOM   9492  O O     . LYS G 1 242 ? 47.980  -30.384 35.054  1.00 50.88  ? 243 LYS G O     1 
ATOM   9493  C CB    . LYS G 1 242 ? 47.714  -31.281 31.912  1.00 43.31  ? 243 LYS G CB    1 
ATOM   9494  C CG    . LYS G 1 242 ? 47.549  -32.442 30.942  1.00 47.41  ? 243 LYS G CG    1 
ATOM   9495  C CD    . LYS G 1 242 ? 46.536  -32.186 29.834  1.00 51.73  ? 243 LYS G CD    1 
ATOM   9496  C CE    . LYS G 1 242 ? 46.908  -31.024 28.969  1.00 59.08  ? 243 LYS G CE    1 
ATOM   9497  N NZ    . LYS G 1 242 ? 45.950  -30.838 27.876  1.00 58.31  ? 243 LYS G NZ    1 
ATOM   9498  N N     . LYS G 1 243 ? 49.459  -29.326 33.711  1.00 48.61  ? 244 LYS G N     1 
ATOM   9499  C CA    . LYS G 1 243 ? 49.507  -28.112 34.509  1.00 53.63  ? 244 LYS G CA    1 
ATOM   9500  C C     . LYS G 1 243 ? 48.438  -27.144 34.011  1.00 50.41  ? 244 LYS G C     1 
ATOM   9501  O O     . LYS G 1 243 ? 47.893  -27.318 32.923  1.00 45.25  ? 244 LYS G O     1 
ATOM   9502  C CB    . LYS G 1 243 ? 50.899  -27.471 34.458  1.00 61.32  ? 244 LYS G CB    1 
ATOM   9503  C CG    . LYS G 1 243 ? 52.005  -28.273 35.133  1.00 68.57  ? 244 LYS G CG    1 
ATOM   9504  C CD    . LYS G 1 243 ? 53.335  -27.535 35.234  1.00 76.26  ? 244 LYS G CD    1 
ATOM   9505  C CE    . LYS G 1 243 ? 53.916  -27.190 33.898  1.00 78.94  ? 244 LYS G CE    1 
ATOM   9506  N NZ    . LYS G 1 243 ? 54.234  -28.389 33.118  1.00 80.13  ? 244 LYS G NZ    1 
ATOM   9507  N N     . LEU G 1 244 ? 48.145  -26.127 34.829  1.00 52.85  ? 245 LEU G N     1 
ATOM   9508  C CA    . LEU G 1 244 ? 47.132  -25.139 34.501  1.00 54.49  ? 245 LEU G CA    1 
ATOM   9509  C C     . LEU G 1 244 ? 47.604  -24.307 33.312  1.00 55.55  ? 245 LEU G C     1 
ATOM   9510  O O     . LEU G 1 244 ? 48.716  -23.785 33.315  1.00 61.25  ? 245 LEU G O     1 
ATOM   9511  C CB    . LEU G 1 244 ? 46.849  -24.259 35.718  1.00 53.74  ? 245 LEU G CB    1 
ATOM   9512  C CG    . LEU G 1 244 ? 46.345  -24.983 36.971  1.00 51.11  ? 245 LEU G CG    1 
ATOM   9513  C CD1   . LEU G 1 244 ? 46.067  -23.992 38.088  1.00 48.90  ? 245 LEU G CD1   1 
ATOM   9514  C CD2   . LEU G 1 244 ? 45.109  -25.810 36.666  1.00 50.81  ? 245 LEU G CD2   1 
ATOM   9515  N N     . GLU G 1 245 ? 46.739  -24.197 32.299  1.00 58.00  ? 246 GLU G N     1 
ATOM   9516  C CA    . GLU G 1 245 ? 47.011  -23.373 31.133  1.00 59.49  ? 246 GLU G CA    1 
ATOM   9517  C C     . GLU G 1 245 ? 46.037  -22.199 31.123  1.00 58.13  ? 246 GLU G C     1 
ATOM   9518  O O     . GLU G 1 245 ? 44.869  -22.354 31.474  1.00 55.02  ? 246 GLU G O     1 
ATOM   9519  C CB    . GLU G 1 245 ? 46.904  -24.205 29.855  1.00 59.67  ? 246 GLU G CB    1 
ATOM   9520  C CG    . GLU G 1 245 ? 47.916  -25.345 29.792  1.00 65.25  ? 246 GLU G CG    1 
ATOM   9521  C CD    . GLU G 1 245 ? 47.833  -26.184 28.529  1.00 68.36  ? 246 GLU G CD    1 
ATOM   9522  O OE1   . GLU G 1 245 ? 48.007  -25.617 27.430  1.00 73.34  ? 246 GLU G OE1   1 
ATOM   9523  O OE2   . GLU G 1 245 ? 47.595  -27.405 28.644  1.00 78.45  ? 246 GLU G OE2   1 
ATOM   9524  N N     . TYR G 1 246 ? 46.534  -21.026 30.720  1.00 50.87  ? 247 TYR G N     1 
ATOM   9525  C CA    . TYR G 1 246 ? 45.744  -19.807 30.750  1.00 51.36  ? 247 TYR G CA    1 
ATOM   9526  C C     . TYR G 1 246 ? 44.545  -19.961 29.819  1.00 43.66  ? 247 TYR G C     1 
ATOM   9527  O O     . TYR G 1 246 ? 44.623  -20.644 28.800  1.00 41.84  ? 247 TYR G O     1 
ATOM   9528  C CB    . TYR G 1 246 ? 46.607  -18.596 30.379  1.00 50.81  ? 247 TYR G CB    1 
ATOM   9529  C CG    . TYR G 1 246 ? 47.744  -18.316 31.353  1.00 54.16  ? 247 TYR G CG    1 
ATOM   9530  C CD1   . TYR G 1 246 ? 47.492  -17.787 32.613  1.00 55.98  ? 247 TYR G CD1   1 
ATOM   9531  C CD2   . TYR G 1 246 ? 49.068  -18.555 31.004  1.00 55.11  ? 247 TYR G CD2   1 
ATOM   9532  C CE1   . TYR G 1 246 ? 48.518  -17.527 33.505  1.00 53.76  ? 247 TYR G CE1   1 
ATOM   9533  C CE2   . TYR G 1 246 ? 50.104  -18.294 31.885  1.00 52.22  ? 247 TYR G CE2   1 
ATOM   9534  C CZ    . TYR G 1 246 ? 49.828  -17.779 33.140  1.00 56.02  ? 247 TYR G CZ    1 
ATOM   9535  O OH    . TYR G 1 246 ? 50.842  -17.520 34.017  1.00 59.53  ? 247 TYR G OH    1 
ATOM   9536  N N     . ASN G 1 247 ? 43.436  -19.316 30.196  1.00 38.95  ? 248 ASN G N     1 
ATOM   9537  C CA    . ASN G 1 247 ? 42.212  -19.343 29.414  1.00 34.26  ? 248 ASN G CA    1 
ATOM   9538  C C     . ASN G 1 247 ? 42.051  -17.997 28.711  1.00 33.73  ? 248 ASN G C     1 
ATOM   9539  O O     . ASN G 1 247 ? 41.303  -17.135 29.168  1.00 34.42  ? 248 ASN G O     1 
ATOM   9540  C CB    . ASN G 1 247 ? 41.014  -19.692 30.290  1.00 34.25  ? 248 ASN G CB    1 
ATOM   9541  C CG    . ASN G 1 247 ? 39.736  -19.812 29.496  1.00 33.77  ? 248 ASN G CG    1 
ATOM   9542  O OD1   . ASN G 1 247 ? 39.714  -19.502 28.300  1.00 36.77  ? 248 ASN G OD1   1 
ATOM   9543  N ND2   . ASN G 1 247 ? 38.665  -20.251 30.141  1.00 31.41  ? 248 ASN G ND2   1 
ATOM   9544  N N     . TYR G 1 248 ? 42.764  -17.838 27.590  1.00 33.34  ? 249 TYR G N     1 
ATOM   9545  C CA    . TYR G 1 248 ? 42.849  -16.563 26.895  1.00 34.16  ? 249 TYR G CA    1 
ATOM   9546  C C     . TYR G 1 248 ? 41.451  -16.075 26.526  1.00 32.60  ? 249 TYR G C     1 
ATOM   9547  O O     . TYR G 1 248 ? 41.191  -14.873 26.530  1.00 31.57  ? 249 TYR G O     1 
ATOM   9548  C CB    . TYR G 1 248 ? 43.747  -16.694 25.660  1.00 34.64  ? 249 TYR G CB    1 
ATOM   9549  C CG    . TYR G 1 248 ? 45.224  -16.887 25.977  1.00 35.69  ? 249 TYR G CG    1 
ATOM   9550  C CD1   . TYR G 1 248 ? 46.012  -15.818 26.384  1.00 38.39  ? 249 TYR G CD1   1 
ATOM   9551  C CD2   . TYR G 1 248 ? 45.833  -18.129 25.852  1.00 37.30  ? 249 TYR G CD2   1 
ATOM   9552  C CE1   . TYR G 1 248 ? 47.356  -15.981 26.676  1.00 39.25  ? 249 TYR G CE1   1 
ATOM   9553  C CE2   . TYR G 1 248 ? 47.177  -18.306 26.135  1.00 37.78  ? 249 TYR G CE2   1 
ATOM   9554  C CZ    . TYR G 1 248 ? 47.941  -17.228 26.547  1.00 38.30  ? 249 TYR G CZ    1 
ATOM   9555  O OH    . TYR G 1 248 ? 49.266  -17.401 26.828  1.00 43.38  ? 249 TYR G OH    1 
ATOM   9556  N N     . ALA G 1 249 ? 40.561  -17.016 26.200  1.00 33.44  ? 250 ALA G N     1 
ATOM   9557  C CA    . ALA G 1 249 ? 39.203  -16.685 25.803  1.00 35.44  ? 250 ALA G CA    1 
ATOM   9558  C C     . ALA G 1 249 ? 38.557  -15.782 26.852  1.00 36.46  ? 250 ALA G C     1 
ATOM   9559  O O     . ALA G 1 249 ? 38.025  -14.724 26.525  1.00 35.44  ? 250 ALA G O     1 
ATOM   9560  C CB    . ALA G 1 249 ? 38.404  -17.955 25.597  1.00 36.51  ? 250 ALA G CB    1 
ATOM   9561  N N     . ILE G 1 250 ? 38.618  -16.213 28.116  1.00 41.63  ? 251 ILE G N     1 
ATOM   9562  C CA    . ILE G 1 250 ? 37.949  -15.514 29.201  1.00 36.48  ? 251 ILE G CA    1 
ATOM   9563  C C     . ILE G 1 250 ? 38.763  -14.279 29.581  1.00 33.76  ? 251 ILE G C     1 
ATOM   9564  O O     . ILE G 1 250 ? 38.205  -13.204 29.788  1.00 32.69  ? 251 ILE G O     1 
ATOM   9565  C CB    . ILE G 1 250 ? 37.732  -16.453 30.402  1.00 38.26  ? 251 ILE G CB    1 
ATOM   9566  C CG1   . ILE G 1 250 ? 37.041  -17.749 29.979  1.00 42.71  ? 251 ILE G CG1   1 
ATOM   9567  C CG2   . ILE G 1 250 ? 36.970  -15.745 31.523  1.00 36.43  ? 251 ILE G CG2   1 
ATOM   9568  C CD1   . ILE G 1 250 ? 35.705  -17.541 29.288  1.00 42.82  ? 251 ILE G CD1   1 
ATOM   9569  N N     . LEU G 1 251 ? 40.086  -14.449 29.674  1.00 32.71  ? 252 LEU G N     1 
ATOM   9570  C CA    . LEU G 1 251 ? 40.977  -13.350 30.003  1.00 34.33  ? 252 LEU G CA    1 
ATOM   9571  C C     . LEU G 1 251 ? 40.642  -12.151 29.120  1.00 38.41  ? 252 LEU G C     1 
ATOM   9572  O O     . LEU G 1 251 ? 40.514  -11.031 29.608  1.00 38.41  ? 252 LEU G O     1 
ATOM   9573  C CB    . LEU G 1 251 ? 42.433  -13.782 29.835  1.00 34.32  ? 252 LEU G CB    1 
ATOM   9574  C CG    . LEU G 1 251 ? 42.941  -14.829 30.831  1.00 31.99  ? 252 LEU G CG    1 
ATOM   9575  C CD1   . LEU G 1 251 ? 44.408  -15.146 30.598  1.00 31.11  ? 252 LEU G CD1   1 
ATOM   9576  C CD2   . LEU G 1 251 ? 42.715  -14.364 32.260  1.00 34.36  ? 252 LEU G CD2   1 
ATOM   9577  N N     . ALA G 1 252 ? 40.499  -12.407 27.815  1.00 44.45  ? 253 ALA G N     1 
ATOM   9578  C CA    . ALA G 1 252 ? 40.201  -11.362 26.851  1.00 48.05  ? 253 ALA G CA    1 
ATOM   9579  C C     . ALA G 1 252 ? 38.922  -10.635 27.257  1.00 48.00  ? 253 ALA G C     1 
ATOM   9580  O O     . ALA G 1 252 ? 38.894  -9.408  27.326  1.00 46.09  ? 253 ALA G O     1 
ATOM   9581  C CB    . ALA G 1 252 ? 40.085  -11.955 25.463  1.00 49.68  ? 253 ALA G CB    1 
ATOM   9582  N N     . LYS G 1 253 ? 37.866  -11.410 27.527  1.00 46.26  ? 254 LYS G N     1 
ATOM   9583  C CA    . LYS G 1 253 ? 36.582  -10.849 27.910  1.00 42.68  ? 254 LYS G CA    1 
ATOM   9584  C C     . LYS G 1 253 ? 36.763  -9.992  29.160  1.00 41.03  ? 254 LYS G C     1 
ATOM   9585  O O     . LYS G 1 253 ? 36.113  -8.959  29.307  1.00 36.93  ? 254 LYS G O     1 
ATOM   9586  C CB    . LYS G 1 253 ? 35.548  -11.960 28.128  1.00 41.59  ? 254 LYS G CB    1 
ATOM   9587  C CG    . LYS G 1 253 ? 35.220  -12.779 26.886  1.00 45.04  ? 254 LYS G CG    1 
ATOM   9588  C CD    . LYS G 1 253 ? 34.131  -13.824 27.095  1.00 48.06  ? 254 LYS G CD    1 
ATOM   9589  C CE    . LYS G 1 253 ? 33.882  -14.648 25.870  1.00 51.87  ? 254 LYS G CE    1 
ATOM   9590  N NZ    . LYS G 1 253 ? 33.491  -13.821 24.725  1.00 55.56  ? 254 LYS G NZ    1 
ATOM   9591  N N     . LEU G 1 254 ? 37.657  -10.434 30.052  1.00 40.84  ? 255 LEU G N     1 
ATOM   9592  C CA    . LEU G 1 254 ? 37.976  -9.686  31.257  1.00 44.81  ? 255 LEU G CA    1 
ATOM   9593  C C     . LEU G 1 254 ? 38.872  -8.506  30.889  1.00 46.85  ? 255 LEU G C     1 
ATOM   9594  O O     . LEU G 1 254 ? 39.100  -7.616  31.704  1.00 50.55  ? 255 LEU G O     1 
ATOM   9595  C CB    . LEU G 1 254 ? 38.644  -10.596 32.286  1.00 46.55  ? 255 LEU G CB    1 
ATOM   9596  C CG    . LEU G 1 254 ? 37.781  -11.734 32.839  1.00 48.77  ? 255 LEU G CG    1 
ATOM   9597  C CD1   . LEU G 1 254 ? 38.528  -12.506 33.913  1.00 47.77  ? 255 LEU G CD1   1 
ATOM   9598  C CD2   . LEU G 1 254 ? 36.463  -11.207 33.377  1.00 50.51  ? 255 LEU G CD2   1 
ATOM   9599  N N     . GLY G 1 255 ? 39.379  -8.520  29.653  1.00 48.58  ? 256 GLY G N     1 
ATOM   9600  C CA    . GLY G 1 255 ? 40.219  -7.447  29.150  1.00 42.30  ? 256 GLY G CA    1 
ATOM   9601  C C     . GLY G 1 255 ? 41.557  -7.399  29.883  1.00 42.21  ? 256 GLY G C     1 
ATOM   9602  O O     . GLY G 1 255 ? 42.117  -6.326  30.091  1.00 40.64  ? 256 GLY G O     1 
ATOM   9603  N N     . ILE G 1 256 ? 42.058  -8.577  30.268  1.00 41.56  ? 257 ILE G N     1 
ATOM   9604  C CA    . ILE G 1 256 ? 43.331  -8.680  30.960  1.00 42.19  ? 257 ILE G CA    1 
ATOM   9605  C C     . ILE G 1 256 ? 44.168  -9.766  30.292  1.00 41.63  ? 257 ILE G C     1 
ATOM   9606  O O     . ILE G 1 256 ? 43.708  -10.435 29.370  1.00 39.56  ? 257 ILE G O     1 
ATOM   9607  C CB    . ILE G 1 256 ? 43.123  -8.970  32.458  1.00 38.57  ? 257 ILE G CB    1 
ATOM   9608  C CG1   . ILE G 1 256 ? 42.534  -10.364 32.682  1.00 36.35  ? 257 ILE G CG1   1 
ATOM   9609  C CG2   . ILE G 1 256 ? 42.273  -7.881  33.113  1.00 40.63  ? 257 ILE G CG2   1 
ATOM   9610  C CD1   . ILE G 1 256 ? 42.406  -10.757 34.143  1.00 36.56  ? 257 ILE G CD1   1 
ATOM   9611  N N     . GLY G 1 257 ? 45.402  -9.930  30.781  1.00 44.19  ? 258 GLY G N     1 
ATOM   9612  C CA    . GLY G 1 257 ? 46.311  -10.942 30.271  1.00 42.97  ? 258 GLY G CA    1 
ATOM   9613  C C     . GLY G 1 257 ? 47.012  -11.676 31.410  1.00 44.68  ? 258 GLY G C     1 
ATOM   9614  O O     . GLY G 1 257 ? 46.860  -11.315 32.575  1.00 40.36  ? 258 GLY G O     1 
ATOM   9615  N N     . PRO G 1 258 ? 47.799  -12.732 31.104  1.00 46.92  ? 259 PRO G N     1 
ATOM   9616  C CA    . PRO G 1 258 ? 48.500  -13.498 32.136  1.00 49.57  ? 259 PRO G CA    1 
ATOM   9617  C C     . PRO G 1 258 ? 49.341  -12.624 33.063  1.00 56.71  ? 259 PRO G C     1 
ATOM   9618  O O     . PRO G 1 258 ? 49.392  -12.860 34.268  1.00 59.28  ? 259 PRO G O     1 
ATOM   9619  C CB    . PRO G 1 258 ? 49.371  -14.474 31.316  1.00 50.37  ? 259 PRO G CB    1 
ATOM   9620  C CG    . PRO G 1 258 ? 48.631  -14.620 30.002  1.00 50.36  ? 259 PRO G CG    1 
ATOM   9621  C CD    . PRO G 1 258 ? 48.032  -13.250 29.747  1.00 50.03  ? 259 PRO G CD    1 
ATOM   9622  N N     . GLU G 1 259 ? 49.999  -11.614 32.483  1.00 60.64  ? 260 GLU G N     1 
ATOM   9623  C CA    . GLU G 1 259 ? 50.932  -10.776 33.218  1.00 62.23  ? 260 GLU G CA    1 
ATOM   9624  C C     . GLU G 1 259 ? 50.167  -9.839  34.149  1.00 58.23  ? 260 GLU G C     1 
ATOM   9625  O O     . GLU G 1 259 ? 50.758  -9.217  35.029  1.00 54.58  ? 260 GLU G O     1 
ATOM   9626  C CB    . GLU G 1 259 ? 51.819  -9.983  32.257  1.00 62.39  ? 260 GLU G CB    1 
ATOM   9627  C CG    . GLU G 1 259 ? 51.042  -9.051  31.330  1.00 65.82  ? 260 GLU G CG    1 
ATOM   9628  C CD    . GLU G 1 259 ? 50.183  -9.756  30.294  1.00 64.47  ? 260 GLU G CD    1 
ATOM   9629  O OE1   . GLU G 1 259 ? 50.197  -11.004 30.257  1.00 59.33  ? 260 GLU G OE1   1 
ATOM   9630  O OE2   . GLU G 1 259 ? 49.500  -9.052  29.521  1.00 64.31  ? 260 GLU G OE2   1 
ATOM   9631  N N     . ASP G 1 260 ? 48.849  -9.746  33.944  1.00 54.55  ? 261 ASP G N     1 
ATOM   9632  C CA    . ASP G 1 260 ? 48.012  -8.858  34.733  1.00 47.61  ? 261 ASP G CA    1 
ATOM   9633  C C     . ASP G 1 260 ? 47.552  -9.584  35.994  1.00 51.22  ? 261 ASP G C     1 
ATOM   9634  O O     . ASP G 1 260 ? 47.116  -8.953  36.954  1.00 50.33  ? 261 ASP G O     1 
ATOM   9635  C CB    . ASP G 1 260 ? 46.847  -8.327  33.914  1.00 48.69  ? 261 ASP G CB    1 
ATOM   9636  C CG    . ASP G 1 260 ? 47.236  -7.520  32.683  1.00 50.39  ? 261 ASP G CG    1 
ATOM   9637  O OD1   . ASP G 1 260 ? 47.979  -6.529  32.844  1.00 52.41  ? 261 ASP G OD1   1 
ATOM   9638  O OD2   . ASP G 1 260 ? 46.792  -7.889  31.576  1.00 53.38  ? 261 ASP G OD2   1 
ATOM   9639  N N     . LEU G 1 261 ? 47.657  -10.917 35.978  1.00 49.10  ? 262 LEU G N     1 
ATOM   9640  C CA    . LEU G 1 261 ? 47.281  -11.728 37.122  1.00 49.58  ? 262 LEU G CA    1 
ATOM   9641  C C     . LEU G 1 261 ? 48.107  -11.295 38.331  1.00 56.78  ? 262 LEU G C     1 
ATOM   9642  O O     . LEU G 1 261 ? 49.319  -11.116 38.229  1.00 57.42  ? 262 LEU G O     1 
ATOM   9643  C CB    . LEU G 1 261 ? 47.479  -13.209 36.805  1.00 47.87  ? 262 LEU G CB    1 
ATOM   9644  C CG    . LEU G 1 261 ? 46.675  -13.754 35.620  1.00 48.26  ? 262 LEU G CG    1 
ATOM   9645  C CD1   . LEU G 1 261 ? 46.849  -15.258 35.488  1.00 45.00  ? 262 LEU G CD1   1 
ATOM   9646  C CD2   . LEU G 1 261 ? 45.206  -13.392 35.749  1.00 50.25  ? 262 LEU G CD2   1 
ATOM   9647  N N     . GLY G 1 262 ? 47.429  -11.122 39.470  1.00 57.41  ? 263 GLY G N     1 
ATOM   9648  C CA    . GLY G 1 262 ? 48.080  -10.701 40.700  1.00 60.77  ? 263 GLY G CA    1 
ATOM   9649  C C     . GLY G 1 262 ? 48.809  -11.856 41.361  1.00 57.38  ? 263 GLY G C     1 
ATOM   9650  O O     . GLY G 1 262 ? 49.788  -11.572 42.083  1.00 57.17  ? 263 GLY G O     1 
ATOM   9651  O OXT   . GLY G 1 262 ? 48.374  -13.006 41.139  1.00 54.15  ? 263 GLY G OXT   1 
ATOM   9652  N N     . LEU H 2 2   ? 45.491  -52.164 75.920  1.00 29.80  ? 4   LEU H N     1 
ATOM   9653  C CA    . LEU H 2 2   ? 45.684  -51.583 74.564  1.00 30.36  ? 4   LEU H CA    1 
ATOM   9654  C C     . LEU H 2 2   ? 44.570  -50.582 74.275  1.00 29.46  ? 4   LEU H C     1 
ATOM   9655  O O     . LEU H 2 2   ? 44.837  -49.420 73.977  1.00 27.04  ? 4   LEU H O     1 
ATOM   9656  C CB    . LEU H 2 2   ? 45.717  -52.691 73.514  1.00 32.62  ? 4   LEU H CB    1 
ATOM   9657  C CG    . LEU H 2 2   ? 46.995  -53.533 73.463  1.00 34.07  ? 4   LEU H CG    1 
ATOM   9658  C CD1   . LEU H 2 2   ? 46.951  -54.500 72.292  1.00 36.20  ? 4   LEU H CD1   1 
ATOM   9659  C CD2   . LEU H 2 2   ? 48.224  -52.645 73.384  1.00 33.89  ? 4   LEU H CD2   1 
ATOM   9660  N N     . SER H 2 3   ? 43.323  -51.057 74.357  1.00 27.78  ? 5   SER H N     1 
ATOM   9661  C CA    . SER H 2 3   ? 42.163  -50.246 74.026  1.00 31.77  ? 5   SER H CA    1 
ATOM   9662  C C     . SER H 2 3   ? 42.150  -48.978 74.875  1.00 32.90  ? 5   SER H C     1 
ATOM   9663  O O     . SER H 2 3   ? 41.862  -47.893 74.374  1.00 33.57  ? 5   SER H O     1 
ATOM   9664  C CB    . SER H 2 3   ? 40.888  -51.030 74.199  1.00 31.77  ? 5   SER H CB    1 
ATOM   9665  O OG    . SER H 2 3   ? 39.761  -50.269 73.788  1.00 34.42  ? 5   SER H OG    1 
ATOM   9666  N N     . ASP H 2 4   ? 42.465  -49.133 76.165  1.00 32.51  ? 6   ASP H N     1 
ATOM   9667  C CA    . ASP H 2 4   ? 42.445  -48.024 77.103  1.00 32.82  ? 6   ASP H CA    1 
ATOM   9668  C C     . ASP H 2 4   ? 43.488  -46.989 76.692  1.00 31.48  ? 6   ASP H C     1 
ATOM   9669  O O     . ASP H 2 4   ? 43.239  -45.788 76.771  1.00 31.20  ? 6   ASP H O     1 
ATOM   9670  C CB    . ASP H 2 4   ? 42.671  -48.500 78.530  1.00 34.26  ? 6   ASP H CB    1 
ATOM   9671  C CG    . ASP H 2 4   ? 41.589  -49.407 79.099  1.00 37.34  ? 6   ASP H CG    1 
ATOM   9672  O OD1   . ASP H 2 4   ? 40.596  -49.656 78.383  1.00 39.70  ? 6   ASP H OD1   1 
ATOM   9673  O OD2   . ASP H 2 4   ? 41.749  -49.857 80.252  1.00 43.28  ? 6   ASP H OD2   1 
ATOM   9674  N N     . PHE H 2 5   ? 44.654  -47.472 76.252  1.00 31.50  ? 7   PHE H N     1 
ATOM   9675  C CA    . PHE H 2 5   ? 45.776  -46.604 75.937  1.00 31.68  ? 7   PHE H CA    1 
ATOM   9676  C C     . PHE H 2 5   ? 45.508  -45.863 74.630  1.00 29.47  ? 7   PHE H C     1 
ATOM   9677  O O     . PHE H 2 5   ? 45.757  -44.663 74.535  1.00 30.96  ? 7   PHE H O     1 
ATOM   9678  C CB    . PHE H 2 5   ? 47.075  -47.414 75.871  1.00 33.29  ? 7   PHE H CB    1 
ATOM   9679  C CG    . PHE H 2 5   ? 48.252  -46.643 75.290  1.00 35.72  ? 7   PHE H CG    1 
ATOM   9680  C CD1   . PHE H 2 5   ? 48.856  -45.617 76.008  1.00 37.32  ? 7   PHE H CD1   1 
ATOM   9681  C CD2   . PHE H 2 5   ? 48.758  -46.952 74.032  1.00 36.43  ? 7   PHE H CD2   1 
ATOM   9682  C CE1   . PHE H 2 5   ? 49.924  -44.913 75.475  1.00 38.55  ? 7   PHE H CE1   1 
ATOM   9683  C CE2   . PHE H 2 5   ? 49.830  -46.248 73.508  1.00 38.10  ? 7   PHE H CE2   1 
ATOM   9684  C CZ    . PHE H 2 5   ? 50.409  -45.231 74.229  1.00 36.53  ? 7   PHE H CZ    1 
ATOM   9685  N N     . PHE H 2 6   ? 45.004  -46.588 73.626  1.00 27.66  ? 8   PHE H N     1 
ATOM   9686  C CA    . PHE H 2 6   ? 44.790  -46.017 72.305  1.00 26.84  ? 8   PHE H CA    1 
ATOM   9687  C C     . PHE H 2 6   ? 43.732  -44.920 72.385  1.00 26.91  ? 8   PHE H C     1 
ATOM   9688  O O     . PHE H 2 6   ? 43.849  -43.894 71.718  1.00 26.84  ? 8   PHE H O     1 
ATOM   9689  C CB    . PHE H 2 6   ? 44.385  -47.091 71.291  1.00 24.79  ? 8   PHE H CB    1 
ATOM   9690  C CG    . PHE H 2 6   ? 45.488  -48.082 70.946  1.00 22.53  ? 8   PHE H CG    1 
ATOM   9691  C CD1   . PHE H 2 6   ? 46.824  -47.770 71.172  1.00 23.45  ? 8   PHE H CD1   1 
ATOM   9692  C CD2   . PHE H 2 6   ? 45.189  -49.313 70.373  1.00 22.16  ? 8   PHE H CD2   1 
ATOM   9693  C CE1   . PHE H 2 6   ? 47.827  -48.673 70.853  1.00 23.96  ? 8   PHE H CE1   1 
ATOM   9694  C CE2   . PHE H 2 6   ? 46.196  -50.209 70.052  1.00 23.34  ? 8   PHE H CE2   1 
ATOM   9695  C CZ    . PHE H 2 6   ? 47.511  -49.887 70.293  1.00 26.39  ? 8   PHE H CZ    1 
ATOM   9696  N N     . THR H 2 7   ? 42.697  -45.153 73.199  1.00 29.05  ? 9   THR H N     1 
ATOM   9697  C CA    . THR H 2 7   ? 41.608  -44.201 73.345  1.00 29.42  ? 9   THR H CA    1 
ATOM   9698  C C     . THR H 2 7   ? 42.157  -42.897 73.918  1.00 28.68  ? 9   THR H C     1 
ATOM   9699  O O     . THR H 2 7   ? 41.890  -41.821 73.388  1.00 27.60  ? 9   THR H O     1 
ATOM   9700  C CB    . THR H 2 7   ? 40.515  -44.795 74.232  1.00 28.45  ? 9   THR H CB    1 
ATOM   9701  O OG1   . THR H 2 7   ? 40.091  -45.981 73.567  1.00 29.95  ? 9   THR H OG1   1 
ATOM   9702  C CG2   . THR H 2 7   ? 39.339  -43.854 74.415  1.00 28.19  ? 9   THR H CG2   1 
ATOM   9703  N N     . GLN H 2 8   ? 42.926  -43.011 75.007  1.00 27.09  ? 10  GLN H N     1 
ATOM   9704  C CA    . GLN H 2 8   ? 43.532  -41.856 75.649  1.00 27.63  ? 10  GLN H CA    1 
ATOM   9705  C C     . GLN H 2 8   ? 44.421  -41.124 74.647  1.00 25.76  ? 10  GLN H C     1 
ATOM   9706  O O     . GLN H 2 8   ? 44.257  -39.928 74.419  1.00 25.55  ? 10  GLN H O     1 
ATOM   9707  C CB    . GLN H 2 8   ? 44.361  -42.281 76.862  1.00 29.14  ? 10  GLN H CB    1 
ATOM   9708  C CG    . GLN H 2 8   ? 43.554  -42.940 77.975  1.00 33.48  ? 10  GLN H CG    1 
ATOM   9709  C CD    . GLN H 2 8   ? 44.410  -43.388 79.140  1.00 37.60  ? 10  GLN H CD    1 
ATOM   9710  O OE1   . GLN H 2 8   ? 45.631  -43.192 79.156  1.00 41.37  ? 10  GLN H OE1   1 
ATOM   9711  N NE2   . GLN H 2 8   ? 43.776  -43.997 80.132  1.00 38.87  ? 10  GLN H NE2   1 
ATOM   9712  N N     . LEU H 2 9   ? 45.362  -41.867 74.056  1.00 33.29  ? 11  LEU H N     1 
ATOM   9713  C CA    . LEU H 2 9   ? 46.358  -41.304 73.159  1.00 35.57  ? 11  LEU H CA    1 
ATOM   9714  C C     . LEU H 2 9   ? 45.677  -40.498 72.055  1.00 33.36  ? 11  LEU H C     1 
ATOM   9715  O O     . LEU H 2 9   ? 46.163  -39.440 71.664  1.00 33.00  ? 11  LEU H O     1 
ATOM   9716  C CB    . LEU H 2 9   ? 47.204  -42.441 72.586  1.00 37.40  ? 11  LEU H CB    1 
ATOM   9717  C CG    . LEU H 2 9   ? 48.249  -42.046 71.538  1.00 39.45  ? 11  LEU H CG    1 
ATOM   9718  C CD1   . LEU H 2 9   ? 49.263  -41.067 72.107  1.00 37.61  ? 11  LEU H CD1   1 
ATOM   9719  C CD2   . LEU H 2 9   ? 48.945  -43.280 70.989  1.00 38.45  ? 11  LEU H CD2   1 
ATOM   9720  N N     . GLY H 2 10  ? 44.548  -41.013 71.560  1.00 31.80  ? 12  GLY H N     1 
ATOM   9721  C CA    . GLY H 2 10  ? 43.866  -40.419 70.422  1.00 31.13  ? 12  GLY H CA    1 
ATOM   9722  C C     . GLY H 2 10  ? 43.179  -39.106 70.790  1.00 32.92  ? 12  GLY H C     1 
ATOM   9723  O O     . GLY H 2 10  ? 42.883  -38.294 69.917  1.00 29.92  ? 12  GLY H O     1 
ATOM   9724  N N     . GLN H 2 11  ? 42.942  -38.904 72.091  1.00 33.74  ? 13  GLN H N     1 
ATOM   9725  C CA    . GLN H 2 11  ? 42.166  -37.767 72.560  1.00 35.80  ? 13  GLN H CA    1 
ATOM   9726  C C     . GLN H 2 11  ? 43.080  -36.726 73.201  1.00 33.61  ? 13  GLN H C     1 
ATOM   9727  O O     . GLN H 2 11  ? 42.811  -35.529 73.115  1.00 31.18  ? 13  GLN H O     1 
ATOM   9728  C CB    . GLN H 2 11  ? 41.106  -38.219 73.564  1.00 40.59  ? 13  GLN H CB    1 
ATOM   9729  C CG    . GLN H 2 11  ? 40.016  -39.101 72.964  1.00 44.57  ? 13  GLN H CG    1 
ATOM   9730  C CD    . GLN H 2 11  ? 38.987  -39.543 73.981  1.00 44.92  ? 13  GLN H CD    1 
ATOM   9731  O OE1   . GLN H 2 11  ? 37.804  -39.194 73.896  1.00 56.86  ? 13  GLN H OE1   1 
ATOM   9732  N NE2   . GLN H 2 11  ? 39.432  -40.314 74.962  1.00 42.59  ? 13  GLN H NE2   1 
ATOM   9733  N N     . ASP H 2 12  ? 44.151  -37.194 73.852  1.00 34.93  ? 14  ASP H N     1 
ATOM   9734  C CA    . ASP H 2 12  ? 45.001  -36.329 74.657  1.00 35.41  ? 14  ASP H CA    1 
ATOM   9735  C C     . ASP H 2 12  ? 46.208  -35.880 73.835  1.00 35.70  ? 14  ASP H C     1 
ATOM   9736  O O     . ASP H 2 12  ? 47.107  -36.672 73.557  1.00 34.59  ? 14  ASP H O     1 
ATOM   9737  C CB    . ASP H 2 12  ? 45.415  -37.018 75.948  1.00 37.19  ? 14  ASP H CB    1 
ATOM   9738  C CG    . ASP H 2 12  ? 46.253  -36.174 76.898  1.00 40.90  ? 14  ASP H CG    1 
ATOM   9739  O OD1   . ASP H 2 12  ? 46.561  -35.018 76.538  1.00 45.82  ? 14  ASP H OD1   1 
ATOM   9740  O OD2   . ASP H 2 12  ? 46.586  -36.677 77.991  1.00 44.06  ? 14  ASP H OD2   1 
ATOM   9741  N N     . ALA H 2 13  ? 46.224  -34.591 73.480  1.00 35.77  ? 15  ALA H N     1 
ATOM   9742  C CA    . ALA H 2 13  ? 47.285  -34.023 72.664  1.00 37.15  ? 15  ALA H CA    1 
ATOM   9743  C C     . ALA H 2 13  ? 48.592  -33.992 73.452  1.00 41.45  ? 15  ALA H C     1 
ATOM   9744  O O     . ALA H 2 13  ? 49.672  -34.104 72.875  1.00 41.37  ? 15  ALA H O     1 
ATOM   9745  C CB    . ALA H 2 13  ? 46.888  -32.641 72.195  1.00 38.79  ? 15  ALA H CB    1 
ATOM   9746  N N     . GLN H 2 14  ? 48.482  -33.829 74.774  1.00 41.69  ? 16  GLN H N     1 
ATOM   9747  C CA    . GLN H 2 14  ? 49.646  -33.820 75.643  1.00 47.24  ? 16  GLN H CA    1 
ATOM   9748  C C     . GLN H 2 14  ? 50.333  -35.180 75.569  1.00 45.71  ? 16  GLN H C     1 
ATOM   9749  O O     . GLN H 2 14  ? 51.543  -35.262 75.375  1.00 47.76  ? 16  GLN H O     1 
ATOM   9750  C CB    . GLN H 2 14  ? 49.248  -33.489 77.082  1.00 50.18  ? 16  GLN H CB    1 
ATOM   9751  C CG    . GLN H 2 14  ? 50.417  -33.489 78.060  1.00 59.10  ? 16  GLN H CG    1 
ATOM   9752  C CD    . GLN H 2 14  ? 51.534  -32.555 77.646  1.00 67.08  ? 16  GLN H CD    1 
ATOM   9753  O OE1   . GLN H 2 14  ? 51.343  -31.341 77.514  1.00 70.59  ? 16  GLN H OE1   1 
ATOM   9754  N NE2   . GLN H 2 14  ? 52.714  -33.117 77.432  1.00 71.17  ? 16  GLN H NE2   1 
ATOM   9755  N N     . LEU H 2 15  ? 49.535  -36.243 75.719  1.00 44.81  ? 17  LEU H N     1 
ATOM   9756  C CA    . LEU H 2 15  ? 50.043  -37.603 75.696  1.00 42.84  ? 17  LEU H CA    1 
ATOM   9757  C C     . LEU H 2 15  ? 50.530  -37.940 74.290  1.00 40.80  ? 17  LEU H C     1 
ATOM   9758  O O     . LEU H 2 15  ? 51.505  -38.669 74.124  1.00 41.24  ? 17  LEU H O     1 
ATOM   9759  C CB    . LEU H 2 15  ? 48.946  -38.565 76.152  1.00 45.08  ? 17  LEU H CB    1 
ATOM   9760  C CG    . LEU H 2 15  ? 49.343  -40.042 76.235  1.00 47.14  ? 17  LEU H CG    1 
ATOM   9761  C CD1   . LEU H 2 15  ? 50.363  -40.266 77.339  1.00 48.93  ? 17  LEU H CD1   1 
ATOM   9762  C CD2   . LEU H 2 15  ? 48.123  -40.924 76.442  1.00 48.80  ? 17  LEU H CD2   1 
ATOM   9763  N N     . MET H 2 16  ? 49.832  -37.404 73.283  1.00 38.04  ? 18  MET H N     1 
ATOM   9764  C CA    . MET H 2 16  ? 50.181  -37.648 71.892  1.00 38.89  ? 18  MET H CA    1 
ATOM   9765  C C     . MET H 2 16  ? 51.599  -37.147 71.630  1.00 38.67  ? 18  MET H C     1 
ATOM   9766  O O     . MET H 2 16  ? 52.431  -37.879 71.099  1.00 35.88  ? 18  MET H O     1 
ATOM   9767  C CB    . MET H 2 16  ? 49.202  -36.946 70.942  1.00 38.80  ? 18  MET H CB    1 
ATOM   9768  C CG    . MET H 2 16  ? 49.576  -37.068 69.475  1.00 41.40  ? 18  MET H CG    1 
ATOM   9769  S SD    . MET H 2 16  ? 49.473  -38.758 68.849  1.00 45.34  ? 18  MET H SD    1 
ATOM   9770  C CE    . MET H 2 16  ? 47.693  -38.955 68.689  1.00 42.98  ? 18  MET H CE    1 
ATOM   9771  N N     . GLU H 2 17  ? 51.862  -35.894 72.013  1.00 41.16  ? 19  GLU H N     1 
ATOM   9772  C CA    . GLU H 2 17  ? 53.157  -35.277 71.778  1.00 41.74  ? 19  GLU H CA    1 
ATOM   9773  C C     . GLU H 2 17  ? 54.230  -36.035 72.557  1.00 41.76  ? 19  GLU H C     1 
ATOM   9774  O O     . GLU H 2 17  ? 55.369  -36.137 72.107  1.00 39.15  ? 19  GLU H O     1 
ATOM   9775  C CB    . GLU H 2 17  ? 53.118  -33.794 72.145  1.00 45.18  ? 19  GLU H CB    1 
ATOM   9776  C CG    . GLU H 2 17  ? 52.251  -32.966 71.201  1.00 50.15  ? 19  GLU H CG    1 
ATOM   9777  C CD    . GLU H 2 17  ? 52.703  -33.007 69.752  1.00 55.13  ? 19  GLU H CD    1 
ATOM   9778  O OE1   . GLU H 2 17  ? 53.805  -32.496 69.462  1.00 56.82  ? 19  GLU H OE1   1 
ATOM   9779  O OE2   . GLU H 2 17  ? 51.958  -33.561 68.915  1.00 60.53  ? 19  GLU H OE2   1 
ATOM   9780  N N     . ASP H 2 18  ? 53.848  -36.571 73.722  1.00 41.78  ? 20  ASP H N     1 
ATOM   9781  C CA    . ASP H 2 18  ? 54.758  -37.354 74.542  1.00 42.68  ? 20  ASP H CA    1 
ATOM   9782  C C     . ASP H 2 18  ? 55.093  -38.657 73.822  1.00 38.08  ? 20  ASP H C     1 
ATOM   9783  O O     . ASP H 2 18  ? 56.226  -39.130 73.881  1.00 35.69  ? 20  ASP H O     1 
ATOM   9784  C CB    . ASP H 2 18  ? 54.173  -37.627 75.919  1.00 50.14  ? 20  ASP H CB    1 
ATOM   9785  C CG    . ASP H 2 18  ? 53.994  -36.406 76.809  1.00 58.52  ? 20  ASP H CG    1 
ATOM   9786  O OD1   . ASP H 2 18  ? 54.411  -35.307 76.388  1.00 68.14  ? 20  ASP H OD1   1 
ATOM   9787  O OD2   . ASP H 2 18  ? 53.433  -36.565 77.914  1.00 62.48  ? 20  ASP H OD2   1 
ATOM   9788  N N     . TYR H 2 19  ? 54.089  -39.228 73.149  1.00 36.26  ? 21  TYR H N     1 
ATOM   9789  C CA    . TYR H 2 19  ? 54.241  -40.499 72.462  1.00 35.76  ? 21  TYR H CA    1 
ATOM   9790  C C     . TYR H 2 19  ? 55.226  -40.343 71.307  1.00 39.00  ? 21  TYR H C     1 
ATOM   9791  O O     . TYR H 2 19  ? 56.176  -41.114 71.190  1.00 40.16  ? 21  TYR H O     1 
ATOM   9792  C CB    . TYR H 2 19  ? 52.877  -41.004 71.980  1.00 34.98  ? 21  TYR H CB    1 
ATOM   9793  C CG    . TYR H 2 19  ? 52.944  -42.216 71.060  1.00 36.20  ? 21  TYR H CG    1 
ATOM   9794  C CD1   . TYR H 2 19  ? 53.114  -43.497 71.571  1.00 34.43  ? 21  TYR H CD1   1 
ATOM   9795  C CD2   . TYR H 2 19  ? 52.827  -42.080 69.682  1.00 34.56  ? 21  TYR H CD2   1 
ATOM   9796  C CE1   . TYR H 2 19  ? 53.177  -44.604 70.740  1.00 34.99  ? 21  TYR H CE1   1 
ATOM   9797  C CE2   . TYR H 2 19  ? 52.883  -43.178 68.841  1.00 36.12  ? 21  TYR H CE2   1 
ATOM   9798  C CZ    . TYR H 2 19  ? 53.059  -44.444 69.371  1.00 34.96  ? 21  TYR H CZ    1 
ATOM   9799  O OH    . TYR H 2 19  ? 53.115  -45.532 68.549  1.00 44.35  ? 21  TYR H OH    1 
ATOM   9800  N N     . LYS H 2 20  ? 54.988  -39.339 70.455  1.00 43.15  ? 22  LYS H N     1 
ATOM   9801  C CA    . LYS H 2 20  ? 55.806  -39.133 69.271  1.00 46.97  ? 22  LYS H CA    1 
ATOM   9802  C C     . LYS H 2 20  ? 57.242  -38.819 69.687  1.00 49.51  ? 22  LYS H C     1 
ATOM   9803  O O     . LYS H 2 20  ? 58.181  -39.111 68.950  1.00 54.10  ? 22  LYS H O     1 
ATOM   9804  C CB    . LYS H 2 20  ? 55.232  -38.023 68.382  1.00 52.06  ? 22  LYS H CB    1 
ATOM   9805  C CG    . LYS H 2 20  ? 53.876  -38.332 67.759  1.00 56.75  ? 22  LYS H CG    1 
ATOM   9806  C CD    . LYS H 2 20  ? 53.516  -37.419 66.593  1.00 61.12  ? 22  LYS H CD    1 
ATOM   9807  C CE    . LYS H 2 20  ? 53.574  -35.969 66.951  1.00 66.09  ? 22  LYS H CE    1 
ATOM   9808  N NZ    . LYS H 2 20  ? 53.364  -35.115 65.779  1.00 70.16  ? 22  LYS H NZ    1 
ATOM   9809  N N     . GLN H 2 21  ? 57.400  -38.221 70.872  1.00 49.91  ? 23  GLN H N     1 
ATOM   9810  C CA    . GLN H 2 21  ? 58.718  -37.921 71.407  1.00 48.70  ? 23  GLN H CA    1 
ATOM   9811  C C     . GLN H 2 21  ? 59.470  -39.225 71.658  1.00 44.05  ? 23  GLN H C     1 
ATOM   9812  O O     . GLN H 2 21  ? 60.640  -39.349 71.304  1.00 38.68  ? 23  GLN H O     1 
ATOM   9813  C CB    . GLN H 2 21  ? 58.619  -37.101 72.694  1.00 48.25  ? 23  GLN H CB    1 
ATOM   9814  C CG    . GLN H 2 21  ? 58.291  -35.628 72.471  1.00 53.95  ? 23  GLN H CG    1 
ATOM   9815  C CD    . GLN H 2 21  ? 59.404  -34.870 71.781  1.00 58.72  ? 23  GLN H CD    1 
ATOM   9816  O OE1   . GLN H 2 21  ? 59.833  -35.218 70.675  1.00 60.29  ? 23  GLN H OE1   1 
ATOM   9817  N NE2   . GLN H 2 21  ? 59.890  -33.824 72.434  1.00 60.83  ? 23  GLN H NE2   1 
ATOM   9818  N N     . ASN H 2 22  ? 58.779  -40.193 72.269  1.00 37.61  ? 24  ASN H N     1 
ATOM   9819  C CA    . ASN H 2 22  ? 59.398  -41.451 72.652  1.00 38.17  ? 24  ASN H CA    1 
ATOM   9820  C C     . ASN H 2 22  ? 58.327  -42.538 72.716  1.00 35.16  ? 24  ASN H C     1 
ATOM   9821  O O     . ASN H 2 22  ? 57.822  -42.858 73.789  1.00 38.15  ? 24  ASN H O     1 
ATOM   9822  C CB    . ASN H 2 22  ? 60.159  -41.304 73.965  1.00 42.57  ? 24  ASN H CB    1 
ATOM   9823  C CG    . ASN H 2 22  ? 60.973  -42.530 74.299  1.00 44.66  ? 24  ASN H CG    1 
ATOM   9824  O OD1   . ASN H 2 22  ? 60.870  -43.553 73.614  1.00 44.82  ? 24  ASN H OD1   1 
ATOM   9825  N ND2   . ASN H 2 22  ? 61.781  -42.449 75.346  1.00 42.90  ? 24  ASN H ND2   1 
ATOM   9826  N N     . PRO H 2 23  ? 57.948  -43.133 71.562  1.00 32.88  ? 25  PRO H N     1 
ATOM   9827  C CA    . PRO H 2 23  ? 56.894  -44.151 71.524  1.00 34.04  ? 25  PRO H CA    1 
ATOM   9828  C C     . PRO H 2 23  ? 57.064  -45.288 72.532  1.00 34.70  ? 25  PRO H C     1 
ATOM   9829  O O     . PRO H 2 23  ? 56.162  -45.555 73.323  1.00 32.18  ? 25  PRO H O     1 
ATOM   9830  C CB    . PRO H 2 23  ? 56.974  -44.656 70.069  1.00 33.97  ? 25  PRO H CB    1 
ATOM   9831  C CG    . PRO H 2 23  ? 57.484  -43.462 69.294  1.00 33.38  ? 25  PRO H CG    1 
ATOM   9832  C CD    . PRO H 2 23  ? 58.485  -42.813 70.231  1.00 34.09  ? 25  PRO H CD    1 
ATOM   9833  N N     . GLU H 2 24  ? 58.220  -45.959 72.485  1.00 36.00  ? 26  GLU H N     1 
ATOM   9834  C CA    . GLU H 2 24  ? 58.450  -47.148 73.291  1.00 40.55  ? 26  GLU H CA    1 
ATOM   9835  C C     . GLU H 2 24  ? 58.372  -46.803 74.777  1.00 37.07  ? 26  GLU H C     1 
ATOM   9836  O O     . GLU H 2 24  ? 57.880  -47.599 75.573  1.00 33.13  ? 26  GLU H O     1 
ATOM   9837  C CB    . GLU H 2 24  ? 59.795  -47.800 72.967  1.00 49.96  ? 26  GLU H CB    1 
ATOM   9838  C CG    . GLU H 2 24  ? 59.750  -48.706 71.741  1.00 56.24  ? 26  GLU H CG    1 
ATOM   9839  C CD    . GLU H 2 24  ? 61.006  -49.535 71.541  1.00 62.90  ? 26  GLU H CD    1 
ATOM   9840  O OE1   . GLU H 2 24  ? 61.596  -49.462 70.443  1.00 75.79  ? 26  GLU H OE1   1 
ATOM   9841  O OE2   . GLU H 2 24  ? 61.399  -50.248 72.488  1.00 65.95  ? 26  GLU H OE2   1 
ATOM   9842  N N     . ALA H 2 25  ? 58.879  -45.622 75.141  1.00 35.65  ? 27  ALA H N     1 
ATOM   9843  C CA    . ALA H 2 25  ? 58.882  -45.189 76.529  1.00 37.09  ? 27  ALA H CA    1 
ATOM   9844  C C     . ALA H 2 25  ? 57.446  -45.042 77.026  1.00 38.08  ? 27  ALA H C     1 
ATOM   9845  O O     . ALA H 2 25  ? 57.095  -45.550 78.089  1.00 37.30  ? 27  ALA H O     1 
ATOM   9846  C CB    . ALA H 2 25  ? 59.650  -43.892 76.666  1.00 40.18  ? 27  ALA H CB    1 
ATOM   9847  N N     . VAL H 2 26  ? 56.622  -44.354 76.230  1.00 35.30  ? 28  VAL H N     1 
ATOM   9848  C CA    . VAL H 2 26  ? 55.250  -44.058 76.609  1.00 38.15  ? 28  VAL H CA    1 
ATOM   9849  C C     . VAL H 2 26  ? 54.450  -45.357 76.666  1.00 39.33  ? 28  VAL H C     1 
ATOM   9850  O O     . VAL H 2 26  ? 53.636  -45.545 77.566  1.00 39.36  ? 28  VAL H O     1 
ATOM   9851  C CB    . VAL H 2 26  ? 54.610  -43.049 75.637  1.00 36.04  ? 28  VAL H CB    1 
ATOM   9852  C CG1   . VAL H 2 26  ? 53.111  -42.907 75.875  1.00 39.53  ? 28  VAL H CG1   1 
ATOM   9853  C CG2   . VAL H 2 26  ? 55.297  -41.689 75.702  1.00 35.70  ? 28  VAL H CG2   1 
ATOM   9854  N N     . MET H 2 27  ? 54.691  -46.250 75.700  1.00 39.55  ? 29  MET H N     1 
ATOM   9855  C CA    . MET H 2 27  ? 53.935  -47.488 75.598  1.00 38.31  ? 29  MET H CA    1 
ATOM   9856  C C     . MET H 2 27  ? 54.283  -48.410 76.764  1.00 38.96  ? 29  MET H C     1 
ATOM   9857  O O     . MET H 2 27  ? 53.401  -49.049 77.334  1.00 38.65  ? 29  MET H O     1 
ATOM   9858  C CB    . MET H 2 27  ? 54.201  -48.196 74.265  1.00 35.43  ? 29  MET H CB    1 
ATOM   9859  C CG    . MET H 2 27  ? 53.391  -47.641 73.109  1.00 37.89  ? 29  MET H CG    1 
ATOM   9860  S SD    . MET H 2 27  ? 53.630  -48.560 71.576  1.00 36.47  ? 29  MET H SD    1 
ATOM   9861  C CE    . MET H 2 27  ? 55.363  -48.199 71.260  1.00 39.41  ? 29  MET H CE    1 
ATOM   9862  N N     . ARG H 2 28  ? 55.572  -48.480 77.109  1.00 42.08  ? 30  ARG H N     1 
ATOM   9863  C CA    . ARG H 2 28  ? 56.010  -49.280 78.241  1.00 47.11  ? 30  ARG H CA    1 
ATOM   9864  C C     . ARG H 2 28  ? 55.420  -48.700 79.524  1.00 44.00  ? 30  ARG H C     1 
ATOM   9865  O O     . ARG H 2 28  ? 55.082  -49.439 80.445  1.00 46.72  ? 30  ARG H O     1 
ATOM   9866  C CB    . ARG H 2 28  ? 57.539  -49.345 78.336  1.00 51.05  ? 30  ARG H CB    1 
ATOM   9867  C CG    . ARG H 2 28  ? 58.187  -50.346 77.390  1.00 58.03  ? 30  ARG H CG    1 
ATOM   9868  C CD    . ARG H 2 28  ? 59.670  -50.524 77.683  1.00 66.33  ? 30  ARG H CD    1 
ATOM   9869  N NE    . ARG H 2 28  ? 60.243  -51.678 76.981  1.00 74.95  ? 30  ARG H NE    1 
ATOM   9870  C CZ    . ARG H 2 28  ? 60.324  -51.804 75.662  1.00 78.89  ? 30  ARG H CZ    1 
ATOM   9871  N NH1   . ARG H 2 28  ? 60.833  -52.903 75.135  1.00 80.94  ? 30  ARG H NH1   1 
ATOM   9872  N NH2   . ARG H 2 28  ? 59.890  -50.836 74.875  1.00 80.28  ? 30  ARG H NH2   1 
ATOM   9873  N N     . ALA H 2 29  ? 55.293  -47.370 79.560  1.00 42.53  ? 31  ALA H N     1 
ATOM   9874  C CA    . ALA H 2 29  ? 54.812  -46.671 80.739  1.00 43.09  ? 31  ALA H CA    1 
ATOM   9875  C C     . ALA H 2 29  ? 53.341  -47.000 80.982  1.00 42.24  ? 31  ALA H C     1 
ATOM   9876  O O     . ALA H 2 29  ? 52.857  -46.895 82.106  1.00 47.32  ? 31  ALA H O     1 
ATOM   9877  C CB    . ALA H 2 29  ? 55.028  -45.183 80.577  1.00 39.43  ? 31  ALA H CB    1 
ATOM   9878  N N     . HIS H 2 30  ? 52.640  -47.400 79.916  1.00 42.24  ? 32  HIS H N     1 
ATOM   9879  C CA    . HIS H 2 30  ? 51.227  -47.729 80.010  1.00 42.16  ? 32  HIS H CA    1 
ATOM   9880  C C     . HIS H 2 30  ? 51.058  -49.247 80.009  1.00 39.05  ? 32  HIS H C     1 
ATOM   9881  O O     . HIS H 2 30  ? 49.943  -49.754 79.901  1.00 38.17  ? 32  HIS H O     1 
ATOM   9882  C CB    . HIS H 2 30  ? 50.436  -47.006 78.914  1.00 40.57  ? 32  HIS H CB    1 
ATOM   9883  C CG    . HIS H 2 30  ? 50.290  -45.542 79.169  1.00 40.28  ? 32  HIS H CG    1 
ATOM   9884  N ND1   . HIS H 2 30  ? 51.260  -44.620 78.838  1.00 39.53  ? 32  HIS H ND1   1 
ATOM   9885  C CD2   . HIS H 2 30  ? 49.304  -44.848 79.758  1.00 39.02  ? 32  HIS H CD2   1 
ATOM   9886  C CE1   . HIS H 2 30  ? 50.855  -43.411 79.203  1.00 41.55  ? 32  HIS H CE1   1 
ATOM   9887  N NE2   . HIS H 2 30  ? 49.670  -43.526 79.762  1.00 40.36  ? 32  HIS H NE2   1 
ATOM   9888  N N     . GLY H 2 31  ? 52.184  -49.959 80.127  1.00 39.55  ? 33  GLY H N     1 
ATOM   9889  C CA    . GLY H 2 31  ? 52.177  -51.382 80.427  1.00 41.81  ? 33  GLY H CA    1 
ATOM   9890  C C     . GLY H 2 31  ? 51.855  -52.239 79.205  1.00 44.72  ? 33  GLY H C     1 
ATOM   9891  O O     . GLY H 2 31  ? 51.279  -53.317 79.341  1.00 44.47  ? 33  GLY H O     1 
ATOM   9892  N N     . LEU H 2 32  ? 52.240  -51.764 78.016  1.00 44.17  ? 34  LEU H N     1 
ATOM   9893  C CA    . LEU H 2 32  ? 52.106  -52.559 76.806  1.00 43.44  ? 34  LEU H CA    1 
ATOM   9894  C C     . LEU H 2 32  ? 53.220  -53.603 76.776  1.00 42.77  ? 34  LEU H C     1 
ATOM   9895  O O     . LEU H 2 32  ? 54.362  -53.307 77.120  1.00 40.12  ? 34  LEU H O     1 
ATOM   9896  C CB    . LEU H 2 32  ? 52.134  -51.677 75.557  1.00 43.27  ? 34  LEU H CB    1 
ATOM   9897  C CG    . LEU H 2 32  ? 50.864  -50.866 75.277  1.00 42.52  ? 34  LEU H CG    1 
ATOM   9898  C CD1   . LEU H 2 32  ? 50.693  -49.735 76.276  1.00 43.95  ? 34  LEU H CD1   1 
ATOM   9899  C CD2   . LEU H 2 32  ? 50.873  -50.330 73.854  1.00 43.04  ? 34  LEU H CD2   1 
ATOM   9900  N N     . THR H 2 33  ? 52.866  -54.825 76.362  1.00 44.48  ? 35  THR H N     1 
ATOM   9901  C CA    . THR H 2 33  ? 53.810  -55.930 76.315  1.00 42.01  ? 35  THR H CA    1 
ATOM   9902  C C     . THR H 2 33  ? 54.779  -55.716 75.155  1.00 41.52  ? 35  THR H C     1 
ATOM   9903  O O     . THR H 2 33  ? 54.535  -54.890 74.278  1.00 37.22  ? 35  THR H O     1 
ATOM   9904  C CB    . THR H 2 33  ? 53.055  -57.251 76.173  1.00 41.94  ? 35  THR H CB    1 
ATOM   9905  O OG1   . THR H 2 33  ? 52.409  -57.184 74.906  1.00 39.99  ? 35  THR H OG1   1 
ATOM   9906  C CG2   . THR H 2 33  ? 52.034  -57.463 77.277  1.00 43.37  ? 35  THR H CG2   1 
ATOM   9907  N N     . ASP H 2 34  ? 55.870  -56.489 75.160  1.00 43.48  ? 36  ASP H N     1 
ATOM   9908  C CA    . ASP H 2 34  ? 56.901  -56.385 74.143  1.00 47.23  ? 36  ASP H CA    1 
ATOM   9909  C C     . ASP H 2 34  ? 56.300  -56.705 72.777  1.00 45.49  ? 36  ASP H C     1 
ATOM   9910  O O     . ASP H 2 34  ? 56.582  -56.022 71.795  1.00 43.44  ? 36  ASP H O     1 
ATOM   9911  C CB    . ASP H 2 34  ? 58.083  -57.287 74.466  1.00 52.83  ? 36  ASP H CB    1 
ATOM   9912  C CG    . ASP H 2 34  ? 58.813  -56.967 75.762  1.00 58.78  ? 36  ASP H CG    1 
ATOM   9913  O OD1   . ASP H 2 34  ? 58.443  -55.967 76.412  1.00 63.85  ? 36  ASP H OD1   1 
ATOM   9914  O OD2   . ASP H 2 34  ? 59.745  -57.722 76.112  1.00 64.90  ? 36  ASP H OD2   1 
ATOM   9915  N N     . GLU H 2 35  ? 55.469  -57.752 72.733  1.00 46.84  ? 37  GLU H N     1 
ATOM   9916  C CA    . GLU H 2 35  ? 54.859  -58.199 71.492  1.00 47.47  ? 37  GLU H CA    1 
ATOM   9917  C C     . GLU H 2 35  ? 53.910  -57.120 70.978  1.00 45.05  ? 37  GLU H C     1 
ATOM   9918  O O     . GLU H 2 35  ? 53.828  -56.880 69.775  1.00 40.93  ? 37  GLU H O     1 
ATOM   9919  C CB    . GLU H 2 35  ? 54.125  -59.524 71.699  1.00 52.89  ? 37  GLU H CB    1 
ATOM   9920  C CG    . GLU H 2 35  ? 52.956  -59.426 72.675  1.00 57.64  ? 37  GLU H CG    1 
ATOM   9921  C CD    . GLU H 2 35  ? 52.239  -60.741 72.927  1.00 65.05  ? 37  GLU H CD    1 
ATOM   9922  O OE1   . GLU H 2 35  ? 51.706  -61.323 71.958  1.00 65.46  ? 37  GLU H OE1   1 
ATOM   9923  O OE2   . GLU H 2 35  ? 52.214  -61.184 74.096  1.00 63.21  ? 37  GLU H OE2   1 
ATOM   9924  N N     . GLN H 2 36  ? 53.195  -56.478 71.907  1.00 47.10  ? 38  GLN H N     1 
ATOM   9925  C CA    . GLN H 2 36  ? 52.255  -55.423 71.564  1.00 45.94  ? 38  GLN H CA    1 
ATOM   9926  C C     . GLN H 2 36  ? 53.020  -54.241 70.977  1.00 43.63  ? 38  GLN H C     1 
ATOM   9927  O O     . GLN H 2 36  ? 52.604  -53.662 69.975  1.00 44.64  ? 38  GLN H O     1 
ATOM   9928  C CB    . GLN H 2 36  ? 51.447  -55.014 72.795  1.00 46.84  ? 38  GLN H CB    1 
ATOM   9929  C CG    . GLN H 2 36  ? 50.510  -56.102 73.310  1.00 46.12  ? 38  GLN H CG    1 
ATOM   9930  C CD    . GLN H 2 36  ? 49.815  -55.728 74.601  1.00 45.21  ? 38  GLN H CD    1 
ATOM   9931  O OE1   . GLN H 2 36  ? 50.029  -54.646 75.158  1.00 40.52  ? 38  GLN H OE1   1 
ATOM   9932  N NE2   . GLN H 2 36  ? 48.976  -56.628 75.093  1.00 44.78  ? 38  GLN H NE2   1 
ATOM   9933  N N     . ILE H 2 37  ? 54.146  -53.898 71.610  1.00 42.00  ? 39  ILE H N     1 
ATOM   9934  C CA    . ILE H 2 37  ? 54.982  -52.800 71.155  1.00 44.55  ? 39  ILE H CA    1 
ATOM   9935  C C     . ILE H 2 37  ? 55.547  -53.149 69.781  1.00 43.56  ? 39  ILE H C     1 
ATOM   9936  O O     . ILE H 2 37  ? 55.572  -52.309 68.884  1.00 42.03  ? 39  ILE H O     1 
ATOM   9937  C CB    . ILE H 2 37  ? 56.095  -52.498 72.176  1.00 45.23  ? 39  ILE H CB    1 
ATOM   9938  C CG1   . ILE H 2 37  ? 55.516  -52.038 73.515  1.00 45.91  ? 39  ILE H CG1   1 
ATOM   9939  C CG2   . ILE H 2 37  ? 57.093  -51.483 71.616  1.00 45.08  ? 39  ILE H CG2   1 
ATOM   9940  C CD1   . ILE H 2 37  ? 56.563  -51.661 74.548  1.00 46.27  ? 39  ILE H CD1   1 
ATOM   9941  N N     . ASN H 2 38  ? 55.989  -54.402 69.630  1.00 43.81  ? 40  ASN H N     1 
ATOM   9942  C CA    . ASN H 2 38  ? 56.566  -54.874 68.383  1.00 46.31  ? 40  ASN H CA    1 
ATOM   9943  C C     . ASN H 2 38  ? 55.550  -54.706 67.256  1.00 44.68  ? 40  ASN H C     1 
ATOM   9944  O O     . ASN H 2 38  ? 55.889  -54.235 66.172  1.00 43.04  ? 40  ASN H O     1 
ATOM   9945  C CB    . ASN H 2 38  ? 57.031  -56.321 68.496  1.00 52.48  ? 40  ASN H CB    1 
ATOM   9946  C CG    . ASN H 2 38  ? 57.556  -56.853 67.185  1.00 55.54  ? 40  ASN H CG    1 
ATOM   9947  O OD1   . ASN H 2 38  ? 58.531  -56.320 66.643  1.00 56.04  ? 40  ASN H OD1   1 
ATOM   9948  N ND2   . ASN H 2 38  ? 56.925  -57.893 66.657  1.00 59.44  ? 40  ASN H ND2   1 
ATOM   9949  N N     . ALA H 2 39  ? 54.303  -55.104 67.528  1.00 42.16  ? 41  ALA H N     1 
ATOM   9950  C CA    . ALA H 2 39  ? 53.238  -55.042 66.541  1.00 40.30  ? 41  ALA H CA    1 
ATOM   9951  C C     . ALA H 2 39  ? 53.019  -53.597 66.102  1.00 37.50  ? 41  ALA H C     1 
ATOM   9952  O O     . ALA H 2 39  ? 52.715  -53.335 64.940  1.00 34.23  ? 41  ALA H O     1 
ATOM   9953  C CB    . ALA H 2 39  ? 51.973  -55.644 67.114  1.00 40.33  ? 41  ALA H CB    1 
ATOM   9954  N N     . VAL H 2 40  ? 53.172  -52.669 67.052  1.00 35.72  ? 42  VAL H N     1 
ATOM   9955  C CA    . VAL H 2 40  ? 52.982  -51.253 66.785  1.00 36.12  ? 42  VAL H CA    1 
ATOM   9956  C C     . VAL H 2 40  ? 54.107  -50.765 65.877  1.00 36.34  ? 42  VAL H C     1 
ATOM   9957  O O     . VAL H 2 40  ? 53.860  -50.076 64.891  1.00 35.88  ? 42  VAL H O     1 
ATOM   9958  C CB    . VAL H 2 40  ? 52.932  -50.432 68.088  1.00 37.44  ? 42  VAL H CB    1 
ATOM   9959  C CG1   . VAL H 2 40  ? 53.025  -48.935 67.817  1.00 38.04  ? 42  VAL H CG1   1 
ATOM   9960  C CG2   . VAL H 2 40  ? 51.695  -50.755 68.916  1.00 36.83  ? 42  VAL H CG2   1 
ATOM   9961  N N     . MET H 2 41  ? 55.342  -51.134 66.227  1.00 38.39  ? 43  MET H N     1 
ATOM   9962  C CA    . MET H 2 41  ? 56.519  -50.632 65.539  1.00 41.01  ? 43  MET H CA    1 
ATOM   9963  C C     . MET H 2 41  ? 56.603  -51.236 64.140  1.00 40.08  ? 43  MET H C     1 
ATOM   9964  O O     . MET H 2 41  ? 57.103  -50.598 63.216  1.00 41.18  ? 43  MET H O     1 
ATOM   9965  C CB    . MET H 2 41  ? 57.792  -50.954 66.330  1.00 44.92  ? 43  MET H CB    1 
ATOM   9966  C CG    . MET H 2 41  ? 57.858  -50.272 67.685  1.00 46.33  ? 43  MET H CG    1 
ATOM   9967  S SD    . MET H 2 41  ? 57.504  -48.505 67.589  1.00 51.15  ? 43  MET H SD    1 
ATOM   9968  C CE    . MET H 2 41  ? 58.639  -48.012 66.285  1.00 53.09  ? 43  MET H CE    1 
ATOM   9969  N N     . THR H 2 42  ? 56.105  -52.469 63.993  1.00 38.42  ? 44  THR H N     1 
ATOM   9970  C CA    . THR H 2 42  ? 56.129  -53.157 62.714  1.00 40.21  ? 44  THR H CA    1 
ATOM   9971  C C     . THR H 2 42  ? 54.927  -52.717 61.882  1.00 40.13  ? 44  THR H C     1 
ATOM   9972  O O     . THR H 2 42  ? 54.888  -52.940 60.675  1.00 41.56  ? 44  THR H O     1 
ATOM   9973  C CB    . THR H 2 42  ? 56.138  -54.669 62.937  1.00 43.88  ? 44  THR H CB    1 
ATOM   9974  O OG1   . THR H 2 42  ? 54.960  -54.954 63.684  1.00 43.60  ? 44  THR H OG1   1 
ATOM   9975  C CG2   . THR H 2 42  ? 57.367  -55.140 63.693  1.00 44.06  ? 44  THR H CG2   1 
ATOM   9976  N N     . GLY H 2 43  ? 53.951  -52.090 62.547  1.00 41.16  ? 45  GLY H N     1 
ATOM   9977  C CA    . GLY H 2 43  ? 52.748  -51.619 61.884  1.00 39.35  ? 45  GLY H CA    1 
ATOM   9978  C C     . GLY H 2 43  ? 51.832  -52.780 61.506  1.00 42.38  ? 45  GLY H C     1 
ATOM   9979  O O     . GLY H 2 43  ? 51.200  -52.760 60.452  1.00 49.56  ? 45  GLY H O     1 
ATOM   9980  N N     . ASP H 2 44  ? 51.771  -53.788 62.384  1.00 42.59  ? 46  ASP H N     1 
ATOM   9981  C CA    . ASP H 2 44  ? 50.931  -54.954 62.167  1.00 44.06  ? 46  ASP H CA    1 
ATOM   9982  C C     . ASP H 2 44  ? 49.617  -54.771 62.921  1.00 42.69  ? 46  ASP H C     1 
ATOM   9983  O O     . ASP H 2 44  ? 49.460  -55.266 64.034  1.00 42.45  ? 46  ASP H O     1 
ATOM   9984  C CB    . ASP H 2 44  ? 51.644  -56.232 62.579  1.00 47.42  ? 46  ASP H CB    1 
ATOM   9985  C CG    . ASP H 2 44  ? 50.869  -57.520 62.336  1.00 51.20  ? 46  ASP H CG    1 
ATOM   9986  O OD1   . ASP H 2 44  ? 49.718  -57.431 61.858  1.00 52.13  ? 46  ASP H OD1   1 
ATOM   9987  O OD2   . ASP H 2 44  ? 51.424  -58.601 62.622  1.00 53.30  ? 46  ASP H OD2   1 
ATOM   9988  N N     . MET H 2 45  ? 48.671  -54.070 62.287  1.00 44.88  ? 47  MET H N     1 
ATOM   9989  C CA    . MET H 2 45  ? 47.410  -53.724 62.922  1.00 46.17  ? 47  MET H CA    1 
ATOM   9990  C C     . MET H 2 45  ? 46.641  -54.994 63.283  1.00 51.05  ? 47  MET H C     1 
ATOM   9991  O O     . MET H 2 45  ? 45.982  -55.047 64.319  1.00 54.69  ? 47  MET H O     1 
ATOM   9992  C CB    . MET H 2 45  ? 46.554  -52.845 62.002  1.00 46.59  ? 47  MET H CB    1 
ATOM   9993  C CG    . MET H 2 45  ? 47.148  -51.475 61.710  1.00 45.14  ? 47  MET H CG    1 
ATOM   9994  S SD    . MET H 2 45  ? 47.592  -50.546 63.192  1.00 42.92  ? 47  MET H SD    1 
ATOM   9995  C CE    . MET H 2 45  ? 49.249  -51.162 63.521  1.00 44.24  ? 47  MET H CE    1 
ATOM   9996  N N     . GLU H 2 46  ? 46.732  -56.013 62.420  1.00 52.30  ? 48  GLU H N     1 
ATOM   9997  C CA    . GLU H 2 46  ? 45.995  -57.252 62.618  1.00 57.72  ? 48  GLU H CA    1 
ATOM   9998  C C     . GLU H 2 46  ? 46.351  -57.851 63.976  1.00 59.29  ? 48  GLU H C     1 
ATOM   9999  O O     . GLU H 2 46  ? 45.470  -58.110 64.791  1.00 65.98  ? 48  GLU H O     1 
ATOM   10000 C CB    . GLU H 2 46  ? 46.274  -58.244 61.489  1.00 61.97  ? 48  GLU H CB    1 
ATOM   10001 C CG    . GLU H 2 46  ? 45.734  -59.645 61.763  1.00 69.94  ? 48  GLU H CG    1 
ATOM   10002 C CD    . GLU H 2 46  ? 44.225  -59.731 61.913  1.00 72.49  ? 48  GLU H CD    1 
ATOM   10003 O OE1   . GLU H 2 46  ? 43.555  -58.683 61.805  1.00 71.61  ? 48  GLU H OE1   1 
ATOM   10004 O OE2   . GLU H 2 46  ? 43.719  -60.852 62.136  1.00 72.77  ? 48  GLU H OE2   1 
ATOM   10005 N N     . LYS H 2 47  ? 47.649  -58.075 64.205  1.00 59.60  ? 49  LYS H N     1 
ATOM   10006 C CA    . LYS H 2 47  ? 48.118  -58.629 65.463  1.00 58.45  ? 49  LYS H CA    1 
ATOM   10007 C C     . LYS H 2 47  ? 47.544  -57.826 66.625  1.00 57.38  ? 49  LYS H C     1 
ATOM   10008 O O     . LYS H 2 47  ? 47.087  -58.396 67.614  1.00 60.45  ? 49  LYS H O     1 
ATOM   10009 C CB    . LYS H 2 47  ? 49.646  -58.604 65.538  1.00 59.30  ? 49  LYS H CB    1 
ATOM   10010 C CG    . LYS H 2 47  ? 50.219  -59.076 66.860  1.00 59.72  ? 49  LYS H CG    1 
ATOM   10011 C CD    . LYS H 2 47  ? 49.793  -60.498 67.195  1.00 60.92  ? 49  LYS H CD    1 
ATOM   10012 C CE    . LYS H 2 47  ? 50.955  -61.352 67.579  1.00 60.86  ? 49  LYS H CE    1 
ATOM   10013 N NZ    . LYS H 2 47  ? 50.536  -62.707 67.944  1.00 62.31  ? 49  LYS H NZ    1 
ATOM   10014 N N     . LEU H 2 48  ? 47.595  -56.497 66.501  1.00 51.78  ? 50  LEU H N     1 
ATOM   10015 C CA    . LEU H 2 48  ? 47.091  -55.617 67.541  1.00 49.56  ? 50  LEU H CA    1 
ATOM   10016 C C     . LEU H 2 48  ? 45.617  -55.927 67.782  1.00 50.19  ? 50  LEU H C     1 
ATOM   10017 O O     . LEU H 2 48  ? 45.137  -55.845 68.909  1.00 47.84  ? 50  LEU H O     1 
ATOM   10018 C CB    . LEU H 2 48  ? 47.301  -54.154 67.156  1.00 46.04  ? 50  LEU H CB    1 
ATOM   10019 C CG    . LEU H 2 48  ? 48.734  -53.629 67.279  1.00 44.35  ? 50  LEU H CG    1 
ATOM   10020 C CD1   . LEU H 2 48  ? 48.798  -52.154 66.926  1.00 42.82  ? 50  LEU H CD1   1 
ATOM   10021 C CD2   . LEU H 2 48  ? 49.279  -53.872 68.676  1.00 44.04  ? 50  LEU H CD2   1 
ATOM   10022 N N     . LYS H 2 49  ? 44.913  -56.284 66.703  1.00 53.33  ? 51  LYS H N     1 
ATOM   10023 C CA    . LYS H 2 49  ? 43.510  -56.650 66.785  1.00 56.20  ? 51  LYS H CA    1 
ATOM   10024 C C     . LYS H 2 49  ? 43.392  -58.050 67.382  1.00 56.26  ? 51  LYS H C     1 
ATOM   10025 O O     . LYS H 2 49  ? 42.454  -58.337 68.122  1.00 64.46  ? 51  LYS H O     1 
ATOM   10026 C CB    . LYS H 2 49  ? 42.866  -56.564 65.397  1.00 58.90  ? 51  LYS H CB    1 
ATOM   10027 C CG    . LYS H 2 49  ? 42.787  -55.157 64.823  1.00 59.75  ? 51  LYS H CG    1 
ATOM   10028 C CD    . LYS H 2 49  ? 42.131  -55.076 63.451  1.00 65.52  ? 51  LYS H CD    1 
ATOM   10029 C CE    . LYS H 2 49  ? 41.874  -53.664 63.029  1.00 65.58  ? 51  LYS H CE    1 
ATOM   10030 N NZ    . LYS H 2 49  ? 40.945  -53.597 61.899  1.00 64.79  ? 51  LYS H NZ    1 
ATOM   10031 N N     . THR H 2 50  ? 44.360  -58.910 67.052  1.00 59.38  ? 52  THR H N     1 
ATOM   10032 C CA    . THR H 2 50  ? 44.399  -60.267 67.569  1.00 60.14  ? 52  THR H CA    1 
ATOM   10033 C C     . THR H 2 50  ? 44.620  -60.225 69.078  1.00 59.53  ? 52  THR H C     1 
ATOM   10034 O O     . THR H 2 50  ? 44.008  -60.989 69.821  1.00 56.18  ? 52  THR H O     1 
ATOM   10035 C CB    . THR H 2 50  ? 45.503  -61.052 66.861  1.00 61.09  ? 52  THR H CB    1 
ATOM   10036 O OG1   . THR H 2 50  ? 45.081  -61.158 65.505  1.00 66.74  ? 52  THR H OG1   1 
ATOM   10037 C CG2   . THR H 2 50  ? 45.709  -62.434 67.455  1.00 63.84  ? 52  THR H CG2   1 
ATOM   10038 N N     . LEU H 2 51  ? 45.505  -59.323 69.517  1.00 59.86  ? 53  LEU H N     1 
ATOM   10039 C CA    . LEU H 2 51  ? 45.842  -59.196 70.925  1.00 58.24  ? 53  LEU H CA    1 
ATOM   10040 C C     . LEU H 2 51  ? 44.755  -58.397 71.639  1.00 58.10  ? 53  LEU H C     1 
ATOM   10041 O O     . LEU H 2 51  ? 44.689  -58.392 72.866  1.00 53.43  ? 53  LEU H O     1 
ATOM   10042 C CB    . LEU H 2 51  ? 47.215  -58.541 71.073  1.00 54.18  ? 53  LEU H CB    1 
ATOM   10043 C CG    . LEU H 2 51  ? 48.408  -59.376 70.596  1.00 53.94  ? 53  LEU H CG    1 
ATOM   10044 C CD1   . LEU H 2 51  ? 49.697  -58.575 70.662  1.00 49.40  ? 53  LEU H CD1   1 
ATOM   10045 C CD2   . LEU H 2 51  ? 48.533  -60.654 71.408  1.00 56.50  ? 53  LEU H CD2   1 
ATOM   10046 N N     . SER H 2 52  ? 43.906  -57.727 70.853  1.00 57.37  ? 54  SER H N     1 
ATOM   10047 C CA    . SER H 2 52  ? 42.786  -56.974 71.394  1.00 63.02  ? 54  SER H CA    1 
ATOM   10048 C C     . SER H 2 52  ? 41.490  -57.747 71.166  1.00 69.43  ? 54  SER H C     1 
ATOM   10049 O O     . SER H 2 52  ? 40.450  -57.155 70.885  1.00 74.84  ? 54  SER H O     1 
ATOM   10050 C CB    . SER H 2 52  ? 42.715  -55.595 70.788  1.00 63.24  ? 54  SER H CB    1 
ATOM   10051 O OG    . SER H 2 52  ? 41.613  -54.864 71.309  1.00 64.19  ? 54  SER H OG    1 
ATOM   10052 N N     . GLY H 2 53  ? 41.570  -59.076 71.295  1.00 68.62  ? 55  GLY H N     1 
ATOM   10053 C CA    . GLY H 2 53  ? 40.427  -59.942 71.061  1.00 69.20  ? 55  GLY H CA    1 
ATOM   10054 C C     . GLY H 2 53  ? 39.478  -59.329 70.037  1.00 69.07  ? 55  GLY H C     1 
ATOM   10055 O O     . GLY H 2 53  ? 38.268  -59.286 70.251  1.00 75.10  ? 55  GLY H O     1 
ATOM   10056 N N     . ASP H 2 54  ? 40.048  -58.857 68.923  1.00 72.56  ? 56  ASP H N     1 
ATOM   10057 C CA    . ASP H 2 54  ? 39.282  -58.178 67.892  1.00 79.33  ? 56  ASP H CA    1 
ATOM   10058 C C     . ASP H 2 54  ? 39.202  -59.068 66.656  1.00 81.05  ? 56  ASP H C     1 
ATOM   10059 O O     . ASP H 2 54  ? 39.618  -58.669 65.570  1.00 86.95  ? 56  ASP H O     1 
ATOM   10060 C CB    . ASP H 2 54  ? 39.885  -56.819 67.567  1.00 86.70  ? 56  ASP H CB    1 
ATOM   10061 C CG    . ASP H 2 54  ? 39.039  -55.924 66.673  1.00 92.37  ? 56  ASP H CG    1 
ATOM   10062 O OD1   . ASP H 2 54  ? 37.903  -56.327 66.346  1.00 104.50 ? 56  ASP H OD1   1 
ATOM   10063 O OD2   . ASP H 2 54  ? 39.526  -54.833 66.308  1.00 91.80  ? 56  ASP H OD2   1 
ATOM   10064 N N     . SER H 2 55  ? 38.659  -60.276 66.838  1.00 80.35  ? 57  SER H N     1 
ATOM   10065 C CA    . SER H 2 55  ? 38.496  -61.221 65.746  1.00 80.96  ? 57  SER H CA    1 
ATOM   10066 C C     . SER H 2 55  ? 37.566  -60.636 64.687  1.00 82.76  ? 57  SER H C     1 
ATOM   10067 O O     . SER H 2 55  ? 37.544  -61.099 63.548  1.00 90.22  ? 57  SER H O     1 
ATOM   10068 C CB    . SER H 2 55  ? 37.990  -62.551 66.249  1.00 80.24  ? 57  SER H CB    1 
ATOM   10069 O OG    . SER H 2 55  ? 36.866  -62.382 67.102  1.00 74.46  ? 57  SER H OG    1 
ATOM   10070 N N     . SER H 2 56  ? 36.803  -59.610 65.079  1.00 83.76  ? 58  SER H N     1 
ATOM   10071 C CA    . SER H 2 56  ? 35.876  -58.946 64.179  1.00 83.10  ? 58  SER H CA    1 
ATOM   10072 C C     . SER H 2 56  ? 36.180  -59.347 62.728  1.00 79.19  ? 58  SER H C     1 
ATOM   10073 O O     . SER H 2 56  ? 36.763  -58.504 62.010  1.00 80.19  ? 58  SER H O     1 
ATOM   10074 C CB    . SER H 2 56  ? 35.928  -57.449 64.355  1.00 85.67  ? 58  SER H CB    1 
ATOM   10075 O OG    . SER H 2 56  ? 35.014  -56.799 63.481  1.00 90.36  ? 58  SER H OG    1 
ATOM   10076 N N     . ALA H 2 60  ? 32.444  -54.846 57.255  1.00 68.99  ? 62  ALA H N     1 
ATOM   10077 C CA    . ALA H 2 60  ? 32.368  -54.184 55.930  1.00 70.00  ? 62  ALA H CA    1 
ATOM   10078 C C     . ALA H 2 60  ? 32.061  -52.701 56.119  1.00 68.18  ? 62  ALA H C     1 
ATOM   10079 O O     . ALA H 2 60  ? 31.005  -52.340 56.634  1.00 69.35  ? 62  ALA H O     1 
ATOM   10080 C CB    . ALA H 2 60  ? 31.328  -54.868 55.071  1.00 69.93  ? 62  ALA H CB    1 
ATOM   10081 N N     . LEU H 2 61  ? 33.004  -51.852 55.696  1.00 61.33  ? 63  LEU H N     1 
ATOM   10082 C CA    . LEU H 2 61  ? 32.917  -50.421 55.932  1.00 57.37  ? 63  LEU H CA    1 
ATOM   10083 C C     . LEU H 2 61  ? 32.361  -49.723 54.693  1.00 54.54  ? 63  LEU H C     1 
ATOM   10084 O O     . LEU H 2 61  ? 32.345  -48.496 54.623  1.00 52.89  ? 63  LEU H O     1 
ATOM   10085 C CB    . LEU H 2 61  ? 34.303  -49.895 56.303  1.00 58.90  ? 63  LEU H CB    1 
ATOM   10086 C CG    . LEU H 2 61  ? 34.998  -50.613 57.465  1.00 62.06  ? 63  LEU H CG    1 
ATOM   10087 C CD1   . LEU H 2 61  ? 36.333  -49.965 57.789  1.00 65.87  ? 63  LEU H CD1   1 
ATOM   10088 C CD2   . LEU H 2 61  ? 34.105  -50.647 58.694  1.00 58.42  ? 63  LEU H CD2   1 
ATOM   10089 N N     . VAL H 2 62  ? 31.909  -50.522 53.721  1.00 48.65  ? 64  VAL H N     1 
ATOM   10090 C CA    . VAL H 2 62  ? 31.307  -49.999 52.506  1.00 48.83  ? 64  VAL H CA    1 
ATOM   10091 C C     . VAL H 2 62  ? 29.845  -49.643 52.762  1.00 48.58  ? 64  VAL H C     1 
ATOM   10092 O O     . VAL H 2 62  ? 29.053  -50.521 53.107  1.00 41.02  ? 64  VAL H O     1 
ATOM   10093 C CB    . VAL H 2 62  ? 31.433  -51.022 51.359  1.00 53.47  ? 64  VAL H CB    1 
ATOM   10094 C CG1   . VAL H 2 62  ? 30.743  -50.539 50.090  1.00 54.07  ? 64  VAL H CG1   1 
ATOM   10095 C CG2   . VAL H 2 62  ? 32.886  -51.385 51.076  1.00 54.52  ? 64  VAL H CG2   1 
HETATM 10096 N N     . IML H 2 63  ? 29.434  -48.362 52.601  1.00 50.03  ? 65  IML H N     1 
HETATM 10097 C CA    . IML H 2 63  ? 28.013  -48.020 52.752  1.00 47.43  ? 65  IML H CA    1 
HETATM 10098 C C     . IML H 2 63  ? 27.510  -47.233 51.545  1.00 46.23  ? 65  IML H C     1 
HETATM 10099 O O     . IML H 2 63  ? 26.750  -46.279 51.697  1.00 43.36  ? 65  IML H O     1 
HETATM 10100 C CB    . IML H 2 63  ? 27.761  -47.237 54.062  1.00 47.45  ? 65  IML H CB    1 
HETATM 10101 C CN    . IML H 2 63  ? 30.346  -47.280 52.268  1.00 52.71  ? 65  IML H CN    1 
HETATM 10102 C CG2   . IML H 2 63  ? 26.499  -47.723 54.757  1.00 47.15  ? 65  IML H CG2   1 
HETATM 10103 C CG1   . IML H 2 63  ? 28.972  -47.281 54.999  1.00 49.61  ? 65  IML H CG1   1 
HETATM 10104 C CD1   . IML H 2 63  ? 29.087  -46.078 55.908  1.00 46.10  ? 65  IML H CD1   1 
ATOM   10105 N N     . SER H 2 64  ? 27.933  -47.650 50.346  1.00 48.87  ? 66  SER H N     1 
ATOM   10106 C CA    . SER H 2 64  ? 27.521  -46.988 49.119  1.00 44.99  ? 66  SER H CA    1 
ATOM   10107 C C     . SER H 2 64  ? 27.833  -47.865 47.908  1.00 41.22  ? 66  SER H C     1 
ATOM   10108 O O     . SER H 2 64  ? 28.628  -48.797 47.996  1.00 47.00  ? 66  SER H O     1 
ATOM   10109 C CB    . SER H 2 64  ? 28.173  -45.633 48.988  1.00 44.54  ? 66  SER H CB    1 
ATOM   10110 O OG    . SER H 2 64  ? 29.590  -45.742 49.006  1.00 43.93  ? 66  SER H OG    1 
ATOM   10111 N N     . HIS H 2 65  ? 27.186  -47.545 46.781  1.00 38.59  ? 67  HIS H N     1 
ATOM   10112 C CA    . HIS H 2 65  ? 27.443  -48.211 45.515  1.00 42.00  ? 67  HIS H CA    1 
ATOM   10113 C C     . HIS H 2 65  ? 27.426  -47.173 44.396  1.00 39.36  ? 67  HIS H C     1 
ATOM   10114 O O     . HIS H 2 65  ? 27.106  -46.010 44.627  1.00 40.11  ? 67  HIS H O     1 
ATOM   10115 C CB    . HIS H 2 65  ? 26.416  -49.319 45.257  1.00 44.78  ? 67  HIS H CB    1 
ATOM   10116 C CG    . HIS H 2 65  ? 25.003  -48.839 45.249  1.00 46.76  ? 67  HIS H CG    1 
ATOM   10117 N ND1   . HIS H 2 65  ? 24.453  -48.149 44.190  1.00 48.79  ? 67  HIS H ND1   1 
ATOM   10118 C CD2   . HIS H 2 65  ? 24.041  -48.919 46.178  1.00 51.90  ? 67  HIS H CD2   1 
ATOM   10119 C CE1   . HIS H 2 65  ? 23.195  -47.842 44.475  1.00 51.39  ? 67  HIS H CE1   1 
ATOM   10120 N NE2   . HIS H 2 65  ? 22.923  -48.303 45.676  1.00 53.15  ? 67  HIS H NE2   1 
ATOM   10121 N N     . GLY H 2 66  ? 27.763  -47.614 43.180  1.00 40.86  ? 68  GLY H N     1 
ATOM   10122 C CA    . GLY H 2 66  ? 27.814  -46.728 42.030  1.00 40.06  ? 68  GLY H CA    1 
ATOM   10123 C C     . GLY H 2 66  ? 27.088  -47.324 40.828  1.00 42.55  ? 68  GLY H C     1 
ATOM   10124 O O     . GLY H 2 66  ? 27.433  -47.032 39.686  1.00 43.03  ? 68  GLY H O     1 
ATOM   10125 N N     . ASN H 2 67  ? 26.080  -48.161 41.100  1.00 43.79  ? 69  ASN H N     1 
ATOM   10126 C CA    . ASN H 2 67  ? 25.276  -48.761 40.048  1.00 46.29  ? 69  ASN H CA    1 
ATOM   10127 C C     . ASN H 2 67  ? 24.090  -47.851 39.741  1.00 47.07  ? 69  ASN H C     1 
ATOM   10128 O O     . ASN H 2 67  ? 23.207  -48.215 38.967  1.00 49.09  ? 69  ASN H O     1 
ATOM   10129 C CB    . ASN H 2 67  ? 24.824  -50.171 40.415  1.00 46.33  ? 69  ASN H CB    1 
ATOM   10130 C CG    . ASN H 2 67  ? 25.990  -51.108 40.625  1.00 47.44  ? 69  ASN H CG    1 
ATOM   10131 O OD1   . ASN H 2 67  ? 27.145  -50.669 40.651  1.00 47.42  ? 69  ASN H OD1   1 
ATOM   10132 N ND2   . ASN H 2 67  ? 25.712  -52.394 40.787  1.00 48.05  ? 69  ASN H ND2   1 
ATOM   10133 N N     . GLY H 2 68  ? 24.085  -46.666 40.361  1.00 47.58  ? 70  GLY H N     1 
ATOM   10134 C CA    . GLY H 2 68  ? 23.039  -45.682 40.139  1.00 48.67  ? 70  GLY H CA    1 
ATOM   10135 C C     . GLY H 2 68  ? 21.734  -46.108 40.787  1.00 50.11  ? 70  GLY H C     1 
ATOM   10136 O O     . GLY H 2 68  ? 20.766  -45.326 40.681  1.00 51.35  ? 70  GLY H O     1 
HETATM 10137 N N     . SAH I 4 .   ? 16.743  -16.448 0.816   1.00 36.90  ? 301 SAH A N     1 
HETATM 10138 C CA    . SAH I 4 .   ? 15.325  -16.087 0.545   1.00 35.68  ? 301 SAH A CA    1 
HETATM 10139 C CB    . SAH I 4 .   ? 15.188  -15.355 -0.793  1.00 37.34  ? 301 SAH A CB    1 
HETATM 10140 C CG    . SAH I 4 .   ? 16.218  -14.262 -0.998  1.00 38.89  ? 301 SAH A CG    1 
HETATM 10141 S SD    . SAH I 4 .   ? 16.134  -13.508 -2.643  1.00 39.37  ? 301 SAH A SD    1 
HETATM 10142 C C     . SAH I 4 .   ? 14.474  -17.362 0.511   1.00 33.79  ? 301 SAH A C     1 
HETATM 10143 O O     . SAH I 4 .   ? 14.979  -18.396 0.989   1.00 35.77  ? 301 SAH A O     1 
HETATM 10144 O OXT   . SAH I 4 .   ? 13.340  -17.273 0.003   1.00 33.49  ? 301 SAH A OXT   1 
HETATM 10145 C "C5'" . SAH I 4 .   ? 14.683  -12.436 -2.490  1.00 39.17  ? 301 SAH A "C5'" 1 
HETATM 10146 C "C4'" . SAH I 4 .   ? 13.515  -12.872 -3.341  1.00 35.06  ? 301 SAH A "C4'" 1 
HETATM 10147 O "O4'" . SAH I 4 .   ? 12.855  -13.997 -2.717  1.00 36.82  ? 301 SAH A "O4'" 1 
HETATM 10148 C "C3'" . SAH I 4 .   ? 12.421  -11.827 -3.518  1.00 34.60  ? 301 SAH A "C3'" 1 
HETATM 10149 O "O3'" . SAH I 4 .   ? 12.727  -10.938 -4.586  1.00 32.08  ? 301 SAH A "O3'" 1 
HETATM 10150 C "C2'" . SAH I 4 .   ? 11.213  -12.714 -3.824  1.00 34.14  ? 301 SAH A "C2'" 1 
HETATM 10151 O "O2'" . SAH I 4 .   ? 11.190  -13.148 -5.166  1.00 33.39  ? 301 SAH A "O2'" 1 
HETATM 10152 C "C1'" . SAH I 4 .   ? 11.455  -13.874 -2.861  1.00 35.78  ? 301 SAH A "C1'" 1 
HETATM 10153 N N9    . SAH I 4 .   ? 10.873  -13.666 -1.540  1.00 36.93  ? 301 SAH A N9    1 
HETATM 10154 C C8    . SAH I 4 .   ? 11.517  -13.187 -0.427  1.00 39.64  ? 301 SAH A C8    1 
HETATM 10155 N N7    . SAH I 4 .   ? 10.741  -13.097 0.624   1.00 38.24  ? 301 SAH A N7    1 
HETATM 10156 C C5    . SAH I 4 .   ? 9.505   -13.541 0.177   1.00 39.56  ? 301 SAH A C5    1 
HETATM 10157 C C6    . SAH I 4 .   ? 8.261   -13.684 0.822   1.00 40.26  ? 301 SAH A C6    1 
HETATM 10158 N N6    . SAH I 4 .   ? 8.054   -13.385 2.101   1.00 39.28  ? 301 SAH A N6    1 
HETATM 10159 N N1    . SAH I 4 .   ? 7.227   -14.155 0.086   1.00 40.46  ? 301 SAH A N1    1 
HETATM 10160 C C2    . SAH I 4 .   ? 7.443   -14.456 -1.200  1.00 41.07  ? 301 SAH A C2    1 
HETATM 10161 N N3    . SAH I 4 .   ? 8.563   -14.362 -1.910  1.00 40.02  ? 301 SAH A N3    1 
HETATM 10162 C C4    . SAH I 4 .   ? 9.572   -13.893 -1.157  1.00 39.30  ? 301 SAH A C4    1 
HETATM 10163 N N     . SAH J 4 .   ? 9.283   -34.657 0.660   0.50 20.32  ? 301 SAH C N     1 
HETATM 10164 C CA    . SAH J 4 .   ? 10.663  -35.164 0.428   0.50 20.89  ? 301 SAH C CA    1 
HETATM 10165 C CB    . SAH J 4 .   ? 10.783  -35.815 -0.953  0.50 20.73  ? 301 SAH C CB    1 
HETATM 10166 C CG    . SAH J 4 .   ? 9.983   -37.096 -1.089  0.50 21.16  ? 301 SAH C CG    1 
HETATM 10167 S SD    . SAH J 4 .   ? 10.010  -37.777 -2.765  0.50 21.98  ? 301 SAH C SD    1 
HETATM 10168 C C     . SAH J 4 .   ? 11.654  -33.999 0.528   0.50 21.68  ? 301 SAH C C     1 
HETATM 10169 O O     . SAH J 4 .   ? 11.287  -32.992 1.166   0.50 21.46  ? 301 SAH C O     1 
HETATM 10170 O OXT   . SAH J 4 .   ? 12.757  -34.143 -0.037  0.50 21.55  ? 301 SAH C OXT   1 
HETATM 10171 C "C5'" . SAH J 4 .   ? 11.419  -38.910 -2.692  0.50 21.11  ? 301 SAH C "C5'" 1 
HETATM 10172 C "C4'" . SAH J 4 .   ? 12.627  -38.405 -3.440  0.50 20.43  ? 301 SAH C "C4'" 1 
HETATM 10173 O "O4'" . SAH J 4 .   ? 13.248  -37.337 -2.688  0.50 19.90  ? 301 SAH C "O4'" 1 
HETATM 10174 C "C3'" . SAH J 4 .   ? 13.740  -39.423 -3.647  0.50 20.52  ? 301 SAH C "C3'" 1 
HETATM 10175 O "O3'" . SAH J 4 .   ? 13.489  -40.244 -4.781  0.50 20.95  ? 301 SAH C "O3'" 1 
HETATM 10176 C "C2'" . SAH J 4 .   ? 14.941  -38.501 -3.856  0.50 19.92  ? 301 SAH C "C2'" 1 
HETATM 10177 O "O2'" . SAH J 4 .   ? 15.006  -37.983 -5.167  0.50 19.24  ? 301 SAH C "O2'" 1 
HETATM 10178 C "C1'" . SAH J 4 .   ? 14.651  -37.400 -2.837  0.50 19.64  ? 301 SAH C "C1'" 1 
HETATM 10179 N N9    . SAH J 4 .   ? 15.247  -37.650 -1.530  0.50 19.89  ? 301 SAH C N9    1 
HETATM 10180 C C8    . SAH J 4 .   ? 14.628  -38.199 -0.435  0.50 18.28  ? 301 SAH C C8    1 
HETATM 10181 N N7    . SAH J 4 .   ? 15.419  -38.318 0.602   0.50 19.29  ? 301 SAH C N7    1 
HETATM 10182 C C5    . SAH J 4 .   ? 16.638  -37.821 0.165   0.50 18.81  ? 301 SAH C C5    1 
HETATM 10183 C C6    . SAH J 4 .   ? 17.885  -37.676 0.802   0.50 17.95  ? 301 SAH C C6    1 
HETATM 10184 N N6    . SAH J 4 .   ? 18.116  -38.029 2.063   0.50 18.78  ? 301 SAH C N6    1 
HETATM 10185 N N1    . SAH J 4 .   ? 18.898  -37.145 0.078   0.50 16.81  ? 301 SAH C N1    1 
HETATM 10186 C C2    . SAH J 4 .   ? 18.659  -36.790 -1.191  0.50 15.90  ? 301 SAH C C2    1 
HETATM 10187 N N3    . SAH J 4 .   ? 17.533  -36.877 -1.891  0.50 16.43  ? 301 SAH C N3    1 
HETATM 10188 C C4    . SAH J 4 .   ? 16.546  -37.407 -1.150  0.50 18.62  ? 301 SAH C C4    1 
HETATM 10189 N N     . SAH K 4 .   ? 39.250  -23.528 55.094  1.00 32.66  ? 301 SAH E N     1 
HETATM 10190 C CA    . SAH K 4 .   ? 37.826  -23.209 54.805  1.00 30.78  ? 301 SAH E CA    1 
HETATM 10191 C CB    . SAH K 4 .   ? 37.686  -22.483 53.464  1.00 30.49  ? 301 SAH E CB    1 
HETATM 10192 C CG    . SAH K 4 .   ? 38.707  -21.381 53.258  1.00 32.39  ? 301 SAH E CG    1 
HETATM 10193 S SD    . SAH K 4 .   ? 38.624  -20.640 51.607  1.00 32.82  ? 301 SAH E SD    1 
HETATM 10194 C C     . SAH K 4 .   ? 37.015  -24.508 54.762  1.00 32.10  ? 301 SAH E C     1 
HETATM 10195 O O     . SAH K 4 .   ? 37.436  -25.464 55.442  1.00 31.88  ? 301 SAH E O     1 
HETATM 10196 O OXT   . SAH K 4 .   ? 35.995  -24.519 54.042  1.00 29.21  ? 301 SAH E OXT   1 
HETATM 10197 C "C5'" . SAH K 4 .   ? 37.181  -19.561 51.752  1.00 32.19  ? 301 SAH E "C5'" 1 
HETATM 10198 C "C4'" . SAH K 4 .   ? 36.014  -20.000 50.903  1.00 31.94  ? 301 SAH E "C4'" 1 
HETATM 10199 O "O4'" . SAH K 4 .   ? 35.362  -21.128 51.530  1.00 31.74  ? 301 SAH E "O4'" 1 
HETATM 10200 C "C3'" . SAH K 4 .   ? 34.917  -18.958 50.727  1.00 33.27  ? 301 SAH E "C3'" 1 
HETATM 10201 O "O3'" . SAH K 4 .   ? 35.208  -18.083 49.644  1.00 29.73  ? 301 SAH E "O3'" 1 
HETATM 10202 C "C2'" . SAH K 4 .   ? 33.705  -19.846 50.445  1.00 32.69  ? 301 SAH E "C2'" 1 
HETATM 10203 O "O2'" . SAH K 4 .   ? 33.658  -20.279 49.104  1.00 31.43  ? 301 SAH E "O2'" 1 
HETATM 10204 C "C1'" . SAH K 4 .   ? 33.961  -21.007 51.403  1.00 33.63  ? 301 SAH E "C1'" 1 
HETATM 10205 N N9    . SAH K 4 .   ? 33.393  -20.805 52.731  1.00 38.80  ? 301 SAH E N9    1 
HETATM 10206 C C8    . SAH K 4 .   ? 34.052  -20.355 53.848  1.00 36.70  ? 301 SAH E C8    1 
HETATM 10207 N N7    . SAH K 4 .   ? 33.284  -20.266 54.904  1.00 32.11  ? 301 SAH E N7    1 
HETATM 10208 C C5    . SAH K 4 .   ? 32.038  -20.681 54.461  1.00 36.26  ? 301 SAH E C5    1 
HETATM 10209 C C6    . SAH K 4 .   ? 30.797  -20.812 55.112  1.00 35.84  ? 301 SAH E C6    1 
HETATM 10210 N N6    . SAH K 4 .   ? 30.604  -20.527 56.397  1.00 33.91  ? 301 SAH E N6    1 
HETATM 10211 N N1    . SAH K 4 .   ? 29.749  -21.256 54.377  1.00 36.60  ? 301 SAH E N1    1 
HETATM 10212 C C2    . SAH K 4 .   ? 29.952  -21.542 53.085  1.00 35.70  ? 301 SAH E C2    1 
HETATM 10213 N N3    . SAH K 4 .   ? 31.069  -21.458 52.369  1.00 35.90  ? 301 SAH E N3    1 
HETATM 10214 C C4    . SAH K 4 .   ? 32.091  -21.017 53.121  1.00 38.64  ? 301 SAH E C4    1 
HETATM 10215 N N     . SAH L 4 .   ? 31.832  -41.715 54.975  0.70 22.91  ? 301 SAH G N     1 
HETATM 10216 C CA    . SAH L 4 .   ? 33.210  -42.225 54.736  0.70 23.82  ? 301 SAH G CA    1 
HETATM 10217 C CB    . SAH L 4 .   ? 33.314  -42.906 53.367  0.70 24.68  ? 301 SAH G CB    1 
HETATM 10218 C CG    . SAH L 4 .   ? 32.525  -44.199 53.274  0.70 26.63  ? 301 SAH G CG    1 
HETATM 10219 S SD    . SAH L 4 .   ? 32.540  -44.923 51.618  0.70 27.13  ? 301 SAH G SD    1 
HETATM 10220 C C     . SAH L 4 .   ? 34.201  -41.056 54.798  0.70 24.28  ? 301 SAH G C     1 
HETATM 10221 O O     . SAH L 4 .   ? 33.733  -39.925 55.039  0.70 24.89  ? 301 SAH G O     1 
HETATM 10222 O OXT   . SAH L 4 .   ? 35.404  -41.319 54.601  0.70 22.79  ? 301 SAH G OXT   1 
HETATM 10223 C "C5'" . SAH L 4 .   ? 33.967  -46.029 51.698  0.70 23.74  ? 301 SAH G "C5'" 1 
HETATM 10224 C "C4'" . SAH L 4 .   ? 35.147  -45.544 50.894  0.70 21.97  ? 301 SAH G "C4'" 1 
HETATM 10225 O "O4'" . SAH L 4 .   ? 35.780  -44.441 51.582  0.70 20.53  ? 301 SAH G "O4'" 1 
HETATM 10226 C "C3'" . SAH L 4 .   ? 36.259  -46.565 50.695  0.70 22.16  ? 301 SAH G "C3'" 1 
HETATM 10227 O "O3'" . SAH L 4 .   ? 35.990  -47.422 49.593  0.70 24.46  ? 301 SAH G "O3'" 1 
HETATM 10228 C "C2'" . SAH L 4 .   ? 37.452  -45.646 50.433  0.70 20.74  ? 301 SAH G "C2'" 1 
HETATM 10229 O "O2'" . SAH L 4 .   ? 37.478  -45.165 49.107  0.70 20.36  ? 301 SAH G "O2'" 1 
HETATM 10230 C "C1'" . SAH L 4 .   ? 37.181  -44.525 51.434  0.70 19.77  ? 301 SAH G "C1'" 1 
HETATM 10231 N N9    . SAH L 4 .   ? 37.776  -44.763 52.745  0.70 18.57  ? 301 SAH G N9    1 
HETATM 10232 C C8    . SAH L 4 .   ? 37.161  -45.296 53.849  0.70 18.83  ? 301 SAH G C8    1 
HETATM 10233 N N7    . SAH L 4 .   ? 37.954  -45.406 54.885  0.70 19.97  ? 301 SAH G N7    1 
HETATM 10234 C C5    . SAH L 4 .   ? 39.173  -44.916 54.438  0.70 18.75  ? 301 SAH G C5    1 
HETATM 10235 C C6    . SAH L 4 .   ? 40.423  -44.765 55.070  0.70 18.46  ? 301 SAH G C6    1 
HETATM 10236 N N6    . SAH L 4 .   ? 40.660  -45.103 56.333  0.70 19.57  ? 301 SAH G N6    1 
HETATM 10237 N N1    . SAH L 4 .   ? 41.434  -44.244 54.335  0.70 17.90  ? 301 SAH G N1    1 
HETATM 10238 C C2    . SAH L 4 .   ? 41.191  -43.905 53.063  0.70 16.96  ? 301 SAH G C2    1 
HETATM 10239 N N3    . SAH L 4 .   ? 40.062  -44.000 52.368  0.70 17.30  ? 301 SAH G N3    1 
HETATM 10240 C C4    . SAH L 4 .   ? 39.077  -44.518 53.119  0.70 18.20  ? 301 SAH G C4    1 
HETATM 10241 O O     . HOH M 5 .   ? 12.586  -25.062 -19.611 1.00 38.37  ? 401 HOH A O     1 
HETATM 10242 O O     . HOH M 5 .   ? 14.378  -23.435 -6.661  1.00 33.99  ? 402 HOH A O     1 
HETATM 10243 O O     . HOH M 5 .   ? 6.160   -36.031 -9.378  1.00 35.21  ? 403 HOH A O     1 
HETATM 10244 O O     . HOH M 5 .   ? 31.678  -27.034 5.679   1.00 37.52  ? 404 HOH A O     1 
HETATM 10245 O O     . HOH M 5 .   ? 5.001   -11.015 4.128   1.00 21.28  ? 405 HOH A O     1 
HETATM 10246 O O     . HOH M 5 .   ? 17.926  -14.830 2.297   1.00 25.48  ? 406 HOH A O     1 
HETATM 10247 O O     . HOH M 5 .   ? 1.517   -7.120  -0.209  1.00 48.08  ? 407 HOH A O     1 
HETATM 10248 O O     . HOH M 5 .   ? 2.074   -34.654 -5.952  1.00 42.68  ? 408 HOH A O     1 
HETATM 10249 O O     . HOH M 5 .   ? 12.620  -14.866 -24.459 1.00 29.63  ? 409 HOH A O     1 
HETATM 10250 O O     . HOH M 5 .   ? 12.211  -15.109 13.649  1.00 34.33  ? 410 HOH A O     1 
HETATM 10251 O O     . HOH M 5 .   ? 2.884   -17.719 4.381   1.00 25.03  ? 411 HOH A O     1 
HETATM 10252 O O     . HOH M 5 .   ? 38.106  -22.524 11.894  1.00 30.35  ? 412 HOH A O     1 
HETATM 10253 O O     . HOH M 5 .   ? 2.214   -9.816  1.604   1.00 38.11  ? 413 HOH A O     1 
HETATM 10254 O O     . HOH M 5 .   ? 21.410  -0.106  -4.450  1.00 29.37  ? 414 HOH A O     1 
HETATM 10255 O O     . HOH M 5 .   ? 19.161  -23.244 8.701   1.00 31.68  ? 415 HOH A O     1 
HETATM 10256 O O     . HOH M 5 .   ? 14.673  -17.919 -24.348 1.00 19.82  ? 416 HOH A O     1 
HETATM 10257 O O     . HOH M 5 .   ? -1.760  -26.716 1.233   1.00 27.29  ? 417 HOH A O     1 
HETATM 10258 O O     . HOH M 5 .   ? 7.569   -33.806 -12.332 1.00 25.40  ? 418 HOH A O     1 
HETATM 10259 O O     . HOH M 5 .   ? -0.333  -5.830  -21.081 1.00 29.88  ? 419 HOH A O     1 
HETATM 10260 O O     . HOH M 5 .   ? -3.570  -29.101 -3.993  1.00 26.44  ? 420 HOH A O     1 
HETATM 10261 O O     . HOH M 5 .   ? 4.605   -8.622  7.924   1.00 32.67  ? 421 HOH A O     1 
HETATM 10262 O O     . HOH M 5 .   ? 16.092  -22.940 9.544   1.00 28.67  ? 422 HOH A O     1 
HETATM 10263 O O     . HOH M 5 .   ? 26.049  1.250   3.718   1.00 51.66  ? 423 HOH A O     1 
HETATM 10264 O O     . HOH M 5 .   ? 8.680   3.731   -19.184 1.00 43.09  ? 424 HOH A O     1 
HETATM 10265 O O     . HOH M 5 .   ? 10.076  -9.010  -6.376  1.00 19.94  ? 425 HOH A O     1 
HETATM 10266 O O     . HOH M 5 .   ? 18.657  -7.521  10.120  1.00 31.40  ? 426 HOH A O     1 
HETATM 10267 O O     . HOH M 5 .   ? 5.260   -17.669 5.978   1.00 20.54  ? 427 HOH A O     1 
HETATM 10268 O O     . HOH M 5 .   ? -4.252  -15.450 1.085   1.00 34.50  ? 428 HOH A O     1 
HETATM 10269 O O     . HOH M 5 .   ? 21.703  2.345   -4.421  1.00 30.24  ? 429 HOH A O     1 
HETATM 10270 O O     . HOH M 5 .   ? 35.719  -15.001 -1.864  1.00 47.11  ? 430 HOH A O     1 
HETATM 10271 O O     . HOH M 5 .   ? -1.540  -30.131 -22.976 1.00 34.82  ? 431 HOH A O     1 
HETATM 10272 O O     . HOH M 5 .   ? 2.814   -30.483 -23.464 1.00 39.17  ? 432 HOH A O     1 
HETATM 10273 O O     . HOH M 5 .   ? 5.708   -54.580 -24.498 1.00 37.73  ? 433 HOH A O     1 
HETATM 10274 O O     . HOH M 5 .   ? 5.070   -20.113 5.965   1.00 28.23  ? 434 HOH A O     1 
HETATM 10275 O O     . HOH M 5 .   ? 18.197  -17.375 -11.965 1.00 20.28  ? 435 HOH A O     1 
HETATM 10276 O O     . HOH M 5 .   ? 14.215  -51.641 -23.710 1.00 46.95  ? 436 HOH A O     1 
HETATM 10277 O O     . HOH M 5 .   ? 26.765  -17.047 23.021  1.00 43.95  ? 437 HOH A O     1 
HETATM 10278 O O     . HOH M 5 .   ? 14.298  -24.248 -1.039  1.00 28.78  ? 438 HOH A O     1 
HETATM 10279 O O     . HOH M 5 .   ? 27.104  -21.376 17.416  1.00 36.06  ? 439 HOH A O     1 
HETATM 10280 O O     . HOH M 5 .   ? 28.331  0.191   7.744   1.00 36.42  ? 440 HOH A O     1 
HETATM 10281 O O     . HOH M 5 .   ? 27.955  -2.498  12.587  1.00 35.71  ? 441 HOH A O     1 
HETATM 10282 O O     . HOH M 5 .   ? 9.320   -8.638  4.495   1.00 45.34  ? 442 HOH A O     1 
HETATM 10283 O O     . HOH M 5 .   ? 22.013  -18.731 -21.750 1.00 37.64  ? 443 HOH A O     1 
HETATM 10284 O O     . HOH M 5 .   ? 12.235  -45.778 -29.963 1.00 35.16  ? 444 HOH A O     1 
HETATM 10285 O O     . HOH M 5 .   ? 23.977  -3.333  13.565  1.00 40.28  ? 445 HOH A O     1 
HETATM 10286 O O     . HOH M 5 .   ? 4.515   -28.814 -10.413 1.00 23.11  ? 446 HOH A O     1 
HETATM 10287 O O     . HOH M 5 .   ? 36.920  -22.177 -1.099  1.00 33.00  ? 447 HOH A O     1 
HETATM 10288 O O     . HOH M 5 .   ? -2.486  -21.490 -9.434  1.00 30.05  ? 448 HOH A O     1 
HETATM 10289 O O     . HOH M 5 .   ? 31.496  -24.059 10.711  1.00 33.81  ? 449 HOH A O     1 
HETATM 10290 O O     . HOH M 5 .   ? 32.649  -4.331  5.717   1.00 37.92  ? 450 HOH A O     1 
HETATM 10291 O O     . HOH M 5 .   ? -4.878  -19.458 -16.991 1.00 24.68  ? 451 HOH A O     1 
HETATM 10292 O O     . HOH M 5 .   ? 27.896  -30.626 10.474  1.00 32.02  ? 452 HOH A O     1 
HETATM 10293 O O     . HOH M 5 .   ? 13.993  -23.710 8.545   1.00 27.51  ? 453 HOH A O     1 
HETATM 10294 O O     . HOH M 5 .   ? 19.971  -5.553  16.084  1.00 27.95  ? 454 HOH A O     1 
HETATM 10295 O O     . HOH M 5 .   ? 13.861  -14.916 21.321  1.00 30.88  ? 455 HOH A O     1 
HETATM 10296 O O     . HOH M 5 .   ? 20.818  3.910   -12.030 1.00 56.13  ? 456 HOH A O     1 
HETATM 10297 O O     . HOH M 5 .   ? 18.638  0.185   3.660   1.00 42.34  ? 457 HOH A O     1 
HETATM 10298 O O     . HOH M 5 .   ? 42.500  -14.444 7.439   1.00 38.39  ? 458 HOH A O     1 
HETATM 10299 O O     . HOH M 5 .   ? 8.277   -2.731  -8.405  1.00 31.76  ? 459 HOH A O     1 
HETATM 10300 O O     . HOH M 5 .   ? -7.370  -48.894 -20.929 1.00 41.40  ? 460 HOH A O     1 
HETATM 10301 O O     . HOH M 5 .   ? 2.241   -2.408  0.124   1.00 40.23  ? 461 HOH A O     1 
HETATM 10302 O O     . HOH M 5 .   ? 6.774   -53.985 -21.457 1.00 43.83  ? 462 HOH A O     1 
HETATM 10303 O O     . HOH M 5 .   ? -3.546  -24.734 -0.505  1.00 40.30  ? 463 HOH A O     1 
HETATM 10304 O O     . HOH M 5 .   ? 10.890  -13.297 10.098  1.00 43.24  ? 464 HOH A O     1 
HETATM 10305 O O     . HOH M 5 .   ? 15.710  -49.628 -26.023 1.00 34.19  ? 465 HOH A O     1 
HETATM 10306 O O     . HOH M 5 .   ? 23.406  -0.472  12.202  1.00 38.90  ? 466 HOH A O     1 
HETATM 10307 O O     . HOH M 5 .   ? 15.630  3.840   -20.622 1.00 29.38  ? 467 HOH A O     1 
HETATM 10308 O O     . HOH M 5 .   ? -5.868  -12.353 9.396   1.00 32.00  ? 468 HOH A O     1 
HETATM 10309 O O     . HOH M 5 .   ? 27.764  -6.906  22.706  1.00 27.47  ? 469 HOH A O     1 
HETATM 10310 O O     . HOH M 5 .   ? -7.132  -32.398 -22.919 1.00 37.69  ? 470 HOH A O     1 
HETATM 10311 O O     . HOH M 5 .   ? -2.704  -32.085 -14.350 1.00 29.67  ? 471 HOH A O     1 
HETATM 10312 O O     . HOH M 5 .   ? 28.965  -28.632 5.692   1.00 38.79  ? 472 HOH A O     1 
HETATM 10313 O O     . HOH M 5 .   ? -6.628  -45.952 -20.111 1.00 37.95  ? 473 HOH A O     1 
HETATM 10314 O O     . HOH M 5 .   ? 16.842  -52.483 -26.133 1.00 43.55  ? 474 HOH A O     1 
HETATM 10315 O O     . HOH M 5 .   ? -7.234  -43.536 -19.674 1.00 45.76  ? 475 HOH A O     1 
HETATM 10316 O O     . HOH N 5 .   ? 7.401   -13.809 23.360  1.00 42.87  ? 101 HOH B O     1 
HETATM 10317 O O     . HOH N 5 .   ? -1.404  2.304   7.276   1.00 50.79  ? 102 HOH B O     1 
HETATM 10318 O O     . HOH N 5 .   ? -14.029 -12.905 20.094  1.00 28.95  ? 103 HOH B O     1 
HETATM 10319 O O     . HOH N 5 .   ? 3.319   -13.809 25.208  1.00 39.91  ? 104 HOH B O     1 
HETATM 10320 O O     . HOH N 5 .   ? 3.295   -21.776 26.263  1.00 46.54  ? 105 HOH B O     1 
HETATM 10321 O O     . HOH N 5 .   ? -0.482  3.511   11.710  1.00 42.91  ? 106 HOH B O     1 
HETATM 10322 O O     . HOH N 5 .   ? -5.491  -13.056 11.555  1.00 34.11  ? 107 HOH B O     1 
HETATM 10323 O O     . HOH N 5 .   ? 12.236  -17.238 21.020  1.00 49.52  ? 108 HOH B O     1 
HETATM 10324 O O     . HOH N 5 .   ? -11.354 -23.762 13.489  1.00 35.53  ? 109 HOH B O     1 
HETATM 10325 O O     . HOH N 5 .   ? 5.385   -19.087 12.805  1.00 33.49  ? 110 HOH B O     1 
HETATM 10326 O O     . HOH N 5 .   ? -1.551  -27.376 18.089  1.00 35.99  ? 111 HOH B O     1 
HETATM 10327 O O     . HOH N 5 .   ? 9.906   3.409   18.665  1.00 40.13  ? 112 HOH B O     1 
HETATM 10328 O O     . HOH O 5 .   ? -1.329  -52.457 9.245   1.00 32.80  ? 401 HOH C O     1 
HETATM 10329 O O     . HOH O 5 .   ? 4.326   -21.458 9.495   1.00 34.83  ? 402 HOH C O     1 
HETATM 10330 O O     . HOH O 5 .   ? 14.474  -33.434 11.992  1.00 25.97  ? 403 HOH C O     1 
HETATM 10331 O O     . HOH O 5 .   ? -11.552 -32.189 18.064  1.00 44.52  ? 404 HOH C O     1 
HETATM 10332 O O     . HOH O 5 .   ? -3.466  -42.612 -4.646  1.00 33.74  ? 405 HOH C O     1 
HETATM 10333 O O     . HOH O 5 .   ? 7.218   -24.452 8.545   1.00 25.97  ? 406 HOH C O     1 
HETATM 10334 O O     . HOH O 5 .   ? 8.812   -26.329 19.486  1.00 19.75  ? 407 HOH C O     1 
HETATM 10335 O O     . HOH O 5 .   ? 11.187  -41.805 -11.507 1.00 28.85  ? 408 HOH C O     1 
HETATM 10336 O O     . HOH O 5 .   ? 7.513   -43.562 10.115  1.00 25.98  ? 409 HOH C O     1 
HETATM 10337 O O     . HOH O 5 .   ? 28.908  -31.059 -14.487 1.00 45.97  ? 410 HOH C O     1 
HETATM 10338 O O     . HOH O 5 .   ? 16.238  -42.178 -5.903  1.00 33.47  ? 411 HOH C O     1 
HETATM 10339 O O     . HOH O 5 .   ? 19.421  -48.137 -25.885 1.00 39.57  ? 412 HOH C O     1 
HETATM 10340 O O     . HOH O 5 .   ? 15.788  -26.034 -23.556 1.00 35.35  ? 413 HOH C O     1 
HETATM 10341 O O     . HOH O 5 .   ? -5.353  -27.513 10.590  1.00 30.97  ? 414 HOH C O     1 
HETATM 10342 O O     . HOH O 5 .   ? 11.382  -53.382 -5.579  1.00 36.65  ? 415 HOH C O     1 
HETATM 10343 O O     . HOH O 5 .   ? 18.917  -21.740 -22.208 1.00 30.82  ? 416 HOH C O     1 
HETATM 10344 O O     . HOH O 5 .   ? 29.390  -30.702 -20.412 1.00 35.08  ? 417 HOH C O     1 
HETATM 10345 O O     . HOH O 5 .   ? 12.132  -28.958 8.426   1.00 35.47  ? 418 HOH C O     1 
HETATM 10346 O O     . HOH O 5 .   ? 9.969   -55.290 -5.685  1.00 33.03  ? 419 HOH C O     1 
HETATM 10347 O O     . HOH O 5 .   ? -6.780  -44.132 11.183  1.00 33.43  ? 420 HOH C O     1 
HETATM 10348 O O     . HOH O 5 .   ? -2.001  -25.206 4.156   1.00 21.11  ? 421 HOH C O     1 
HETATM 10349 O O     . HOH O 5 .   ? 20.882  -40.525 4.034   1.00 25.10  ? 422 HOH C O     1 
HETATM 10350 O O     . HOH O 5 .   ? -6.647  -46.480 5.522   1.00 23.97  ? 423 HOH C O     1 
HETATM 10351 O O     . HOH O 5 .   ? 3.366   -34.907 23.650  1.00 41.30  ? 424 HOH C O     1 
HETATM 10352 O O     . HOH O 5 .   ? 19.462  -54.352 -17.685 1.00 40.71  ? 425 HOH C O     1 
HETATM 10353 O O     . HOH O 5 .   ? -7.881  -25.747 13.149  1.00 26.99  ? 426 HOH C O     1 
HETATM 10354 O O     . HOH O 5 .   ? 22.975  -54.426 -15.314 1.00 38.22  ? 427 HOH C O     1 
HETATM 10355 O O     . HOH O 5 .   ? 21.323  -22.338 -10.224 1.00 36.01  ? 428 HOH C O     1 
HETATM 10356 O O     . HOH O 5 .   ? 21.659  -42.985 7.528   1.00 29.12  ? 429 HOH C O     1 
HETATM 10357 O O     . HOH O 5 .   ? 16.032  -39.110 3.614   1.00 20.66  ? 430 HOH C O     1 
HETATM 10358 O O     . HOH O 5 .   ? -11.932 -45.246 2.675   1.00 39.94  ? 431 HOH C O     1 
HETATM 10359 O O     . HOH O 5 .   ? -7.940  -37.702 -3.178  1.00 42.29  ? 432 HOH C O     1 
HETATM 10360 O O     . HOH O 5 .   ? 14.787  -37.719 26.410  1.00 41.62  ? 433 HOH C O     1 
HETATM 10361 O O     . HOH O 5 .   ? -10.930 -47.259 7.217   1.00 49.88  ? 434 HOH C O     1 
HETATM 10362 O O     . HOH O 5 .   ? 16.219  -42.726 -25.085 1.00 35.80  ? 435 HOH C O     1 
HETATM 10363 O O     . HOH O 5 .   ? 12.541  -27.043 1.519   1.00 25.71  ? 436 HOH C O     1 
HETATM 10364 O O     . HOH O 5 .   ? 12.279  -36.591 21.310  1.00 33.66  ? 437 HOH C O     1 
HETATM 10365 O O     . HOH O 5 .   ? 21.067  -31.275 6.008   1.00 23.38  ? 438 HOH C O     1 
HETATM 10366 O O     . HOH O 5 .   ? 3.544   -53.123 -18.992 1.00 36.96  ? 439 HOH C O     1 
HETATM 10367 O O     . HOH O 5 .   ? -4.277  -30.490 13.932  1.00 23.72  ? 440 HOH C O     1 
HETATM 10368 O O     . HOH O 5 .   ? 30.601  -25.371 -4.235  1.00 42.26  ? 441 HOH C O     1 
HETATM 10369 O O     . HOH O 5 .   ? 27.929  -24.454 1.035   1.00 33.26  ? 442 HOH C O     1 
HETATM 10370 O O     . HOH O 5 .   ? 4.465   -49.575 9.790   1.00 44.44  ? 443 HOH C O     1 
HETATM 10371 O O     . HOH O 5 .   ? -1.347  -30.039 17.350  1.00 25.17  ? 444 HOH C O     1 
HETATM 10372 O O     . HOH O 5 .   ? 21.099  -49.159 -8.497  1.00 40.59  ? 445 HOH C O     1 
HETATM 10373 O O     . HOH O 5 .   ? -8.232  -36.873 21.496  1.00 35.00  ? 446 HOH C O     1 
HETATM 10374 O O     . HOH O 5 .   ? 27.933  -26.417 -11.305 1.00 40.56  ? 447 HOH C O     1 
HETATM 10375 O O     . HOH O 5 .   ? 7.635   -43.371 -11.326 1.00 58.98  ? 448 HOH C O     1 
HETATM 10376 O O     . HOH O 5 .   ? -5.551  -41.760 -4.767  1.00 38.32  ? 449 HOH C O     1 
HETATM 10377 O O     . HOH O 5 .   ? 26.041  -20.412 -6.868  1.00 39.42  ? 450 HOH C O     1 
HETATM 10378 O O     . HOH O 5 .   ? -12.235 -45.839 11.277  1.00 33.61  ? 451 HOH C O     1 
HETATM 10379 O O     . HOH O 5 .   ? 19.172  -49.060 -23.397 1.00 41.90  ? 452 HOH C O     1 
HETATM 10380 O O     . HOH O 5 .   ? 29.310  -29.216 -10.343 1.00 44.72  ? 453 HOH C O     1 
HETATM 10381 O O     . HOH O 5 .   ? 30.015  -26.344 0.257   1.00 35.98  ? 454 HOH C O     1 
HETATM 10382 O O     . HOH O 5 .   ? 8.026   -50.855 4.908   1.00 45.65  ? 455 HOH C O     1 
HETATM 10383 O O     . HOH O 5 .   ? 6.757   -33.681 -28.799 1.00 33.04  ? 456 HOH C O     1 
HETATM 10384 O O     . HOH O 5 .   ? 24.833  -32.147 7.094   1.00 40.16  ? 457 HOH C O     1 
HETATM 10385 O O     . HOH O 5 .   ? -12.172 -48.020 3.036   1.00 34.12  ? 458 HOH C O     1 
HETATM 10386 O O     . HOH O 5 .   ? -5.605  -52.928 -3.464  1.00 34.73  ? 459 HOH C O     1 
HETATM 10387 O O     . HOH O 5 .   ? 24.197  -51.512 -9.007  1.00 38.85  ? 460 HOH C O     1 
HETATM 10388 O O     . HOH O 5 .   ? -2.185  -29.193 0.524   1.00 27.67  ? 461 HOH C O     1 
HETATM 10389 O O     . HOH O 5 .   ? 11.319  -24.961 21.315  1.00 31.67  ? 462 HOH C O     1 
HETATM 10390 O O     . HOH P 5 .   ? 31.061  -38.217 11.899  1.00 28.81  ? 101 HOH D O     1 
HETATM 10391 O O     . HOH P 5 .   ? 13.536  -32.064 17.811  1.00 32.13  ? 102 HOH D O     1 
HETATM 10392 O O     . HOH P 5 .   ? 35.322  -41.002 9.110   1.00 35.53  ? 103 HOH D O     1 
HETATM 10393 O O     . HOH P 5 .   ? 20.760  -31.758 13.079  1.00 20.60  ? 104 HOH D O     1 
HETATM 10394 O O     . HOH P 5 .   ? 15.890  -48.425 9.758   1.00 45.21  ? 105 HOH D O     1 
HETATM 10395 O O     . HOH P 5 .   ? 20.255  -50.944 3.397   1.00 47.87  ? 106 HOH D O     1 
HETATM 10396 O O     . HOH P 5 .   ? -1.928  -41.919 -16.632 1.00 32.84  ? 107 HOH D O     1 
HETATM 10397 O O     . HOH P 5 .   ? 38.135  -49.482 10.489  1.00 38.66  ? 108 HOH D O     1 
HETATM 10398 O O     . HOH P 5 .   ? 40.131  -45.585 17.463  1.00 45.61  ? 109 HOH D O     1 
HETATM 10399 O O     . HOH P 5 .   ? 35.561  -26.319 20.520  1.00 55.28  ? 110 HOH D O     1 
HETATM 10400 O O     . HOH P 5 .   ? 13.847  -34.391 21.023  1.00 24.07  ? 111 HOH D O     1 
HETATM 10401 O O     . HOH P 5 .   ? 18.072  -27.397 20.654  1.00 31.62  ? 112 HOH D O     1 
HETATM 10402 O O     . HOH P 5 .   ? 27.723  -23.907 18.825  1.00 35.47  ? 113 HOH D O     1 
HETATM 10403 O O     . HOH P 5 .   ? 33.568  -53.297 14.622  1.00 39.17  ? 114 HOH D O     1 
HETATM 10404 O O     . HOH P 5 .   ? 30.248  -36.183 29.259  1.00 38.59  ? 115 HOH D O     1 
HETATM 10405 O O     . HOH P 5 .   ? 35.708  -28.419 22.064  1.00 44.50  ? 116 HOH D O     1 
HETATM 10406 O O     . HOH Q 5 .   ? 36.302  -29.577 62.694  1.00 31.17  ? 401 HOH E O     1 
HETATM 10407 O O     . HOH Q 5 .   ? 44.064  -36.764 63.857  1.00 47.62  ? 402 HOH E O     1 
HETATM 10408 O O     . HOH Q 5 .   ? 20.883  -33.559 55.357  1.00 22.32  ? 403 HOH E O     1 
HETATM 10409 O O     . HOH Q 5 .   ? 24.319  -41.528 49.046  1.00 35.73  ? 404 HOH E O     1 
HETATM 10410 O O     . HOH Q 5 .   ? 36.871  -29.868 47.448  1.00 32.80  ? 405 HOH E O     1 
HETATM 10411 O O     . HOH Q 5 .   ? 23.923  -36.609 37.147  1.00 26.19  ? 406 HOH E O     1 
HETATM 10412 O O     . HOH Q 5 .   ? 23.521  -58.342 38.796  1.00 26.45  ? 407 HOH E O     1 
HETATM 10413 O O     . HOH Q 5 .   ? 35.364  -32.831 34.648  1.00 39.74  ? 408 HOH E O     1 
HETATM 10414 O O     . HOH Q 5 .   ? 34.833  -22.155 68.293  1.00 35.46  ? 409 HOH E O     1 
HETATM 10415 O O     . HOH Q 5 .   ? 49.789  -6.159  63.388  1.00 41.94  ? 410 HOH E O     1 
HETATM 10416 O O     . HOH Q 5 .   ? 26.807  -40.224 32.404  1.00 39.02  ? 411 HOH E O     1 
HETATM 10417 O O     . HOH Q 5 .   ? 25.687  -24.679 58.545  1.00 25.25  ? 412 HOH E O     1 
HETATM 10418 O O     . HOH Q 5 .   ? 27.396  -27.935 60.801  1.00 28.60  ? 413 HOH E O     1 
HETATM 10419 O O     . HOH Q 5 .   ? 41.985  -30.008 63.007  1.00 33.59  ? 414 HOH E O     1 
HETATM 10420 O O     . HOH Q 5 .   ? 65.510  -21.595 65.689  1.00 34.08  ? 415 HOH E O     1 
HETATM 10421 O O     . HOH Q 5 .   ? 19.557  -27.381 39.498  1.00 17.21  ? 416 HOH E O     1 
HETATM 10422 O O     . HOH Q 5 .   ? 27.642  -17.914 58.261  1.00 17.33  ? 417 HOH E O     1 
HETATM 10423 O O     . HOH Q 5 .   ? 60.431  -30.136 65.926  1.00 28.76  ? 418 HOH E O     1 
HETATM 10424 O O     . HOH Q 5 .   ? 26.786  -35.916 43.400  1.00 28.05  ? 419 HOH E O     1 
HETATM 10425 O O     . HOH Q 5 .   ? 50.163  -33.425 58.486  1.00 27.78  ? 420 HOH E O     1 
HETATM 10426 O O     . HOH Q 5 .   ? 44.892  -5.478  35.478  1.00 41.18  ? 421 HOH E O     1 
HETATM 10427 O O     . HOH Q 5 .   ? 52.866  -27.608 67.904  1.00 41.49  ? 422 HOH E O     1 
HETATM 10428 O O     . HOH Q 5 .   ? 55.899  -6.918  55.620  1.00 31.29  ? 423 HOH E O     1 
HETATM 10429 O O     . HOH Q 5 .   ? 32.715  -16.210 47.827  1.00 17.81  ? 424 HOH E O     1 
HETATM 10430 O O     . HOH Q 5 .   ? 41.121  -15.159 64.464  1.00 25.11  ? 425 HOH E O     1 
HETATM 10431 O O     . HOH Q 5 .   ? 24.082  -60.979 35.164  1.00 42.36  ? 426 HOH E O     1 
HETATM 10432 O O     . HOH Q 5 .   ? 45.246  -8.245  52.614  1.00 36.97  ? 427 HOH E O     1 
HETATM 10433 O O     . HOH Q 5 .   ? 56.897  -12.413 64.111  1.00 33.87  ? 428 HOH E O     1 
HETATM 10434 O O     . HOH Q 5 .   ? 50.107  -29.219 54.692  1.00 41.28  ? 429 HOH E O     1 
HETATM 10435 O O     . HOH Q 5 .   ? 64.863  -21.743 61.491  1.00 35.28  ? 430 HOH E O     1 
HETATM 10436 O O     . HOH Q 5 .   ? 45.626  -21.726 42.488  1.00 39.34  ? 431 HOH E O     1 
HETATM 10437 O O     . HOH Q 5 .   ? 52.598  -7.498  64.339  1.00 48.15  ? 432 HOH E O     1 
HETATM 10438 O O     . HOH Q 5 .   ? 36.521  -21.950 75.316  1.00 32.16  ? 433 HOH E O     1 
HETATM 10439 O O     . HOH Q 5 .   ? 24.965  -30.354 30.055  1.00 33.73  ? 434 HOH E O     1 
HETATM 10440 O O     . HOH Q 5 .   ? 36.446  -31.715 53.534  1.00 28.83  ? 435 HOH E O     1 
HETATM 10441 O O     . HOH Q 5 .   ? 38.638  -30.147 63.817  1.00 39.04  ? 436 HOH E O     1 
HETATM 10442 O O     . HOH Q 5 .   ? 19.498  -17.461 61.217  1.00 30.49  ? 437 HOH E O     1 
HETATM 10443 O O     . HOH Q 5 .   ? 21.024  -31.616 44.092  1.00 36.51  ? 438 HOH E O     1 
HETATM 10444 O O     . HOH Q 5 .   ? 36.112  -31.810 55.970  1.00 19.30  ? 439 HOH E O     1 
HETATM 10445 O O     . HOH Q 5 .   ? 57.139  -21.502 75.242  1.00 40.49  ? 440 HOH E O     1 
HETATM 10446 O O     . HOH Q 5 .   ? 36.678  -4.816  48.483  1.00 42.36  ? 441 HOH E O     1 
HETATM 10447 O O     . HOH Q 5 .   ? 55.271  -11.565 59.992  1.00 33.16  ? 442 HOH E O     1 
HETATM 10448 O O     . HOH Q 5 .   ? 17.889  -22.602 55.697  1.00 40.31  ? 443 HOH E O     1 
HETATM 10449 O O     . HOH Q 5 .   ? 35.795  -21.703 29.507  1.00 26.88  ? 444 HOH E O     1 
HETATM 10450 O O     . HOH Q 5 .   ? 37.863  -22.467 78.083  1.00 39.75  ? 445 HOH E O     1 
HETATM 10451 O O     . HOH Q 5 .   ? 35.448  -29.255 76.079  1.00 38.68  ? 446 HOH E O     1 
HETATM 10452 O O     . HOH Q 5 .   ? 24.750  -13.147 27.752  1.00 36.83  ? 447 HOH E O     1 
HETATM 10453 O O     . HOH Q 5 .   ? 41.907  -21.651 25.702  1.00 38.19  ? 448 HOH E O     1 
HETATM 10454 O O     . HOH Q 5 .   ? 43.737  -30.814 80.783  1.00 33.60  ? 449 HOH E O     1 
HETATM 10455 O O     . HOH Q 5 .   ? 56.569  -21.899 51.488  1.00 49.60  ? 450 HOH E O     1 
HETATM 10456 O O     . HOH Q 5 .   ? 50.142  -30.491 72.819  1.00 26.26  ? 451 HOH E O     1 
HETATM 10457 O O     . HOH Q 5 .   ? 18.661  -32.639 54.218  1.00 34.90  ? 452 HOH E O     1 
HETATM 10458 O O     . HOH Q 5 .   ? 46.544  -38.572 65.501  1.00 50.13  ? 453 HOH E O     1 
HETATM 10459 O O     . HOH Q 5 .   ? 56.760  -19.277 42.836  1.00 35.14  ? 454 HOH E O     1 
HETATM 10460 O O     . HOH R 5 .   ? 25.651  -21.317 79.228  1.00 37.96  ? 101 HOH F O     1 
HETATM 10461 O O     . HOH R 5 .   ? 14.870  -31.192 70.593  1.00 38.79  ? 102 HOH F O     1 
HETATM 10462 O O     . HOH R 5 .   ? 11.413  -15.699 63.119  1.00 29.51  ? 103 HOH F O     1 
HETATM 10463 O O     . HOH R 5 .   ? 14.174  -11.594 77.242  1.00 39.32  ? 104 HOH F O     1 
HETATM 10464 O O     . HOH R 5 .   ? 11.089  -5.302  75.916  1.00 40.08  ? 105 HOH F O     1 
HETATM 10465 O O     . HOH R 5 .   ? 28.765  -11.872 75.806  1.00 38.44  ? 106 HOH F O     1 
HETATM 10466 O O     . HOH R 5 .   ? 27.663  -26.218 67.269  1.00 25.99  ? 107 HOH F O     1 
HETATM 10467 O O     . HOH R 5 .   ? 13.147  -5.238  67.614  1.00 38.12  ? 108 HOH F O     1 
HETATM 10468 O O     . HOH R 5 .   ? 30.537  -20.721 77.861  1.00 31.27  ? 109 HOH F O     1 
HETATM 10469 O O     . HOH R 5 .   ? 31.112  -30.364 74.784  1.00 44.81  ? 110 HOH F O     1 
HETATM 10470 O O     . HOH R 5 .   ? 33.096  -15.242 80.727  1.00 41.60  ? 111 HOH F O     1 
HETATM 10471 O O     . HOH R 5 .   ? 32.269  -1.864  70.293  1.00 40.15  ? 112 HOH F O     1 
HETATM 10472 O O     . HOH R 5 .   ? 15.489  -5.329  68.975  1.00 47.40  ? 113 HOH F O     1 
HETATM 10473 O O     . HOH R 5 .   ? 16.330  -21.083 65.115  1.00 27.39  ? 114 HOH F O     1 
HETATM 10474 O O     . HOH R 5 .   ? 24.338  -2.435  71.323  1.00 33.42  ? 115 HOH F O     1 
HETATM 10475 O O     . HOH R 5 .   ? 34.050  -31.312 75.451  1.00 31.47  ? 116 HOH F O     1 
HETATM 10476 O O     . HOH S 5 .   ? 30.335  -51.893 42.393  1.00 37.99  ? 401 HOH G O     1 
HETATM 10477 O O     . HOH S 5 .   ? 43.094  -34.767 36.570  1.00 27.89  ? 402 HOH G O     1 
HETATM 10478 O O     . HOH S 5 .   ? 42.892  -4.104  30.266  1.00 35.14  ? 403 HOH G O     1 
HETATM 10479 O O     . HOH S 5 .   ? 21.781  -37.368 71.864  1.00 33.78  ? 404 HOH G O     1 
HETATM 10480 O O     . HOH S 5 .   ? 37.306  -40.155 66.475  1.00 26.93  ? 405 HOH G O     1 
HETATM 10481 O O     . HOH S 5 .   ? 52.199  -11.567 42.442  1.00 32.35  ? 406 HOH G O     1 
HETATM 10482 O O     . HOH S 5 .   ? 26.859  -28.652 63.929  1.00 25.20  ? 407 HOH G O     1 
HETATM 10483 O O     . HOH S 5 .   ? 43.991  -28.853 44.062  1.00 26.37  ? 408 HOH G O     1 
HETATM 10484 O O     . HOH S 5 .   ? 45.936  -27.372 31.417  1.00 34.64  ? 409 HOH G O     1 
HETATM 10485 O O     . HOH S 5 .   ? 32.329  -35.526 63.932  1.00 20.06  ? 410 HOH G O     1 
HETATM 10486 O O     . HOH S 5 .   ? 33.544  -42.625 32.753  1.00 28.83  ? 411 HOH G O     1 
HETATM 10487 O O     . HOH S 5 .   ? 50.882  -15.671 27.595  1.00 43.85  ? 412 HOH G O     1 
HETATM 10488 O O     . HOH S 5 .   ? 16.076  -53.689 59.554  1.00 30.15  ? 413 HOH G O     1 
HETATM 10489 O O     . HOH S 5 .   ? 38.651  -49.270 48.351  1.00 23.35  ? 414 HOH G O     1 
HETATM 10490 O O     . HOH S 5 .   ? 29.994  -40.959 41.638  1.00 28.82  ? 415 HOH G O     1 
HETATM 10491 O O     . HOH S 5 .   ? 29.784  -35.173 63.105  1.00 40.02  ? 416 HOH G O     1 
HETATM 10492 O O     . HOH S 5 .   ? 33.622  -48.791 42.918  1.00 23.21  ? 417 HOH G O     1 
HETATM 10493 O O     . HOH S 5 .   ? 11.008  -39.152 72.430  1.00 38.07  ? 418 HOH G O     1 
HETATM 10494 O O     . HOH S 5 .   ? 40.887  -24.655 42.237  1.00 24.98  ? 419 HOH G O     1 
HETATM 10495 O O     . HOH S 5 .   ? 46.764  -40.661 27.774  1.00 37.52  ? 420 HOH G O     1 
HETATM 10496 O O     . HOH S 5 .   ? 8.702   -40.710 67.740  1.00 29.66  ? 421 HOH G O     1 
HETATM 10497 O O     . HOH S 5 .   ? 34.657  -34.971 63.224  1.00 32.24  ? 422 HOH G O     1 
HETATM 10498 O O     . HOH S 5 .   ? 41.941  -61.188 37.651  1.00 44.67  ? 423 HOH G O     1 
HETATM 10499 O O     . HOH S 5 .   ? 9.552   -49.421 66.161  1.00 36.41  ? 424 HOH G O     1 
HETATM 10500 O O     . HOH S 5 .   ? 20.622  -32.303 58.360  1.00 26.69  ? 425 HOH G O     1 
HETATM 10501 O O     . HOH S 5 .   ? 40.069  -55.581 45.450  1.00 32.21  ? 426 HOH G O     1 
HETATM 10502 O O     . HOH S 5 .   ? 19.724  -59.949 48.504  1.00 35.07  ? 427 HOH G O     1 
HETATM 10503 O O     . HOH S 5 .   ? 20.679  -57.312 66.744  1.00 44.08  ? 428 HOH G O     1 
HETATM 10504 O O     . HOH S 5 .   ? 44.698  -44.778 24.856  1.00 45.33  ? 429 HOH G O     1 
HETATM 10505 O O     . HOH S 5 .   ? 52.093  -28.995 50.508  1.00 28.74  ? 430 HOH G O     1 
HETATM 10506 O O     . HOH S 5 .   ? 51.899  -43.001 66.048  1.00 40.25  ? 431 HOH G O     1 
HETATM 10507 O O     . HOH S 5 .   ? 50.721  -26.077 27.294  1.00 42.62  ? 432 HOH G O     1 
HETATM 10508 O O     . HOH S 5 .   ? 15.921  -51.458 65.392  1.00 27.11  ? 433 HOH G O     1 
HETATM 10509 O O     . HOH S 5 .   ? 18.372  -37.884 68.262  1.00 21.21  ? 434 HOH G O     1 
HETATM 10510 O O     . HOH S 5 .   ? 38.580  -46.370 57.819  1.00 22.16  ? 435 HOH G O     1 
HETATM 10511 O O     . HOH S 5 .   ? 47.606  -22.947 42.132  1.00 45.93  ? 436 HOH G O     1 
HETATM 10512 O O     . HOH S 5 .   ? 42.001  -54.131 74.372  1.00 42.90  ? 437 HOH G O     1 
HETATM 10513 O O     . HOH S 5 .   ? 35.069  -34.122 55.750  1.00 18.14  ? 438 HOH G O     1 
HETATM 10514 O O     . HOH S 5 .   ? 43.731  -37.986 60.039  1.00 34.00  ? 439 HOH G O     1 
HETATM 10515 O O     . HOH S 5 .   ? 37.614  -36.699 27.104  1.00 34.81  ? 440 HOH G O     1 
HETATM 10516 O O     . HOH S 5 .   ? 44.184  -56.591 46.323  1.00 28.99  ? 441 HOH G O     1 
HETATM 10517 O O     . HOH S 5 .   ? 11.222  -36.713 52.852  1.00 38.26  ? 442 HOH G O     1 
HETATM 10518 O O     . HOH S 5 .   ? 36.102  -41.521 75.167  1.00 26.16  ? 443 HOH G O     1 
HETATM 10519 O O     . HOH S 5 .   ? 38.741  -49.753 29.059  1.00 43.28  ? 444 HOH G O     1 
HETATM 10520 O O     . HOH S 5 .   ? 33.858  -41.341 30.090  1.00 34.74  ? 445 HOH G O     1 
HETATM 10521 O O     . HOH S 5 .   ? 16.507  -34.365 74.661  1.00 29.51  ? 446 HOH G O     1 
HETATM 10522 O O     . HOH S 5 .   ? 16.995  -34.437 65.269  1.00 31.34  ? 447 HOH G O     1 
HETATM 10523 O O     . HOH S 5 .   ? 41.887  -55.830 27.724  1.00 45.79  ? 448 HOH G O     1 
HETATM 10524 O O     . HOH S 5 .   ? 50.122  -43.749 27.983  1.00 32.45  ? 449 HOH G O     1 
HETATM 10525 O O     . HOH S 5 .   ? 29.623  -50.209 43.909  1.00 34.16  ? 450 HOH G O     1 
HETATM 10526 O O     . HOH S 5 .   ? 49.115  -21.325 29.030  1.00 39.92  ? 451 HOH G O     1 
HETATM 10527 O O     . HOH S 5 .   ? 45.333  -48.587 27.339  1.00 45.79  ? 452 HOH G O     1 
HETATM 10528 O O     . HOH S 5 .   ? 53.874  -36.345 50.595  1.00 26.73  ? 453 HOH G O     1 
HETATM 10529 O O     . HOH S 5 .   ? 14.723  -30.923 67.403  1.00 49.51  ? 454 HOH G O     1 
HETATM 10530 O O     . HOH S 5 .   ? 40.076  -34.993 26.998  1.00 50.07  ? 455 HOH G O     1 
HETATM 10531 O O     . HOH S 5 .   ? 20.549  -35.917 54.629  1.00 26.86  ? 456 HOH G O     1 
HETATM 10532 O O     . HOH S 5 .   ? 54.384  -33.862 51.645  1.00 30.95  ? 457 HOH G O     1 
HETATM 10533 O O     . HOH S 5 .   ? 37.060  -33.037 29.085  1.00 66.92  ? 458 HOH G O     1 
HETATM 10534 O O     . HOH T 5 .   ? 50.245  -64.669 69.504  1.00 48.24  ? 101 HOH H O     1 
HETATM 10535 O O     . HOH T 5 .   ? 48.600  -55.535 60.081  1.00 49.72  ? 102 HOH H O     1 
HETATM 10536 O O     . HOH T 5 .   ? 43.362  -39.051 67.334  1.00 27.50  ? 103 HOH H O     1 
HETATM 10537 O O     . HOH T 5 .   ? 20.941  -44.741 37.933  1.00 47.09  ? 104 HOH H O     1 
HETATM 10538 O O     . HOH T 5 .   ? 35.935  -58.645 68.683  1.00 55.77  ? 105 HOH H O     1 
HETATM 10539 O O     . HOH T 5 .   ? 40.660  -34.264 74.609  1.00 46.22  ? 106 HOH H O     1 
HETATM 10540 O O     . HOH T 5 .   ? 58.046  -47.813 63.216  1.00 44.39  ? 107 HOH H O     1 
HETATM 10541 O O     . HOH T 5 .   ? 50.946  -61.162 61.202  1.00 42.63  ? 108 HOH H O     1 
HETATM 10542 O O     . HOH T 5 .   ? 39.837  -60.137 61.822  1.00 37.98  ? 109 HOH H O     1 
HETATM 10543 O O     . HOH T 5 .   ? 48.631  -59.876 74.854  1.00 44.97  ? 110 HOH H O     1 
HETATM 10544 O O     . HOH T 5 .   ? 54.692  -35.592 62.622  1.00 46.41  ? 111 HOH H O     1 
HETATM 10545 O O     . HOH T 5 .   ? 51.990  -29.066 69.727  1.00 23.27  ? 112 HOH H O     1 
HETATM 10546 O O     . HOH T 5 .   ? 54.912  -62.212 66.210  1.00 49.45  ? 113 HOH H O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N     . GLY A 1   ? 0.4467 0.4450 0.4946 -0.0550 0.0177  -0.0279 2   GLY A N     
2     C CA    . GLY A 1   ? 0.4700 0.4646 0.5121 -0.0540 0.0196  -0.0288 2   GLY A CA    
3     C C     . GLY A 1   ? 0.4781 0.4744 0.5207 -0.0517 0.0224  -0.0289 2   GLY A C     
4     O O     . GLY A 1   ? 0.4994 0.4996 0.5472 -0.0511 0.0234  -0.0284 2   GLY A O     
5     N N     . SER A 2   ? 0.4337 0.4273 0.4709 -0.0503 0.0234  -0.0297 3   SER A N     
6     C CA    . SER A 2   ? 0.4105 0.4051 0.4475 -0.0483 0.0256  -0.0299 3   SER A CA    
7     C C     . SER A 2   ? 0.4008 0.3922 0.4321 -0.0475 0.0272  -0.0305 3   SER A C     
8     O O     . SER A 2   ? 0.4011 0.3893 0.4285 -0.0481 0.0264  -0.0309 3   SER A O     
9     C CB    . SER A 2   ? 0.4355 0.4313 0.4729 -0.0471 0.0244  -0.0298 3   SER A CB    
10    O OG    . SER A 2   ? 0.4309 0.4243 0.4636 -0.0472 0.0229  -0.0300 3   SER A OG    
11    N N     . LEU A 3   ? 0.4116 0.4038 0.4426 -0.0460 0.0294  -0.0307 4   LEU A N     
12    C CA    . LEU A 3   ? 0.3959 0.3856 0.4221 -0.0450 0.0309  -0.0312 4   LEU A CA    
13    C C     . LEU A 3   ? 0.3854 0.3758 0.4101 -0.0433 0.0315  -0.0314 4   LEU A C     
14    O O     . LEU A 3   ? 0.3950 0.3875 0.4226 -0.0426 0.0321  -0.0314 4   LEU A O     
15    C CB    . LEU A 3   ? 0.4223 0.4122 0.4494 -0.0453 0.0331  -0.0309 4   LEU A CB    
16    C CG    . LEU A 3   ? 0.4550 0.4425 0.4775 -0.0442 0.0348  -0.0312 4   LEU A CG    
17    C CD1   . LEU A 3   ? 0.4597 0.4433 0.4775 -0.0445 0.0337  -0.0316 4   LEU A CD1   
18    C CD2   . LEU A 3   ? 0.4340 0.4224 0.4579 -0.0444 0.0371  -0.0308 4   LEU A CD2   
19    N N     . VAL A 4   ? 0.4018 0.3904 0.4218 -0.0427 0.0311  -0.0317 5   VAL A N     
20    C CA    . VAL A 4   ? 0.3927 0.3819 0.4108 -0.0414 0.0317  -0.0317 5   VAL A CA    
21    C C     . VAL A 4   ? 0.3939 0.3812 0.4075 -0.0405 0.0331  -0.0320 5   VAL A C     
22    O O     . VAL A 4   ? 0.4255 0.4108 0.4358 -0.0405 0.0326  -0.0322 5   VAL A O     
23    C CB    . VAL A 4   ? 0.4466 0.4365 0.4638 -0.0414 0.0298  -0.0312 5   VAL A CB    
24    C CG1   . VAL A 4   ? 0.4698 0.4604 0.4849 -0.0403 0.0303  -0.0309 5   VAL A CG1   
25    C CG2   . VAL A 4   ? 0.4641 0.4556 0.4858 -0.0421 0.0282  -0.0308 5   VAL A CG2   
26    N N     . CYS A 5   ? 0.3738 0.3617 0.3873 -0.0396 0.0348  -0.0320 6   CYS A N     
27    C CA    . CYS A 5   ? 0.3786 0.3651 0.3882 -0.0386 0.0361  -0.0322 6   CYS A CA    
28    C C     . CYS A 5   ? 0.3577 0.3454 0.3654 -0.0376 0.0359  -0.0320 6   CYS A C     
29    O O     . CYS A 5   ? 0.3263 0.3156 0.3360 -0.0375 0.0358  -0.0318 6   CYS A O     
30    C CB    . CYS A 5   ? 0.4272 0.4135 0.4374 -0.0383 0.0381  -0.0322 6   CYS A CB    
31    S SG    . CYS A 5   ? 0.5530 0.5383 0.5655 -0.0398 0.0385  -0.0320 6   CYS A SG    
32    N N     . VAL A 6   ? 0.3618 0.3488 0.3657 -0.0368 0.0358  -0.0319 7   VAL A N     
33    C CA    . VAL A 6   ? 0.3560 0.3448 0.3582 -0.0360 0.0356  -0.0314 7   VAL A CA    
34    C C     . VAL A 6   ? 0.3605 0.3488 0.3592 -0.0345 0.0368  -0.0315 7   VAL A C     
35    O O     . VAL A 6   ? 0.3157 0.3016 0.3126 -0.0341 0.0376  -0.0320 7   VAL A O     
36    C CB    . VAL A 6   ? 0.3943 0.3841 0.3956 -0.0363 0.0340  -0.0310 7   VAL A CB    
37    C CG1   . VAL A 6   ? 0.3891 0.3794 0.3938 -0.0376 0.0325  -0.0308 7   VAL A CG1   
38    C CG2   . VAL A 6   ? 0.3547 0.3425 0.3523 -0.0356 0.0339  -0.0317 7   VAL A CG2   
39    N N     . GLY A 7   ? 0.3587 0.3494 0.3566 -0.0339 0.0369  -0.0309 8   GLY A N     
40    C CA    . GLY A 7   ? 0.3648 0.3558 0.3597 -0.0324 0.0379  -0.0308 8   GLY A CA    
41    C C     . GLY A 7   ? 0.3282 0.3215 0.3209 -0.0315 0.0373  -0.0302 8   GLY A C     
42    O O     . GLY A 7   ? 0.3556 0.3511 0.3496 -0.0324 0.0363  -0.0294 8   GLY A O     
43    N N     . THR A 8   ? 0.3235 0.3162 0.3129 -0.0297 0.0381  -0.0305 9   THR A N     
44    C CA    . THR A 8   ? 0.3605 0.3557 0.3475 -0.0284 0.0379  -0.0300 9   THR A CA    
45    C C     . THR A 8   ? 0.3432 0.3420 0.3299 -0.0274 0.0386  -0.0290 9   THR A C     
46    O O     . THR A 8   ? 0.3750 0.3774 0.3606 -0.0265 0.0386  -0.0282 9   THR A O     
47    C CB    . THR A 8   ? 0.3585 0.3505 0.3419 -0.0268 0.0381  -0.0312 9   THR A CB    
48    O OG1   . THR A 8   ? 0.3959 0.3856 0.3779 -0.0256 0.0391  -0.0316 9   THR A OG1   
49    C CG2   . THR A 8   ? 0.3786 0.3672 0.3625 -0.0282 0.0371  -0.0321 9   THR A CG2   
50    N N     . GLY A 9   ? 0.3843 0.3823 0.3719 -0.0275 0.0392  -0.0290 10  GLY A N     
51    C CA    . GLY A 9   ? 0.3388 0.3399 0.3260 -0.0266 0.0397  -0.0281 10  GLY A CA    
52    C C     . GLY A 9   ? 0.3867 0.3867 0.3707 -0.0241 0.0407  -0.0286 10  GLY A C     
53    O O     . GLY A 9   ? 0.4176 0.4133 0.3998 -0.0234 0.0410  -0.0297 10  GLY A O     
54    N N     . LEU A 10  ? 0.3430 0.3467 0.3264 -0.0227 0.0410  -0.0276 11  LEU A N     
55    C CA    . LEU A 10  ? 0.3572 0.3602 0.3376 -0.0200 0.0419  -0.0279 11  LEU A CA    
56    C C     . LEU A 10  ? 0.3502 0.3564 0.3288 -0.0179 0.0421  -0.0277 11  LEU A C     
57    O O     . LEU A 10  ? 0.3687 0.3726 0.3442 -0.0153 0.0427  -0.0286 11  LEU A O     
58    C CB    . LEU A 10  ? 0.3722 0.3772 0.3533 -0.0197 0.0422  -0.0270 11  LEU A CB    
59    C CG    . LEU A 10  ? 0.4212 0.4223 0.4026 -0.0207 0.0424  -0.0276 11  LEU A CG    
60    C CD1   . LEU A 10  ? 0.4322 0.4357 0.4139 -0.0204 0.0424  -0.0267 11  LEU A CD1   
61    C CD2   . LEU A 10  ? 0.4339 0.4297 0.4126 -0.0194 0.0431  -0.0286 11  LEU A CD2   
62    N N     . GLN A 11  ? 0.3989 0.4103 0.3792 -0.0188 0.0417  -0.0264 12  GLN A N     
63    C CA    . GLN A 11  ? 0.4546 0.4702 0.4333 -0.0169 0.0421  -0.0260 12  GLN A CA    
64    C C     . GLN A 11  ? 0.4721 0.4847 0.4489 -0.0169 0.0418  -0.0272 12  GLN A C     
65    O O     . GLN A 11  ? 0.5262 0.5355 0.5043 -0.0191 0.0409  -0.0277 12  GLN A O     
66    C CB    . GLN A 11  ? 0.4537 0.4764 0.4350 -0.0181 0.0417  -0.0238 12  GLN A CB    
67    C CG    . GLN A 11  ? 0.4787 0.5059 0.4609 -0.0171 0.0421  -0.0224 12  GLN A CG    
68    C CD    . GLN A 11  ? 0.5382 0.5673 0.5175 -0.0131 0.0433  -0.0228 12  GLN A CD    
69    O OE1   . GLN A 11  ? 0.5491 0.5754 0.5253 -0.0110 0.0439  -0.0243 12  GLN A OE1   
70    N NE2   . GLN A 11  ? 0.5412 0.5751 0.5216 -0.0120 0.0437  -0.0214 12  GLN A NE2   
71    N N     . LEU A 12  ? 0.5003 0.5143 0.4739 -0.0141 0.0423  -0.0278 13  LEU A N     
72    C CA    . LEU A 12  ? 0.4425 0.4535 0.4135 -0.0136 0.0419  -0.0292 13  LEU A CA    
73    C C     . LEU A 12  ? 0.3916 0.4065 0.3640 -0.0157 0.0412  -0.0280 13  LEU A C     
74    O O     . LEU A 12  ? 0.3587 0.3801 0.3317 -0.0153 0.0417  -0.0263 13  LEU A O     
75    C CB    . LEU A 12  ? 0.4593 0.4704 0.4259 -0.0095 0.0428  -0.0303 13  LEU A CB    
76    C CG    . LEU A 12  ? 0.4403 0.4490 0.4032 -0.0084 0.0423  -0.0320 13  LEU A CG    
77    C CD1   . LEU A 12  ? 0.4632 0.4635 0.4248 -0.0094 0.0412  -0.0339 13  LEU A CD1   
78    C CD2   . LEU A 12  ? 0.4368 0.4476 0.3955 -0.0040 0.0434  -0.0328 13  LEU A CD2   
79    N N     . ALA A 13  ? 0.3680 0.3791 0.3414 -0.0181 0.0401  -0.0286 14  ALA A N     
80    C CA    . ALA A 13  ? 0.3713 0.3846 0.3449 -0.0196 0.0392  -0.0279 14  ALA A CA    
81    C C     . ALA A 13  ? 0.4075 0.4254 0.3853 -0.0223 0.0386  -0.0255 14  ALA A C     
82    O O     . ALA A 13  ? 0.4317 0.4492 0.4111 -0.0246 0.0374  -0.0249 14  ALA A O     
83    C CB    . ALA A 13  ? 0.4045 0.4211 0.3742 -0.0169 0.0399  -0.0281 14  ALA A CB    
84    N N     . GLY A 14  ? 0.3904 0.4125 0.3699 -0.0221 0.0393  -0.0240 15  GLY A N     
85    C CA    . GLY A 14  ? 0.3894 0.4165 0.3722 -0.0244 0.0386  -0.0215 15  GLY A CA    
86    C C     . GLY A 14  ? 0.3922 0.4170 0.3786 -0.0269 0.0377  -0.0212 15  GLY A C     
87    O O     . GLY A 14  ? 0.4099 0.4371 0.3991 -0.0293 0.0366  -0.0193 15  GLY A O     
88    N N     . GLN A 15  ? 0.3792 0.3990 0.3653 -0.0262 0.0381  -0.0230 16  GLN A N     
89    C CA    . GLN A 15  ? 0.3786 0.3967 0.3675 -0.0279 0.0376  -0.0229 16  GLN A CA    
90    C C     . GLN A 15  ? 0.3889 0.4018 0.3791 -0.0295 0.0368  -0.0241 16  GLN A C     
91    O O     . GLN A 15  ? 0.3708 0.3814 0.3628 -0.0305 0.0366  -0.0245 16  GLN A O     
92    C CB    . GLN A 15  ? 0.3708 0.3880 0.3586 -0.0261 0.0387  -0.0235 16  GLN A CB    
93    C CG    . GLN A 15  ? 0.3907 0.4079 0.3808 -0.0276 0.0382  -0.0230 16  GLN A CG    
94    C CD    . GLN A 15  ? 0.3856 0.4034 0.3745 -0.0258 0.0391  -0.0231 16  GLN A CD    
95    O OE1   . GLN A 15  ? 0.3425 0.3565 0.3294 -0.0243 0.0400  -0.0245 16  GLN A OE1   
96    N NE2   . GLN A 15  ? 0.4100 0.4327 0.4002 -0.0261 0.0387  -0.0215 16  GLN A NE2   
97    N N     . ILE A 16  ? 0.3716 0.3831 0.3609 -0.0297 0.0364  -0.0247 17  ILE A N     
98    C CA    . ILE A 16  ? 0.3386 0.3463 0.3296 -0.0313 0.0354  -0.0255 17  ILE A CA    
99    C C     . ILE A 16  ? 0.3273 0.3370 0.3210 -0.0335 0.0339  -0.0239 17  ILE A C     
100   O O     . ILE A 16  ? 0.3370 0.3508 0.3303 -0.0337 0.0335  -0.0223 17  ILE A O     
101   C CB    . ILE A 16  ? 0.3938 0.3984 0.3824 -0.0305 0.0354  -0.0269 17  ILE A CB    
102   C CG1   . ILE A 16  ? 0.3877 0.3886 0.3786 -0.0321 0.0345  -0.0278 17  ILE A CG1   
103   C CG2   . ILE A 16  ? 0.3842 0.3918 0.3708 -0.0300 0.0349  -0.0262 17  ILE A CG2   
104   C CD1   . ILE A 16  ? 0.4292 0.4268 0.4180 -0.0317 0.0342  -0.0292 17  ILE A CD1   
105   N N     A SER A 17  ? 0.3192 0.3263 0.3158 -0.0350 0.0330  -0.0243 18  SER A N     
106   N N     B SER A 17  ? 0.2884 0.2956 0.2850 -0.0350 0.0330  -0.0243 18  SER A N     
107   C CA    A SER A 17  ? 0.3416 0.3496 0.3408 -0.0369 0.0313  -0.0230 18  SER A CA    
108   C CA    B SER A 17  ? 0.2857 0.2938 0.2850 -0.0369 0.0313  -0.0230 18  SER A CA    
109   C C     A SER A 17  ? 0.3279 0.3366 0.3263 -0.0373 0.0304  -0.0225 18  SER A C     
110   C C     B SER A 17  ? 0.2990 0.3076 0.2975 -0.0373 0.0304  -0.0225 18  SER A C     
111   O O     A SER A 17  ? 0.3609 0.3678 0.3572 -0.0363 0.0309  -0.0238 18  SER A O     
112   O O     B SER A 17  ? 0.3319 0.3386 0.3283 -0.0364 0.0309  -0.0238 18  SER A O     
113   C CB    A SER A 17  ? 0.3737 0.3786 0.3760 -0.0379 0.0307  -0.0239 18  SER A CB    
114   C CB    B SER A 17  ? 0.2754 0.2805 0.2777 -0.0379 0.0307  -0.0238 18  SER A CB    
115   O OG    A SER A 17  ? 0.4258 0.4302 0.4284 -0.0375 0.0315  -0.0244 18  SER A OG    
116   O OG    B SER A 17  ? 0.2493 0.2514 0.2521 -0.0378 0.0307  -0.0252 18  SER A OG    
117   N N     . VAL A 18  ? 0.3158 0.3267 0.3156 -0.0389 0.0289  -0.0205 19  VAL A N     
118   C CA    . VAL A 18  ? 0.3104 0.3222 0.3092 -0.0394 0.0279  -0.0197 19  VAL A CA    
119   C C     . VAL A 18  ? 0.3214 0.3293 0.3214 -0.0397 0.0271  -0.0212 19  VAL A C     
120   O O     . VAL A 18  ? 0.3396 0.3468 0.3375 -0.0391 0.0270  -0.0220 19  VAL A O     
121   C CB    . VAL A 18  ? 0.3269 0.3416 0.3273 -0.0413 0.0263  -0.0170 19  VAL A CB    
122   C CG1   . VAL A 18  ? 0.3386 0.3541 0.3380 -0.0420 0.0250  -0.0160 19  VAL A CG1   
123   C CG2   . VAL A 18  ? 0.3297 0.3492 0.3292 -0.0413 0.0270  -0.0152 19  VAL A CG2   
124   N N     . LEU A 19  ? 0.3443 0.3498 0.3477 -0.0405 0.0265  -0.0217 20  LEU A N     
125   C CA    . LEU A 19  ? 0.3340 0.3366 0.3394 -0.0409 0.0257  -0.0229 20  LEU A CA    
126   C C     . LEU A 19  ? 0.3220 0.3224 0.3258 -0.0397 0.0271  -0.0249 20  LEU A C     
127   O O     . LEU A 19  ? 0.3249 0.3238 0.3286 -0.0398 0.0265  -0.0257 20  LEU A O     
128   C CB    . LEU A 19  ? 0.3845 0.3855 0.3938 -0.0416 0.0250  -0.0230 20  LEU A CB    
129   C CG    . LEU A 19  ? 0.4315 0.4302 0.4437 -0.0417 0.0243  -0.0241 20  LEU A CG    
130   C CD1   . LEU A 19  ? 0.4756 0.4747 0.4883 -0.0427 0.0223  -0.0230 20  LEU A CD1   
131   C CD2   . LEU A 19  ? 0.4376 0.4348 0.4531 -0.0417 0.0241  -0.0246 20  LEU A CD2   
132   N N     . SER A 20  ? 0.2870 0.2871 0.2896 -0.0386 0.0288  -0.0257 21  SER A N     
133   C CA    . SER A 20  ? 0.3317 0.3293 0.3327 -0.0375 0.0301  -0.0274 21  SER A CA    
134   C C     . SER A 20  ? 0.3327 0.3302 0.3300 -0.0367 0.0301  -0.0278 21  SER A C     
135   O O     . SER A 20  ? 0.3782 0.3729 0.3746 -0.0365 0.0302  -0.0291 21  SER A O     
136   C CB    . SER A 20  ? 0.3074 0.3049 0.3079 -0.0366 0.0318  -0.0278 21  SER A CB    
137   O OG    . SER A 20  ? 0.3106 0.3077 0.3142 -0.0372 0.0317  -0.0278 21  SER A OG    
138   N N     . ARG A 21  ? 0.3758 0.3762 0.3708 -0.0362 0.0301  -0.0267 22  ARG A N     
139   C CA    . ARG A 21  ? 0.3837 0.3843 0.3745 -0.0350 0.0301  -0.0272 22  ARG A CA    
140   C C     . ARG A 21  ? 0.3615 0.3608 0.3526 -0.0361 0.0283  -0.0274 22  ARG A C     
141   O O     . ARG A 21  ? 0.3278 0.3249 0.3162 -0.0355 0.0279  -0.0287 22  ARG A O     
142   C CB    . ARG A 21  ? 0.4294 0.4345 0.4182 -0.0342 0.0305  -0.0257 22  ARG A CB    
143   C CG    . ARG A 21  ? 0.4335 0.4394 0.4175 -0.0325 0.0308  -0.0263 22  ARG A CG    
144   C CD    . ARG A 21  ? 0.4576 0.4690 0.4399 -0.0315 0.0316  -0.0246 22  ARG A CD    
145   N NE    . ARG A 21  ? 0.4693 0.4816 0.4466 -0.0292 0.0323  -0.0255 22  ARG A NE    
146   C CZ    . ARG A 21  ? 0.5067 0.5187 0.4815 -0.0292 0.0312  -0.0258 22  ARG A CZ    
147   N NH1   . ARG A 21  ? 0.4971 0.5083 0.4740 -0.0315 0.0294  -0.0250 22  ARG A NH1   
148   N NH2   . ARG A 21  ? 0.5666 0.5791 0.5363 -0.0267 0.0319  -0.0270 22  ARG A NH2   
149   N N     . SER A 22  ? 0.3685 0.3691 0.3630 -0.0378 0.0269  -0.0260 23  SER A N     
150   C CA    . SER A 22  ? 0.3753 0.3752 0.3704 -0.0390 0.0249  -0.0258 23  SER A CA    
151   C C     . SER A 22  ? 0.3696 0.3659 0.3664 -0.0394 0.0245  -0.0274 23  SER A C     
152   O O     . SER A 22  ? 0.3898 0.3849 0.3855 -0.0399 0.0231  -0.0279 23  SER A O     
153   C CB    . SER A 22  ? 0.3740 0.3758 0.3725 -0.0405 0.0235  -0.0238 23  SER A CB    
154   O OG    . SER A 22  ? 0.3675 0.3688 0.3667 -0.0416 0.0215  -0.0234 23  SER A OG    
155   N N     . TYR A 23  ? 0.3785 0.3735 0.3780 -0.0394 0.0256  -0.0280 24  TYR A N     
156   C CA    . TYR A 23  ? 0.3405 0.3328 0.3421 -0.0400 0.0255  -0.0292 24  TYR A CA    
157   C C     . TYR A 23  ? 0.3599 0.3496 0.3576 -0.0393 0.0257  -0.0307 24  TYR A C     
158   O O     . TYR A 23  ? 0.3836 0.3713 0.3817 -0.0402 0.0244  -0.0313 24  TYR A O     
159   C CB    . TYR A 23  ? 0.3119 0.3037 0.3166 -0.0399 0.0269  -0.0295 24  TYR A CB    
160   C CG    . TYR A 23  ? 0.3283 0.3212 0.3378 -0.0408 0.0262  -0.0288 24  TYR A CG    
161   C CD1   . TYR A 23  ? 0.3047 0.2971 0.3176 -0.0417 0.0250  -0.0290 24  TYR A CD1   
162   C CD2   . TYR A 23  ? 0.3261 0.3204 0.3368 -0.0406 0.0265  -0.0281 24  TYR A CD2   
163   C CE1   . TYR A 23  ? 0.3070 0.3004 0.3243 -0.0421 0.0243  -0.0285 24  TYR A CE1   
164   C CE2   . TYR A 23  ? 0.3264 0.3210 0.3412 -0.0411 0.0257  -0.0277 24  TYR A CE2   
165   C CZ    . TYR A 23  ? 0.3364 0.3307 0.3545 -0.0417 0.0247  -0.0279 24  TYR A CZ    
166   O OH    . TYR A 23  ? 0.3562 0.3507 0.3783 -0.0418 0.0238  -0.0277 24  TYR A OH    
167   N N     . ILE A 24  ? 0.3379 0.3274 0.3319 -0.0377 0.0271  -0.0311 25  ILE A N     
168   C CA    . ILE A 24  ? 0.3791 0.3655 0.3689 -0.0366 0.0273  -0.0326 25  ILE A CA    
169   C C     . ILE A 24  ? 0.4188 0.4047 0.4055 -0.0366 0.0256  -0.0330 25  ILE A C     
170   O O     . ILE A 24  ? 0.3949 0.3773 0.3799 -0.0369 0.0245  -0.0343 25  ILE A O     
171   C CB    . ILE A 24  ? 0.3637 0.3505 0.3502 -0.0344 0.0292  -0.0328 25  ILE A CB    
172   C CG1   . ILE A 24  ? 0.3780 0.3645 0.3669 -0.0344 0.0308  -0.0326 25  ILE A CG1   
173   C CG2   . ILE A 24  ? 0.4194 0.4028 0.4008 -0.0328 0.0291  -0.0344 25  ILE A CG2   
174   C CD1   . ILE A 24  ? 0.3787 0.3658 0.3647 -0.0323 0.0324  -0.0327 25  ILE A CD1   
175   N N     . GLU A 25  ? 0.4398 0.4292 0.4257 -0.0365 0.0251  -0.0317 26  GLU A N     
176   C CA    . GLU A 25  ? 0.4999 0.4897 0.4822 -0.0363 0.0236  -0.0320 26  GLU A CA    
177   C C     . GLU A 25  ? 0.4961 0.4838 0.4803 -0.0382 0.0213  -0.0323 26  GLU A C     
178   O O     . GLU A 25  ? 0.5269 0.5121 0.5077 -0.0380 0.0200  -0.0336 26  GLU A O     
179   C CB    . GLU A 25  ? 0.5740 0.5686 0.5560 -0.0362 0.0237  -0.0300 26  GLU A CB    
180   C CG    . GLU A 25  ? 0.6882 0.6838 0.6662 -0.0360 0.0222  -0.0299 26  GLU A CG    
181   C CD    . GLU A 25  ? 0.7847 0.7854 0.7624 -0.0362 0.0223  -0.0275 26  GLU A CD    
182   O OE1   . GLU A 25  ? 0.7964 0.7997 0.7773 -0.0366 0.0233  -0.0259 26  GLU A OE1   
183   O OE2   . GLU A 25  ? 0.8147 0.8168 0.7891 -0.0360 0.0212  -0.0272 26  GLU A OE2   
184   N N     . HIS A 26  ? 0.4670 0.4558 0.4568 -0.0399 0.0208  -0.0312 27  HIS A N     
185   C CA    . HIS A 26  ? 0.4600 0.4480 0.4524 -0.0416 0.0185  -0.0311 27  HIS A CA    
186   C C     . HIS A 26  ? 0.4466 0.4317 0.4421 -0.0426 0.0186  -0.0321 27  HIS A C     
187   O O     . HIS A 26  ? 0.4583 0.4434 0.4574 -0.0442 0.0169  -0.0319 27  HIS A O     
188   C CB    . HIS A 26  ? 0.4831 0.4742 0.4799 -0.0427 0.0176  -0.0292 27  HIS A CB    
189   C CG    . HIS A 26  ? 0.5205 0.5144 0.5145 -0.0424 0.0171  -0.0277 27  HIS A CG    
190   N ND1   . HIS A 26  ? 0.5650 0.5616 0.5594 -0.0419 0.0183  -0.0263 27  HIS A ND1   
191   C CD2   . HIS A 26  ? 0.5796 0.5742 0.5705 -0.0426 0.0153  -0.0273 27  HIS A CD2   
192   C CE1   . HIS A 26  ? 0.6006 0.5998 0.5925 -0.0420 0.0175  -0.0248 27  HIS A CE1   
193   N NE2   . HIS A 26  ? 0.6152 0.6132 0.6047 -0.0423 0.0157  -0.0255 27  HIS A NE2   
194   N N     . ALA A 27  ? 0.4476 0.4308 0.4418 -0.0416 0.0204  -0.0331 28  ALA A N     
195   C CA    . ALA A 27  ? 0.3903 0.3710 0.3871 -0.0426 0.0207  -0.0337 28  ALA A CA    
196   C C     . ALA A 27  ? 0.4453 0.4223 0.4396 -0.0435 0.0187  -0.0350 28  ALA A C     
197   O O     . ALA A 27  ? 0.5090 0.4842 0.4979 -0.0424 0.0180  -0.0360 28  ALA A O     
198   C CB    . ALA A 27  ? 0.3520 0.3316 0.3479 -0.0414 0.0231  -0.0341 28  ALA A CB    
199   N N     . ASP A 28  ? 0.4224 0.3985 0.4207 -0.0454 0.0178  -0.0349 29  ASP A N     
200   C CA    . ASP A 28  ? 0.4424 0.4147 0.4390 -0.0467 0.0157  -0.0359 29  ASP A CA    
201   C C     . ASP A 28  ? 0.4181 0.3859 0.4109 -0.0459 0.0167  -0.0371 29  ASP A C     
202   O O     . ASP A 28  ? 0.4038 0.3674 0.3922 -0.0458 0.0152  -0.0385 29  ASP A O     
203   C CB    . ASP A 28  ? 0.5180 0.4915 0.5207 -0.0492 0.0144  -0.0351 29  ASP A CB    
204   C CG    . ASP A 28  ? 0.5937 0.5708 0.5998 -0.0501 0.0125  -0.0341 29  ASP A CG    
205   O OD1   . ASP A 28  ? 0.6240 0.6023 0.6272 -0.0490 0.0120  -0.0340 29  ASP A OD1   
206   O OD2   . ASP A 28  ? 0.6950 0.6738 0.7067 -0.0518 0.0116  -0.0333 29  ASP A OD2   
207   N N     . ILE A 29  ? 0.4048 0.3734 0.3993 -0.0452 0.0193  -0.0366 30  ILE A N     
208   C CA    . ILE A 29  ? 0.3865 0.3510 0.3779 -0.0443 0.0204  -0.0374 30  ILE A CA    
209   C C     . ILE A 29  ? 0.3758 0.3427 0.3681 -0.0428 0.0233  -0.0367 30  ILE A C     
210   O O     . ILE A 29  ? 0.3848 0.3556 0.3816 -0.0433 0.0244  -0.0355 30  ILE A O     
211   C CB    . ILE A 29  ? 0.4007 0.3623 0.3946 -0.0467 0.0195  -0.0372 30  ILE A CB    
212   C CG1   . ILE A 29  ? 0.4194 0.3756 0.4092 -0.0460 0.0200  -0.0381 30  ILE A CG1   
213   C CG2   . ILE A 29  ? 0.4009 0.3665 0.4017 -0.0483 0.0208  -0.0356 30  ILE A CG2   
214   C CD1   . ILE A 29  ? 0.4418 0.3945 0.4335 -0.0487 0.0186  -0.0377 30  ILE A CD1   
215   N N     . VAL A 30  ? 0.3736 0.3379 0.3613 -0.0408 0.0244  -0.0374 31  VAL A N     
216   C CA    . VAL A 30  ? 0.3812 0.3474 0.3689 -0.0391 0.0269  -0.0368 31  VAL A CA    
217   C C     . VAL A 30  ? 0.4151 0.3774 0.4013 -0.0388 0.0279  -0.0371 31  VAL A C     
218   O O     . VAL A 30  ? 0.5061 0.4638 0.4878 -0.0379 0.0271  -0.0382 31  VAL A O     
219   C CB    . VAL A 30  ? 0.3643 0.3325 0.3482 -0.0367 0.0275  -0.0372 31  VAL A CB    
220   C CG1   . VAL A 30  ? 0.3398 0.3104 0.3241 -0.0351 0.0298  -0.0365 31  VAL A CG1   
221   C CG2   . VAL A 30  ? 0.3695 0.3415 0.3547 -0.0372 0.0263  -0.0366 31  VAL A CG2   
222   N N     . PHE A 31  ? 0.3791 0.3431 0.3687 -0.0394 0.0297  -0.0360 32  PHE A N     
223   C CA    . PHE A 31  ? 0.3940 0.3550 0.3822 -0.0390 0.0309  -0.0358 32  PHE A CA    
224   C C     . PHE A 31  ? 0.3795 0.3423 0.3656 -0.0364 0.0328  -0.0357 32  PHE A C     
225   O O     . PHE A 31  ? 0.4113 0.3785 0.4001 -0.0363 0.0340  -0.0349 32  PHE A O     
226   C CB    . PHE A 31  ? 0.3789 0.3408 0.3718 -0.0412 0.0317  -0.0346 32  PHE A CB    
227   C CG    . PHE A 31  ? 0.4298 0.3897 0.4248 -0.0439 0.0297  -0.0344 32  PHE A CG    
228   C CD1   . PHE A 31  ? 0.4478 0.4105 0.4462 -0.0453 0.0283  -0.0344 32  PHE A CD1   
229   C CD2   . PHE A 31  ? 0.4367 0.3919 0.4305 -0.0451 0.0292  -0.0342 32  PHE A CD2   
230   C CE1   . PHE A 31  ? 0.4585 0.4197 0.4591 -0.0479 0.0264  -0.0342 32  PHE A CE1   
231   C CE2   . PHE A 31  ? 0.4223 0.3758 0.4184 -0.0479 0.0272  -0.0339 32  PHE A CE2   
232   C CZ    . PHE A 31  ? 0.4221 0.3788 0.4216 -0.0493 0.0258  -0.0339 32  PHE A CZ    
233   N N     . SER A 32  ? 0.3814 0.3408 0.3626 -0.0344 0.0328  -0.0365 33  SER A N     
234   C CA    . SER A 32  ? 0.3990 0.3605 0.3778 -0.0317 0.0342  -0.0365 33  SER A CA    
235   C C     . SER A 32  ? 0.4119 0.3711 0.3894 -0.0307 0.0355  -0.0360 33  SER A C     
236   O O     . SER A 32  ? 0.4285 0.3828 0.4046 -0.0312 0.0349  -0.0361 33  SER A O     
237   C CB    . SER A 32  ? 0.4061 0.3668 0.3805 -0.0295 0.0333  -0.0377 33  SER A CB    
238   O OG    . SER A 32  ? 0.4046 0.3591 0.3752 -0.0289 0.0321  -0.0389 33  SER A OG    
239   N N     . LEU A 33  ? 0.4194 0.3822 0.3972 -0.0293 0.0371  -0.0353 34  LEU A N     
240   C CA    . LEU A 33  ? 0.4238 0.3850 0.3996 -0.0278 0.0382  -0.0349 34  LEU A CA    
241   C C     . LEU A 33  ? 0.4040 0.3693 0.3785 -0.0253 0.0391  -0.0347 34  LEU A C     
242   O O     . LEU A 33  ? 0.4378 0.4072 0.4147 -0.0257 0.0401  -0.0339 34  LEU A O     
243   C CB    . LEU A 33  ? 0.4376 0.3993 0.4165 -0.0296 0.0394  -0.0337 34  LEU A CB    
244   C CG    . LEU A 33  ? 0.4661 0.4245 0.4426 -0.0287 0.0401  -0.0330 34  LEU A CG    
245   C CD1   . LEU A 33  ? 0.4788 0.4389 0.4582 -0.0303 0.0415  -0.0317 34  LEU A CD1   
246   C CD2   . LEU A 33  ? 0.4887 0.4479 0.4620 -0.0256 0.0407  -0.0332 34  LEU A CD2   
247   N N     . LEU A 34  ? 0.4196 0.3838 0.3903 -0.0228 0.0387  -0.0356 35  LEU A N     
248   C CA    . LEU A 34  ? 0.4393 0.4082 0.4091 -0.0206 0.0394  -0.0354 35  LEU A CA    
249   C C     . LEU A 34  ? 0.4715 0.4389 0.4381 -0.0177 0.0401  -0.0353 35  LEU A C     
250   O O     . LEU A 34  ? 0.5014 0.4632 0.4657 -0.0171 0.0397  -0.0358 35  LEU A O     
251   C CB    . LEU A 34  ? 0.4649 0.4351 0.4329 -0.0197 0.0385  -0.0363 35  LEU A CB    
252   C CG    . LEU A 34  ? 0.5249 0.4981 0.4961 -0.0222 0.0378  -0.0360 35  LEU A CG    
253   C CD1   . LEU A 34  ? 0.5816 0.5514 0.5552 -0.0250 0.0370  -0.0361 35  LEU A CD1   
254   C CD2   . LEU A 34  ? 0.5408 0.5151 0.5095 -0.0211 0.0369  -0.0368 35  LEU A CD2   
255   N N     . PRO A 35  ? 0.5033 0.4757 0.4700 -0.0159 0.0410  -0.0346 36  PRO A N     
256   C CA    . PRO A 35  ? 0.5485 0.5203 0.5128 -0.0131 0.0417  -0.0343 36  PRO A CA    
257   C C     . PRO A 35  ? 0.6128 0.5804 0.5726 -0.0100 0.0412  -0.0357 36  PRO A C     
258   O O     . PRO A 35  ? 0.5951 0.5578 0.5527 -0.0088 0.0411  -0.0358 36  PRO A O     
259   C CB    . PRO A 35  ? 0.5539 0.5331 0.5199 -0.0122 0.0425  -0.0332 36  PRO A CB    
260   C CG    . PRO A 35  ? 0.5705 0.5531 0.5403 -0.0153 0.0422  -0.0327 36  PRO A CG    
261   C CD    . PRO A 35  ? 0.5391 0.5180 0.5083 -0.0166 0.0412  -0.0339 36  PRO A CD    
262   N N     . ASP A 36  ? 0.6150 0.5843 0.5732 -0.0087 0.0408  -0.0367 37  ASP A N     
263   C CA    . ASP A 36  ? 0.6310 0.5973 0.5845 -0.0050 0.0404  -0.0382 37  ASP A CA    
264   C C     . ASP A 36  ? 0.5682 0.5319 0.5196 -0.0054 0.0392  -0.0399 37  ASP A C     
265   O O     . ASP A 36  ? 0.5565 0.5206 0.5104 -0.0086 0.0386  -0.0397 37  ASP A O     
266   C CB    . ASP A 36  ? 0.6568 0.6292 0.6096 -0.0016 0.0416  -0.0377 37  ASP A CB    
267   C CG    . ASP A 36  ? 0.7027 0.6834 0.6583 -0.0026 0.0422  -0.0366 37  ASP A CG    
268   O OD1   . ASP A 36  ? 0.7042 0.6855 0.6592 -0.0034 0.0417  -0.0373 37  ASP A OD1   
269   O OD2   . ASP A 36  ? 0.7328 0.7190 0.6911 -0.0028 0.0431  -0.0349 37  ASP A OD2   
270   N N     . GLY A 37  ? 0.5794 0.5408 0.5261 -0.0018 0.0389  -0.0415 38  GLY A N     
271   C CA    . GLY A 37  ? 0.5498 0.5081 0.4934 -0.0016 0.0376  -0.0435 38  GLY A CA    
272   C C     . GLY A 37  ? 0.5077 0.4734 0.4520 -0.0014 0.0382  -0.0432 38  GLY A C     
273   O O     . GLY A 37  ? 0.5540 0.5189 0.4977 -0.0030 0.0371  -0.0439 38  GLY A O     
274   N N     . PHE A 38  ? 0.4519 0.4249 0.3974 0.0005  0.0398  -0.0418 39  PHE A N     
275   C CA    . PHE A 38  ? 0.4282 0.4090 0.3749 0.0003  0.0404  -0.0409 39  PHE A CA    
276   C C     . PHE A 38  ? 0.4186 0.4008 0.3695 -0.0043 0.0397  -0.0397 39  PHE A C     
277   O O     . PHE A 38  ? 0.4068 0.3910 0.3573 -0.0054 0.0392  -0.0398 39  PHE A O     
278   C CB    . PHE A 38  ? 0.4295 0.4183 0.3780 0.0023  0.0422  -0.0392 39  PHE A CB    
279   C CG    . PHE A 38  ? 0.4383 0.4274 0.3827 0.0075  0.0430  -0.0402 39  PHE A CG    
280   C CD1   . PHE A 38  ? 0.4424 0.4334 0.3828 0.0106  0.0433  -0.0416 39  PHE A CD1   
281   C CD2   . PHE A 38  ? 0.4344 0.4224 0.3791 0.0094  0.0436  -0.0398 39  PHE A CD2   
282   C CE1   . PHE A 38  ? 0.4689 0.4605 0.4056 0.0157  0.0442  -0.0427 39  PHE A CE1   
283   C CE2   . PHE A 38  ? 0.4513 0.4398 0.3925 0.0145  0.0443  -0.0408 39  PHE A CE2   
284   C CZ    . PHE A 38  ? 0.4681 0.4584 0.4054 0.0177  0.0446  -0.0423 39  PHE A CZ    
285   N N     . SER A 39  ? 0.4384 0.4193 0.3931 -0.0069 0.0398  -0.0386 40  SER A N     
286   C CA    . SER A 39  ? 0.4647 0.4468 0.4237 -0.0110 0.0392  -0.0375 40  SER A CA    
287   C C     . SER A 39  ? 0.4724 0.4486 0.4303 -0.0129 0.0376  -0.0389 40  SER A C     
288   O O     . SER A 39  ? 0.5224 0.5003 0.4826 -0.0154 0.0368  -0.0385 40  SER A O     
289   C CB    . SER A 39  ? 0.4633 0.4456 0.4260 -0.0127 0.0398  -0.0362 40  SER A CB    
290   O OG    . SER A 39  ? 0.5222 0.5063 0.4890 -0.0162 0.0393  -0.0352 40  SER A OG    
291   N N     . GLN A 40  ? 0.5014 0.4708 0.4561 -0.0117 0.0369  -0.0405 41  GLN A N     
292   C CA    . GLN A 40  ? 0.4760 0.4395 0.4298 -0.0136 0.0351  -0.0418 41  GLN A CA    
293   C C     . GLN A 40  ? 0.4202 0.3844 0.3708 -0.0127 0.0340  -0.0430 41  GLN A C     
294   O O     . GLN A 40  ? 0.3932 0.3563 0.3450 -0.0153 0.0326  -0.0432 41  GLN A O     
295   C CB    . GLN A 40  ? 0.5254 0.4811 0.4763 -0.0126 0.0344  -0.0430 41  GLN A CB    
296   C CG    . GLN A 40  ? 0.5579 0.5077 0.5095 -0.0157 0.0325  -0.0436 41  GLN A CG    
297   C CD    . GLN A 40  ? 0.5521 0.5042 0.5095 -0.0195 0.0328  -0.0418 41  GLN A CD    
298   O OE1   . GLN A 40  ? 0.6341 0.5914 0.5948 -0.0198 0.0343  -0.0403 41  GLN A OE1   
299   N NE2   . GLN A 40  ? 0.5252 0.4736 0.4841 -0.0224 0.0312  -0.0421 41  GLN A NE2   
300   N N     . ARG A 41  ? 0.4338 0.4001 0.3805 -0.0090 0.0348  -0.0438 42  ARG A N     
301   C CA    A ARG A 41  ? 0.4474 0.4151 0.3904 -0.0076 0.0341  -0.0450 42  ARG A CA    
302   C CA    B ARG A 41  ? 0.4435 0.4111 0.3865 -0.0076 0.0341  -0.0450 42  ARG A CA    
303   C C     . ARG A 41  ? 0.4198 0.3944 0.3664 -0.0101 0.0343  -0.0431 42  ARG A C     
304   O O     . ARG A 41  ? 0.4127 0.3866 0.3586 -0.0117 0.0329  -0.0436 42  ARG A O     
305   C CB    A ARG A 41  ? 0.4678 0.4379 0.4063 -0.0028 0.0354  -0.0459 42  ARG A CB    
306   C CB    B ARG A 41  ? 0.4594 0.4285 0.3976 -0.0027 0.0352  -0.0461 42  ARG A CB    
307   C CG    A ARG A 41  ? 0.4990 0.4620 0.4332 0.0004  0.0350  -0.0480 42  ARG A CG    
308   C CG    B ARG A 41  ? 0.4840 0.4446 0.4165 -0.0001 0.0340  -0.0490 42  ARG A CG    
309   C CD    A ARG A 41  ? 0.4992 0.4538 0.4291 0.0001  0.0326  -0.0505 42  ARG A CD    
310   C CD    B ARG A 41  ? 0.4895 0.4513 0.4177 0.0052  0.0353  -0.0501 42  ARG A CD    
311   N NE    A ARG A 41  ? 0.5017 0.4496 0.4262 0.0039  0.0321  -0.0528 42  ARG A NE    
312   N NE    B ARG A 41  ? 0.4988 0.4600 0.4287 0.0065  0.0364  -0.0491 42  ARG A NE    
313   C CZ    A ARG A 41  ? 0.5338 0.4834 0.4570 0.0078  0.0337  -0.0528 42  ARG A CZ    
314   C CZ    B ARG A 41  ? 0.4840 0.4520 0.4155 0.0087  0.0384  -0.0476 42  ARG A CZ    
315   N NH1   A ARG A 41  ? 0.5149 0.4729 0.4420 0.0081  0.0359  -0.0505 42  ARG A NH1   
316   N NH1   B ARG A 41  ? 0.4924 0.4689 0.4244 0.0097  0.0397  -0.0467 42  ARG A NH1   
317   N NH2   A ARG A 41  ? 0.5476 0.4903 0.4658 0.0114  0.0329  -0.0550 42  ARG A NH2   
318   N NH2   B ARG A 41  ? 0.4747 0.4415 0.4075 0.0097  0.0391  -0.0469 42  ARG A NH2   
319   N N     . TRP A 42  ? 0.4183 0.3992 0.3686 -0.0104 0.0359  -0.0410 43  TRP A N     
320   C CA    . TRP A 42  ? 0.3887 0.3758 0.3427 -0.0128 0.0360  -0.0389 43  TRP A CA    
321   C C     . TRP A 42  ? 0.3774 0.3615 0.3343 -0.0166 0.0343  -0.0388 43  TRP A C     
322   O O     . TRP A 42  ? 0.3776 0.3637 0.3347 -0.0180 0.0333  -0.0384 43  TRP A O     
323   C CB    . TRP A 42  ? 0.4100 0.4024 0.3681 -0.0133 0.0375  -0.0367 43  TRP A CB    
324   C CG    . TRP A 42  ? 0.4077 0.4044 0.3704 -0.0166 0.0371  -0.0346 43  TRP A CG    
325   C CD1   . TRP A 42  ? 0.4193 0.4219 0.3825 -0.0171 0.0371  -0.0330 43  TRP A CD1   
326   C CD2   . TRP A 42  ? 0.4111 0.4064 0.3785 -0.0197 0.0365  -0.0338 43  TRP A CD2   
327   N NE1   . TRP A 42  ? 0.3852 0.3895 0.3531 -0.0204 0.0364  -0.0313 43  TRP A NE1   
328   C CE2   . TRP A 42  ? 0.3977 0.3977 0.3682 -0.0218 0.0361  -0.0319 43  TRP A CE2   
329   C CE3   . TRP A 42  ? 0.4036 0.3942 0.3729 -0.0208 0.0365  -0.0344 43  TRP A CE3   
330   C CZ2   . TRP A 42  ? 0.3685 0.3683 0.3437 -0.0247 0.0355  -0.0309 43  TRP A CZ2   
331   C CZ3   . TRP A 42  ? 0.4146 0.4057 0.3885 -0.0236 0.0361  -0.0334 43  TRP A CZ3   
332   C CH2   . TRP A 42  ? 0.4074 0.4028 0.3841 -0.0254 0.0356  -0.0318 43  TRP A CH2   
333   N N     . LEU A 43  ? 0.3866 0.3663 0.3459 -0.0182 0.0340  -0.0391 44  LEU A N     
334   C CA    . LEU A 43  ? 0.3968 0.3744 0.3597 -0.0217 0.0326  -0.0388 44  LEU A CA    
335   C C     . LEU A 43  ? 0.3644 0.3382 0.3243 -0.0221 0.0306  -0.0403 44  LEU A C     
336   O O     . LEU A 43  ? 0.3454 0.3205 0.3074 -0.0243 0.0293  -0.0398 44  LEU A O     
337   C CB    . LEU A 43  ? 0.4311 0.4048 0.3964 -0.0228 0.0329  -0.0387 44  LEU A CB    
338   C CG    . LEU A 43  ? 0.4631 0.4347 0.4323 -0.0262 0.0317  -0.0385 44  LEU A CG    
339   C CD1   . LEU A 43  ? 0.4600 0.4367 0.4338 -0.0281 0.0317  -0.0368 44  LEU A CD1   
340   C CD2   . LEU A 43  ? 0.4520 0.4199 0.4228 -0.0270 0.0323  -0.0384 44  LEU A CD2   
341   N N     . THR A 44  ? 0.3706 0.3395 0.3255 -0.0199 0.0301  -0.0423 45  THR A N     
342   C CA    . THR A 44  ? 0.4068 0.3707 0.3583 -0.0203 0.0279  -0.0442 45  THR A CA    
343   C C     . THR A 44  ? 0.4559 0.4240 0.4054 -0.0199 0.0273  -0.0441 45  THR A C     
344   O O     . THR A 44  ? 0.4395 0.4054 0.3880 -0.0214 0.0252  -0.0449 45  THR A O     
345   C CB    . THR A 44  ? 0.4285 0.3862 0.3746 -0.0175 0.0276  -0.0464 45  THR A CB    
346   O OG1   . THR A 44  ? 0.5026 0.4567 0.4513 -0.0186 0.0279  -0.0459 45  THR A OG1   
347   C CG2   . THR A 44  ? 0.4372 0.3891 0.3790 -0.0177 0.0250  -0.0486 45  THR A CG2   
348   N N     . LYS A 45  ? 0.5008 0.4749 0.4495 -0.0179 0.0291  -0.0430 46  LYS A N     
349   C CA    . LYS A 45  ? 0.5321 0.5109 0.4787 -0.0174 0.0288  -0.0426 46  LYS A CA    
350   C C     . LYS A 45  ? 0.5100 0.4924 0.4618 -0.0209 0.0280  -0.0404 46  LYS A C     
351   O O     . LYS A 45  ? 0.4479 0.4317 0.3985 -0.0218 0.0267  -0.0401 46  LYS A O     
352   C CB    . LYS A 45  ? 0.6256 0.6103 0.5701 -0.0141 0.0310  -0.0419 46  LYS A CB    
353   C CG    . LYS A 45  ? 0.6967 0.6782 0.6354 -0.0099 0.0317  -0.0442 46  LYS A CG    
354   C CD    . LYS A 45  ? 0.7872 0.7755 0.7236 -0.0065 0.0339  -0.0435 46  LYS A CD    
355   C CE    . LYS A 45  ? 0.8674 0.8604 0.8011 -0.0063 0.0336  -0.0430 46  LYS A CE    
356   N NZ    . LYS A 45  ? 0.9021 0.9023 0.8337 -0.0029 0.0358  -0.0422 46  LYS A NZ    
357   N N     . LEU A 46  ? 0.4967 0.4805 0.4542 -0.0228 0.0288  -0.0388 47  LEU A N     
358   C CA    . LEU A 46  ? 0.4895 0.4758 0.4521 -0.0260 0.0280  -0.0369 47  LEU A CA    
359   C C     . LEU A 46  ? 0.4810 0.4627 0.4446 -0.0282 0.0257  -0.0379 47  LEU A C     
360   O O     . LEU A 46  ? 0.5299 0.5129 0.4941 -0.0297 0.0241  -0.0373 47  LEU A O     
361   C CB    . LEU A 46  ? 0.5199 0.5080 0.4877 -0.0270 0.0293  -0.0354 47  LEU A CB    
362   C CG    . LEU A 46  ? 0.5205 0.5147 0.4892 -0.0262 0.0309  -0.0335 47  LEU A CG    
363   C CD1   . LEU A 46  ? 0.5066 0.5018 0.4804 -0.0276 0.0317  -0.0323 47  LEU A CD1   
364   C CD2   . LEU A 46  ? 0.5323 0.5312 0.5011 -0.0271 0.0301  -0.0319 47  LEU A CD2   
365   N N     . ASN A 47  ? 0.4436 0.4200 0.4073 -0.0284 0.0255  -0.0393 48  ASN A N     
366   C CA    . ASN A 47  ? 0.4119 0.3840 0.3771 -0.0307 0.0234  -0.0400 48  ASN A CA    
367   C C     . ASN A 47  ? 0.3787 0.3444 0.3399 -0.0296 0.0228  -0.0422 48  ASN A C     
368   O O     . ASN A 47  ? 0.3943 0.3578 0.3558 -0.0288 0.0241  -0.0424 48  ASN A O     
369   C CB    . ASN A 47  ? 0.4181 0.3914 0.3901 -0.0333 0.0237  -0.0386 48  ASN A CB    
370   C CG    . ASN A 47  ? 0.4191 0.3899 0.3936 -0.0359 0.0214  -0.0388 48  ASN A CG    
371   O OD1   . ASN A 47  ? 0.4465 0.4124 0.4185 -0.0362 0.0200  -0.0403 48  ASN A OD1   
372   N ND2   . ASN A 47  ? 0.4008 0.3748 0.3804 -0.0379 0.0209  -0.0373 48  ASN A ND2   
373   N N     . PRO A 48  ? 0.4221 0.3840 0.3793 -0.0296 0.0206  -0.0439 49  PRO A N     
374   C CA    . PRO A 48  ? 0.4545 0.4094 0.4071 -0.0284 0.0196  -0.0461 49  PRO A CA    
375   C C     . PRO A 48  ? 0.4711 0.4215 0.4273 -0.0310 0.0188  -0.0460 49  PRO A C     
376   O O     . PRO A 48  ? 0.4804 0.4254 0.4340 -0.0300 0.0187  -0.0472 49  PRO A O     
377   C CB    . PRO A 48  ? 0.4540 0.4068 0.4016 -0.0281 0.0171  -0.0478 49  PRO A CB    
378   C CG    . PRO A 48  ? 0.4602 0.4176 0.4123 -0.0309 0.0161  -0.0461 49  PRO A CG    
379   C CD    . PRO A 48  ? 0.4221 0.3859 0.3785 -0.0307 0.0186  -0.0437 49  PRO A CD    
380   N N     . ASN A 49  ? 0.5238 0.4767 0.4860 -0.0342 0.0182  -0.0444 50  ASN A N     
381   C CA    . ASN A 49  ? 0.5863 0.5360 0.5524 -0.0369 0.0174  -0.0440 50  ASN A CA    
382   C C     . ASN A 49  ? 0.5563 0.5078 0.5260 -0.0367 0.0201  -0.0426 50  ASN A C     
383   O O     . ASN A 49  ? 0.5182 0.4740 0.4935 -0.0383 0.0210  -0.0409 50  ASN A O     
384   C CB    . ASN A 49  ? 0.6514 0.6033 0.6224 -0.0401 0.0155  -0.0430 50  ASN A CB    
385   C CG    . ASN A 49  ? 0.7358 0.6849 0.7108 -0.0430 0.0146  -0.0425 50  ASN A CG    
386   O OD1   . ASN A 49  ? 0.7016 0.6464 0.6752 -0.0428 0.0151  -0.0429 50  ASN A OD1   
387   N ND2   . ASN A 49  ? 0.7716 0.7231 0.7516 -0.0457 0.0131  -0.0415 50  ASN A ND2   
388   N N     . VAL A 50  ? 0.5137 0.4617 0.4799 -0.0347 0.0211  -0.0434 51  VAL A N     
389   C CA    . VAL A 50  ? 0.5058 0.4553 0.4745 -0.0342 0.0236  -0.0422 51  VAL A CA    
390   C C     . VAL A 50  ? 0.4684 0.4120 0.4368 -0.0352 0.0231  -0.0423 51  VAL A C     
391   O O     . VAL A 50  ? 0.4843 0.4219 0.4481 -0.0345 0.0215  -0.0439 51  VAL A O     
392   C CB    . VAL A 50  ? 0.5159 0.4676 0.4812 -0.0306 0.0255  -0.0424 51  VAL A CB    
393   C CG1   . VAL A 50  ? 0.5191 0.4713 0.4861 -0.0300 0.0277  -0.0414 51  VAL A CG1   
394   C CG2   . VAL A 50  ? 0.5402 0.4984 0.5065 -0.0300 0.0262  -0.0417 51  VAL A CG2   
395   N N     . ILE A 51  ? 0.4471 0.3923 0.4201 -0.0369 0.0245  -0.0407 52  ILE A N     
396   C CA    . ILE A 51  ? 0.4249 0.3654 0.3978 -0.0378 0.0246  -0.0402 52  ILE A CA    
397   C C     . ILE A 51  ? 0.4008 0.3432 0.3738 -0.0359 0.0273  -0.0393 52  ILE A C     
398   O O     . ILE A 51  ? 0.3600 0.3079 0.3365 -0.0361 0.0291  -0.0382 52  ILE A O     
399   C CB    . ILE A 51  ? 0.4582 0.3992 0.4366 -0.0417 0.0239  -0.0389 52  ILE A CB    
400   C CG1   . ILE A 51  ? 0.4611 0.4000 0.4394 -0.0437 0.0208  -0.0398 52  ILE A CG1   
401   C CG2   . ILE A 51  ? 0.4915 0.4285 0.4702 -0.0428 0.0244  -0.0379 52  ILE A CG2   
402   C CD1   . ILE A 51  ? 0.5051 0.4448 0.4890 -0.0475 0.0198  -0.0383 52  ILE A CD1   
403   N N     . ASN A 52  ? 0.3795 0.3168 0.3482 -0.0341 0.0274  -0.0399 53  ASN A N     
404   C CA    . ASN A 52  ? 0.4114 0.3500 0.3793 -0.0319 0.0296  -0.0392 53  ASN A CA    
405   C C     . ASN A 52  ? 0.4231 0.3607 0.3941 -0.0341 0.0305  -0.0374 53  ASN A C     
406   O O     . ASN A 52  ? 0.3930 0.3248 0.3628 -0.0354 0.0292  -0.0373 53  ASN A O     
407   C CB    . ASN A 52  ? 0.4317 0.3660 0.3936 -0.0284 0.0293  -0.0407 53  ASN A CB    
408   C CG    . ASN A 52  ? 0.4699 0.4064 0.4310 -0.0259 0.0315  -0.0398 53  ASN A CG    
409   O OD1   . ASN A 52  ? 0.4780 0.4186 0.4429 -0.0271 0.0331  -0.0382 53  ASN A OD1   
410   N ND2   . ASN A 52  ? 0.4698 0.4037 0.4261 -0.0224 0.0314  -0.0410 53  ASN A ND2   
411   N N     . LEU A 53  ? 0.4373 0.3803 0.4119 -0.0345 0.0326  -0.0361 54  LEU A N     
412   C CA    . LEU A 53  ? 0.4186 0.3618 0.3961 -0.0364 0.0338  -0.0343 54  LEU A CA    
413   C C     . LEU A 53  ? 0.3940 0.3328 0.3677 -0.0347 0.0343  -0.0339 54  LEU A C     
414   O O     . LEU A 53  ? 0.4028 0.3397 0.3776 -0.0363 0.0348  -0.0324 54  LEU A O     
415   C CB    . LEU A 53  ? 0.4431 0.3932 0.4247 -0.0366 0.0358  -0.0334 54  LEU A CB    
416   C CG    . LEU A 53  ? 0.4369 0.3913 0.4228 -0.0384 0.0353  -0.0334 54  LEU A CG    
417   C CD1   . LEU A 53  ? 0.4104 0.3706 0.3997 -0.0381 0.0371  -0.0327 54  LEU A CD1   
418   C CD2   . LEU A 53  ? 0.4281 0.3808 0.4170 -0.0415 0.0342  -0.0328 54  LEU A CD2   
419   N N     . GLN A 54  ? 0.3905 0.3282 0.3600 -0.0313 0.0343  -0.0351 55  GLN A N     
420   C CA    . GLN A 54  ? 0.4699 0.4038 0.4357 -0.0291 0.0347  -0.0348 55  GLN A CA    
421   C C     . GLN A 54  ? 0.5119 0.4384 0.4762 -0.0308 0.0332  -0.0344 55  GLN A C     
422   O O     . GLN A 54  ? 0.5149 0.4383 0.4776 -0.0302 0.0337  -0.0333 55  GLN A O     
423   C CB    . GLN A 54  ? 0.5726 0.5059 0.5340 -0.0252 0.0344  -0.0365 55  GLN A CB    
424   C CG    . GLN A 54  ? 0.6238 0.5550 0.5819 -0.0222 0.0352  -0.0362 55  GLN A CG    
425   C CD    . GLN A 54  ? 0.7044 0.6416 0.6649 -0.0217 0.0374  -0.0347 55  GLN A CD    
426   O OE1   . GLN A 54  ? 0.8197 0.7555 0.7802 -0.0221 0.0381  -0.0333 55  GLN A OE1   
427   N NE2   . GLN A 54  ? 0.6742 0.6178 0.6364 -0.0210 0.0382  -0.0350 55  GLN A NE2   
428   N N     . GLN A 55  ? 0.4916 0.4153 0.4565 -0.0331 0.0312  -0.0351 56  GLN A N     
429   C CA    . GLN A 55  ? 0.5054 0.4213 0.4684 -0.0347 0.0291  -0.0349 56  GLN A CA    
430   C C     . GLN A 55  ? 0.5282 0.4441 0.4946 -0.0380 0.0299  -0.0323 56  GLN A C     
431   O O     . GLN A 55  ? 0.5286 0.4381 0.4935 -0.0395 0.0284  -0.0315 56  GLN A O     
432   C CB    . GLN A 55  ? 0.5140 0.4277 0.4771 -0.0366 0.0266  -0.0363 56  GLN A CB    
433   C CG    . GLN A 55  ? 0.4893 0.4083 0.4585 -0.0402 0.0268  -0.0351 56  GLN A CG    
434   C CD    . GLN A 55  ? 0.5088 0.4265 0.4781 -0.0417 0.0242  -0.0366 56  GLN A CD    
435   O OE1   . GLN A 55  ? 0.5599 0.4793 0.5272 -0.0397 0.0238  -0.0384 56  GLN A OE1   
436   N NE2   . GLN A 55  ? 0.5067 0.4216 0.4783 -0.0455 0.0224  -0.0357 56  GLN A NE2   
437   N N     . PHE A 56  ? 0.5138 0.4369 0.4845 -0.0389 0.0322  -0.0309 57  PHE A N     
438   C CA    . PHE A 56  ? 0.4933 0.4178 0.4677 -0.0420 0.0333  -0.0284 57  PHE A CA    
439   C C     . PHE A 56  ? 0.5014 0.4254 0.4738 -0.0404 0.0351  -0.0270 57  PHE A C     
440   O O     . PHE A 56  ? 0.4394 0.3643 0.4138 -0.0426 0.0362  -0.0247 57  PHE A O     
441   C CB    . PHE A 56  ? 0.4836 0.4158 0.4637 -0.0438 0.0347  -0.0278 57  PHE A CB    
442   C CG    . PHE A 56  ? 0.4789 0.4115 0.4616 -0.0460 0.0328  -0.0287 57  PHE A CG    
443   C CD1   . PHE A 56  ? 0.5012 0.4304 0.4855 -0.0494 0.0310  -0.0276 57  PHE A CD1   
444   C CD2   . PHE A 56  ? 0.4788 0.4154 0.4625 -0.0448 0.0325  -0.0303 57  PHE A CD2   
445   C CE1   . PHE A 56  ? 0.5216 0.4514 0.5084 -0.0515 0.0290  -0.0283 57  PHE A CE1   
446   C CE2   . PHE A 56  ? 0.5007 0.4376 0.4866 -0.0468 0.0306  -0.0309 57  PHE A CE2   
447   C CZ    . PHE A 56  ? 0.5004 0.4340 0.4879 -0.0501 0.0288  -0.0300 57  PHE A CZ    
448   N N     . TYR A 57  ? 0.5085 0.4316 0.4769 -0.0366 0.0354  -0.0282 58  TYR A N     
449   C CA    . TYR A 57  ? 0.5089 0.4311 0.4750 -0.0349 0.0367  -0.0269 58  TYR A CA    
450   C C     . TYR A 57  ? 0.5355 0.4491 0.4982 -0.0352 0.0350  -0.0261 58  TYR A C     
451   O O     . TYR A 57  ? 0.5207 0.4286 0.4814 -0.0355 0.0326  -0.0273 58  TYR A O     
452   C CB    . TYR A 57  ? 0.5132 0.4380 0.4768 -0.0307 0.0375  -0.0283 58  TYR A CB    
453   C CG    . TYR A 57  ? 0.5301 0.4632 0.4970 -0.0305 0.0394  -0.0284 58  TYR A CG    
454   C CD1   . TYR A 57  ? 0.5511 0.4881 0.5196 -0.0309 0.0414  -0.0268 58  TYR A CD1   
455   C CD2   . TYR A 57  ? 0.5178 0.4544 0.4859 -0.0298 0.0390  -0.0301 58  TYR A CD2   
456   C CE1   . TYR A 57  ? 0.5402 0.4840 0.5114 -0.0306 0.0428  -0.0271 58  TYR A CE1   
457   C CE2   . TYR A 57  ? 0.5254 0.4688 0.4963 -0.0297 0.0405  -0.0301 58  TYR A CE2   
458   C CZ    . TYR A 57  ? 0.5139 0.4607 0.4864 -0.0301 0.0422  -0.0287 58  TYR A CZ    
459   O OH    . TYR A 57  ? 0.5452 0.4981 0.5203 -0.0300 0.0433  -0.0289 58  TYR A OH    
460   N N     . ALA A 58  ? 0.5232 0.4357 0.4848 -0.0352 0.0360  -0.0240 59  ALA A N     
461   C CA    . ALA A 58  ? 0.5644 0.4687 0.5227 -0.0355 0.0344  -0.0227 59  ALA A CA    
462   C C     . ALA A 58  ? 0.6464 0.5439 0.5999 -0.0324 0.0321  -0.0252 59  ALA A C     
463   O O     . ALA A 58  ? 0.6641 0.5641 0.6158 -0.0287 0.0326  -0.0271 59  ALA A O     
464   C CB    . ALA A 58  ? 0.5433 0.4481 0.5002 -0.0345 0.0360  -0.0206 59  ALA A CB    
465   N N     . GLN A 59  ? 0.7392 0.6284 0.6907 -0.0340 0.0295  -0.0251 60  GLN A N     
466   C CA    . GLN A 59  ? 0.8474 0.7293 0.7940 -0.0312 0.0270  -0.0276 60  GLN A CA    
467   C C     . GLN A 59  ? 0.9213 0.7938 0.8639 -0.0307 0.0253  -0.0263 60  GLN A C     
468   O O     . GLN A 59  ? 0.9240 0.7921 0.8677 -0.0346 0.0240  -0.0241 60  GLN A O     
469   C CB    . GLN A 59  ? 0.9146 0.7941 0.8619 -0.0334 0.0248  -0.0293 60  GLN A CB    
470   C CG    . GLN A 59  ? 0.9365 0.8245 0.8873 -0.0336 0.0261  -0.0307 60  GLN A CG    
471   C CD    . GLN A 59  ? 0.9221 0.8132 0.8703 -0.0289 0.0270  -0.0331 60  GLN A CD    
472   O OE1   . GLN A 59  ? 0.8847 0.7706 0.8282 -0.0259 0.0253  -0.0354 60  GLN A OE1   
473   N NE2   . GLN A 59  ? 0.8730 0.7729 0.8242 -0.0281 0.0296  -0.0326 60  GLN A NE2   
474   N N     . ASN A 60  ? 0.9646 0.8342 0.9028 -0.0259 0.0252  -0.0274 61  ASN A N     
475   C CA    . ASN A 60  ? 0.9599 0.8199 0.8936 -0.0246 0.0232  -0.0266 61  ASN A CA    
476   C C     . ASN A 60  ? 0.8922 0.7534 0.8275 -0.0266 0.0246  -0.0228 61  ASN A C     
477   O O     . ASN A 60  ? 1.0518 0.9093 0.9884 -0.0309 0.0237  -0.0203 61  ASN A O     
478   C CB    . ASN A 60  ? 0.9882 0.8385 0.9200 -0.0270 0.0197  -0.0274 61  ASN A CB    
479   C CG    . ASN A 60  ? 1.0108 0.8601 0.9408 -0.0251 0.0182  -0.0312 61  ASN A CG    
480   O OD1   . ASN A 60  ? 1.0288 0.8777 0.9551 -0.0200 0.0183  -0.0338 61  ASN A OD1   
481   N ND2   . ASN A 60  ? 1.0261 0.8755 0.9586 -0.0291 0.0169  -0.0316 61  ASN A ND2   
482   N N     . GLY A 61  ? 0.8413 0.7077 0.7763 -0.0236 0.0269  -0.0222 62  GLY A N     
483   C CA    . GLY A 61  ? 0.7646 0.6323 0.7002 -0.0248 0.0283  -0.0187 62  GLY A CA    
484   C C     . GLY A 61  ? 0.6956 0.5641 0.6349 -0.0306 0.0286  -0.0158 62  GLY A C     
485   O O     . GLY A 61  ? 0.7037 0.5681 0.6421 -0.0326 0.0282  -0.0128 62  GLY A O     
486   N N     . GLU A 62  ? 0.7304 0.6047 0.6740 -0.0333 0.0294  -0.0167 63  GLU A N     
487   C CA    . GLU A 62  ? 0.6986 0.5751 0.6464 -0.0387 0.0299  -0.0142 63  GLU A CA    
488   C C     . GLU A 62  ? 0.6410 0.5268 0.5919 -0.0394 0.0333  -0.0122 63  GLU A C     
489   O O     . GLU A 62  ? 0.5152 0.4075 0.4668 -0.0367 0.0352  -0.0138 63  GLU A O     
490   C CB    . GLU A 62  ? 0.7404 0.6185 0.6913 -0.0409 0.0289  -0.0161 63  GLU A CB    
491   C CG    . GLU A 62  ? 0.7825 0.6654 0.7388 -0.0461 0.0299  -0.0137 63  GLU A CG    
492   C CD    . GLU A 62  ? 0.8555 0.7405 0.8152 -0.0482 0.0288  -0.0155 63  GLU A CD    
493   O OE1   . GLU A 62  ? 0.9068 0.7967 0.8672 -0.0459 0.0296  -0.0182 63  GLU A OE1   
494   O OE2   . GLU A 62  ? 0.9346 0.8165 0.8963 -0.0524 0.0270  -0.0141 63  GLU A OE2   
495   N N     . VAL A 63  ? 0.6182 0.5045 0.5711 -0.0432 0.0341  -0.0088 64  VAL A N     
496   C CA    . VAL A 63  ? 0.6206 0.5154 0.5763 -0.0442 0.0373  -0.0069 64  VAL A CA    
497   C C     . VAL A 63  ? 0.5997 0.5015 0.5609 -0.0471 0.0385  -0.0073 64  VAL A C     
498   O O     . VAL A 63  ? 0.5844 0.4855 0.5485 -0.0512 0.0379  -0.0055 64  VAL A O     
499   C CB    . VAL A 63  ? 0.6480 0.5405 0.6025 -0.0465 0.0378  -0.0027 64  VAL A CB    
500   C CG1   . VAL A 63  ? 0.6560 0.5576 0.6135 -0.0479 0.0412  -0.0008 64  VAL A CG1   
501   C CG2   . VAL A 63  ? 0.6496 0.5355 0.5987 -0.0433 0.0366  -0.0021 64  VAL A CG2   
502   N N     . LYS A 64  ? 0.5632 0.4720 0.5261 -0.0450 0.0402  -0.0096 65  LYS A N     
503   C CA    . LYS A 64  ? 0.5770 0.4924 0.5450 -0.0470 0.0411  -0.0105 65  LYS A CA    
504   C C     . LYS A 64  ? 0.5479 0.4718 0.5176 -0.0453 0.0440  -0.0111 65  LYS A C     
505   O O     . LYS A 64  ? 0.4425 0.3675 0.4100 -0.0418 0.0442  -0.0130 65  LYS A O     
506   C CB    . LYS A 64  ? 0.5999 0.5127 0.5680 -0.0463 0.0389  -0.0135 65  LYS A CB    
507   C CG    . LYS A 64  ? 0.6452 0.5640 0.6186 -0.0485 0.0393  -0.0144 65  LYS A CG    
508   C CD    . LYS A 64  ? 0.6905 0.6063 0.6634 -0.0479 0.0369  -0.0172 65  LYS A CD    
509   C CE    . LYS A 64  ? 0.7091 0.6307 0.6873 -0.0501 0.0371  -0.0178 65  LYS A CE    
510   N NZ    . LYS A 64  ? 0.7424 0.6611 0.7197 -0.0495 0.0347  -0.0204 65  LYS A NZ    
511   N N     . ASN A 65  ? 0.5354 0.4655 0.5091 -0.0478 0.0460  -0.0096 66  ASN A N     
512   C CA    . ASN A 65  ? 0.5724 0.5102 0.5478 -0.0464 0.0486  -0.0103 66  ASN A CA    
513   C C     . ASN A 65  ? 0.5452 0.4865 0.5231 -0.0453 0.0482  -0.0133 66  ASN A C     
514   O O     . ASN A 65  ? 0.5874 0.5287 0.5684 -0.0472 0.0471  -0.0138 66  ASN A O     
515   C CB    . ASN A 65  ? 0.5775 0.5206 0.5562 -0.0492 0.0509  -0.0078 66  ASN A CB    
516   C CG    . ASN A 65  ? 0.5673 0.5177 0.5468 -0.0474 0.0534  -0.0086 66  ASN A CG    
517   O OD1   . ASN A 65  ? 0.5522 0.5061 0.5335 -0.0459 0.0536  -0.0111 66  ASN A OD1   
518   N ND2   . ASN A 65  ? 0.5334 0.4858 0.5114 -0.0475 0.0554  -0.0064 66  ASN A ND2   
519   N N     . ARG A 66  ? 0.5509 0.4951 0.5274 -0.0422 0.0489  -0.0150 67  ARG A N     
520   C CA    . ARG A 66  ? 0.5463 0.4932 0.5245 -0.0409 0.0484  -0.0177 67  ARG A CA    
521   C C     . ARG A 66  ? 0.5454 0.4979 0.5288 -0.0430 0.0494  -0.0178 67  ARG A C     
522   O O     . ARG A 66  ? 0.4670 0.4208 0.4526 -0.0430 0.0484  -0.0195 67  ARG A O     
523   C CB    . ARG A 66  ? 0.5548 0.5044 0.5308 -0.0376 0.0491  -0.0191 67  ARG A CB    
524   C CG    . ARG A 66  ? 0.5776 0.5225 0.5490 -0.0350 0.0479  -0.0194 67  ARG A CG    
525   C CD    . ARG A 66  ? 0.6048 0.5529 0.5752 -0.0320 0.0480  -0.0212 67  ARG A CD    
526   N NE    . ARG A 66  ? 0.6427 0.5961 0.6139 -0.0316 0.0498  -0.0209 67  ARG A NE    
527   C CZ    . ARG A 66  ? 0.7046 0.6581 0.6734 -0.0309 0.0507  -0.0195 67  ARG A CZ    
528   N NH1   . ARG A 66  ? 0.7003 0.6488 0.6660 -0.0306 0.0502  -0.0180 67  ARG A NH1   
529   N NH2   . ARG A 66  ? 0.7403 0.6985 0.7096 -0.0305 0.0521  -0.0196 67  ARG A NH2   
530   N N     . ARG A 67  ? 0.5662 0.5222 0.5514 -0.0445 0.0514  -0.0159 68  ARG A N     
531   C CA    . ARG A 67  ? 0.6383 0.6000 0.6286 -0.0461 0.0526  -0.0159 68  ARG A CA    
532   C C     . ARG A 67  ? 0.5829 0.5429 0.5764 -0.0488 0.0508  -0.0156 68  ARG A C     
533   O O     . ARG A 67  ? 0.5515 0.5155 0.5492 -0.0496 0.0508  -0.0165 68  ARG A O     
534   C CB    . ARG A 67  ? 0.7219 0.6876 0.7130 -0.0471 0.0552  -0.0137 68  ARG A CB    
535   C CG    . ARG A 67  ? 0.8075 0.7746 0.7950 -0.0446 0.0567  -0.0140 68  ARG A CG    
536   C CD    . ARG A 67  ? 0.8700 0.8411 0.8578 -0.0454 0.0593  -0.0119 68  ARG A CD    
537   N NE    . ARG A 67  ? 0.9177 0.8953 0.9099 -0.0458 0.0610  -0.0126 68  ARG A NE    
538   C CZ    . ARG A 67  ? 0.8965 0.8787 0.8884 -0.0440 0.0629  -0.0135 68  ARG A CZ    
539   N NH1   . ARG A 67  ? 0.9099 0.8911 0.8971 -0.0420 0.0634  -0.0137 68  ARG A NH1   
540   N NH2   . ARG A 67  ? 0.9264 0.9141 0.9223 -0.0441 0.0642  -0.0142 68  ARG A NH2   
541   N N     . ASP A 68  ? 0.5473 0.5011 0.5386 -0.0502 0.0491  -0.0144 69  ASP A N     
542   C CA    . ASP A 68  ? 0.5115 0.4626 0.5052 -0.0529 0.0470  -0.0142 69  ASP A CA    
543   C C     . ASP A 68  ? 0.4821 0.4305 0.4744 -0.0513 0.0447  -0.0170 69  ASP A C     
544   O O     . ASP A 68  ? 0.4706 0.4198 0.4660 -0.0528 0.0433  -0.0178 69  ASP A O     
545   C CB    . ASP A 68  ? 0.5077 0.4527 0.4993 -0.0552 0.0458  -0.0118 69  ASP A CB    
546   C CG    . ASP A 68  ? 0.5359 0.4838 0.5290 -0.0573 0.0479  -0.0085 69  ASP A CG    
547   O OD1   . ASP A 68  ? 0.5463 0.5003 0.5444 -0.0594 0.0492  -0.0074 69  ASP A OD1   
548   O OD2   . ASP A 68  ? 0.5403 0.4846 0.5295 -0.0568 0.0482  -0.0069 69  ASP A OD2   
549   N N     . THR A 69  ? 0.4451 0.3905 0.4328 -0.0481 0.0444  -0.0184 70  THR A N     
550   C CA    . THR A 69  ? 0.4552 0.3986 0.4411 -0.0461 0.0426  -0.0210 70  THR A CA    
551   C C     . THR A 69  ? 0.4250 0.3747 0.4147 -0.0458 0.0433  -0.0224 70  THR A C     
552   O O     . THR A 69  ? 0.3880 0.3374 0.3789 -0.0463 0.0416  -0.0237 70  THR A O     
553   C CB    . THR A 69  ? 0.4745 0.4153 0.4554 -0.0427 0.0427  -0.0219 70  THR A CB    
554   O OG1   . THR A 69  ? 0.5691 0.5029 0.5465 -0.0430 0.0415  -0.0207 70  THR A OG1   
555   C CG2   . THR A 69  ? 0.4875 0.4281 0.4668 -0.0402 0.0415  -0.0244 70  THR A CG2   
556   N N     . TYR A 70  ? 0.3988 0.3540 0.3900 -0.0449 0.0456  -0.0221 71  TYR A N     
557   C CA    . TYR A 70  ? 0.4059 0.3667 0.4004 -0.0443 0.0462  -0.0234 71  TYR A CA    
558   C C     . TYR A 70  ? 0.4401 0.4035 0.4397 -0.0470 0.0458  -0.0228 71  TYR A C     
559   O O     . TYR A 70  ? 0.4866 0.4521 0.4886 -0.0470 0.0448  -0.0241 71  TYR A O     
560   C CB    . TYR A 70  ? 0.3905 0.3556 0.3849 -0.0428 0.0485  -0.0231 71  TYR A CB    
561   C CG    . TYR A 70  ? 0.3964 0.3595 0.3861 -0.0402 0.0487  -0.0236 71  TYR A CG    
562   C CD1   . TYR A 70  ? 0.3975 0.3576 0.3843 -0.0385 0.0471  -0.0249 71  TYR A CD1   
563   C CD2   . TYR A 70  ? 0.4379 0.4022 0.4259 -0.0394 0.0505  -0.0225 71  TYR A CD2   
564   C CE1   . TYR A 70  ? 0.4095 0.3685 0.3925 -0.0360 0.0473  -0.0252 71  TYR A CE1   
565   C CE2   . TYR A 70  ? 0.4430 0.4059 0.4270 -0.0371 0.0505  -0.0228 71  TYR A CE2   
566   C CZ    . TYR A 70  ? 0.4287 0.3891 0.4104 -0.0353 0.0489  -0.0241 71  TYR A CZ    
567   O OH    . TYR A 70  ? 0.4879 0.4474 0.4661 -0.0329 0.0489  -0.0242 71  TYR A OH    
568   N N     . GLU A 71  ? 0.4485 0.4121 0.4500 -0.0494 0.0465  -0.0207 72  GLU A N     
569   C CA    . GLU A 71  ? 0.4695 0.4363 0.4763 -0.0521 0.0463  -0.0198 72  GLU A CA    
570   C C     . GLU A 71  ? 0.4812 0.4442 0.4883 -0.0536 0.0433  -0.0206 72  GLU A C     
571   O O     . GLU A 71  ? 0.4812 0.4473 0.4925 -0.0548 0.0424  -0.0209 72  GLU A O     
572   C CB    . GLU A 71  ? 0.5330 0.5009 0.5414 -0.0545 0.0477  -0.0170 72  GLU A CB    
573   C CG    . GLU A 71  ? 0.5815 0.5533 0.5960 -0.0576 0.0475  -0.0157 72  GLU A CG    
574   C CD    . GLU A 71  ? 0.6228 0.6018 0.6419 -0.0566 0.0488  -0.0166 72  GLU A CD    
575   O OE1   . GLU A 71  ? 0.6243 0.6050 0.6418 -0.0537 0.0499  -0.0183 72  GLU A OE1   
576   O OE2   . GLU A 71  ? 0.6994 0.6823 0.7239 -0.0587 0.0486  -0.0157 72  GLU A OE2   
577   N N     . GLN A 72  ? 0.4434 0.3995 0.4459 -0.0534 0.0415  -0.0208 73  GLN A N     
578   C CA    . GLN A 72  ? 0.4495 0.4009 0.4510 -0.0545 0.0385  -0.0218 73  GLN A CA    
579   C C     . GLN A 72  ? 0.4130 0.3658 0.4139 -0.0523 0.0376  -0.0243 73  GLN A C     
580   O O     . GLN A 72  ? 0.4115 0.3638 0.4138 -0.0534 0.0355  -0.0252 73  GLN A O     
581   C CB    . GLN A 72  ? 0.4616 0.4050 0.4579 -0.0543 0.0370  -0.0217 73  GLN A CB    
582   C CG    . GLN A 72  ? 0.4641 0.4053 0.4611 -0.0572 0.0372  -0.0188 73  GLN A CG    
583   C CD    . GLN A 72  ? 0.4991 0.4317 0.4907 -0.0567 0.0356  -0.0187 73  GLN A CD    
584   O OE1   . GLN A 72  ? 0.5067 0.4351 0.4937 -0.0538 0.0345  -0.0208 73  GLN A OE1   
585   N NE2   . GLN A 72  ? 0.5002 0.4302 0.4923 -0.0595 0.0354  -0.0160 73  GLN A NE2   
586   N N     . MET A 73  ? 0.3995 0.3539 0.3980 -0.0492 0.0391  -0.0253 74  MET A N     
587   C CA    . MET A 73  ? 0.3801 0.3363 0.3780 -0.0472 0.0385  -0.0273 74  MET A CA    
588   C C     . MET A 73  ? 0.3920 0.3540 0.3954 -0.0484 0.0387  -0.0273 74  MET A C     
589   O O     . MET A 73  ? 0.4099 0.3721 0.4142 -0.0487 0.0368  -0.0283 74  MET A O     
590   C CB    . MET A 73  ? 0.3603 0.3180 0.3554 -0.0441 0.0401  -0.0279 74  MET A CB    
591   C CG    . MET A 73  ? 0.3609 0.3133 0.3504 -0.0422 0.0396  -0.0283 74  MET A CG    
592   S SD    . MET A 73  ? 0.3625 0.3177 0.3495 -0.0388 0.0414  -0.0288 74  MET A SD    
593   C CE    . MET A 73  ? 0.3903 0.3389 0.3711 -0.0366 0.0405  -0.0291 74  MET A CE    
594   N N     . VAL A 74  ? 0.4086 0.3753 0.4154 -0.0488 0.0408  -0.0261 75  VAL A N     
595   C CA    . VAL A 74  ? 0.3858 0.3581 0.3978 -0.0493 0.0413  -0.0261 75  VAL A CA    
596   C C     . VAL A 74  ? 0.4286 0.4009 0.4442 -0.0521 0.0393  -0.0256 75  VAL A C     
597   O O     . VAL A 74  ? 0.4553 0.4299 0.4735 -0.0522 0.0381  -0.0264 75  VAL A O     
598   C CB    . VAL A 74  ? 0.3631 0.3400 0.3778 -0.0492 0.0440  -0.0250 75  VAL A CB    
599   C CG1   . VAL A 74  ? 0.3469 0.3296 0.3674 -0.0497 0.0444  -0.0250 75  VAL A CG1   
600   C CG2   . VAL A 74  ? 0.3977 0.3748 0.4089 -0.0465 0.0457  -0.0257 75  VAL A CG2   
601   N N     . ASN A 75  ? 0.4194 0.3889 0.4350 -0.0544 0.0388  -0.0242 76  ASN A N     
602   C CA    . ASN A 75  ? 0.4609 0.4304 0.4801 -0.0575 0.0368  -0.0234 76  ASN A CA    
603   C C     . ASN A 75  ? 0.4431 0.4091 0.4602 -0.0573 0.0338  -0.0251 76  ASN A C     
604   O O     . ASN A 75  ? 0.4805 0.4490 0.5012 -0.0585 0.0323  -0.0253 76  ASN A O     
605   C CB    . ASN A 75  ? 0.4669 0.4334 0.4860 -0.0601 0.0366  -0.0213 76  ASN A CB    
606   C CG    . ASN A 75  ? 0.5904 0.5569 0.6134 -0.0636 0.0342  -0.0204 76  ASN A CG    
607   O OD1   . ASN A 75  ? 0.5908 0.5510 0.6110 -0.0652 0.0317  -0.0205 76  ASN A OD1   
608   N ND2   . ASN A 75  ? 0.6311 0.6043 0.6604 -0.0648 0.0349  -0.0195 76  ASN A ND2   
609   N N     . ALA A 76  ? 0.4216 0.3818 0.4326 -0.0557 0.0329  -0.0264 77  ALA A N     
610   C CA    . ALA A 76  ? 0.3817 0.3382 0.3895 -0.0551 0.0302  -0.0282 77  ALA A CA    
611   C C     . ALA A 76  ? 0.3603 0.3215 0.3702 -0.0539 0.0301  -0.0292 77  ALA A C     
612   O O     . ALA A 76  ? 0.3351 0.2964 0.3461 -0.0549 0.0278  -0.0298 77  ALA A O     
613   C CB    . ALA A 76  ? 0.3839 0.3347 0.3850 -0.0527 0.0300  -0.0294 77  ALA A CB    
614   N N     . ILE A 77  ? 0.3221 0.2870 0.3323 -0.0517 0.0324  -0.0293 78  ILE A N     
615   C CA    . ILE A 77  ? 0.3037 0.2727 0.3156 -0.0504 0.0323  -0.0301 78  ILE A CA    
616   C C     . ILE A 77  ? 0.3025 0.2758 0.3207 -0.0524 0.0316  -0.0293 78  ILE A C     
617   O O     . ILE A 77  ? 0.3112 0.2854 0.3304 -0.0526 0.0297  -0.0299 78  ILE A O     
618   C CB    . ILE A 77  ? 0.2848 0.2567 0.2963 -0.0480 0.0348  -0.0302 78  ILE A CB    
619   C CG1   . ILE A 77  ? 0.2824 0.2507 0.2881 -0.0460 0.0353  -0.0309 78  ILE A CG1   
620   C CG2   . ILE A 77  ? 0.3011 0.2770 0.3148 -0.0470 0.0345  -0.0308 78  ILE A CG2   
621   C CD1   . ILE A 77  ? 0.2730 0.2438 0.2780 -0.0439 0.0376  -0.0308 78  ILE A CD1   
622   N N     . LEU A 78  ? 0.3312 0.3075 0.3535 -0.0537 0.0332  -0.0279 79  LEU A N     
623   C CA    . LEU A 78  ? 0.3886 0.3700 0.4174 -0.0552 0.0330  -0.0270 79  LEU A CA    
624   C C     . LEU A 78  ? 0.4003 0.3799 0.4305 -0.0578 0.0300  -0.0267 79  LEU A C     
625   O O     . LEU A 78  ? 0.4355 0.4185 0.4699 -0.0586 0.0286  -0.0266 79  LEU A O     
626   C CB    . LEU A 78  ? 0.4279 0.4130 0.4603 -0.0558 0.0356  -0.0254 79  LEU A CB    
627   C CG    . LEU A 78  ? 0.4628 0.4514 0.4956 -0.0533 0.0384  -0.0257 79  LEU A CG    
628   C CD1   . LEU A 78  ? 0.4931 0.4855 0.5291 -0.0520 0.0377  -0.0266 79  LEU A CD1   
629   C CD2   . LEU A 78  ? 0.4879 0.4728 0.5147 -0.0512 0.0393  -0.0266 79  LEU A CD2   
630   N N     . ASP A 79  ? 0.4122 0.3863 0.4388 -0.0592 0.0287  -0.0267 80  ASP A N     
631   C CA    . ASP A 79  ? 0.4726 0.4439 0.4997 -0.0618 0.0255  -0.0266 80  ASP A CA    
632   C C     . ASP A 79  ? 0.4717 0.4429 0.4975 -0.0609 0.0232  -0.0282 80  ASP A C     
633   O O     . ASP A 79  ? 0.4815 0.4547 0.5109 -0.0627 0.0210  -0.0278 80  ASP A O     
634   C CB    . ASP A 79  ? 0.5169 0.4810 0.5391 -0.0629 0.0243  -0.0267 80  ASP A CB    
635   C CG    . ASP A 79  ? 0.5706 0.5346 0.5948 -0.0650 0.0257  -0.0245 80  ASP A CG    
636   O OD1   . ASP A 79  ? 0.6827 0.6529 0.7124 -0.0656 0.0278  -0.0229 80  ASP A OD1   
637   O OD2   . ASP A 79  ? 0.6128 0.5704 0.6329 -0.0658 0.0247  -0.0244 80  ASP A OD2   
638   N N     . ALA A 80  ? 0.4339 0.4031 0.4547 -0.0580 0.0237  -0.0297 81  ALA A N     
639   C CA    . ALA A 80  ? 0.4341 0.4032 0.4529 -0.0569 0.0218  -0.0310 81  ALA A CA    
640   C C     . ALA A 80  ? 0.3978 0.3732 0.4225 -0.0570 0.0219  -0.0303 81  ALA A C     
641   O O     . ALA A 80  ? 0.3405 0.3169 0.3666 -0.0579 0.0195  -0.0305 81  ALA A O     
642   C CB    . ALA A 80  ? 0.4312 0.3983 0.4443 -0.0539 0.0229  -0.0323 81  ALA A CB    
643   N N     . VAL A 81  ? 0.3848 0.3643 0.4125 -0.0558 0.0246  -0.0296 82  VAL A N     
644   C CA    . VAL A 81  ? 0.3916 0.3767 0.4246 -0.0553 0.0250  -0.0291 82  VAL A CA    
645   C C     . VAL A 81  ? 0.3925 0.3806 0.4315 -0.0578 0.0235  -0.0279 82  VAL A C     
646   O O     . VAL A 81  ? 0.4023 0.3930 0.4443 -0.0581 0.0217  -0.0278 82  VAL A O     
647   C CB    . VAL A 81  ? 0.3716 0.3597 0.4061 -0.0535 0.0282  -0.0288 82  VAL A CB    
648   C CG1   . VAL A 81  ? 0.3649 0.3583 0.4049 -0.0527 0.0284  -0.0285 82  VAL A CG1   
649   C CG2   . VAL A 81  ? 0.3567 0.3421 0.3855 -0.0512 0.0294  -0.0298 82  VAL A CG2   
650   N N     . ARG A 82  ? 0.4081 0.3961 0.4489 -0.0598 0.0243  -0.0268 83  ARG A N     
651   C CA    . ARG A 82  ? 0.4192 0.4108 0.4662 -0.0624 0.0233  -0.0253 83  ARG A CA    
652   C C     . ARG A 82  ? 0.4037 0.3929 0.4502 -0.0644 0.0193  -0.0257 83  ARG A C     
653   O O     . ARG A 82  ? 0.3422 0.3352 0.3940 -0.0660 0.0177  -0.0248 83  ARG A O     
654   C CB    . ARG A 82  ? 0.4721 0.4633 0.5202 -0.0644 0.0248  -0.0239 83  ARG A CB    
655   C CG    . ARG A 82  ? 0.4801 0.4743 0.5291 -0.0625 0.0287  -0.0233 83  ARG A CG    
656   C CD    . ARG A 82  ? 0.5365 0.5288 0.5844 -0.0643 0.0301  -0.0220 83  ARG A CD    
657   N NE    . ARG A 82  ? 0.5705 0.5654 0.6183 -0.0623 0.0337  -0.0216 83  ARG A NE    
658   C CZ    . ARG A 82  ? 0.5804 0.5733 0.6260 -0.0630 0.0355  -0.0205 83  ARG A CZ    
659   N NH1   . ARG A 82  ? 0.6206 0.6084 0.6638 -0.0654 0.0338  -0.0198 83  ARG A NH1   
660   N NH2   . ARG A 82  ? 0.5736 0.5692 0.6189 -0.0611 0.0387  -0.0203 83  ARG A NH2   
661   N N     . ALA A 83  ? 0.4046 0.3874 0.4441 -0.0640 0.0178  -0.0271 84  ALA A N     
662   C CA    . ALA A 83  ? 0.4037 0.3834 0.4413 -0.0656 0.0140  -0.0279 84  ALA A CA    
663   C C     . ALA A 83  ? 0.3726 0.3551 0.4110 -0.0642 0.0126  -0.0284 84  ALA A C     
664   O O     . ALA A 83  ? 0.3752 0.3575 0.4142 -0.0657 0.0095  -0.0286 84  ALA A O     
665   C CB    . ALA A 83  ? 0.4285 0.4006 0.4580 -0.0651 0.0131  -0.0295 84  ALA A CB    
666   N N     . GLY A 84  ? 0.3477 0.3328 0.3860 -0.0615 0.0149  -0.0287 85  GLY A N     
667   C CA    . GLY A 84  ? 0.3513 0.3392 0.3908 -0.0602 0.0139  -0.0289 85  GLY A CA    
668   C C     . GLY A 84  ? 0.3852 0.3698 0.4179 -0.0580 0.0138  -0.0302 85  GLY A C     
669   O O     . GLY A 84  ? 0.4255 0.4112 0.4576 -0.0574 0.0121  -0.0304 85  GLY A O     
670   N N     . LYS A 85  ? 0.3801 0.3612 0.4079 -0.0569 0.0155  -0.0310 86  LYS A N     
671   C CA    . LYS A 85  ? 0.4397 0.4181 0.4611 -0.0548 0.0157  -0.0322 86  LYS A CA    
672   C C     . LYS A 85  ? 0.4167 0.3981 0.4389 -0.0526 0.0182  -0.0319 86  LYS A C     
673   O O     . LYS A 85  ? 0.3966 0.3795 0.4211 -0.0521 0.0206  -0.0314 86  LYS A O     
674   C CB    . LYS A 85  ? 0.4846 0.4576 0.5002 -0.0544 0.0163  -0.0332 86  LYS A CB    
675   C CG    . LYS A 85  ? 0.4899 0.4586 0.5039 -0.0566 0.0138  -0.0337 86  LYS A CG    
676   C CD    . LYS A 85  ? 0.5323 0.4950 0.5403 -0.0558 0.0143  -0.0349 86  LYS A CD    
677   C CE    . LYS A 85  ? 0.5398 0.4976 0.5463 -0.0581 0.0115  -0.0354 86  LYS A CE    
678   N NZ    . LYS A 85  ? 0.5674 0.5241 0.5717 -0.0587 0.0082  -0.0364 86  LYS A NZ    
679   N N     . LYS A 86  ? 0.4342 0.4164 0.4542 -0.0513 0.0174  -0.0321 87  LYS A N     
680   C CA    . LYS A 86  ? 0.4284 0.4125 0.4480 -0.0493 0.0193  -0.0318 87  LYS A CA    
681   C C     . LYS A 86  ? 0.4214 0.4029 0.4362 -0.0480 0.0213  -0.0326 87  LYS A C     
682   O O     . LYS A 86  ? 0.5025 0.4820 0.5120 -0.0469 0.0209  -0.0333 87  LYS A O     
683   C CB    . LYS A 86  ? 0.4140 0.3995 0.4322 -0.0487 0.0177  -0.0315 87  LYS A CB    
684   C CG    . LYS A 86  ? 0.4311 0.4186 0.4493 -0.0471 0.0192  -0.0310 87  LYS A CG    
685   C CD    . LYS A 86  ? 0.4685 0.4577 0.4863 -0.0469 0.0174  -0.0302 87  LYS A CD    
686   C CE    . LYS A 86  ? 0.5053 0.4929 0.5175 -0.0469 0.0160  -0.0306 87  LYS A CE    
687   N NZ    . LYS A 86  ? 0.5303 0.5198 0.5420 -0.0468 0.0144  -0.0295 87  LYS A NZ    
688   N N     . THR A 87  ? 0.3985 0.3801 0.4150 -0.0478 0.0235  -0.0324 88  THR A N     
689   C CA    . THR A 87  ? 0.3507 0.3295 0.3631 -0.0468 0.0252  -0.0329 88  THR A CA    
690   C C     . THR A 87  ? 0.3621 0.3426 0.3733 -0.0448 0.0271  -0.0328 88  THR A C     
691   O O     . THR A 87  ? 0.3692 0.3528 0.3840 -0.0446 0.0278  -0.0322 88  THR A O     
692   C CB    . THR A 87  ? 0.3691 0.3471 0.3839 -0.0480 0.0263  -0.0325 88  THR A CB    
693   O OG1   . THR A 87  ? 0.3218 0.2987 0.3383 -0.0502 0.0242  -0.0324 88  THR A OG1   
694   C CG2   . THR A 87  ? 0.3758 0.3503 0.3863 -0.0471 0.0278  -0.0329 88  THR A CG2   
695   N N     . VAL A 88  ? 0.3633 0.3417 0.3693 -0.0433 0.0277  -0.0334 89  VAL A N     
696   C CA    . VAL A 88  ? 0.3477 0.3276 0.3522 -0.0416 0.0294  -0.0333 89  VAL A CA    
697   C C     . VAL A 88  ? 0.3399 0.3172 0.3415 -0.0406 0.0310  -0.0336 89  VAL A C     
698   O O     . VAL A 88  ? 0.3460 0.3198 0.3439 -0.0404 0.0304  -0.0343 89  VAL A O     
699   C CB    . VAL A 88  ? 0.3637 0.3447 0.3651 -0.0405 0.0286  -0.0333 89  VAL A CB    
700   C CG1   . VAL A 88  ? 0.3929 0.3751 0.3921 -0.0387 0.0303  -0.0331 89  VAL A CG1   
701   C CG2   . VAL A 88  ? 0.3690 0.3529 0.3736 -0.0413 0.0271  -0.0325 89  VAL A CG2   
702   N N     . CYS A 89  ? 0.3961 0.3749 0.3990 -0.0400 0.0329  -0.0332 90  CYS A N     
703   C CA    . CYS A 89  ? 0.4173 0.3941 0.4174 -0.0390 0.0345  -0.0333 90  CYS A CA    
704   C C     . CYS A 89  ? 0.4290 0.4072 0.4264 -0.0370 0.0352  -0.0333 90  CYS A C     
705   O O     . CYS A 89  ? 0.4388 0.4200 0.4381 -0.0368 0.0357  -0.0329 90  CYS A O     
706   C CB    . CYS A 89  ? 0.4853 0.4628 0.4884 -0.0397 0.0360  -0.0327 90  CYS A CB    
707   S SG    . CYS A 89  ? 0.6696 0.6446 0.6692 -0.0385 0.0379  -0.0326 90  CYS A SG    
708   N N     . ALA A 90  ? 0.3966 0.3726 0.3895 -0.0356 0.0352  -0.0338 91  ALA A N     
709   C CA    . ALA A 90  ? 0.3800 0.3579 0.3704 -0.0336 0.0359  -0.0337 91  ALA A CA    
710   C C     . ALA A 90  ? 0.3923 0.3687 0.3804 -0.0322 0.0373  -0.0337 91  ALA A C     
711   O O     . ALA A 90  ? 0.4534 0.4262 0.4383 -0.0313 0.0372  -0.0343 91  ALA A O     
712   C CB    . ALA A 90  ? 0.3774 0.3550 0.3644 -0.0326 0.0347  -0.0343 91  ALA A CB    
713   N N     . LEU A 91  ? 0.4337 0.4124 0.4234 -0.0321 0.0385  -0.0330 92  LEU A N     
714   C CA    . LEU A 91  ? 0.4571 0.4349 0.4447 -0.0307 0.0398  -0.0328 92  LEU A CA    
715   C C     . LEU A 91  ? 0.4439 0.4252 0.4304 -0.0292 0.0401  -0.0324 92  LEU A C     
716   O O     . LEU A 91  ? 0.5307 0.5152 0.5190 -0.0297 0.0396  -0.0320 92  LEU A O     
717   C CB    . LEU A 91  ? 0.4902 0.4680 0.4803 -0.0318 0.0409  -0.0324 92  LEU A CB    
718   C CG    . LEU A 91  ? 0.5222 0.4980 0.5145 -0.0337 0.0407  -0.0324 92  LEU A CG    
719   C CD1   . LEU A 91  ? 0.5458 0.5220 0.5398 -0.0343 0.0422  -0.0318 92  LEU A CD1   
720   C CD2   . LEU A 91  ? 0.5636 0.5350 0.5532 -0.0337 0.0399  -0.0327 92  LEU A CD2   
721   N N     . TYR A 92  ? 0.4159 0.3963 0.3994 -0.0273 0.0409  -0.0323 93  TYR A N     
722   C CA    . TYR A 92  ? 0.4285 0.4125 0.4110 -0.0257 0.0412  -0.0318 93  TYR A CA    
723   C C     . TYR A 92  ? 0.4565 0.4433 0.4415 -0.0267 0.0416  -0.0311 93  TYR A C     
724   O O     . TYR A 92  ? 0.4638 0.4490 0.4501 -0.0276 0.0421  -0.0311 93  TYR A O     
725   C CB    . TYR A 92  ? 0.4447 0.4270 0.4235 -0.0232 0.0417  -0.0319 93  TYR A CB    
726   C CG    . TYR A 92  ? 0.4314 0.4115 0.4097 -0.0231 0.0426  -0.0315 93  TYR A CG    
727   C CD1   . TYR A 92  ? 0.4334 0.4088 0.4111 -0.0239 0.0427  -0.0318 93  TYR A CD1   
728   C CD2   . TYR A 92  ? 0.4503 0.4332 0.4286 -0.0222 0.0433  -0.0307 93  TYR A CD2   
729   C CE1   . TYR A 92  ? 0.4321 0.4057 0.4092 -0.0238 0.0436  -0.0312 93  TYR A CE1   
730   C CE2   . TYR A 92  ? 0.4263 0.4072 0.4037 -0.0220 0.0440  -0.0303 93  TYR A CE2   
731   C CZ    . TYR A 92  ? 0.4364 0.4127 0.4131 -0.0228 0.0443  -0.0305 93  TYR A CZ    
732   O OH    . TYR A 92  ? 0.5204 0.4950 0.4961 -0.0227 0.0451  -0.0298 93  TYR A OH    
733   N N     . GLY A 93  ? 0.3778 0.3686 0.3634 -0.0264 0.0413  -0.0303 94  GLY A N     
734   C CA    . GLY A 93  ? 0.4010 0.3941 0.3888 -0.0274 0.0412  -0.0298 94  GLY A CA    
735   C C     . GLY A 93  ? 0.4076 0.4000 0.3985 -0.0293 0.0407  -0.0301 94  GLY A C     
736   O O     . GLY A 93  ? 0.4294 0.4217 0.4214 -0.0302 0.0399  -0.0303 94  GLY A O     
737   N N     . HIS A 94  ? 0.3621 0.3541 0.3541 -0.0299 0.0411  -0.0303 95  HIS A N     
738   C CA    . HIS A 94  ? 0.3798 0.3713 0.3748 -0.0313 0.0408  -0.0308 95  HIS A CA    
739   C C     . HIS A 94  ? 0.3931 0.3819 0.3883 -0.0316 0.0418  -0.0314 95  HIS A C     
740   O O     . HIS A 94  ? 0.3640 0.3513 0.3575 -0.0309 0.0429  -0.0314 95  HIS A O     
741   C CB    . HIS A 94  ? 0.3839 0.3765 0.3798 -0.0315 0.0407  -0.0309 95  HIS A CB    
742   C CG    . HIS A 94  ? 0.4074 0.3996 0.4062 -0.0325 0.0402  -0.0315 95  HIS A CG    
743   N ND1   . HIS A 94  ? 0.4548 0.4457 0.4553 -0.0330 0.0408  -0.0321 95  HIS A ND1   
744   C CD2   . HIS A 94  ? 0.4299 0.4229 0.4302 -0.0330 0.0392  -0.0317 95  HIS A CD2   
745   C CE1   . HIS A 94  ? 0.4269 0.4180 0.4300 -0.0334 0.0402  -0.0326 95  HIS A CE1   
746   N NE2   . HIS A 94  ? 0.4408 0.4328 0.4436 -0.0335 0.0392  -0.0324 95  HIS A NE2   
747   N N     . PRO A 95  ? 0.4063 0.3945 0.4039 -0.0327 0.0412  -0.0317 96  PRO A N     
748   C CA    . PRO A 95  ? 0.4327 0.4187 0.4309 -0.0332 0.0418  -0.0319 96  PRO A CA    
749   C C     . PRO A 95  ? 0.4301 0.4161 0.4297 -0.0335 0.0432  -0.0321 96  PRO A C     
750   O O     . PRO A 95  ? 0.4194 0.4040 0.4194 -0.0341 0.0439  -0.0319 96  PRO A O     
751   C CB    . PRO A 95  ? 0.3986 0.3849 0.3993 -0.0344 0.0405  -0.0320 96  PRO A CB    
752   C CG    . PRO A 95  ? 0.3833 0.3719 0.3858 -0.0346 0.0396  -0.0319 96  PRO A CG    
753   C CD    . PRO A 95  ? 0.3725 0.3622 0.3725 -0.0335 0.0397  -0.0315 96  PRO A CD    
754   N N     . GLY A 96  ? 0.4207 0.4082 0.4207 -0.0331 0.0434  -0.0323 97  GLY A N     
755   C CA    . GLY A 96  ? 0.4406 0.4285 0.4417 -0.0331 0.0446  -0.0327 97  GLY A CA    
756   C C     . GLY A 96  ? 0.4466 0.4346 0.4449 -0.0321 0.0455  -0.0327 97  GLY A C     
757   O O     . GLY A 96  ? 0.4728 0.4614 0.4714 -0.0318 0.0464  -0.0332 97  GLY A O     
758   N N     . VAL A 97  ? 0.4379 0.4256 0.4335 -0.0314 0.0451  -0.0322 98  VAL A N     
759   C CA    . VAL A 97  ? 0.4763 0.4642 0.4691 -0.0304 0.0456  -0.0320 98  VAL A CA    
760   C C     . VAL A 97  ? 0.4881 0.4742 0.4783 -0.0298 0.0467  -0.0313 98  VAL A C     
761   O O     . VAL A 97  ? 0.4792 0.4641 0.4681 -0.0294 0.0463  -0.0309 98  VAL A O     
762   C CB    . VAL A 97  ? 0.5072 0.4967 0.4991 -0.0300 0.0442  -0.0317 98  VAL A CB    
763   C CG1   . VAL A 97  ? 0.4997 0.4896 0.4888 -0.0290 0.0446  -0.0313 98  VAL A CG1   
764   C CG2   . VAL A 97  ? 0.4950 0.4859 0.4894 -0.0308 0.0429  -0.0322 98  VAL A CG2   
765   N N     . PHE A 98  ? 0.4781 0.4638 0.4673 -0.0297 0.0481  -0.0312 99  PHE A N     
766   C CA    . PHE A 98  ? 0.4357 0.4192 0.4224 -0.0294 0.0492  -0.0302 99  PHE A CA    
767   C C     . PHE A 98  ? 0.4388 0.4202 0.4264 -0.0302 0.0489  -0.0299 99  PHE A C     
768   O O     . PHE A 98  ? 0.3925 0.3716 0.3779 -0.0297 0.0487  -0.0293 99  PHE A O     
769   C CB    . PHE A 98  ? 0.4144 0.3977 0.3978 -0.0280 0.0488  -0.0297 99  PHE A CB    
770   C CG    . PHE A 98  ? 0.3964 0.3812 0.3782 -0.0274 0.0491  -0.0298 99  PHE A CG    
771   C CD1   . PHE A 98  ? 0.3746 0.3616 0.3575 -0.0274 0.0481  -0.0306 99  PHE A CD1   
772   C CD2   . PHE A 98  ? 0.3922 0.3760 0.3713 -0.0269 0.0502  -0.0291 99  PHE A CD2   
773   C CE1   . PHE A 98  ? 0.4029 0.3909 0.3841 -0.0269 0.0481  -0.0309 99  PHE A CE1   
774   C CE2   . PHE A 98  ? 0.4078 0.3929 0.3851 -0.0263 0.0504  -0.0293 99  PHE A CE2   
775   C CZ    . PHE A 98  ? 0.3827 0.3698 0.3610 -0.0263 0.0492  -0.0303 99  PHE A CZ    
776   N N     . ALA A 99  ? 0.4868 0.4691 0.4779 -0.0314 0.0486  -0.0304 100 ALA A N     
777   C CA    . ALA A 99  ? 0.5132 0.4936 0.5055 -0.0325 0.0481  -0.0302 100 ALA A CA    
778   C C     . ALA A 99  ? 0.5738 0.5555 0.5697 -0.0339 0.0488  -0.0302 100 ALA A C     
779   O O     . ALA A 99  ? 0.6454 0.6294 0.6442 -0.0342 0.0484  -0.0309 100 ALA A O     
780   C CB    . ALA A 99  ? 0.5287 0.5092 0.5213 -0.0323 0.0465  -0.0308 100 ALA A CB    
781   N N     . CYS A 100 ? 0.5345 0.5150 0.5305 -0.0349 0.0498  -0.0292 101 CYS A N     
782   C CA    . CYS A 100 ? 0.5125 0.4950 0.5121 -0.0362 0.0508  -0.0289 101 CYS A CA    
783   C C     . CYS A 100 ? 0.4703 0.4522 0.4728 -0.0378 0.0495  -0.0288 101 CYS A C     
784   O O     . CYS A 100 ? 0.4340 0.4186 0.4405 -0.0387 0.0497  -0.0289 101 CYS A O     
785   C CB    . CYS A 100 ? 0.5435 0.5255 0.5419 -0.0368 0.0525  -0.0274 101 CYS A CB    
786   S SG    . CYS A 100 ? 0.5975 0.5745 0.5934 -0.0380 0.0517  -0.0261 101 CYS A SG    
787   N N     . VAL A 101 ? 0.5280 0.5066 0.5285 -0.0380 0.0481  -0.0288 102 VAL A N     
788   C CA    . VAL A 101 ? 0.4791 0.4564 0.4815 -0.0396 0.0466  -0.0288 102 VAL A CA    
789   C C     . VAL A 101 ? 0.4310 0.4115 0.4372 -0.0398 0.0458  -0.0296 102 VAL A C     
790   O O     . VAL A 101 ? 0.4775 0.4596 0.4876 -0.0413 0.0456  -0.0292 102 VAL A O     
791   C CB    . VAL A 101 ? 0.5064 0.4796 0.5052 -0.0391 0.0449  -0.0292 102 VAL A CB    
792   C CG1   . VAL A 101 ? 0.4772 0.4490 0.4777 -0.0406 0.0430  -0.0295 102 VAL A CG1   
793   C CG2   . VAL A 101 ? 0.5526 0.5219 0.5478 -0.0388 0.0454  -0.0283 102 VAL A CG2   
794   N N     . SER A 102 ? 0.4072 0.3886 0.4124 -0.0384 0.0452  -0.0305 103 SER A N     
795   C CA    . SER A 102 ? 0.4657 0.4496 0.4741 -0.0385 0.0441  -0.0311 103 SER A CA    
796   C C     . SER A 102 ? 0.4431 0.4302 0.4554 -0.0387 0.0452  -0.0311 103 SER A C     
797   O O     . SER A 102 ? 0.4626 0.4514 0.4787 -0.0396 0.0446  -0.0311 103 SER A O     
798   C CB    . SER A 102 ? 0.5328 0.5170 0.5391 -0.0371 0.0434  -0.0317 103 SER A CB    
799   O OG    . SER A 102 ? 0.6161 0.5980 0.6190 -0.0367 0.0424  -0.0318 103 SER A OG    
800   N N     . HIS A 103 ? 0.4274 0.4154 0.4385 -0.0376 0.0469  -0.0312 104 HIS A N     
801   C CA    . HIS A 103 ? 0.3852 0.3764 0.3994 -0.0373 0.0483  -0.0314 104 HIS A CA    
802   C C     . HIS A 103 ? 0.3431 0.3357 0.3606 -0.0388 0.0490  -0.0305 104 HIS A C     
803   O O     . HIS A 103 ? 0.3009 0.2964 0.3227 -0.0390 0.0491  -0.0306 104 HIS A O     
804   C CB    . HIS A 103 ? 0.3869 0.3784 0.3983 -0.0359 0.0499  -0.0317 104 HIS A CB    
805   C CG    . HIS A 103 ? 0.3239 0.3148 0.3330 -0.0346 0.0490  -0.0326 104 HIS A CG    
806   N ND1   . HIS A 103 ? 0.3088 0.3010 0.3196 -0.0338 0.0483  -0.0337 104 HIS A ND1   
807   C CD2   . HIS A 103 ? 0.3176 0.3067 0.3229 -0.0340 0.0486  -0.0325 104 HIS A CD2   
808   C CE1   . HIS A 103 ? 0.3311 0.3224 0.3394 -0.0331 0.0474  -0.0341 104 HIS A CE1   
809   N NE2   . HIS A 103 ? 0.3267 0.3165 0.3318 -0.0332 0.0476  -0.0334 104 HIS A NE2   
810   N N     . MET A 104 ? 0.3297 0.3203 0.3453 -0.0399 0.0495  -0.0293 105 MET A N     
811   C CA    . MET A 104 ? 0.3734 0.3653 0.3921 -0.0418 0.0502  -0.0280 105 MET A CA    
812   C C     . MET A 104 ? 0.3643 0.3566 0.3866 -0.0432 0.0482  -0.0280 105 MET A C     
813   O O     . MET A 104 ? 0.3712 0.3670 0.3982 -0.0441 0.0486  -0.0275 105 MET A O     
814   C CB    . MET A 104 ? 0.4092 0.3978 0.4248 -0.0430 0.0506  -0.0266 105 MET A CB    
815   C CG    . MET A 104 ? 0.4396 0.4284 0.4523 -0.0420 0.0528  -0.0261 105 MET A CG    
816   S SD    . MET A 104 ? 0.5296 0.5136 0.5380 -0.0430 0.0528  -0.0244 105 MET A SD    
817   C CE    . MET A 104 ? 0.5358 0.5206 0.5483 -0.0462 0.0528  -0.0224 105 MET A CE    
818   N N     . ALA A 105 ? 0.3550 0.3441 0.3751 -0.0433 0.0461  -0.0286 106 ALA A N     
819   C CA    . ALA A 105 ? 0.3682 0.3571 0.3909 -0.0447 0.0439  -0.0287 106 ALA A CA    
820   C C     . ALA A 105 ? 0.3610 0.3538 0.3880 -0.0441 0.0436  -0.0292 106 ALA A C     
821   O O     . ALA A 105 ? 0.3697 0.3650 0.4012 -0.0454 0.0430  -0.0287 106 ALA A O     
822   C CB    . ALA A 105 ? 0.4002 0.3852 0.4188 -0.0444 0.0420  -0.0294 106 ALA A CB    
823   N N     . ILE A 106 ? 0.3702 0.3635 0.3960 -0.0422 0.0437  -0.0302 107 ILE A N     
824   C CA    . ILE A 106 ? 0.3491 0.3453 0.3785 -0.0413 0.0431  -0.0309 107 ILE A CA    
825   C C     . ILE A 106 ? 0.3519 0.3521 0.3856 -0.0412 0.0449  -0.0305 107 ILE A C     
826   O O     . ILE A 106 ? 0.3789 0.3818 0.4172 -0.0414 0.0441  -0.0304 107 ILE A O     
827   C CB    . ILE A 106 ? 0.3501 0.3455 0.3770 -0.0395 0.0430  -0.0319 107 ILE A CB    
828   C CG1   . ILE A 106 ? 0.3401 0.3329 0.3636 -0.0396 0.0412  -0.0320 107 ILE A CG1   
829   C CG2   . ILE A 106 ? 0.3641 0.3621 0.3946 -0.0384 0.0426  -0.0325 107 ILE A CG2   
830   C CD1   . ILE A 106 ? 0.3190 0.3114 0.3403 -0.0382 0.0408  -0.0326 107 ILE A CD1   
831   N N     . THR A 107 ? 0.3693 0.3701 0.4015 -0.0407 0.0473  -0.0302 108 THR A N     
832   C CA    . THR A 107 ? 0.3808 0.3858 0.4165 -0.0403 0.0494  -0.0299 108 THR A CA    
833   C C     . THR A 107 ? 0.3855 0.3930 0.4258 -0.0425 0.0490  -0.0284 108 THR A C     
834   O O     . THR A 107 ? 0.4020 0.4136 0.4473 -0.0421 0.0491  -0.0284 108 THR A O     
835   C CB    . THR A 107 ? 0.4098 0.4146 0.4422 -0.0398 0.0518  -0.0295 108 THR A CB    
836   O OG1   . THR A 107 ? 0.3996 0.4028 0.4285 -0.0377 0.0519  -0.0309 108 THR A OG1   
837   C CG2   . THR A 107 ? 0.4602 0.4699 0.4959 -0.0395 0.0543  -0.0288 108 THR A CG2   
838   N N     . ARG A 108 ? 0.3813 0.3861 0.4200 -0.0446 0.0483  -0.0273 109 ARG A N     
839   C CA    . ARG A 108 ? 0.3960 0.4025 0.4386 -0.0472 0.0477  -0.0257 109 ARG A CA    
840   C C     . ARG A 108 ? 0.3792 0.3865 0.4253 -0.0478 0.0451  -0.0261 109 ARG A C     
841   O O     . ARG A 108 ? 0.4078 0.4192 0.4593 -0.0489 0.0449  -0.0251 109 ARG A O     
842   C CB    . ARG A 108 ? 0.4240 0.4261 0.4631 -0.0493 0.0472  -0.0246 109 ARG A CB    
843   C CG    . ARG A 108 ? 0.4785 0.4822 0.5214 -0.0523 0.0468  -0.0227 109 ARG A CG    
844   C CD    . ARG A 108 ? 0.5247 0.5233 0.5636 -0.0542 0.0463  -0.0216 109 ARG A CD    
845   N NE    . ARG A 108 ? 0.5515 0.5492 0.5866 -0.0530 0.0488  -0.0212 109 ARG A NE    
846   C CZ    . ARG A 108 ? 0.5565 0.5500 0.5880 -0.0542 0.0489  -0.0200 109 ARG A CZ    
847   N NH1   . ARG A 108 ? 0.5592 0.5486 0.5902 -0.0566 0.0466  -0.0193 109 ARG A NH1   
848   N NH2   . ARG A 108 ? 0.5526 0.5456 0.5807 -0.0529 0.0510  -0.0197 109 ARG A NH2   
849   N N     . ALA A 109 ? 0.3625 0.3664 0.4056 -0.0471 0.0431  -0.0273 110 ALA A N     
850   C CA    . ALA A 109 ? 0.3781 0.3822 0.4236 -0.0476 0.0404  -0.0276 110 ALA A CA    
851   C C     . ALA A 109 ? 0.3790 0.3881 0.4299 -0.0462 0.0408  -0.0278 110 ALA A C     
852   O O     . ALA A 109 ? 0.3752 0.3870 0.4307 -0.0472 0.0394  -0.0272 110 ALA A O     
853   C CB    . ALA A 109 ? 0.4274 0.4274 0.4683 -0.0467 0.0387  -0.0287 110 ALA A CB    
854   N N     . LYS A 110 ? 0.4170 0.4271 0.4670 -0.0438 0.0425  -0.0288 111 LYS A N     
855   C CA    . LYS A 110 ? 0.4672 0.4812 0.5215 -0.0419 0.0429  -0.0294 111 LYS A CA    
856   C C     . LYS A 110 ? 0.4523 0.4718 0.5121 -0.0425 0.0446  -0.0282 111 LYS A C     
857   O O     . LYS A 110 ? 0.4153 0.4385 0.4804 -0.0420 0.0438  -0.0280 111 LYS A O     
858   C CB    . LYS A 110 ? 0.4596 0.4729 0.5112 -0.0392 0.0445  -0.0308 111 LYS A CB    
859   C CG    . LYS A 110 ? 0.4709 0.4799 0.5184 -0.0384 0.0427  -0.0318 111 LYS A CG    
860   C CD    . LYS A 110 ? 0.4960 0.5042 0.5408 -0.0361 0.0440  -0.0331 111 LYS A CD    
861   C CE    . LYS A 110 ? 0.5194 0.5241 0.5612 -0.0356 0.0420  -0.0338 111 LYS A CE    
862   N NZ    . LYS A 110 ? 0.5604 0.5657 0.6055 -0.0353 0.0397  -0.0339 111 LYS A NZ    
863   N N     . ALA A 111 ? 0.5124 0.5325 0.5709 -0.0435 0.0468  -0.0272 112 ALA A N     
864   C CA    . ALA A 111 ? 0.4877 0.5135 0.5511 -0.0441 0.0488  -0.0258 112 ALA A CA    
865   C C     . ALA A 111 ? 0.4713 0.4992 0.5396 -0.0468 0.0467  -0.0243 112 ALA A C     
866   O O     . ALA A 111 ? 0.4839 0.5179 0.5582 -0.0471 0.0476  -0.0232 112 ALA A O     
867   C CB    . ALA A 111 ? 0.4767 0.5020 0.5370 -0.0450 0.0512  -0.0248 112 ALA A CB    
868   N N     . GLU A 112 ? 0.4469 0.4701 0.5128 -0.0487 0.0439  -0.0243 113 GLU A N     
869   C CA    . GLU A 112 ? 0.4439 0.4681 0.5135 -0.0514 0.0415  -0.0231 113 GLU A CA    
870   C C     . GLU A 112 ? 0.4318 0.4567 0.5039 -0.0504 0.0389  -0.0239 113 GLU A C     
871   O O     . GLU A 112 ? 0.4224 0.4481 0.4975 -0.0524 0.0364  -0.0231 113 GLU A O     
872   C CB    . GLU A 112 ? 0.5340 0.5524 0.5991 -0.0541 0.0398  -0.0226 113 GLU A CB    
873   C CG    . GLU A 112 ? 0.5813 0.5987 0.6441 -0.0553 0.0421  -0.0214 113 GLU A CG    
874   C CD    . GLU A 112 ? 0.6196 0.6308 0.6780 -0.0577 0.0403  -0.0210 113 GLU A CD    
875   O OE1   . GLU A 112 ? 0.6516 0.6594 0.7087 -0.0586 0.0373  -0.0217 113 GLU A OE1   
876   O OE2   . GLU A 112 ? 0.5887 0.5983 0.6449 -0.0587 0.0419  -0.0199 113 GLU A OE2   
877   N N     . GLY A 113 ? 0.4076 0.4320 0.4783 -0.0474 0.0394  -0.0255 114 GLY A N     
878   C CA    . GLY A 113 ? 0.3935 0.4189 0.4669 -0.0460 0.0372  -0.0262 114 GLY A CA    
879   C C     . GLY A 113 ? 0.3772 0.3973 0.4464 -0.0468 0.0342  -0.0267 114 GLY A C     
880   O O     . GLY A 113 ? 0.3258 0.3465 0.3973 -0.0471 0.0317  -0.0266 114 GLY A O     
881   N N     . PHE A 114 ? 0.3384 0.3536 0.4012 -0.0471 0.0347  -0.0273 115 PHE A N     
882   C CA    . PHE A 114 ? 0.3655 0.3761 0.4238 -0.0475 0.0323  -0.0279 115 PHE A CA    
883   C C     . PHE A 114 ? 0.3891 0.3979 0.4442 -0.0451 0.0328  -0.0291 115 PHE A C     
884   O O     . PHE A 114 ? 0.3416 0.3508 0.3957 -0.0435 0.0351  -0.0296 115 PHE A O     
885   C CB    . PHE A 114 ? 0.3574 0.3638 0.4109 -0.0493 0.0320  -0.0278 115 PHE A CB    
886   C CG    . PHE A 114 ? 0.3415 0.3486 0.3975 -0.0521 0.0308  -0.0266 115 PHE A CG    
887   C CD1   . PHE A 114 ? 0.3173 0.3247 0.3754 -0.0536 0.0278  -0.0263 115 PHE A CD1   
888   C CD2   . PHE A 114 ? 0.3383 0.3454 0.3944 -0.0536 0.0325  -0.0257 115 PHE A CD2   
889   C CE1   . PHE A 114 ? 0.3468 0.3546 0.4072 -0.0564 0.0264  -0.0252 115 PHE A CE1   
890   C CE2   . PHE A 114 ? 0.3300 0.3375 0.3885 -0.0565 0.0312  -0.0245 115 PHE A CE2   
891   C CZ    . PHE A 114 ? 0.3260 0.3338 0.3867 -0.0580 0.0280  -0.0243 115 PHE A CZ    
892   N N     . SER A 115 ? 0.3668 0.3736 0.4202 -0.0449 0.0304  -0.0293 116 SER A N     
893   C CA    . SER A 115 ? 0.4773 0.4819 0.5272 -0.0432 0.0304  -0.0301 116 SER A CA    
894   C C     . SER A 115 ? 0.4332 0.4345 0.4773 -0.0434 0.0316  -0.0305 116 SER A C     
895   O O     . SER A 115 ? 0.4178 0.4169 0.4590 -0.0448 0.0308  -0.0303 116 SER A O     
896   C CB    . SER A 115 ? 0.5135 0.5171 0.5630 -0.0434 0.0275  -0.0298 116 SER A CB    
897   O OG    . SER A 115 ? 0.5704 0.5722 0.6169 -0.0421 0.0274  -0.0302 116 SER A OG    
898   N N     . ALA A 116 ? 0.3866 0.3875 0.4288 -0.0418 0.0335  -0.0311 117 ALA A N     
899   C CA    . ALA A 116 ? 0.3622 0.3604 0.3992 -0.0416 0.0348  -0.0314 117 ALA A CA    
900   C C     . ALA A 116 ? 0.3318 0.3295 0.3669 -0.0399 0.0354  -0.0321 117 ALA A C     
901   O O     . ALA A 116 ? 0.3043 0.3037 0.3420 -0.0386 0.0362  -0.0326 117 ALA A O     
902   C CB    . ALA A 116 ? 0.3683 0.3669 0.4053 -0.0422 0.0369  -0.0311 117 ALA A CB    
903   N N     . LYS A 117 ? 0.3240 0.3195 0.3547 -0.0398 0.0350  -0.0321 118 LYS A N     
904   C CA    . LYS A 117 ? 0.3430 0.3378 0.3717 -0.0385 0.0353  -0.0326 118 LYS A CA    
905   C C     . LYS A 117 ? 0.3099 0.3029 0.3336 -0.0385 0.0359  -0.0325 118 LYS A C     
906   O O     . LYS A 117 ? 0.3593 0.3512 0.3811 -0.0392 0.0357  -0.0322 118 LYS A O     
907   C CB    . LYS A 117 ? 0.3475 0.3425 0.3776 -0.0383 0.0331  -0.0324 118 LYS A CB    
908   C CG    . LYS A 117 ? 0.3522 0.3464 0.3805 -0.0394 0.0312  -0.0315 118 LYS A CG    
909   C CD    . LYS A 117 ? 0.3925 0.3869 0.4219 -0.0394 0.0290  -0.0310 118 LYS A CD    
910   C CE    . LYS A 117 ? 0.4067 0.4009 0.4341 -0.0404 0.0273  -0.0300 118 LYS A CE    
911   N NZ    . LYS A 117 ? 0.3783 0.3726 0.4067 -0.0405 0.0252  -0.0291 118 LYS A NZ    
912   N N     . MET A 118 ? 0.3225 0.3152 0.3443 -0.0375 0.0364  -0.0328 119 MET A N     
913   C CA    . MET A 118 ? 0.3586 0.3502 0.3761 -0.0372 0.0369  -0.0327 119 MET A CA    
914   C C     . MET A 118 ? 0.4129 0.4048 0.4294 -0.0370 0.0355  -0.0323 119 MET A C     
915   O O     . MET A 118 ? 0.4682 0.4603 0.4862 -0.0366 0.0350  -0.0326 119 MET A O     
916   C CB    . MET A 118 ? 0.3870 0.3784 0.4030 -0.0363 0.0390  -0.0331 119 MET A CB    
917   C CG    . MET A 118 ? 0.3976 0.3881 0.4094 -0.0358 0.0395  -0.0329 119 MET A CG    
918   S SD    . MET A 118 ? 0.4048 0.3950 0.4147 -0.0348 0.0417  -0.0334 119 MET A SD    
919   C CE    . MET A 118 ? 0.4410 0.4309 0.4522 -0.0355 0.0431  -0.0331 119 MET A CE    
920   N N     . GLU A 119 ? 0.3990 0.3907 0.4126 -0.0372 0.0349  -0.0317 120 GLU A N     
921   C CA    . GLU A 119 ? 0.3836 0.3762 0.3961 -0.0373 0.0338  -0.0309 120 GLU A CA    
922   C C     . GLU A 119 ? 0.3843 0.3770 0.3938 -0.0365 0.0349  -0.0309 120 GLU A C     
923   O O     . GLU A 119 ? 0.3727 0.3649 0.3797 -0.0359 0.0360  -0.0310 120 GLU A O     
924   C CB    . GLU A 119 ? 0.3787 0.3719 0.3902 -0.0379 0.0324  -0.0300 120 GLU A CB    
925   C CG    . GLU A 119 ? 0.4339 0.4272 0.4484 -0.0388 0.0308  -0.0298 120 GLU A CG    
926   C CD    . GLU A 119 ? 0.4936 0.4873 0.5107 -0.0391 0.0294  -0.0293 120 GLU A CD    
927   O OE1   . GLU A 119 ? 0.5131 0.5069 0.5295 -0.0389 0.0294  -0.0291 120 GLU A OE1   
928   O OE2   . GLU A 119 ? 0.5579 0.5516 0.5779 -0.0396 0.0280  -0.0291 120 GLU A OE2   
929   N N     . PRO A 120 ? 0.3363 0.3296 0.3458 -0.0364 0.0344  -0.0307 121 PRO A N     
930   C CA    . PRO A 120 ? 0.3449 0.3387 0.3518 -0.0357 0.0353  -0.0306 121 PRO A CA    
931   C C     . PRO A 120 ? 0.3395 0.3349 0.3439 -0.0356 0.0352  -0.0296 121 PRO A C     
932   O O     . PRO A 120 ? 0.2785 0.2751 0.2833 -0.0362 0.0340  -0.0287 121 PRO A O     
933   C CB    . PRO A 120 ? 0.3629 0.3567 0.3710 -0.0361 0.0342  -0.0307 121 PRO A CB    
934   C CG    . PRO A 120 ? 0.3781 0.3720 0.3888 -0.0371 0.0323  -0.0301 121 PRO A CG    
935   C CD    . PRO A 120 ? 0.3405 0.3337 0.3526 -0.0370 0.0328  -0.0305 121 PRO A CD    
936   N N     . GLY A 121 ? 0.3240 0.3195 0.3258 -0.0345 0.0364  -0.0297 122 GLY A N     
937   C CA    . GLY A 121 ? 0.3461 0.3435 0.3455 -0.0339 0.0366  -0.0288 122 GLY A CA    
938   C C     . GLY A 121 ? 0.3221 0.3211 0.3202 -0.0332 0.0369  -0.0284 122 GLY A C     
939   O O     . GLY A 121 ? 0.3238 0.3220 0.3226 -0.0335 0.0369  -0.0288 122 GLY A O     
940   N N     . ILE A 122 ? 0.3372 0.3386 0.3335 -0.0324 0.0371  -0.0275 123 ILE A N     
941   C CA    . ILE A 122 ? 0.3377 0.3413 0.3329 -0.0317 0.0373  -0.0268 123 ILE A CA    
942   C C     . ILE A 122 ? 0.3613 0.3629 0.3540 -0.0300 0.0388  -0.0276 123 ILE A C     
943   O O     . ILE A 122 ? 0.3929 0.3938 0.3837 -0.0287 0.0396  -0.0278 123 ILE A O     
944   C CB    . ILE A 122 ? 0.3797 0.3876 0.3744 -0.0315 0.0368  -0.0252 123 ILE A CB    
945   C CG1   . ILE A 122 ? 0.3754 0.3851 0.3726 -0.0335 0.0352  -0.0241 123 ILE A CG1   
946   C CG2   . ILE A 122 ? 0.3982 0.4090 0.3922 -0.0308 0.0370  -0.0244 123 ILE A CG2   
947   C CD1   . ILE A 122 ? 0.3516 0.3660 0.3484 -0.0334 0.0349  -0.0223 123 ILE A CD1   
948   N N     . SER A 123 ? 0.3338 0.3344 0.3264 -0.0300 0.0392  -0.0280 124 SER A N     
949   C CA    . SER A 123 ? 0.3571 0.3556 0.3474 -0.0286 0.0405  -0.0286 124 SER A CA    
950   C C     . SER A 123 ? 0.3829 0.3839 0.3713 -0.0272 0.0406  -0.0277 124 SER A C     
951   O O     . SER A 123 ? 0.4248 0.4296 0.4141 -0.0275 0.0397  -0.0266 124 SER A O     
952   C CB    . SER A 123 ? 0.3684 0.3648 0.3591 -0.0292 0.0409  -0.0294 124 SER A CB    
953   O OG    . SER A 123 ? 0.4179 0.4159 0.4089 -0.0297 0.0400  -0.0292 124 SER A OG    
954   N N     . ALA A 124 ? 0.3650 0.3642 0.3511 -0.0258 0.0417  -0.0279 125 ALA A N     
955   C CA    . ALA A 124 ? 0.3838 0.3851 0.3681 -0.0241 0.0418  -0.0270 125 ALA A CA    
956   C C     . ALA A 124 ? 0.3826 0.3863 0.3677 -0.0250 0.0409  -0.0265 125 ALA A C     
957   O O     . ALA A 124 ? 0.3648 0.3720 0.3496 -0.0243 0.0404  -0.0255 125 ALA A O     
958   C CB    . ALA A 124 ? 0.4087 0.4068 0.3903 -0.0225 0.0430  -0.0273 125 ALA A CB    
959   N N     . GLU A 125 ? 0.3910 0.3928 0.3771 -0.0265 0.0406  -0.0274 126 GLU A N     
960   C CA    . GLU A 125 ? 0.4240 0.4271 0.4105 -0.0275 0.0395  -0.0273 126 GLU A CA    
961   C C     . GLU A 125 ? 0.3918 0.3984 0.3807 -0.0288 0.0378  -0.0263 126 GLU A C     
962   O O     . GLU A 125 ? 0.3975 0.4071 0.3865 -0.0291 0.0366  -0.0253 126 GLU A O     
963   C CB    . GLU A 125 ? 0.4911 0.4910 0.4778 -0.0283 0.0397  -0.0287 126 GLU A CB    
964   C CG    . GLU A 125 ? 0.5292 0.5296 0.5159 -0.0292 0.0383  -0.0290 126 GLU A CG    
965   C CD    . GLU A 125 ? 0.6128 0.6103 0.5999 -0.0298 0.0385  -0.0306 126 GLU A CD    
966   O OE1   . GLU A 125 ? 0.6298 0.6252 0.6155 -0.0290 0.0401  -0.0314 126 GLU A OE1   
967   O OE2   . GLU A 125 ? 0.7049 0.7022 0.6937 -0.0310 0.0369  -0.0311 126 GLU A OE2   
968   N N     . ALA A 126 ? 0.3757 0.3819 0.3665 -0.0298 0.0375  -0.0264 127 ALA A N     
969   C CA    . ALA A 126 ? 0.3618 0.3711 0.3548 -0.0313 0.0359  -0.0252 127 ALA A CA    
970   C C     . ALA A 126 ? 0.3360 0.3500 0.3287 -0.0305 0.0359  -0.0235 127 ALA A C     
971   O O     . ALA A 126 ? 0.3318 0.3494 0.3260 -0.0317 0.0345  -0.0221 127 ALA A O     
972   C CB    . ALA A 126 ? 0.3802 0.3882 0.3747 -0.0321 0.0359  -0.0255 127 ALA A CB    
973   N N     . CYS A 127 ? 0.2994 0.3135 0.2902 -0.0283 0.0374  -0.0236 128 CYS A N     
974   C CA    . CYS A 127 ? 0.2971 0.3158 0.2875 -0.0268 0.0377  -0.0222 128 CYS A CA    
975   C C     . CYS A 127 ? 0.3224 0.3435 0.3123 -0.0263 0.0373  -0.0214 128 CYS A C     
976   O O     . CYS A 127 ? 0.3334 0.3599 0.3244 -0.0261 0.0367  -0.0198 128 CYS A O     
977   C CB    . CYS A 127 ? 0.3156 0.3327 0.3036 -0.0243 0.0393  -0.0230 128 CYS A CB    
978   S SG    . CYS A 127 ? 0.3858 0.4006 0.3741 -0.0248 0.0396  -0.0237 128 CYS A SG    
979   N N     . LEU A 128 ? 0.3494 0.3670 0.3379 -0.0261 0.0374  -0.0225 129 LEU A N     
980   C CA    . LEU A 128 ? 0.3634 0.3827 0.3509 -0.0254 0.0370  -0.0219 129 LEU A CA    
981   C C     . LEU A 128 ? 0.3406 0.3634 0.3303 -0.0277 0.0349  -0.0208 129 LEU A C     
982   O O     . LEU A 128 ? 0.3330 0.3607 0.3236 -0.0274 0.0341  -0.0192 129 LEU A O     
983   C CB    . LEU A 128 ? 0.3949 0.4093 0.3800 -0.0250 0.0376  -0.0234 129 LEU A CB    
984   C CG    . LEU A 128 ? 0.4261 0.4416 0.4095 -0.0241 0.0372  -0.0229 129 LEU A CG    
985   C CD1   . LEU A 128 ? 0.4562 0.4670 0.4370 -0.0235 0.0382  -0.0241 129 LEU A CD1   
986   C CD2   . LEU A 128 ? 0.4074 0.4256 0.3924 -0.0262 0.0350  -0.0223 129 LEU A CD2   
987   N N     . TRP A 129 ? 0.3457 0.3658 0.3365 -0.0299 0.0337  -0.0216 130 TRP A N     
988   C CA    . TRP A 129 ? 0.3279 0.3499 0.3205 -0.0323 0.0314  -0.0208 130 TRP A CA    
989   C C     . TRP A 129 ? 0.3353 0.3636 0.3304 -0.0331 0.0306  -0.0183 130 TRP A C     
990   O O     . TRP A 129 ? 0.2904 0.3225 0.2866 -0.0341 0.0290  -0.0168 130 TRP A O     
991   C CB    . TRP A 129 ? 0.3465 0.3644 0.3402 -0.0342 0.0304  -0.0220 130 TRP A CB    
992   C CG    . TRP A 129 ? 0.3708 0.3832 0.3623 -0.0334 0.0314  -0.0243 130 TRP A CG    
993   C CD1   . TRP A 129 ? 0.3918 0.4005 0.3837 -0.0335 0.0321  -0.0258 130 TRP A CD1   
994   C CD2   . TRP A 129 ? 0.3432 0.3540 0.3320 -0.0324 0.0317  -0.0253 130 TRP A CD2   
995   N NE1   . TRP A 129 ? 0.3982 0.4033 0.3879 -0.0326 0.0331  -0.0275 130 TRP A NE1   
996   C CE2   . TRP A 129 ? 0.3884 0.3946 0.3760 -0.0319 0.0329  -0.0272 130 TRP A CE2   
997   C CE3   . TRP A 129 ? 0.3529 0.3659 0.3402 -0.0318 0.0311  -0.0246 130 TRP A CE3   
998   C CZ2   . TRP A 129 ? 0.3619 0.3659 0.3467 -0.0308 0.0337  -0.0284 130 TRP A CZ2   
999   C CZ3   . TRP A 129 ? 0.3809 0.3912 0.3653 -0.0308 0.0317  -0.0258 130 TRP A CZ3   
1000  C CH2   . TRP A 129 ? 0.3367 0.3426 0.3197 -0.0303 0.0330  -0.0277 130 TRP A CH2   
1001  N N     . ALA A 130 ? 0.3201 0.3495 0.3160 -0.0326 0.0317  -0.0179 131 ALA A N     
1002  C CA    . ALA A 130 ? 0.3448 0.3803 0.3429 -0.0333 0.0312  -0.0155 131 ALA A CA    
1003  C C     . ALA A 130 ? 0.3553 0.3964 0.3530 -0.0311 0.0321  -0.0142 131 ALA A C     
1004  O O     . ALA A 130 ? 0.3575 0.4045 0.3574 -0.0321 0.0310  -0.0120 131 ALA A O     
1005  C CB    . ALA A 130 ? 0.3297 0.3645 0.3280 -0.0331 0.0322  -0.0157 131 ALA A CB    
1006  N N     . ASP A 131 ? 0.3839 0.4230 0.3790 -0.0280 0.0341  -0.0155 132 ASP A N     
1007  C CA    . ASP A 131 ? 0.3930 0.4367 0.3875 -0.0252 0.0351  -0.0145 132 ASP A CA    
1008  C C     . ASP A 131 ? 0.4240 0.4702 0.4189 -0.0256 0.0337  -0.0136 132 ASP A C     
1009  O O     . ASP A 131 ? 0.4247 0.4775 0.4212 -0.0248 0.0335  -0.0116 132 ASP A O     
1010  C CB    . ASP A 131 ? 0.4116 0.4512 0.4028 -0.0220 0.0371  -0.0162 132 ASP A CB    
1011  C CG    . ASP A 131 ? 0.4516 0.4895 0.4422 -0.0213 0.0383  -0.0170 132 ASP A CG    
1012  O OD1   . ASP A 131 ? 0.5831 0.6231 0.5756 -0.0233 0.0377  -0.0162 132 ASP A OD1   
1013  O OD2   . ASP A 131 ? 0.4956 0.5299 0.4835 -0.0188 0.0397  -0.0184 132 ASP A OD2   
1014  N N     . LEU A 132 ? 0.4221 0.4632 0.4157 -0.0266 0.0329  -0.0150 133 LEU A N     
1015  C CA    . LEU A 132 ? 0.4618 0.5046 0.4552 -0.0269 0.0314  -0.0144 133 LEU A CA    
1016  C C     . LEU A 132 ? 0.4757 0.5205 0.4718 -0.0305 0.0288  -0.0132 133 LEU A C     
1017  O O     . LEU A 132 ? 0.4811 0.5284 0.4776 -0.0314 0.0270  -0.0123 133 LEU A O     
1018  C CB    . LEU A 132 ? 0.4926 0.5291 0.4827 -0.0259 0.0319  -0.0164 133 LEU A CB    
1019  C CG    . LEU A 132 ? 0.5332 0.5677 0.5206 -0.0225 0.0341  -0.0170 133 LEU A CG    
1020  C CD1   . LEU A 132 ? 0.5497 0.5812 0.5366 -0.0216 0.0359  -0.0181 133 LEU A CD1   
1021  C CD2   . LEU A 132 ? 0.5792 0.6089 0.5635 -0.0219 0.0342  -0.0183 133 LEU A CD2   
1022  N N     . GLY A 133 ? 0.4530 0.4965 0.4506 -0.0327 0.0283  -0.0133 134 GLY A N     
1023  C CA    . GLY A 133 ? 0.5188 0.5631 0.5188 -0.0363 0.0255  -0.0123 134 GLY A CA    
1024  C C     . GLY A 133 ? 0.4997 0.5388 0.4979 -0.0374 0.0239  -0.0140 134 GLY A C     
1025  O O     . GLY A 133 ? 0.4526 0.4938 0.4517 -0.0392 0.0214  -0.0130 134 GLY A O     
1026  N N     . ILE A 134 ? 0.5029 0.5355 0.4984 -0.0362 0.0252  -0.0166 135 ILE A N     
1027  C CA    . ILE A 134 ? 0.4617 0.4892 0.4550 -0.0368 0.0240  -0.0186 135 ILE A CA    
1028  C C     . ILE A 134 ? 0.4318 0.4539 0.4252 -0.0381 0.0238  -0.0203 135 ILE A C     
1029  O O     . ILE A 134 ? 0.3917 0.4121 0.3853 -0.0371 0.0257  -0.0209 135 ILE A O     
1030  C CB    . ILE A 134 ? 0.4770 0.5022 0.4668 -0.0340 0.0260  -0.0199 135 ILE A CB    
1031  C CG1   . ILE A 134 ? 0.5032 0.5336 0.4928 -0.0325 0.0261  -0.0182 135 ILE A CG1   
1032  C CG2   . ILE A 134 ? 0.5029 0.5230 0.4900 -0.0345 0.0251  -0.0221 135 ILE A CG2   
1033  C CD1   . ILE A 134 ? 0.5406 0.5686 0.5267 -0.0297 0.0278  -0.0192 135 ILE A CD1   
1034  N N     . ASP A 135 ? 0.4785 0.4979 0.4720 -0.0401 0.0212  -0.0211 136 ASP A N     
1035  C CA    . ASP A 135 ? 0.5277 0.5416 0.5211 -0.0410 0.0207  -0.0229 136 ASP A CA    
1036  C C     . ASP A 135 ? 0.5236 0.5326 0.5135 -0.0393 0.0217  -0.0257 136 ASP A C     
1037  O O     . ASP A 135 ? 0.5258 0.5339 0.5135 -0.0394 0.0205  -0.0264 136 ASP A O     
1038  C CB    . ASP A 135 ? 0.5499 0.5631 0.5453 -0.0441 0.0172  -0.0222 136 ASP A CB    
1039  C CG    . ASP A 135 ? 0.5221 0.5295 0.5176 -0.0448 0.0164  -0.0241 136 ASP A CG    
1040  O OD1   . ASP A 135 ? 0.5553 0.5596 0.5496 -0.0428 0.0187  -0.0260 136 ASP A OD1   
1041  O OD2   . ASP A 135 ? 0.5499 0.5561 0.5471 -0.0473 0.0134  -0.0234 136 ASP A OD2   
1042  N N     . PRO A 136 ? 0.4865 0.4923 0.4758 -0.0378 0.0241  -0.0273 137 PRO A N     
1043  C CA    . PRO A 136 ? 0.4485 0.4504 0.4346 -0.0362 0.0254  -0.0297 137 PRO A CA    
1044  C C     . PRO A 136 ? 0.4523 0.4503 0.4371 -0.0371 0.0232  -0.0315 137 PRO A C     
1045  O O     . PRO A 136 ? 0.4688 0.4644 0.4502 -0.0359 0.0237  -0.0333 137 PRO A O     
1046  C CB    . PRO A 136 ? 0.4459 0.4459 0.4328 -0.0351 0.0279  -0.0304 137 PRO A CB    
1047  C CG    . PRO A 136 ? 0.4327 0.4342 0.4232 -0.0367 0.0268  -0.0291 137 PRO A CG    
1048  C CD    . PRO A 136 ? 0.4571 0.4633 0.4486 -0.0378 0.0254  -0.0267 137 PRO A CD    
1049  N N     . GLY A 137 ? 0.4510 0.4482 0.4381 -0.0392 0.0206  -0.0311 138 GLY A N     
1050  C CA    . GLY A 137 ? 0.5189 0.5118 0.5048 -0.0402 0.0180  -0.0330 138 GLY A CA    
1051  C C     . GLY A 137 ? 0.4885 0.4823 0.4727 -0.0414 0.0153  -0.0326 138 GLY A C     
1052  O O     . GLY A 137 ? 0.5475 0.5373 0.5293 -0.0417 0.0132  -0.0345 138 GLY A O     
1053  N N     . ASN A 138 ? 0.4742 0.4733 0.4595 -0.0420 0.0153  -0.0300 139 ASN A N     
1054  C CA    . ASN A 138 ? 0.4843 0.4855 0.4688 -0.0434 0.0125  -0.0291 139 ASN A CA    
1055  C C     . ASN A 138 ? 0.4117 0.4094 0.3915 -0.0420 0.0123  -0.0316 139 ASN A C     
1056  O O     . ASN A 138 ? 0.3763 0.3712 0.3544 -0.0434 0.0092  -0.0327 139 ASN A O     
1057  C CB    . ASN A 138 ? 0.5089 0.5169 0.4951 -0.0433 0.0133  -0.0262 139 ASN A CB    
1058  C CG    . ASN A 138 ? 0.5322 0.5430 0.5185 -0.0452 0.0101  -0.0248 139 ASN A CG    
1059  O OD1   . ASN A 138 ? 0.5728 0.5836 0.5612 -0.0481 0.0069  -0.0239 139 ASN A OD1   
1060  N ND2   . ASN A 138 ? 0.5240 0.5374 0.5082 -0.0437 0.0108  -0.0245 139 ASN A ND2   
1061  N N     . SER A 139 ? 0.4039 0.4015 0.3812 -0.0394 0.0156  -0.0325 140 SER A N     
1062  C CA    . SER A 139 ? 0.4252 0.4199 0.3977 -0.0378 0.0159  -0.0347 140 SER A CA    
1063  C C     . SER A 139 ? 0.3966 0.3890 0.3674 -0.0353 0.0196  -0.0363 140 SER A C     
1064  O O     . SER A 139 ? 0.4514 0.4428 0.4183 -0.0336 0.0210  -0.0375 140 SER A O     
1065  C CB    . SER A 139 ? 0.4232 0.4214 0.3938 -0.0374 0.0155  -0.0333 140 SER A CB    
1066  O OG    . SER A 139 ? 0.3980 0.3999 0.3696 -0.0359 0.0184  -0.0315 140 SER A OG    
1067  N N     . GLY A 140 ? 0.3783 0.3702 0.3522 -0.0353 0.0211  -0.0362 141 GLY A N     
1068  C CA    . GLY A 140 ? 0.4044 0.3944 0.3775 -0.0333 0.0243  -0.0376 141 GLY A CA    
1069  C C     . GLY A 140 ? 0.3889 0.3819 0.3626 -0.0321 0.0273  -0.0359 141 GLY A C     
1070  O O     . GLY A 140 ? 0.3595 0.3558 0.3333 -0.0322 0.0270  -0.0339 141 GLY A O     
1071  N N     . HIS A 141 ? 0.4256 0.4173 0.3996 -0.0309 0.0300  -0.0366 142 HIS A N     
1072  C CA    . HIS A 141 ? 0.3777 0.3713 0.3526 -0.0299 0.0326  -0.0351 142 HIS A CA    
1073  C C     . HIS A 141 ? 0.3766 0.3684 0.3496 -0.0284 0.0354  -0.0362 142 HIS A C     
1074  O O     . HIS A 141 ? 0.3608 0.3504 0.3338 -0.0281 0.0359  -0.0380 142 HIS A O     
1075  C CB    . HIS A 141 ? 0.4078 0.4025 0.3868 -0.0309 0.0325  -0.0341 142 HIS A CB    
1076  C CG    . HIS A 141 ? 0.4132 0.4084 0.3932 -0.0299 0.0351  -0.0334 142 HIS A CG    
1077  N ND1   . HIS A 141 ? 0.4171 0.4118 0.4000 -0.0304 0.0356  -0.0335 142 HIS A ND1   
1078  C CD2   . HIS A 141 ? 0.3956 0.3913 0.3738 -0.0286 0.0370  -0.0327 142 HIS A CD2   
1079  C CE1   . HIS A 141 ? 0.4247 0.4196 0.4075 -0.0295 0.0377  -0.0329 142 HIS A CE1   
1080  N NE2   . HIS A 141 ? 0.3933 0.3887 0.3734 -0.0284 0.0386  -0.0324 142 HIS A NE2   
1081  N N     . GLN A 142 ? 0.3468 0.3396 0.3181 -0.0273 0.0372  -0.0350 143 GLN A N     
1082  C CA    . GLN A 142 ? 0.3583 0.3498 0.3280 -0.0262 0.0400  -0.0354 143 GLN A CA    
1083  C C     . GLN A 142 ? 0.3027 0.2951 0.2736 -0.0258 0.0416  -0.0336 143 GLN A C     
1084  O O     . GLN A 142 ? 0.2828 0.2768 0.2535 -0.0256 0.0410  -0.0321 143 GLN A O     
1085  C CB    . GLN A 142 ? 0.3740 0.3651 0.3392 -0.0252 0.0405  -0.0357 143 GLN A CB    
1086  C CG    . GLN A 142 ? 0.4537 0.4434 0.4167 -0.0252 0.0390  -0.0378 143 GLN A CG    
1087  C CD    . GLN A 142 ? 0.4487 0.4380 0.4067 -0.0241 0.0396  -0.0381 143 GLN A CD    
1088  O OE1   . GLN A 142 ? 0.4980 0.4860 0.4536 -0.0233 0.0408  -0.0398 143 GLN A OE1   
1089  N NE2   . GLN A 142 ? 0.4341 0.4249 0.3904 -0.0241 0.0387  -0.0365 143 GLN A NE2   
1090  N N     . SER A 143 ? 0.3188 0.3100 0.2910 -0.0257 0.0436  -0.0339 144 SER A N     
1091  C CA    . SER A 143 ? 0.3108 0.3020 0.2838 -0.0254 0.0450  -0.0325 144 SER A CA    
1092  C C     . SER A 143 ? 0.3411 0.3309 0.3125 -0.0249 0.0474  -0.0324 144 SER A C     
1093  O O     . SER A 143 ? 0.3999 0.3893 0.3719 -0.0251 0.0484  -0.0335 144 SER A O     
1094  C CB    . SER A 143 ? 0.2906 0.2820 0.2673 -0.0262 0.0447  -0.0325 144 SER A CB    
1095  O OG    . SER A 143 ? 0.2902 0.2834 0.2682 -0.0266 0.0428  -0.0318 144 SER A OG    
1096  N N     . PHE A 144 ? 0.3270 0.3162 0.2963 -0.0243 0.0482  -0.0308 145 PHE A N     
1097  C CA    . PHE A 144 ? 0.3621 0.3500 0.3301 -0.0242 0.0504  -0.0302 145 PHE A CA    
1098  C C     . PHE A 144 ? 0.3330 0.3195 0.3012 -0.0240 0.0508  -0.0286 145 PHE A C     
1099  O O     . PHE A 144 ? 0.3292 0.3159 0.2968 -0.0233 0.0496  -0.0278 145 PHE A O     
1100  C CB    . PHE A 144 ? 0.3418 0.3297 0.3057 -0.0234 0.0510  -0.0298 145 PHE A CB    
1101  C CG    . PHE A 144 ? 0.3423 0.3311 0.3048 -0.0232 0.0506  -0.0316 145 PHE A CG    
1102  C CD1   . PHE A 144 ? 0.3534 0.3423 0.3166 -0.0233 0.0520  -0.0329 145 PHE A CD1   
1103  C CD2   . PHE A 144 ? 0.3664 0.3558 0.3269 -0.0229 0.0486  -0.0321 145 PHE A CD2   
1104  C CE1   . PHE A 144 ? 0.3779 0.3671 0.3395 -0.0228 0.0515  -0.0348 145 PHE A CE1   
1105  C CE2   . PHE A 144 ? 0.3842 0.3738 0.3432 -0.0227 0.0478  -0.0339 145 PHE A CE2   
1106  C CZ    . PHE A 144 ? 0.3928 0.3820 0.3521 -0.0226 0.0493  -0.0354 145 PHE A CZ    
1107  N N     . GLU A 145 ? 0.3467 0.3318 0.3158 -0.0247 0.0523  -0.0280 146 GLU A N     
1108  C CA    . GLU A 145 ? 0.3882 0.3710 0.3567 -0.0246 0.0527  -0.0265 146 GLU A CA    
1109  C C     . GLU A 145 ? 0.3914 0.3733 0.3557 -0.0237 0.0531  -0.0251 146 GLU A C     
1110  O O     . GLU A 145 ? 0.3825 0.3651 0.3450 -0.0238 0.0542  -0.0250 146 GLU A O     
1111  C CB    . GLU A 145 ? 0.4444 0.4262 0.4152 -0.0260 0.0540  -0.0262 146 GLU A CB    
1112  C CG    . GLU A 145 ? 0.4991 0.4778 0.4699 -0.0262 0.0537  -0.0250 146 GLU A CG    
1113  C CD    . GLU A 145 ? 0.5446 0.5208 0.5119 -0.0258 0.0543  -0.0232 146 GLU A CD    
1114  O OE1   . GLU A 145 ? 0.6275 0.6048 0.5924 -0.0254 0.0551  -0.0226 146 GLU A OE1   
1115  O OE2   . GLU A 145 ? 0.5945 0.5674 0.5614 -0.0259 0.0539  -0.0222 146 GLU A OE2   
1116  N N     . ALA A 146 ? 0.4474 0.4278 0.4102 -0.0226 0.0522  -0.0240 147 ALA A N     
1117  C CA    . ALA A 146 ? 0.4411 0.4210 0.4002 -0.0214 0.0520  -0.0227 147 ALA A CA    
1118  C C     . ALA A 146 ? 0.4721 0.4501 0.4289 -0.0221 0.0537  -0.0212 147 ALA A C     
1119  O O     . ALA A 146 ? 0.4781 0.4569 0.4318 -0.0216 0.0540  -0.0206 147 ALA A O     
1120  C CB    . ALA A 146 ? 0.4178 0.3962 0.3761 -0.0199 0.0508  -0.0218 147 ALA A CB    
1121  N N     . SER A 147 ? 0.4816 0.4575 0.4400 -0.0233 0.0546  -0.0206 148 SER A N     
1122  C CA    . SER A 147 ? 0.4786 0.4527 0.4352 -0.0242 0.0561  -0.0187 148 SER A CA    
1123  C C     . SER A 147 ? 0.4688 0.4460 0.4259 -0.0252 0.0578  -0.0193 148 SER A C     
1124  O O     . SER A 147 ? 0.4560 0.4334 0.4104 -0.0254 0.0591  -0.0179 148 SER A O     
1125  C CB    . SER A 147 ? 0.5208 0.4916 0.4791 -0.0254 0.0562  -0.0177 148 SER A CB    
1126  O OG    . SER A 147 ? 0.5417 0.5092 0.4986 -0.0242 0.0547  -0.0171 148 SER A OG    
1127  N N     . GLN A 148 ? 0.4469 0.4264 0.4073 -0.0256 0.0578  -0.0213 149 GLN A N     
1128  C CA    . GLN A 148 ? 0.4787 0.4611 0.4397 -0.0260 0.0594  -0.0223 149 GLN A CA    
1129  C C     . GLN A 148 ? 0.4756 0.4595 0.4329 -0.0247 0.0592  -0.0230 149 GLN A C     
1130  O O     . GLN A 148 ? 0.5051 0.4908 0.4608 -0.0247 0.0607  -0.0231 149 GLN A O     
1131  C CB    . GLN A 148 ? 0.4694 0.4534 0.4348 -0.0265 0.0591  -0.0243 149 GLN A CB    
1132  C CG    . GLN A 148 ? 0.4885 0.4754 0.4549 -0.0267 0.0608  -0.0254 149 GLN A CG    
1133  C CD    . GLN A 148 ? 0.5170 0.5052 0.4874 -0.0268 0.0601  -0.0275 149 GLN A CD    
1134  O OE1   . GLN A 148 ? 0.4907 0.4803 0.4609 -0.0259 0.0596  -0.0295 149 GLN A OE1   
1135  N NE2   . GLN A 148 ? 0.4802 0.4679 0.4544 -0.0280 0.0599  -0.0272 149 GLN A NE2   
1136  N N     . PHE A 149 ? 0.4333 0.4168 0.3894 -0.0236 0.0572  -0.0234 150 PHE A N     
1137  C CA    . PHE A 149 ? 0.4193 0.4041 0.3720 -0.0226 0.0564  -0.0242 150 PHE A CA    
1138  C C     . PHE A 149 ? 0.4236 0.4076 0.3718 -0.0221 0.0571  -0.0221 150 PHE A C     
1139  O O     . PHE A 149 ? 0.4094 0.3944 0.3541 -0.0213 0.0568  -0.0225 150 PHE A O     
1140  C CB    . PHE A 149 ? 0.3935 0.3786 0.3468 -0.0218 0.0539  -0.0249 150 PHE A CB    
1141  C CG    . PHE A 149 ? 0.4264 0.4129 0.3766 -0.0210 0.0526  -0.0256 150 PHE A CG    
1142  C CD1   . PHE A 149 ? 0.4364 0.4243 0.3871 -0.0211 0.0519  -0.0278 150 PHE A CD1   
1143  C CD2   . PHE A 149 ? 0.4247 0.4108 0.3712 -0.0200 0.0520  -0.0240 150 PHE A CD2   
1144  C CE1   . PHE A 149 ? 0.4245 0.4133 0.3720 -0.0205 0.0504  -0.0286 150 PHE A CE1   
1145  C CE2   . PHE A 149 ? 0.4549 0.4424 0.3985 -0.0194 0.0505  -0.0246 150 PHE A CE2   
1146  C CZ    . PHE A 149 ? 0.4186 0.4073 0.3626 -0.0197 0.0497  -0.0269 150 PHE A CZ    
1147  N N     . MET A 150 ? 0.4581 0.4398 0.4062 -0.0227 0.0580  -0.0199 151 MET A N     
1148  C CA    . MET A 150 ? 0.4749 0.4553 0.4188 -0.0224 0.0586  -0.0175 151 MET A CA    
1149  C C     . MET A 150 ? 0.5352 0.5162 0.4787 -0.0237 0.0611  -0.0162 151 MET A C     
1150  O O     . MET A 150 ? 0.6032 0.5848 0.5428 -0.0235 0.0621  -0.0148 151 MET A O     
1151  C CB    . MET A 150 ? 0.4958 0.4727 0.4394 -0.0220 0.0574  -0.0156 151 MET A CB    
1152  C CG    . MET A 150 ? 0.4873 0.4643 0.4305 -0.0203 0.0551  -0.0162 151 MET A CG    
1153  S SD    . MET A 150 ? 0.5195 0.4924 0.4621 -0.0192 0.0539  -0.0142 151 MET A SD    
1154  C CE    . MET A 150 ? 0.5529 0.5235 0.4904 -0.0190 0.0545  -0.0111 151 MET A CE    
1155  N N     . PHE A 151 ? 0.4876 0.4688 0.4353 -0.0251 0.0621  -0.0165 152 PHE A N     
1156  C CA    . PHE A 151 ? 0.4996 0.4818 0.4479 -0.0266 0.0645  -0.0149 152 PHE A CA    
1157  C C     . PHE A 151 ? 0.5072 0.4936 0.4555 -0.0263 0.0662  -0.0166 152 PHE A C     
1158  O O     . PHE A 151 ? 0.4553 0.4437 0.4025 -0.0269 0.0685  -0.0152 152 PHE A O     
1159  C CB    . PHE A 151 ? 0.5102 0.4908 0.4630 -0.0283 0.0645  -0.0143 152 PHE A CB    
1160  C CG    . PHE A 151 ? 0.5108 0.4867 0.4632 -0.0285 0.0628  -0.0127 152 PHE A CG    
1161  C CD1   . PHE A 151 ? 0.5295 0.5028 0.4776 -0.0275 0.0620  -0.0109 152 PHE A CD1   
1162  C CD2   . PHE A 151 ? 0.5322 0.5060 0.4882 -0.0294 0.0619  -0.0131 152 PHE A CD2   
1163  C CE1   . PHE A 151 ? 0.5825 0.5512 0.5301 -0.0273 0.0604  -0.0096 152 PHE A CE1   
1164  C CE2   . PHE A 151 ? 0.4932 0.4623 0.4484 -0.0292 0.0603  -0.0120 152 PHE A CE2   
1165  C CZ    . PHE A 151 ? 0.5345 0.5010 0.4855 -0.0281 0.0596  -0.0103 152 PHE A CZ    
1166  N N     . PHE A 152 ? 0.4943 0.4820 0.4440 -0.0252 0.0652  -0.0196 153 PHE A N     
1167  C CA    . PHE A 152 ? 0.4936 0.4846 0.4435 -0.0246 0.0665  -0.0217 153 PHE A CA    
1168  C C     . PHE A 152 ? 0.4611 0.4524 0.4072 -0.0229 0.0651  -0.0237 153 PHE A C     
1169  O O     . PHE A 152 ? 0.4482 0.4376 0.3920 -0.0224 0.0632  -0.0232 153 PHE A O     
1170  C CB    . PHE A 152 ? 0.4979 0.4898 0.4534 -0.0251 0.0664  -0.0235 153 PHE A CB    
1171  C CG    . PHE A 152 ? 0.5547 0.5467 0.5141 -0.0270 0.0677  -0.0216 153 PHE A CG    
1172  C CD1   . PHE A 152 ? 0.5833 0.5785 0.5437 -0.0276 0.0703  -0.0206 153 PHE A CD1   
1173  C CD2   . PHE A 152 ? 0.6339 0.6231 0.5960 -0.0281 0.0661  -0.0208 153 PHE A CD2   
1174  C CE1   . PHE A 152 ? 0.6338 0.6293 0.5980 -0.0296 0.0713  -0.0187 153 PHE A CE1   
1175  C CE2   . PHE A 152 ? 0.6051 0.5940 0.5705 -0.0299 0.0670  -0.0192 153 PHE A CE2   
1176  C CZ    . PHE A 152 ? 0.6290 0.6211 0.5957 -0.0309 0.0694  -0.0181 153 PHE A CZ    
1177  N N     . ASN A 153 ? 0.4461 0.4397 0.3914 -0.0220 0.0661  -0.0259 154 ASN A N     
1178  C CA    . ASN A 153 ? 0.4675 0.4612 0.4086 -0.0204 0.0648  -0.0279 154 ASN A CA    
1179  C C     . ASN A 153 ? 0.4580 0.4509 0.4019 -0.0201 0.0624  -0.0306 154 ASN A C     
1180  O O     . ASN A 153 ? 0.4557 0.4496 0.4021 -0.0198 0.0629  -0.0327 154 ASN A O     
1181  C CB    . ASN A 153 ? 0.4998 0.4961 0.4376 -0.0193 0.0671  -0.0288 154 ASN A CB    
1182  C CG    . ASN A 153 ? 0.5017 0.4991 0.4364 -0.0198 0.0694  -0.0257 154 ASN A CG    
1183  O OD1   . ASN A 153 ? 0.5171 0.5129 0.4481 -0.0199 0.0685  -0.0238 154 ASN A OD1   
1184  N ND2   . ASN A 153 ? 0.5407 0.5409 0.4769 -0.0202 0.0724  -0.0249 154 ASN A ND2   
1185  N N     . HIS A 154 ? 0.4259 0.4171 0.3692 -0.0202 0.0598  -0.0304 155 HIS A N     
1186  C CA    . HIS A 154 ? 0.4150 0.4056 0.3606 -0.0202 0.0572  -0.0325 155 HIS A CA    
1187  C C     . HIS A 154 ? 0.4141 0.4042 0.3556 -0.0195 0.0549  -0.0331 155 HIS A C     
1188  O O     . HIS A 154 ? 0.3933 0.3830 0.3323 -0.0194 0.0543  -0.0312 155 HIS A O     
1189  C CB    . HIS A 154 ? 0.4069 0.3966 0.3570 -0.0212 0.0562  -0.0315 155 HIS A CB    
1190  C CG    . HIS A 154 ? 0.3909 0.3810 0.3456 -0.0220 0.0576  -0.0316 155 HIS A CG    
1191  N ND1   . HIS A 154 ? 0.3919 0.3830 0.3487 -0.0218 0.0582  -0.0337 155 HIS A ND1   
1192  C CD2   . HIS A 154 ? 0.3892 0.3786 0.3468 -0.0230 0.0583  -0.0299 155 HIS A CD2   
1193  C CE1   . HIS A 154 ? 0.4121 0.4036 0.3731 -0.0226 0.0592  -0.0331 155 HIS A CE1   
1194  N NE2   . HIS A 154 ? 0.3807 0.3711 0.3423 -0.0235 0.0593  -0.0309 155 HIS A NE2   
1195  N N     . VAL A 155 ? 0.4498 0.4397 0.3906 -0.0190 0.0534  -0.0358 156 VAL A N     
1196  C CA    . VAL A 155 ? 0.4706 0.4600 0.4079 -0.0187 0.0507  -0.0366 156 VAL A CA    
1197  C C     . VAL A 155 ? 0.5263 0.5152 0.4672 -0.0196 0.0478  -0.0376 156 VAL A C     
1198  O O     . VAL A 155 ? 0.5911 0.5793 0.5343 -0.0197 0.0473  -0.0397 156 VAL A O     
1199  C CB    . VAL A 155 ? 0.4729 0.4621 0.4054 -0.0175 0.0510  -0.0390 156 VAL A CB    
1200  C CG1   . VAL A 155 ? 0.4428 0.4311 0.3718 -0.0174 0.0477  -0.0401 156 VAL A CG1   
1201  C CG2   . VAL A 155 ? 0.4813 0.4716 0.4099 -0.0167 0.0540  -0.0377 156 VAL A CG2   
1202  N N     . PRO A 156 ? 0.5053 0.4946 0.4470 -0.0201 0.0459  -0.0359 157 PRO A N     
1203  C CA    . PRO A 156 ? 0.4996 0.4891 0.4449 -0.0211 0.0432  -0.0364 157 PRO A CA    
1204  C C     . PRO A 156 ? 0.5102 0.4993 0.4533 -0.0214 0.0402  -0.0381 157 PRO A C     
1205  O O     . PRO A 156 ? 0.4671 0.4560 0.4054 -0.0208 0.0397  -0.0384 157 PRO A O     
1206  C CB    . PRO A 156 ? 0.4974 0.4883 0.4440 -0.0213 0.0429  -0.0337 157 PRO A CB    
1207  C CG    . PRO A 156 ? 0.5200 0.5109 0.4617 -0.0203 0.0436  -0.0324 157 PRO A CG    
1208  C CD    . PRO A 156 ? 0.4925 0.4825 0.4318 -0.0197 0.0462  -0.0334 157 PRO A CD    
1209  N N     . ASP A 157 ? 0.4815 0.4702 0.4280 -0.0225 0.0381  -0.0391 158 ASP A N     
1210  C CA    . ASP A 157 ? 0.5357 0.5238 0.4809 -0.0233 0.0347  -0.0404 158 ASP A CA    
1211  C C     . ASP A 157 ? 0.5207 0.5113 0.4674 -0.0243 0.0326  -0.0381 158 ASP A C     
1212  O O     . ASP A 157 ? 0.5210 0.5131 0.4722 -0.0252 0.0321  -0.0369 158 ASP A O     
1213  C CB    . ASP A 157 ? 0.5207 0.5069 0.4687 -0.0241 0.0333  -0.0424 158 ASP A CB    
1214  C CG    . ASP A 157 ? 0.5266 0.5116 0.4738 -0.0254 0.0293  -0.0436 158 ASP A CG    
1215  O OD1   . ASP A 157 ? 0.5468 0.5331 0.4917 -0.0258 0.0275  -0.0426 158 ASP A OD1   
1216  O OD2   . ASP A 157 ? 0.5712 0.5538 0.5200 -0.0260 0.0279  -0.0453 158 ASP A OD2   
1217  N N     . PRO A 158 ? 0.5863 0.5778 0.5293 -0.0239 0.0313  -0.0375 159 PRO A N     
1218  C CA    . PRO A 158 ? 0.6186 0.6132 0.5630 -0.0244 0.0295  -0.0350 159 PRO A CA    
1219  C C     . PRO A 158 ? 0.5986 0.5946 0.5463 -0.0264 0.0261  -0.0349 159 PRO A C     
1220  O O     . PRO A 158 ? 0.5892 0.5885 0.5384 -0.0268 0.0245  -0.0330 159 PRO A O     
1221  C CB    . PRO A 158 ? 0.6639 0.6587 0.6029 -0.0235 0.0290  -0.0347 159 PRO A CB    
1222  C CG    . PRO A 158 ? 0.6702 0.6618 0.6050 -0.0233 0.0287  -0.0377 159 PRO A CG    
1223  C CD    . PRO A 158 ? 0.6389 0.6287 0.5760 -0.0229 0.0313  -0.0390 159 PRO A CD    
1224  N N     . THR A 159 ? 0.5662 0.5598 0.5154 -0.0274 0.0251  -0.0369 160 THR A N     
1225  C CA    . THR A 159 ? 0.5733 0.5678 0.5256 -0.0296 0.0218  -0.0367 160 THR A CA    
1226  C C     . THR A 159 ? 0.5521 0.5479 0.5099 -0.0304 0.0227  -0.0356 160 THR A C     
1227  O O     . THR A 159 ? 0.5945 0.5918 0.5558 -0.0323 0.0203  -0.0348 160 THR A O     
1228  C CB    . THR A 159 ? 0.5759 0.5663 0.5259 -0.0304 0.0194  -0.0396 160 THR A CB    
1229  O OG1   . THR A 159 ? 0.5450 0.5325 0.4954 -0.0294 0.0218  -0.0414 160 THR A OG1   
1230  C CG2   . THR A 159 ? 0.6006 0.5896 0.5446 -0.0295 0.0184  -0.0410 160 THR A CG2   
1231  N N     . THR A 160 ? 0.5450 0.5403 0.5036 -0.0290 0.0261  -0.0355 161 THR A N     
1232  C CA    . THR A 160 ? 0.5108 0.5069 0.4740 -0.0296 0.0271  -0.0348 161 THR A CA    
1233  C C     . THR A 160 ? 0.5184 0.5179 0.4834 -0.0288 0.0286  -0.0323 161 THR A C     
1234  O O     . THR A 160 ? 0.5281 0.5289 0.4907 -0.0276 0.0292  -0.0313 161 THR A O     
1235  C CB    . THR A 160 ? 0.4571 0.4500 0.4202 -0.0287 0.0295  -0.0366 161 THR A CB    
1236  O OG1   . THR A 160 ? 0.5284 0.5216 0.4897 -0.0271 0.0324  -0.0359 161 THR A OG1   
1237  C CG2   . THR A 160 ? 0.4939 0.4832 0.4540 -0.0285 0.0285  -0.0394 161 THR A CG2   
1238  N N     . HIS A 161 ? 0.4905 0.4912 0.4595 -0.0294 0.0291  -0.0314 162 HIS A N     
1239  C CA    . HIS A 161 ? 0.4734 0.4766 0.4439 -0.0283 0.0309  -0.0295 162 HIS A CA    
1240  C C     . HIS A 161 ? 0.4435 0.4440 0.4127 -0.0269 0.0340  -0.0302 162 HIS A C     
1241  O O     . HIS A 161 ? 0.4022 0.4007 0.3729 -0.0273 0.0349  -0.0314 162 HIS A O     
1242  C CB    . HIS A 161 ? 0.4970 0.5028 0.4718 -0.0295 0.0301  -0.0283 162 HIS A CB    
1243  C CG    . HIS A 161 ? 0.4562 0.4662 0.4326 -0.0307 0.0276  -0.0267 162 HIS A CG    
1244  N ND1   . HIS A 161 ? 0.3981 0.4125 0.3753 -0.0296 0.0278  -0.0246 162 HIS A ND1   
1245  C CD2   . HIS A 161 ? 0.4388 0.4495 0.4165 -0.0328 0.0247  -0.0267 162 HIS A CD2   
1246  C CE1   . HIS A 161 ? 0.3950 0.4131 0.3740 -0.0312 0.0253  -0.0233 162 HIS A CE1   
1247  N NE2   . HIS A 161 ? 0.4226 0.4385 0.4020 -0.0333 0.0233  -0.0244 162 HIS A NE2   
1248  N N     . LEU A 162 ? 0.3967 0.3973 0.3634 -0.0253 0.0354  -0.0294 163 LEU A N     
1249  C CA    . LEU A 162 ? 0.4141 0.4122 0.3794 -0.0242 0.0381  -0.0296 163 LEU A CA    
1250  C C     . LEU A 162 ? 0.3474 0.3462 0.3146 -0.0235 0.0393  -0.0283 163 LEU A C     
1251  O O     . LEU A 162 ? 0.3433 0.3444 0.3107 -0.0227 0.0387  -0.0268 163 LEU A O     
1252  C CB    . LEU A 162 ? 0.3751 0.3722 0.3359 -0.0231 0.0387  -0.0294 163 LEU A CB    
1253  C CG    . LEU A 162 ? 0.4039 0.3987 0.3629 -0.0222 0.0414  -0.0292 163 LEU A CG    
1254  C CD1   . LEU A 162 ? 0.4177 0.4105 0.3776 -0.0228 0.0428  -0.0308 163 LEU A CD1   
1255  C CD2   . LEU A 162 ? 0.3981 0.3924 0.3526 -0.0212 0.0418  -0.0285 163 LEU A CD2   
1256  N N     . LEU A 163 ? 0.3403 0.3369 0.3087 -0.0236 0.0410  -0.0288 164 LEU A N     
1257  C CA    . LEU A 163 ? 0.3414 0.3378 0.3110 -0.0229 0.0421  -0.0279 164 LEU A CA    
1258  C C     . LEU A 163 ? 0.3487 0.3421 0.3164 -0.0223 0.0443  -0.0278 164 LEU A C     
1259  O O     . LEU A 163 ? 0.3636 0.3554 0.3314 -0.0230 0.0453  -0.0288 164 LEU A O     
1260  C CB    . LEU A 163 ? 0.3528 0.3497 0.3261 -0.0240 0.0419  -0.0284 164 LEU A CB    
1261  C CG    . LEU A 163 ? 0.3934 0.3935 0.3689 -0.0248 0.0399  -0.0279 164 LEU A CG    
1262  C CD1   . LEU A 163 ? 0.3752 0.3755 0.3539 -0.0257 0.0399  -0.0281 164 LEU A CD1   
1263  C CD2   . LEU A 163 ? 0.4721 0.4752 0.4471 -0.0236 0.0392  -0.0263 164 LEU A CD2   
1264  N N     . LEU A 164 ? 0.3354 0.3281 0.3014 -0.0210 0.0448  -0.0264 165 LEU A N     
1265  C CA    . LEU A 164 ? 0.3444 0.3340 0.3089 -0.0206 0.0466  -0.0259 165 LEU A CA    
1266  C C     . LEU A 164 ? 0.3328 0.3210 0.2989 -0.0203 0.0469  -0.0255 165 LEU A C     
1267  O O     . LEU A 164 ? 0.3565 0.3451 0.3220 -0.0188 0.0464  -0.0247 165 LEU A O     
1268  C CB    . LEU A 164 ? 0.3362 0.3250 0.2969 -0.0194 0.0467  -0.0246 165 LEU A CB    
1269  C CG    . LEU A 164 ? 0.3415 0.3313 0.2997 -0.0196 0.0464  -0.0249 165 LEU A CG    
1270  C CD1   . LEU A 164 ? 0.3381 0.3267 0.2924 -0.0184 0.0467  -0.0234 165 LEU A CD1   
1271  C CD2   . LEU A 164 ? 0.3415 0.3307 0.3002 -0.0208 0.0474  -0.0264 165 LEU A CD2   
1272  N N     . TRP A 165 ? 0.3152 0.3019 0.2832 -0.0215 0.0478  -0.0263 166 TRP A N     
1273  C CA    . TRP A 165 ? 0.3204 0.3056 0.2899 -0.0214 0.0479  -0.0262 166 TRP A CA    
1274  C C     . TRP A 165 ? 0.3641 0.3456 0.3314 -0.0208 0.0488  -0.0251 166 TRP A C     
1275  O O     . TRP A 165 ? 0.3549 0.3352 0.3201 -0.0210 0.0497  -0.0244 166 TRP A O     
1276  C CB    . TRP A 165 ? 0.3232 0.3085 0.2959 -0.0231 0.0481  -0.0273 166 TRP A CB    
1277  C CG    . TRP A 165 ? 0.3020 0.2902 0.2769 -0.0238 0.0470  -0.0282 166 TRP A CG    
1278  C CD1   . TRP A 165 ? 0.3072 0.2971 0.2815 -0.0239 0.0464  -0.0286 166 TRP A CD1   
1279  C CD2   . TRP A 165 ? 0.2836 0.2729 0.2613 -0.0245 0.0462  -0.0288 166 TRP A CD2   
1280  N NE1   . TRP A 165 ? 0.2641 0.2559 0.2409 -0.0248 0.0451  -0.0294 166 TRP A NE1   
1281  C CE2   . TRP A 165 ? 0.2815 0.2732 0.2605 -0.0252 0.0451  -0.0293 166 TRP A CE2   
1282  C CE3   . TRP A 165 ? 0.2721 0.2605 0.2512 -0.0247 0.0461  -0.0288 166 TRP A CE3   
1283  C CZ2   . TRP A 165 ? 0.2591 0.2522 0.2409 -0.0261 0.0439  -0.0297 166 TRP A CZ2   
1284  C CZ3   . TRP A 165 ? 0.2820 0.2722 0.2637 -0.0255 0.0451  -0.0292 166 TRP A CZ3   
1285  C CH2   . TRP A 165 ? 0.2738 0.2664 0.2569 -0.0262 0.0441  -0.0295 166 TRP A CH2   
1286  N N     . GLN A 166 ? 0.3518 0.3314 0.3194 -0.0202 0.0485  -0.0250 167 GLN A N     
1287  C CA    . GLN A 166 ? 0.3605 0.3357 0.3260 -0.0197 0.0490  -0.0241 167 GLN A CA    
1288  C C     . GLN A 166 ? 0.3710 0.3455 0.3333 -0.0185 0.0491  -0.0227 167 GLN A C     
1289  O O     . GLN A 166 ? 0.3825 0.3544 0.3431 -0.0192 0.0499  -0.0217 167 GLN A O     
1290  C CB    . GLN A 166 ? 0.3973 0.3702 0.3640 -0.0219 0.0499  -0.0241 167 GLN A CB    
1291  C CG    . GLN A 166 ? 0.4320 0.4053 0.4019 -0.0230 0.0496  -0.0253 167 GLN A CG    
1292  C CD    . GLN A 166 ? 0.4589 0.4303 0.4304 -0.0251 0.0504  -0.0251 167 GLN A CD    
1293  O OE1   . GLN A 166 ? 0.5502 0.5205 0.5207 -0.0259 0.0515  -0.0240 167 GLN A OE1   
1294  N NE2   . GLN A 166 ? 0.4461 0.4177 0.4204 -0.0262 0.0500  -0.0260 167 GLN A NE2   
1295  N N     . ILE A 167 ? 0.3769 0.3540 0.3383 -0.0167 0.0482  -0.0225 168 ILE A N     
1296  C CA    . ILE A 167 ? 0.4064 0.3832 0.3647 -0.0153 0.0480  -0.0212 168 ILE A CA    
1297  C C     . ILE A 167 ? 0.4639 0.4362 0.4199 -0.0138 0.0479  -0.0201 168 ILE A C     
1298  O O     . ILE A 167 ? 0.5044 0.4750 0.4576 -0.0129 0.0478  -0.0187 168 ILE A O     
1299  C CB    . ILE A 167 ? 0.3917 0.3732 0.3504 -0.0139 0.0468  -0.0213 168 ILE A CB    
1300  C CG1   . ILE A 167 ? 0.3740 0.3557 0.3297 -0.0126 0.0464  -0.0199 168 ILE A CG1   
1301  C CG2   . ILE A 167 ? 0.3576 0.3403 0.3176 -0.0122 0.0460  -0.0216 168 ILE A CG2   
1302  C CD1   . ILE A 167 ? 0.3668 0.3483 0.3208 -0.0142 0.0471  -0.0197 168 ILE A CD1   
1303  N N     . ALA A 168 ? 0.4700 0.4399 0.4269 -0.0134 0.0476  -0.0208 169 ALA A N     
1304  C CA    . ALA A 168 ? 0.4881 0.4531 0.4427 -0.0116 0.0471  -0.0201 169 ALA A CA    
1305  C C     . ALA A 168 ? 0.4517 0.4117 0.4045 -0.0132 0.0477  -0.0188 169 ALA A C     
1306  O O     . ALA A 168 ? 0.4811 0.4370 0.4312 -0.0119 0.0472  -0.0176 169 ALA A O     
1307  C CB    . ALA A 168 ? 0.5328 0.4966 0.4885 -0.0110 0.0466  -0.0215 169 ALA A CB    
1308  N N     . ILE A 169 ? 0.4911 0.4518 0.4458 -0.0161 0.0488  -0.0190 170 ILE A N     
1309  C CA    . ILE A 169 ? 0.4663 0.4233 0.4201 -0.0180 0.0495  -0.0176 170 ILE A CA    
1310  C C     . ILE A 169 ? 0.4887 0.4487 0.4421 -0.0192 0.0508  -0.0167 170 ILE A C     
1311  O O     . ILE A 169 ? 0.5208 0.4801 0.4747 -0.0214 0.0519  -0.0159 170 ILE A O     
1312  C CB    . ILE A 169 ? 0.4917 0.4468 0.4481 -0.0202 0.0497  -0.0184 170 ILE A CB    
1313  C CG1   . ILE A 169 ? 0.5306 0.4907 0.4906 -0.0215 0.0503  -0.0200 170 ILE A CG1   
1314  C CG2   . ILE A 169 ? 0.5371 0.4879 0.4928 -0.0189 0.0483  -0.0191 170 ILE A CG2   
1315  C CD1   . ILE A 169 ? 0.5299 0.4887 0.4927 -0.0236 0.0503  -0.0207 170 ILE A CD1   
1316  N N     . ALA A 170 ? 0.4502 0.4137 0.4025 -0.0178 0.0505  -0.0169 171 ALA A N     
1317  C CA    . ALA A 170 ? 0.4244 0.3907 0.3756 -0.0186 0.0515  -0.0164 171 ALA A CA    
1318  C C     . ALA A 170 ? 0.4185 0.3816 0.3667 -0.0191 0.0522  -0.0140 171 ALA A C     
1319  O O     . ALA A 170 ? 0.4159 0.3761 0.3612 -0.0175 0.0513  -0.0126 171 ALA A O     
1320  C CB    . ALA A 170 ? 0.4155 0.3854 0.3657 -0.0168 0.0505  -0.0168 171 ALA A CB    
1321  N N     . GLY A 171 ? 0.4341 0.3977 0.3829 -0.0213 0.0538  -0.0135 172 GLY A N     
1322  C CA    . GLY A 171 ? 0.4466 0.4081 0.3925 -0.0222 0.0548  -0.0110 172 GLY A CA    
1323  C C     . GLY A 171 ? 0.4589 0.4154 0.4053 -0.0236 0.0547  -0.0095 172 GLY A C     
1324  O O     . GLY A 171 ? 0.4190 0.3729 0.3632 -0.0246 0.0552  -0.0069 172 GLY A O     
1325  N N     . GLU A 172 ? 0.4964 0.4514 0.4457 -0.0239 0.0539  -0.0109 173 GLU A N     
1326  C CA    . GLU A 172 ? 0.5329 0.4829 0.4829 -0.0255 0.0534  -0.0099 173 GLU A CA    
1327  C C     . GLU A 172 ? 0.4869 0.4392 0.4400 -0.0285 0.0550  -0.0095 173 GLU A C     
1328  O O     . GLU A 172 ? 0.5038 0.4586 0.4604 -0.0292 0.0552  -0.0115 173 GLU A O     
1329  C CB    . GLU A 172 ? 0.6381 0.5856 0.5893 -0.0242 0.0517  -0.0117 173 GLU A CB    
1330  C CG    . GLU A 172 ? 0.7299 0.6705 0.6801 -0.0249 0.0505  -0.0106 173 GLU A CG    
1331  C CD    . GLU A 172 ? 0.7369 0.6762 0.6891 -0.0284 0.0512  -0.0092 173 GLU A CD    
1332  O OE1   . GLU A 172 ? 0.7764 0.7182 0.7323 -0.0300 0.0516  -0.0107 173 GLU A OE1   
1333  O OE2   . GLU A 172 ? 0.7062 0.6424 0.6566 -0.0298 0.0514  -0.0065 173 GLU A OE2   
1334  N N     . HIS A 173 ? 0.5052 0.4566 0.4570 -0.0303 0.0562  -0.0069 174 HIS A N     
1335  C CA    . HIS A 173 ? 0.4574 0.4127 0.4118 -0.0328 0.0582  -0.0063 174 HIS A CA    
1336  C C     . HIS A 173 ? 0.4251 0.3779 0.3826 -0.0355 0.0579  -0.0055 174 HIS A C     
1337  O O     . HIS A 173 ? 0.4354 0.3920 0.3964 -0.0375 0.0594  -0.0055 174 HIS A O     
1338  C CB    . HIS A 173 ? 0.4822 0.4388 0.4335 -0.0334 0.0599  -0.0036 174 HIS A CB    
1339  C CG    . HIS A 173 ? 0.5096 0.4606 0.4582 -0.0343 0.0590  -0.0004 174 HIS A CG    
1340  N ND1   . HIS A 173 ? 0.5528 0.4999 0.4974 -0.0321 0.0575  0.0003  174 HIS A ND1   
1341  C CD2   . HIS A 173 ? 0.5382 0.4868 0.4875 -0.0371 0.0594  0.0023  174 HIS A CD2   
1342  C CE1   . HIS A 173 ? 0.5788 0.5207 0.5216 -0.0335 0.0568  0.0033  174 HIS A CE1   
1343  N NE2   . HIS A 173 ? 0.5813 0.5240 0.5269 -0.0367 0.0579  0.0047  174 HIS A NE2   
1344  N N     . THR A 174 ? 0.4310 0.3775 0.3875 -0.0356 0.0559  -0.0048 175 THR A N     
1345  C CA    . THR A 174 ? 0.4980 0.4411 0.4568 -0.0384 0.0552  -0.0037 175 THR A CA    
1346  C C     . THR A 174 ? 0.5373 0.4813 0.4998 -0.0386 0.0543  -0.0065 175 THR A C     
1347  O O     . THR A 174 ? 0.5941 0.5383 0.5600 -0.0413 0.0542  -0.0061 175 THR A O     
1348  C CB    . THR A 174 ? 0.4729 0.4080 0.4283 -0.0384 0.0531  -0.0019 175 THR A CB    
1349  O OG1   . THR A 174 ? 0.4551 0.3872 0.4089 -0.0353 0.0513  -0.0043 175 THR A OG1   
1350  C CG2   . THR A 174 ? 0.4835 0.4175 0.4351 -0.0381 0.0538  0.0011  175 THR A CG2   
1351  N N     . LEU A 175 ? 0.5519 0.4968 0.5138 -0.0358 0.0535  -0.0092 176 LEU A N     
1352  C CA    . LEU A 175 ? 0.5526 0.4983 0.5174 -0.0356 0.0525  -0.0118 176 LEU A CA    
1353  C C     . LEU A 175 ? 0.5790 0.5180 0.5431 -0.0362 0.0503  -0.0118 176 LEU A C     
1354  O O     . LEU A 175 ? 0.5510 0.4901 0.5180 -0.0376 0.0495  -0.0130 176 LEU A O     
1355  C CB    . LEU A 175 ? 0.5805 0.5316 0.5499 -0.0378 0.0540  -0.0121 176 LEU A CB    
1356  C CG    . LEU A 175 ? 0.6130 0.5705 0.5830 -0.0372 0.0561  -0.0125 176 LEU A CG    
1357  C CD1   . LEU A 175 ? 0.6205 0.5829 0.5953 -0.0387 0.0572  -0.0134 176 LEU A CD1   
1358  C CD2   . LEU A 175 ? 0.6931 0.6520 0.6610 -0.0341 0.0557  -0.0144 176 LEU A CD2   
1359  N N     . THR A 176 ? 0.6464 0.5795 0.6066 -0.0351 0.0491  -0.0106 177 THR A N     
1360  C CA    . THR A 176 ? 0.5893 0.5151 0.5481 -0.0354 0.0467  -0.0108 177 THR A CA    
1361  C C     . THR A 176 ? 0.5971 0.5190 0.5519 -0.0315 0.0453  -0.0120 177 THR A C     
1362  O O     . THR A 176 ? 0.6283 0.5440 0.5812 -0.0307 0.0432  -0.0128 177 THR A O     
1363  C CB    . THR A 176 ? 0.5876 0.5089 0.5460 -0.0384 0.0463  -0.0076 177 THR A CB    
1364  O OG1   . THR A 176 ? 0.5971 0.5167 0.5517 -0.0370 0.0467  -0.0057 177 THR A OG1   
1365  C CG2   . THR A 176 ? 0.5905 0.5168 0.5531 -0.0422 0.0481  -0.0061 177 THR A CG2   
1366  N N     . GLN A 177 ? 0.5628 0.4887 0.5162 -0.0290 0.0464  -0.0121 178 GLN A N     
1367  C CA    . GLN A 177 ? 0.5608 0.4848 0.5111 -0.0250 0.0453  -0.0133 178 GLN A CA    
1368  C C     . GLN A 177 ? 0.5843 0.5141 0.5365 -0.0232 0.0457  -0.0159 178 GLN A C     
1369  O O     . GLN A 177 ? 0.5265 0.4618 0.4818 -0.0248 0.0470  -0.0165 178 GLN A O     
1370  C CB    . GLN A 177 ? 0.5737 0.4981 0.5211 -0.0235 0.0459  -0.0113 178 GLN A CB    
1371  C CG    . GLN A 177 ? 0.6246 0.5434 0.5699 -0.0254 0.0455  -0.0082 178 GLN A CG    
1372  C CD    . GLN A 177 ? 0.6703 0.5804 0.6124 -0.0238 0.0431  -0.0080 178 GLN A CD    
1373  O OE1   . GLN A 177 ? 0.6472 0.5555 0.5884 -0.0210 0.0418  -0.0104 178 GLN A OE1   
1374  N NE2   . GLN A 177 ? 0.6576 0.5621 0.5979 -0.0256 0.0424  -0.0052 178 GLN A NE2   
1375  N N     . PHE A 178 ? 0.6179 0.5462 0.5681 -0.0199 0.0445  -0.0175 179 PHE A N     
1376  C CA    . PHE A 178 ? 0.6128 0.5465 0.5647 -0.0182 0.0447  -0.0197 179 PHE A CA    
1377  C C     . PHE A 178 ? 0.5426 0.4798 0.4930 -0.0151 0.0450  -0.0195 179 PHE A C     
1378  O O     . PHE A 178 ? 0.6340 0.5755 0.5854 -0.0133 0.0450  -0.0210 179 PHE A O     
1379  C CB    . PHE A 178 ? 0.6113 0.5417 0.5627 -0.0171 0.0432  -0.0217 179 PHE A CB    
1380  C CG    . PHE A 178 ? 0.6471 0.5774 0.6015 -0.0203 0.0430  -0.0225 179 PHE A CG    
1381  C CD1   . PHE A 178 ? 0.6614 0.5980 0.6192 -0.0214 0.0439  -0.0236 179 PHE A CD1   
1382  C CD2   . PHE A 178 ? 0.6985 0.6223 0.6521 -0.0223 0.0418  -0.0221 179 PHE A CD2   
1383  C CE1   . PHE A 178 ? 0.6793 0.6159 0.6399 -0.0242 0.0437  -0.0242 179 PHE A CE1   
1384  C CE2   . PHE A 178 ? 0.7220 0.6462 0.6786 -0.0252 0.0414  -0.0227 179 PHE A CE2   
1385  C CZ    . PHE A 178 ? 0.7364 0.6672 0.6965 -0.0261 0.0424  -0.0238 179 PHE A CZ    
1386  N N     . HIS A 179 ? 0.5432 0.4787 0.4912 -0.0146 0.0452  -0.0175 180 HIS A N     
1387  C CA    . HIS A 179 ? 0.6117 0.5511 0.5586 -0.0122 0.0454  -0.0170 180 HIS A CA    
1388  C C     . HIS A 179 ? 0.6179 0.5563 0.5629 -0.0132 0.0461  -0.0145 180 HIS A C     
1389  O O     . HIS A 179 ? 0.6457 0.5793 0.5898 -0.0152 0.0460  -0.0130 180 HIS A O     
1390  C CB    . HIS A 179 ? 0.6830 0.6203 0.6275 -0.0081 0.0441  -0.0177 180 HIS A CB    
1391  C CG    . HIS A 179 ? 0.7708 0.7003 0.7118 -0.0069 0.0430  -0.0163 180 HIS A CG    
1392  N ND1   . HIS A 179 ? 0.8180 0.7462 0.7566 -0.0060 0.0428  -0.0142 180 HIS A ND1   
1393  C CD2   . HIS A 179 ? 0.8203 0.7427 0.7597 -0.0067 0.0417  -0.0168 180 HIS A CD2   
1394  C CE1   . HIS A 179 ? 0.8898 0.8102 0.8255 -0.0051 0.0415  -0.0132 180 HIS A CE1   
1395  N NE2   . HIS A 179 ? 0.9368 0.8534 0.8730 -0.0056 0.0407  -0.0149 180 HIS A NE2   
1396  N N     . THR A 180 ? 0.6612 0.6043 0.6057 -0.0121 0.0466  -0.0140 181 THR A N     
1397  C CA    . THR A 180 ? 0.6638 0.6067 0.6062 -0.0128 0.0471  -0.0117 181 THR A CA    
1398  C C     . THR A 180 ? 0.6313 0.5719 0.5704 -0.0096 0.0459  -0.0105 181 THR A C     
1399  O O     . THR A 180 ? 0.5373 0.4756 0.4758 -0.0069 0.0447  -0.0114 181 THR A O     
1400  C CB    . THR A 180 ? 0.6473 0.5968 0.5912 -0.0140 0.0484  -0.0121 181 THR A CB    
1401  O OG1   . THR A 180 ? 0.7448 0.6935 0.6862 -0.0151 0.0491  -0.0099 181 THR A OG1   
1402  C CG2   . THR A 180 ? 0.6680 0.6225 0.6122 -0.0116 0.0478  -0.0132 181 THR A CG2   
1403  N N     . SER A 181 ? 0.6794 0.6209 0.6163 -0.0097 0.0462  -0.0085 182 SER A N     
1404  C CA    . SER A 181 ? 0.6627 0.6024 0.5965 -0.0066 0.0450  -0.0070 182 SER A CA    
1405  C C     . SER A 181 ? 0.6821 0.6283 0.6158 -0.0054 0.0451  -0.0071 182 SER A C     
1406  O O     . SER A 181 ? 0.5951 0.5463 0.5305 -0.0073 0.0461  -0.0079 182 SER A O     
1407  C CB    . SER A 181 ? 0.7105 0.6444 0.6411 -0.0077 0.0448  -0.0041 182 SER A CB    
1408  O OG    . SER A 181 ? 0.7855 0.7221 0.7158 -0.0106 0.0464  -0.0028 182 SER A OG    
1409  N N     . SER A 182 ? 0.7045 0.6507 0.6363 -0.0022 0.0437  -0.0062 183 SER A N     
1410  C CA    . SER A 182 ? 0.6982 0.6505 0.6300 -0.0009 0.0433  -0.0061 183 SER A CA    
1411  C C     . SER A 182 ? 0.6909 0.6444 0.6205 -0.0030 0.0441  -0.0045 183 SER A C     
1412  O O     . SER A 182 ? 0.7131 0.6721 0.6431 -0.0034 0.0442  -0.0051 183 SER A O     
1413  C CB    . SER A 182 ? 0.6678 0.6196 0.5980 0.0031  0.0417  -0.0053 183 SER A CB    
1414  O OG    . SER A 182 ? 0.6526 0.5981 0.5792 0.0039  0.0410  -0.0029 183 SER A OG    
1415  N N     . ASP A 183 ? 0.6750 0.6233 0.6021 -0.0044 0.0446  -0.0025 184 ASP A N     
1416  C CA    . ASP A 183 ? 0.6569 0.6061 0.5813 -0.0063 0.0455  -0.0007 184 ASP A CA    
1417  C C     . ASP A 183 ? 0.6287 0.5821 0.5553 -0.0092 0.0472  -0.0023 184 ASP A C     
1418  O O     . ASP A 183 ? 0.5548 0.5121 0.4802 -0.0099 0.0478  -0.0022 184 ASP A O     
1419  C CB    . ASP A 183 ? 0.7117 0.6545 0.6333 -0.0073 0.0456  0.0022  184 ASP A CB    
1420  C CG    . ASP A 183 ? 0.8184 0.7568 0.7418 -0.0096 0.0463  0.0020  184 ASP A CG    
1421  O OD1   . ASP A 183 ? 0.8375 0.7733 0.7626 -0.0083 0.0454  0.0005  184 ASP A OD1   
1422  O OD2   . ASP A 183 ? 0.8358 0.7735 0.7587 -0.0126 0.0477  0.0035  184 ASP A OD2   
1423  N N     . ARG A 184 ? 0.6129 0.5654 0.5428 -0.0106 0.0480  -0.0039 185 ARG A N     
1424  C CA    . ARG A 184 ? 0.5904 0.5465 0.5229 -0.0131 0.0496  -0.0056 185 ARG A CA    
1425  C C     . ARG A 184 ? 0.5611 0.5230 0.4952 -0.0122 0.0491  -0.0078 185 ARG A C     
1426  O O     . ARG A 184 ? 0.4949 0.4605 0.4296 -0.0136 0.0500  -0.0088 185 ARG A O     
1427  C CB    . ARG A 184 ? 0.6429 0.5966 0.5786 -0.0147 0.0501  -0.0067 185 ARG A CB    
1428  C CG    . ARG A 184 ? 0.7130 0.6611 0.6475 -0.0164 0.0505  -0.0045 185 ARG A CG    
1429  C CD    . ARG A 184 ? 0.7690 0.7188 0.7027 -0.0190 0.0524  -0.0029 185 ARG A CD    
1430  N NE    . ARG A 184 ? 0.8291 0.7741 0.7625 -0.0212 0.0529  -0.0007 185 ARG A NE    
1431  C CZ    . ARG A 184 ? 0.8901 0.8329 0.8204 -0.0222 0.0533  0.0024  185 ARG A CZ    
1432  N NH1   . ARG A 184 ? 0.9487 0.8935 0.8756 -0.0210 0.0534  0.0036  185 ARG A NH1   
1433  N NH2   . ARG A 184 ? 0.9132 0.8517 0.8439 -0.0245 0.0535  0.0045  185 ARG A NH2   
1434  N N     . LEU A 185 ? 0.5612 0.5239 0.4962 -0.0098 0.0475  -0.0085 186 LEU A N     
1435  C CA    . LEU A 185 ? 0.5380 0.5062 0.4751 -0.0091 0.0468  -0.0103 186 LEU A CA    
1436  C C     . LEU A 185 ? 0.5153 0.4865 0.4497 -0.0085 0.0461  -0.0094 186 LEU A C     
1437  O O     . LEU A 185 ? 0.5535 0.5292 0.4890 -0.0090 0.0457  -0.0107 186 LEU A O     
1438  C CB    . LEU A 185 ? 0.5433 0.5119 0.4823 -0.0067 0.0456  -0.0110 186 LEU A CB    
1439  C CG    . LEU A 185 ? 0.5360 0.5021 0.4775 -0.0072 0.0460  -0.0123 186 LEU A CG    
1440  C CD1   . LEU A 185 ? 0.5255 0.4926 0.4683 -0.0044 0.0449  -0.0130 186 LEU A CD1   
1441  C CD2   . LEU A 185 ? 0.5418 0.5105 0.4862 -0.0098 0.0470  -0.0140 186 LEU A CD2   
1442  N N     . GLN A 186 ? 0.5280 0.4965 0.4588 -0.0074 0.0457  -0.0070 187 GLN A N     
1443  C CA    . GLN A 186 ? 0.5737 0.5446 0.5014 -0.0067 0.0448  -0.0060 187 GLN A CA    
1444  C C     . GLN A 186 ? 0.5760 0.5484 0.5020 -0.0090 0.0462  -0.0063 187 GLN A C     
1445  O O     . GLN A 186 ? 0.5650 0.5410 0.4898 -0.0091 0.0455  -0.0070 187 GLN A O     
1446  C CB    . GLN A 186 ? 0.5636 0.5307 0.4878 -0.0049 0.0440  -0.0032 187 GLN A CB    
1447  C CG    . GLN A 186 ? 0.5547 0.5242 0.4753 -0.0040 0.0429  -0.0017 187 GLN A CG    
1448  C CD    . GLN A 186 ? 0.5524 0.5273 0.4746 -0.0026 0.0411  -0.0029 187 GLN A CD    
1449  O OE1   . GLN A 186 ? 0.5576 0.5335 0.4823 -0.0004 0.0399  -0.0031 187 GLN A OE1   
1450  N NE2   . GLN A 186 ? 0.5871 0.5657 0.5081 -0.0038 0.0408  -0.0036 187 GLN A NE2   
1451  N N     . ILE A 187 ? 0.5555 0.5251 0.4814 -0.0109 0.0481  -0.0059 188 ILE A N     
1452  C CA    . ILE A 187 ? 0.5792 0.5504 0.5036 -0.0129 0.0498  -0.0063 188 ILE A CA    
1453  C C     . ILE A 187 ? 0.5360 0.5113 0.4635 -0.0137 0.0498  -0.0094 188 ILE A C     
1454  O O     . ILE A 187 ? 0.5474 0.5253 0.4731 -0.0142 0.0500  -0.0104 188 ILE A O     
1455  C CB    . ILE A 187 ? 0.6039 0.5719 0.5285 -0.0148 0.0518  -0.0051 188 ILE A CB    
1456  C CG1   . ILE A 187 ? 0.6253 0.5897 0.5458 -0.0146 0.0518  -0.0017 188 ILE A CG1   
1457  C CG2   . ILE A 187 ? 0.6332 0.6041 0.5584 -0.0168 0.0538  -0.0064 188 ILE A CG2   
1458  C CD1   . ILE A 187 ? 0.6556 0.6156 0.5770 -0.0162 0.0530  0.0001  188 ILE A CD1   
1459  N N     . LEU A 188 ? 0.4891 0.4644 0.4208 -0.0137 0.0495  -0.0109 189 LEU A N     
1460  C CA    . LEU A 188 ? 0.4681 0.4466 0.4030 -0.0145 0.0493  -0.0135 189 LEU A CA    
1461  C C     . LEU A 188 ? 0.4544 0.4364 0.3885 -0.0134 0.0473  -0.0142 189 LEU A C     
1462  O O     . LEU A 188 ? 0.4183 0.4028 0.3524 -0.0143 0.0471  -0.0159 189 LEU A O     
1463  C CB    . LEU A 188 ? 0.4930 0.4707 0.4322 -0.0146 0.0492  -0.0145 189 LEU A CB    
1464  C CG    . LEU A 188 ? 0.5218 0.5027 0.4646 -0.0153 0.0487  -0.0169 189 LEU A CG    
1465  C CD1   . LEU A 188 ? 0.5000 0.4821 0.4429 -0.0169 0.0499  -0.0184 189 LEU A CD1   
1466  C CD2   . LEU A 188 ? 0.5347 0.5145 0.4811 -0.0154 0.0487  -0.0176 189 LEU A CD2   
1467  N N     . VAL A 189 ? 0.4732 0.4553 0.4065 -0.0115 0.0457  -0.0128 190 VAL A N     
1468  C CA    . VAL A 189 ? 0.5290 0.5147 0.4618 -0.0106 0.0436  -0.0130 190 VAL A CA    
1469  C C     . VAL A 189 ? 0.5457 0.5322 0.4743 -0.0112 0.0435  -0.0129 190 VAL A C     
1470  O O     . VAL A 189 ? 0.6008 0.5902 0.5293 -0.0117 0.0423  -0.0143 190 VAL A O     
1471  C CB    . VAL A 189 ? 0.5376 0.5233 0.4701 -0.0081 0.0422  -0.0111 190 VAL A CB    
1472  C CG1   . VAL A 189 ? 0.5569 0.5465 0.4882 -0.0072 0.0399  -0.0107 190 VAL A CG1   
1473  C CG2   . VAL A 189 ? 0.5648 0.5507 0.5013 -0.0072 0.0420  -0.0117 190 VAL A CG2   
1474  N N     . GLU A 190 ? 0.5574 0.5410 0.4821 -0.0111 0.0447  -0.0111 191 GLU A N     
1475  C CA    . GLU A 190 ? 0.6315 0.6157 0.5515 -0.0114 0.0448  -0.0106 191 GLU A CA    
1476  C C     . GLU A 190 ? 0.5544 0.5400 0.4746 -0.0130 0.0461  -0.0131 191 GLU A C     
1477  O O     . GLU A 190 ? 0.5367 0.5240 0.4540 -0.0132 0.0452  -0.0142 191 GLU A O     
1478  C CB    . GLU A 190 ? 0.7152 0.6961 0.6315 -0.0112 0.0462  -0.0079 191 GLU A CB    
1479  C CG    . GLU A 190 ? 0.7600 0.7392 0.6755 -0.0092 0.0447  -0.0054 191 GLU A CG    
1480  C CD    . GLU A 190 ? 0.8638 0.8390 0.7759 -0.0092 0.0458  -0.0024 191 GLU A CD    
1481  O OE1   . GLU A 190 ? 0.9501 0.9243 0.8607 -0.0109 0.0479  -0.0021 191 GLU A OE1   
1482  O OE2   . GLU A 190 ? 0.9246 0.8977 0.8357 -0.0074 0.0444  -0.0003 191 GLU A OE2   
1483  N N     . GLN A 191 ? 0.4864 0.4709 0.4098 -0.0142 0.0479  -0.0141 192 GLN A N     
1484  C CA    . GLN A 191 ? 0.4737 0.4593 0.3979 -0.0154 0.0492  -0.0164 192 GLN A CA    
1485  C C     . GLN A 191 ? 0.4964 0.4843 0.4228 -0.0156 0.0472  -0.0189 192 GLN A C     
1486  O O     . GLN A 191 ? 0.4744 0.4634 0.3993 -0.0161 0.0471  -0.0209 192 GLN A O     
1487  C CB    . GLN A 191 ? 0.5025 0.4865 0.4301 -0.0165 0.0513  -0.0165 192 GLN A CB    
1488  C CG    . GLN A 191 ? 0.4994 0.4849 0.4301 -0.0175 0.0520  -0.0193 192 GLN A CG    
1489  C CD    . GLN A 191 ? 0.5333 0.5175 0.4676 -0.0186 0.0540  -0.0192 192 GLN A CD    
1490  O OE1   . GLN A 191 ? 0.5264 0.5088 0.4628 -0.0187 0.0538  -0.0179 192 GLN A OE1   
1491  N NE2   . GLN A 191 ? 0.4795 0.4648 0.4144 -0.0194 0.0557  -0.0206 192 GLN A NE2   
1492  N N     . LEU A 192 ? 0.5176 0.5063 0.4475 -0.0152 0.0455  -0.0188 193 LEU A N     
1493  C CA    . LEU A 192 ? 0.4951 0.4862 0.4277 -0.0156 0.0435  -0.0207 193 LEU A CA    
1494  C C     . LEU A 192 ? 0.4676 0.4607 0.3971 -0.0152 0.0411  -0.0206 193 LEU A C     
1495  O O     . LEU A 192 ? 0.4633 0.4582 0.3940 -0.0159 0.0392  -0.0223 193 LEU A O     
1496  C CB    . LEU A 192 ? 0.5075 0.4994 0.4447 -0.0153 0.0428  -0.0202 193 LEU A CB    
1497  C CG    . LEU A 192 ? 0.5309 0.5214 0.4718 -0.0161 0.0445  -0.0209 193 LEU A CG    
1498  C CD1   . LEU A 192 ? 0.5051 0.4962 0.4494 -0.0153 0.0439  -0.0202 193 LEU A CD1   
1499  C CD2   . LEU A 192 ? 0.5378 0.5291 0.4807 -0.0175 0.0445  -0.0233 193 LEU A CD2   
1500  N N     . ASN A 193 ? 0.5041 0.4966 0.4295 -0.0141 0.0410  -0.0187 194 ASN A N     
1501  C CA    . ASN A 193 ? 0.5311 0.5256 0.4535 -0.0136 0.0386  -0.0183 194 ASN A CA    
1502  C C     . ASN A 193 ? 0.5410 0.5353 0.4595 -0.0144 0.0384  -0.0203 194 ASN A C     
1503  O O     . ASN A 193 ? 0.5583 0.5538 0.4736 -0.0142 0.0362  -0.0205 194 ASN A O     
1504  C CB    . ASN A 193 ? 0.5381 0.5319 0.4574 -0.0120 0.0384  -0.0154 194 ASN A CB    
1505  C CG    . ASN A 193 ? 0.5276 0.5241 0.4451 -0.0113 0.0353  -0.0147 194 ASN A CG    
1506  O OD1   . ASN A 193 ? 0.5041 0.5035 0.4249 -0.0116 0.0332  -0.0154 194 ASN A OD1   
1507  N ND2   . ASN A 193 ? 0.5325 0.5283 0.4447 -0.0106 0.0351  -0.0133 194 ASN A ND2   
1508  N N     . GLN A 194 ? 0.5035 0.4963 0.4223 -0.0151 0.0407  -0.0220 195 GLN A N     
1509  C CA    . GLN A 194 ? 0.5279 0.5205 0.4433 -0.0155 0.0408  -0.0244 195 GLN A CA    
1510  C C     . GLN A 194 ? 0.5304 0.5239 0.4478 -0.0164 0.0380  -0.0267 195 GLN A C     
1511  O O     . GLN A 194 ? 0.5223 0.5158 0.4361 -0.0165 0.0364  -0.0284 195 GLN A O     
1512  C CB    . GLN A 194 ? 0.5427 0.5339 0.4585 -0.0159 0.0440  -0.0254 195 GLN A CB    
1513  C CG    . GLN A 194 ? 0.5155 0.5057 0.4285 -0.0154 0.0468  -0.0230 195 GLN A CG    
1514  C CD    . GLN A 194 ? 0.5561 0.5457 0.4709 -0.0160 0.0499  -0.0236 195 GLN A CD    
1515  O OE1   . GLN A 194 ? 0.6145 0.6046 0.5278 -0.0159 0.0510  -0.0259 195 GLN A OE1   
1516  N NE2   . GLN A 194 ? 0.5746 0.5632 0.4926 -0.0164 0.0514  -0.0217 195 GLN A NE2   
1517  N N     . TRP A 195 ? 0.5431 0.5375 0.4663 -0.0171 0.0374  -0.0268 196 TRP A N     
1518  C CA    . TRP A 195 ? 0.5345 0.5297 0.4604 -0.0183 0.0350  -0.0288 196 TRP A CA    
1519  C C     . TRP A 195 ? 0.5171 0.5151 0.4465 -0.0186 0.0325  -0.0272 196 TRP A C     
1520  O O     . TRP A 195 ? 0.5531 0.5525 0.4836 -0.0197 0.0296  -0.0281 196 TRP A O     
1521  C CB    . TRP A 195 ? 0.5415 0.5354 0.4712 -0.0191 0.0365  -0.0305 196 TRP A CB    
1522  C CG    . TRP A 195 ? 0.4889 0.4809 0.4162 -0.0186 0.0394  -0.0317 196 TRP A CG    
1523  C CD1   . TRP A 195 ? 0.4475 0.4383 0.3722 -0.0185 0.0395  -0.0343 196 TRP A CD1   
1524  C CD2   . TRP A 195 ? 0.4397 0.4310 0.3674 -0.0181 0.0427  -0.0302 196 TRP A CD2   
1525  N NE1   . TRP A 195 ? 0.4406 0.4306 0.3640 -0.0178 0.0428  -0.0345 196 TRP A NE1   
1526  C CE2   . TRP A 195 ? 0.4554 0.4458 0.3808 -0.0178 0.0448  -0.0319 196 TRP A CE2   
1527  C CE3   . TRP A 195 ? 0.4691 0.4604 0.3987 -0.0178 0.0440  -0.0277 196 TRP A CE3   
1528  C CZ2   . TRP A 195 ? 0.4301 0.4201 0.3555 -0.0175 0.0481  -0.0308 196 TRP A CZ2   
1529  C CZ3   . TRP A 195 ? 0.4747 0.4649 0.4041 -0.0177 0.0470  -0.0267 196 TRP A CZ3   
1530  C CH2   . TRP A 195 ? 0.4424 0.4322 0.3699 -0.0177 0.0490  -0.0281 196 TRP A CH2   
1531  N N     . TYR A 196 ? 0.4864 0.4853 0.4175 -0.0176 0.0335  -0.0247 197 TYR A N     
1532  C CA    . TYR A 196 ? 0.4676 0.4697 0.4025 -0.0174 0.0317  -0.0232 197 TYR A CA    
1533  C C     . TYR A 196 ? 0.4565 0.4600 0.3891 -0.0158 0.0309  -0.0208 197 TYR A C     
1534  O O     . TYR A 196 ? 0.4842 0.4856 0.4143 -0.0145 0.0329  -0.0195 197 TYR A O     
1535  C CB    . TYR A 196 ? 0.4381 0.4402 0.3778 -0.0173 0.0334  -0.0228 197 TYR A CB    
1536  C CG    . TYR A 196 ? 0.4223 0.4232 0.3648 -0.0188 0.0341  -0.0249 197 TYR A CG    
1537  C CD1   . TYR A 196 ? 0.4424 0.4453 0.3884 -0.0203 0.0320  -0.0257 197 TYR A CD1   
1538  C CD2   . TYR A 196 ? 0.4186 0.4164 0.3603 -0.0189 0.0367  -0.0259 197 TYR A CD2   
1539  C CE1   . TYR A 196 ? 0.4250 0.4265 0.3734 -0.0216 0.0324  -0.0274 197 TYR A CE1   
1540  C CE2   . TYR A 196 ? 0.4315 0.4283 0.3759 -0.0200 0.0372  -0.0278 197 TYR A CE2   
1541  C CZ    . TYR A 196 ? 0.4129 0.4114 0.3606 -0.0213 0.0350  -0.0286 197 TYR A CZ    
1542  O OH    . TYR A 196 ? 0.4522 0.4494 0.4024 -0.0224 0.0354  -0.0303 197 TYR A OH    
1543  N N     . PRO A 197 ? 0.4902 0.4973 0.4237 -0.0158 0.0280  -0.0199 198 PRO A N     
1544  C CA    . PRO A 197 ? 0.5350 0.5440 0.4670 -0.0140 0.0270  -0.0174 198 PRO A CA    
1545  C C     . PRO A 197 ? 0.5336 0.5427 0.4683 -0.0122 0.0287  -0.0156 198 PRO A C     
1546  O O     . PRO A 197 ? 0.5629 0.5715 0.5012 -0.0125 0.0301  -0.0162 198 PRO A O     
1547  C CB    . PRO A 197 ? 0.5221 0.5356 0.4560 -0.0149 0.0234  -0.0171 198 PRO A CB    
1548  C CG    . PRO A 197 ? 0.5352 0.5478 0.4695 -0.0174 0.0223  -0.0197 198 PRO A CG    
1549  C CD    . PRO A 197 ? 0.5045 0.5142 0.4408 -0.0177 0.0253  -0.0210 198 PRO A CD    
1550  N N     . LEU A 198 ? 0.5719 0.5812 0.5044 -0.0101 0.0284  -0.0134 199 LEU A N     
1551  C CA    . LEU A 198 ? 0.5995 0.6080 0.5337 -0.0080 0.0299  -0.0117 199 LEU A CA    
1552  C C     . LEU A 198 ? 0.6002 0.6135 0.5396 -0.0072 0.0286  -0.0111 199 LEU A C     
1553  O O     . LEU A 198 ? 0.5763 0.5891 0.5182 -0.0058 0.0300  -0.0107 199 LEU A O     
1554  C CB    . LEU A 198 ? 0.5905 0.5974 0.5205 -0.0059 0.0297  -0.0095 199 LEU A CB    
1555  C CG    . LEU A 198 ? 0.6482 0.6506 0.5729 -0.0065 0.0313  -0.0095 199 LEU A CG    
1556  C CD1   . LEU A 198 ? 0.6318 0.6323 0.5528 -0.0044 0.0311  -0.0069 199 LEU A CD1   
1557  C CD2   . LEU A 198 ? 0.6490 0.6476 0.5746 -0.0076 0.0342  -0.0107 199 LEU A CD2   
1558  N N     . ASP A 199 ? 0.5798 0.5979 0.5208 -0.0081 0.0260  -0.0110 200 ASP A N     
1559  C CA    . ASP A 199 ? 0.6037 0.6275 0.5498 -0.0076 0.0247  -0.0101 200 ASP A CA    
1560  C C     . ASP A 199 ? 0.5747 0.5998 0.5246 -0.0100 0.0248  -0.0117 200 ASP A C     
1561  O O     . ASP A 199 ? 0.5591 0.5895 0.5135 -0.0103 0.0236  -0.0110 200 ASP A O     
1562  C CB    . ASP A 199 ? 0.6736 0.7026 0.6198 -0.0073 0.0216  -0.0086 200 ASP A CB    
1563  C CG    . ASP A 199 ? 0.7567 0.7861 0.7011 -0.0102 0.0193  -0.0098 200 ASP A CG    
1564  O OD1   . ASP A 199 ? 0.8207 0.8463 0.7637 -0.0121 0.0202  -0.0120 200 ASP A OD1   
1565  O OD2   . ASP A 199 ? 0.8847 0.9184 0.8293 -0.0103 0.0164  -0.0086 200 ASP A OD2   
1566  N N     . HIS A 200 ? 0.5189 0.5395 0.4672 -0.0118 0.0262  -0.0138 201 HIS A N     
1567  C CA    . HIS A 200 ? 0.5383 0.5593 0.4900 -0.0140 0.0263  -0.0154 201 HIS A CA    
1568  C C     . HIS A 200 ? 0.4806 0.5028 0.4362 -0.0129 0.0280  -0.0148 201 HIS A C     
1569  O O     . HIS A 200 ? 0.4223 0.4411 0.3767 -0.0113 0.0302  -0.0147 201 HIS A O     
1570  C CB    . HIS A 200 ? 0.5319 0.5476 0.4808 -0.0156 0.0276  -0.0176 201 HIS A CB    
1571  C CG    . HIS A 200 ? 0.5099 0.5255 0.4620 -0.0178 0.0275  -0.0193 201 HIS A CG    
1572  N ND1   . HIS A 200 ? 0.4748 0.4920 0.4278 -0.0200 0.0249  -0.0201 201 HIS A ND1   
1573  C CD2   . HIS A 200 ? 0.4997 0.5135 0.4541 -0.0182 0.0294  -0.0201 201 HIS A CD2   
1574  C CE1   . HIS A 200 ? 0.4778 0.4942 0.4337 -0.0216 0.0253  -0.0214 201 HIS A CE1   
1575  N NE2   . HIS A 200 ? 0.4848 0.4993 0.4416 -0.0205 0.0281  -0.0214 201 HIS A NE2   
1576  N N     . GLU A 201 ? 0.4596 0.4866 0.4196 -0.0139 0.0267  -0.0144 202 GLU A N     
1577  C CA    . GLU A 201 ? 0.4855 0.5146 0.4492 -0.0128 0.0281  -0.0139 202 GLU A CA    
1578  C C     . GLU A 201 ? 0.4542 0.4789 0.4182 -0.0141 0.0301  -0.0157 202 GLU A C     
1579  O O     . GLU A 201 ? 0.4374 0.4612 0.4022 -0.0166 0.0294  -0.0170 202 GLU A O     
1580  C CB    . GLU A 201 ? 0.4949 0.5311 0.4632 -0.0138 0.0263  -0.0127 202 GLU A CB    
1581  C CG    . GLU A 201 ? 0.5683 0.6073 0.5400 -0.0125 0.0278  -0.0121 202 GLU A CG    
1582  C CD    . GLU A 201 ? 0.5945 0.6412 0.5710 -0.0136 0.0262  -0.0106 202 GLU A CD    
1583  O OE1   . GLU A 201 ? 0.5786 0.6305 0.5571 -0.0112 0.0265  -0.0089 202 GLU A OE1   
1584  O OE2   . GLU A 201 ? 0.5756 0.6231 0.5539 -0.0169 0.0248  -0.0110 202 GLU A OE2   
1585  N N     . VAL A 202 ? 0.4511 0.4727 0.4143 -0.0122 0.0323  -0.0158 203 VAL A N     
1586  C CA    . VAL A 202 ? 0.4487 0.4667 0.4127 -0.0131 0.0341  -0.0172 203 VAL A CA    
1587  C C     . VAL A 202 ? 0.4404 0.4610 0.4075 -0.0119 0.0348  -0.0167 203 VAL A C     
1588  O O     . VAL A 202 ? 0.4542 0.4794 0.4227 -0.0101 0.0342  -0.0153 203 VAL A O     
1589  C CB    . VAL A 202 ? 0.4786 0.4904 0.4389 -0.0123 0.0360  -0.0178 203 VAL A CB    
1590  C CG1   . VAL A 202 ? 0.5453 0.5546 0.5025 -0.0137 0.0357  -0.0186 203 VAL A CG1   
1591  C CG2   . VAL A 202 ? 0.4812 0.4920 0.4397 -0.0093 0.0366  -0.0164 203 VAL A CG2   
1592  N N     . VAL A 203 ? 0.4569 0.4749 0.4251 -0.0128 0.0362  -0.0179 204 VAL A N     
1593  C CA    . VAL A 203 ? 0.3971 0.4175 0.3680 -0.0120 0.0368  -0.0177 204 VAL A CA    
1594  C C     . VAL A 203 ? 0.3993 0.4144 0.3690 -0.0113 0.0387  -0.0188 204 VAL A C     
1595  O O     . VAL A 203 ? 0.4132 0.4245 0.3825 -0.0131 0.0394  -0.0200 204 VAL A O     
1596  C CB    . VAL A 203 ? 0.4028 0.4270 0.3773 -0.0146 0.0357  -0.0178 204 VAL A CB    
1597  C CG1   . VAL A 203 ? 0.4128 0.4396 0.3897 -0.0138 0.0366  -0.0175 204 VAL A CG1   
1598  C CG2   . VAL A 203 ? 0.4008 0.4303 0.3767 -0.0157 0.0335  -0.0166 204 VAL A CG2   
1599  N N     . ILE A 204 ? 0.3930 0.4079 0.3621 -0.0085 0.0396  -0.0183 205 ILE A N     
1600  C CA    . ILE A 204 ? 0.3917 0.4019 0.3599 -0.0079 0.0410  -0.0193 205 ILE A CA    
1601  C C     . ILE A 204 ? 0.3906 0.4038 0.3615 -0.0083 0.0412  -0.0197 205 ILE A C     
1602  O O     . ILE A 204 ? 0.3912 0.4090 0.3633 -0.0064 0.0410  -0.0189 205 ILE A O     
1603  C CB    . ILE A 204 ? 0.3954 0.4025 0.3608 -0.0046 0.0416  -0.0188 205 ILE A CB    
1604  C CG1   . ILE A 204 ? 0.4087 0.4129 0.3712 -0.0043 0.0414  -0.0181 205 ILE A CG1   
1605  C CG2   . ILE A 204 ? 0.3780 0.3800 0.3425 -0.0041 0.0427  -0.0199 205 ILE A CG2   
1606  C CD1   . ILE A 204 ? 0.4421 0.4430 0.4019 -0.0010 0.0416  -0.0173 205 ILE A CD1   
1607  N N     . TYR A 205 ? 0.3706 0.3815 0.3425 -0.0106 0.0415  -0.0209 206 TYR A N     
1608  C CA    . TYR A 205 ? 0.3897 0.4034 0.3642 -0.0115 0.0415  -0.0211 206 TYR A CA    
1609  C C     . TYR A 205 ? 0.3948 0.4041 0.3681 -0.0107 0.0427  -0.0222 206 TYR A C     
1610  O O     . TYR A 205 ? 0.4117 0.4155 0.3834 -0.0111 0.0433  -0.0230 206 TYR A O     
1611  C CB    . TYR A 205 ? 0.4080 0.4228 0.3848 -0.0148 0.0407  -0.0214 206 TYR A CB    
1612  C CG    . TYR A 205 ? 0.4375 0.4542 0.4167 -0.0161 0.0406  -0.0216 206 TYR A CG    
1613  C CD1   . TYR A 205 ? 0.4372 0.4600 0.4185 -0.0157 0.0401  -0.0204 206 TYR A CD1   
1614  C CD2   . TYR A 205 ? 0.4557 0.4685 0.4353 -0.0176 0.0411  -0.0229 206 TYR A CD2   
1615  C CE1   . TYR A 205 ? 0.4801 0.5048 0.4633 -0.0169 0.0400  -0.0203 206 TYR A CE1   
1616  C CE2   . TYR A 205 ? 0.4559 0.4703 0.4374 -0.0187 0.0409  -0.0229 206 TYR A CE2   
1617  C CZ    . TYR A 205 ? 0.4691 0.4894 0.4524 -0.0184 0.0404  -0.0216 206 TYR A CZ    
1618  O OH    . TYR A 205 ? 0.5149 0.5370 0.4999 -0.0196 0.0402  -0.0214 206 TYR A OH    
1619  N N     . GLU A 206 ? 0.3822 0.3944 0.3565 -0.0095 0.0428  -0.0222 207 GLU A N     
1620  C CA    . GLU A 206 ? 0.4278 0.4363 0.4011 -0.0089 0.0436  -0.0234 207 GLU A CA    
1621  C C     . GLU A 206 ? 0.4381 0.4511 0.4135 -0.0096 0.0434  -0.0232 207 GLU A C     
1622  O O     . GLU A 206 ? 0.5282 0.5461 0.5039 -0.0076 0.0435  -0.0225 207 GLU A O     
1623  C CB    . GLU A 206 ? 0.4311 0.4368 0.4013 -0.0054 0.0441  -0.0237 207 GLU A CB    
1624  C CG    . GLU A 206 ? 0.4572 0.4577 0.4250 -0.0048 0.0442  -0.0236 207 GLU A CG    
1625  C CD    . GLU A 206 ? 0.5063 0.5032 0.4710 -0.0013 0.0445  -0.0238 207 GLU A CD    
1626  O OE1   . GLU A 206 ? 0.6174 0.6159 0.5817 0.0010  0.0446  -0.0243 207 GLU A OE1   
1627  O OE2   . GLU A 206 ? 0.5205 0.5128 0.4830 -0.0007 0.0444  -0.0235 207 GLU A OE2   
1628  N N     . ALA A 207 ? 0.4278 0.4394 0.4047 -0.0123 0.0432  -0.0239 208 ALA A N     
1629  C CA    . ALA A 207 ? 0.4434 0.4586 0.4221 -0.0133 0.0429  -0.0236 208 ALA A CA    
1630  C C     . ALA A 207 ? 0.3988 0.4135 0.3755 -0.0106 0.0437  -0.0243 208 ALA A C     
1631  O O     . ALA A 207 ? 0.4345 0.4436 0.4086 -0.0093 0.0441  -0.0255 208 ALA A O     
1632  C CB    . ALA A 207 ? 0.4613 0.4739 0.4417 -0.0164 0.0425  -0.0243 208 ALA A CB    
1633  N N     . ALA A 208 ? 0.3840 0.4045 0.3617 -0.0100 0.0437  -0.0234 209 ALA A N     
1634  C CA    . ALA A 208 ? 0.3487 0.3694 0.3241 -0.0073 0.0444  -0.0242 209 ALA A CA    
1635  C C     . ALA A 208 ? 0.3018 0.3181 0.2766 -0.0088 0.0442  -0.0255 209 ALA A C     
1636  O O     . ALA A 208 ? 0.2862 0.3026 0.2632 -0.0119 0.0436  -0.0252 209 ALA A O     
1637  C CB    . ALA A 208 ? 0.3452 0.3743 0.3222 -0.0063 0.0447  -0.0226 209 ALA A CB    
1638  N N     . ASN A 209 ? 0.2725 0.2845 0.2439 -0.0064 0.0446  -0.0271 210 ASN A N     
1639  C CA    . ASN A 209 ? 0.2843 0.2920 0.2546 -0.0076 0.0443  -0.0285 210 ASN A CA    
1640  C C     . ASN A 209 ? 0.2837 0.2953 0.2528 -0.0061 0.0445  -0.0286 210 ASN A C     
1641  O O     . ASN A 209 ? 0.2800 0.2897 0.2485 -0.0073 0.0440  -0.0294 210 ASN A O     
1642  C CB    . ASN A 209 ? 0.3087 0.3084 0.2760 -0.0065 0.0442  -0.0302 210 ASN A CB    
1643  C CG    . ASN A 209 ? 0.3073 0.3033 0.2758 -0.0084 0.0440  -0.0299 210 ASN A CG    
1644  O OD1   . ASN A 209 ? 0.3265 0.3220 0.2976 -0.0116 0.0437  -0.0297 210 ASN A OD1   
1645  N ND2   . ASN A 209 ? 0.3254 0.3188 0.2921 -0.0065 0.0443  -0.0299 210 ASN A ND2   
1646  N N     . LEU A 210 ? 0.2884 0.3057 0.2570 -0.0033 0.0453  -0.0277 211 LEU A N     
1647  C CA    . LEU A 210 ? 0.3067 0.3285 0.2738 -0.0013 0.0458  -0.0277 211 LEU A CA    
1648  C C     . LEU A 210 ? 0.2851 0.3163 0.2555 -0.0022 0.0462  -0.0252 211 LEU A C     
1649  O O     . LEU A 210 ? 0.2716 0.3062 0.2444 -0.0026 0.0461  -0.0237 211 LEU A O     
1650  C CB    . LEU A 210 ? 0.3464 0.3665 0.3094 0.0036  0.0466  -0.0292 211 LEU A CB    
1651  C CG    . LEU A 210 ? 0.3831 0.3936 0.3422 0.0046  0.0460  -0.0318 211 LEU A CG    
1652  C CD1   . LEU A 210 ? 0.4131 0.4220 0.3679 0.0097  0.0466  -0.0332 211 LEU A CD1   
1653  C CD2   . LEU A 210 ? 0.3929 0.4005 0.3512 0.0023  0.0452  -0.0328 211 LEU A CD2   
1654  N N     . PRO A 211 ? 0.2657 0.3016 0.2362 -0.0026 0.0463  -0.0245 212 PRO A N     
1655  C CA    . PRO A 211 ? 0.2703 0.3153 0.2441 -0.0041 0.0465  -0.0217 212 PRO A CA    
1656  C C     . PRO A 211 ? 0.3243 0.3765 0.2984 -0.0008 0.0477  -0.0205 212 PRO A C     
1657  O O     . PRO A 211 ? 0.3246 0.3844 0.3022 -0.0022 0.0476  -0.0179 212 PRO A O     
1658  C CB    . PRO A 211 ? 0.2680 0.3149 0.2408 -0.0050 0.0465  -0.0215 212 PRO A CB    
1659  C CG    . PRO A 211 ? 0.2608 0.3019 0.2286 -0.0019 0.0469  -0.0244 212 PRO A CG    
1660  C CD    . PRO A 211 ? 0.2552 0.2878 0.2223 -0.0019 0.0463  -0.0262 212 PRO A CD    
1661  N N     . ILE A 212 ? 0.3360 0.3856 0.3064 0.0037  0.0486  -0.0224 213 ILE A N     
1662  C CA    . ILE A 212 ? 0.3620 0.4181 0.3324 0.0076  0.0498  -0.0215 213 ILE A CA    
1663  C C     . ILE A 212 ? 0.3693 0.4224 0.3403 0.0085  0.0494  -0.0216 213 ILE A C     
1664  O O     . ILE A 212 ? 0.3971 0.4547 0.3683 0.0119  0.0501  -0.0210 213 ILE A O     
1665  C CB    . ILE A 212 ? 0.4234 0.4792 0.3890 0.0125  0.0510  -0.0235 213 ILE A CB    
1666  C CG1   . ILE A 212 ? 0.4588 0.5033 0.4200 0.0141  0.0504  -0.0267 213 ILE A CG1   
1667  C CG2   . ILE A 212 ? 0.4491 0.5097 0.4140 0.0118  0.0515  -0.0229 213 ILE A CG2   
1668  C CD1   . ILE A 212 ? 0.4818 0.5215 0.4429 0.0155  0.0500  -0.0272 213 ILE A CD1   
1669  N N     . GLN A 213 ? 0.3792 0.4250 0.3507 0.0055  0.0482  -0.0224 214 GLN A N     
1670  C CA    . GLN A 213 ? 0.3759 0.4180 0.3475 0.0061  0.0478  -0.0226 214 GLN A CA    
1671  C C     . GLN A 213 ? 0.3784 0.4250 0.3544 0.0028  0.0470  -0.0203 214 GLN A C     
1672  O O     . GLN A 213 ? 0.3668 0.4143 0.3452 -0.0012 0.0462  -0.0194 214 GLN A O     
1673  C CB    . GLN A 213 ? 0.4104 0.4420 0.3796 0.0051  0.0472  -0.0247 214 GLN A CB    
1674  C CG    . GLN A 213 ? 0.4053 0.4323 0.3740 0.0056  0.0468  -0.0248 214 GLN A CG    
1675  C CD    . GLN A 213 ? 0.4313 0.4488 0.3982 0.0039  0.0462  -0.0265 214 GLN A CD    
1676  O OE1   . GLN A 213 ? 0.4364 0.4505 0.4026 0.0022  0.0460  -0.0276 214 GLN A OE1   
1677  N NE2   . GLN A 213 ? 0.4394 0.4528 0.4055 0.0043  0.0460  -0.0265 214 GLN A NE2   
1678  N N     . ALA A 214 ? 0.4385 0.4875 0.4152 0.0045  0.0469  -0.0193 215 ALA A N     
1679  C CA    . ALA A 214 ? 0.4561 0.5083 0.4363 0.0015  0.0458  -0.0175 215 ALA A CA    
1680  C C     . ALA A 214 ? 0.4332 0.4773 0.4123 0.0000  0.0451  -0.0186 215 ALA A C     
1681  O O     . ALA A 214 ? 0.4310 0.4690 0.4069 0.0025  0.0455  -0.0202 215 ALA A O     
1682  C CB    . ALA A 214 ? 0.4510 0.5111 0.4330 0.0040  0.0461  -0.0156 215 ALA A CB    
1683  N N     . PRO A 215 ? 0.4326 0.4762 0.4140 -0.0040 0.0439  -0.0179 216 PRO A N     
1684  C CA    . PRO A 215 ? 0.4665 0.5031 0.4468 -0.0053 0.0434  -0.0190 216 PRO A CA    
1685  C C     . PRO A 215 ? 0.4509 0.4877 0.4301 -0.0030 0.0432  -0.0184 216 PRO A C     
1686  O O     . PRO A 215 ? 0.5041 0.5475 0.4848 -0.0014 0.0431  -0.0169 216 PRO A O     
1687  C CB    . PRO A 215 ? 0.4681 0.5058 0.4513 -0.0097 0.0421  -0.0182 216 PRO A CB    
1688  C CG    . PRO A 215 ? 0.4538 0.5004 0.4400 -0.0103 0.0416  -0.0160 216 PRO A CG    
1689  C CD    . PRO A 215 ? 0.4384 0.4882 0.4236 -0.0073 0.0430  -0.0161 216 PRO A CD    
1690  N N     . ARG A 216 ? 0.4348 0.4644 0.4116 -0.0030 0.0432  -0.0196 217 ARG A N     
1691  C CA    . ARG A 216 ? 0.4093 0.4383 0.3850 -0.0012 0.0429  -0.0190 217 ARG A CA    
1692  C C     . ARG A 216 ? 0.3825 0.4125 0.3598 -0.0043 0.0417  -0.0182 217 ARG A C     
1693  O O     . ARG A 216 ? 0.3196 0.3454 0.2967 -0.0071 0.0415  -0.0190 217 ARG A O     
1694  C CB    . ARG A 216 ? 0.3952 0.4158 0.3671 0.0004  0.0435  -0.0204 217 ARG A CB    
1695  C CG    . ARG A 216 ? 0.4034 0.4228 0.3736 0.0024  0.0431  -0.0196 217 ARG A CG    
1696  C CD    . ARG A 216 ? 0.4240 0.4347 0.3906 0.0033  0.0435  -0.0206 217 ARG A CD    
1697  N NE    . ARG A 216 ? 0.4411 0.4506 0.4059 0.0052  0.0430  -0.0196 217 ARG A NE    
1698  C CZ    . ARG A 216 ? 0.4681 0.4705 0.4298 0.0058  0.0431  -0.0198 217 ARG A CZ    
1699  N NH1   . ARG A 216 ? 0.4724 0.4686 0.4328 0.0044  0.0436  -0.0210 217 ARG A NH1   
1700  N NH2   . ARG A 216 ? 0.4664 0.4682 0.4266 0.0076  0.0426  -0.0186 217 ARG A NH2   
1701  N N     . ILE A 217 ? 0.4112 0.4472 0.3900 -0.0037 0.0409  -0.0165 218 ILE A N     
1702  C CA    . ILE A 217 ? 0.4306 0.4677 0.4105 -0.0063 0.0394  -0.0158 218 ILE A CA    
1703  C C     . ILE A 217 ? 0.4795 0.5180 0.4582 -0.0039 0.0389  -0.0148 218 ILE A C     
1704  O O     . ILE A 217 ? 0.4464 0.4919 0.4274 -0.0034 0.0380  -0.0131 218 ILE A O     
1705  C CB    . ILE A 217 ? 0.4582 0.5018 0.4419 -0.0091 0.0382  -0.0145 218 ILE A CB    
1706  C CG1   . ILE A 217 ? 0.4253 0.4676 0.4101 -0.0112 0.0387  -0.0153 218 ILE A CG1   
1707  C CG2   . ILE A 217 ? 0.4925 0.5363 0.4770 -0.0120 0.0364  -0.0141 218 ILE A CG2   
1708  C CD1   . ILE A 217 ? 0.4503 0.4984 0.4388 -0.0142 0.0374  -0.0138 218 ILE A CD1   
1709  N N     . GLU A 218 ? 0.4858 0.5179 0.4611 -0.0026 0.0394  -0.0156 219 GLU A N     
1710  C CA    . GLU A 218 ? 0.5208 0.5531 0.4943 -0.0001 0.0389  -0.0146 219 GLU A CA    
1711  C C     . GLU A 218 ? 0.4934 0.5249 0.4663 -0.0024 0.0375  -0.0142 219 GLU A C     
1712  O O     . GLU A 218 ? 0.4097 0.4354 0.3805 -0.0041 0.0378  -0.0153 219 GLU A O     
1713  C CB    . GLU A 218 ? 0.5538 0.5794 0.5238 0.0028  0.0400  -0.0155 219 GLU A CB    
1714  C CG    . GLU A 218 ? 0.6050 0.6303 0.5729 0.0058  0.0394  -0.0143 219 GLU A CG    
1715  C CD    . GLU A 218 ? 0.6852 0.7035 0.6496 0.0087  0.0403  -0.0150 219 GLU A CD    
1716  O OE1   . GLU A 218 ? 0.6603 0.6743 0.6239 0.0085  0.0413  -0.0164 219 GLU A OE1   
1717  O OE2   . GLU A 218 ? 0.7527 0.7696 0.7151 0.0111  0.0397  -0.0140 219 GLU A OE2   
1718  N N     . ARG A 219 ? 0.5103 0.5481 0.4850 -0.0024 0.0360  -0.0126 220 ARG A N     
1719  C CA    . ARG A 219 ? 0.4966 0.5342 0.4704 -0.0044 0.0344  -0.0123 220 ARG A CA    
1720  C C     . ARG A 219 ? 0.4872 0.5231 0.4581 -0.0017 0.0341  -0.0114 220 ARG A C     
1721  O O     . ARG A 219 ? 0.4849 0.5241 0.4564 0.0016  0.0342  -0.0103 220 ARG A O     
1722  C CB    . ARG A 219 ? 0.5247 0.5699 0.5023 -0.0065 0.0324  -0.0109 220 ARG A CB    
1723  C CG    . ARG A 219 ? 0.5837 0.6307 0.5643 -0.0094 0.0324  -0.0114 220 ARG A CG    
1724  C CD    . ARG A 219 ? 0.6046 0.6593 0.5891 -0.0114 0.0304  -0.0096 220 ARG A CD    
1725  N NE    . ARG A 219 ? 0.6288 0.6850 0.6162 -0.0143 0.0303  -0.0098 220 ARG A NE    
1726  C CZ    . ARG A 219 ? 0.6727 0.7243 0.6596 -0.0173 0.0298  -0.0112 220 ARG A CZ    
1727  N NH1   . ARG A 219 ? 0.7187 0.7643 0.7023 -0.0180 0.0294  -0.0126 220 ARG A NH1   
1728  N NH2   . ARG A 219 ? 0.6327 0.6857 0.6222 -0.0196 0.0296  -0.0111 220 ARG A NH2   
1729  N N     . LEU A 220 ? 0.4863 0.5173 0.4541 -0.0029 0.0338  -0.0119 221 LEU A N     
1730  C CA    . LEU A 220 ? 0.4798 0.5086 0.4443 -0.0006 0.0335  -0.0110 221 LEU A CA    
1731  C C     . LEU A 220 ? 0.5026 0.5280 0.4641 -0.0029 0.0327  -0.0114 221 LEU A C     
1732  O O     . LEU A 220 ? 0.4632 0.4858 0.4244 -0.0057 0.0332  -0.0129 221 LEU A O     
1733  C CB    . LEU A 220 ? 0.5152 0.5383 0.4773 0.0021  0.0352  -0.0113 221 LEU A CB    
1734  C CG    . LEU A 220 ? 0.5004 0.5162 0.4603 0.0003  0.0367  -0.0129 221 LEU A CG    
1735  C CD1   . LEU A 220 ? 0.5303 0.5405 0.4879 0.0029  0.0380  -0.0130 221 LEU A CD1   
1736  C CD2   . LEU A 220 ? 0.4905 0.5074 0.4533 -0.0023 0.0373  -0.0143 221 LEU A CD2   
1737  N N     . PRO A 221 ? 0.4908 0.5163 0.4497 -0.0017 0.0315  -0.0102 222 PRO A N     
1738  C CA    . PRO A 221 ? 0.5152 0.5374 0.4705 -0.0035 0.0310  -0.0106 222 PRO A CA    
1739  C C     . PRO A 221 ? 0.5103 0.5252 0.4624 -0.0038 0.0331  -0.0116 222 PRO A C     
1740  O O     . PRO A 221 ? 0.4723 0.4839 0.4235 -0.0017 0.0344  -0.0111 222 PRO A O     
1741  C CB    . PRO A 221 ? 0.5075 0.5319 0.4610 -0.0014 0.0293  -0.0087 222 PRO A CB    
1742  C CG    . PRO A 221 ? 0.5282 0.5541 0.4832 0.0022  0.0299  -0.0074 222 PRO A CG    
1743  C CD    . PRO A 221 ? 0.5169 0.5459 0.4762 0.0017  0.0307  -0.0083 222 PRO A CD    
1744  N N     . LEU A 222 ? 0.5182 0.5306 0.4687 -0.0064 0.0333  -0.0129 223 LEU A N     
1745  C CA    . LEU A 222 ? 0.5455 0.5520 0.4934 -0.0071 0.0354  -0.0137 223 LEU A CA    
1746  C C     . LEU A 222 ? 0.5149 0.5176 0.4595 -0.0048 0.0361  -0.0121 223 LEU A C     
1747  O O     . LEU A 222 ? 0.5283 0.5264 0.4721 -0.0046 0.0379  -0.0123 223 LEU A O     
1748  C CB    . LEU A 222 ? 0.5776 0.5830 0.5233 -0.0095 0.0351  -0.0150 223 LEU A CB    
1749  C CG    . LEU A 222 ? 0.6157 0.6158 0.5588 -0.0104 0.0374  -0.0158 223 LEU A CG    
1750  C CD1   . LEU A 222 ? 0.6160 0.6147 0.5623 -0.0114 0.0389  -0.0171 223 LEU A CD1   
1751  C CD2   . LEU A 222 ? 0.6193 0.6190 0.5594 -0.0120 0.0371  -0.0168 223 LEU A CD2   
1752  N N     . ALA A 223 ? 0.4886 0.4934 0.4315 -0.0032 0.0345  -0.0105 224 ALA A N     
1753  C CA    . ALA A 223 ? 0.5030 0.5041 0.4422 -0.0012 0.0348  -0.0087 224 ALA A CA    
1754  C C     . ALA A 223 ? 0.4991 0.4976 0.4394 0.0013  0.0357  -0.0082 224 ALA A C     
1755  O O     . ALA A 223 ? 0.4517 0.4450 0.3892 0.0023  0.0365  -0.0072 224 ALA A O     
1756  C CB    . ALA A 223 ? 0.5460 0.5504 0.4836 0.0001  0.0326  -0.0071 224 ALA A CB    
1757  N N     . ASN A 224 ? 0.4900 0.4922 0.4343 0.0022  0.0355  -0.0088 225 ASN A N     
1758  C CA    . ASN A 224 ? 0.5098 0.5102 0.4549 0.0051  0.0360  -0.0085 225 ASN A CA    
1759  C C     . ASN A 224 ? 0.4977 0.4938 0.4436 0.0039  0.0379  -0.0100 225 ASN A C     
1760  O O     . ASN A 224 ? 0.5374 0.5311 0.4836 0.0061  0.0384  -0.0101 225 ASN A O     
1761  C CB    . ASN A 224 ? 0.5437 0.5509 0.4924 0.0072  0.0350  -0.0082 225 ASN A CB    
1762  C CG    . ASN A 224 ? 0.5631 0.5747 0.5114 0.0087  0.0330  -0.0064 225 ASN A CG    
1763  O OD1   . ASN A 224 ? 0.6341 0.6434 0.5790 0.0083  0.0324  -0.0054 225 ASN A OD1   
1764  N ND2   . ASN A 224 ? 0.5740 0.5923 0.5258 0.0106  0.0321  -0.0058 225 ASN A ND2   
1765  N N     . LEU A 225 ? 0.5419 0.5370 0.4880 0.0006  0.0387  -0.0112 226 LEU A N     
1766  C CA    . LEU A 225 ? 0.5057 0.4973 0.4528 -0.0008 0.0403  -0.0127 226 LEU A CA    
1767  C C     . LEU A 225 ? 0.5173 0.5023 0.4619 0.0005  0.0411  -0.0119 226 LEU A C     
1768  O O     . LEU A 225 ? 0.4705 0.4532 0.4162 0.0014  0.0416  -0.0127 226 LEU A O     
1769  C CB    . LEU A 225 ? 0.5269 0.5179 0.4739 -0.0042 0.0410  -0.0138 226 LEU A CB    
1770  C CG    . LEU A 225 ? 0.5534 0.5412 0.5018 -0.0059 0.0426  -0.0151 226 LEU A CG    
1771  C CD1   . LEU A 225 ? 0.5779 0.5689 0.5302 -0.0060 0.0424  -0.0164 226 LEU A CD1   
1772  C CD2   . LEU A 225 ? 0.5551 0.5420 0.5028 -0.0087 0.0435  -0.0159 226 LEU A CD2   
1773  N N     . PRO A 226 ? 0.4972 0.4787 0.4383 0.0007  0.0410  -0.0104 227 PRO A N     
1774  C CA    . PRO A 226 ? 0.5087 0.4833 0.4473 0.0014  0.0416  -0.0094 227 PRO A CA    
1775  C C     . PRO A 226 ? 0.4713 0.4439 0.4099 0.0049  0.0409  -0.0092 227 PRO A C     
1776  O O     . PRO A 226 ? 0.4692 0.4356 0.4064 0.0053  0.0412  -0.0091 227 PRO A O     
1777  C CB    . PRO A 226 ? 0.5136 0.4865 0.4483 0.0012  0.0413  -0.0074 227 PRO A CB    
1778  C CG    . PRO A 226 ? 0.5093 0.4875 0.4445 -0.0008 0.0412  -0.0080 227 PRO A CG    
1779  C CD    . PRO A 226 ? 0.4787 0.4626 0.4177 0.0000  0.0403  -0.0094 227 PRO A CD    
1780  N N     . GLN A 227 ? 0.4722 0.4500 0.4124 0.0074  0.0398  -0.0092 228 GLN A N     
1781  C CA    . GLN A 227 ? 0.5016 0.4782 0.4417 0.0114  0.0391  -0.0090 228 GLN A CA    
1782  C C     . GLN A 227 ? 0.4739 0.4539 0.4173 0.0119  0.0396  -0.0109 228 GLN A C     
1783  O O     . GLN A 227 ? 0.4533 0.4331 0.3969 0.0153  0.0393  -0.0112 228 GLN A O     
1784  C CB    . GLN A 227 ? 0.5881 0.5687 0.5277 0.0144  0.0377  -0.0074 228 GLN A CB    
1785  C CG    . GLN A 227 ? 0.6503 0.6267 0.5859 0.0148  0.0369  -0.0052 228 GLN A CG    
1786  C CD    . GLN A 227 ? 0.6737 0.6508 0.6080 0.0111  0.0373  -0.0047 228 GLN A CD    
1787  O OE1   . GLN A 227 ? 0.7424 0.7256 0.6782 0.0098  0.0368  -0.0050 228 GLN A OE1   
1788  N NE2   . GLN A 227 ? 0.7479 0.7188 0.6792 0.0094  0.0381  -0.0039 228 GLN A NE2   
1789  N N     . ALA A 228 ? 0.4067 0.3899 0.3526 0.0087  0.0403  -0.0122 229 ALA A N     
1790  C CA    . ALA A 228 ? 0.4072 0.3943 0.3564 0.0088  0.0407  -0.0137 229 ALA A CA    
1791  C C     . ALA A 228 ? 0.4447 0.4259 0.3931 0.0091  0.0415  -0.0150 229 ALA A C     
1792  O O     . ALA A 228 ? 0.4518 0.4263 0.3978 0.0081  0.0418  -0.0148 229 ALA A O     
1793  C CB    . ALA A 228 ? 0.4246 0.4161 0.3764 0.0052  0.0410  -0.0144 229 ALA A CB    
1794  N N     . HIS A 229 ? 0.4771 0.4613 0.4275 0.0105  0.0417  -0.0163 230 HIS A N     
1795  C CA    . HIS A 229 ? 0.5190 0.4982 0.4687 0.0108  0.0423  -0.0178 230 HIS A CA    
1796  C C     . HIS A 229 ? 0.5078 0.4880 0.4598 0.0069  0.0430  -0.0190 230 HIS A C     
1797  O O     . HIS A 229 ? 0.5710 0.5572 0.5258 0.0062  0.0432  -0.0195 230 HIS A O     
1798  C CB    . HIS A 229 ? 0.5940 0.5755 0.5439 0.0148  0.0421  -0.0185 230 HIS A CB    
1799  C CG    . HIS A 229 ? 0.6264 0.6029 0.5752 0.0154  0.0425  -0.0204 230 HIS A CG    
1800  N ND1   . HIS A 229 ? 0.7009 0.6688 0.6462 0.0170  0.0420  -0.0207 230 HIS A ND1   
1801  C CD2   . HIS A 229 ? 0.6340 0.6123 0.5843 0.0144  0.0430  -0.0219 230 HIS A CD2   
1802  C CE1   . HIS A 229 ? 0.7235 0.6883 0.6682 0.0170  0.0421  -0.0225 230 HIS A CE1   
1803  N NE2   . HIS A 229 ? 0.6529 0.6240 0.6006 0.0155  0.0428  -0.0233 230 HIS A NE2   
1804  N N     . LEU A 230 ? 0.5065 0.4807 0.4573 0.0044  0.0434  -0.0192 231 LEU A N     
1805  C CA    . LEU A 230 ? 0.5102 0.4850 0.4632 0.0008  0.0441  -0.0202 231 LEU A CA    
1806  C C     . LEU A 230 ? 0.5111 0.4812 0.4637 0.0006  0.0443  -0.0216 231 LEU A C     
1807  O O     . LEU A 230 ? 0.5332 0.4974 0.4832 0.0023  0.0439  -0.0216 231 LEU A O     
1808  C CB    . LEU A 230 ? 0.5047 0.4776 0.4571 -0.0022 0.0446  -0.0194 231 LEU A CB    
1809  C CG    . LEU A 230 ? 0.4813 0.4587 0.4338 -0.0024 0.0443  -0.0183 231 LEU A CG    
1810  C CD1   . LEU A 230 ? 0.4804 0.4559 0.4321 -0.0052 0.0450  -0.0178 231 LEU A CD1   
1811  C CD2   . LEU A 230 ? 0.4834 0.4679 0.4390 -0.0028 0.0439  -0.0189 231 LEU A CD2   
1812  N N     . MET A 231 ? 0.4813 0.4540 0.4365 -0.0015 0.0446  -0.0228 232 MET A N     
1813  C CA    . MET A 231 ? 0.4652 0.4339 0.4203 -0.0022 0.0447  -0.0242 232 MET A CA    
1814  C C     . MET A 231 ? 0.4108 0.3795 0.3682 -0.0062 0.0452  -0.0245 232 MET A C     
1815  O O     . MET A 231 ? 0.4029 0.3757 0.3622 -0.0079 0.0455  -0.0240 232 MET A O     
1816  C CB    . MET A 231 ? 0.5124 0.4845 0.4682 -0.0002 0.0445  -0.0254 232 MET A CB    
1817  C CG    . MET A 231 ? 0.5950 0.5667 0.5484 0.0042  0.0441  -0.0254 232 MET A CG    
1818  S SD    . MET A 231 ? 0.7070 0.6685 0.6561 0.0060  0.0433  -0.0258 232 MET A SD    
1819  C CE    . MET A 231 ? 0.7449 0.7024 0.6943 0.0035  0.0432  -0.0276 232 MET A CE    
1820  N N     . PRO A 232 ? 0.4538 0.4181 0.4112 -0.0077 0.0451  -0.0253 233 PRO A N     
1821  C CA    . PRO A 232 ? 0.4692 0.4338 0.4291 -0.0113 0.0456  -0.0256 233 PRO A CA    
1822  C C     . PRO A 232 ? 0.5144 0.4853 0.4774 -0.0125 0.0459  -0.0261 233 PRO A C     
1823  O O     . PRO A 232 ? 0.4958 0.4682 0.4607 -0.0148 0.0464  -0.0259 233 PRO A O     
1824  C CB    . PRO A 232 ? 0.4701 0.4298 0.4295 -0.0119 0.0451  -0.0266 233 PRO A CB    
1825  C CG    . PRO A 232 ? 0.4674 0.4218 0.4231 -0.0092 0.0444  -0.0265 233 PRO A CG    
1826  C CD    . PRO A 232 ? 0.4769 0.4354 0.4317 -0.0060 0.0444  -0.0261 233 PRO A CD    
1827  N N     . ILE A 233 ? 0.5407 0.5152 0.5042 -0.0107 0.0454  -0.0266 234 ILE A N     
1828  C CA    . ILE A 233 ? 0.5877 0.5678 0.5541 -0.0120 0.0454  -0.0269 234 ILE A CA    
1829  C C     . ILE A 233 ? 0.5416 0.5265 0.5087 -0.0116 0.0453  -0.0259 234 ILE A C     
1830  O O     . ILE A 233 ? 0.6108 0.6006 0.5801 -0.0123 0.0450  -0.0258 234 ILE A O     
1831  C CB    . ILE A 233 ? 0.6527 0.6346 0.6193 -0.0106 0.0450  -0.0277 234 ILE A CB    
1832  C CG1   . ILE A 233 ? 0.6840 0.6680 0.6487 -0.0070 0.0449  -0.0273 234 ILE A CG1   
1833  C CG2   . ILE A 233 ? 0.6933 0.6702 0.6590 -0.0112 0.0447  -0.0288 234 ILE A CG2   
1834  C CD1   . ILE A 233 ? 0.7619 0.7487 0.7265 -0.0054 0.0448  -0.0280 234 ILE A CD1   
1835  N N     . SER A 234 ? 0.5048 0.4880 0.4699 -0.0106 0.0454  -0.0250 235 SER A N     
1836  C CA    . SER A 234 ? 0.4819 0.4695 0.4473 -0.0102 0.0451  -0.0240 235 SER A CA    
1837  C C     . SER A 234 ? 0.4525 0.4409 0.4192 -0.0129 0.0453  -0.0241 235 SER A C     
1838  O O     . SER A 234 ? 0.5213 0.5062 0.4873 -0.0143 0.0459  -0.0242 235 SER A O     
1839  C CB    . SER A 234 ? 0.5013 0.4869 0.4638 -0.0079 0.0450  -0.0230 235 SER A CB    
1840  O OG    . SER A 234 ? 0.4812 0.4665 0.4425 -0.0048 0.0448  -0.0231 235 SER A OG    
1841  N N     . THR A 235 ? 0.4741 0.4675 0.4427 -0.0137 0.0446  -0.0240 236 THR A N     
1842  C CA    . THR A 235 ? 0.4216 0.4158 0.3910 -0.0158 0.0444  -0.0242 236 THR A CA    
1843  C C     . THR A 235 ? 0.4105 0.4077 0.3789 -0.0151 0.0435  -0.0233 236 THR A C     
1844  O O     . THR A 235 ? 0.3862 0.3873 0.3554 -0.0138 0.0427  -0.0225 236 THR A O     
1845  C CB    . THR A 235 ? 0.4348 0.4314 0.4074 -0.0178 0.0439  -0.0250 236 THR A CB    
1846  O OG1   . THR A 235 ? 0.4986 0.4925 0.4719 -0.0182 0.0446  -0.0257 236 THR A OG1   
1847  C CG2   . THR A 235 ? 0.4287 0.4255 0.4020 -0.0198 0.0436  -0.0256 236 THR A CG2   
1848  N N     . LEU A 236 ? 0.3933 0.3891 0.3601 -0.0158 0.0437  -0.0233 237 LEU A N     
1849  C CA    . LEU A 236 ? 0.3349 0.3331 0.3003 -0.0153 0.0427  -0.0225 237 LEU A CA    
1850  C C     . LEU A 236 ? 0.3444 0.3451 0.3114 -0.0173 0.0416  -0.0232 237 LEU A C     
1851  O O     . LEU A 236 ? 0.3075 0.3062 0.2743 -0.0189 0.0421  -0.0243 237 LEU A O     
1852  C CB    . LEU A 236 ? 0.3192 0.3140 0.2810 -0.0147 0.0435  -0.0219 237 LEU A CB    
1853  C CG    . LEU A 236 ? 0.3078 0.3047 0.2676 -0.0142 0.0424  -0.0211 237 LEU A CG    
1854  C CD1   . LEU A 236 ? 0.3083 0.3088 0.2687 -0.0122 0.0412  -0.0199 237 LEU A CD1   
1855  C CD2   . LEU A 236 ? 0.3230 0.3165 0.2791 -0.0138 0.0433  -0.0205 237 LEU A CD2   
1856  N N     . LEU A 237 ? 0.3447 0.3499 0.3131 -0.0173 0.0400  -0.0226 238 LEU A N     
1857  C CA    . LEU A 237 ? 0.3735 0.3809 0.3433 -0.0193 0.0385  -0.0231 238 LEU A CA    
1858  C C     . LEU A 237 ? 0.4451 0.4535 0.4124 -0.0190 0.0373  -0.0225 238 LEU A C     
1859  O O     . LEU A 237 ? 0.4670 0.4782 0.4340 -0.0175 0.0366  -0.0211 238 LEU A O     
1860  C CB    . LEU A 237 ? 0.3913 0.4030 0.3645 -0.0201 0.0372  -0.0225 238 LEU A CB    
1861  C CG    . LEU A 237 ? 0.4004 0.4146 0.3751 -0.0223 0.0350  -0.0226 238 LEU A CG    
1862  C CD1   . LEU A 237 ? 0.3962 0.4069 0.3713 -0.0242 0.0350  -0.0243 238 LEU A CD1   
1863  C CD2   . LEU A 237 ? 0.3986 0.4182 0.3767 -0.0228 0.0338  -0.0211 238 LEU A CD2   
1864  N N     . ILE A 238 ? 0.4715 0.4777 0.4370 -0.0202 0.0370  -0.0237 239 ILE A N     
1865  C CA    . ILE A 238 ? 0.4819 0.4887 0.4446 -0.0201 0.0357  -0.0235 239 ILE A CA    
1866  C C     . ILE A 238 ? 0.4464 0.4550 0.4106 -0.0222 0.0334  -0.0244 239 ILE A C     
1867  O O     . ILE A 238 ? 0.4564 0.4623 0.4200 -0.0234 0.0334  -0.0261 239 ILE A O     
1868  C CB    . ILE A 238 ? 0.5052 0.5082 0.4640 -0.0196 0.0372  -0.0242 239 ILE A CB    
1869  C CG1   . ILE A 238 ? 0.5219 0.5226 0.4795 -0.0179 0.0392  -0.0231 239 ILE A CG1   
1870  C CG2   . ILE A 238 ? 0.4718 0.4753 0.4272 -0.0195 0.0357  -0.0241 239 ILE A CG2   
1871  C CD1   . ILE A 238 ? 0.5345 0.5317 0.4884 -0.0177 0.0408  -0.0233 239 ILE A CD1   
1872  N N     . PRO A 239 ? 0.4205 0.4335 0.3866 -0.0226 0.0312  -0.0231 240 PRO A N     
1873  C CA    . PRO A 239 ? 0.3886 0.4030 0.3562 -0.0250 0.0286  -0.0236 240 PRO A CA    
1874  C C     . PRO A 239 ? 0.3484 0.3602 0.3122 -0.0256 0.0273  -0.0250 240 PRO A C     
1875  O O     . PRO A 239 ? 0.2997 0.3099 0.2598 -0.0241 0.0283  -0.0251 240 PRO A O     
1876  C CB    . PRO A 239 ? 0.3831 0.4035 0.3533 -0.0250 0.0268  -0.0214 240 PRO A CB    
1877  C CG    . PRO A 239 ? 0.4186 0.4405 0.3895 -0.0225 0.0290  -0.0201 240 PRO A CG    
1878  C CD    . PRO A 239 ? 0.4205 0.4374 0.3875 -0.0209 0.0311  -0.0210 240 PRO A CD    
1879  N N     . PRO A 240 ? 0.3348 0.3460 0.2992 -0.0277 0.0250  -0.0262 241 PRO A N     
1880  C CA    . PRO A 240 ? 0.3471 0.3556 0.3075 -0.0282 0.0234  -0.0278 241 PRO A CA    
1881  C C     . PRO A 240 ? 0.3488 0.3593 0.3062 -0.0271 0.0225  -0.0266 241 PRO A C     
1882  O O     . PRO A 240 ? 0.3674 0.3824 0.3269 -0.0269 0.0215  -0.0245 241 PRO A O     
1883  C CB    . PRO A 240 ? 0.3471 0.3559 0.3097 -0.0308 0.0202  -0.0284 241 PRO A CB    
1884  C CG    . PRO A 240 ? 0.3579 0.3674 0.3251 -0.0316 0.0212  -0.0279 241 PRO A CG    
1885  C CD    . PRO A 240 ? 0.3592 0.3719 0.3279 -0.0298 0.0236  -0.0259 241 PRO A CD    
1886  N N     . ALA A 241 ? 0.3879 0.3952 0.3403 -0.0263 0.0229  -0.0281 242 ALA A N     
1887  C CA    . ALA A 241 ? 0.3918 0.4005 0.3406 -0.0255 0.0216  -0.0271 242 ALA A CA    
1888  C C     . ALA A 241 ? 0.4322 0.4406 0.3793 -0.0273 0.0180  -0.0283 242 ALA A C     
1889  O O     . ALA A 241 ? 0.4315 0.4426 0.3776 -0.0275 0.0156  -0.0271 242 ALA A O     
1890  C CB    . ALA A 241 ? 0.4086 0.4143 0.3527 -0.0235 0.0243  -0.0276 242 ALA A CB    
1891  N N     . LYS A 242 ? 0.4623 0.4671 0.4089 -0.0285 0.0173  -0.0308 243 LYS A N     
1892  C CA    . LYS A 242 ? 0.5694 0.5728 0.5144 -0.0304 0.0136  -0.0323 243 LYS A CA    
1893  C C     . LYS A 242 ? 0.6243 0.6274 0.5739 -0.0327 0.0119  -0.0327 243 LYS A C     
1894  O O     . LYS A 242 ? 0.5836 0.5867 0.5367 -0.0326 0.0140  -0.0324 243 LYS A O     
1895  C CB    . LYS A 242 ? 0.5706 0.5690 0.5097 -0.0296 0.0139  -0.0354 243 LYS A CB    
1896  C CG    . LYS A 242 ? 0.5971 0.5949 0.5310 -0.0273 0.0162  -0.0353 243 LYS A CG    
1897  C CD    . LYS A 242 ? 0.6371 0.6302 0.5659 -0.0263 0.0174  -0.0385 243 LYS A CD    
1898  C CE    . LYS A 242 ? 0.6312 0.6220 0.5632 -0.0265 0.0191  -0.0400 243 LYS A CE    
1899  N NZ    . LYS A 242 ? 0.6908 0.6772 0.6190 -0.0261 0.0187  -0.0435 243 LYS A NZ    
1900  N N     . LYS A 243 ? 0.6770 0.6793 0.6263 -0.0350 0.0078  -0.0335 244 LYS A N     
1901  C CA    . LYS A 243 ? 0.6981 0.6991 0.6511 -0.0374 0.0057  -0.0340 244 LYS A CA    
1902  C C     . LYS A 243 ? 0.6695 0.6638 0.6190 -0.0371 0.0056  -0.0376 244 LYS A C     
1903  O O     . LYS A 243 ? 0.6732 0.6647 0.6176 -0.0351 0.0072  -0.0396 244 LYS A O     
1904  C CB    . LYS A 243 ? 0.7711 0.7747 0.7259 -0.0403 0.0010  -0.0326 244 LYS A CB    
1905  C CG    . LYS A 243 ? 0.7901 0.8006 0.7469 -0.0402 0.0005  -0.0293 244 LYS A CG    
1906  C CD    . LYS A 243 ? 0.7712 0.7844 0.7295 -0.0432 -0.0043 -0.0280 244 LYS A CD    
1907  C CE    . LYS A 243 ? 0.7613 0.7718 0.7220 -0.0464 -0.0074 -0.0287 244 LYS A CE    
1908  N NZ    . LYS A 243 ? 0.7110 0.7141 0.6665 -0.0468 -0.0095 -0.0324 244 LYS A NZ    
1909  N N     . LEU A 244 ? 0.6984 0.6904 0.6509 -0.0391 0.0037  -0.0383 245 LEU A N     
1910  C CA    . LEU A 244 ? 0.7078 0.6933 0.6576 -0.0386 0.0034  -0.0418 245 LEU A CA    
1911  C C     . LEU A 244 ? 0.7130 0.6948 0.6578 -0.0393 -0.0004 -0.0441 245 LEU A C     
1912  O O     . LEU A 244 ? 0.6539 0.6359 0.6001 -0.0421 -0.0046 -0.0433 245 LEU A O     
1913  C CB    . LEU A 244 ? 0.7200 0.7044 0.6748 -0.0405 0.0024  -0.0414 245 LEU A CB    
1914  C CG    . LEU A 244 ? 0.6966 0.6844 0.6562 -0.0399 0.0059  -0.0393 245 LEU A CG    
1915  C CD1   . LEU A 244 ? 0.7241 0.7114 0.6886 -0.0422 0.0043  -0.0384 245 LEU A CD1   
1916  C CD2   . LEU A 244 ? 0.6773 0.6631 0.6348 -0.0369 0.0102  -0.0410 245 LEU A CD2   
1917  N N     . GLU A 245 ? 0.7693 0.7477 0.7081 -0.0369 0.0012  -0.0469 246 GLU A N     
1918  C CA    . GLU A 245 ? 0.7770 0.7510 0.7101 -0.0370 -0.0022 -0.0498 246 GLU A CA    
1919  C C     . GLU A 245 ? 0.7949 0.7624 0.7271 -0.0368 -0.0032 -0.0532 246 GLU A C     
1920  O O     . GLU A 245 ? 0.8077 0.7741 0.7417 -0.0353 -0.0001 -0.0539 246 GLU A O     
1921  C CB    . GLU A 245 ? 0.7870 0.7610 0.7136 -0.0343 0.0000  -0.0510 246 GLU A CB    
1922  C CG    . GLU A 245 ? 0.7960 0.7756 0.7226 -0.0346 -0.0001 -0.0478 246 GLU A CG    
1923  C CD    . GLU A 245 ? 0.8060 0.7856 0.7262 -0.0319 0.0021  -0.0486 246 GLU A CD    
1924  O OE1   . GLU A 245 ? 0.8088 0.7886 0.7249 -0.0324 -0.0007 -0.0488 246 GLU A OE1   
1925  O OE2   . GLU A 245 ? 0.8684 0.8480 0.7877 -0.0296 0.0065  -0.0489 246 GLU A OE2   
1926  N N     . TYR A 246 ? 0.7701 0.7330 0.6993 -0.0383 -0.0079 -0.0553 247 TYR A N     
1927  C CA    . TYR A 246 ? 0.7605 0.7166 0.6887 -0.0382 -0.0098 -0.0585 247 TYR A CA    
1928  C C     . TYR A 246 ? 0.7037 0.6561 0.6261 -0.0342 -0.0067 -0.0623 247 TYR A C     
1929  O O     . TYR A 246 ? 0.7058 0.6595 0.6231 -0.0323 -0.0051 -0.0631 247 TYR A O     
1930  C CB    . TYR A 246 ? 0.7728 0.7245 0.6992 -0.0411 -0.0160 -0.0597 247 TYR A CB    
1931  C CG    . TYR A 246 ? 0.8081 0.7628 0.7410 -0.0453 -0.0194 -0.0560 247 TYR A CG    
1932  C CD1   . TYR A 246 ? 0.8076 0.7608 0.7458 -0.0469 -0.0199 -0.0552 247 TYR A CD1   
1933  C CD2   . TYR A 246 ? 0.8104 0.7697 0.7443 -0.0479 -0.0221 -0.0533 247 TYR A CD2   
1934  C CE1   . TYR A 246 ? 0.7987 0.7551 0.7428 -0.0508 -0.0228 -0.0516 247 TYR A CE1   
1935  C CE2   . TYR A 246 ? 0.7408 0.7036 0.6808 -0.0518 -0.0250 -0.0498 247 TYR A CE2   
1936  C CZ    . TYR A 246 ? 0.7898 0.7512 0.7349 -0.0533 -0.0252 -0.0489 247 TYR A CZ    
1937  O OH    . TYR A 246 ? 0.7795 0.7448 0.7307 -0.0573 -0.0279 -0.0451 247 TYR A OH    
1938  N N     . ASN A 247 ? 0.6893 0.6374 0.6127 -0.0330 -0.0059 -0.0646 248 ASN A N     
1939  C CA    . ASN A 247 ? 0.6806 0.6255 0.5992 -0.0291 -0.0030 -0.0683 248 ASN A CA    
1940  C C     . ASN A 247 ? 0.6620 0.5990 0.5760 -0.0287 -0.0071 -0.0726 248 ASN A C     
1941  O O     . ASN A 247 ? 0.6410 0.5737 0.5570 -0.0283 -0.0079 -0.0742 248 ASN A O     
1942  C CB    . ASN A 247 ? 0.6500 0.5965 0.5731 -0.0274 0.0014  -0.0678 248 ASN A CB    
1943  C CG    . ASN A 247 ? 0.6768 0.6219 0.5955 -0.0233 0.0051  -0.0709 248 ASN A CG    
1944  O OD1   . ASN A 247 ? 0.7477 0.6907 0.6596 -0.0215 0.0047  -0.0736 248 ASN A OD1   
1945  N ND2   . ASN A 247 ? 0.7050 0.6517 0.6275 -0.0218 0.0089  -0.0706 248 ASN A ND2   
1946  N N     . TYR A 248 ? 0.6474 0.5823 0.5549 -0.0287 -0.0098 -0.0744 249 TYR A N     
1947  C CA    . TYR A 248 ? 0.6231 0.5501 0.5258 -0.0287 -0.0146 -0.0784 249 TYR A CA    
1948  C C     . TYR A 248 ? 0.6173 0.5395 0.5168 -0.0246 -0.0123 -0.0826 249 TYR A C     
1949  O O     . TYR A 248 ? 0.5822 0.4976 0.4813 -0.0245 -0.0155 -0.0854 249 TYR A O     
1950  C CB    . TYR A 248 ? 0.6096 0.5360 0.5053 -0.0290 -0.0173 -0.0795 249 TYR A CB    
1951  C CG    . TYR A 248 ? 0.6159 0.5471 0.5147 -0.0330 -0.0201 -0.0754 249 TYR A CG    
1952  C CD1   . TYR A 248 ? 0.6251 0.5539 0.5272 -0.0371 -0.0256 -0.0743 249 TYR A CD1   
1953  C CD2   . TYR A 248 ? 0.6352 0.5733 0.5338 -0.0327 -0.0173 -0.0725 249 TYR A CD2   
1954  C CE1   . TYR A 248 ? 0.6376 0.5715 0.5430 -0.0407 -0.0281 -0.0704 249 TYR A CE1   
1955  C CE2   . TYR A 248 ? 0.6807 0.6235 0.5824 -0.0360 -0.0198 -0.0688 249 TYR A CE2   
1956  C CZ    . TYR A 248 ? 0.6473 0.5883 0.5525 -0.0400 -0.0252 -0.0677 249 TYR A CZ    
1957  O OH    . TYR A 248 ? 0.6598 0.6063 0.5684 -0.0432 -0.0276 -0.0639 249 TYR A OH    
1958  N N     . ALA A 249 ? 0.6380 0.5640 0.5355 -0.0211 -0.0067 -0.0831 250 ALA A N     
1959  C CA    . ALA A 249 ? 0.6524 0.5753 0.5467 -0.0168 -0.0040 -0.0870 250 ALA A CA    
1960  C C     . ALA A 249 ? 0.6167 0.5360 0.5166 -0.0169 -0.0048 -0.0876 250 ALA A C     
1961  O O     . ALA A 249 ? 0.6398 0.5524 0.5367 -0.0149 -0.0069 -0.0916 250 ALA A O     
1962  C CB    . ALA A 249 ? 0.6807 0.6099 0.5747 -0.0140 0.0025  -0.0858 250 ALA A CB    
1963  N N     . ILE A 250 ? 0.6385 0.5622 0.5463 -0.0192 -0.0034 -0.0835 251 ILE A N     
1964  C CA    . ILE A 250 ? 0.6235 0.5449 0.5370 -0.0193 -0.0036 -0.0834 251 ILE A CA    
1965  C C     . ILE A 250 ? 0.5684 0.4837 0.4832 -0.0227 -0.0100 -0.0836 251 ILE A C     
1966  O O     . ILE A 250 ? 0.5261 0.4353 0.4414 -0.0218 -0.0121 -0.0860 251 ILE A O     
1967  C CB    . ILE A 250 ? 0.6396 0.5679 0.5606 -0.0205 0.0002  -0.0791 251 ILE A CB    
1968  C CG1   . ILE A 250 ? 0.6876 0.6215 0.6073 -0.0175 0.0062  -0.0788 251 ILE A CG1   
1969  C CG2   . ILE A 250 ? 0.6255 0.5514 0.5524 -0.0209 -0.0005 -0.0788 251 ILE A CG2   
1970  C CD1   . ILE A 250 ? 0.7602 0.6917 0.6768 -0.0130 0.0089  -0.0826 251 ILE A CD1   
1971  N N     . LEU A 251 ? 0.6146 0.5318 0.5301 -0.0266 -0.0131 -0.0809 252 LEU A N     
1972  C CA    . LEU A 251 ? 0.6102 0.5225 0.5271 -0.0304 -0.0193 -0.0804 252 LEU A CA    
1973  C C     . LEU A 251 ? 0.6054 0.5083 0.5158 -0.0286 -0.0232 -0.0856 252 LEU A C     
1974  O O     . LEU A 251 ? 0.5819 0.4783 0.4938 -0.0299 -0.0272 -0.0866 252 LEU A O     
1975  C CB    . LEU A 251 ? 0.5878 0.5043 0.5053 -0.0343 -0.0218 -0.0771 252 LEU A CB    
1976  C CG    . LEU A 251 ? 0.5533 0.4787 0.4776 -0.0363 -0.0188 -0.0719 252 LEU A CG    
1977  C CD1   . LEU A 251 ? 0.5518 0.4813 0.4763 -0.0397 -0.0216 -0.0690 252 LEU A CD1   
1978  C CD2   . LEU A 251 ? 0.5388 0.4642 0.4704 -0.0383 -0.0193 -0.0695 252 LEU A CD2   
1979  N N     . ALA A 252 ? 0.6312 0.5332 0.5341 -0.0255 -0.0219 -0.0889 253 ALA A N     
1980  C CA    . ALA A 252 ? 0.6709 0.5640 0.5663 -0.0233 -0.0254 -0.0942 253 ALA A CA    
1981  C C     . ALA A 252 ? 0.6495 0.5377 0.5458 -0.0198 -0.0241 -0.0973 253 ALA A C     
1982  O O     . ALA A 252 ? 0.6235 0.5030 0.5181 -0.0199 -0.0287 -0.1001 253 ALA A O     
1983  C CB    . ALA A 252 ? 0.6576 0.5522 0.5449 -0.0203 -0.0233 -0.0968 253 ALA A CB    
1984  N N     . LYS A 253 ? 0.6551 0.5487 0.5540 -0.0167 -0.0180 -0.0967 254 LYS A N     
1985  C CA    . LYS A 253 ? 0.6760 0.5664 0.5767 -0.0132 -0.0162 -0.0991 254 LYS A CA    
1986  C C     . LYS A 253 ? 0.6957 0.5826 0.6030 -0.0164 -0.0198 -0.0970 254 LYS A C     
1987  O O     . LYS A 253 ? 0.6809 0.5610 0.5882 -0.0145 -0.0217 -0.0997 254 LYS A O     
1988  C CB    . LYS A 253 ? 0.7033 0.6015 0.6066 -0.0101 -0.0091 -0.0978 254 LYS A CB    
1989  C CG    . LYS A 253 ? 0.7088 0.6097 0.6052 -0.0060 -0.0052 -0.1004 254 LYS A CG    
1990  C CD    . LYS A 253 ? 0.7678 0.6769 0.6676 -0.0037 0.0017  -0.0985 254 LYS A CD    
1991  C CE    . LYS A 253 ? 0.8108 0.7220 0.7036 0.0006  0.0056  -0.1014 254 LYS A CE    
1992  N NZ    . LYS A 253 ? 0.8257 0.7375 0.7122 -0.0006 0.0042  -0.1013 254 LYS A NZ    
1993  N N     . LEU A 254 ? 0.7346 0.6264 0.6477 -0.0211 -0.0206 -0.0919 255 LEU A N     
1994  C CA    . LEU A 254 ? 0.7434 0.6327 0.6628 -0.0248 -0.0241 -0.0893 255 LEU A CA    
1995  C C     . LEU A 254 ? 0.7800 0.6609 0.6963 -0.0276 -0.0313 -0.0908 255 LEU A C     
1996  O O     . LEU A 254 ? 0.7996 0.6761 0.7197 -0.0303 -0.0352 -0.0895 255 LEU A O     
1997  C CB    . LEU A 254 ? 0.7057 0.6037 0.6318 -0.0286 -0.0222 -0.0835 255 LEU A CB    
1998  C CG    . LEU A 254 ? 0.6982 0.6037 0.6284 -0.0264 -0.0158 -0.0815 255 LEU A CG    
1999  C CD1   . LEU A 254 ? 0.6522 0.5654 0.5884 -0.0301 -0.0146 -0.0761 255 LEU A CD1   
2000  C CD2   . LEU A 254 ? 0.7012 0.6038 0.6347 -0.0240 -0.0146 -0.0828 255 LEU A CD2   
2001  N N     . GLY A 255 ? 0.7804 0.6592 0.6896 -0.0271 -0.0331 -0.0934 256 GLY A N     
2002  C CA    . GLY A 255 ? 0.7948 0.6654 0.7002 -0.0298 -0.0402 -0.0952 256 GLY A CA    
2003  C C     . GLY A 255 ? 0.8190 0.6927 0.7297 -0.0362 -0.0439 -0.0901 256 GLY A C     
2004  O O     . GLY A 255 ? 0.7835 0.6506 0.6947 -0.0396 -0.0500 -0.0900 256 GLY A O     
2005  N N     . ILE A 256 ? 0.7897 0.6734 0.7043 -0.0378 -0.0403 -0.0858 257 ILE A N     
2006  C CA    . ILE A 256 ? 0.7542 0.6426 0.6742 -0.0434 -0.0430 -0.0807 257 ILE A CA    
2007  C C     . ILE A 256 ? 0.6734 0.5693 0.5914 -0.0440 -0.0412 -0.0790 257 ILE A C     
2008  O O     . ILE A 256 ? 0.6460 0.5428 0.5584 -0.0403 -0.0382 -0.0818 257 ILE A O     
2009  C CB    . ILE A 256 ? 0.7624 0.6561 0.6910 -0.0450 -0.0403 -0.0763 257 ILE A CB    
2010  C CG1   . ILE A 256 ? 0.7613 0.6639 0.6919 -0.0421 -0.0332 -0.0748 257 ILE A CG1   
2011  C CG2   . ILE A 256 ? 0.8302 0.7165 0.7606 -0.0441 -0.0420 -0.0779 257 ILE A CG2   
2012  C CD1   . ILE A 256 ? 0.7700 0.6778 0.7085 -0.0435 -0.0306 -0.0707 257 ILE A CD1   
2013  N N     . GLY A 257 ? 0.6835 0.5849 0.6063 -0.0487 -0.0432 -0.0743 258 GLY A N     
2014  C CA    . GLY A 257 ? 0.6394 0.5484 0.5614 -0.0495 -0.0419 -0.0721 258 GLY A CA    
2015  C C     . GLY A 257 ? 0.6079 0.5253 0.5379 -0.0535 -0.0416 -0.0661 258 GLY A C     
2016  O O     . GLY A 257 ? 0.5451 0.4623 0.4808 -0.0558 -0.0425 -0.0638 258 GLY A O     
2017  N N     . PRO A 258 ? 0.5813 0.5065 0.5117 -0.0542 -0.0401 -0.0635 259 PRO A N     
2018  C CA    . PRO A 258 ? 0.6006 0.5346 0.5384 -0.0574 -0.0394 -0.0580 259 PRO A CA    
2019  C C     . PRO A 258 ? 0.6420 0.5749 0.5850 -0.0625 -0.0446 -0.0552 259 PRO A C     
2020  O O     . PRO A 258 ? 0.6777 0.6152 0.6272 -0.0642 -0.0431 -0.0515 259 PRO A O     
2021  C CB    . PRO A 258 ? 0.5533 0.4930 0.4885 -0.0574 -0.0393 -0.0569 259 PRO A CB    
2022  C CG    . PRO A 258 ? 0.5456 0.4821 0.4733 -0.0527 -0.0363 -0.0611 259 PRO A CG    
2023  C CD    . PRO A 258 ? 0.5742 0.5004 0.4979 -0.0517 -0.0389 -0.0657 259 PRO A CD    
2024  N N     . GLU A 259 ? 0.6530 0.5796 0.5927 -0.0650 -0.0506 -0.0568 260 GLU A N     
2025  C CA    . GLU A 259 ? 0.6930 0.6187 0.6373 -0.0705 -0.0561 -0.0538 260 GLU A CA    
2026  C C     . GLU A 259 ? 0.6989 0.6192 0.6464 -0.0710 -0.0566 -0.0539 260 GLU A C     
2027  O O     . GLU A 259 ? 0.6319 0.5526 0.5846 -0.0755 -0.0600 -0.0505 260 GLU A O     
2028  C CB    . GLU A 259 ? 0.7183 0.6377 0.6577 -0.0730 -0.0628 -0.0560 260 GLU A CB    
2029  C CG    . GLU A 259 ? 0.7670 0.6870 0.7116 -0.0794 -0.0688 -0.0521 260 GLU A CG    
2030  C CD    . GLU A 259 ? 0.8024 0.7172 0.7425 -0.0823 -0.0756 -0.0538 260 GLU A CD    
2031  O OE1   . GLU A 259 ? 0.7955 0.7146 0.7327 -0.0818 -0.0755 -0.0540 260 GLU A OE1   
2032  O OE2   . GLU A 259 ? 0.8181 0.7241 0.7575 -0.0851 -0.0811 -0.0550 260 GLU A OE2   
2033  N N     . ASP A 260 ? 0.7028 0.6184 0.6472 -0.0664 -0.0531 -0.0577 261 ASP A N     
2034  C CA    . ASP A 260 ? 0.7173 0.6270 0.6641 -0.0661 -0.0536 -0.0583 261 ASP A CA    
2035  C C     . ASP A 260 ? 0.7189 0.6359 0.6717 -0.0651 -0.0481 -0.0551 261 ASP A C     
2036  O O     . ASP A 260 ? 0.7837 0.6977 0.7397 -0.0654 -0.0482 -0.0545 261 ASP A O     
2037  C CB    . ASP A 260 ? 0.7498 0.6497 0.6899 -0.0617 -0.0536 -0.0644 261 ASP A CB    
2038  C CG    . ASP A 260 ? 0.7319 0.6241 0.6649 -0.0621 -0.0588 -0.0682 261 ASP A CG    
2039  O OD1   . ASP A 260 ? 0.7247 0.6128 0.6587 -0.0667 -0.0650 -0.0670 261 ASP A OD1   
2040  O OD2   . ASP A 260 ? 0.8389 0.7293 0.7653 -0.0579 -0.0566 -0.0724 261 ASP A OD2   
2041  N N     . LEU A 261 ? 0.6827 0.6088 0.6368 -0.0639 -0.0436 -0.0531 262 LEU A N     
2042  C CA    . LEU A 261 ? 0.7238 0.6569 0.6831 -0.0628 -0.0385 -0.0501 262 LEU A CA    
2043  C C     . LEU A 261 ? 0.7273 0.6648 0.6935 -0.0676 -0.0407 -0.0450 262 LEU A C     
2044  O O     . LEU A 261 ? 0.8260 0.7679 0.7940 -0.0712 -0.0435 -0.0421 262 LEU A O     
2045  C CB    . LEU A 261 ? 0.6970 0.6380 0.6553 -0.0603 -0.0336 -0.0494 262 LEU A CB    
2046  C CG    . LEU A 261 ? 0.7420 0.6797 0.6934 -0.0557 -0.0311 -0.0539 262 LEU A CG    
2047  C CD1   . LEU A 261 ? 0.7075 0.6528 0.6591 -0.0531 -0.0254 -0.0527 262 LEU A CD1   
2048  C CD2   . LEU A 261 ? 0.7757 0.7057 0.7248 -0.0527 -0.0302 -0.0579 262 LEU A CD2   
2049  N N     . GLY A 262 ? 0.7415 0.6781 0.7116 -0.0677 -0.0395 -0.0437 263 GLY A N     
2050  C CA    . GLY A 262 ? 0.7421 0.6823 0.7184 -0.0721 -0.0415 -0.0389 263 GLY A CA    
2051  C C     . GLY A 262 ? 0.7111 0.6628 0.6918 -0.0727 -0.0378 -0.0347 263 GLY A C     
2052  O O     . GLY A 262 ? 0.7051 0.6604 0.6848 -0.0688 -0.0326 -0.0356 263 GLY A O     
2053  O OXT   . GLY A 262 ? 0.6918 0.6486 0.6767 -0.0769 -0.0403 -0.0304 263 GLY A OXT   
2109  N N     . GLN B 8   ? 0.4132 0.4411 0.4047 -0.0396 0.0463  -0.0391 10  GLN B N     
2110  C CA    . GLN B 8   ? 0.4514 0.4866 0.4447 -0.0363 0.0457  -0.0317 10  GLN B CA    
2111  C C     . GLN B 8   ? 0.4119 0.4359 0.4073 -0.0366 0.0458  -0.0270 10  GLN B C     
2112  O O     . GLN B 8   ? 0.5163 0.5398 0.5158 -0.0353 0.0463  -0.0213 10  GLN B O     
2113  C CB    . GLN B 8   ? 0.5300 0.5784 0.5224 -0.0340 0.0458  -0.0318 10  GLN B CB    
2114  C CG    . GLN B 8   ? 0.6059 0.6633 0.6002 -0.0300 0.0464  -0.0225 10  GLN B CG    
2115  C CD    . GLN B 8   ? 0.7054 0.7793 0.6981 -0.0272 0.0465  -0.0225 10  GLN B CD    
2116  O OE1   . GLN B 8   ? 0.7720 0.8604 0.7632 -0.0260 0.0458  -0.0285 10  GLN B OE1   
2117  N NE2   . GLN B 8   ? 0.6957 0.7694 0.6896 -0.0261 0.0474  -0.0168 10  GLN B NE2   
2118  N N     . LEU B 9   ? 0.3981 0.4141 0.3917 -0.0379 0.0457  -0.0300 11  LEU B N     
2119  C CA    . LEU B 9   ? 0.4178 0.4269 0.4136 -0.0380 0.0456  -0.0278 11  LEU B CA    
2120  C C     . LEU B 9   ? 0.4301 0.4329 0.4288 -0.0390 0.0453  -0.0275 11  LEU B C     
2121  O O     . LEU B 9   ? 0.4962 0.4973 0.5005 -0.0391 0.0456  -0.0252 11  LEU B O     
2122  C CB    . LEU B 9   ? 0.4370 0.4411 0.4290 -0.0378 0.0455  -0.0314 11  LEU B CB    
2123  C CG    . LEU B 9   ? 0.4544 0.4546 0.4481 -0.0373 0.0450  -0.0310 11  LEU B CG    
2124  C CD1   . LEU B 9   ? 0.4293 0.4354 0.4281 -0.0373 0.0453  -0.0279 11  LEU B CD1   
2125  C CD2   . LEU B 9   ? 0.4538 0.4499 0.4423 -0.0354 0.0451  -0.0339 11  LEU B CD2   
2126  N N     . GLY B 10  ? 0.4229 0.4230 0.4190 -0.0400 0.0452  -0.0306 12  GLY B N     
2127  C CA    . GLY B 10  ? 0.4221 0.4174 0.4201 -0.0406 0.0449  -0.0314 12  GLY B CA    
2128  C C     . GLY B 10  ? 0.4150 0.4136 0.4181 -0.0398 0.0449  -0.0282 12  GLY B C     
2129  O O     . GLY B 10  ? 0.4073 0.4027 0.4138 -0.0401 0.0446  -0.0290 12  GLY B O     
2130  N N     . GLN B 11  ? 0.4264 0.4326 0.4301 -0.0381 0.0455  -0.0245 13  GLN B N     
2131  C CA    . GLN B 11  ? 0.4198 0.4303 0.4274 -0.0356 0.0462  -0.0200 13  GLN B CA    
2132  C C     . GLN B 11  ? 0.3984 0.4095 0.4119 -0.0336 0.0482  -0.0128 13  GLN B C     
2133  O O     . GLN B 11  ? 0.4016 0.4108 0.4210 -0.0315 0.0500  -0.0081 13  GLN B O     
2134  C CB    . GLN B 11  ? 0.4698 0.4921 0.4734 -0.0338 0.0458  -0.0207 13  GLN B CB    
2135  C CG    . GLN B 11  ? 0.5242 0.5466 0.5243 -0.0366 0.0450  -0.0281 13  GLN B CG    
2136  C CD    . GLN B 11  ? 0.5514 0.5884 0.5496 -0.0352 0.0448  -0.0308 13  GLN B CD    
2137  O OE1   . GLN B 11  ? 0.6538 0.7000 0.6535 -0.0311 0.0447  -0.0271 13  GLN B OE1   
2138  N NE2   . GLN B 11  ? 0.6113 0.6516 0.6071 -0.0381 0.0452  -0.0378 13  GLN B NE2   
2139  N N     . ASP B 12  ? 0.3866 0.4000 0.3989 -0.0340 0.0487  -0.0116 14  ASP B N     
2140  C CA    . ASP B 12  ? 0.3809 0.3969 0.3985 -0.0322 0.0516  -0.0040 14  ASP B CA    
2141  C C     . ASP B 12  ? 0.3476 0.3553 0.3718 -0.0354 0.0527  -0.0056 14  ASP B C     
2142  O O     . ASP B 12  ? 0.3411 0.3491 0.3624 -0.0372 0.0513  -0.0097 14  ASP B O     
2143  C CB    . ASP B 12  ? 0.3913 0.4196 0.4040 -0.0300 0.0516  -0.0017 14  ASP B CB    
2144  C CG    . ASP B 12  ? 0.4949 0.5285 0.5122 -0.0272 0.0553  0.0080  14  ASP B CG    
2145  O OD1   . ASP B 12  ? 0.5477 0.5733 0.5737 -0.0276 0.0586  0.0130  14  ASP B OD1   
2146  O OD2   . ASP B 12  ? 0.5207 0.5671 0.5340 -0.0247 0.0554  0.0101  14  ASP B OD2   
2147  N N     . ALA B 13  ? 0.3253 0.3267 0.3594 -0.0358 0.0555  -0.0026 15  ALA B N     
2148  C CA    . ALA B 13  ? 0.3336 0.3290 0.3768 -0.0394 0.0570  -0.0062 15  ALA B CA    
2149  C C     . ALA B 13  ? 0.3635 0.3631 0.4092 -0.0402 0.0594  -0.0025 15  ALA B C     
2150  O O     . ALA B 13  ? 0.3497 0.3486 0.3995 -0.0434 0.0594  -0.0077 15  ALA B O     
2151  C CB    . ALA B 13  ? 0.3360 0.3237 0.3912 -0.0397 0.0604  -0.0046 15  ALA B CB    
2152  N N     . GLN B 14  ? 0.3764 0.3827 0.4195 -0.0369 0.0615  0.0062  16  GLN B N     
2153  C CA    . GLN B 14  ? 0.4152 0.4277 0.4602 -0.0372 0.0642  0.0108  16  GLN B CA    
2154  C C     . GLN B 14  ? 0.4060 0.4240 0.4422 -0.0383 0.0600  0.0036  16  GLN B C     
2155  O O     . GLN B 14  ? 0.4411 0.4594 0.4809 -0.0410 0.0604  0.0003  16  GLN B O     
2156  C CB    . GLN B 14  ? 0.4804 0.5020 0.5230 -0.0319 0.0671  0.0220  16  GLN B CB    
2157  C CG    . GLN B 14  ? 0.5838 0.6127 0.6292 -0.0318 0.0709  0.0285  16  GLN B CG    
2158  C CD    . GLN B 14  ? 0.6800 0.6999 0.7401 -0.0359 0.0769  0.0311  16  GLN B CD    
2159  O OE1   . GLN B 14  ? 0.7274 0.7356 0.7963 -0.0390 0.0780  0.0270  16  GLN B OE1   
2160  N NE2   . GLN B 14  ? 0.7455 0.7717 0.8094 -0.0364 0.0811  0.0371  16  GLN B NE2   
2161  N N     . LEU B 15  ? 0.3977 0.4202 0.4234 -0.0360 0.0563  0.0009  17  LEU B N     
2162  C CA    . LEU B 15  ? 0.4295 0.4555 0.4474 -0.0362 0.0531  -0.0055 17  LEU B CA    
2163  C C     . LEU B 15  ? 0.4320 0.4500 0.4504 -0.0387 0.0511  -0.0131 17  LEU B C     
2164  O O     . LEU B 15  ? 0.5061 0.5262 0.5221 -0.0389 0.0500  -0.0169 17  LEU B O     
2165  C CB    . LEU B 15  ? 0.4105 0.4416 0.4200 -0.0340 0.0508  -0.0079 17  LEU B CB    
2166  C CG    . LEU B 15  ? 0.4752 0.5081 0.4779 -0.0341 0.0484  -0.0150 17  LEU B CG    
2167  C CD1   . LEU B 15  ? 0.4834 0.5257 0.4857 -0.0328 0.0490  -0.0135 17  LEU B CD1   
2168  C CD2   . LEU B 15  ? 0.4172 0.4537 0.4146 -0.0332 0.0471  -0.0191 17  LEU B CD2   
2169  N N     . MET B 16  ? 0.4551 0.4658 0.4766 -0.0399 0.0508  -0.0151 18  MET B N     
2170  C CA    . MET B 16  ? 0.4797 0.4857 0.5013 -0.0412 0.0490  -0.0221 18  MET B CA    
2171  C C     . MET B 16  ? 0.4517 0.4605 0.4810 -0.0431 0.0502  -0.0244 18  MET B C     
2172  O O     . MET B 16  ? 0.3579 0.3694 0.3840 -0.0424 0.0484  -0.0296 18  MET B O     
2173  C CB    . MET B 16  ? 0.5339 0.5341 0.5590 -0.0419 0.0488  -0.0238 18  MET B CB    
2174  C CG    . MET B 16  ? 0.5791 0.5781 0.6055 -0.0427 0.0471  -0.0311 18  MET B CG    
2175  S SD    . MET B 16  ? 0.7005 0.6999 0.7142 -0.0400 0.0445  -0.0345 18  MET B SD    
2176  C CE    . MET B 16  ? 0.5565 0.5508 0.5652 -0.0398 0.0441  -0.0336 18  MET B CE    
2177  N N     . GLU B 17  ? 0.5032 0.5116 0.5431 -0.0451 0.0540  -0.0204 19  GLU B N     
2178  C CA    . GLU B 17  ? 0.5529 0.5644 0.6028 -0.0482 0.0563  -0.0234 19  GLU B CA    
2179  C C     . GLU B 17  ? 0.5368 0.5565 0.5819 -0.0472 0.0558  -0.0224 19  GLU B C     
2180  O O     . GLU B 17  ? 0.4979 0.5231 0.5461 -0.0485 0.0555  -0.0280 19  GLU B O     
2181  C CB    . GLU B 17  ? 0.6465 0.6537 0.7105 -0.0509 0.0619  -0.0184 19  GLU B CB    
2182  C CG    . GLU B 17  ? 0.7159 0.7152 0.7875 -0.0521 0.0626  -0.0217 19  GLU B CG    
2183  C CD    . GLU B 17  ? 0.8107 0.8125 0.8871 -0.0544 0.0603  -0.0339 19  GLU B CD    
2184  O OE1   . GLU B 17  ? 0.9413 0.9477 1.0281 -0.0579 0.0626  -0.0392 19  GLU B OE1   
2185  O OE2   . GLU B 17  ? 0.8843 0.8853 0.9543 -0.0525 0.0565  -0.0383 19  GLU B OE2   
2186  N N     . ASP B 18  ? 0.5421 0.5646 0.5796 -0.0446 0.0557  -0.0161 20  ASP B N     
2187  C CA    . ASP B 18  ? 0.5684 0.5997 0.6008 -0.0430 0.0551  -0.0155 20  ASP B CA    
2188  C C     . ASP B 18  ? 0.4973 0.5292 0.5211 -0.0409 0.0509  -0.0230 20  ASP B C     
2189  O O     . ASP B 18  ? 0.4396 0.4779 0.4625 -0.0403 0.0503  -0.0261 20  ASP B O     
2190  C CB    . ASP B 18  ? 0.6158 0.6525 0.6424 -0.0401 0.0557  -0.0087 20  ASP B CB    
2191  C CG    . ASP B 18  ? 0.6602 0.6983 0.6942 -0.0401 0.0605  0.0011  20  ASP B CG    
2192  O OD1   . ASP B 18  ? 0.7060 0.7386 0.7513 -0.0433 0.0643  0.0027  20  ASP B OD1   
2193  O OD2   . ASP B 18  ? 0.6711 0.7167 0.7000 -0.0366 0.0609  0.0070  20  ASP B OD2   
2194  N N     . TYR B 19  ? 0.4438 0.4689 0.4613 -0.0395 0.0486  -0.0254 21  TYR B N     
2195  C CA    . TYR B 19  ? 0.4480 0.4716 0.4573 -0.0366 0.0460  -0.0305 21  TYR B CA    
2196  C C     . TYR B 19  ? 0.4807 0.5073 0.4937 -0.0366 0.0453  -0.0358 21  TYR B C     
2197  O O     . TYR B 19  ? 0.4970 0.5284 0.5057 -0.0335 0.0440  -0.0388 21  TYR B O     
2198  C CB    . TYR B 19  ? 0.4116 0.4272 0.4153 -0.0358 0.0450  -0.0310 21  TYR B CB    
2199  C CG    . TYR B 19  ? 0.3835 0.3955 0.3797 -0.0325 0.0437  -0.0346 21  TYR B CG    
2200  C CD1   . TYR B 19  ? 0.4005 0.4115 0.3901 -0.0299 0.0438  -0.0352 21  TYR B CD1   
2201  C CD2   . TYR B 19  ? 0.3727 0.3831 0.3689 -0.0314 0.0430  -0.0374 21  TYR B CD2   
2202  C CE1   . TYR B 19  ? 0.3891 0.3950 0.3727 -0.0261 0.0440  -0.0370 21  TYR B CE1   
2203  C CE2   . TYR B 19  ? 0.3574 0.3652 0.3464 -0.0270 0.0427  -0.0387 21  TYR B CE2   
2204  C CZ    . TYR B 19  ? 0.3817 0.3859 0.3644 -0.0243 0.0436  -0.0378 21  TYR B CZ    
2205  O OH    . TYR B 19  ? 0.4327 0.4325 0.4090 -0.0194 0.0446  -0.0377 21  TYR B OH    
2206  N N     . LYS B 20  ? 0.5255 0.5508 0.5472 -0.0395 0.0462  -0.0376 22  LYS B N     
2207  C CA    . LYS B 20  ? 0.5634 0.5947 0.5903 -0.0397 0.0455  -0.0447 22  LYS B CA    
2208  C C     . LYS B 20  ? 0.5774 0.6191 0.6080 -0.0400 0.0461  -0.0471 22  LYS B C     
2209  O O     . LYS B 20  ? 0.6413 0.6913 0.6692 -0.0368 0.0443  -0.0526 22  LYS B O     
2210  C CB    . LYS B 20  ? 0.6271 0.6563 0.6662 -0.0440 0.0473  -0.0473 22  LYS B CB    
2211  C CG    . LYS B 20  ? 0.6979 0.7194 0.7340 -0.0432 0.0462  -0.0468 22  LYS B CG    
2212  C CD    . LYS B 20  ? 0.7441 0.7685 0.7718 -0.0390 0.0432  -0.0513 22  LYS B CD    
2213  C CE    . LYS B 20  ? 0.8473 0.8653 0.8730 -0.0387 0.0426  -0.0509 22  LYS B CE    
2214  N NZ    . LYS B 20  ? 0.8465 0.8683 0.8642 -0.0342 0.0407  -0.0538 22  LYS B NZ    
2215  N N     . GLN B 21  ? 0.5703 0.6128 0.6068 -0.0433 0.0491  -0.0424 23  GLN B N     
2216  C CA    . GLN B 21  ? 0.5327 0.5856 0.5746 -0.0447 0.0505  -0.0443 23  GLN B CA    
2217  C C     . GLN B 21  ? 0.4935 0.5524 0.5240 -0.0393 0.0477  -0.0451 23  GLN B C     
2218  O O     . GLN B 21  ? 0.4616 0.5310 0.4932 -0.0378 0.0467  -0.0507 23  GLN B O     
2219  C CB    . GLN B 21  ? 0.5834 0.6356 0.6329 -0.0486 0.0551  -0.0368 23  GLN B CB    
2220  C CG    . GLN B 21  ? 0.6371 0.6841 0.7018 -0.0541 0.0597  -0.0363 23  GLN B CG    
2221  C CD    . GLN B 21  ? 0.6257 0.6802 0.7031 -0.0581 0.0611  -0.0464 23  GLN B CD    
2222  O OE1   . GLN B 21  ? 0.6897 0.7421 0.7740 -0.0599 0.0608  -0.0533 23  GLN B OE1   
2223  N NE2   . GLN B 21  ? 0.6295 0.6949 0.7109 -0.0597 0.0626  -0.0486 23  GLN B NE2   
2224  N N     . ASN B 22  ? 0.3938 0.4468 0.4142 -0.0362 0.0465  -0.0403 24  ASN B N     
2225  C CA    . ASN B 22  ? 0.3935 0.4503 0.4047 -0.0313 0.0447  -0.0411 24  ASN B CA    
2226  C C     . ASN B 22  ? 0.3768 0.4237 0.3783 -0.0280 0.0435  -0.0394 24  ASN B C     
2227  O O     . ASN B 22  ? 0.3829 0.4283 0.3820 -0.0284 0.0440  -0.0361 24  ASN B O     
2228  C CB    . ASN B 22  ? 0.4278 0.4932 0.4412 -0.0324 0.0463  -0.0381 24  ASN B CB    
2229  C CG    . ASN B 22  ? 0.4603 0.5329 0.4670 -0.0273 0.0445  -0.0414 24  ASN B CG    
2230  O OD1   . ASN B 22  ? 0.4581 0.5250 0.4561 -0.0225 0.0427  -0.0426 24  ASN B OD1   
2231  N ND2   . ASN B 22  ? 0.4681 0.5531 0.4796 -0.0283 0.0454  -0.0429 24  ASN B ND2   
2232  N N     . PRO B 23  ? 0.3523 0.3934 0.3486 -0.0247 0.0422  -0.0418 25  PRO B N     
2233  C CA    . PRO B 23  ? 0.3909 0.4214 0.3797 -0.0225 0.0422  -0.0403 25  PRO B CA    
2234  C C     . PRO B 23  ? 0.3829 0.4127 0.3666 -0.0197 0.0426  -0.0404 25  PRO B C     
2235  O O     . PRO B 23  ? 0.3578 0.3833 0.3404 -0.0214 0.0434  -0.0394 25  PRO B O     
2236  C CB    . PRO B 23  ? 0.3833 0.4113 0.3679 -0.0180 0.0416  -0.0422 25  PRO B CB    
2237  C CG    . PRO B 23  ? 0.3665 0.4037 0.3585 -0.0200 0.0407  -0.0455 25  PRO B CG    
2238  C CD    . PRO B 23  ? 0.3710 0.4175 0.3692 -0.0228 0.0412  -0.0462 25  PRO B CD    
2239  N N     . GLU B 24  ? 0.3923 0.4279 0.3735 -0.0153 0.0421  -0.0425 26  GLU B N     
2240  C CA    . GLU B 24  ? 0.4770 0.5120 0.4541 -0.0119 0.0426  -0.0439 26  GLU B CA    
2241  C C     . GLU B 24  ? 0.4751 0.5176 0.4555 -0.0156 0.0427  -0.0433 26  GLU B C     
2242  O O     . GLU B 24  ? 0.4335 0.4737 0.4123 -0.0155 0.0434  -0.0448 26  GLU B O     
2243  C CB    . GLU B 24  ? 0.5930 0.6344 0.5672 -0.0057 0.0419  -0.0462 26  GLU B CB    
2244  C CG    . GLU B 24  ? 0.6885 0.7230 0.6572 0.0009  0.0425  -0.0458 26  GLU B CG    
2245  C CD    . GLU B 24  ? 0.8129 0.8520 0.7774 0.0091  0.0426  -0.0473 26  GLU B CD    
2246  O OE1   . GLU B 24  ? 0.9231 0.9766 0.8897 0.0100  0.0407  -0.0497 26  GLU B OE1   
2247  O OE2   . GLU B 24  ? 0.8034 0.8315 0.7631 0.0147  0.0449  -0.0462 26  GLU B OE2   
2248  N N     . ALA B 25  ? 0.4496 0.5024 0.4354 -0.0186 0.0425  -0.0414 27  ALA B N     
2249  C CA    . ALA B 25  ? 0.4451 0.5075 0.4339 -0.0210 0.0433  -0.0390 27  ALA B CA    
2250  C C     . ALA B 25  ? 0.4457 0.5039 0.4344 -0.0233 0.0440  -0.0367 27  ALA B C     
2251  O O     . ALA B 25  ? 0.4331 0.4974 0.4201 -0.0224 0.0441  -0.0378 27  ALA B O     
2252  C CB    . ALA B 25  ? 0.4388 0.5100 0.4349 -0.0244 0.0445  -0.0358 27  ALA B CB    
2253  N N     . VAL B 26  ? 0.4281 0.4776 0.4187 -0.0259 0.0443  -0.0345 28  VAL B N     
2254  C CA    . VAL B 26  ? 0.4118 0.4585 0.4027 -0.0278 0.0449  -0.0322 28  VAL B CA    
2255  C C     . VAL B 26  ? 0.4184 0.4598 0.4043 -0.0263 0.0445  -0.0371 28  VAL B C     
2256  O O     . VAL B 26  ? 0.4257 0.4726 0.4114 -0.0267 0.0448  -0.0381 28  VAL B O     
2257  C CB    . VAL B 26  ? 0.4009 0.4393 0.3954 -0.0305 0.0453  -0.0296 28  VAL B CB    
2258  C CG1   . VAL B 26  ? 0.3785 0.4143 0.3727 -0.0317 0.0457  -0.0277 28  VAL B CG1   
2259  C CG2   . VAL B 26  ? 0.4042 0.4469 0.4065 -0.0329 0.0468  -0.0259 28  VAL B CG2   
2260  N N     . MET B 27  ? 0.4293 0.4607 0.4119 -0.0242 0.0445  -0.0403 29  MET B N     
2261  C CA    . MET B 27  ? 0.4291 0.4521 0.4089 -0.0233 0.0457  -0.0446 29  MET B CA    
2262  C C     . MET B 27  ? 0.4334 0.4638 0.4130 -0.0215 0.0461  -0.0496 29  MET B C     
2263  O O     . MET B 27  ? 0.4214 0.4522 0.4021 -0.0229 0.0472  -0.0541 29  MET B O     
2264  C CB    . MET B 27  ? 0.4167 0.4276 0.3930 -0.0202 0.0467  -0.0449 29  MET B CB    
2265  C CG    . MET B 27  ? 0.4557 0.4587 0.4318 -0.0219 0.0470  -0.0421 29  MET B CG    
2266  S SD    . MET B 27  ? 0.4524 0.4442 0.4234 -0.0167 0.0488  -0.0410 29  MET B SD    
2267  C CE    . MET B 27  ? 0.4577 0.4601 0.4280 -0.0121 0.0465  -0.0406 29  MET B CE    
2268  N N     . ARG B 28  ? 0.4242 0.4620 0.4033 -0.0186 0.0452  -0.0498 30  ARG B N     
2269  C CA    . ARG B 28  ? 0.4921 0.5381 0.4713 -0.0163 0.0454  -0.0553 30  ARG B CA    
2270  C C     . ARG B 28  ? 0.4898 0.5516 0.4715 -0.0184 0.0448  -0.0557 30  ARG B C     
2271  O O     . ARG B 28  ? 0.4813 0.5505 0.4641 -0.0176 0.0452  -0.0625 30  ARG B O     
2272  C CB    . ARG B 28  ? 0.5797 0.6321 0.5577 -0.0124 0.0444  -0.0551 30  ARG B CB    
2273  C CG    . ARG B 28  ? 0.6817 0.7241 0.6570 -0.0094 0.0444  -0.0529 30  ARG B CG    
2274  C CD    . ARG B 28  ? 0.6988 0.7482 0.6726 -0.0041 0.0437  -0.0548 30  ARG B CD    
2275  N NE    . ARG B 28  ? 0.7399 0.7838 0.7120 0.0006  0.0453  -0.0601 30  ARG B NE    
2276  C CZ    . ARG B 28  ? 0.7974 0.8312 0.7663 0.0067  0.0468  -0.0602 30  ARG B CZ    
2277  N NH1   . ARG B 28  ? 0.8102 0.8412 0.7761 0.0094  0.0463  -0.0558 30  ARG B NH1   
2278  N NH2   . ARG B 28  ? 0.7770 0.8044 0.7462 0.0108  0.0492  -0.0650 30  ARG B NH2   
2279  N N     . ALA B 29  ? 0.4100 0.4775 0.3931 -0.0206 0.0443  -0.0486 31  ALA B N     
2280  C CA    . ALA B 29  ? 0.4433 0.5271 0.4280 -0.0211 0.0443  -0.0463 31  ALA B CA    
2281  C C     . ALA B 29  ? 0.4428 0.5261 0.4279 -0.0226 0.0446  -0.0500 31  ALA B C     
2282  O O     . ALA B 29  ? 0.4578 0.5577 0.4437 -0.0216 0.0444  -0.0515 31  ALA B O     
2283  C CB    . ALA B 29  ? 0.4792 0.5663 0.4664 -0.0224 0.0449  -0.0365 31  ALA B CB    
2284  N N     . HIS B 30  ? 0.3994 0.4658 0.3841 -0.0247 0.0452  -0.0517 32  HIS B N     
2285  C CA    . HIS B 30  ? 0.4397 0.5048 0.4255 -0.0269 0.0459  -0.0558 32  HIS B CA    
2286  C C     . HIS B 30  ? 0.4105 0.4698 0.3976 -0.0273 0.0476  -0.0663 32  HIS B C     
2287  O O     . HIS B 30  ? 0.4055 0.4607 0.3949 -0.0300 0.0491  -0.0715 32  HIS B O     
2288  C CB    . HIS B 30  ? 0.4326 0.4847 0.4182 -0.0292 0.0461  -0.0506 32  HIS B CB    
2289  C CG    . HIS B 30  ? 0.4630 0.5218 0.4497 -0.0292 0.0455  -0.0419 32  HIS B CG    
2290  N ND1   . HIS B 30  ? 0.4609 0.5186 0.4487 -0.0286 0.0454  -0.0353 32  HIS B ND1   
2291  C CD2   . HIS B 30  ? 0.4867 0.5534 0.4746 -0.0292 0.0455  -0.0389 32  HIS B CD2   
2292  C CE1   . HIS B 30  ? 0.5178 0.5803 0.5081 -0.0288 0.0461  -0.0281 32  HIS B CE1   
2293  N NE2   . HIS B 30  ? 0.5307 0.5987 0.5205 -0.0285 0.0460  -0.0296 32  HIS B NE2   
2294  N N     . GLY B 31  ? 0.4312 0.4898 0.4179 -0.0246 0.0479  -0.0695 33  GLY B N     
2295  C CA    . GLY B 31  ? 0.4588 0.5145 0.4487 -0.0243 0.0501  -0.0802 33  GLY B CA    
2296  C C     . GLY B 31  ? 0.4935 0.5255 0.4835 -0.0249 0.0536  -0.0809 33  GLY B C     
2297  O O     . GLY B 31  ? 0.4540 0.4795 0.4487 -0.0263 0.0571  -0.0895 33  GLY B O     
2298  N N     . LEU B 32  ? 0.5043 0.5247 0.4900 -0.0237 0.0531  -0.0720 34  LEU B N     
2299  C CA    . LEU B 32  ? 0.5264 0.5266 0.5109 -0.0226 0.0566  -0.0706 34  LEU B CA    
2300  C C     . LEU B 32  ? 0.5666 0.5613 0.5503 -0.0171 0.0583  -0.0725 34  LEU B C     
2301  O O     . LEU B 32  ? 0.5472 0.5510 0.5283 -0.0136 0.0555  -0.0704 34  LEU B O     
2302  C CB    . LEU B 32  ? 0.5472 0.5410 0.5274 -0.0222 0.0552  -0.0615 34  LEU B CB    
2303  C CG    . LEU B 32  ? 0.5479 0.5410 0.5293 -0.0270 0.0550  -0.0598 34  LEU B CG    
2304  C CD1   . LEU B 32  ? 0.5635 0.5732 0.5465 -0.0294 0.0518  -0.0595 34  LEU B CD1   
2305  C CD2   . LEU B 32  ? 0.5981 0.5828 0.5759 -0.0259 0.0545  -0.0526 34  LEU B CD2   
2306  N N     . THR B 33  ? 0.6333 0.6126 0.6199 -0.0164 0.0636  -0.0764 35  THR B N     
2307  C CA    . THR B 33  ? 0.6388 0.6106 0.6257 -0.0104 0.0664  -0.0783 35  THR B CA    
2308  C C     . THR B 33  ? 0.6265 0.5922 0.6060 -0.0038 0.0656  -0.0685 35  THR B C     
2309  O O     . THR B 33  ? 0.4722 0.4375 0.4476 -0.0047 0.0638  -0.0616 35  THR B O     
2310  C CB    . THR B 33  ? 0.6900 0.6450 0.6838 -0.0117 0.0737  -0.0844 35  THR B CB    
2311  O OG1   . THR B 33  ? 0.7405 0.6809 0.7320 -0.0127 0.0769  -0.0769 35  THR B OG1   
2312  C CG2   . THR B 33  ? 0.6902 0.6545 0.6929 -0.0185 0.0746  -0.0966 35  THR B CG2   
2313  N N     . ASP B 34  ? 0.6338 0.5965 0.6120 0.0034  0.0670  -0.0689 36  ASP B N     
2314  C CA    . ASP B 34  ? 0.7060 0.6671 0.6771 0.0112  0.0661  -0.0609 36  ASP B CA    
2315  C C     . ASP B 34  ? 0.6803 0.6248 0.6486 0.0136  0.0707  -0.0536 36  ASP B C     
2316  O O     . ASP B 34  ? 0.6885 0.6363 0.6509 0.0169  0.0686  -0.0466 36  ASP B O     
2317  C CB    . ASP B 34  ? 0.7364 0.6981 0.7071 0.0193  0.0672  -0.0633 36  ASP B CB    
2318  C CG    . ASP B 34  ? 0.8001 0.7801 0.7730 0.0179  0.0628  -0.0703 36  ASP B CG    
2319  O OD1   . ASP B 34  ? 0.8193 0.8153 0.7896 0.0162  0.0576  -0.0679 36  ASP B OD1   
2320  O OD2   . ASP B 34  ? 0.9582 0.9368 0.9365 0.0185  0.0652  -0.0784 36  ASP B OD2   
2321  N N     . GLU B 35  ? 0.6399 0.5679 0.6134 0.0118  0.0774  -0.0558 37  GLU B N     
2322  C CA    . GLU B 35  ? 0.6846 0.5958 0.6562 0.0142  0.0834  -0.0482 37  GLU B CA    
2323  C C     . GLU B 35  ? 0.6701 0.5855 0.6400 0.0076  0.0806  -0.0452 37  GLU B C     
2324  O O     . GLU B 35  ? 0.6121 0.5232 0.5768 0.0112  0.0819  -0.0370 37  GLU B O     
2325  C CB    . GLU B 35  ? 0.7646 0.6568 0.7447 0.0124  0.0924  -0.0524 37  GLU B CB    
2326  C CG    . GLU B 35  ? 0.8597 0.7556 0.8491 0.0012  0.0923  -0.0637 37  GLU B CG    
2327  C CD    . GLU B 35  ? 0.9342 0.8127 0.9348 -0.0017 0.1017  -0.0707 37  GLU B CD    
2328  O OE1   . GLU B 35  ? 0.9851 0.8455 0.9871 -0.0010 0.1094  -0.0643 37  GLU B OE1   
2329  O OE2   . GLU B 35  ? 0.9389 0.8229 0.9477 -0.0047 0.1019  -0.0828 37  GLU B OE2   
2330  N N     . GLN B 36  ? 0.6280 0.5534 0.6024 -0.0011 0.0769  -0.0520 38  GLN B N     
2331  C CA    . GLN B 36  ? 0.6009 0.5311 0.5745 -0.0072 0.0741  -0.0500 38  GLN B CA    
2332  C C     . GLN B 36  ? 0.5853 0.5275 0.5526 -0.0042 0.0681  -0.0445 38  GLN B C     
2333  O O     . GLN B 36  ? 0.5320 0.4741 0.4968 -0.0050 0.0672  -0.0398 38  GLN B O     
2334  C CB    . GLN B 36  ? 0.5785 0.5184 0.5581 -0.0155 0.0718  -0.0584 38  GLN B CB    
2335  C CG    . GLN B 36  ? 0.6279 0.5586 0.6157 -0.0200 0.0779  -0.0664 38  GLN B CG    
2336  C CD    . GLN B 36  ? 0.6102 0.5561 0.6038 -0.0266 0.0751  -0.0760 38  GLN B CD    
2337  O OE1   . GLN B 36  ? 0.5929 0.5554 0.5839 -0.0269 0.0690  -0.0755 38  GLN B OE1   
2338  N NE2   . GLN B 36  ? 0.6554 0.5966 0.6576 -0.0316 0.0802  -0.0850 38  GLN B NE2   
2339  N N     . ILE B 37  ? 0.5724 0.5258 0.5385 -0.0011 0.0642  -0.0460 39  ILE B N     
2340  C CA    . ILE B 37  ? 0.5275 0.4937 0.4901 0.0009  0.0592  -0.0427 39  ILE B CA    
2341  C C     . ILE B 37  ? 0.5304 0.4929 0.4872 0.0092  0.0607  -0.0367 39  ILE B C     
2342  O O     . ILE B 37  ? 0.5290 0.4982 0.4836 0.0096  0.0582  -0.0338 39  ILE B O     
2343  C CB    . ILE B 37  ? 0.4892 0.4691 0.4531 0.0015  0.0555  -0.0463 39  ILE B CB    
2344  C CG1   . ILE B 37  ? 0.5268 0.5141 0.4957 -0.0056 0.0540  -0.0510 39  ILE B CG1   
2345  C CG2   . ILE B 37  ? 0.4840 0.4766 0.4459 0.0036  0.0515  -0.0438 39  ILE B CG2   
2346  C CD1   . ILE B 37  ? 0.5753 0.5777 0.5455 -0.0050 0.0510  -0.0537 39  ILE B CD1   
2347  N N     . ASN B 38  ? 0.5639 0.5170 0.5187 0.0163  0.0651  -0.0351 40  ASN B N     
2348  C CA    . ASN B 38  ? 0.6058 0.5567 0.5542 0.0264  0.0674  -0.0283 40  ASN B CA    
2349  C C     . ASN B 38  ? 0.6069 0.5511 0.5532 0.0256  0.0700  -0.0227 40  ASN B C     
2350  O O     . ASN B 38  ? 0.6156 0.5685 0.5571 0.0308  0.0683  -0.0184 40  ASN B O     
2351  C CB    . ASN B 38  ? 0.6474 0.5864 0.5950 0.0346  0.0731  -0.0266 40  ASN B CB    
2352  C CG    . ASN B 38  ? 0.6475 0.5855 0.5876 0.0470  0.0760  -0.0177 40  ASN B CG    
2353  O OD1   . ASN B 38  ? 0.6602 0.6148 0.5957 0.0530  0.0715  -0.0170 40  ASN B OD1   
2354  N ND2   . ASN B 38  ? 0.6695 0.5898 0.6088 0.0511  0.0839  -0.0110 40  ASN B ND2   
2355  N N     . ALA B 39  ? 0.6230 0.5538 0.5737 0.0191  0.0742  -0.0236 41  ALA B N     
2356  C CA    . ALA B 39  ? 0.6000 0.5239 0.5494 0.0175  0.0774  -0.0187 41  ALA B CA    
2357  C C     . ALA B 39  ? 0.5275 0.4660 0.4759 0.0136  0.0710  -0.0195 41  ALA B C     
2358  O O     . ALA B 39  ? 0.5732 0.5146 0.5176 0.0171  0.0714  -0.0146 41  ALA B O     
2359  C CB    . ALA B 39  ? 0.6041 0.5142 0.5603 0.0094  0.0824  -0.0222 41  ALA B CB    
2360  N N     . VAL B 40  ? 0.4732 0.4212 0.4257 0.0068  0.0656  -0.0258 42  VAL B N     
2361  C CA    . VAL B 40  ? 0.4585 0.4183 0.4124 0.0025  0.0604  -0.0272 42  VAL B CA    
2362  C C     . VAL B 40  ? 0.4604 0.4335 0.4107 0.0092  0.0572  -0.0259 42  VAL B C     
2363  O O     . VAL B 40  ? 0.4495 0.4298 0.3994 0.0095  0.0554  -0.0253 42  VAL B O     
2364  C CB    . VAL B 40  ? 0.4456 0.4119 0.4052 -0.0052 0.0566  -0.0326 42  VAL B CB    
2365  C CG1   . VAL B 40  ? 0.4267 0.4044 0.3890 -0.0085 0.0521  -0.0336 42  VAL B CG1   
2366  C CG2   . VAL B 40  ? 0.4404 0.3985 0.4038 -0.0116 0.0591  -0.0353 42  VAL B CG2   
2367  N N     . MET B 41  ? 0.5072 0.4853 0.4559 0.0147  0.0565  -0.0267 43  MET B N     
2368  C CA    . MET B 41  ? 0.5410 0.5351 0.4874 0.0208  0.0533  -0.0274 43  MET B CA    
2369  C C     . MET B 41  ? 0.5307 0.5260 0.4703 0.0306  0.0559  -0.0216 43  MET B C     
2370  O O     . MET B 41  ? 0.4855 0.4967 0.4239 0.0344  0.0530  -0.0229 43  MET B O     
2371  C CB    . MET B 41  ? 0.5657 0.5658 0.5120 0.0245  0.0521  -0.0299 43  MET B CB    
2372  C CG    . MET B 41  ? 0.6009 0.6054 0.5537 0.0160  0.0492  -0.0351 43  MET B CG    
2373  S SD    . MET B 41  ? 0.7172 0.7335 0.6769 0.0077  0.0452  -0.0385 43  MET B SD    
2374  C CE    . MET B 41  ? 0.6800 0.7135 0.6379 0.0152  0.0431  -0.0403 43  MET B CE    
2375  N N     . THR B 42  ? 0.5705 0.5499 0.5063 0.0350  0.0620  -0.0154 44  THR B N     
2376  C CA    . THR B 42  ? 0.5968 0.5760 0.5255 0.0455  0.0660  -0.0075 44  THR B CA    
2377  C C     . THR B 42  ? 0.6213 0.5959 0.5503 0.0410  0.0677  -0.0048 44  THR B C     
2378  O O     . THR B 42  ? 0.7034 0.6821 0.6269 0.0488  0.0704  0.0016  44  THR B O     
2379  C CB    . THR B 42  ? 0.6292 0.5922 0.5548 0.0532  0.0730  -0.0010 44  THR B CB    
2380  O OG1   . THR B 42  ? 0.6722 0.6164 0.6038 0.0438  0.0767  -0.0030 44  THR B OG1   
2381  C CG2   . THR B 42  ? 0.6462 0.6158 0.5707 0.0595  0.0711  -0.0035 44  THR B CG2   
2382  N N     . GLY B 43  ? 0.6546 0.6228 0.5901 0.0292  0.0663  -0.0096 45  GLY B N     
2383  C CA    . GLY B 43  ? 0.6974 0.6633 0.6341 0.0240  0.0670  -0.0087 45  GLY B CA    
2384  C C     . GLY B 43  ? 0.7597 0.7088 0.6941 0.0260  0.0751  -0.0012 45  GLY B C     
2385  O O     . GLY B 43  ? 0.7566 0.7070 0.6887 0.0271  0.0772  0.0029  45  GLY B O     
2386  N N     . ASP B 44  ? 0.7472 0.6808 0.6833 0.0262  0.0802  0.0000  46  ASP B N     
2387  C CA    . ASP B 44  ? 0.7338 0.6488 0.6705 0.0268  0.0895  0.0062  46  ASP B CA    
2388  C C     . ASP B 44  ? 0.6693 0.5760 0.6137 0.0141  0.0904  0.0002  46  ASP B C     
2389  O O     . ASP B 44  ? 0.5811 0.4787 0.5317 0.0085  0.0922  -0.0054 46  ASP B O     
2390  C CB    . ASP B 44  ? 0.8325 0.7344 0.7692 0.0334  0.0955  0.0095  46  ASP B CB    
2391  C CG    . ASP B 44  ? 0.9131 0.7933 0.8525 0.0343  0.1069  0.0163  46  ASP B CG    
2392  O OD1   . ASP B 44  ? 0.9282 0.8044 0.8691 0.0294  0.1102  0.0187  46  ASP B OD1   
2393  O OD2   . ASP B 44  ? 0.9822 0.8496 0.9231 0.0400  0.1130  0.0190  46  ASP B OD2   
2394  N N     . MET B 45  ? 0.6657 0.5777 0.6098 0.0102  0.0891  0.0008  47  MET B N     
2395  C CA    . MET B 45  ? 0.6801 0.5880 0.6308 -0.0011 0.0892  -0.0051 47  MET B CA    
2396  C C     . MET B 45  ? 0.7235 0.6127 0.6797 -0.0044 0.0986  -0.0044 47  MET B C     
2397  O O     . MET B 45  ? 0.7478 0.6335 0.7115 -0.0133 0.0989  -0.0126 47  MET B O     
2398  C CB    . MET B 45  ? 0.6701 0.5863 0.6191 -0.0029 0.0873  -0.0034 47  MET B CB    
2399  C CG    . MET B 45  ? 0.6560 0.5904 0.6026 -0.0012 0.0786  -0.0063 47  MET B CG    
2400  S SD    . MET B 45  ? 0.5770 0.5182 0.5298 -0.0089 0.0710  -0.0160 47  MET B SD    
2401  C CE    . MET B 45  ? 0.5981 0.5400 0.5486 -0.0024 0.0702  -0.0158 47  MET B CE    
2402  N N     . GLU B 46  ? 0.7348 0.6131 0.6878 0.0030  0.1069  0.0052  48  GLU B N     
2403  C CA    . GLU B 46  ? 0.7769 0.6354 0.7368 0.0000  0.1178  0.0068  48  GLU B CA    
2404  C C     . GLU B 46  ? 0.7481 0.5997 0.7161 -0.0050 0.1182  -0.0031 48  GLU B C     
2405  O O     . GLU B 46  ? 0.7317 0.5773 0.7093 -0.0147 0.1214  -0.0113 48  GLU B O     
2406  C CB    . GLU B 46  ? 0.8584 0.7060 0.8132 0.0115  0.1269  0.0204  48  GLU B CB    
2407  C CG    . GLU B 46  ? 0.9803 0.8347 0.9282 0.0162  0.1288  0.0304  48  GLU B CG    
2408  C CD    . GLU B 46  ? 1.0835 0.9314 1.0377 0.0063  0.1342  0.0293  48  GLU B CD    
2409  O OE1   . GLU B 46  ? 1.2343 1.0885 1.1833 0.0096  0.1360  0.0371  48  GLU B OE1   
2410  O OE2   . GLU B 46  ? 1.1646 1.0032 1.1292 -0.0045 0.1365  0.0198  48  GLU B OE2   
2411  N N     . LYS B 47  ? 0.7517 0.6067 0.7162 0.0021  0.1147  -0.0030 49  LYS B N     
2412  C CA    . LYS B 47  ? 0.7547 0.6046 0.7263 -0.0007 0.1153  -0.0119 49  LYS B CA    
2413  C C     . LYS B 47  ? 0.6822 0.5439 0.6594 -0.0116 0.1083  -0.0243 49  LYS B C     
2414  O O     . LYS B 47  ? 0.7114 0.5686 0.6980 -0.0180 0.1112  -0.0339 49  LYS B O     
2415  C CB    . LYS B 47  ? 0.7900 0.6454 0.7555 0.0094  0.1115  -0.0094 49  LYS B CB    
2416  C CG    . LYS B 47  ? 0.8508 0.7024 0.8231 0.0078  0.1120  -0.0185 49  LYS B CG    
2417  C CD    . LYS B 47  ? 0.9091 0.7676 0.8752 0.0181  0.1082  -0.0162 49  LYS B CD    
2418  C CE    . LYS B 47  ? 0.9339 0.7825 0.8940 0.0310  0.1148  -0.0037 49  LYS B CE    
2419  N NZ    . LYS B 47  ? 0.9377 0.7624 0.9056 0.0318  0.1269  -0.0017 49  LYS B NZ    
2420  N N     . LEU B 48  ? 0.5873 0.4653 0.5594 -0.0130 0.0996  -0.0244 50  LEU B N     
2421  C CA    . LEU B 48  ? 0.5891 0.4798 0.5651 -0.0212 0.0930  -0.0337 50  LEU B CA    
2422  C C     . LEU B 48  ? 0.6030 0.4885 0.5876 -0.0304 0.0978  -0.0403 50  LEU B C     
2423  O O     . LEU B 48  ? 0.5531 0.4454 0.5442 -0.0365 0.0959  -0.0503 50  LEU B O     
2424  C CB    . LEU B 48  ? 0.5778 0.4832 0.5482 -0.0208 0.0850  -0.0311 50  LEU B CB    
2425  C CG    . LEU B 48  ? 0.6164 0.5314 0.5808 -0.0137 0.0793  -0.0280 50  LEU B CG    
2426  C CD1   . LEU B 48  ? 0.6139 0.5430 0.5765 -0.0156 0.0722  -0.0281 50  LEU B CD1   
2427  C CD2   . LEU B 48  ? 0.6176 0.5358 0.5845 -0.0134 0.0774  -0.0335 50  LEU B CD2   
2428  N N     . LYS B 49  ? 0.7228 0.5986 0.7076 -0.0312 0.1041  -0.0347 51  LYS B N     
2429  C CA    . LYS B 49  ? 0.8269 0.6985 0.8204 -0.0402 0.1093  -0.0408 51  LYS B CA    
2430  C C     . LYS B 49  ? 0.8063 0.6647 0.8103 -0.0433 0.1178  -0.0478 51  LYS B C     
2431  O O     . LYS B 49  ? 0.8805 0.7429 0.8944 -0.0519 0.1191  -0.0595 51  LYS B O     
2432  C CB    . LYS B 49  ? 0.9179 0.7835 0.9086 -0.0397 0.1142  -0.0321 51  LYS B CB    
2433  C CG    . LYS B 49  ? 0.9889 0.8684 0.9709 -0.0372 0.1062  -0.0272 51  LYS B CG    
2434  C CD    . LYS B 49  ? 1.0464 0.9226 1.0256 -0.0362 0.1109  -0.0192 51  LYS B CD    
2435  C CE    . LYS B 49  ? 1.0441 0.9355 1.0164 -0.0339 0.1027  -0.0168 51  LYS B CE    
2436  N NZ    . LYS B 49  ? 1.0700 0.9607 1.0395 -0.0326 0.1071  -0.0098 51  LYS B NZ    
2437  N N     . THR B 50  ? 0.8080 0.6519 0.8106 -0.0359 0.1237  -0.0409 52  THR B N     
2438  C CA    . THR B 50  ? 0.8284 0.6569 0.8419 -0.0376 0.1329  -0.0468 52  THR B CA    
2439  C C     . THR B 50  ? 0.8137 0.6540 0.8325 -0.0408 0.1272  -0.0605 52  THR B C     
2440  O O     . THR B 50  ? 0.7471 0.5840 0.7787 -0.0475 0.1324  -0.0728 52  THR B O     
2441  C CB    . THR B 50  ? 0.8385 0.6504 0.8475 -0.0265 0.1396  -0.0346 52  THR B CB    
2442  O OG1   . THR B 50  ? 0.8923 0.6952 0.8980 -0.0245 0.1462  -0.0226 52  THR B OG1   
2443  C CG2   . THR B 50  ? 0.9043 0.6990 0.9253 -0.0270 0.1492  -0.0407 52  THR B CG2   
2444  N N     . LEU B 51  ? 0.7650 0.6205 0.7745 -0.0359 0.1169  -0.0589 53  LEU B N     
2445  C CA    . LEU B 51  ? 0.7310 0.5999 0.7437 -0.0372 0.1112  -0.0696 53  LEU B CA    
2446  C C     . LEU B 51  ? 0.7461 0.6327 0.7633 -0.0460 0.1062  -0.0799 53  LEU B C     
2447  O O     . LEU B 51  ? 0.7831 0.6825 0.8056 -0.0487 0.1033  -0.0910 53  LEU B O     
2448  C CB    . LEU B 51  ? 0.7008 0.5794 0.7026 -0.0289 0.1031  -0.0630 53  LEU B CB    
2449  C CG    . LEU B 51  ? 0.6896 0.5552 0.6863 -0.0186 0.1071  -0.0538 53  LEU B CG    
2450  C CD1   . LEU B 51  ? 0.6487 0.5282 0.6361 -0.0117 0.0985  -0.0498 53  LEU B CD1   
2451  C CD2   . LEU B 51  ? 0.6874 0.5390 0.6938 -0.0179 0.1152  -0.0602 53  LEU B CD2   
2452  N N     . SER B 52  ? 0.7933 0.6823 0.8082 -0.0497 0.1054  -0.0760 54  SER B N     
2453  C CA    . SER B 52  ? 0.8063 0.7125 0.8248 -0.0568 0.1010  -0.0845 54  SER B CA    
2454  C C     . SER B 52  ? 0.8732 0.7747 0.9050 -0.0653 0.1091  -0.0957 54  SER B C     
2455  O O     . SER B 52  ? 0.9126 0.8290 0.9522 -0.0704 0.1076  -0.1090 54  SER B O     
2456  C CB    . SER B 52  ? 0.7790 0.6913 0.7895 -0.0563 0.0960  -0.0761 54  SER B CB    
2457  O OG    . SER B 52  ? 0.7671 0.6973 0.7802 -0.0615 0.0913  -0.0833 54  SER B OG    
2458  N N     . GLY B 53  ? 0.9611 0.8433 0.9958 -0.0665 0.1182  -0.0903 55  GLY B N     
2459  C CA    . GLY B 53  ? 0.9509 0.8259 1.0000 -0.0753 0.1277  -0.1005 55  GLY B CA    
2460  C C     . GLY B 53  ? 0.9666 0.8287 1.0152 -0.0774 0.1345  -0.0914 55  GLY B C     
2461  O O     . GLY B 53  ? 0.8855 0.7471 0.9220 -0.0718 0.1307  -0.0782 55  GLY B O     
2462  N N     . ASP B 54  ? 1.0770 0.9301 1.1397 -0.0858 0.1449  -0.0995 56  ASP B N     
2463  C CA    . ASP B 54  ? 1.1137 0.9549 1.1779 -0.0889 0.1530  -0.0918 56  ASP B CA    
2464  C C     . ASP B 54  ? 1.1558 0.9708 1.2183 -0.0821 0.1631  -0.0776 56  ASP B C     
2465  O O     . ASP B 54  ? 1.1704 0.9689 1.2433 -0.0870 0.1759  -0.0765 56  ASP B O     
2466  C CB    . ASP B 54  ? 1.1276 0.9827 1.1794 -0.0870 0.1444  -0.0838 56  ASP B CB    
2467  C CG    . ASP B 54  ? 1.1411 1.0214 1.1944 -0.0926 0.1354  -0.0958 56  ASP B CG    
2468  O OD1   . ASP B 54  ? 1.1279 1.0142 1.1939 -0.1019 0.1400  -0.1090 56  ASP B OD1   
2469  O OD2   . ASP B 54  ? 1.1330 1.0274 1.1753 -0.0873 0.1245  -0.0918 56  ASP B OD2   
2470  N N     . ALA B 60  ? 0.9238 0.8171 0.9150 -0.0658 0.1457  -0.0020 62  ALA B N     
2471  C CA    . ALA B 60  ? 0.9071 0.8133 0.8891 -0.0590 0.1431  0.0063  62  ALA B CA    
2472  C C     . ALA B 60  ? 0.8708 0.7961 0.8501 -0.0597 0.1299  -0.0028 62  ALA B C     
2473  O O     . ALA B 60  ? 0.9418 0.8713 0.9278 -0.0676 0.1261  -0.0142 62  ALA B O     
2474  C CB    . ALA B 60  ? 0.8964 0.7998 0.8823 -0.0630 0.1544  0.0119  62  ALA B CB    
2475  N N     . LEU B 61  ? 0.8176 0.7552 0.7878 -0.0509 0.1234  0.0020  63  LEU B N     
2476  C CA    . LEU B 61  ? 0.7717 0.7254 0.7403 -0.0504 0.1115  -0.0062 63  LEU B CA    
2477  C C     . LEU B 61  ? 0.7163 0.6856 0.6808 -0.0468 0.1100  -0.0037 63  LEU B C     
2478  O O     . LEU B 61  ? 0.6081 0.5909 0.5712 -0.0446 0.1008  -0.0094 63  LEU B O     
2479  C CB    . LEU B 61  ? 0.7919 0.7472 0.7561 -0.0439 0.1037  -0.0066 63  LEU B CB    
2480  C CG    . LEU B 61  ? 0.8695 0.8225 0.8387 -0.0487 0.0975  -0.0159 63  LEU B CG    
2481  C CD1   . LEU B 61  ? 0.8636 0.8019 0.8385 -0.0545 0.1041  -0.0177 63  LEU B CD1   
2482  C CD2   . LEU B 61  ? 0.8733 0.8306 0.8382 -0.0422 0.0899  -0.0159 63  LEU B CD2   
2483  N N     . VAL B 62  ? 0.6964 0.6637 0.6598 -0.0462 0.1196  0.0047  64  VAL B N     
2484  C CA    . VAL B 62  ? 0.6893 0.6730 0.6489 -0.0428 0.1191  0.0073  64  VAL B CA    
2485  C C     . VAL B 62  ? 0.6431 0.6337 0.6096 -0.0519 0.1176  -0.0022 64  VAL B C     
2486  O O     . VAL B 62  ? 0.6042 0.5860 0.5773 -0.0601 0.1255  -0.0031 64  VAL B O     
2487  C CB    . VAL B 62  ? 0.7200 0.7001 0.6754 -0.0378 0.1309  0.0217  64  VAL B CB    
2488  C CG1   . VAL B 62  ? 0.7010 0.7024 0.6498 -0.0306 0.1291  0.0256  64  VAL B CG1   
2489  C CG2   . VAL B 62  ? 0.7694 0.7373 0.7199 -0.0299 0.1352  0.0316  64  VAL B CG2   
2490  N N     . IML B 63  ? 0.5993 0.6062 0.5654 -0.0508 0.1079  -0.0101 65  IML B N     
2491  C CA    . IML B 63  ? 0.6036 0.6183 0.5758 -0.0583 0.1066  -0.0187 65  IML B CA    
2492  C C     . IML B 63  ? 0.6022 0.6356 0.5713 -0.0542 0.1046  -0.0185 65  IML B C     
2493  O O     . IML B 63  ? 0.5679 0.6127 0.5404 -0.0565 0.0985  -0.0274 65  IML B O     
2494  C CB    . IML B 63  ? 0.5422 0.5580 0.5191 -0.0615 0.0974  -0.0298 65  IML B CB    
2495  C CN    . IML B 63  ? 0.5609 0.5786 0.5221 -0.0425 0.0987  -0.0117 65  IML B CN    
2496  C CG2   . IML B 63  ? 0.5478 0.5694 0.5316 -0.0696 0.0979  -0.0382 65  IML B CG2   
2497  C CG1   . IML B 63  ? 0.5380 0.5390 0.5157 -0.0623 0.0973  -0.0294 65  IML B CG1   
2498  C CD1   . IML B 63  ? 0.4978 0.5014 0.4782 -0.0628 0.0882  -0.0376 65  IML B CD1   
2499  N N     . SER B 64  ? 0.6284 0.6660 0.5912 -0.0476 0.1100  -0.0080 66  SER B N     
2500  C CA    . SER B 64  ? 0.6331 0.6912 0.5923 -0.0425 0.1084  -0.0075 66  SER B CA    
2501  C C     . SER B 64  ? 0.6456 0.7063 0.5975 -0.0353 0.1175  0.0069  66  SER B C     
2502  O O     . SER B 64  ? 0.7055 0.7514 0.6550 -0.0330 0.1240  0.0163  66  SER B O     
2503  C CB    . SER B 64  ? 0.6310 0.7032 0.5889 -0.0365 0.0966  -0.0158 66  SER B CB    
2504  O OG    . SER B 64  ? 0.6185 0.6868 0.5720 -0.0296 0.0940  -0.0122 66  SER B OG    
2505  N N     . HIS B 65  ? 0.5989 0.6797 0.5475 -0.0309 0.1180  0.0087  67  HIS B N     
2506  C CA    . HIS B 65  ? 0.6189 0.7074 0.5597 -0.0222 0.1264  0.0231  67  HIS B CA    
2507  C C     . HIS B 65  ? 0.6228 0.7408 0.5585 -0.0130 0.1196  0.0197  67  HIS B C     
2508  O O     . HIS B 65  ? 0.6294 0.7590 0.5691 -0.0148 0.1097  0.0060  67  HIS B O     
2509  C CB    . HIS B 65  ? 0.6425 0.7233 0.5863 -0.0286 0.1399  0.0320  67  HIS B CB    
2510  C CG    . HIS B 65  ? 0.6533 0.7455 0.6031 -0.0365 0.1384  0.0227  67  HIS B CG    
2511  N ND1   . HIS B 65  ? 0.6223 0.7401 0.5686 -0.0314 0.1356  0.0213  67  HIS B ND1   
2512  C CD2   . HIS B 65  ? 0.6437 0.7277 0.6029 -0.0485 0.1389  0.0134  67  HIS B CD2   
2513  C CE1   . HIS B 65  ? 0.6300 0.7531 0.5831 -0.0401 0.1347  0.0121  67  HIS B CE1   
2514  N NE2   . HIS B 65  ? 0.6392 0.7426 0.6001 -0.0504 0.1367  0.0072  67  HIS B NE2   
2515  N N     . GLY B 66  ? 0.6643 0.7950 0.5915 -0.0025 0.1256  0.0323  68  GLY B N     
2516  C CA    . GLY B 66  ? 0.6504 0.8127 0.5723 0.0076  0.1200  0.0293  68  GLY B CA    
2517  C C     . GLY B 66  ? 0.6901 0.8675 0.6075 0.0112  0.1297  0.0408  68  GLY B C     
2518  O O     . GLY B 66  ? 0.6458 0.8480 0.5553 0.0233  0.1299  0.0463  68  GLY B O     
2519  N N     . ASN B 67  ? 0.6779 0.8418 0.6008 0.0007  0.1380  0.0437  69  ASN B N     
2520  C CA    . ASN B 67  ? 0.6893 0.8658 0.6097 0.0021  0.1484  0.0545  69  ASN B CA    
2521  C C     . ASN B 67  ? 0.6848 0.8783 0.6108 -0.0042 0.1425  0.0408  69  ASN B C     
2522  O O     . ASN B 67  ? 0.6500 0.8537 0.5761 -0.0060 0.1505  0.0466  69  ASN B O     
2523  C CB    . ASN B 67  ? 0.6790 0.8293 0.6026 -0.0048 0.1642  0.0688  69  ASN B CB    
2524  C CG    . ASN B 67  ? 0.6758 0.8119 0.5930 0.0040  0.1717  0.0848  69  ASN B CG    
2525  O OD1   . ASN B 67  ? 0.7066 0.8532 0.6165 0.0151  0.1641  0.0844  69  ASN B OD1   
2526  N ND2   . ASN B 67  ? 0.6894 0.8020 0.6101 -0.0006 0.1868  0.0984  69  ASN B ND2   
2527  N N     . GLY B 68  ? 0.6911 0.8876 0.6221 -0.0073 0.1292  0.0230  70  GLY B N     
2528  C CA    . GLY B 68  ? 0.6953 0.9074 0.6321 -0.0120 0.1225  0.0089  70  GLY B CA    
2529  C C     . GLY B 68  ? 0.6873 0.8835 0.6323 -0.0256 0.1280  0.0065  70  GLY B C     
2530  O O     . GLY B 68  ? 0.7055 0.8833 0.6513 -0.0305 0.1399  0.0182  70  GLY B O     
2531  N N     . GLY C 1   ? 0.5911 0.5938 0.6260 -0.0608 0.0652  -0.0415 2   GLY C N     
2532  C CA    . GLY C 1   ? 0.5429 0.5419 0.5736 -0.0607 0.0625  -0.0413 2   GLY C CA    
2533  C C     . GLY C 1   ? 0.5436 0.5428 0.5718 -0.0584 0.0598  -0.0421 2   GLY C C     
2534  O O     . GLY C 1   ? 0.4694 0.4719 0.5003 -0.0569 0.0593  -0.0431 2   GLY C O     
2535  N N     . SER C 2   ? 0.4856 0.4812 0.5084 -0.0580 0.0582  -0.0417 3   SER C N     
2536  C CA    . SER C 2   ? 0.4425 0.4378 0.4625 -0.0560 0.0559  -0.0422 3   SER C CA    
2537  C C     . SER C 2   ? 0.4185 0.4109 0.4350 -0.0561 0.0538  -0.0420 3   SER C C     
2538  O O     . SER C 2   ? 0.3896 0.3792 0.4043 -0.0574 0.0545  -0.0411 3   SER C O     
2539  C CB    . SER C 2   ? 0.4322 0.4264 0.4480 -0.0547 0.0572  -0.0417 3   SER C CB    
2540  O OG    . SER C 2   ? 0.4722 0.4628 0.4832 -0.0555 0.0587  -0.0403 3   SER C OG    
2541  N N     . LEU C 3   ? 0.4092 0.4019 0.4245 -0.0546 0.0513  -0.0427 4   LEU C N     
2542  C CA    . LEU C 3   ? 0.3828 0.3731 0.3949 -0.0544 0.0494  -0.0426 4   LEU C CA    
2543  C C     . LEU C 3   ? 0.3655 0.3549 0.3732 -0.0528 0.0486  -0.0423 4   LEU C C     
2544  O O     . LEU C 3   ? 0.3368 0.3278 0.3449 -0.0516 0.0482  -0.0429 4   LEU C O     
2545  C CB    . LEU C 3   ? 0.4156 0.4074 0.4310 -0.0542 0.0470  -0.0439 4   LEU C CB    
2546  C CG    . LEU C 3   ? 0.3768 0.3665 0.3892 -0.0536 0.0449  -0.0440 4   LEU C CG    
2547  C CD1   . LEU C 3   ? 0.3806 0.3670 0.3907 -0.0548 0.0457  -0.0429 4   LEU C CD1   
2548  C CD2   . LEU C 3   ? 0.3855 0.3766 0.4007 -0.0532 0.0424  -0.0455 4   LEU C CD2   
2549  N N     . VAL C 4   ? 0.3447 0.3314 0.3481 -0.0530 0.0485  -0.0414 5   VAL C N     
2550  C CA    . VAL C 4   ? 0.3246 0.3105 0.3241 -0.0518 0.0476  -0.0412 5   VAL C CA    
2551  C C     . VAL C 4   ? 0.3078 0.2922 0.3053 -0.0517 0.0460  -0.0409 5   VAL C C     
2552  O O     . VAL C 4   ? 0.2801 0.2625 0.2760 -0.0525 0.0465  -0.0401 5   VAL C O     
2553  C CB    . VAL C 4   ? 0.3359 0.3203 0.3318 -0.0520 0.0492  -0.0403 5   VAL C CB    
2554  C CG1   . VAL C 4   ? 0.3449 0.3284 0.3369 -0.0512 0.0482  -0.0400 5   VAL C CG1   
2555  C CG2   . VAL C 4   ? 0.3479 0.3336 0.3454 -0.0518 0.0509  -0.0406 5   VAL C CG2   
2556  N N     . CYS C 5   ? 0.3090 0.2943 0.3065 -0.0505 0.0441  -0.0416 6   CYS C N     
2557  C CA    . CYS C 5   ? 0.3218 0.3060 0.3173 -0.0500 0.0427  -0.0415 6   CYS C CA    
2558  C C     . CYS C 5   ? 0.3226 0.3064 0.3145 -0.0494 0.0426  -0.0409 6   CYS C C     
2559  O O     . CYS C 5   ? 0.2933 0.2780 0.2845 -0.0488 0.0425  -0.0411 6   CYS C O     
2560  C CB    . CYS C 5   ? 0.3646 0.3499 0.3620 -0.0491 0.0408  -0.0427 6   CYS C CB    
2561  S SG    . CYS C 5   ? 0.4288 0.4149 0.4311 -0.0501 0.0405  -0.0438 6   CYS C SG    
2562  N N     . VAL C 6   ? 0.3359 0.3183 0.3254 -0.0496 0.0425  -0.0401 7   VAL C N     
2563  C CA    . VAL C 6   ? 0.3411 0.3235 0.3275 -0.0493 0.0424  -0.0394 7   VAL C CA    
2564  C C     . VAL C 6   ? 0.3551 0.3374 0.3405 -0.0484 0.0410  -0.0393 7   VAL C C     
2565  O O     . VAL C 6   ? 0.3890 0.3704 0.3754 -0.0482 0.0405  -0.0395 7   VAL C O     
2566  C CB    . VAL C 6   ? 0.3599 0.3410 0.3441 -0.0502 0.0437  -0.0385 7   VAL C CB    
2567  C CG1   . VAL C 6   ? 0.3239 0.3049 0.3090 -0.0509 0.0453  -0.0386 7   VAL C CG1   
2568  C CG2   . VAL C 6   ? 0.3726 0.3519 0.3559 -0.0505 0.0438  -0.0378 7   VAL C CG2   
2569  N N     . GLY C 7   ? 0.3614 0.3447 0.3449 -0.0479 0.0406  -0.0390 8   GLY C N     
2570  C CA    . GLY C 7   ? 0.3555 0.3392 0.3380 -0.0470 0.0396  -0.0388 8   GLY C CA    
2571  C C     . GLY C 7   ? 0.4084 0.3917 0.3888 -0.0474 0.0398  -0.0378 8   GLY C C     
2572  O O     . GLY C 7   ? 0.3961 0.3794 0.3752 -0.0482 0.0405  -0.0375 8   GLY C O     
2573  N N     . THR C 8   ? 0.4004 0.3833 0.3800 -0.0465 0.0390  -0.0375 9   THR C N     
2574  C CA    . THR C 8   ? 0.4456 0.4282 0.4231 -0.0466 0.0389  -0.0366 9   THR C CA    
2575  C C     . THR C 8   ? 0.3919 0.3771 0.3692 -0.0456 0.0379  -0.0365 9   THR C C     
2576  O O     . THR C 8   ? 0.3837 0.3696 0.3597 -0.0454 0.0374  -0.0358 9   THR C O     
2577  C CB    . THR C 8   ? 0.4585 0.4386 0.4354 -0.0462 0.0388  -0.0361 9   THR C CB    
2578  O OG1   . THR C 8   ? 0.4331 0.4132 0.4110 -0.0449 0.0379  -0.0366 9   THR C OG1   
2579  C CG2   . THR C 8   ? 0.4637 0.4415 0.4411 -0.0475 0.0401  -0.0360 9   THR C CG2   
2580  N N     . GLY C 9   ? 0.3648 0.3517 0.3434 -0.0451 0.0377  -0.0371 10  GLY C N     
2581  C CA    . GLY C 9   ? 0.3708 0.3604 0.3494 -0.0441 0.0371  -0.0371 10  GLY C CA    
2582  C C     . GLY C 9   ? 0.3584 0.3478 0.3369 -0.0424 0.0363  -0.0370 10  GLY C C     
2583  O O     . GLY C 9   ? 0.5268 0.5136 0.5052 -0.0420 0.0362  -0.0371 10  GLY C O     
2584  N N     . LEU C 10  ? 0.3543 0.3464 0.3330 -0.0414 0.0358  -0.0368 11  LEU C N     
2585  C CA    . LEU C 10  ? 0.3423 0.3345 0.3209 -0.0394 0.0351  -0.0368 11  LEU C CA    
2586  C C     . LEU C 10  ? 0.3173 0.3098 0.2949 -0.0391 0.0345  -0.0359 11  LEU C C     
2587  O O     . LEU C 10  ? 0.3410 0.3314 0.3177 -0.0379 0.0340  -0.0356 11  LEU C O     
2588  C CB    . LEU C 10  ? 0.3327 0.3280 0.3122 -0.0381 0.0350  -0.0371 11  LEU C CB    
2589  C CG    . LEU C 10  ? 0.3348 0.3292 0.3146 -0.0376 0.0353  -0.0380 11  LEU C CG    
2590  C CD1   . LEU C 10  ? 0.3532 0.3442 0.3325 -0.0366 0.0348  -0.0386 11  LEU C CD1   
2591  C CD2   . LEU C 10  ? 0.3594 0.3534 0.3394 -0.0393 0.0360  -0.0382 11  LEU C CD2   
2592  N N     . GLN C 11  ? 0.3213 0.3163 0.2989 -0.0403 0.0345  -0.0355 12  GLN C N     
2593  C CA    . GLN C 11  ? 0.3630 0.3587 0.3396 -0.0400 0.0336  -0.0347 12  GLN C CA    
2594  C C     . GLN C 11  ? 0.3872 0.3791 0.3617 -0.0408 0.0338  -0.0342 12  GLN C C     
2595  O O     . GLN C 11  ? 0.4633 0.4529 0.4375 -0.0422 0.0347  -0.0345 12  GLN C O     
2596  C CB    . GLN C 11  ? 0.3653 0.3648 0.3426 -0.0412 0.0334  -0.0346 12  GLN C CB    
2597  C CG    . GLN C 11  ? 0.3705 0.3745 0.3498 -0.0399 0.0329  -0.0346 12  GLN C CG    
2598  C CD    . GLN C 11  ? 0.3652 0.3701 0.3443 -0.0377 0.0317  -0.0341 12  GLN C CD    
2599  O OE1   . GLN C 11  ? 0.3134 0.3149 0.2904 -0.0370 0.0312  -0.0337 12  GLN C OE1   
2600  N NE2   . GLN C 11  ? 0.4130 0.4224 0.3940 -0.0365 0.0312  -0.0341 12  GLN C NE2   
2601  N N     . LEU C 12  ? 0.3894 0.3804 0.3623 -0.0398 0.0329  -0.0335 13  LEU C N     
2602  C CA    . LEU C 12  ? 0.3702 0.3572 0.3405 -0.0402 0.0332  -0.0328 13  LEU C CA    
2603  C C     . LEU C 12  ? 0.3417 0.3289 0.3107 -0.0421 0.0335  -0.0327 13  LEU C C     
2604  O O     . LEU C 12  ? 0.3649 0.3548 0.3336 -0.0422 0.0325  -0.0325 13  LEU C O     
2605  C CB    . LEU C 12  ? 0.3580 0.3441 0.3267 -0.0382 0.0321  -0.0321 13  LEU C CB    
2606  C CG    . LEU C 12  ? 0.3217 0.3036 0.2870 -0.0384 0.0322  -0.0311 13  LEU C CG    
2607  C CD1   . LEU C 12  ? 0.3688 0.3461 0.3336 -0.0389 0.0335  -0.0310 13  LEU C CD1   
2608  C CD2   . LEU C 12  ? 0.3041 0.2858 0.2675 -0.0361 0.0308  -0.0302 13  LEU C CD2   
2609  N N     . ALA C 13  ? 0.3530 0.3373 0.3212 -0.0436 0.0348  -0.0327 14  ALA C N     
2610  C CA    . ALA C 13  ? 0.3742 0.3571 0.3401 -0.0450 0.0353  -0.0324 14  ALA C CA    
2611  C C     . ALA C 13  ? 0.3823 0.3677 0.3491 -0.0465 0.0355  -0.0331 14  ALA C C     
2612  O O     . ALA C 13  ? 0.4140 0.3978 0.3799 -0.0479 0.0366  -0.0333 14  ALA C O     
2613  C CB    . ALA C 13  ? 0.3536 0.3360 0.3167 -0.0442 0.0341  -0.0316 14  ALA C CB    
2614  N N     . GLY C 14  ? 0.3566 0.3459 0.3252 -0.0462 0.0345  -0.0335 15  GLY C N     
2615  C CA    . GLY C 14  ? 0.3195 0.3109 0.2884 -0.0478 0.0344  -0.0339 15  GLY C CA    
2616  C C     . GLY C 14  ? 0.3421 0.3348 0.3133 -0.0484 0.0353  -0.0346 15  GLY C C     
2617  O O     . GLY C 14  ? 0.2872 0.2811 0.2587 -0.0498 0.0354  -0.0350 15  GLY C O     
2618  N N     . GLN C 15  ? 0.3261 0.3183 0.2989 -0.0474 0.0358  -0.0348 16  GLN C N     
2619  C CA    . GLN C 15  ? 0.3828 0.3761 0.3574 -0.0476 0.0364  -0.0354 16  GLN C CA    
2620  C C     . GLN C 15  ? 0.3885 0.3790 0.3630 -0.0482 0.0376  -0.0357 16  GLN C C     
2621  O O     . GLN C 15  ? 0.4501 0.4411 0.4259 -0.0482 0.0381  -0.0362 16  GLN C O     
2622  C CB    . GLN C 15  ? 0.4073 0.4024 0.3837 -0.0458 0.0360  -0.0355 16  GLN C CB    
2623  C CG    . GLN C 15  ? 0.4353 0.4324 0.4132 -0.0459 0.0364  -0.0359 16  GLN C CG    
2624  C CD    . GLN C 15  ? 0.4634 0.4630 0.4426 -0.0442 0.0360  -0.0360 16  GLN C CD    
2625  O OE1   . GLN C 15  ? 0.4050 0.4035 0.3844 -0.0426 0.0358  -0.0361 16  GLN C OE1   
2626  N NE2   . GLN C 15  ? 0.4451 0.4483 0.4254 -0.0446 0.0360  -0.0358 16  GLN C NE2   
2627  N N     . ILE C 16  ? 0.3509 0.3388 0.3239 -0.0487 0.0381  -0.0355 17  ILE C N     
2628  C CA    . ILE C 16  ? 0.3468 0.3325 0.3200 -0.0493 0.0393  -0.0358 17  ILE C CA    
2629  C C     . ILE C 16  ? 0.3285 0.3140 0.3005 -0.0507 0.0399  -0.0361 17  ILE C C     
2630  O O     . ILE C 16  ? 0.2755 0.2615 0.2459 -0.0513 0.0394  -0.0358 17  ILE C O     
2631  C CB    . ILE C 16  ? 0.3566 0.3395 0.3289 -0.0493 0.0399  -0.0354 17  ILE C CB    
2632  C CG1   . ILE C 16  ? 0.3470 0.3284 0.3203 -0.0499 0.0412  -0.0358 17  ILE C CG1   
2633  C CG2   . ILE C 16  ? 0.3446 0.3264 0.3139 -0.0498 0.0398  -0.0347 17  ILE C CG2   
2634  C CD1   . ILE C 16  ? 0.3480 0.3269 0.3210 -0.0501 0.0421  -0.0353 17  ILE C CD1   
2635  N N     . SER C 17  ? 0.3091 0.2936 0.2819 -0.0510 0.0409  -0.0365 18  SER C N     
2636  C CA    . SER C 17  ? 0.3808 0.3645 0.3522 -0.0521 0.0416  -0.0368 18  SER C CA    
2637  C C     . SER C 17  ? 0.4099 0.3913 0.3789 -0.0527 0.0423  -0.0366 18  SER C C     
2638  O O     . SER C 17  ? 0.3528 0.3331 0.3217 -0.0523 0.0426  -0.0361 18  SER C O     
2639  C CB    . SER C 17  ? 0.3842 0.3675 0.3570 -0.0519 0.0424  -0.0374 18  SER C CB    
2640  O OG    . SER C 17  ? 0.3754 0.3574 0.3491 -0.0515 0.0433  -0.0375 18  SER C OG    
2641  N N     . VAL C 18  ? 0.3955 0.3759 0.3624 -0.0537 0.0427  -0.0368 19  VAL C N     
2642  C CA    . VAL C 18  ? 0.4035 0.3815 0.3674 -0.0542 0.0434  -0.0366 19  VAL C CA    
2643  C C     . VAL C 18  ? 0.3773 0.3537 0.3420 -0.0539 0.0452  -0.0367 19  VAL C C     
2644  O O     . VAL C 18  ? 0.3239 0.2987 0.2872 -0.0539 0.0460  -0.0363 19  VAL C O     
2645  C CB    . VAL C 18  ? 0.3953 0.3723 0.3566 -0.0554 0.0434  -0.0371 19  VAL C CB    
2646  C CG1   . VAL C 18  ? 0.3893 0.3634 0.3471 -0.0557 0.0443  -0.0371 19  VAL C CG1   
2647  C CG2   . VAL C 18  ? 0.4141 0.3931 0.3750 -0.0560 0.0416  -0.0370 19  VAL C CG2   
2648  N N     . LEU C 19  ? 0.3498 0.3267 0.3168 -0.0536 0.0457  -0.0372 20  LEU C N     
2649  C CA    . LEU C 19  ? 0.3860 0.3621 0.3543 -0.0532 0.0472  -0.0375 20  LEU C CA    
2650  C C     . LEU C 19  ? 0.3807 0.3575 0.3516 -0.0528 0.0473  -0.0371 20  LEU C C     
2651  O O     . LEU C 19  ? 0.4008 0.3764 0.3718 -0.0529 0.0486  -0.0369 20  LEU C O     
2652  C CB    . LEU C 19  ? 0.3782 0.3547 0.3481 -0.0528 0.0475  -0.0381 20  LEU C CB    
2653  C CG    . LEU C 19  ? 0.4262 0.4025 0.3980 -0.0523 0.0490  -0.0385 20  LEU C CG    
2654  C CD1   . LEU C 19  ? 0.4497 0.4238 0.4190 -0.0527 0.0506  -0.0385 20  LEU C CD1   
2655  C CD2   . LEU C 19  ? 0.4236 0.4005 0.3969 -0.0515 0.0488  -0.0391 20  LEU C CD2   
2656  N N     . SER C 20  ? 0.3813 0.3597 0.3539 -0.0523 0.0459  -0.0372 21  SER C N     
2657  C CA    . SER C 20  ? 0.3697 0.3485 0.3448 -0.0518 0.0457  -0.0370 21  SER C CA    
2658  C C     . SER C 20  ? 0.3703 0.3475 0.3436 -0.0521 0.0460  -0.0362 21  SER C C     
2659  O O     . SER C 20  ? 0.4247 0.4010 0.3993 -0.0523 0.0469  -0.0360 21  SER C O     
2660  C CB    . SER C 20  ? 0.3609 0.3414 0.3375 -0.0510 0.0441  -0.0373 21  SER C CB    
2661  O OG    . SER C 20  ? 0.3434 0.3250 0.3213 -0.0506 0.0440  -0.0380 21  SER C OG    
2662  N N     . ARG C 21  ? 0.3594 0.3361 0.3297 -0.0522 0.0453  -0.0357 22  ARG C N     
2663  C CA    . ARG C 21  ? 0.3603 0.3352 0.3281 -0.0523 0.0455  -0.0348 22  ARG C CA    
2664  C C     . ARG C 21  ? 0.3442 0.3169 0.3107 -0.0530 0.0475  -0.0345 22  ARG C C     
2665  O O     . ARG C 21  ? 0.3024 0.2734 0.2686 -0.0531 0.0485  -0.0338 22  ARG C O     
2666  C CB    . ARG C 21  ? 0.4236 0.3987 0.3884 -0.0523 0.0442  -0.0345 22  ARG C CB    
2667  C CG    . ARG C 21  ? 0.4342 0.4075 0.3960 -0.0520 0.0439  -0.0335 22  ARG C CG    
2668  C CD    . ARG C 21  ? 0.4532 0.4274 0.4124 -0.0519 0.0423  -0.0334 22  ARG C CD    
2669  N NE    . ARG C 21  ? 0.4615 0.4340 0.4177 -0.0513 0.0417  -0.0324 22  ARG C NE    
2670  C CZ    . ARG C 21  ? 0.5076 0.4770 0.4604 -0.0514 0.0428  -0.0317 22  ARG C CZ    
2671  N NH1   . ARG C 21  ? 0.5866 0.5545 0.5387 -0.0523 0.0447  -0.0319 22  ARG C NH1   
2672  N NH2   . ARG C 21  ? 0.5041 0.4719 0.4542 -0.0506 0.0420  -0.0307 22  ARG C NH2   
2673  N N     . SER C 22  ? 0.3671 0.3398 0.3329 -0.0534 0.0484  -0.0351 23  SER C N     
2674  C CA    . SER C 22  ? 0.3519 0.3227 0.3164 -0.0538 0.0505  -0.0350 23  SER C CA    
2675  C C     . SER C 22  ? 0.3600 0.3313 0.3282 -0.0539 0.0519  -0.0350 23  SER C C     
2676  O O     . SER C 22  ? 0.3665 0.3361 0.3338 -0.0543 0.0537  -0.0344 23  SER C O     
2677  C CB    . SER C 22  ? 0.3745 0.3452 0.3378 -0.0540 0.0510  -0.0357 23  SER C CB    
2678  O OG    . SER C 22  ? 0.3559 0.3248 0.3174 -0.0542 0.0532  -0.0356 23  SER C OG    
2679  N N     . TYR C 23  ? 0.3287 0.3021 0.3008 -0.0535 0.0511  -0.0357 24  TYR C N     
2680  C CA    . TYR C 23  ? 0.3037 0.2779 0.2798 -0.0537 0.0521  -0.0359 24  TYR C CA    
2681  C C     . TYR C 23  ? 0.2880 0.2609 0.2643 -0.0541 0.0522  -0.0351 24  TYR C C     
2682  O O     . TYR C 23  ? 0.2953 0.2676 0.2731 -0.0548 0.0539  -0.0348 24  TYR C O     
2683  C CB    . TYR C 23  ? 0.3186 0.2953 0.2983 -0.0531 0.0507  -0.0369 24  TYR C CB    
2684  C CG    . TYR C 23  ? 0.3354 0.3133 0.3164 -0.0527 0.0512  -0.0377 24  TYR C CG    
2685  C CD1   . TYR C 23  ? 0.3679 0.3465 0.3514 -0.0528 0.0529  -0.0380 24  TYR C CD1   
2686  C CD2   . TYR C 23  ? 0.3620 0.3405 0.3418 -0.0521 0.0501  -0.0381 24  TYR C CD2   
2687  C CE1   . TYR C 23  ? 0.3825 0.3622 0.3671 -0.0521 0.0534  -0.0387 24  TYR C CE1   
2688  C CE2   . TYR C 23  ? 0.3732 0.3522 0.3537 -0.0515 0.0506  -0.0388 24  TYR C CE2   
2689  C CZ    . TYR C 23  ? 0.4230 0.4026 0.4058 -0.0514 0.0521  -0.0391 24  TYR C CZ    
2690  O OH    . TYR C 23  ? 0.5079 0.4879 0.4913 -0.0505 0.0526  -0.0398 24  TYR C OH    
2691  N N     . ILE C 24  ? 0.2871 0.2595 0.2619 -0.0537 0.0505  -0.0347 25  ILE C N     
2692  C CA    . ILE C 24  ? 0.3163 0.2868 0.2906 -0.0538 0.0504  -0.0339 25  ILE C CA    
2693  C C     . ILE C 24  ? 0.3464 0.3140 0.3173 -0.0544 0.0522  -0.0328 25  ILE C C     
2694  O O     . ILE C 24  ? 0.3584 0.3242 0.3297 -0.0550 0.0534  -0.0321 25  ILE C O     
2695  C CB    . ILE C 24  ? 0.3067 0.2773 0.2798 -0.0528 0.0482  -0.0337 25  ILE C CB    
2696  C CG1   . ILE C 24  ? 0.2788 0.2519 0.2551 -0.0522 0.0467  -0.0348 25  ILE C CG1   
2697  C CG2   . ILE C 24  ? 0.2978 0.2656 0.2692 -0.0527 0.0482  -0.0327 25  ILE C CG2   
2698  C CD1   . ILE C 24  ? 0.2759 0.2494 0.2511 -0.0511 0.0448  -0.0347 25  ILE C CD1   
2699  N N     . GLU C 25  ? 0.3481 0.3152 0.3154 -0.0543 0.0525  -0.0326 26  GLU C N     
2700  C CA    . GLU C 25  ? 0.3942 0.3584 0.3572 -0.0545 0.0539  -0.0315 26  GLU C CA    
2701  C C     . GLU C 25  ? 0.3964 0.3599 0.3606 -0.0554 0.0568  -0.0314 26  GLU C C     
2702  O O     . GLU C 25  ? 0.3857 0.3466 0.3480 -0.0559 0.0584  -0.0303 26  GLU C O     
2703  C CB    . GLU C 25  ? 0.4161 0.3802 0.3751 -0.0542 0.0532  -0.0317 26  GLU C CB    
2704  C CG    . GLU C 25  ? 0.4592 0.4200 0.4128 -0.0543 0.0543  -0.0307 26  GLU C CG    
2705  C CD    . GLU C 25  ? 0.4957 0.4561 0.4452 -0.0541 0.0534  -0.0311 26  GLU C CD    
2706  O OE1   . GLU C 25  ? 0.5327 0.4954 0.4837 -0.0541 0.0521  -0.0321 26  GLU C OE1   
2707  O OE2   . GLU C 25  ? 0.5816 0.5393 0.5262 -0.0540 0.0540  -0.0304 26  GLU C OE2   
2708  N N     . HIS C 26  ? 0.3938 0.3597 0.3614 -0.0555 0.0575  -0.0324 27  HIS C N     
2709  C CA    . HIS C 26  ? 0.4122 0.3781 0.3813 -0.0561 0.0602  -0.0324 27  HIS C CA    
2710  C C     . HIS C 26  ? 0.4167 0.3845 0.3916 -0.0568 0.0608  -0.0328 27  HIS C C     
2711  O O     . HIS C 26  ? 0.4012 0.3701 0.3788 -0.0573 0.0630  -0.0329 27  HIS C O     
2712  C CB    . HIS C 26  ? 0.4240 0.3911 0.3926 -0.0556 0.0608  -0.0333 27  HIS C CB    
2713  C CG    . HIS C 26  ? 0.4411 0.4060 0.4039 -0.0553 0.0606  -0.0331 27  HIS C CG    
2714  N ND1   . HIS C 26  ? 0.4923 0.4576 0.4533 -0.0548 0.0585  -0.0337 27  HIS C ND1   
2715  C CD2   . HIS C 26  ? 0.4644 0.4265 0.4226 -0.0554 0.0624  -0.0324 27  HIS C CD2   
2716  C CE1   . HIS C 26  ? 0.4651 0.4280 0.4207 -0.0548 0.0587  -0.0335 27  HIS C CE1   
2717  N NE2   . HIS C 26  ? 0.4747 0.4356 0.4284 -0.0550 0.0611  -0.0327 27  HIS C NE2   
2718  N N     . ALA C 27  ? 0.4206 0.3889 0.3975 -0.0568 0.0588  -0.0329 28  ALA C N     
2719  C CA    . ALA C 27  ? 0.4271 0.3970 0.4094 -0.0575 0.0589  -0.0334 28  ALA C CA    
2720  C C     . ALA C 27  ? 0.3910 0.3585 0.3733 -0.0588 0.0611  -0.0323 28  ALA C C     
2721  O O     . ALA C 27  ? 0.4194 0.3835 0.3971 -0.0588 0.0615  -0.0310 28  ALA C O     
2722  C CB    . ALA C 27  ? 0.4173 0.3877 0.4008 -0.0569 0.0562  -0.0340 28  ALA C CB    
2723  N N     . ASP C 28  ? 0.4210 0.3903 0.4083 -0.0599 0.0624  -0.0327 29  ASP C N     
2724  C CA    . ASP C 28  ? 0.4222 0.3894 0.4105 -0.0615 0.0646  -0.0317 29  ASP C CA    
2725  C C     . ASP C 28  ? 0.4399 0.4048 0.4280 -0.0618 0.0628  -0.0315 29  ASP C C     
2726  O O     . ASP C 28  ? 0.4308 0.3919 0.4161 -0.0625 0.0638  -0.0301 29  ASP C O     
2727  C CB    . ASP C 28  ? 0.4602 0.4308 0.4548 -0.0627 0.0663  -0.0324 29  ASP C CB    
2728  C CG    . ASP C 28  ? 0.4947 0.4675 0.4899 -0.0623 0.0685  -0.0327 29  ASP C CG    
2729  O OD1   . ASP C 28  ? 0.5913 0.5626 0.5814 -0.0612 0.0688  -0.0323 29  ASP C OD1   
2730  O OD2   . ASP C 28  ? 0.4767 0.4529 0.4775 -0.0630 0.0699  -0.0333 29  ASP C OD2   
2731  N N     . ILE C 29  ? 0.4101 0.3771 0.4010 -0.0612 0.0601  -0.0328 30  ILE C N     
2732  C CA    . ILE C 29  ? 0.4078 0.3729 0.3989 -0.0612 0.0582  -0.0329 30  ILE C CA    
2733  C C     . ILE C 29  ? 0.4067 0.3735 0.3976 -0.0595 0.0552  -0.0340 30  ILE C C     
2734  O O     . ILE C 29  ? 0.4046 0.3749 0.3976 -0.0589 0.0546  -0.0350 30  ILE C O     
2735  C CB    . ILE C 29  ? 0.3944 0.3601 0.3910 -0.0631 0.0588  -0.0335 30  ILE C CB    
2736  C CG1   . ILE C 29  ? 0.4237 0.3859 0.4195 -0.0634 0.0574  -0.0333 30  ILE C CG1   
2737  C CG2   . ILE C 29  ? 0.3986 0.3692 0.4007 -0.0629 0.0577  -0.0353 30  ILE C CG2   
2738  C CD1   . ILE C 29  ? 0.4412 0.4035 0.4421 -0.0655 0.0579  -0.0340 30  ILE C CD1   
2739  N N     . VAL C 30  ? 0.3658 0.3303 0.3542 -0.0587 0.0535  -0.0337 31  VAL C N     
2740  C CA    . VAL C 30  ? 0.3536 0.3196 0.3414 -0.0571 0.0509  -0.0346 31  VAL C CA    
2741  C C     . VAL C 30  ? 0.3318 0.2964 0.3210 -0.0569 0.0492  -0.0352 31  VAL C C     
2742  O O     . VAL C 30  ? 0.3326 0.2935 0.3199 -0.0573 0.0495  -0.0344 31  VAL C O     
2743  C CB    . VAL C 30  ? 0.3498 0.3147 0.3325 -0.0557 0.0502  -0.0337 31  VAL C CB    
2744  C CG1   . VAL C 30  ? 0.3505 0.3173 0.3330 -0.0541 0.0478  -0.0345 31  VAL C CG1   
2745  C CG2   . VAL C 30  ? 0.3545 0.3202 0.3353 -0.0559 0.0518  -0.0331 31  VAL C CG2   
2746  N N     . PHE C 31  ? 0.3418 0.3090 0.3339 -0.0564 0.0475  -0.0368 32  PHE C N     
2747  C CA    . PHE C 31  ? 0.3772 0.3433 0.3700 -0.0558 0.0455  -0.0376 32  PHE C CA    
2748  C C     . PHE C 31  ? 0.4092 0.3760 0.3991 -0.0536 0.0438  -0.0377 32  PHE C C     
2749  O O     . PHE C 31  ? 0.4604 0.4302 0.4506 -0.0528 0.0433  -0.0382 32  PHE C O     
2750  C CB    . PHE C 31  ? 0.3803 0.3488 0.3780 -0.0565 0.0447  -0.0393 32  PHE C CB    
2751  C CG    . PHE C 31  ? 0.3865 0.3546 0.3878 -0.0588 0.0464  -0.0393 32  PHE C CG    
2752  C CD1   . PHE C 31  ? 0.3897 0.3603 0.3932 -0.0598 0.0484  -0.0390 32  PHE C CD1   
2753  C CD2   . PHE C 31  ? 0.3764 0.3418 0.3791 -0.0600 0.0460  -0.0397 32  PHE C CD2   
2754  C CE1   . PHE C 31  ? 0.3997 0.3705 0.4069 -0.0620 0.0501  -0.0390 32  PHE C CE1   
2755  C CE2   . PHE C 31  ? 0.3668 0.3322 0.3733 -0.0624 0.0476  -0.0397 32  PHE C CE2   
2756  C CZ    . PHE C 31  ? 0.3773 0.3455 0.3861 -0.0634 0.0497  -0.0393 32  PHE C CZ    
2757  N N     . SER C 32  ? 0.4249 0.3887 0.4120 -0.0527 0.0430  -0.0372 33  SER C N     
2758  C CA    . SER C 32  ? 0.4318 0.3963 0.4161 -0.0507 0.0416  -0.0370 33  SER C CA    
2759  C C     . SER C 32  ? 0.4071 0.3711 0.3918 -0.0494 0.0398  -0.0381 33  SER C C     
2760  O O     . SER C 32  ? 0.4168 0.3782 0.4026 -0.0500 0.0394  -0.0387 33  SER C O     
2761  C CB    . SER C 32  ? 0.3761 0.3379 0.3564 -0.0502 0.0422  -0.0354 33  SER C CB    
2762  O OG    . SER C 32  ? 0.3943 0.3518 0.3736 -0.0505 0.0424  -0.0349 33  SER C OG    
2763  N N     . LEU C 33  ? 0.4351 0.4015 0.4188 -0.0476 0.0386  -0.0385 34  LEU C N     
2764  C CA    . LEU C 33  ? 0.4958 0.4616 0.4789 -0.0459 0.0370  -0.0393 34  LEU C CA    
2765  C C     . LEU C 33  ? 0.4883 0.4561 0.4691 -0.0441 0.0365  -0.0387 34  LEU C C     
2766  O O     . LEU C 33  ? 0.5175 0.4885 0.4989 -0.0434 0.0360  -0.0393 34  LEU C O     
2767  C CB    . LEU C 33  ? 0.5299 0.4975 0.5156 -0.0459 0.0360  -0.0410 34  LEU C CB    
2768  C CG    . LEU C 33  ? 0.5541 0.5200 0.5393 -0.0445 0.0345  -0.0422 34  LEU C CG    
2769  C CD1   . LEU C 33  ? 0.6151 0.5831 0.6022 -0.0442 0.0334  -0.0438 34  LEU C CD1   
2770  C CD2   . LEU C 33  ? 0.5480 0.5139 0.5302 -0.0422 0.0339  -0.0416 34  LEU C CD2   
2771  N N     . LEU C 34  ? 0.5167 0.4826 0.4949 -0.0433 0.0366  -0.0376 35  LEU C N     
2772  C CA    . LEU C 34  ? 0.6101 0.5782 0.5865 -0.0419 0.0361  -0.0368 35  LEU C CA    
2773  C C     . LEU C 34  ? 0.6349 0.6023 0.6101 -0.0395 0.0350  -0.0371 35  LEU C C     
2774  O O     . LEU C 34  ? 0.6058 0.5698 0.5806 -0.0390 0.0346  -0.0374 35  LEU C O     
2775  C CB    . LEU C 34  ? 0.6612 0.6281 0.6355 -0.0425 0.0370  -0.0353 35  LEU C CB    
2776  C CG    . LEU C 34  ? 0.6731 0.6404 0.6483 -0.0447 0.0384  -0.0351 35  LEU C CG    
2777  C CD1   . LEU C 34  ? 0.6552 0.6212 0.6275 -0.0450 0.0391  -0.0336 35  LEU C CD1   
2778  C CD2   . LEU C 34  ? 0.6584 0.6296 0.6354 -0.0451 0.0384  -0.0359 35  LEU C CD2   
2779  N N     . PRO C 35  ? 0.6346 0.6052 0.6092 -0.0380 0.0344  -0.0369 36  PRO C N     
2780  C CA    . PRO C 35  ? 0.6255 0.5963 0.5993 -0.0355 0.0334  -0.0372 36  PRO C CA    
2781  C C     . PRO C 35  ? 0.5944 0.5617 0.5659 -0.0341 0.0330  -0.0363 36  PRO C C     
2782  O O     . PRO C 35  ? 0.6460 0.6110 0.6166 -0.0324 0.0324  -0.0369 36  PRO C O     
2783  C CB    . PRO C 35  ? 0.6409 0.6168 0.6153 -0.0347 0.0332  -0.0370 36  PRO C CB    
2784  C CG    . PRO C 35  ? 0.6692 0.6471 0.6447 -0.0369 0.0340  -0.0370 36  PRO C CG    
2785  C CD    . PRO C 35  ? 0.6250 0.5995 0.6000 -0.0386 0.0347  -0.0364 36  PRO C CD    
2786  N N     . ASP C 36  ? 0.5386 0.5051 0.5085 -0.0347 0.0334  -0.0350 37  ASP C N     
2787  C CA    . ASP C 36  ? 0.5409 0.5043 0.5081 -0.0331 0.0329  -0.0339 37  ASP C CA    
2788  C C     . ASP C 36  ? 0.5126 0.4728 0.4781 -0.0347 0.0338  -0.0327 37  ASP C C     
2789  O O     . ASP C 36  ? 0.4906 0.4510 0.4571 -0.0371 0.0349  -0.0327 37  ASP C O     
2790  C CB    . ASP C 36  ? 0.5760 0.5433 0.5428 -0.0309 0.0320  -0.0334 37  ASP C CB    
2791  C CG    . ASP C 36  ? 0.5919 0.5638 0.5596 -0.0321 0.0321  -0.0331 37  ASP C CG    
2792  O OD1   . ASP C 36  ? 0.5761 0.5466 0.5424 -0.0336 0.0326  -0.0322 37  ASP C OD1   
2793  O OD2   . ASP C 36  ? 0.6747 0.6513 0.6443 -0.0316 0.0318  -0.0337 37  ASP C OD2   
2794  N N     . GLY C 37  ? 0.5133 0.4703 0.4757 -0.0333 0.0334  -0.0315 38  GLY C N     
2795  C CA    . GLY C 37  ? 0.4544 0.4074 0.4142 -0.0345 0.0344  -0.0301 38  GLY C CA    
2796  C C     . GLY C 37  ? 0.4411 0.3968 0.3996 -0.0347 0.0343  -0.0292 38  GLY C C     
2797  O O     . GLY C 37  ? 0.3292 0.2824 0.2856 -0.0361 0.0353  -0.0281 38  GLY C O     
2798  N N     . PHE C 38  ? 0.4269 0.3878 0.3866 -0.0335 0.0332  -0.0296 39  PHE C N     
2799  C CA    . PHE C 38  ? 0.4315 0.3955 0.3903 -0.0340 0.0329  -0.0290 39  PHE C CA    
2800  C C     . PHE C 38  ? 0.4117 0.3773 0.3723 -0.0368 0.0342  -0.0296 39  PHE C C     
2801  O O     . PHE C 38  ? 0.4312 0.3961 0.3900 -0.0381 0.0348  -0.0289 39  PHE C O     
2802  C CB    . PHE C 38  ? 0.4394 0.4089 0.3997 -0.0322 0.0313  -0.0293 39  PHE C CB    
2803  C CG    . PHE C 38  ? 0.4527 0.4213 0.4110 -0.0292 0.0299  -0.0286 39  PHE C CG    
2804  C CD1   . PHE C 38  ? 0.4679 0.4352 0.4230 -0.0283 0.0292  -0.0273 39  PHE C CD1   
2805  C CD2   . PHE C 38  ? 0.4232 0.3925 0.3829 -0.0269 0.0293  -0.0293 39  PHE C CD2   
2806  C CE1   . PHE C 38  ? 0.4640 0.4306 0.4173 -0.0252 0.0277  -0.0267 39  PHE C CE1   
2807  C CE2   . PHE C 38  ? 0.4201 0.3888 0.3781 -0.0238 0.0281  -0.0286 39  PHE C CE2   
2808  C CZ    . PHE C 38  ? 0.4421 0.4095 0.3970 -0.0229 0.0272  -0.0273 39  PHE C CZ    
2809  N N     . SER C 39  ? 0.4205 0.3878 0.3843 -0.0375 0.0345  -0.0308 40  SER C N     
2810  C CA    . SER C 39  ? 0.4692 0.4378 0.4348 -0.0398 0.0357  -0.0314 40  SER C CA    
2811  C C     . SER C 39  ? 0.4490 0.4134 0.4140 -0.0415 0.0372  -0.0311 40  SER C C     
2812  O O     . SER C 39  ? 0.4428 0.4076 0.4083 -0.0433 0.0384  -0.0311 40  SER C O     
2813  C CB    . SER C 39  ? 0.4884 0.4599 0.4573 -0.0398 0.0355  -0.0328 40  SER C CB    
2814  O OG    . SER C 39  ? 0.5882 0.5609 0.5587 -0.0418 0.0365  -0.0334 40  SER C OG    
2815  N N     . GLN C 40  ? 0.4478 0.4081 0.4117 -0.0408 0.0372  -0.0307 41  GLN C N     
2816  C CA    . GLN C 40  ? 0.4358 0.3920 0.3995 -0.0425 0.0388  -0.0303 41  GLN C CA    
2817  C C     . GLN C 40  ? 0.4103 0.3641 0.3704 -0.0431 0.0397  -0.0287 41  GLN C C     
2818  O O     . GLN C 40  ? 0.3865 0.3391 0.3467 -0.0450 0.0415  -0.0285 41  GLN C O     
2819  C CB    . GLN C 40  ? 0.4617 0.4137 0.4249 -0.0417 0.0384  -0.0303 41  GLN C CB    
2820  C CG    . GLN C 40  ? 0.4651 0.4137 0.4297 -0.0439 0.0399  -0.0305 41  GLN C CG    
2821  C CD    . GLN C 40  ? 0.4937 0.4454 0.4625 -0.0455 0.0403  -0.0320 41  GLN C CD    
2822  O OE1   . GLN C 40  ? 0.4701 0.4244 0.4410 -0.0446 0.0391  -0.0333 41  GLN C OE1   
2823  N NE2   . GLN C 40  ? 0.5273 0.4790 0.4975 -0.0477 0.0420  -0.0318 41  GLN C NE2   
2824  N N     A ARG C 41  ? 0.4097 0.3629 0.3666 -0.0412 0.0386  -0.0278 42  ARG C N     
2825  N N     B ARG C 41  ? 0.4196 0.3728 0.3764 -0.0412 0.0386  -0.0278 42  ARG C N     
2826  C CA    A ARG C 41  ? 0.4491 0.4002 0.4019 -0.0414 0.0392  -0.0263 42  ARG C CA    
2827  C CA    B ARG C 41  ? 0.4678 0.4188 0.4206 -0.0414 0.0392  -0.0263 42  ARG C CA    
2828  C C     A ARG C 41  ? 0.4416 0.3960 0.3948 -0.0428 0.0397  -0.0267 42  ARG C C     
2829  C C     B ARG C 41  ? 0.4508 0.4051 0.4040 -0.0427 0.0397  -0.0267 42  ARG C C     
2830  O O     A ARG C 41  ? 0.4655 0.4178 0.4169 -0.0442 0.0413  -0.0260 42  ARG C O     
2831  O O     B ARG C 41  ? 0.4724 0.4247 0.4237 -0.0441 0.0413  -0.0260 42  ARG C O     
2832  C CB    A ARG C 41  ? 0.4458 0.3963 0.3953 -0.0388 0.0374  -0.0254 42  ARG C CB    
2833  C CB    B ARG C 41  ? 0.4796 0.4298 0.4290 -0.0388 0.0375  -0.0254 42  ARG C CB    
2834  C CG    A ARG C 41  ? 0.4894 0.4347 0.4366 -0.0373 0.0372  -0.0245 42  ARG C CG    
2835  C CG    B ARG C 41  ? 0.5430 0.4877 0.4901 -0.0375 0.0375  -0.0244 42  ARG C CG    
2836  C CD    A ARG C 41  ? 0.5016 0.4461 0.4449 -0.0346 0.0356  -0.0233 42  ARG C CD    
2837  C CD    B ARG C 41  ? 0.5654 0.5090 0.5085 -0.0347 0.0358  -0.0233 42  ARG C CD    
2838  N NE    A ARG C 41  ? 0.5098 0.4482 0.4500 -0.0331 0.0356  -0.0222 42  ARG C NE    
2839  N NE    B ARG C 41  ? 0.5798 0.5280 0.5250 -0.0325 0.0337  -0.0241 42  ARG C NE    
2840  C CZ    A ARG C 41  ? 0.5458 0.4835 0.4850 -0.0302 0.0340  -0.0221 42  ARG C CZ    
2841  C CZ    B ARG C 41  ? 0.5808 0.5294 0.5284 -0.0315 0.0332  -0.0251 42  ARG C CZ    
2842  N NH1   A ARG C 41  ? 0.5579 0.5013 0.4994 -0.0285 0.0322  -0.0230 42  ARG C NH1   
2843  N NH1   B ARG C 41  ? 0.5578 0.5107 0.5071 -0.0293 0.0315  -0.0257 42  ARG C NH1   
2844  N NH2   A ARG C 41  ? 0.5534 0.4848 0.4894 -0.0290 0.0342  -0.0210 42  ARG C NH2   
2845  N NH2   B ARG C 41  ? 0.5945 0.5394 0.5431 -0.0326 0.0344  -0.0254 42  ARG C NH2   
2846  N N     . TRP C 42  ? 0.4535 0.4127 0.4089 -0.0423 0.0384  -0.0277 43  TRP C N     
2847  C CA    . TRP C 42  ? 0.3928 0.3551 0.3487 -0.0436 0.0388  -0.0282 43  TRP C CA    
2848  C C     . TRP C 42  ? 0.4418 0.4030 0.3991 -0.0457 0.0409  -0.0285 43  TRP C C     
2849  O O     . TRP C 42  ? 0.4329 0.3934 0.3883 -0.0468 0.0420  -0.0282 43  TRP C O     
2850  C CB    . TRP C 42  ? 0.3744 0.3418 0.3332 -0.0431 0.0374  -0.0293 43  TRP C CB    
2851  C CG    . TRP C 42  ? 0.3264 0.2964 0.2864 -0.0448 0.0380  -0.0301 43  TRP C CG    
2852  C CD1   . TRP C 42  ? 0.3044 0.2755 0.2623 -0.0453 0.0377  -0.0299 43  TRP C CD1   
2853  C CD2   . TRP C 42  ? 0.3410 0.3125 0.3043 -0.0459 0.0389  -0.0312 43  TRP C CD2   
2854  N NE1   . TRP C 42  ? 0.3029 0.2758 0.2625 -0.0468 0.0385  -0.0308 43  TRP C NE1   
2855  C CE2   . TRP C 42  ? 0.3202 0.2935 0.2831 -0.0470 0.0392  -0.0315 43  TRP C CE2   
2856  C CE3   . TRP C 42  ? 0.3411 0.3127 0.3075 -0.0460 0.0393  -0.0319 43  TRP C CE3   
2857  C CZ2   . TRP C 42  ? 0.3300 0.3048 0.2953 -0.0481 0.0400  -0.0325 43  TRP C CZ2   
2858  C CZ3   . TRP C 42  ? 0.3628 0.3362 0.3316 -0.0470 0.0400  -0.0329 43  TRP C CZ3   
2859  C CH2   . TRP C 42  ? 0.3509 0.3259 0.3192 -0.0480 0.0404  -0.0331 43  TRP C CH2   
2860  N N     . LEU C 43  ? 0.4099 0.3711 0.3706 -0.0462 0.0414  -0.0293 44  LEU C N     
2861  C CA    . LEU C 43  ? 0.4262 0.3873 0.3893 -0.0481 0.0432  -0.0298 44  LEU C CA    
2862  C C     . LEU C 43  ? 0.4362 0.3932 0.3970 -0.0491 0.0451  -0.0287 44  LEU C C     
2863  O O     . LEU C 43  ? 0.3828 0.3398 0.3436 -0.0504 0.0468  -0.0286 44  LEU C O     
2864  C CB    . LEU C 43  ? 0.4594 0.4212 0.4264 -0.0482 0.0429  -0.0310 44  LEU C CB    
2865  C CG    . LEU C 43  ? 0.4947 0.4569 0.4650 -0.0500 0.0445  -0.0316 44  LEU C CG    
2866  C CD1   . LEU C 43  ? 0.5093 0.4749 0.4807 -0.0505 0.0448  -0.0323 44  LEU C CD1   
2867  C CD2   . LEU C 43  ? 0.5073 0.4696 0.4810 -0.0500 0.0439  -0.0327 44  LEU C CD2   
2868  N N     . THR C 44  ? 0.4506 0.4039 0.4092 -0.0483 0.0449  -0.0277 45  THR C N     
2869  C CA    . THR C 44  ? 0.5434 0.4922 0.4997 -0.0493 0.0469  -0.0264 45  THR C CA    
2870  C C     . THR C 44  ? 0.5369 0.4848 0.4890 -0.0495 0.0478  -0.0254 45  THR C C     
2871  O O     . THR C 44  ? 0.5491 0.4950 0.5003 -0.0509 0.0502  -0.0247 45  THR C O     
2872  C CB    . THR C 44  ? 0.5840 0.5286 0.5381 -0.0481 0.0462  -0.0254 45  THR C CB    
2873  O OG1   . THR C 44  ? 0.5533 0.4986 0.5113 -0.0483 0.0456  -0.0266 45  THR C OG1   
2874  C CG2   . THR C 44  ? 0.5686 0.5079 0.5196 -0.0491 0.0484  -0.0238 45  THR C CG2   
2875  N N     . LYS C 45  ? 0.5831 0.5327 0.5327 -0.0480 0.0460  -0.0253 46  LYS C N     
2876  C CA    . LYS C 45  ? 0.5998 0.5486 0.5449 -0.0480 0.0464  -0.0245 46  LYS C CA    
2877  C C     . LYS C 45  ? 0.5809 0.5324 0.5278 -0.0494 0.0475  -0.0255 46  LYS C C     
2878  O O     . LYS C 45  ? 0.5695 0.5196 0.5131 -0.0500 0.0488  -0.0250 46  LYS C O     
2879  C CB    . LYS C 45  ? 0.7163 0.6664 0.6588 -0.0461 0.0438  -0.0243 46  LYS C CB    
2880  C CG    . LYS C 45  ? 0.7860 0.7332 0.7262 -0.0442 0.0426  -0.0232 46  LYS C CG    
2881  C CD    . LYS C 45  ? 0.8664 0.8153 0.8039 -0.0422 0.0400  -0.0230 46  LYS C CD    
2882  C CE    . LYS C 45  ? 0.9204 0.8682 0.8531 -0.0423 0.0400  -0.0223 46  LYS C CE    
2883  N NZ    . LYS C 45  ? 0.9582 0.9079 0.8886 -0.0403 0.0372  -0.0221 46  LYS C NZ    
2884  N N     . LEU C 46  ? 0.5236 0.4788 0.4753 -0.0499 0.0470  -0.0270 47  LEU C N     
2885  C CA    . LEU C 46  ? 0.4658 0.4235 0.4192 -0.0510 0.0479  -0.0280 47  LEU C CA    
2886  C C     . LEU C 46  ? 0.4820 0.4383 0.4372 -0.0524 0.0506  -0.0279 47  LEU C C     
2887  O O     . LEU C 46  ? 0.4892 0.4456 0.4437 -0.0532 0.0522  -0.0280 47  LEU C O     
2888  C CB    . LEU C 46  ? 0.4908 0.4526 0.4483 -0.0507 0.0464  -0.0294 47  LEU C CB    
2889  C CG    . LEU C 46  ? 0.5529 0.5173 0.5110 -0.0513 0.0464  -0.0303 47  LEU C CG    
2890  C CD1   . LEU C 46  ? 0.5736 0.5414 0.5358 -0.0511 0.0453  -0.0315 47  LEU C CD1   
2891  C CD2   . LEU C 46  ? 0.5979 0.5612 0.5559 -0.0524 0.0488  -0.0304 47  LEU C CD2   
2892  N N     . ASN C 47  ? 0.4054 0.3605 0.3632 -0.0527 0.0511  -0.0277 48  ASN C N     
2893  C CA    . ASN C 47  ? 0.4462 0.4003 0.4065 -0.0543 0.0536  -0.0276 48  ASN C CA    
2894  C C     . ASN C 47  ? 0.4621 0.4130 0.4228 -0.0545 0.0538  -0.0269 48  ASN C C     
2895  O O     . ASN C 47  ? 0.4995 0.4511 0.4626 -0.0540 0.0521  -0.0276 48  ASN C O     
2896  C CB    . ASN C 47  ? 0.4516 0.4095 0.4172 -0.0550 0.0537  -0.0292 48  ASN C CB    
2897  C CG    . ASN C 47  ? 0.3886 0.3462 0.3569 -0.0565 0.0564  -0.0291 48  ASN C CG    
2898  O OD1   . ASN C 47  ? 0.4154 0.3706 0.3844 -0.0574 0.0575  -0.0284 48  ASN C OD1   
2899  N ND2   . ASN C 47  ? 0.3569 0.3170 0.3269 -0.0569 0.0575  -0.0299 48  ASN C ND2   
2900  N N     . PRO C 48  ? 0.5224 0.4693 0.4803 -0.0553 0.0559  -0.0254 49  PRO C N     
2901  C CA    . PRO C 48  ? 0.5847 0.5277 0.5422 -0.0555 0.0561  -0.0245 49  PRO C CA    
2902  C C     . PRO C 48  ? 0.5949 0.5386 0.5580 -0.0571 0.0568  -0.0254 49  PRO C C     
2903  O O     . PRO C 48  ? 0.5671 0.5085 0.5309 -0.0570 0.0559  -0.0254 49  PRO C O     
2904  C CB    . PRO C 48  ? 0.5848 0.5235 0.5374 -0.0561 0.0586  -0.0226 49  PRO C CB    
2905  C CG    . PRO C 48  ? 0.5727 0.5138 0.5259 -0.0570 0.0605  -0.0230 49  PRO C CG    
2906  C CD    . PRO C 48  ? 0.5919 0.5375 0.5467 -0.0559 0.0582  -0.0246 49  PRO C CD    
2907  N N     . ASN C 49  ? 0.5779 0.5249 0.5452 -0.0584 0.0582  -0.0263 50  ASN C N     
2908  C CA    . ASN C 49  ? 0.5631 0.5114 0.5361 -0.0601 0.0588  -0.0273 50  ASN C CA    
2909  C C     . ASN C 49  ? 0.5447 0.4961 0.5211 -0.0592 0.0560  -0.0291 50  ASN C C     
2910  O O     . ASN C 49  ? 0.5048 0.4604 0.4845 -0.0591 0.0555  -0.0303 50  ASN C O     
2911  C CB    . ASN C 49  ? 0.6085 0.5595 0.5849 -0.0616 0.0613  -0.0276 50  ASN C CB    
2912  C CG    . ASN C 49  ? 0.6263 0.5784 0.6086 -0.0635 0.0621  -0.0284 50  ASN C CG    
2913  O OD1   . ASN C 49  ? 0.6685 0.6186 0.6520 -0.0640 0.0610  -0.0286 50  ASN C OD1   
2914  N ND2   . ASN C 49  ? 0.6342 0.5896 0.6205 -0.0647 0.0641  -0.0290 50  ASN C ND2   
2915  N N     . VAL C 50  ? 0.5427 0.4917 0.5180 -0.0583 0.0542  -0.0291 51  VAL C N     
2916  C CA    . VAL C 50  ? 0.4581 0.4095 0.4358 -0.0572 0.0516  -0.0306 51  VAL C CA    
2917  C C     . VAL C 50  ? 0.4392 0.3883 0.4193 -0.0580 0.0510  -0.0312 51  VAL C C     
2918  O O     . VAL C 50  ? 0.4304 0.3748 0.4080 -0.0583 0.0516  -0.0301 51  VAL C O     
2919  C CB    . VAL C 50  ? 0.4766 0.4280 0.4504 -0.0548 0.0496  -0.0303 51  VAL C CB    
2920  C CG1   . VAL C 50  ? 0.4592 0.4126 0.4351 -0.0535 0.0471  -0.0318 51  VAL C CG1   
2921  C CG2   . VAL C 50  ? 0.4479 0.4017 0.4196 -0.0542 0.0498  -0.0300 51  VAL C CG2   
2922  N N     . ILE C 51  ? 0.4581 0.4103 0.4428 -0.0583 0.0499  -0.0330 52  ILE C N     
2923  C CA    . ILE C 51  ? 0.4606 0.4109 0.4473 -0.0587 0.0486  -0.0340 52  ILE C CA    
2924  C C     . ILE C 51  ? 0.4240 0.3761 0.4103 -0.0565 0.0459  -0.0352 52  ILE C C     
2925  O O     . ILE C 51  ? 0.4455 0.4019 0.4337 -0.0559 0.0451  -0.0362 52  ILE C O     
2926  C CB    . ILE C 51  ? 0.5126 0.4648 0.5050 -0.0610 0.0493  -0.0351 52  ILE C CB    
2927  C CG1   . ILE C 51  ? 0.5078 0.4584 0.5008 -0.0633 0.0524  -0.0338 52  ILE C CG1   
2928  C CG2   . ILE C 51  ? 0.4819 0.4324 0.4764 -0.0614 0.0475  -0.0366 52  ILE C CG2   
2929  C CD1   . ILE C 51  ? 0.5678 0.5205 0.5593 -0.0631 0.0542  -0.0328 52  ILE C CD1   
2930  N N     . ASN C 52  ? 0.4099 0.3585 0.3936 -0.0553 0.0446  -0.0351 53  ASN C N     
2931  C CA    . ASN C 52  ? 0.3973 0.3472 0.3802 -0.0530 0.0423  -0.0362 53  ASN C CA    
2932  C C     . ASN C 52  ? 0.3872 0.3378 0.3737 -0.0535 0.0409  -0.0381 53  ASN C C     
2933  O O     . ASN C 52  ? 0.3996 0.3468 0.3872 -0.0549 0.0411  -0.0385 53  ASN C O     
2934  C CB    . ASN C 52  ? 0.4072 0.3533 0.3857 -0.0510 0.0415  -0.0352 53  ASN C CB    
2935  C CG    . ASN C 52  ? 0.4232 0.3713 0.4009 -0.0485 0.0395  -0.0361 53  ASN C CG    
2936  O OD1   . ASN C 52  ? 0.4840 0.4358 0.4642 -0.0483 0.0386  -0.0375 53  ASN C OD1   
2937  N ND2   . ASN C 52  ? 0.4584 0.4042 0.4325 -0.0464 0.0387  -0.0353 53  ASN C ND2   
2938  N N     . LEU C 53  ? 0.4077 0.3624 0.3958 -0.0524 0.0396  -0.0394 54  LEU C N     
2939  C CA    . LEU C 53  ? 0.4236 0.3793 0.4147 -0.0527 0.0381  -0.0414 54  LEU C CA    
2940  C C     . LEU C 53  ? 0.4792 0.4317 0.4680 -0.0510 0.0364  -0.0421 54  LEU C C     
2941  O O     . LEU C 53  ? 0.4725 0.4244 0.4631 -0.0513 0.0350  -0.0438 54  LEU C O     
2942  C CB    . LEU C 53  ? 0.3967 0.3575 0.3896 -0.0519 0.0374  -0.0423 54  LEU C CB    
2943  C CG    . LEU C 53  ? 0.4089 0.3729 0.4043 -0.0533 0.0390  -0.0419 54  LEU C CG    
2944  C CD1   . LEU C 53  ? 0.3832 0.3516 0.3798 -0.0523 0.0381  -0.0428 54  LEU C CD1   
2945  C CD2   . LEU C 53  ? 0.4330 0.3965 0.4323 -0.0558 0.0399  -0.0423 54  LEU C CD2   
2946  N N     . GLN C 54  ? 0.5321 0.4826 0.5169 -0.0492 0.0364  -0.0409 55  GLN C N     
2947  C CA    . GLN C 54  ? 0.5826 0.5303 0.5649 -0.0471 0.0349  -0.0415 55  GLN C CA    
2948  C C     . GLN C 54  ? 0.5526 0.4951 0.5352 -0.0483 0.0346  -0.0422 55  GLN C C     
2949  O O     . GLN C 54  ? 0.4826 0.4227 0.4638 -0.0469 0.0331  -0.0434 55  GLN C O     
2950  C CB    . GLN C 54  ? 0.6493 0.5957 0.6276 -0.0451 0.0353  -0.0398 55  GLN C CB    
2951  C CG    . GLN C 54  ? 0.7312 0.6767 0.7070 -0.0422 0.0338  -0.0404 55  GLN C CG    
2952  C CD    . GLN C 54  ? 0.8306 0.7812 0.8073 -0.0406 0.0329  -0.0413 55  GLN C CD    
2953  O OE1   . GLN C 54  ? 0.9148 0.8654 0.8917 -0.0396 0.0317  -0.0428 55  GLN C OE1   
2954  N NE2   . GLN C 54  ? 0.8914 0.8460 0.8683 -0.0406 0.0336  -0.0403 55  GLN C NE2   
2955  N N     . GLN C 55  ? 0.5034 0.4442 0.4877 -0.0510 0.0361  -0.0415 56  GLN C N     
2956  C CA    . GLN C 55  ? 0.5361 0.4714 0.5205 -0.0527 0.0362  -0.0418 56  GLN C CA    
2957  C C     . GLN C 55  ? 0.5349 0.4709 0.5227 -0.0537 0.0346  -0.0442 56  GLN C C     
2958  O O     . GLN C 55  ? 0.5440 0.4752 0.5315 -0.0546 0.0340  -0.0450 56  GLN C O     
2959  C CB    . GLN C 55  ? 0.5499 0.4839 0.5356 -0.0555 0.0386  -0.0403 56  GLN C CB    
2960  C CG    . GLN C 55  ? 0.5296 0.4689 0.5201 -0.0576 0.0395  -0.0408 56  GLN C CG    
2961  C CD    . GLN C 55  ? 0.5242 0.4622 0.5160 -0.0603 0.0422  -0.0393 56  GLN C CD    
2962  O OE1   . GLN C 55  ? 0.5714 0.5055 0.5643 -0.0625 0.0429  -0.0393 56  GLN C OE1   
2963  N NE2   . GLN C 55  ? 0.5206 0.4615 0.5119 -0.0602 0.0438  -0.0380 56  GLN C NE2   
2964  N N     . PHE C 56  ? 0.5582 0.4996 0.5488 -0.0535 0.0338  -0.0454 57  PHE C N     
2965  C CA    . PHE C 56  ? 0.5337 0.4764 0.5279 -0.0547 0.0322  -0.0477 57  PHE C CA    
2966  C C     . PHE C 56  ? 0.5020 0.4437 0.4938 -0.0521 0.0299  -0.0493 57  PHE C C     
2967  O O     . PHE C 56  ? 0.4114 0.3531 0.4050 -0.0526 0.0282  -0.0514 57  PHE C O     
2968  C CB    . PHE C 56  ? 0.5634 0.5123 0.5617 -0.0556 0.0326  -0.0481 57  PHE C CB    
2969  C CG    . PHE C 56  ? 0.5662 0.5161 0.5675 -0.0584 0.0349  -0.0468 57  PHE C CG    
2970  C CD1   . PHE C 56  ? 0.5652 0.5134 0.5701 -0.0613 0.0353  -0.0474 57  PHE C CD1   
2971  C CD2   . PHE C 56  ? 0.6034 0.5560 0.6041 -0.0581 0.0367  -0.0452 57  PHE C CD2   
2972  C CE1   . PHE C 56  ? 0.5405 0.4898 0.5481 -0.0638 0.0378  -0.0462 57  PHE C CE1   
2973  C CE2   . PHE C 56  ? 0.5421 0.4955 0.5452 -0.0604 0.0390  -0.0441 57  PHE C CE2   
2974  C CZ    . PHE C 56  ? 0.5644 0.5163 0.5711 -0.0632 0.0397  -0.0445 57  PHE C CZ    
2975  N N     . TYR C 57  ? 0.5461 0.4869 0.5337 -0.0493 0.0299  -0.0484 58  TYR C N     
2976  C CA    . TYR C 57  ? 0.5412 0.4808 0.5260 -0.0466 0.0280  -0.0498 58  TYR C CA    
2977  C C     . TYR C 57  ? 0.5880 0.5209 0.5710 -0.0468 0.0273  -0.0506 58  TYR C C     
2978  O O     . TYR C 57  ? 0.6247 0.5539 0.6078 -0.0487 0.0285  -0.0495 58  TYR C O     
2979  C CB    . TYR C 57  ? 0.5195 0.4606 0.5009 -0.0435 0.0284  -0.0486 58  TYR C CB    
2980  C CG    . TYR C 57  ? 0.5276 0.4750 0.5103 -0.0428 0.0286  -0.0483 58  TYR C CG    
2981  C CD1   . TYR C 57  ? 0.5565 0.5065 0.5394 -0.0415 0.0272  -0.0499 58  TYR C CD1   
2982  C CD2   . TYR C 57  ? 0.5076 0.4578 0.4908 -0.0434 0.0302  -0.0465 58  TYR C CD2   
2983  C CE1   . TYR C 57  ? 0.5666 0.5216 0.5502 -0.0408 0.0276  -0.0496 58  TYR C CE1   
2984  C CE2   . TYR C 57  ? 0.5242 0.4795 0.5083 -0.0429 0.0304  -0.0463 58  TYR C CE2   
2985  C CZ    . TYR C 57  ? 0.5411 0.4988 0.5255 -0.0416 0.0292  -0.0478 58  TYR C CZ    
2986  O OH    . TYR C 57  ? 0.6047 0.5668 0.5896 -0.0411 0.0295  -0.0475 58  TYR C OH    
2987  N N     . ALA C 58  ? 0.6078 0.5391 0.5890 -0.0449 0.0254  -0.0525 59  ALA C N     
2988  C CA    . ALA C 58  ? 0.6359 0.5605 0.6148 -0.0449 0.0244  -0.0535 59  ALA C CA    
2989  C C     . ALA C 58  ? 0.6259 0.5460 0.6014 -0.0439 0.0258  -0.0514 59  ALA C C     
2990  O O     . ALA C 58  ? 0.6013 0.5233 0.5745 -0.0415 0.0265  -0.0500 59  ALA C O     
2991  C CB    . ALA C 58  ? 0.6485 0.5723 0.6248 -0.0421 0.0224  -0.0555 59  ALA C CB    
2992  N N     . GLN C 59  ? 0.7146 0.6285 0.6896 -0.0458 0.0262  -0.0513 60  GLN C N     
2993  C CA    . GLN C 59  ? 0.8248 0.7338 0.7963 -0.0451 0.0275  -0.0493 60  GLN C CA    
2994  C C     . GLN C 59  ? 0.8536 0.7548 0.8216 -0.0441 0.0263  -0.0504 60  GLN C C     
2995  O O     . GLN C 59  ? 0.8063 0.7038 0.7757 -0.0465 0.0256  -0.0520 60  GLN C O     
2996  C CB    . GLN C 59  ? 0.9402 0.8484 0.9139 -0.0485 0.0295  -0.0475 60  GLN C CB    
2997  C CG    . GLN C 59  ? 0.9988 0.9141 0.9758 -0.0496 0.0307  -0.0465 60  GLN C CG    
2998  C CD    . GLN C 59  ? 1.0228 0.9416 0.9973 -0.0466 0.0312  -0.0450 60  GLN C CD    
2999  O OE1   . GLN C 59  ? 1.0315 0.9474 1.0025 -0.0452 0.0320  -0.0432 60  GLN C OE1   
3000  N NE2   . GLN C 59  ? 0.9706 0.8958 0.9471 -0.0458 0.0306  -0.0457 60  GLN C NE2   
3001  N N     . ASN C 60  ? 0.8841 0.7828 0.8476 -0.0404 0.0262  -0.0497 61  ASN C N     
3002  C CA    . ASN C 60  ? 0.9176 0.8084 0.8770 -0.0388 0.0253  -0.0506 61  ASN C CA    
3003  C C     . ASN C 60  ? 0.8223 0.7128 0.7815 -0.0378 0.0232  -0.0536 61  ASN C C     
3004  O O     . ASN C 60  ? 0.8363 0.7229 0.7965 -0.0402 0.0222  -0.0553 61  ASN C O     
3005  C CB    . ASN C 60  ? 1.0352 0.9190 0.9944 -0.0420 0.0262  -0.0499 61  ASN C CB    
3006  C CG    . ASN C 60  ? 1.1217 1.0056 1.0807 -0.0432 0.0284  -0.0469 61  ASN C CG    
3007  O OD1   . ASN C 60  ? 1.0943 0.9777 1.0499 -0.0402 0.0290  -0.0451 61  ASN C OD1   
3008  N ND2   . ASN C 60  ? 1.1549 1.0399 1.1178 -0.0473 0.0297  -0.0464 61  ASN C ND2   
3009  N N     . GLY C 61  ? 0.7090 0.6036 0.6667 -0.0342 0.0225  -0.0541 62  GLY C N     
3010  C CA    . GLY C 61  ? 0.6830 0.5773 0.6396 -0.0326 0.0206  -0.0568 62  GLY C CA    
3011  C C     . GLY C 61  ? 0.6617 0.5556 0.6216 -0.0362 0.0193  -0.0590 62  GLY C C     
3012  O O     . GLY C 61  ? 0.7129 0.6022 0.6711 -0.0359 0.0176  -0.0613 62  GLY C O     
3013  N N     . GLU C 62  ? 0.6737 0.5724 0.6384 -0.0394 0.0201  -0.0582 63  GLU C N     
3014  C CA    . GLU C 62  ? 0.6629 0.5627 0.6317 -0.0429 0.0189  -0.0601 63  GLU C CA    
3015  C C     . GLU C 62  ? 0.6288 0.5345 0.5988 -0.0416 0.0174  -0.0618 63  GLU C C     
3016  O O     . GLU C 62  ? 0.6524 0.5634 0.6221 -0.0394 0.0181  -0.0607 63  GLU C O     
3017  C CB    . GLU C 62  ? 0.7116 0.6139 0.6851 -0.0468 0.0205  -0.0585 63  GLU C CB    
3018  C CG    . GLU C 62  ? 0.7698 0.6758 0.7486 -0.0500 0.0194  -0.0603 63  GLU C CG    
3019  C CD    . GLU C 62  ? 0.8164 0.7257 0.8002 -0.0536 0.0212  -0.0588 63  GLU C CD    
3020  O OE1   . GLU C 62  ? 0.8825 0.7963 0.8668 -0.0529 0.0229  -0.0568 63  GLU C OE1   
3021  O OE2   . GLU C 62  ? 0.8466 0.7539 0.8337 -0.0572 0.0211  -0.0597 63  GLU C OE2   
3022  N N     . VAL C 63  ? 0.6206 0.5252 0.5919 -0.0430 0.0152  -0.0645 64  VAL C N     
3023  C CA    . VAL C 63  ? 0.6110 0.5208 0.5834 -0.0420 0.0136  -0.0662 64  VAL C CA    
3024  C C     . VAL C 63  ? 0.5833 0.4990 0.5617 -0.0452 0.0139  -0.0659 64  VAL C C     
3025  O O     . VAL C 63  ? 0.5833 0.4979 0.5654 -0.0487 0.0132  -0.0669 64  VAL C O     
3026  C CB    . VAL C 63  ? 0.6536 0.5592 0.6239 -0.0415 0.0108  -0.0694 64  VAL C CB    
3027  C CG1   . VAL C 63  ? 0.6358 0.5467 0.6070 -0.0405 0.0090  -0.0712 64  VAL C CG1   
3028  C CG2   . VAL C 63  ? 0.6329 0.5323 0.5970 -0.0381 0.0106  -0.0699 64  VAL C CG2   
3029  N N     . LYS C 64  ? 0.5847 0.5069 0.5643 -0.0441 0.0150  -0.0644 65  LYS C N     
3030  C CA    . LYS C 64  ? 0.5587 0.4866 0.5436 -0.0466 0.0156  -0.0638 65  LYS C CA    
3031  C C     . LYS C 64  ? 0.5043 0.4383 0.4891 -0.0444 0.0153  -0.0638 65  LYS C C     
3032  O O     . LYS C 64  ? 0.4932 0.4287 0.4752 -0.0419 0.0165  -0.0623 65  LYS C O     
3033  C CB    . LYS C 64  ? 0.5788 0.5070 0.5655 -0.0484 0.0183  -0.0611 65  LYS C CB    
3034  C CG    . LYS C 64  ? 0.5709 0.5045 0.5630 -0.0512 0.0193  -0.0604 65  LYS C CG    
3035  C CD    . LYS C 64  ? 0.5693 0.5024 0.5624 -0.0529 0.0221  -0.0578 65  LYS C CD    
3036  C CE    . LYS C 64  ? 0.5325 0.4706 0.5311 -0.0556 0.0232  -0.0573 65  LYS C CE    
3037  N NZ    . LYS C 64  ? 0.5266 0.4636 0.5255 -0.0572 0.0259  -0.0548 65  LYS C NZ    
3038  N N     . ASN C 65  ? 0.4919 0.4294 0.4797 -0.0454 0.0136  -0.0654 66  ASN C N     
3039  C CA    . ASN C 65  ? 0.5248 0.4678 0.5126 -0.0436 0.0133  -0.0654 66  ASN C CA    
3040  C C     . ASN C 65  ? 0.5021 0.4493 0.4921 -0.0443 0.0158  -0.0628 66  ASN C C     
3041  O O     . ASN C 65  ? 0.5450 0.4927 0.5387 -0.0470 0.0171  -0.0619 66  ASN C O     
3042  C CB    . ASN C 65  ? 0.5273 0.4727 0.5180 -0.0446 0.0109  -0.0677 66  ASN C CB    
3043  C CG    . ASN C 65  ? 0.5898 0.5393 0.5788 -0.0420 0.0102  -0.0679 66  ASN C CG    
3044  O OD1   . ASN C 65  ? 0.5952 0.5485 0.5846 -0.0413 0.0119  -0.0660 66  ASN C OD1   
3045  N ND2   . ASN C 65  ? 0.5710 0.5195 0.5577 -0.0404 0.0076  -0.0702 66  ASN C ND2   
3046  N N     . ARG C 66  ? 0.5288 0.4790 0.5165 -0.0418 0.0167  -0.0617 67  ARG C N     
3047  C CA    . ARG C 66  ? 0.5600 0.5139 0.5491 -0.0423 0.0189  -0.0594 67  ARG C CA    
3048  C C     . ARG C 66  ? 0.5322 0.4906 0.5259 -0.0440 0.0187  -0.0597 67  ARG C C     
3049  O O     . ARG C 66  ? 0.5454 0.5065 0.5413 -0.0452 0.0205  -0.0580 67  ARG C O     
3050  C CB    . ARG C 66  ? 0.6090 0.5648 0.5946 -0.0393 0.0197  -0.0583 67  ARG C CB    
3051  C CG    . ARG C 66  ? 0.6231 0.5753 0.6047 -0.0374 0.0203  -0.0577 67  ARG C CG    
3052  C CD    . ARG C 66  ? 0.6096 0.5646 0.5893 -0.0355 0.0219  -0.0558 67  ARG C CD    
3053  N NE    . ARG C 66  ? 0.6157 0.5742 0.5943 -0.0338 0.0215  -0.0563 67  ARG C NE    
3054  C CZ    . ARG C 66  ? 0.5978 0.5553 0.5734 -0.0314 0.0203  -0.0576 67  ARG C CZ    
3055  N NH1   . ARG C 66  ? 0.5585 0.5117 0.5318 -0.0304 0.0194  -0.0588 67  ARG C NH1   
3056  N NH2   . ARG C 66  ? 0.5859 0.5465 0.5605 -0.0301 0.0202  -0.0577 67  ARG C NH2   
3057  N N     . ARG C 67  ? 0.5272 0.4864 0.5222 -0.0441 0.0164  -0.0619 68  ARG C N     
3058  C CA    . ARG C 67  ? 0.5245 0.4880 0.5241 -0.0456 0.0158  -0.0624 68  ARG C CA    
3059  C C     . ARG C 67  ? 0.4923 0.4558 0.4967 -0.0489 0.0170  -0.0619 68  ARG C C     
3060  O O     . ARG C 67  ? 0.5417 0.5089 0.5497 -0.0502 0.0181  -0.0610 68  ARG C O     
3061  C CB    . ARG C 67  ? 0.5289 0.4928 0.5289 -0.0450 0.0127  -0.0650 68  ARG C CB    
3062  C CG    . ARG C 67  ? 0.5660 0.5306 0.5615 -0.0416 0.0116  -0.0655 68  ARG C CG    
3063  C CD    . ARG C 67  ? 0.5946 0.5592 0.5901 -0.0411 0.0084  -0.0682 68  ARG C CD    
3064  N NE    . ARG C 67  ? 0.5910 0.5563 0.5820 -0.0378 0.0074  -0.0685 68  ARG C NE    
3065  C CZ    . ARG C 67  ? 0.6597 0.6287 0.6505 -0.0366 0.0082  -0.0674 68  ARG C CZ    
3066  N NH1   . ARG C 67  ? 0.6940 0.6664 0.6889 -0.0382 0.0097  -0.0660 68  ARG C NH1   
3067  N NH2   . ARG C 67  ? 0.6600 0.6290 0.6462 -0.0338 0.0075  -0.0677 68  ARG C NH2   
3068  N N     . ASP C 68  ? 0.5184 0.4771 0.5223 -0.0503 0.0169  -0.0623 69  ASP C N     
3069  C CA    . ASP C 68  ? 0.5329 0.4909 0.5410 -0.0537 0.0182  -0.0618 69  ASP C CA    
3070  C C     . ASP C 68  ? 0.5270 0.4849 0.5341 -0.0539 0.0213  -0.0590 69  ASP C C     
3071  O O     . ASP C 68  ? 0.5910 0.5511 0.6018 -0.0561 0.0230  -0.0579 69  ASP C O     
3072  C CB    . ASP C 68  ? 0.5872 0.5396 0.5947 -0.0551 0.0170  -0.0631 69  ASP C CB    
3073  C CG    . ASP C 68  ? 0.6083 0.5606 0.6173 -0.0554 0.0138  -0.0661 69  ASP C CG    
3074  O OD1   . ASP C 68  ? 0.5970 0.5534 0.6112 -0.0572 0.0129  -0.0671 69  ASP C OD1   
3075  O OD2   . ASP C 68  ? 0.6348 0.5831 0.6396 -0.0537 0.0121  -0.0675 69  ASP C OD2   
3076  N N     . THR C 69  ? 0.4379 0.3933 0.4400 -0.0516 0.0219  -0.0579 70  THR C N     
3077  C CA    . THR C 69  ? 0.3749 0.3302 0.3755 -0.0515 0.0245  -0.0554 70  THR C CA    
3078  C C     . THR C 69  ? 0.4119 0.3725 0.4149 -0.0519 0.0257  -0.0543 70  THR C C     
3079  O O     . THR C 69  ? 0.3989 0.3602 0.4040 -0.0537 0.0277  -0.0530 70  THR C O     
3080  C CB    . THR C 69  ? 0.3914 0.3445 0.3865 -0.0485 0.0244  -0.0547 70  THR C CB    
3081  O OG1   . THR C 69  ? 0.3594 0.3071 0.3525 -0.0484 0.0235  -0.0556 70  THR C OG1   
3082  C CG2   . THR C 69  ? 0.4076 0.3611 0.4011 -0.0481 0.0267  -0.0522 70  THR C CG2   
3083  N N     . TYR C 70  ? 0.3603 0.3242 0.3627 -0.0499 0.0247  -0.0550 71  TYR C N     
3084  C CA    . TYR C 70  ? 0.3839 0.3524 0.3879 -0.0498 0.0257  -0.0541 71  TYR C CA    
3085  C C     . TYR C 70  ? 0.4199 0.3910 0.4294 -0.0523 0.0261  -0.0545 71  TYR C C     
3086  O O     . TYR C 70  ? 0.4922 0.4656 0.5034 -0.0532 0.0280  -0.0532 71  TYR C O     
3087  C CB    . TYR C 70  ? 0.3574 0.3283 0.3595 -0.0473 0.0243  -0.0549 71  TYR C CB    
3088  C CG    . TYR C 70  ? 0.3511 0.3200 0.3481 -0.0448 0.0242  -0.0544 71  TYR C CG    
3089  C CD1   . TYR C 70  ? 0.3374 0.3042 0.3322 -0.0447 0.0257  -0.0528 71  TYR C CD1   
3090  C CD2   . TYR C 70  ? 0.3543 0.3238 0.3489 -0.0426 0.0226  -0.0555 71  TYR C CD2   
3091  C CE1   . TYR C 70  ? 0.3783 0.3440 0.3691 -0.0424 0.0257  -0.0524 71  TYR C CE1   
3092  C CE2   . TYR C 70  ? 0.3724 0.3405 0.3628 -0.0403 0.0228  -0.0551 71  TYR C CE2   
3093  C CZ    . TYR C 70  ? 0.3678 0.3343 0.3565 -0.0402 0.0243  -0.0535 71  TYR C CZ    
3094  O OH    . TYR C 70  ? 0.4026 0.3683 0.3876 -0.0379 0.0245  -0.0531 71  TYR C OH    
3095  N N     . GLU C 71  ? 0.4325 0.4031 0.4447 -0.0534 0.0242  -0.0565 72  GLU C N     
3096  C CA    . GLU C 71  ? 0.4273 0.4008 0.4454 -0.0558 0.0243  -0.0572 72  GLU C CA    
3097  C C     . GLU C 71  ? 0.4527 0.4248 0.4725 -0.0583 0.0271  -0.0555 72  GLU C C     
3098  O O     . GLU C 71  ? 0.4041 0.3794 0.4274 -0.0596 0.0288  -0.0548 72  GLU C O     
3099  C CB    . GLU C 71  ? 0.4383 0.4111 0.4589 -0.0568 0.0216  -0.0596 72  GLU C CB    
3100  C CG    . GLU C 71  ? 0.4347 0.4109 0.4621 -0.0595 0.0217  -0.0605 72  GLU C CG    
3101  C CD    . GLU C 71  ? 0.4730 0.4550 0.5035 -0.0589 0.0223  -0.0601 72  GLU C CD    
3102  O OE1   . GLU C 71  ? 0.4972 0.4813 0.5262 -0.0565 0.0205  -0.0609 72  GLU C OE1   
3103  O OE2   . GLU C 71  ? 0.4593 0.4434 0.4934 -0.0607 0.0246  -0.0589 72  GLU C OE2   
3104  N N     . GLN C 72  ? 0.4530 0.4199 0.4700 -0.0589 0.0275  -0.0550 73  GLN C N     
3105  C CA    . GLN C 72  ? 0.4963 0.4608 0.5140 -0.0611 0.0301  -0.0533 73  GLN C CA    
3106  C C     . GLN C 72  ? 0.5088 0.4747 0.5243 -0.0602 0.0325  -0.0511 73  GLN C C     
3107  O O     . GLN C 72  ? 0.5976 0.5639 0.6148 -0.0620 0.0349  -0.0497 73  GLN C O     
3108  C CB    . GLN C 72  ? 0.5006 0.4588 0.5150 -0.0614 0.0298  -0.0532 73  GLN C CB    
3109  C CG    . GLN C 72  ? 0.5132 0.4694 0.5300 -0.0629 0.0276  -0.0555 73  GLN C CG    
3110  C CD    . GLN C 72  ? 0.5113 0.4605 0.5243 -0.0631 0.0274  -0.0555 73  GLN C CD    
3111  O OE1   . GLN C 72  ? 0.4477 0.3937 0.4562 -0.0617 0.0287  -0.0537 73  GLN C OE1   
3112  N NE2   . GLN C 72  ? 0.5694 0.5161 0.5841 -0.0646 0.0255  -0.0575 73  GLN C NE2   
3113  N N     . MET C 73  ? 0.5062 0.4727 0.5178 -0.0574 0.0319  -0.0507 74  MET C N     
3114  C CA    . MET C 73  ? 0.4782 0.4461 0.4875 -0.0565 0.0337  -0.0488 74  MET C CA    
3115  C C     . MET C 73  ? 0.4538 0.4264 0.4668 -0.0572 0.0347  -0.0488 74  MET C C     
3116  O O     . MET C 73  ? 0.4641 0.4373 0.4774 -0.0581 0.0370  -0.0473 74  MET C O     
3117  C CB    . MET C 73  ? 0.5140 0.4821 0.5190 -0.0536 0.0327  -0.0487 74  MET C CB    
3118  C CG    . MET C 73  ? 0.5466 0.5104 0.5474 -0.0524 0.0323  -0.0482 74  MET C CG    
3119  S SD    . MET C 73  ? 0.5342 0.4991 0.5308 -0.0491 0.0312  -0.0482 74  MET C SD    
3120  C CE    . MET C 73  ? 0.5027 0.4624 0.4952 -0.0479 0.0310  -0.0476 74  MET C CE    
3121  N N     . VAL C 74  ? 0.4366 0.4125 0.4522 -0.0566 0.0329  -0.0504 75  VAL C N     
3122  C CA    . VAL C 74  ? 0.4340 0.4145 0.4530 -0.0568 0.0336  -0.0506 75  VAL C CA    
3123  C C     . VAL C 74  ? 0.4121 0.3935 0.4359 -0.0595 0.0353  -0.0504 75  VAL C C     
3124  O O     . VAL C 74  ? 0.4289 0.4126 0.4541 -0.0600 0.0373  -0.0494 75  VAL C O     
3125  C CB    . VAL C 74  ? 0.4139 0.3973 0.4346 -0.0554 0.0310  -0.0525 75  VAL C CB    
3126  C CG1   . VAL C 74  ? 0.3821 0.3702 0.4070 -0.0556 0.0314  -0.0528 75  VAL C CG1   
3127  C CG2   . VAL C 74  ? 0.4369 0.4196 0.4527 -0.0526 0.0298  -0.0524 75  VAL C CG2   
3128  N N     . ASN C 75  ? 0.3892 0.3688 0.4153 -0.0613 0.0345  -0.0513 76  ASN C N     
3129  C CA    . ASN C 75  ? 0.3930 0.3738 0.4244 -0.0642 0.0360  -0.0513 76  ASN C CA    
3130  C C     . ASN C 75  ? 0.3574 0.3358 0.3869 -0.0654 0.0394  -0.0490 76  ASN C C     
3131  O O     . ASN C 75  ? 0.3675 0.3484 0.4004 -0.0669 0.0416  -0.0484 76  ASN C O     
3132  C CB    . ASN C 75  ? 0.4279 0.4066 0.4618 -0.0661 0.0344  -0.0529 76  ASN C CB    
3133  C CG    . ASN C 75  ? 0.4382 0.4187 0.4782 -0.0694 0.0360  -0.0530 76  ASN C CG    
3134  O OD1   . ASN C 75  ? 0.5198 0.5056 0.5648 -0.0698 0.0364  -0.0534 76  ASN C OD1   
3135  N ND2   . ASN C 75  ? 0.5156 0.4917 0.5555 -0.0717 0.0370  -0.0525 76  ASN C ND2   
3136  N N     . ALA C 76  ? 0.3662 0.3400 0.3902 -0.0646 0.0397  -0.0478 77  ALA C N     
3137  C CA    . ALA C 76  ? 0.3874 0.3584 0.4086 -0.0654 0.0425  -0.0457 77  ALA C CA    
3138  C C     . ALA C 76  ? 0.4461 0.4202 0.4666 -0.0643 0.0442  -0.0445 77  ALA C C     
3139  O O     . ALA C 76  ? 0.4012 0.3751 0.4220 -0.0656 0.0469  -0.0432 77  ALA C O     
3140  C CB    . ALA C 76  ? 0.3561 0.3219 0.3715 -0.0641 0.0419  -0.0448 77  ALA C CB    
3141  N N     . ILE C 77  ? 0.4236 0.4002 0.4427 -0.0620 0.0427  -0.0452 78  ILE C N     
3142  C CA    . ILE C 77  ? 0.4259 0.4049 0.4437 -0.0609 0.0441  -0.0443 78  ILE C CA    
3143  C C     . ILE C 77  ? 0.4173 0.4004 0.4404 -0.0621 0.0453  -0.0448 78  ILE C C     
3144  O O     . ILE C 77  ? 0.4556 0.4394 0.4786 -0.0625 0.0478  -0.0436 78  ILE C O     
3145  C CB    . ILE C 77  ? 0.3724 0.3527 0.3876 -0.0584 0.0421  -0.0448 78  ILE C CB    
3146  C CG1   . ILE C 77  ? 0.3767 0.3534 0.3868 -0.0571 0.0411  -0.0443 78  ILE C CG1   
3147  C CG2   . ILE C 77  ? 0.3825 0.3653 0.3968 -0.0574 0.0434  -0.0442 78  ILE C CG2   
3148  C CD1   . ILE C 77  ? 0.3535 0.3314 0.3610 -0.0548 0.0394  -0.0448 78  ILE C CD1   
3149  N N     . LEU C 78  ? 0.4011 0.3871 0.4290 -0.0624 0.0436  -0.0465 79  LEU C N     
3150  C CA    . LEU C 78  ? 0.4401 0.4308 0.4736 -0.0631 0.0444  -0.0472 79  LEU C CA    
3151  C C     . LEU C 78  ? 0.4542 0.4447 0.4909 -0.0658 0.0472  -0.0464 79  LEU C C     
3152  O O     . LEU C 78  ? 0.4551 0.4485 0.4943 -0.0662 0.0494  -0.0459 79  LEU C O     
3153  C CB    . LEU C 78  ? 0.4869 0.4806 0.5246 -0.0628 0.0414  -0.0494 79  LEU C CB    
3154  C CG    . LEU C 78  ? 0.5261 0.5218 0.5622 -0.0600 0.0392  -0.0503 79  LEU C CG    
3155  C CD1   . LEU C 78  ? 0.5503 0.5492 0.5871 -0.0589 0.0409  -0.0496 79  LEU C CD1   
3156  C CD2   . LEU C 78  ? 0.5916 0.5836 0.6212 -0.0583 0.0382  -0.0497 79  LEU C CD2   
3157  N N     . ASP C 79  ? 0.4550 0.4418 0.4914 -0.0677 0.0473  -0.0461 80  ASP C N     
3158  C CA    . ASP C 79  ? 0.4731 0.4590 0.5121 -0.0705 0.0501  -0.0452 80  ASP C CA    
3159  C C     . ASP C 79  ? 0.4653 0.4506 0.5013 -0.0702 0.0534  -0.0432 80  ASP C C     
3160  O O     . ASP C 79  ? 0.5085 0.4961 0.5480 -0.0716 0.0561  -0.0427 80  ASP C O     
3161  C CB    . ASP C 79  ? 0.4764 0.4569 0.5136 -0.0721 0.0498  -0.0449 80  ASP C CB    
3162  C CG    . ASP C 79  ? 0.5023 0.4835 0.5443 -0.0737 0.0475  -0.0469 80  ASP C CG    
3163  O OD1   . ASP C 79  ? 0.5245 0.5108 0.5716 -0.0736 0.0460  -0.0485 80  ASP C OD1   
3164  O OD2   . ASP C 79  ? 0.6158 0.5922 0.6561 -0.0750 0.0470  -0.0468 80  ASP C OD2   
3165  N N     . ALA C 80  ? 0.4189 0.4013 0.4484 -0.0682 0.0532  -0.0422 81  ALA C N     
3166  C CA    . ALA C 80  ? 0.3953 0.3767 0.4210 -0.0677 0.0559  -0.0404 81  ALA C CA    
3167  C C     . ALA C 80  ? 0.3627 0.3489 0.3911 -0.0668 0.0569  -0.0409 81  ALA C C     
3168  O O     . ALA C 80  ? 0.3318 0.3188 0.3608 -0.0675 0.0599  -0.0399 81  ALA C O     
3169  C CB    . ALA C 80  ? 0.4052 0.3831 0.4240 -0.0658 0.0548  -0.0395 81  ALA C CB    
3170  N N     . VAL C 81  ? 0.3235 0.3128 0.3534 -0.0651 0.0544  -0.0423 82  VAL C N     
3171  C CA    . VAL C 81  ? 0.3325 0.3260 0.3644 -0.0637 0.0549  -0.0428 82  VAL C CA    
3172  C C     . VAL C 81  ? 0.3422 0.3398 0.3811 -0.0653 0.0565  -0.0434 82  VAL C C     
3173  O O     . VAL C 81  ? 0.3261 0.3258 0.3661 -0.0651 0.0590  -0.0429 82  VAL C O     
3174  C CB    . VAL C 81  ? 0.3423 0.3376 0.3739 -0.0615 0.0517  -0.0442 82  VAL C CB    
3175  C CG1   . VAL C 81  ? 0.3433 0.3426 0.3769 -0.0599 0.0521  -0.0447 82  VAL C CG1   
3176  C CG2   . VAL C 81  ? 0.3518 0.3435 0.3769 -0.0600 0.0504  -0.0436 82  VAL C CG2   
3177  N N     . ARG C 82  ? 0.3643 0.3632 0.4081 -0.0668 0.0550  -0.0446 83  ARG C N     
3178  C CA    . ARG C 82  ? 0.3642 0.3676 0.4155 -0.0686 0.0562  -0.0453 83  ARG C CA    
3179  C C     . ARG C 82  ? 0.3586 0.3605 0.4101 -0.0708 0.0603  -0.0436 83  ARG C C     
3180  O O     . ARG C 82  ? 0.3339 0.3398 0.3905 -0.0717 0.0626  -0.0437 83  ARG C O     
3181  C CB    . ARG C 82  ? 0.3997 0.4042 0.4558 -0.0700 0.0535  -0.0470 83  ARG C CB    
3182  C CG    . ARG C 82  ? 0.4111 0.4184 0.4683 -0.0678 0.0497  -0.0489 83  ARG C CG    
3183  C CD    . ARG C 82  ? 0.4318 0.4400 0.4933 -0.0693 0.0469  -0.0507 83  ARG C CD    
3184  N NE    . ARG C 82  ? 0.4414 0.4439 0.4986 -0.0701 0.0457  -0.0505 83  ARG C NE    
3185  C CZ    . ARG C 82  ? 0.4348 0.4357 0.4899 -0.0689 0.0423  -0.0518 83  ARG C CZ    
3186  N NH1   . ARG C 82  ? 0.4548 0.4592 0.5114 -0.0670 0.0396  -0.0534 83  ARG C NH1   
3187  N NH2   . ARG C 82  ? 0.4216 0.4171 0.4726 -0.0696 0.0416  -0.0515 83  ARG C NH2   
3188  N N     . ALA C 83  ? 0.3544 0.3505 0.4002 -0.0715 0.0612  -0.0421 84  ALA C N     
3189  C CA    . ALA C 83  ? 0.3572 0.3509 0.4017 -0.0733 0.0650  -0.0403 84  ALA C CA    
3190  C C     . ALA C 83  ? 0.3421 0.3371 0.3843 -0.0718 0.0676  -0.0394 84  ALA C C     
3191  O O     . ALA C 83  ? 0.3611 0.3567 0.4048 -0.0731 0.0712  -0.0384 84  ALA C O     
3192  C CB    . ALA C 83  ? 0.3668 0.3537 0.4049 -0.0738 0.0648  -0.0390 84  ALA C CB    
3193  N N     . GLY C 84  ? 0.3404 0.3355 0.3787 -0.0691 0.0660  -0.0397 85  GLY C N     
3194  C CA    . GLY C 84  ? 0.3412 0.3373 0.3771 -0.0674 0.0680  -0.0391 85  GLY C CA    
3195  C C     . GLY C 84  ? 0.3661 0.3573 0.3935 -0.0660 0.0678  -0.0379 85  GLY C C     
3196  O O     . GLY C 84  ? 0.4003 0.3913 0.4245 -0.0647 0.0693  -0.0374 85  GLY C O     
3197  N N     . LYS C 85  ? 0.4089 0.3962 0.4329 -0.0663 0.0659  -0.0376 86  LYS C N     
3198  C CA    . LYS C 85  ? 0.4308 0.4137 0.4472 -0.0652 0.0656  -0.0364 86  LYS C CA    
3199  C C     . LYS C 85  ? 0.4477 0.4319 0.4620 -0.0628 0.0632  -0.0373 86  LYS C C     
3200  O O     . LYS C 85  ? 0.4097 0.3964 0.4270 -0.0621 0.0607  -0.0387 86  LYS C O     
3201  C CB    . LYS C 85  ? 0.4367 0.4155 0.4507 -0.0660 0.0641  -0.0359 86  LYS C CB    
3202  C CG    . LYS C 85  ? 0.4886 0.4654 0.5045 -0.0685 0.0662  -0.0350 86  LYS C CG    
3203  C CD    . LYS C 85  ? 0.5140 0.4863 0.5274 -0.0691 0.0646  -0.0346 86  LYS C CD    
3204  C CE    . LYS C 85  ? 0.5414 0.5114 0.5570 -0.0717 0.0666  -0.0338 86  LYS C CE    
3205  N NZ    . LYS C 85  ? 0.5406 0.5084 0.5532 -0.0725 0.0703  -0.0319 86  LYS C NZ    
3206  N N     . LYS C 86  ? 0.4379 0.4202 0.4467 -0.0617 0.0641  -0.0365 87  LYS C N     
3207  C CA    . LYS C 86  ? 0.4930 0.4756 0.4989 -0.0598 0.0620  -0.0371 87  LYS C CA    
3208  C C     . LYS C 86  ? 0.4854 0.4656 0.4885 -0.0594 0.0594  -0.0370 87  LYS C C     
3209  O O     . LYS C 86  ? 0.4203 0.3972 0.4184 -0.0594 0.0595  -0.0359 87  LYS C O     
3210  C CB    . LYS C 86  ? 0.5127 0.4937 0.5137 -0.0590 0.0637  -0.0363 87  LYS C CB    
3211  C CG    . LYS C 86  ? 0.5531 0.5342 0.5510 -0.0572 0.0619  -0.0369 87  LYS C CG    
3212  C CD    . LYS C 86  ? 0.6010 0.5806 0.5945 -0.0566 0.0636  -0.0364 87  LYS C CD    
3213  C CE    . LYS C 86  ? 0.6135 0.5893 0.6018 -0.0572 0.0648  -0.0350 87  LYS C CE    
3214  N NZ    . LYS C 86  ? 0.6475 0.6216 0.6310 -0.0565 0.0662  -0.0348 87  LYS C NZ    
3215  N N     . THR C 87  ? 0.4533 0.4354 0.4596 -0.0591 0.0570  -0.0382 88  THR C N     
3216  C CA    . THR C 87  ? 0.4328 0.4129 0.4375 -0.0589 0.0547  -0.0382 88  THR C CA    
3217  C C     . THR C 87  ? 0.4172 0.3974 0.4187 -0.0571 0.0527  -0.0385 88  THR C C     
3218  O O     . THR C 87  ? 0.4200 0.4025 0.4224 -0.0561 0.0521  -0.0393 88  THR C O     
3219  C CB    . THR C 87  ? 0.4168 0.3986 0.4266 -0.0596 0.0533  -0.0395 88  THR C CB    
3220  O OG1   . THR C 87  ? 0.4006 0.3824 0.4136 -0.0616 0.0555  -0.0391 88  THR C OG1   
3221  C CG2   . THR C 87  ? 0.4275 0.4069 0.4356 -0.0593 0.0511  -0.0397 88  THR C CG2   
3222  N N     . VAL C 88  ? 0.4136 0.3911 0.4111 -0.0567 0.0516  -0.0378 89  VAL C N     
3223  C CA    . VAL C 88  ? 0.4446 0.4224 0.4394 -0.0552 0.0497  -0.0381 89  VAL C CA    
3224  C C     . VAL C 88  ? 0.4500 0.4267 0.4448 -0.0548 0.0477  -0.0384 89  VAL C C     
3225  O O     . VAL C 88  ? 0.4563 0.4304 0.4502 -0.0554 0.0480  -0.0378 89  VAL C O     
3226  C CB    . VAL C 88  ? 0.4668 0.4428 0.4567 -0.0548 0.0504  -0.0370 89  VAL C CB    
3227  C CG1   . VAL C 88  ? 0.4630 0.4392 0.4504 -0.0536 0.0484  -0.0371 89  VAL C CG1   
3228  C CG2   . VAL C 88  ? 0.4657 0.4425 0.4550 -0.0550 0.0522  -0.0368 89  VAL C CG2   
3229  N N     . CYS C 89  ? 0.5105 0.4889 0.5061 -0.0536 0.0458  -0.0394 90  CYS C N     
3230  C CA    . CYS C 89  ? 0.5716 0.5491 0.5667 -0.0528 0.0439  -0.0399 90  CYS C CA    
3231  C C     . CYS C 89  ? 0.5547 0.5321 0.5461 -0.0515 0.0430  -0.0394 90  CYS C C     
3232  O O     . CYS C 89  ? 0.6206 0.5999 0.6116 -0.0507 0.0425  -0.0398 90  CYS C O     
3233  C CB    . CYS C 89  ? 0.6208 0.6002 0.6191 -0.0524 0.0424  -0.0414 90  CYS C CB    
3234  S SG    . CYS C 89  ? 0.7195 0.6975 0.7167 -0.0512 0.0401  -0.0422 90  CYS C SG    
3235  N N     . ALA C 90  ? 0.4750 0.4501 0.4637 -0.0512 0.0428  -0.0385 91  ALA C N     
3236  C CA    . ALA C 90  ? 0.3872 0.3626 0.3729 -0.0500 0.0420  -0.0380 91  ALA C CA    
3237  C C     . ALA C 90  ? 0.4068 0.3819 0.3923 -0.0487 0.0403  -0.0386 91  ALA C C     
3238  O O     . ALA C 90  ? 0.3880 0.3607 0.3725 -0.0484 0.0400  -0.0382 91  ALA C O     
3239  C CB    . ALA C 90  ? 0.3684 0.3416 0.3509 -0.0503 0.0429  -0.0366 91  ALA C CB    
3240  N N     . LEU C 91  ? 0.4220 0.3994 0.4081 -0.0477 0.0393  -0.0394 92  LEU C N     
3241  C CA    . LEU C 91  ? 0.3971 0.3746 0.3828 -0.0462 0.0378  -0.0400 92  LEU C CA    
3242  C C     . LEU C 91  ? 0.4079 0.3870 0.3915 -0.0452 0.0375  -0.0394 92  LEU C C     
3243  O O     . LEU C 91  ? 0.3716 0.3522 0.3546 -0.0457 0.0382  -0.0390 92  LEU C O     
3244  C CB    . LEU C 91  ? 0.4008 0.3795 0.3885 -0.0458 0.0370  -0.0414 92  LEU C CB    
3245  C CG    . LEU C 91  ? 0.3892 0.3673 0.3798 -0.0470 0.0371  -0.0422 92  LEU C CG    
3246  C CD1   . LEU C 91  ? 0.3870 0.3662 0.3792 -0.0462 0.0357  -0.0437 92  LEU C CD1   
3247  C CD2   . LEU C 91  ? 0.3659 0.3410 0.3566 -0.0477 0.0372  -0.0419 92  LEU C CD2   
3248  N N     . TYR C 92  ? 0.3730 0.3517 0.3554 -0.0437 0.0366  -0.0394 93  TYR C N     
3249  C CA    . TYR C 92  ? 0.3771 0.3578 0.3580 -0.0426 0.0363  -0.0389 93  TYR C CA    
3250  C C     . TYR C 92  ? 0.4182 0.4015 0.3998 -0.0422 0.0362  -0.0395 93  TYR C C     
3251  O O     . TYR C 92  ? 0.4057 0.3888 0.3883 -0.0420 0.0358  -0.0405 93  TYR C O     
3252  C CB    . TYR C 92  ? 0.3629 0.3426 0.3427 -0.0409 0.0354  -0.0388 93  TYR C CB    
3253  C CG    . TYR C 92  ? 0.3897 0.3693 0.3700 -0.0395 0.0346  -0.0400 93  TYR C CG    
3254  C CD1   . TYR C 92  ? 0.4009 0.3832 0.3810 -0.0383 0.0343  -0.0403 93  TYR C CD1   
3255  C CD2   . TYR C 92  ? 0.4454 0.4220 0.4260 -0.0394 0.0341  -0.0407 93  TYR C CD2   
3256  C CE1   . TYR C 92  ? 0.4087 0.3907 0.3887 -0.0369 0.0336  -0.0414 93  TYR C CE1   
3257  C CE2   . TYR C 92  ? 0.4383 0.4146 0.4189 -0.0380 0.0332  -0.0419 93  TYR C CE2   
3258  C CZ    . TYR C 92  ? 0.4285 0.4074 0.4086 -0.0366 0.0329  -0.0423 93  TYR C CZ    
3259  O OH    . TYR C 92  ? 0.5560 0.5342 0.5355 -0.0352 0.0321  -0.0435 93  TYR C OH    
3260  N N     . GLY C 93  ? 0.4307 0.4162 0.4114 -0.0422 0.0364  -0.0389 94  GLY C N     
3261  C CA    . GLY C 93  ? 0.4148 0.4026 0.3958 -0.0420 0.0365  -0.0392 94  GLY C CA    
3262  C C     . GLY C 93  ? 0.3567 0.3441 0.3384 -0.0432 0.0371  -0.0396 94  GLY C C     
3263  O O     . GLY C 93  ? 0.3991 0.3858 0.3807 -0.0445 0.0378  -0.0392 94  GLY C O     
3264  N N     . HIS C 94  ? 0.3508 0.3385 0.3330 -0.0425 0.0368  -0.0403 95  HIS C N     
3265  C CA    . HIS C 94  ? 0.3938 0.3813 0.3767 -0.0432 0.0371  -0.0407 95  HIS C CA    
3266  C C     . HIS C 94  ? 0.4355 0.4217 0.4201 -0.0430 0.0365  -0.0417 95  HIS C C     
3267  O O     . HIS C 94  ? 0.4153 0.4011 0.4000 -0.0419 0.0356  -0.0424 95  HIS C O     
3268  C CB    . HIS C 94  ? 0.4115 0.4001 0.3935 -0.0425 0.0372  -0.0409 95  HIS C CB    
3269  C CG    . HIS C 94  ? 0.3727 0.3610 0.3551 -0.0429 0.0375  -0.0411 95  HIS C CG    
3270  N ND1   . HIS C 94  ? 0.3260 0.3135 0.3101 -0.0431 0.0373  -0.0418 95  HIS C ND1   
3271  C CD2   . HIS C 94  ? 0.3468 0.3352 0.3280 -0.0430 0.0381  -0.0408 95  HIS C CD2   
3272  C CE1   . HIS C 94  ? 0.3532 0.3407 0.3372 -0.0431 0.0377  -0.0419 95  HIS C CE1   
3273  N NE2   . HIS C 94  ? 0.3367 0.3245 0.3188 -0.0430 0.0382  -0.0413 95  HIS C NE2   
3274  N N     . PRO C 95  ? 0.3987 0.3843 0.3848 -0.0442 0.0371  -0.0417 96  PRO C N     
3275  C CA    . PRO C 95  ? 0.4082 0.3929 0.3965 -0.0445 0.0367  -0.0425 96  PRO C CA    
3276  C C     . PRO C 95  ? 0.3832 0.3684 0.3725 -0.0435 0.0354  -0.0438 96  PRO C C     
3277  O O     . PRO C 95  ? 0.3746 0.3591 0.3655 -0.0435 0.0345  -0.0446 96  PRO C O     
3278  C CB    . PRO C 95  ? 0.4146 0.3992 0.4042 -0.0459 0.0380  -0.0422 96  PRO C CB    
3279  C CG    . PRO C 95  ? 0.3968 0.3823 0.3848 -0.0459 0.0387  -0.0416 96  PRO C CG    
3280  C CD    . PRO C 95  ? 0.4093 0.3951 0.3950 -0.0453 0.0383  -0.0411 96  PRO C CD    
3281  N N     . GLY C 96  ? 0.3535 0.3398 0.3418 -0.0426 0.0353  -0.0438 97  GLY C N     
3282  C CA    . GLY C 96  ? 0.3663 0.3530 0.3550 -0.0415 0.0341  -0.0449 97  GLY C CA    
3283  C C     . GLY C 96  ? 0.3876 0.3744 0.3738 -0.0398 0.0334  -0.0451 97  GLY C C     
3284  O O     . GLY C 96  ? 0.4012 0.3882 0.3868 -0.0387 0.0326  -0.0457 97  GLY C O     
3285  N N     . VAL C 97  ? 0.4209 0.4075 0.4055 -0.0396 0.0338  -0.0444 98  VAL C N     
3286  C CA    . VAL C 97  ? 0.4391 0.4260 0.4214 -0.0381 0.0335  -0.0444 98  VAL C CA    
3287  C C     . VAL C 97  ? 0.3889 0.3747 0.3711 -0.0371 0.0324  -0.0453 98  VAL C C     
3288  O O     . VAL C 97  ? 0.3616 0.3468 0.3439 -0.0374 0.0326  -0.0449 98  VAL C O     
3289  C CB    . VAL C 97  ? 0.3887 0.3768 0.3697 -0.0384 0.0347  -0.0432 98  VAL C CB    
3290  C CG1   . VAL C 97  ? 0.4201 0.4089 0.3992 -0.0368 0.0346  -0.0432 98  VAL C CG1   
3291  C CG2   . VAL C 97  ? 0.3621 0.3508 0.3426 -0.0392 0.0357  -0.0425 98  VAL C CG2   
3292  N N     . PHE C 98  ? 0.4036 0.3888 0.3852 -0.0358 0.0311  -0.0465 99  PHE C N     
3293  C CA    . PHE C 98  ? 0.4169 0.4004 0.3980 -0.0349 0.0299  -0.0476 99  PHE C CA    
3294  C C     . PHE C 98  ? 0.3912 0.3735 0.3748 -0.0364 0.0297  -0.0478 99  PHE C C     
3295  O O     . PHE C 98  ? 0.4427 0.4234 0.4257 -0.0362 0.0296  -0.0479 99  PHE C O     
3296  C CB    . PHE C 98  ? 0.4381 0.4217 0.4169 -0.0334 0.0304  -0.0472 99  PHE C CB    
3297  C CG    . PHE C 98  ? 0.4513 0.4357 0.4275 -0.0317 0.0305  -0.0473 99  PHE C CG    
3298  C CD1   . PHE C 98  ? 0.4273 0.4136 0.4027 -0.0320 0.0318  -0.0461 99  PHE C CD1   
3299  C CD2   . PHE C 98  ? 0.5050 0.4881 0.4791 -0.0298 0.0293  -0.0485 99  PHE C CD2   
3300  C CE1   . PHE C 98  ? 0.4692 0.4559 0.4420 -0.0305 0.0322  -0.0460 99  PHE C CE1   
3301  C CE2   . PHE C 98  ? 0.4521 0.4357 0.4234 -0.0282 0.0296  -0.0485 99  PHE C CE2   
3302  C CZ    . PHE C 98  ? 0.4441 0.4295 0.4148 -0.0285 0.0311  -0.0471 99  PHE C CZ    
3303  N N     . ALA C 99  ? 0.3624 0.3452 0.3485 -0.0379 0.0298  -0.0479 100 ALA C N     
3304  C CA    . ALA C 99  ? 0.3752 0.3569 0.3638 -0.0396 0.0299  -0.0480 100 ALA C CA    
3305  C C     . ALA C 99  ? 0.3898 0.3724 0.3814 -0.0404 0.0292  -0.0490 100 ALA C C     
3306  O O     . ALA C 99  ? 0.4912 0.4756 0.4835 -0.0406 0.0298  -0.0486 100 ALA C O     
3307  C CB    . ALA C 99  ? 0.3517 0.3335 0.3404 -0.0408 0.0316  -0.0465 100 ALA C CB    
3308  N N     . CYS C 100 ? 0.3949 0.3763 0.3883 -0.0410 0.0280  -0.0503 101 CYS C N     
3309  C CA    . CYS C 100 ? 0.4188 0.4015 0.4154 -0.0416 0.0269  -0.0515 101 CYS C CA    
3310  C C     . CYS C 100 ? 0.4138 0.3968 0.4142 -0.0439 0.0279  -0.0512 101 CYS C C     
3311  O O     . CYS C 100 ? 0.3878 0.3728 0.3915 -0.0446 0.0276  -0.0519 101 CYS C O     
3312  C CB    . CYS C 100 ? 0.4834 0.4649 0.4799 -0.0408 0.0246  -0.0534 101 CYS C CB    
3313  S SG    . CYS C 100 ? 0.4717 0.4494 0.4679 -0.0417 0.0243  -0.0538 101 CYS C SG    
3314  N N     . VAL C 101 ? 0.4417 0.4229 0.4414 -0.0449 0.0293  -0.0501 102 VAL C N     
3315  C CA    . VAL C 101 ? 0.4043 0.3853 0.4070 -0.0471 0.0306  -0.0496 102 VAL C CA    
3316  C C     . VAL C 101 ? 0.3793 0.3629 0.3838 -0.0477 0.0320  -0.0489 102 VAL C C     
3317  O O     . VAL C 101 ? 0.3375 0.3229 0.3458 -0.0487 0.0321  -0.0495 102 VAL C O     
3318  C CB    . VAL C 101 ? 0.4691 0.4471 0.4698 -0.0478 0.0318  -0.0483 102 VAL C CB    
3319  C CG1   . VAL C 101 ? 0.5338 0.5115 0.5368 -0.0500 0.0336  -0.0475 102 VAL C CG1   
3320  C CG2   . VAL C 101 ? 0.4958 0.4707 0.4950 -0.0472 0.0305  -0.0492 102 VAL C CG2   
3321  N N     . SER C 102 ? 0.3273 0.3113 0.3290 -0.0469 0.0331  -0.0477 103 SER C N     
3322  C CA    . SER C 102 ? 0.3368 0.3226 0.3393 -0.0473 0.0346  -0.0469 103 SER C CA    
3323  C C     . SER C 102 ? 0.3353 0.3236 0.3403 -0.0466 0.0336  -0.0480 103 SER C C     
3324  O O     . SER C 102 ? 0.3846 0.3746 0.3930 -0.0475 0.0343  -0.0483 103 SER C O     
3325  C CB    . SER C 102 ? 0.3685 0.3541 0.3674 -0.0465 0.0355  -0.0457 103 SER C CB    
3326  O OG    . SER C 102 ? 0.3936 0.3774 0.3908 -0.0473 0.0366  -0.0446 103 SER C OG    
3327  N N     . HIS C 103 ? 0.3568 0.3454 0.3599 -0.0449 0.0320  -0.0487 104 HIS C N     
3328  C CA    . HIS C 103 ? 0.3403 0.3309 0.3449 -0.0438 0.0309  -0.0497 104 HIS C CA    
3329  C C     . HIS C 103 ? 0.3672 0.3594 0.3766 -0.0447 0.0298  -0.0510 104 HIS C C     
3330  O O     . HIS C 103 ? 0.4185 0.4131 0.4307 -0.0445 0.0296  -0.0515 104 HIS C O     
3331  C CB    . HIS C 103 ? 0.3350 0.3251 0.3364 -0.0417 0.0292  -0.0502 104 HIS C CB    
3332  C CG    . HIS C 103 ? 0.3003 0.2898 0.2978 -0.0408 0.0303  -0.0489 104 HIS C CG    
3333  N ND1   . HIS C 103 ? 0.2744 0.2624 0.2688 -0.0405 0.0307  -0.0483 104 HIS C ND1   
3334  C CD2   . HIS C 103 ? 0.2700 0.2601 0.2662 -0.0402 0.0311  -0.0483 104 HIS C CD2   
3335  C CE1   . HIS C 103 ? 0.2583 0.2464 0.2500 -0.0399 0.0317  -0.0472 104 HIS C CE1   
3336  N NE2   . HIS C 103 ? 0.2374 0.2265 0.2301 -0.0398 0.0320  -0.0472 104 HIS C NE2   
3337  N N     . MET C 104 ? 0.3873 0.3779 0.3975 -0.0458 0.0291  -0.0517 105 MET C N     
3338  C CA    . MET C 104 ? 0.4153 0.4071 0.4301 -0.0470 0.0280  -0.0531 105 MET C CA    
3339  C C     . MET C 104 ? 0.3666 0.3597 0.3852 -0.0491 0.0301  -0.0523 105 MET C C     
3340  O O     . MET C 104 ? 0.3359 0.3317 0.3593 -0.0499 0.0298  -0.0533 105 MET C O     
3341  C CB    . MET C 104 ? 0.4458 0.4347 0.4598 -0.0476 0.0267  -0.0539 105 MET C CB    
3342  C CG    . MET C 104 ? 0.5008 0.4888 0.5119 -0.0456 0.0243  -0.0551 105 MET C CG    
3343  S SD    . MET C 104 ? 0.5387 0.5227 0.5483 -0.0461 0.0229  -0.0562 105 MET C SD    
3344  C CE    . MET C 104 ? 0.6705 0.6558 0.6865 -0.0487 0.0220  -0.0577 105 MET C CE    
3345  N N     . ALA C 105 ? 0.3594 0.3507 0.3759 -0.0499 0.0324  -0.0507 106 ALA C N     
3346  C CA    . ALA C 105 ? 0.3201 0.3121 0.3392 -0.0517 0.0347  -0.0498 106 ALA C CA    
3347  C C     . ALA C 105 ? 0.3346 0.3295 0.3552 -0.0510 0.0357  -0.0496 106 ALA C C     
3348  O O     . ALA C 105 ? 0.3302 0.3276 0.3552 -0.0520 0.0367  -0.0499 106 ALA C O     
3349  C CB    . ALA C 105 ? 0.3324 0.3213 0.3481 -0.0524 0.0366  -0.0482 106 ALA C CB    
3350  N N     . ILE C 106 ? 0.3418 0.3365 0.3587 -0.0492 0.0356  -0.0491 107 ILE C N     
3351  C CA    . ILE C 106 ? 0.3509 0.3477 0.3683 -0.0482 0.0366  -0.0488 107 ILE C CA    
3352  C C     . ILE C 106 ? 0.3811 0.3811 0.4026 -0.0474 0.0349  -0.0503 107 ILE C C     
3353  O O     . ILE C 106 ? 0.4493 0.4518 0.4741 -0.0474 0.0360  -0.0504 107 ILE C O     
3354  C CB    . ILE C 106 ? 0.3175 0.3127 0.3298 -0.0467 0.0366  -0.0480 107 ILE C CB    
3355  C CG1   . ILE C 106 ? 0.3175 0.3102 0.3263 -0.0476 0.0383  -0.0466 107 ILE C CG1   
3356  C CG2   . ILE C 106 ? 0.3043 0.3011 0.3168 -0.0454 0.0372  -0.0480 107 ILE C CG2   
3357  C CD1   . ILE C 106 ? 0.3011 0.2927 0.3055 -0.0464 0.0386  -0.0458 107 ILE C CD1   
3358  N N     . THR C 107 ? 0.4357 0.4357 0.4568 -0.0464 0.0323  -0.0515 108 THR C N     
3359  C CA    . THR C 107 ? 0.4743 0.4772 0.4987 -0.0453 0.0302  -0.0530 108 THR C CA    
3360  C C     . THR C 107 ? 0.4962 0.5020 0.5271 -0.0472 0.0305  -0.0538 108 THR C C     
3361  O O     . THR C 107 ? 0.5566 0.5660 0.5915 -0.0466 0.0304  -0.0544 108 THR C O     
3362  C CB    . THR C 107 ? 0.5032 0.5050 0.5254 -0.0441 0.0274  -0.0541 108 THR C CB    
3363  O OG1   . THR C 107 ? 0.4978 0.4976 0.5145 -0.0422 0.0276  -0.0532 108 THR C OG1   
3364  C CG2   . THR C 107 ? 0.5179 0.5227 0.5436 -0.0430 0.0248  -0.0559 108 THR C CG2   
3365  N N     . ARG C 108 ? 0.5268 0.5310 0.5588 -0.0494 0.0309  -0.0538 109 ARG C N     
3366  C CA    . ARG C 108 ? 0.4846 0.4911 0.5227 -0.0516 0.0312  -0.0546 109 ARG C CA    
3367  C C     . ARG C 108 ? 0.4352 0.4434 0.4757 -0.0526 0.0344  -0.0534 109 ARG C C     
3368  O O     . ARG C 108 ? 0.3821 0.3941 0.4285 -0.0535 0.0349  -0.0541 109 ARG C O     
3369  C CB    . ARG C 108 ? 0.5337 0.5372 0.5715 -0.0536 0.0309  -0.0548 109 ARG C CB    
3370  C CG    . ARG C 108 ? 0.5692 0.5748 0.6135 -0.0561 0.0306  -0.0559 109 ARG C CG    
3371  C CD    . ARG C 108 ? 0.6038 0.6056 0.6472 -0.0580 0.0300  -0.0562 109 ARG C CD    
3372  N NE    . ARG C 108 ? 0.6189 0.6183 0.6585 -0.0563 0.0271  -0.0574 109 ARG C NE    
3373  C CZ    . ARG C 108 ? 0.6410 0.6367 0.6790 -0.0573 0.0260  -0.0579 109 ARG C CZ    
3374  N NH1   . ARG C 108 ? 0.6546 0.6482 0.6944 -0.0600 0.0275  -0.0575 109 ARG C NH1   
3375  N NH2   . ARG C 108 ? 0.6690 0.6627 0.7032 -0.0555 0.0235  -0.0590 109 ARG C NH2   
3376  N N     . ALA C 109 ? 0.3898 0.3954 0.4257 -0.0523 0.0366  -0.0517 110 ALA C N     
3377  C CA    . ALA C 109 ? 0.4188 0.4253 0.4558 -0.0530 0.0397  -0.0505 110 ALA C CA    
3378  C C     . ALA C 109 ? 0.4266 0.4370 0.4663 -0.0513 0.0398  -0.0510 110 ALA C C     
3379  O O     . ALA C 109 ? 0.4418 0.4552 0.4861 -0.0521 0.0415  -0.0511 110 ALA C O     
3380  C CB    . ALA C 109 ? 0.3906 0.3933 0.4215 -0.0528 0.0414  -0.0489 110 ALA C CB    
3381  N N     . LYS C 110 ? 0.4615 0.4716 0.4982 -0.0489 0.0381  -0.0514 111 LYS C N     
3382  C CA    . LYS C 110 ? 0.5000 0.5130 0.5383 -0.0468 0.0380  -0.0518 111 LYS C CA    
3383  C C     . LYS C 110 ? 0.5042 0.5220 0.5494 -0.0469 0.0364  -0.0534 111 LYS C C     
3384  O O     . LYS C 110 ? 0.4653 0.4866 0.5145 -0.0464 0.0374  -0.0536 111 LYS C O     
3385  C CB    . LYS C 110 ? 0.5563 0.5674 0.5895 -0.0443 0.0363  -0.0517 111 LYS C CB    
3386  C CG    . LYS C 110 ? 0.5789 0.5860 0.6057 -0.0441 0.0379  -0.0502 111 LYS C CG    
3387  C CD    . LYS C 110 ? 0.6123 0.6177 0.6345 -0.0419 0.0365  -0.0501 111 LYS C CD    
3388  C CE    . LYS C 110 ? 0.6364 0.6382 0.6530 -0.0420 0.0381  -0.0487 111 LYS C CE    
3389  N NZ    . LYS C 110 ? 0.6702 0.6719 0.6868 -0.0423 0.0407  -0.0479 111 LYS C NZ    
3390  N N     . ALA C 111 ? 0.5096 0.5274 0.5560 -0.0476 0.0337  -0.0546 112 ALA C N     
3391  C CA    . ALA C 111 ? 0.5329 0.5551 0.5856 -0.0477 0.0315  -0.0564 112 ALA C CA    
3392  C C     . ALA C 111 ? 0.4874 0.5130 0.5468 -0.0501 0.0338  -0.0564 112 ALA C C     
3393  O O     . ALA C 111 ? 0.4732 0.5038 0.5388 -0.0499 0.0330  -0.0575 112 ALA C O     
3394  C CB    . ALA C 111 ? 0.5285 0.5492 0.5805 -0.0483 0.0285  -0.0576 112 ALA C CB    
3395  N N     . GLU C 112 ? 0.4907 0.5134 0.5486 -0.0524 0.0365  -0.0550 113 GLU C N     
3396  C CA    . GLU C 112 ? 0.4896 0.5148 0.5530 -0.0549 0.0391  -0.0547 113 GLU C CA    
3397  C C     . GLU C 112 ? 0.5103 0.5364 0.5732 -0.0540 0.0425  -0.0535 113 GLU C C     
3398  O O     . GLU C 112 ? 0.4959 0.5235 0.5621 -0.0559 0.0454  -0.0528 113 GLU C O     
3399  C CB    . GLU C 112 ? 0.5572 0.5785 0.6192 -0.0577 0.0402  -0.0540 113 GLU C CB    
3400  C CG    . GLU C 112 ? 0.5989 0.6188 0.6613 -0.0586 0.0370  -0.0554 113 GLU C CG    
3401  C CD    . GLU C 112 ? 0.6805 0.6960 0.7412 -0.0613 0.0380  -0.0547 113 GLU C CD    
3402  O OE1   . GLU C 112 ? 0.7724 0.7862 0.8320 -0.0626 0.0413  -0.0531 113 GLU C OE1   
3403  O OE2   . GLU C 112 ? 0.6918 0.7054 0.7521 -0.0619 0.0355  -0.0558 113 GLU C OE2   
3404  N N     . GLY C 113 ? 0.4773 0.5023 0.5357 -0.0512 0.0421  -0.0531 114 GLY C N     
3405  C CA    . GLY C 113 ? 0.4880 0.5140 0.5458 -0.0499 0.0448  -0.0522 114 GLY C CA    
3406  C C     . GLY C 113 ? 0.4845 0.5061 0.5372 -0.0510 0.0479  -0.0504 114 GLY C C     
3407  O O     . GLY C 113 ? 0.4732 0.4956 0.5265 -0.0509 0.0509  -0.0497 114 GLY C O     
3408  N N     . PHE C 114 ? 0.4518 0.4688 0.4993 -0.0517 0.0471  -0.0498 115 PHE C N     
3409  C CA    . PHE C 114 ? 0.4497 0.4625 0.4919 -0.0526 0.0496  -0.0482 115 PHE C CA    
3410  C C     . PHE C 114 ? 0.4132 0.4229 0.4489 -0.0505 0.0489  -0.0476 115 PHE C C     
3411  O O     . PHE C 114 ? 0.4306 0.4405 0.4652 -0.0489 0.0463  -0.0484 115 PHE C O     
3412  C CB    . PHE C 114 ? 0.4422 0.4520 0.4832 -0.0549 0.0494  -0.0477 115 PHE C CB    
3413  C CG    . PHE C 114 ? 0.4972 0.5090 0.5440 -0.0574 0.0508  -0.0479 115 PHE C CG    
3414  C CD1   . PHE C 114 ? 0.4825 0.4947 0.5305 -0.0587 0.0543  -0.0468 115 PHE C CD1   
3415  C CD2   . PHE C 114 ? 0.4695 0.4824 0.5201 -0.0587 0.0485  -0.0491 115 PHE C CD2   
3416  C CE1   . PHE C 114 ? 0.4924 0.5064 0.5457 -0.0612 0.0558  -0.0469 115 PHE C CE1   
3417  C CE2   . PHE C 114 ? 0.4619 0.4765 0.5179 -0.0614 0.0498  -0.0492 115 PHE C CE2   
3418  C CZ    . PHE C 114 ? 0.4488 0.4640 0.5063 -0.0627 0.0535  -0.0481 115 PHE C CZ    
3419  N N     . SER C 115 ? 0.3858 0.3927 0.4172 -0.0507 0.0513  -0.0464 116 SER C N     
3420  C CA    . SER C 115 ? 0.4353 0.4390 0.4604 -0.0493 0.0509  -0.0458 116 SER C CA    
3421  C C     . SER C 115 ? 0.4015 0.4020 0.4228 -0.0501 0.0495  -0.0453 116 SER C C     
3422  O O     . SER C 115 ? 0.3393 0.3380 0.3598 -0.0518 0.0505  -0.0445 116 SER C O     
3423  C CB    . SER C 115 ? 0.4040 0.4060 0.4261 -0.0492 0.0537  -0.0448 116 SER C CB    
3424  O OG    . SER C 115 ? 0.4404 0.4392 0.4565 -0.0482 0.0532  -0.0443 116 SER C OG    
3425  N N     . ALA C 116 ? 0.3945 0.3942 0.4134 -0.0487 0.0471  -0.0457 117 ALA C N     
3426  C CA    . ALA C 116 ? 0.4153 0.4125 0.4309 -0.0491 0.0457  -0.0454 117 ALA C CA    
3427  C C     . ALA C 116 ? 0.4450 0.4408 0.4563 -0.0475 0.0445  -0.0453 117 ALA C C     
3428  O O     . ALA C 116 ? 0.4543 0.4514 0.4663 -0.0459 0.0433  -0.0460 117 ALA C O     
3429  C CB    . ALA C 116 ? 0.4463 0.4447 0.4653 -0.0497 0.0438  -0.0464 117 ALA C CB    
3430  N N     . LYS C 117 ? 0.4496 0.4426 0.4564 -0.0479 0.0449  -0.0443 118 LYS C N     
3431  C CA    . LYS C 117 ? 0.4139 0.4055 0.4167 -0.0467 0.0439  -0.0441 118 LYS C CA    
3432  C C     . LYS C 117 ? 0.3773 0.3671 0.3773 -0.0473 0.0432  -0.0435 118 LYS C C     
3433  O O     . LYS C 117 ? 0.3547 0.3439 0.3553 -0.0485 0.0435  -0.0432 118 LYS C O     
3434  C CB    . LYS C 117 ? 0.4544 0.4447 0.4544 -0.0464 0.0456  -0.0435 118 LYS C CB    
3435  C CG    . LYS C 117 ? 0.4750 0.4635 0.4727 -0.0478 0.0473  -0.0425 118 LYS C CG    
3436  C CD    . LYS C 117 ? 0.5368 0.5237 0.5312 -0.0475 0.0487  -0.0421 118 LYS C CD    
3437  C CE    . LYS C 117 ? 0.5520 0.5369 0.5436 -0.0488 0.0501  -0.0412 118 LYS C CE    
3438  N NZ    . LYS C 117 ? 0.5269 0.5099 0.5149 -0.0486 0.0512  -0.0410 118 LYS C NZ    
3439  N N     . MET C 118 ? 0.4052 0.3943 0.4023 -0.0464 0.0422  -0.0434 119 MET C N     
3440  C CA    . MET C 118 ? 0.4097 0.3976 0.4042 -0.0466 0.0415  -0.0429 119 MET C CA    
3441  C C     . MET C 118 ? 0.3896 0.3762 0.3804 -0.0466 0.0422  -0.0421 119 MET C C     
3442  O O     . MET C 118 ? 0.3572 0.3438 0.3467 -0.0458 0.0421  -0.0422 119 MET C O     
3443  C CB    . MET C 118 ? 0.4319 0.4203 0.4267 -0.0455 0.0396  -0.0437 119 MET C CB    
3444  C CG    . MET C 118 ? 0.4744 0.4620 0.4666 -0.0453 0.0390  -0.0432 119 MET C CG    
3445  S SD    . MET C 118 ? 0.4826 0.4706 0.4745 -0.0437 0.0369  -0.0441 119 MET C SD    
3446  C CE    . MET C 118 ? 0.4471 0.4357 0.4430 -0.0440 0.0359  -0.0453 119 MET C CE    
3447  N N     . GLU C 119 ? 0.3987 0.3844 0.3877 -0.0476 0.0427  -0.0413 120 GLU C N     
3448  C CA    . GLU C 119 ? 0.4467 0.4315 0.4324 -0.0478 0.0430  -0.0406 120 GLU C CA    
3449  C C     . GLU C 119 ? 0.4390 0.4243 0.4237 -0.0473 0.0418  -0.0405 120 GLU C C     
3450  O O     . GLU C 119 ? 0.4179 0.4033 0.4033 -0.0472 0.0411  -0.0406 120 GLU C O     
3451  C CB    . GLU C 119 ? 0.4464 0.4300 0.4305 -0.0490 0.0441  -0.0399 120 GLU C CB    
3452  C CG    . GLU C 119 ? 0.4992 0.4821 0.4836 -0.0494 0.0457  -0.0400 120 GLU C CG    
3453  C CD    . GLU C 119 ? 0.5139 0.4963 0.4970 -0.0490 0.0462  -0.0402 120 GLU C CD    
3454  O OE1   . GLU C 119 ? 0.6103 0.5919 0.5907 -0.0493 0.0460  -0.0399 120 GLU C OE1   
3455  O OE2   . GLU C 119 ? 0.5436 0.5265 0.5286 -0.0484 0.0467  -0.0407 120 GLU C OE2   
3456  N N     . PRO C 120 ? 0.4565 0.4419 0.4393 -0.0469 0.0415  -0.0404 121 PRO C N     
3457  C CA    . PRO C 120 ? 0.4559 0.4420 0.4378 -0.0464 0.0407  -0.0402 121 PRO C CA    
3458  C C     . PRO C 120 ? 0.4523 0.4387 0.4332 -0.0471 0.0407  -0.0395 121 PRO C C     
3459  O O     . PRO C 120 ? 0.4575 0.4431 0.4372 -0.0482 0.0414  -0.0391 121 PRO C O     
3460  C CB    . PRO C 120 ? 0.4860 0.4720 0.4662 -0.0461 0.0409  -0.0401 121 PRO C CB    
3461  C CG    . PRO C 120 ? 0.5032 0.4879 0.4826 -0.0470 0.0420  -0.0399 121 PRO C CG    
3462  C CD    . PRO C 120 ? 0.4831 0.4677 0.4646 -0.0470 0.0423  -0.0403 121 PRO C CD    
3463  N N     . GLY C 121 ? 0.4471 0.4343 0.4281 -0.0464 0.0398  -0.0395 122 GLY C N     
3464  C CA    . GLY C 121 ? 0.3953 0.3831 0.3755 -0.0467 0.0396  -0.0389 122 GLY C CA    
3465  C C     . GLY C 121 ? 0.3630 0.3527 0.3427 -0.0460 0.0392  -0.0387 122 GLY C C     
3466  O O     . GLY C 121 ? 0.3568 0.3468 0.3363 -0.0454 0.0392  -0.0390 122 GLY C O     
3467  N N     . ILE C 122 ? 0.3416 0.3323 0.3210 -0.0459 0.0388  -0.0382 123 ILE C N     
3468  C CA    . ILE C 122 ? 0.3576 0.3505 0.3369 -0.0452 0.0385  -0.0380 123 ILE C CA    
3469  C C     . ILE C 122 ? 0.3518 0.3450 0.3317 -0.0434 0.0379  -0.0384 123 ILE C C     
3470  O O     . ILE C 122 ? 0.3191 0.3115 0.2991 -0.0429 0.0374  -0.0384 123 ILE C O     
3471  C CB    . ILE C 122 ? 0.3723 0.3669 0.3513 -0.0460 0.0384  -0.0374 123 ILE C CB    
3472  C CG1   . ILE C 122 ? 0.4632 0.4572 0.4412 -0.0478 0.0390  -0.0372 123 ILE C CG1   
3473  C CG2   . ILE C 122 ? 0.3704 0.3680 0.3499 -0.0452 0.0383  -0.0372 123 ILE C CG2   
3474  C CD1   . ILE C 122 ? 0.4738 0.4694 0.4513 -0.0487 0.0386  -0.0367 123 ILE C CD1   
3475  N N     . SER C 123 ? 0.3447 0.3383 0.3245 -0.0424 0.0379  -0.0388 124 SER C N     
3476  C CA    . SER C 123 ? 0.3512 0.3445 0.3311 -0.0406 0.0372  -0.0394 124 SER C CA    
3477  C C     . SER C 123 ? 0.3558 0.3514 0.3355 -0.0394 0.0372  -0.0391 124 SER C C     
3478  O O     . SER C 123 ? 0.3358 0.3337 0.3156 -0.0401 0.0378  -0.0385 124 SER C O     
3479  C CB    . SER C 123 ? 0.3749 0.3672 0.3544 -0.0399 0.0371  -0.0402 124 SER C CB    
3480  O OG    . SER C 123 ? 0.3728 0.3664 0.3514 -0.0399 0.0378  -0.0398 124 SER C OG    
3481  N N     . ALA C 124 ? 0.3570 0.3521 0.3366 -0.0377 0.0366  -0.0396 125 ALA C N     
3482  C CA    . ALA C 124 ? 0.3756 0.3728 0.3550 -0.0361 0.0366  -0.0394 125 ALA C CA    
3483  C C     . ALA C 124 ? 0.3460 0.3455 0.3250 -0.0360 0.0376  -0.0392 125 ALA C C     
3484  O O     . ALA C 124 ? 0.3296 0.3320 0.3091 -0.0355 0.0381  -0.0387 125 ALA C O     
3485  C CB    . ALA C 124 ? 0.3533 0.3488 0.3321 -0.0341 0.0359  -0.0402 125 ALA C CB    
3486  N N     . GLU C 125 ? 0.3709 0.3690 0.3491 -0.0365 0.0379  -0.0395 126 GLU C N     
3487  C CA    . GLU C 125 ? 0.4100 0.4095 0.3874 -0.0365 0.0389  -0.0392 126 GLU C CA    
3488  C C     . GLU C 125 ? 0.4214 0.4229 0.3996 -0.0385 0.0398  -0.0382 126 GLU C C     
3489  O O     . GLU C 125 ? 0.4263 0.4304 0.4048 -0.0386 0.0407  -0.0377 126 GLU C O     
3490  C CB    . GLU C 125 ? 0.4650 0.4620 0.4410 -0.0364 0.0387  -0.0397 126 GLU C CB    
3491  C CG    . GLU C 125 ? 0.4994 0.4969 0.4738 -0.0365 0.0399  -0.0392 126 GLU C CG    
3492  C CD    . GLU C 125 ? 0.5750 0.5699 0.5477 -0.0359 0.0395  -0.0397 126 GLU C CD    
3493  O OE1   . GLU C 125 ? 0.6688 0.6626 0.6406 -0.0341 0.0386  -0.0406 126 GLU C OE1   
3494  O OE2   . GLU C 125 ? 0.7182 0.7123 0.6904 -0.0371 0.0401  -0.0393 126 GLU C OE2   
3495  N N     . ALA C 126 ? 0.4301 0.4303 0.4087 -0.0402 0.0395  -0.0381 127 ALA C N     
3496  C CA    . ALA C 126 ? 0.4259 0.4274 0.4050 -0.0423 0.0401  -0.0374 127 ALA C CA    
3497  C C     . ALA C 126 ? 0.3630 0.3679 0.3436 -0.0423 0.0400  -0.0369 127 ALA C C     
3498  O O     . ALA C 126 ? 0.3767 0.3840 0.3580 -0.0436 0.0406  -0.0364 127 ALA C O     
3499  C CB    . ALA C 126 ? 0.3925 0.3917 0.3714 -0.0436 0.0397  -0.0375 127 ALA C CB    
3500  N N     . CYS C 127 ? 0.3281 0.3331 0.3092 -0.0409 0.0391  -0.0372 128 CYS C N     
3501  C CA    . CYS C 127 ? 0.3417 0.3500 0.3242 -0.0405 0.0387  -0.0368 128 CYS C CA    
3502  C C     . CYS C 127 ? 0.3898 0.4013 0.3730 -0.0393 0.0395  -0.0366 128 CYS C C     
3503  O O     . CYS C 127 ? 0.3317 0.3470 0.3166 -0.0398 0.0398  -0.0361 128 CYS C O     
3504  C CB    . CYS C 127 ? 0.3605 0.3674 0.3429 -0.0389 0.0376  -0.0370 128 CYS C CB    
3505  S SG    . CYS C 127 ? 0.4288 0.4319 0.4102 -0.0404 0.0370  -0.0370 128 CYS C SG    
3506  N N     . LEU C 128 ? 0.4318 0.4419 0.4138 -0.0376 0.0399  -0.0371 129 LEU C N     
3507  C CA    . LEU C 128 ? 0.4335 0.4463 0.4157 -0.0361 0.0409  -0.0369 129 LEU C CA    
3508  C C     . LEU C 128 ? 0.3989 0.4143 0.3819 -0.0380 0.0423  -0.0362 129 LEU C C     
3509  O O     . LEU C 128 ? 0.3486 0.3682 0.3335 -0.0378 0.0431  -0.0358 129 LEU C O     
3510  C CB    . LEU C 128 ? 0.4646 0.4745 0.4446 -0.0343 0.0410  -0.0377 129 LEU C CB    
3511  C CG    . LEU C 128 ? 0.4718 0.4838 0.4513 -0.0323 0.0421  -0.0377 129 LEU C CG    
3512  C CD1   . LEU C 128 ? 0.4892 0.4977 0.4659 -0.0303 0.0418  -0.0386 129 LEU C CD1   
3513  C CD2   . LEU C 128 ? 0.4969 0.5114 0.4767 -0.0337 0.0438  -0.0368 129 LEU C CD2   
3514  N N     . TRP C 129 ? 0.3985 0.4115 0.3803 -0.0397 0.0427  -0.0361 130 TRP C N     
3515  C CA    . TRP C 129 ? 0.3927 0.4070 0.3747 -0.0417 0.0441  -0.0354 130 TRP C CA    
3516  C C     . TRP C 129 ? 0.3621 0.3801 0.3467 -0.0435 0.0440  -0.0349 130 TRP C C     
3517  O O     . TRP C 129 ? 0.3995 0.4207 0.3855 -0.0447 0.0452  -0.0343 130 TRP C O     
3518  C CB    . TRP C 129 ? 0.4039 0.4142 0.3838 -0.0431 0.0442  -0.0354 130 TRP C CB    
3519  C CG    . TRP C 129 ? 0.4292 0.4361 0.4067 -0.0414 0.0441  -0.0359 130 TRP C CG    
3520  C CD1   . TRP C 129 ? 0.4121 0.4155 0.3884 -0.0415 0.0433  -0.0364 130 TRP C CD1   
3521  C CD2   . TRP C 129 ? 0.4341 0.4411 0.4101 -0.0393 0.0447  -0.0361 130 TRP C CD2   
3522  N NE1   . TRP C 129 ? 0.4052 0.4065 0.3796 -0.0396 0.0431  -0.0369 130 TRP C NE1   
3523  C CE2   . TRP C 129 ? 0.4279 0.4311 0.4018 -0.0382 0.0439  -0.0367 130 TRP C CE2   
3524  C CE3   . TRP C 129 ? 0.4064 0.4162 0.3826 -0.0380 0.0458  -0.0357 130 TRP C CE3   
3525  C CZ2   . TRP C 129 ? 0.4031 0.4051 0.3747 -0.0360 0.0441  -0.0371 130 TRP C CZ2   
3526  C CZ3   . TRP C 129 ? 0.3871 0.3955 0.3609 -0.0358 0.0462  -0.0361 130 TRP C CZ3   
3527  C CH2   . TRP C 129 ? 0.3962 0.4006 0.3675 -0.0348 0.0452  -0.0368 130 TRP C CH2   
3528  N N     . ALA C 130 ? 0.3339 0.3516 0.3192 -0.0439 0.0425  -0.0352 131 ALA C N     
3529  C CA    . ALA C 130 ? 0.3095 0.3302 0.2969 -0.0456 0.0419  -0.0349 131 ALA C CA    
3530  C C     . ALA C 130 ? 0.3258 0.3514 0.3158 -0.0441 0.0416  -0.0347 131 ALA C C     
3531  O O     . ALA C 130 ? 0.2959 0.3257 0.2883 -0.0454 0.0417  -0.0344 131 ALA C O     
3532  C CB    . ALA C 130 ? 0.3338 0.3518 0.3203 -0.0464 0.0405  -0.0352 131 ALA C CB    
3533  N N     . ASP C 131 ? 0.3704 0.3954 0.3599 -0.0413 0.0411  -0.0351 132 ASP C N     
3534  C CA    . ASP C 131 ? 0.3756 0.4046 0.3672 -0.0393 0.0407  -0.0350 132 ASP C CA    
3535  C C     . ASP C 131 ? 0.4084 0.4414 0.4015 -0.0386 0.0424  -0.0347 132 ASP C C     
3536  O O     . ASP C 131 ? 0.5064 0.5447 0.5026 -0.0384 0.0425  -0.0344 132 ASP C O     
3537  C CB    . ASP C 131 ? 0.3986 0.4248 0.3887 -0.0366 0.0397  -0.0355 132 ASP C CB    
3538  C CG    . ASP C 131 ? 0.3816 0.4055 0.3710 -0.0369 0.0380  -0.0355 132 ASP C CG    
3539  O OD1   . ASP C 131 ? 0.4245 0.4501 0.4150 -0.0388 0.0374  -0.0352 132 ASP C OD1   
3540  O OD2   . ASP C 131 ? 0.3727 0.3931 0.3604 -0.0353 0.0373  -0.0359 132 ASP C OD2   
3541  N N     . LEU C 132 ? 0.4137 0.4442 0.4047 -0.0381 0.0438  -0.0348 133 LEU C N     
3542  C CA    . LEU C 132 ? 0.4325 0.4661 0.4241 -0.0371 0.0457  -0.0345 133 LEU C CA    
3543  C C     . LEU C 132 ? 0.4819 0.5169 0.4743 -0.0400 0.0472  -0.0338 133 LEU C C     
3544  O O     . LEU C 132 ? 0.5830 0.6205 0.5760 -0.0398 0.0491  -0.0333 133 LEU C O     
3545  C CB    . LEU C 132 ? 0.4824 0.5123 0.4708 -0.0346 0.0462  -0.0350 133 LEU C CB    
3546  C CG    . LEU C 132 ? 0.4574 0.4864 0.4452 -0.0315 0.0450  -0.0357 133 LEU C CG    
3547  C CD1   . LEU C 132 ? 0.5005 0.5264 0.4879 -0.0319 0.0429  -0.0361 133 LEU C CD1   
3548  C CD2   . LEU C 132 ? 0.5316 0.5574 0.5162 -0.0292 0.0456  -0.0363 133 LEU C CD2   
3549  N N     . GLY C 133 ? 0.4557 0.4886 0.4478 -0.0428 0.0465  -0.0337 134 GLY C N     
3550  C CA    . GLY C 133 ? 0.4468 0.4799 0.4391 -0.0458 0.0478  -0.0331 134 GLY C CA    
3551  C C     . GLY C 133 ? 0.4563 0.4868 0.4457 -0.0452 0.0497  -0.0327 134 GLY C C     
3552  O O     . GLY C 133 ? 0.4244 0.4575 0.4148 -0.0461 0.0517  -0.0320 134 GLY C O     
3553  N N     . ILE C 134 ? 0.5091 0.5347 0.4952 -0.0437 0.0491  -0.0332 135 ILE C N     
3554  C CA    . ILE C 134 ? 0.4834 0.5059 0.4662 -0.0428 0.0505  -0.0330 135 ILE C CA    
3555  C C     . ILE C 134 ? 0.4749 0.4922 0.4551 -0.0442 0.0500  -0.0331 135 ILE C C     
3556  O O     . ILE C 134 ? 0.4541 0.4692 0.4340 -0.0442 0.0483  -0.0337 135 ILE C O     
3557  C CB    . ILE C 134 ? 0.5213 0.5428 0.5024 -0.0393 0.0502  -0.0336 135 ILE C CB    
3558  C CG1   . ILE C 134 ? 0.5419 0.5685 0.5254 -0.0376 0.0510  -0.0336 135 ILE C CG1   
3559  C CG2   . ILE C 134 ? 0.5704 0.5881 0.5474 -0.0383 0.0512  -0.0335 135 ILE C CG2   
3560  C CD1   . ILE C 134 ? 0.5601 0.5853 0.5415 -0.0341 0.0507  -0.0343 135 ILE C CD1   
3561  N N     . ASP C 135 ? 0.4079 0.4234 0.3861 -0.0453 0.0516  -0.0324 136 ASP C N     
3562  C CA    . ASP C 135 ? 0.4098 0.4203 0.3852 -0.0463 0.0513  -0.0324 136 ASP C CA    
3563  C C     . ASP C 135 ? 0.3883 0.3953 0.3600 -0.0438 0.0514  -0.0326 136 ASP C C     
3564  O O     . ASP C 135 ? 0.4612 0.4683 0.4311 -0.0429 0.0530  -0.0320 136 ASP C O     
3565  C CB    . ASP C 135 ? 0.3715 0.3814 0.3467 -0.0493 0.0528  -0.0314 136 ASP C CB    
3566  C CG    . ASP C 135 ? 0.3682 0.3726 0.3402 -0.0501 0.0527  -0.0314 136 ASP C CG    
3567  O OD1   . ASP C 135 ? 0.3046 0.3060 0.2746 -0.0482 0.0516  -0.0320 136 ASP C OD1   
3568  O OD2   . ASP C 135 ? 0.4019 0.4052 0.3735 -0.0527 0.0538  -0.0307 136 ASP C OD2   
3569  N N     . PRO C 136 ? 0.3677 0.3715 0.3382 -0.0426 0.0497  -0.0335 137 PRO C N     
3570  C CA    . PRO C 136 ? 0.4135 0.4143 0.3808 -0.0401 0.0493  -0.0339 137 PRO C CA    
3571  C C     . PRO C 136 ? 0.4269 0.4247 0.3907 -0.0403 0.0507  -0.0331 137 PRO C C     
3572  O O     . PRO C 136 ? 0.4339 0.4298 0.3946 -0.0382 0.0508  -0.0332 137 PRO C O     
3573  C CB    . PRO C 136 ? 0.3983 0.3967 0.3659 -0.0397 0.0472  -0.0350 137 PRO C CB    
3574  C CG    . PRO C 136 ? 0.4068 0.4057 0.3765 -0.0424 0.0471  -0.0347 137 PRO C CG    
3575  C CD    . PRO C 136 ? 0.3737 0.3767 0.3457 -0.0436 0.0481  -0.0341 137 PRO C CD    
3576  N N     . GLY C 137 ? 0.4206 0.4178 0.3846 -0.0429 0.0517  -0.0322 138 GLY C N     
3577  C CA    . GLY C 137 ? 0.4202 0.4139 0.3807 -0.0434 0.0531  -0.0313 138 GLY C CA    
3578  C C     . GLY C 137 ? 0.4301 0.4256 0.3900 -0.0440 0.0556  -0.0301 138 GLY C C     
3579  O O     . GLY C 137 ? 0.4260 0.4185 0.3826 -0.0441 0.0571  -0.0291 138 GLY C O     
3580  N N     . ASN C 138 ? 0.4227 0.4232 0.3860 -0.0442 0.0561  -0.0301 139 ASN C N     
3581  C CA    . ASN C 138 ? 0.4552 0.4585 0.4189 -0.0449 0.0586  -0.0290 139 ASN C CA    
3582  C C     . ASN C 138 ? 0.4375 0.4383 0.3967 -0.0424 0.0599  -0.0285 139 ASN C C     
3583  O O     . ASN C 138 ? 0.4193 0.4180 0.3757 -0.0433 0.0619  -0.0273 139 ASN C O     
3584  C CB    . ASN C 138 ? 0.4937 0.5030 0.4618 -0.0448 0.0586  -0.0293 139 ASN C CB    
3585  C CG    . ASN C 138 ? 0.5097 0.5227 0.4790 -0.0457 0.0614  -0.0282 139 ASN C CG    
3586  O OD1   . ASN C 138 ? 0.5268 0.5425 0.4963 -0.0436 0.0623  -0.0282 139 ASN C OD1   
3587  N ND2   . ASN C 138 ? 0.5128 0.5258 0.4829 -0.0490 0.0628  -0.0272 139 ASN C ND2   
3588  N N     . SER C 139 ? 0.4138 0.4145 0.3717 -0.0393 0.0586  -0.0295 140 SER C N     
3589  C CA    . SER C 139 ? 0.4435 0.4418 0.3968 -0.0366 0.0594  -0.0293 140 SER C CA    
3590  C C     . SER C 139 ? 0.4056 0.4002 0.3563 -0.0342 0.0568  -0.0306 140 SER C C     
3591  O O     . SER C 139 ? 0.4510 0.4432 0.3975 -0.0317 0.0568  -0.0308 140 SER C O     
3592  C CB    . SER C 139 ? 0.4745 0.4768 0.4286 -0.0349 0.0608  -0.0294 140 SER C CB    
3593  O OG    . SER C 139 ? 0.4735 0.4785 0.4307 -0.0337 0.0589  -0.0307 140 SER C OG    
3594  N N     . GLY C 140 ? 0.3785 0.3727 0.3317 -0.0351 0.0546  -0.0315 141 GLY C N     
3595  C CA    . GLY C 140 ? 0.3745 0.3659 0.3263 -0.0333 0.0521  -0.0328 141 GLY C CA    
3596  C C     . GLY C 140 ? 0.3771 0.3709 0.3319 -0.0322 0.0504  -0.0342 141 GLY C C     
3597  O O     . GLY C 140 ? 0.3735 0.3709 0.3305 -0.0322 0.0511  -0.0342 141 GLY C O     
3598  N N     . HIS C 141 ? 0.4220 0.4138 0.3769 -0.0314 0.0480  -0.0354 142 HIS C N     
3599  C CA    . HIS C 141 ? 0.4156 0.4089 0.3732 -0.0307 0.0463  -0.0367 142 HIS C CA    
3600  C C     . HIS C 141 ? 0.3831 0.3737 0.3387 -0.0285 0.0442  -0.0381 142 HIS C C     
3601  O O     . HIS C 141 ? 0.4143 0.4022 0.3681 -0.0283 0.0434  -0.0382 142 HIS C O     
3602  C CB    . HIS C 141 ? 0.4529 0.4473 0.4143 -0.0331 0.0456  -0.0367 142 HIS C CB    
3603  C CG    . HIS C 141 ? 0.4450 0.4394 0.4084 -0.0325 0.0436  -0.0380 142 HIS C CG    
3604  N ND1   . HIS C 141 ? 0.5005 0.4939 0.4657 -0.0338 0.0425  -0.0383 142 HIS C ND1   
3605  C CD2   . HIS C 141 ? 0.4912 0.4863 0.4551 -0.0308 0.0427  -0.0389 142 HIS C CD2   
3606  C CE1   . HIS C 141 ? 0.4876 0.4811 0.4543 -0.0331 0.0410  -0.0394 142 HIS C CE1   
3607  N NE2   . HIS C 141 ? 0.5043 0.4986 0.4701 -0.0313 0.0410  -0.0398 142 HIS C NE2   
3608  N N     . GLN C 142 ? 0.3963 0.3876 0.3523 -0.0269 0.0432  -0.0392 143 GLN C N     
3609  C CA    . GLN C 142 ? 0.4038 0.3928 0.3585 -0.0251 0.0409  -0.0408 143 GLN C CA    
3610  C C     . GLN C 142 ? 0.3646 0.3547 0.3224 -0.0251 0.0396  -0.0418 143 GLN C C     
3611  O O     . GLN C 142 ? 0.3794 0.3716 0.3382 -0.0248 0.0405  -0.0416 143 GLN C O     
3612  C CB    . GLN C 142 ? 0.4374 0.4250 0.3878 -0.0224 0.0410  -0.0412 143 GLN C CB    
3613  C CG    . GLN C 142 ? 0.5164 0.5024 0.4629 -0.0220 0.0424  -0.0401 143 GLN C CG    
3614  C CD    . GLN C 142 ? 0.5382 0.5224 0.4798 -0.0191 0.0423  -0.0407 143 GLN C CD    
3615  O OE1   . GLN C 142 ? 0.5717 0.5530 0.5098 -0.0178 0.0413  -0.0409 143 GLN C OE1   
3616  N NE2   . GLN C 142 ? 0.5911 0.5768 0.5322 -0.0178 0.0433  -0.0409 143 GLN C NE2   
3617  N N     . SER C 143 ? 0.3397 0.3282 0.2988 -0.0253 0.0376  -0.0429 144 SER C N     
3618  C CA    . SER C 143 ? 0.3547 0.3434 0.3162 -0.0254 0.0363  -0.0439 144 SER C CA    
3619  C C     . SER C 143 ? 0.3159 0.3021 0.2760 -0.0238 0.0341  -0.0457 144 SER C C     
3620  O O     . SER C 143 ? 0.3217 0.3066 0.2809 -0.0236 0.0330  -0.0462 144 SER C O     
3621  C CB    . SER C 143 ? 0.3558 0.3452 0.3209 -0.0278 0.0361  -0.0435 144 SER C CB    
3622  O OG    . SER C 143 ? 0.4119 0.4035 0.3782 -0.0292 0.0378  -0.0421 144 SER C OG    
3623  N N     . PHE C 144 ? 0.3171 0.3029 0.2772 -0.0227 0.0333  -0.0467 145 PHE C N     
3624  C CA    . PHE C 144 ? 0.3566 0.3399 0.3156 -0.0214 0.0311  -0.0486 145 PHE C CA    
3625  C C     . PHE C 144 ? 0.3775 0.3601 0.3385 -0.0216 0.0303  -0.0494 145 PHE C C     
3626  O O     . PHE C 144 ? 0.4139 0.3978 0.3755 -0.0214 0.0315  -0.0487 145 PHE C O     
3627  C CB    . PHE C 144 ? 0.4073 0.3892 0.3617 -0.0188 0.0310  -0.0493 145 PHE C CB    
3628  C CG    . PHE C 144 ? 0.3886 0.3704 0.3400 -0.0182 0.0318  -0.0485 145 PHE C CG    
3629  C CD1   . PHE C 144 ? 0.4064 0.3867 0.3571 -0.0180 0.0301  -0.0491 145 PHE C CD1   
3630  C CD2   . PHE C 144 ? 0.4080 0.3912 0.3574 -0.0176 0.0343  -0.0470 145 PHE C CD2   
3631  C CE1   . PHE C 144 ? 0.4041 0.3837 0.3515 -0.0172 0.0308  -0.0483 145 PHE C CE1   
3632  C CE2   . PHE C 144 ? 0.4054 0.3879 0.3517 -0.0171 0.0351  -0.0461 145 PHE C CE2   
3633  C CZ    . PHE C 144 ? 0.3941 0.3745 0.3391 -0.0168 0.0333  -0.0468 145 PHE C CZ    
3634  N N     . GLU C 145 ? 0.4583 0.4390 0.4204 -0.0220 0.0283  -0.0508 146 GLU C N     
3635  C CA    . GLU C 145 ? 0.4456 0.4248 0.4090 -0.0221 0.0273  -0.0518 146 GLU C CA    
3636  C C     . GLU C 145 ? 0.4189 0.3962 0.3786 -0.0195 0.0268  -0.0530 146 GLU C C     
3637  O O     . GLU C 145 ? 0.5587 0.5341 0.5158 -0.0182 0.0253  -0.0544 146 GLU C O     
3638  C CB    . GLU C 145 ? 0.4420 0.4198 0.4080 -0.0237 0.0254  -0.0529 146 GLU C CB    
3639  C CG    . GLU C 145 ? 0.4351 0.4114 0.4033 -0.0248 0.0251  -0.0532 146 GLU C CG    
3640  C CD    . GLU C 145 ? 0.4249 0.3981 0.3912 -0.0234 0.0237  -0.0549 146 GLU C CD    
3641  O OE1   . GLU C 145 ? 0.3602 0.3322 0.3235 -0.0215 0.0226  -0.0561 146 GLU C OE1   
3642  O OE2   . GLU C 145 ? 0.3965 0.3682 0.3639 -0.0239 0.0237  -0.0549 146 GLU C OE2   
3643  N N     . ALA C 146 ? 0.3811 0.3587 0.3404 -0.0185 0.0280  -0.0525 147 ALA C N     
3644  C CA    . ALA C 146 ? 0.4043 0.3805 0.3599 -0.0157 0.0280  -0.0534 147 ALA C CA    
3645  C C     . ALA C 146 ? 0.4145 0.3871 0.3676 -0.0147 0.0257  -0.0556 147 ALA C C     
3646  O O     . ALA C 146 ? 0.3989 0.3708 0.3483 -0.0128 0.0255  -0.0562 147 ALA C O     
3647  C CB    . ALA C 146 ? 0.4098 0.3857 0.3662 -0.0151 0.0286  -0.0532 147 ALA C CB    
3648  N N     . SER C 147 ? 0.3974 0.3677 0.3525 -0.0159 0.0239  -0.0568 148 SER C N     
3649  C CA    . SER C 147 ? 0.4262 0.3930 0.3793 -0.0151 0.0214  -0.0591 148 SER C CA    
3650  C C     . SER C 147 ? 0.4697 0.4368 0.4217 -0.0151 0.0201  -0.0598 148 SER C C     
3651  O O     . SER C 147 ? 0.4440 0.4089 0.3925 -0.0133 0.0185  -0.0616 148 SER C O     
3652  C CB    . SER C 147 ? 0.4093 0.3738 0.3654 -0.0170 0.0200  -0.0600 148 SER C CB    
3653  O OG    . SER C 147 ? 0.4131 0.3761 0.3689 -0.0163 0.0209  -0.0597 148 SER C OG    
3654  N N     . GLN C 148 ? 0.4148 0.3847 0.3696 -0.0169 0.0207  -0.0585 149 GLN C N     
3655  C CA    . GLN C 148 ? 0.4555 0.4259 0.4096 -0.0168 0.0194  -0.0590 149 GLN C CA    
3656  C C     . GLN C 148 ? 0.4694 0.4398 0.4184 -0.0142 0.0204  -0.0586 149 GLN C C     
3657  O O     . GLN C 148 ? 0.4494 0.4187 0.3955 -0.0130 0.0189  -0.0596 149 GLN C O     
3658  C CB    . GLN C 148 ? 0.5047 0.4778 0.4627 -0.0191 0.0201  -0.0576 149 GLN C CB    
3659  C CG    . GLN C 148 ? 0.5213 0.4948 0.4787 -0.0188 0.0187  -0.0581 149 GLN C CG    
3660  C CD    . GLN C 148 ? 0.5344 0.5104 0.4951 -0.0206 0.0197  -0.0566 149 GLN C CD    
3661  O OE1   . GLN C 148 ? 0.5064 0.4833 0.4651 -0.0199 0.0208  -0.0554 149 GLN C OE1   
3662  N NE2   . GLN C 148 ? 0.6113 0.5881 0.5766 -0.0229 0.0196  -0.0565 149 GLN C NE2   
3663  N N     . PHE C 149 ? 0.4802 0.4519 0.4281 -0.0135 0.0230  -0.0570 150 PHE C N     
3664  C CA    . PHE C 149 ? 0.5297 0.5018 0.4731 -0.0113 0.0245  -0.0563 150 PHE C CA    
3665  C C     . PHE C 149 ? 0.5223 0.4913 0.4610 -0.0085 0.0234  -0.0582 150 PHE C C     
3666  O O     . PHE C 149 ? 0.4758 0.4439 0.4097 -0.0064 0.0237  -0.0583 150 PHE C O     
3667  C CB    . PHE C 149 ? 0.5854 0.5603 0.5300 -0.0116 0.0276  -0.0542 150 PHE C CB    
3668  C CG    . PHE C 149 ? 0.5564 0.5320 0.4968 -0.0096 0.0297  -0.0533 150 PHE C CG    
3669  C CD1   . PHE C 149 ? 0.5482 0.5227 0.4851 -0.0070 0.0303  -0.0541 150 PHE C CD1   
3670  C CD2   . PHE C 149 ? 0.5621 0.5394 0.5020 -0.0103 0.0313  -0.0516 150 PHE C CD2   
3671  C CE1   . PHE C 149 ? 0.5110 0.4864 0.4442 -0.0052 0.0326  -0.0531 150 PHE C CE1   
3672  C CE2   . PHE C 149 ? 0.5533 0.5312 0.4895 -0.0087 0.0336  -0.0506 150 PHE C CE2   
3673  C CZ    . PHE C 149 ? 0.5426 0.5197 0.4755 -0.0061 0.0343  -0.0513 150 PHE C CZ    
3674  N N     . MET C 150 ? 0.5017 0.4686 0.4413 -0.0086 0.0220  -0.0597 151 MET C N     
3675  C CA    . MET C 150 ? 0.4869 0.4503 0.4220 -0.0060 0.0209  -0.0617 151 MET C CA    
3676  C C     . MET C 150 ? 0.4908 0.4515 0.4246 -0.0060 0.0175  -0.0640 151 MET C C     
3677  O O     . MET C 150 ? 0.6037 0.5620 0.5324 -0.0036 0.0164  -0.0654 151 MET C O     
3678  C CB    . MET C 150 ? 0.4797 0.4417 0.4163 -0.0060 0.0210  -0.0622 151 MET C CB    
3679  C CG    . MET C 150 ? 0.4826 0.4472 0.4199 -0.0053 0.0241  -0.0603 151 MET C CG    
3680  S SD    . MET C 150 ? 0.5028 0.4653 0.4413 -0.0048 0.0240  -0.0609 151 MET C SD    
3681  C CE    . MET C 150 ? 0.5541 0.5118 0.4863 -0.0013 0.0227  -0.0635 151 MET C CE    
3682  N N     . PHE C 151 ? 0.5081 0.4695 0.4466 -0.0086 0.0159  -0.0643 152 PHE C N     
3683  C CA    . PHE C 151 ? 0.5137 0.4730 0.4522 -0.0090 0.0124  -0.0666 152 PHE C CA    
3684  C C     . PHE C 151 ? 0.5178 0.4783 0.4545 -0.0083 0.0114  -0.0665 152 PHE C C     
3685  O O     . PHE C 151 ? 0.5789 0.5372 0.5125 -0.0070 0.0088  -0.0685 152 PHE C O     
3686  C CB    . PHE C 151 ? 0.4820 0.4418 0.4267 -0.0122 0.0113  -0.0669 152 PHE C CB    
3687  C CG    . PHE C 151 ? 0.4656 0.4235 0.4116 -0.0129 0.0121  -0.0671 152 PHE C CG    
3688  C CD1   . PHE C 151 ? 0.4880 0.4431 0.4296 -0.0104 0.0125  -0.0679 152 PHE C CD1   
3689  C CD2   . PHE C 151 ? 0.4685 0.4272 0.4199 -0.0157 0.0124  -0.0664 152 PHE C CD2   
3690  C CE1   . PHE C 151 ? 0.5256 0.4786 0.4682 -0.0107 0.0131  -0.0679 152 PHE C CE1   
3691  C CE2   . PHE C 151 ? 0.5002 0.4567 0.4523 -0.0162 0.0130  -0.0664 152 PHE C CE2   
3692  C CZ    . PHE C 151 ? 0.4981 0.4518 0.4459 -0.0136 0.0133  -0.0672 152 PHE C CZ    
3693  N N     . PHE C 152 ? 0.5249 0.4884 0.4633 -0.0092 0.0135  -0.0643 153 PHE C N     
3694  C CA    . PHE C 152 ? 0.5204 0.4849 0.4573 -0.0085 0.0127  -0.0639 153 PHE C CA    
3695  C C     . PHE C 152 ? 0.5229 0.4877 0.4551 -0.0066 0.0154  -0.0620 153 PHE C C     
3696  O O     . PHE C 152 ? 0.5388 0.5040 0.4702 -0.0062 0.0179  -0.0610 153 PHE C O     
3697  C CB    . PHE C 152 ? 0.4998 0.4670 0.4425 -0.0112 0.0125  -0.0630 153 PHE C CB    
3698  C CG    . PHE C 152 ? 0.5120 0.4792 0.4597 -0.0133 0.0102  -0.0647 153 PHE C CG    
3699  C CD1   . PHE C 152 ? 0.5516 0.5178 0.4991 -0.0129 0.0067  -0.0669 153 PHE C CD1   
3700  C CD2   . PHE C 152 ? 0.5036 0.4718 0.4561 -0.0158 0.0114  -0.0639 153 PHE C CD2   
3701  C CE1   . PHE C 152 ? 0.5476 0.5139 0.5001 -0.0152 0.0047  -0.0685 153 PHE C CE1   
3702  C CE2   . PHE C 152 ? 0.5251 0.4930 0.4820 -0.0178 0.0096  -0.0653 153 PHE C CE2   
3703  C CZ    . PHE C 152 ? 0.5396 0.5067 0.4968 -0.0177 0.0063  -0.0676 153 PHE C CZ    
3704  N N     . ASN C 153 ? 0.5402 0.5050 0.4696 -0.0055 0.0148  -0.0617 154 ASN C N     
3705  C CA    . ASN C 153 ? 0.5238 0.4883 0.4481 -0.0036 0.0172  -0.0600 154 ASN C CA    
3706  C C     . ASN C 153 ? 0.5092 0.4765 0.4365 -0.0054 0.0200  -0.0574 154 ASN C C     
3707  O O     . ASN C 153 ? 0.4416 0.4097 0.3707 -0.0064 0.0193  -0.0568 154 ASN C O     
3708  C CB    . ASN C 153 ? 0.5461 0.5084 0.4648 -0.0011 0.0152  -0.0609 154 ASN C CB    
3709  C CG    . ASN C 153 ? 0.5397 0.4990 0.4544 0.0010  0.0127  -0.0635 154 ASN C CG    
3710  O OD1   . ASN C 153 ? 0.5257 0.4836 0.4374 0.0023  0.0141  -0.0638 154 ASN C OD1   
3711  N ND2   . ASN C 153 ? 0.5590 0.5172 0.4736 0.0013  0.0089  -0.0655 154 ASN C ND2   
3712  N N     . HIS C 154 ? 0.5186 0.4872 0.4463 -0.0058 0.0231  -0.0559 155 HIS C N     
3713  C CA    . HIS C 154 ? 0.5661 0.5372 0.4962 -0.0076 0.0259  -0.0534 155 HIS C CA    
3714  C C     . HIS C 154 ? 0.5645 0.5356 0.4902 -0.0060 0.0289  -0.0519 155 HIS C C     
3715  O O     . HIS C 154 ? 0.5853 0.5562 0.5091 -0.0046 0.0298  -0.0523 155 HIS C O     
3716  C CB    . HIS C 154 ? 0.5749 0.5483 0.5110 -0.0101 0.0267  -0.0529 155 HIS C CB    
3717  C CG    . HIS C 154 ? 0.6182 0.5922 0.5591 -0.0122 0.0247  -0.0536 155 HIS C CG    
3718  N ND1   . HIS C 154 ? 0.6120 0.5861 0.5535 -0.0127 0.0238  -0.0533 155 HIS C ND1   
3719  C CD2   . HIS C 154 ? 0.6605 0.6350 0.6058 -0.0138 0.0236  -0.0544 155 HIS C CD2   
3720  C CE1   . HIS C 154 ? 0.6179 0.5929 0.5642 -0.0146 0.0223  -0.0540 155 HIS C CE1   
3721  N NE2   . HIS C 154 ? 0.6194 0.5945 0.5680 -0.0154 0.0222  -0.0546 155 HIS C NE2   
3722  N N     . VAL C 155 ? 0.5666 0.5379 0.4907 -0.0063 0.0305  -0.0501 156 VAL C N     
3723  C CA    . VAL C 155 ? 0.5256 0.4971 0.4459 -0.0053 0.0337  -0.0484 156 VAL C CA    
3724  C C     . VAL C 155 ? 0.4986 0.4731 0.4230 -0.0080 0.0364  -0.0462 156 VAL C C     
3725  O O     . VAL C 155 ? 0.4393 0.4139 0.3651 -0.0096 0.0366  -0.0451 156 VAL C O     
3726  C CB    . VAL C 155 ? 0.5953 0.5640 0.5095 -0.0034 0.0336  -0.0478 156 VAL C CB    
3727  C CG1   . VAL C 155 ? 0.6115 0.5804 0.5220 -0.0029 0.0374  -0.0457 156 VAL C CG1   
3728  C CG2   . VAL C 155 ? 0.6332 0.5989 0.5427 -0.0006 0.0307  -0.0501 156 VAL C CG2   
3729  N N     . PRO C 156 ? 0.5010 0.4781 0.4276 -0.0084 0.0385  -0.0457 157 PRO C N     
3730  C CA    . PRO C 156 ? 0.4702 0.4504 0.4007 -0.0109 0.0409  -0.0438 157 PRO C CA    
3731  C C     . PRO C 156 ? 0.4853 0.4657 0.4127 -0.0110 0.0440  -0.0418 157 PRO C C     
3732  O O     . PRO C 156 ? 0.4869 0.4654 0.4090 -0.0086 0.0448  -0.0418 157 PRO C O     
3733  C CB    . PRO C 156 ? 0.4734 0.4562 0.4068 -0.0108 0.0416  -0.0443 157 PRO C CB    
3734  C CG    . PRO C 156 ? 0.4714 0.4522 0.4001 -0.0076 0.0412  -0.0457 157 PRO C CG    
3735  C CD    . PRO C 156 ? 0.4810 0.4580 0.4062 -0.0064 0.0384  -0.0470 157 PRO C CD    
3736  N N     . ASP C 157 ? 0.4558 0.4381 0.3864 -0.0136 0.0456  -0.0402 158 ASP C N     
3737  C CA    . ASP C 157 ? 0.4660 0.4489 0.3947 -0.0143 0.0488  -0.0381 158 ASP C CA    
3738  C C     . ASP C 157 ? 0.4720 0.4592 0.4040 -0.0152 0.0513  -0.0373 158 ASP C C     
3739  O O     . ASP C 157 ? 0.4706 0.4606 0.4078 -0.0174 0.0512  -0.0372 158 ASP C O     
3740  C CB    . ASP C 157 ? 0.4602 0.4419 0.3899 -0.0167 0.0490  -0.0369 158 ASP C CB    
3741  C CG    . ASP C 157 ? 0.4606 0.4426 0.3888 -0.0180 0.0523  -0.0347 158 ASP C CG    
3742  O OD1   . ASP C 157 ? 0.4908 0.4745 0.4177 -0.0173 0.0548  -0.0340 158 ASP C OD1   
3743  O OD2   . ASP C 157 ? 0.4586 0.4389 0.3867 -0.0198 0.0525  -0.0337 158 ASP C OD2   
3744  N N     . PRO C 158 ? 0.4447 0.4326 0.3737 -0.0134 0.0535  -0.0369 159 PRO C N     
3745  C CA    . PRO C 158 ? 0.4496 0.4421 0.3820 -0.0137 0.0557  -0.0364 159 PRO C CA    
3746  C C     . PRO C 158 ? 0.4611 0.4570 0.3973 -0.0169 0.0582  -0.0345 159 PRO C C     
3747  O O     . PRO C 158 ? 0.4684 0.4687 0.4080 -0.0174 0.0599  -0.0340 159 PRO C O     
3748  C CB    . PRO C 158 ? 0.4842 0.4759 0.4114 -0.0106 0.0575  -0.0365 159 PRO C CB    
3749  C CG    . PRO C 158 ? 0.5006 0.4878 0.4218 -0.0098 0.0575  -0.0359 159 PRO C CG    
3750  C CD    . PRO C 158 ? 0.4782 0.4626 0.4003 -0.0108 0.0541  -0.0368 159 PRO C CD    
3751  N N     . THR C 159 ? 0.4544 0.4481 0.3900 -0.0189 0.0582  -0.0335 160 THR C N     
3752  C CA    . THR C 159 ? 0.4639 0.4600 0.4026 -0.0222 0.0603  -0.0318 160 THR C CA    
3753  C C     . THR C 159 ? 0.4621 0.4599 0.4062 -0.0247 0.0584  -0.0323 160 THR C C     
3754  O O     . THR C 159 ? 0.4871 0.4877 0.4349 -0.0274 0.0597  -0.0313 160 THR C O     
3755  C CB    . THR C 159 ? 0.4754 0.4676 0.4098 -0.0230 0.0616  -0.0304 160 THR C CB    
3756  O OG1   . THR C 159 ? 0.5338 0.5222 0.4669 -0.0228 0.0588  -0.0312 160 THR C OG1   
3757  C CG2   . THR C 159 ? 0.4704 0.4606 0.3988 -0.0204 0.0636  -0.0298 160 THR C CG2   
3758  N N     . THR C 160 ? 0.4602 0.4562 0.4047 -0.0237 0.0554  -0.0339 161 THR C N     
3759  C CA    . THR C 160 ? 0.4436 0.4403 0.3924 -0.0258 0.0536  -0.0343 161 THR C CA    
3760  C C     . THR C 160 ? 0.3993 0.3995 0.3520 -0.0253 0.0527  -0.0353 161 THR C C     
3761  O O     . THR C 160 ? 0.3969 0.3979 0.3484 -0.0229 0.0529  -0.0359 161 THR C O     
3762  C CB    . THR C 160 ? 0.4551 0.4478 0.4022 -0.0252 0.0509  -0.0354 161 THR C CB    
3763  O OG1   . THR C 160 ? 0.5170 0.5090 0.4630 -0.0226 0.0492  -0.0370 161 THR C OG1   
3764  C CG2   . THR C 160 ? 0.4821 0.4709 0.4245 -0.0248 0.0515  -0.0346 161 THR C CG2   
3765  N N     . HIS C 161 ? 0.3992 0.4010 0.3561 -0.0275 0.0517  -0.0353 162 HIS C N     
3766  C CA    . HIS C 161 ? 0.3693 0.3733 0.3294 -0.0269 0.0503  -0.0363 162 HIS C CA    
3767  C C     . HIS C 161 ? 0.3878 0.3883 0.3465 -0.0254 0.0477  -0.0378 162 HIS C C     
3768  O O     . HIS C 161 ? 0.4165 0.4143 0.3746 -0.0263 0.0465  -0.0381 162 HIS C O     
3769  C CB    . HIS C 161 ? 0.3816 0.3882 0.3462 -0.0297 0.0501  -0.0358 162 HIS C CB    
3770  C CG    . HIS C 161 ? 0.3545 0.3655 0.3214 -0.0310 0.0523  -0.0346 162 HIS C CG    
3771  N ND1   . HIS C 161 ? 0.3370 0.3482 0.3037 -0.0334 0.0541  -0.0333 162 HIS C ND1   
3772  C CD2   . HIS C 161 ? 0.3394 0.3549 0.3091 -0.0304 0.0531  -0.0345 162 HIS C CD2   
3773  C CE1   . HIS C 161 ? 0.3533 0.3692 0.3229 -0.0343 0.0558  -0.0325 162 HIS C CE1   
3774  N NE2   . HIS C 161 ? 0.3602 0.3790 0.3318 -0.0324 0.0552  -0.0332 162 HIS C NE2   
3775  N N     . LEU C 162 ? 0.4028 0.4033 0.3607 -0.0230 0.0470  -0.0389 163 LEU C N     
3776  C CA    . LEU C 162 ? 0.3980 0.3952 0.3545 -0.0215 0.0446  -0.0405 163 LEU C CA    
3777  C C     . LEU C 162 ? 0.3754 0.3735 0.3351 -0.0217 0.0432  -0.0413 163 LEU C C     
3778  O O     . LEU C 162 ? 0.3704 0.3711 0.3316 -0.0208 0.0440  -0.0412 163 LEU C O     
3779  C CB    . LEU C 162 ? 0.4325 0.4280 0.3847 -0.0184 0.0448  -0.0414 163 LEU C CB    
3780  C CG    . LEU C 162 ? 0.4871 0.4791 0.4374 -0.0168 0.0422  -0.0433 163 LEU C CG    
3781  C CD1   . LEU C 162 ? 0.5252 0.5144 0.4745 -0.0177 0.0406  -0.0436 163 LEU C CD1   
3782  C CD2   . LEU C 162 ? 0.5213 0.5118 0.4673 -0.0136 0.0424  -0.0442 163 LEU C CD2   
3783  N N     . LEU C 163 ? 0.4169 0.4129 0.3778 -0.0228 0.0413  -0.0420 164 LEU C N     
3784  C CA    . LEU C 163 ? 0.4094 0.4054 0.3729 -0.0230 0.0399  -0.0426 164 LEU C CA    
3785  C C     . LEU C 163 ? 0.3958 0.3883 0.3576 -0.0215 0.0379  -0.0444 164 LEU C C     
3786  O O     . LEU C 163 ? 0.3983 0.3885 0.3587 -0.0216 0.0368  -0.0450 164 LEU C O     
3787  C CB    . LEU C 163 ? 0.4227 0.4191 0.3892 -0.0258 0.0395  -0.0420 164 LEU C CB    
3788  C CG    . LEU C 163 ? 0.4328 0.4325 0.4012 -0.0276 0.0412  -0.0405 164 LEU C CG    
3789  C CD1   . LEU C 163 ? 0.4291 0.4287 0.4000 -0.0300 0.0405  -0.0402 164 LEU C CD1   
3790  C CD2   . LEU C 163 ? 0.4466 0.4496 0.4161 -0.0267 0.0423  -0.0401 164 LEU C CD2   
3791  N N     . LEU C 164 ? 0.4149 0.4070 0.3769 -0.0200 0.0373  -0.0451 165 LEU C N     
3792  C CA    . LEU C 164 ? 0.3911 0.3797 0.3521 -0.0190 0.0352  -0.0468 165 LEU C CA    
3793  C C     . LEU C 164 ? 0.3724 0.3605 0.3363 -0.0203 0.0343  -0.0469 165 LEU C C     
3794  O O     . LEU C 164 ? 0.3367 0.3260 0.3015 -0.0196 0.0349  -0.0465 165 LEU C O     
3795  C CB    . LEU C 164 ? 0.4240 0.4114 0.3817 -0.0160 0.0353  -0.0479 165 LEU C CB    
3796  C CG    . LEU C 164 ? 0.4207 0.4077 0.3746 -0.0144 0.0360  -0.0480 165 LEU C CG    
3797  C CD1   . LEU C 164 ? 0.4729 0.4578 0.4232 -0.0114 0.0357  -0.0494 165 LEU C CD1   
3798  C CD2   . LEU C 164 ? 0.4214 0.4064 0.3742 -0.0154 0.0347  -0.0484 165 LEU C CD2   
3799  N N     . TRP C 165 ? 0.3777 0.3641 0.3431 -0.0221 0.0330  -0.0473 166 TRP C N     
3800  C CA    . TRP C 165 ? 0.3750 0.3606 0.3429 -0.0235 0.0323  -0.0473 166 TRP C CA    
3801  C C     . TRP C 165 ? 0.3650 0.3472 0.3319 -0.0223 0.0308  -0.0488 166 TRP C C     
3802  O O     . TRP C 165 ? 0.3992 0.3795 0.3637 -0.0208 0.0299  -0.0501 166 TRP C O     
3803  C CB    . TRP C 165 ? 0.3500 0.3354 0.3200 -0.0260 0.0319  -0.0470 166 TRP C CB    
3804  C CG    . TRP C 165 ? 0.3793 0.3673 0.3500 -0.0273 0.0333  -0.0456 166 TRP C CG    
3805  C CD1   . TRP C 165 ? 0.4328 0.4221 0.4017 -0.0266 0.0343  -0.0452 166 TRP C CD1   
3806  C CD2   . TRP C 165 ? 0.3714 0.3606 0.3444 -0.0295 0.0339  -0.0445 166 TRP C CD2   
3807  N NE1   . TRP C 165 ? 0.4325 0.4235 0.4025 -0.0284 0.0354  -0.0439 166 TRP C NE1   
3808  C CE2   . TRP C 165 ? 0.3731 0.3642 0.3456 -0.0301 0.0352  -0.0436 166 TRP C CE2   
3809  C CE3   . TRP C 165 ? 0.3426 0.3313 0.3177 -0.0310 0.0336  -0.0443 166 TRP C CE3   
3810  C CZ2   . TRP C 165 ? 0.4008 0.3931 0.3748 -0.0322 0.0359  -0.0425 166 TRP C CZ2   
3811  C CZ3   . TRP C 165 ? 0.3828 0.3728 0.3592 -0.0329 0.0345  -0.0432 166 TRP C CZ3   
3812  C CH2   . TRP C 165 ? 0.3469 0.3388 0.3229 -0.0335 0.0355  -0.0424 166 TRP C CH2   
3813  N N     . GLN C 166 ? 0.3542 0.3353 0.3227 -0.0229 0.0305  -0.0486 167 GLN C N     
3814  C CA    . GLN C 166 ? 0.4174 0.3947 0.3850 -0.0221 0.0292  -0.0499 167 GLN C CA    
3815  C C     . GLN C 166 ? 0.4326 0.4088 0.3968 -0.0191 0.0291  -0.0510 167 GLN C C     
3816  O O     . GLN C 166 ? 0.4498 0.4230 0.4123 -0.0183 0.0276  -0.0526 167 GLN C O     
3817  C CB    . GLN C 166 ? 0.4293 0.4042 0.3979 -0.0237 0.0276  -0.0511 167 GLN C CB    
3818  C CG    . GLN C 166 ? 0.4455 0.4212 0.4174 -0.0265 0.0279  -0.0501 167 GLN C CG    
3819  C CD    . GLN C 166 ? 0.4862 0.4601 0.4596 -0.0281 0.0266  -0.0513 167 GLN C CD    
3820  O OE1   . GLN C 166 ? 0.4726 0.4449 0.4448 -0.0272 0.0251  -0.0529 167 GLN C OE1   
3821  N NE2   . GLN C 166 ? 0.5601 0.5347 0.5363 -0.0304 0.0270  -0.0505 167 GLN C NE2   
3822  N N     . ILE C 167 ? 0.4223 0.4013 0.3859 -0.0175 0.0306  -0.0500 168 ILE C N     
3823  C CA    . ILE C 167 ? 0.4028 0.3812 0.3633 -0.0145 0.0309  -0.0508 168 ILE C CA    
3824  C C     . ILE C 167 ? 0.4136 0.3884 0.3730 -0.0129 0.0299  -0.0518 168 ILE C C     
3825  O O     . ILE C 167 ? 0.4291 0.4015 0.3854 -0.0105 0.0295  -0.0532 168 ILE C O     
3826  C CB    . ILE C 167 ? 0.3805 0.3636 0.3413 -0.0134 0.0330  -0.0494 168 ILE C CB    
3827  C CG1   . ILE C 167 ? 0.4034 0.3862 0.3609 -0.0101 0.0337  -0.0502 168 ILE C CG1   
3828  C CG2   . ILE C 167 ? 0.3812 0.3666 0.3448 -0.0140 0.0336  -0.0480 168 ILE C CG2   
3829  C CD1   . ILE C 167 ? 0.4063 0.3870 0.3604 -0.0093 0.0332  -0.0514 168 ILE C CD1   
3830  N N     . ALA C 168 ? 0.3758 0.3498 0.3374 -0.0143 0.0296  -0.0511 169 ALA C N     
3831  C CA    . ALA C 168 ? 0.3971 0.3674 0.3576 -0.0129 0.0289  -0.0517 169 ALA C CA    
3832  C C     . ALA C 168 ? 0.3740 0.3390 0.3326 -0.0130 0.0271  -0.0537 169 ALA C C     
3833  O O     . ALA C 168 ? 0.4112 0.3723 0.3676 -0.0111 0.0265  -0.0547 169 ALA C O     
3834  C CB    . ALA C 168 ? 0.4046 0.3751 0.3677 -0.0147 0.0291  -0.0503 169 ALA C CB    
3835  N N     . ILE C 169 ? 0.3691 0.3339 0.3285 -0.0150 0.0262  -0.0544 170 ILE C N     
3836  C CA    . ILE C 169 ? 0.3926 0.3529 0.3509 -0.0155 0.0243  -0.0564 170 ILE C CA    
3837  C C     . ILE C 169 ? 0.3911 0.3520 0.3473 -0.0146 0.0236  -0.0577 170 ILE C C     
3838  O O     . ILE C 169 ? 0.3673 0.3261 0.3235 -0.0157 0.0218  -0.0592 170 ILE C O     
3839  C CB    . ILE C 169 ? 0.4434 0.4027 0.4051 -0.0188 0.0235  -0.0563 170 ILE C CB    
3840  C CG1   . ILE C 169 ? 0.4815 0.4451 0.4460 -0.0209 0.0242  -0.0550 170 ILE C CG1   
3841  C CG2   . ILE C 169 ? 0.5032 0.4603 0.4658 -0.0194 0.0239  -0.0553 170 ILE C CG2   
3842  C CD1   . ILE C 169 ? 0.4928 0.4557 0.4607 -0.0241 0.0237  -0.0549 170 ILE C CD1   
3843  N N     . ALA C 170 ? 0.3946 0.3584 0.3489 -0.0125 0.0250  -0.0570 171 ALA C N     
3844  C CA    . ALA C 170 ? 0.3844 0.3487 0.3360 -0.0113 0.0247  -0.0579 171 ALA C CA    
3845  C C     . ALA C 170 ? 0.4266 0.3862 0.3744 -0.0094 0.0229  -0.0603 171 ALA C C     
3846  O O     . ALA C 170 ? 0.4171 0.3749 0.3622 -0.0068 0.0234  -0.0609 171 ALA C O     
3847  C CB    . ALA C 170 ? 0.3790 0.3471 0.3293 -0.0095 0.0270  -0.0566 171 ALA C CB    
3848  N N     . GLY C 171 ? 0.4513 0.4089 0.3989 -0.0106 0.0208  -0.0619 172 GLY C N     
3849  C CA    . GLY C 171 ? 0.5026 0.4557 0.4466 -0.0091 0.0187  -0.0644 172 GLY C CA    
3850  C C     . GLY C 171 ? 0.5689 0.5180 0.5148 -0.0110 0.0168  -0.0657 172 GLY C C     
3851  O O     . GLY C 171 ? 0.6467 0.5916 0.5901 -0.0104 0.0147  -0.0681 172 GLY C O     
3852  N N     . GLU C 172 ? 0.5392 0.4893 0.4892 -0.0133 0.0176  -0.0643 173 GLU C N     
3853  C CA    . GLU C 172 ? 0.6084 0.5549 0.5606 -0.0155 0.0162  -0.0651 173 GLU C CA    
3854  C C     . GLU C 172 ? 0.5697 0.5167 0.5245 -0.0181 0.0143  -0.0662 173 GLU C C     
3855  O O     . GLU C 172 ? 0.6307 0.5812 0.5894 -0.0203 0.0149  -0.0649 173 GLU C O     
3856  C CB    . GLU C 172 ? 0.6187 0.5663 0.5740 -0.0170 0.0179  -0.0630 173 GLU C CB    
3857  C CG    . GLU C 172 ? 0.6553 0.5979 0.6113 -0.0184 0.0170  -0.0636 173 GLU C CG    
3858  C CD    . GLU C 172 ? 0.7880 0.7290 0.7468 -0.0215 0.0152  -0.0650 173 GLU C CD    
3859  O OE1   . GLU C 172 ? 0.7874 0.7286 0.7498 -0.0242 0.0157  -0.0639 173 GLU C OE1   
3860  O OE2   . GLU C 172 ? 0.9709 0.9107 0.9283 -0.0211 0.0132  -0.0671 173 GLU C OE2   
3861  N N     . HIS C 173 ? 0.4960 0.4396 0.4488 -0.0177 0.0118  -0.0688 174 HIS C N     
3862  C CA    . HIS C 173 ? 0.4627 0.4074 0.4174 -0.0194 0.0097  -0.0701 174 HIS C CA    
3863  C C     . HIS C 173 ? 0.4968 0.4398 0.4559 -0.0228 0.0084  -0.0709 174 HIS C C     
3864  O O     . HIS C 173 ? 0.4926 0.4378 0.4552 -0.0249 0.0072  -0.0714 174 HIS C O     
3865  C CB    . HIS C 173 ? 0.4384 0.3809 0.3884 -0.0171 0.0076  -0.0725 174 HIS C CB    
3866  C CG    . HIS C 173 ? 0.4228 0.3593 0.3700 -0.0164 0.0059  -0.0748 174 HIS C CG    
3867  N ND1   . HIS C 173 ? 0.4310 0.3643 0.3737 -0.0136 0.0070  -0.0749 174 HIS C ND1   
3868  C CD2   . HIS C 173 ? 0.4154 0.3484 0.3636 -0.0182 0.0033  -0.0771 174 HIS C CD2   
3869  C CE1   . HIS C 173 ? 0.4360 0.3637 0.3767 -0.0136 0.0051  -0.0772 174 HIS C CE1   
3870  N NE2   . HIS C 173 ? 0.4261 0.3534 0.3702 -0.0165 0.0028  -0.0786 174 HIS C NE2   
3871  N N     . THR C 174 ? 0.5422 0.4811 0.5010 -0.0233 0.0088  -0.0709 175 THR C N     
3872  C CA    . THR C 174 ? 0.5785 0.5149 0.5410 -0.0266 0.0078  -0.0716 175 THR C CA    
3873  C C     . THR C 174 ? 0.5260 0.4662 0.4936 -0.0293 0.0097  -0.0693 175 THR C C     
3874  O O     . THR C 174 ? 0.5269 0.4675 0.4988 -0.0323 0.0089  -0.0697 175 THR C O     
3875  C CB    . THR C 174 ? 0.6007 0.5309 0.5605 -0.0260 0.0078  -0.0722 175 THR C CB    
3876  O OG1   . THR C 174 ? 0.6634 0.5945 0.6226 -0.0248 0.0105  -0.0697 175 THR C OG1   
3877  C CG2   . THR C 174 ? 0.6440 0.5701 0.5982 -0.0230 0.0062  -0.0746 175 THR C CG2   
3878  N N     . LEU C 175 ? 0.5561 0.4990 0.5232 -0.0281 0.0121  -0.0669 176 LEU C N     
3879  C CA    . LEU C 175 ? 0.5830 0.5291 0.5542 -0.0303 0.0139  -0.0647 176 LEU C CA    
3880  C C     . LEU C 175 ? 0.5733 0.5155 0.5457 -0.0322 0.0146  -0.0641 176 LEU C C     
3881  O O     . LEU C 175 ? 0.5349 0.4784 0.5112 -0.0349 0.0154  -0.0630 176 LEU C O     
3882  C CB    . LEU C 175 ? 0.5557 0.5057 0.5310 -0.0325 0.0132  -0.0650 176 LEU C CB    
3883  C CG    . LEU C 175 ? 0.6242 0.5775 0.5981 -0.0307 0.0124  -0.0655 176 LEU C CG    
3884  C CD1   . LEU C 175 ? 0.5960 0.5533 0.5744 -0.0328 0.0120  -0.0654 176 LEU C CD1   
3885  C CD2   . LEU C 175 ? 0.6640 0.6195 0.6350 -0.0283 0.0143  -0.0638 176 LEU C CD2   
3886  N N     . THR C 176 ? 0.5807 0.5178 0.5496 -0.0306 0.0141  -0.0649 177 THR C N     
3887  C CA    . THR C 176 ? 0.5304 0.4628 0.4995 -0.0320 0.0147  -0.0644 177 THR C CA    
3888  C C     . THR C 176 ? 0.5453 0.4762 0.5111 -0.0294 0.0163  -0.0628 177 THR C C     
3889  O O     . THR C 176 ? 0.5569 0.4848 0.5228 -0.0302 0.0172  -0.0616 177 THR C O     
3890  C CB    . THR C 176 ? 0.5387 0.4655 0.5067 -0.0328 0.0124  -0.0670 177 THR C CB    
3891  O OG1   . THR C 176 ? 0.5260 0.4504 0.4889 -0.0292 0.0117  -0.0683 177 THR C OG1   
3892  C CG2   . THR C 176 ? 0.5366 0.4655 0.5081 -0.0351 0.0105  -0.0689 177 THR C CG2   
3893  N N     . GLN C 177 ? 0.4994 0.4326 0.4624 -0.0262 0.0165  -0.0628 178 GLN C N     
3894  C CA    . GLN C 177 ? 0.5383 0.4710 0.4984 -0.0233 0.0179  -0.0615 178 GLN C CA    
3895  C C     . GLN C 177 ? 0.5435 0.4821 0.5056 -0.0234 0.0198  -0.0591 178 GLN C C     
3896  O O     . GLN C 177 ? 0.4266 0.3697 0.3909 -0.0246 0.0200  -0.0588 178 GLN C O     
3897  C CB    . GLN C 177 ? 0.5266 0.4582 0.4824 -0.0196 0.0173  -0.0630 178 GLN C CB    
3898  C CG    . GLN C 177 ? 0.6232 0.5486 0.5763 -0.0194 0.0152  -0.0656 178 GLN C CG    
3899  C CD    . GLN C 177 ? 0.6603 0.5794 0.6127 -0.0201 0.0151  -0.0656 178 GLN C CD    
3900  O OE1   . GLN C 177 ? 0.6539 0.5731 0.6078 -0.0210 0.0166  -0.0635 178 GLN C OE1   
3901  N NE2   . GLN C 177 ? 0.7362 0.6493 0.6857 -0.0196 0.0134  -0.0679 178 GLN C NE2   
3902  N N     . PHE C 178 ? 0.6097 0.5481 0.5708 -0.0220 0.0212  -0.0574 179 PHE C N     
3903  C CA    . PHE C 178 ? 0.6375 0.5810 0.6004 -0.0223 0.0228  -0.0551 179 PHE C CA    
3904  C C     . PHE C 178 ? 0.6692 0.6164 0.6303 -0.0191 0.0236  -0.0548 179 PHE C C     
3905  O O     . PHE C 178 ? 0.6221 0.5742 0.5847 -0.0192 0.0248  -0.0532 179 PHE C O     
3906  C CB    . PHE C 178 ? 0.7417 0.6829 0.7048 -0.0228 0.0237  -0.0534 179 PHE C CB    
3907  C CG    . PHE C 178 ? 0.8643 0.8023 0.8294 -0.0262 0.0235  -0.0533 179 PHE C CG    
3908  C CD1   . PHE C 178 ? 0.8529 0.7937 0.8215 -0.0292 0.0235  -0.0534 179 PHE C CD1   
3909  C CD2   . PHE C 178 ? 0.9002 0.8322 0.8638 -0.0264 0.0234  -0.0532 179 PHE C CD2   
3910  C CE1   . PHE C 178 ? 0.8095 0.7479 0.7804 -0.0323 0.0236  -0.0533 179 PHE C CE1   
3911  C CE2   . PHE C 178 ? 0.8989 0.8279 0.8644 -0.0297 0.0235  -0.0530 179 PHE C CE2   
3912  C CZ    . PHE C 178 ? 0.8483 0.7808 0.8176 -0.0327 0.0236  -0.0531 179 PHE C CZ    
3913  N N     . HIS C 179 ? 0.6619 0.6066 0.6197 -0.0164 0.0229  -0.0564 180 HIS C N     
3914  C CA    . HIS C 179 ? 0.6752 0.6232 0.6312 -0.0133 0.0237  -0.0562 180 HIS C CA    
3915  C C     . HIS C 179 ? 0.5867 0.5323 0.5394 -0.0114 0.0227  -0.0585 180 HIS C C     
3916  O O     . HIS C 179 ? 0.5892 0.5297 0.5406 -0.0119 0.0211  -0.0602 180 HIS C O     
3917  C CB    . HIS C 179 ? 0.6925 0.6401 0.6473 -0.0108 0.0247  -0.0550 180 HIS C CB    
3918  C CG    . HIS C 179 ? 0.7874 0.7283 0.7395 -0.0095 0.0238  -0.0561 180 HIS C CG    
3919  N ND1   . HIS C 179 ? 0.8625 0.8002 0.8109 -0.0065 0.0232  -0.0578 180 HIS C ND1   
3920  C CD2   . HIS C 179 ? 0.7776 0.7140 0.7299 -0.0107 0.0234  -0.0556 180 HIS C CD2   
3921  C CE1   . HIS C 179 ? 0.8170 0.7482 0.7634 -0.0060 0.0224  -0.0584 180 HIS C CE1   
3922  N NE2   . HIS C 179 ? 0.8137 0.7440 0.7625 -0.0086 0.0226  -0.0570 180 HIS C NE2   
3923  N N     . THR C 180 ? 0.5842 0.5335 0.5355 -0.0092 0.0235  -0.0584 181 THR C N     
3924  C CA    . THR C 180 ? 0.6305 0.5779 0.5782 -0.0070 0.0227  -0.0604 181 THR C CA    
3925  C C     . THR C 180 ? 0.6390 0.5842 0.5832 -0.0032 0.0234  -0.0608 181 THR C C     
3926  O O     . THR C 180 ? 0.5580 0.5016 0.5026 -0.0025 0.0238  -0.0600 181 THR C O     
3927  C CB    . THR C 180 ? 0.6024 0.5546 0.5501 -0.0069 0.0235  -0.0601 181 THR C CB    
3928  O OG1   . THR C 180 ? 0.6267 0.5762 0.5704 -0.0049 0.0225  -0.0622 181 THR C OG1   
3929  C CG2   . THR C 180 ? 0.5924 0.5498 0.5407 -0.0053 0.0258  -0.0582 181 THR C CG2   
3930  N N     . SER C 181 ? 0.6359 0.5810 0.5765 -0.0005 0.0235  -0.0621 182 SER C N     
3931  C CA    . SER C 181 ? 0.6651 0.6084 0.6022 0.0035  0.0243  -0.0627 182 SER C CA    
3932  C C     . SER C 181 ? 0.6601 0.6086 0.5960 0.0059  0.0263  -0.0620 182 SER C C     
3933  O O     . SER C 181 ? 0.6205 0.5727 0.5575 0.0045  0.0267  -0.0615 182 SER C O     
3934  C CB    . SER C 181 ? 0.7100 0.6463 0.6428 0.0049  0.0224  -0.0653 182 SER C CB    
3935  O OG    . SER C 181 ? 0.7245 0.6603 0.6552 0.0045  0.0213  -0.0670 182 SER C OG    
3936  N N     . SER C 182 ? 0.6765 0.6252 0.6103 0.0096  0.0276  -0.0620 183 SER C N     
3937  C CA    . SER C 182 ? 0.6982 0.6520 0.6312 0.0120  0.0298  -0.0613 183 SER C CA    
3938  C C     . SER C 182 ? 0.6547 0.6070 0.5835 0.0130  0.0295  -0.0629 183 SER C C     
3939  O O     . SER C 182 ? 0.6364 0.5932 0.5651 0.0135  0.0312  -0.0621 183 SER C O     
3940  C CB    . SER C 182 ? 0.7297 0.6840 0.6617 0.0159  0.0313  -0.0610 183 SER C CB    
3941  O OG    . SER C 182 ? 0.7312 0.6787 0.6584 0.0185  0.0301  -0.0632 183 SER C OG    
3942  N N     . ASP C 183 ? 0.6546 0.6003 0.5798 0.0133  0.0273  -0.0653 184 ASP C N     
3943  C CA    . ASP C 183 ? 0.6861 0.6296 0.6066 0.0146  0.0265  -0.0671 184 ASP C CA    
3944  C C     . ASP C 183 ? 0.6735 0.6197 0.5959 0.0115  0.0259  -0.0666 184 ASP C C     
3945  O O     . ASP C 183 ? 0.6539 0.6013 0.5734 0.0126  0.0264  -0.0669 184 ASP C O     
3946  C CB    . ASP C 183 ? 0.7650 0.7007 0.6813 0.0157  0.0241  -0.0699 184 ASP C CB    
3947  C CG    . ASP C 183 ? 0.8355 0.7673 0.7545 0.0122  0.0217  -0.0705 184 ASP C CG    
3948  O OD1   . ASP C 183 ? 0.8396 0.7719 0.7620 0.0113  0.0222  -0.0692 184 ASP C OD1   
3949  O OD2   . ASP C 183 ? 0.8775 0.8061 0.7953 0.0106  0.0193  -0.0724 184 ASP C OD2   
3950  N N     . ARG C 184 ? 0.6520 0.5990 0.5791 0.0078  0.0248  -0.0658 185 ARG C N     
3951  C CA    . ARG C 184 ? 0.6794 0.6292 0.6087 0.0049  0.0243  -0.0651 185 ARG C CA    
3952  C C     . ARG C 184 ? 0.6026 0.5587 0.5336 0.0050  0.0269  -0.0628 185 ARG C C     
3953  O O     . ARG C 184 ? 0.5455 0.5033 0.4750 0.0049  0.0273  -0.0626 185 ARG C O     
3954  C CB    . ARG C 184 ? 0.7015 0.6507 0.6356 0.0011  0.0228  -0.0647 185 ARG C CB    
3955  C CG    . ARG C 184 ? 0.7582 0.7019 0.6912 -0.0002 0.0199  -0.0670 185 ARG C CG    
3956  C CD    . ARG C 184 ? 0.8165 0.7544 0.7461 0.0020  0.0190  -0.0688 185 ARG C CD    
3957  N NE    . ARG C 184 ? 0.8263 0.7589 0.7551 0.0004  0.0161  -0.0712 185 ARG C NE    
3958  C CZ    . ARG C 184 ? 0.8422 0.7733 0.7687 0.0004  0.0141  -0.0731 185 ARG C CZ    
3959  N NH1   . ARG C 184 ? 0.8664 0.8004 0.7904 0.0021  0.0149  -0.0729 185 ARG C NH1   
3960  N NH2   . ARG C 184 ? 0.8497 0.7762 0.7761 -0.0014 0.0114  -0.0753 185 ARG C NH2   
3961  N N     . LEU C 185 ? 0.5611 0.5205 0.4952 0.0051  0.0288  -0.0610 186 LEU C N     
3962  C CA    . LEU C 185 ? 0.5492 0.5149 0.4856 0.0047  0.0313  -0.0588 186 LEU C CA    
3963  C C     . LEU C 185 ? 0.5580 0.5251 0.4905 0.0078  0.0331  -0.0589 186 LEU C C     
3964  O O     . LEU C 185 ? 0.5725 0.5438 0.5057 0.0073  0.0349  -0.0575 186 LEU C O     
3965  C CB    . LEU C 185 ? 0.5326 0.5013 0.4730 0.0045  0.0324  -0.0571 186 LEU C CB    
3966  C CG    . LEU C 185 ? 0.5752 0.5429 0.5194 0.0013  0.0310  -0.0566 186 LEU C CG    
3967  C CD1   . LEU C 185 ? 0.5681 0.5388 0.5155 0.0015  0.0322  -0.0549 186 LEU C CD1   
3968  C CD2   . LEU C 185 ? 0.6023 0.5721 0.5489 -0.0021 0.0307  -0.0558 186 LEU C CD2   
3969  N N     . GLN C 186 ? 0.5424 0.5057 0.4706 0.0111  0.0328  -0.0607 187 GLN C N     
3970  C CA    . GLN C 186 ? 0.5944 0.5584 0.5182 0.0144  0.0347  -0.0610 187 GLN C CA    
3971  C C     . GLN C 186 ? 0.6106 0.5734 0.5311 0.0138  0.0340  -0.0616 187 GLN C C     
3972  O O     . GLN C 186 ? 0.6195 0.5851 0.5380 0.0150  0.0361  -0.0607 187 GLN C O     
3973  C CB    . GLN C 186 ? 0.6408 0.6002 0.5605 0.0180  0.0342  -0.0630 187 GLN C CB    
3974  C CG    . GLN C 186 ? 0.6969 0.6562 0.6111 0.0218  0.0361  -0.0636 187 GLN C CG    
3975  C CD    . GLN C 186 ? 0.7035 0.6698 0.6200 0.0226  0.0397  -0.0614 187 GLN C CD    
3976  O OE1   . GLN C 186 ? 0.7070 0.6770 0.6274 0.0230  0.0411  -0.0601 187 GLN C OE1   
3977  N NE2   . GLN C 186 ? 0.6648 0.6328 0.5787 0.0228  0.0411  -0.0608 187 GLN C NE2   
3978  N N     . ILE C 187 ? 0.5894 0.5481 0.5092 0.0121  0.0310  -0.0632 188 ILE C N     
3979  C CA    . ILE C 187 ? 0.5824 0.5396 0.4990 0.0117  0.0297  -0.0640 188 ILE C CA    
3980  C C     . ILE C 187 ? 0.5534 0.5154 0.4735 0.0090  0.0309  -0.0617 188 ILE C C     
3981  O O     . ILE C 187 ? 0.4843 0.4469 0.4015 0.0095  0.0315  -0.0614 188 ILE C O     
3982  C CB    . ILE C 187 ? 0.5990 0.5511 0.5148 0.0104  0.0260  -0.0663 188 ILE C CB    
3983  C CG1   . ILE C 187 ? 0.5588 0.5054 0.4703 0.0131  0.0247  -0.0688 188 ILE C CG1   
3984  C CG2   . ILE C 187 ? 0.6109 0.5624 0.5246 0.0096  0.0244  -0.0669 188 ILE C CG2   
3985  C CD1   . ILE C 187 ? 0.5663 0.5077 0.4772 0.0116  0.0210  -0.0712 188 ILE C CD1   
3986  N N     . LEU C 188 ? 0.5029 0.4679 0.4287 0.0064  0.0313  -0.0602 189 LEU C N     
3987  C CA    . LEU C 188 ? 0.4884 0.4577 0.4177 0.0038  0.0325  -0.0581 189 LEU C CA    
3988  C C     . LEU C 188 ? 0.4314 0.4046 0.3596 0.0052  0.0358  -0.0564 189 LEU C C     
3989  O O     . LEU C 188 ? 0.3906 0.3656 0.3182 0.0043  0.0369  -0.0553 189 LEU C O     
3990  C CB    . LEU C 188 ? 0.4562 0.4275 0.3914 0.0010  0.0323  -0.0569 189 LEU C CB    
3991  C CG    . LEU C 188 ? 0.4454 0.4208 0.3843 -0.0019 0.0334  -0.0549 189 LEU C CG    
3992  C CD1   . LEU C 188 ? 0.4618 0.4358 0.3996 -0.0032 0.0320  -0.0553 189 LEU C CD1   
3993  C CD2   . LEU C 188 ? 0.4089 0.3858 0.3531 -0.0044 0.0331  -0.0540 189 LEU C CD2   
3994  N N     . VAL C 189 ? 0.4497 0.4243 0.3777 0.0075  0.0376  -0.0563 190 VAL C N     
3995  C CA    . VAL C 189 ? 0.4741 0.4529 0.4016 0.0090  0.0409  -0.0547 190 VAL C CA    
3996  C C     . VAL C 189 ? 0.4898 0.4667 0.4112 0.0109  0.0416  -0.0553 190 VAL C C     
3997  O O     . VAL C 189 ? 0.5641 0.5437 0.4852 0.0102  0.0437  -0.0537 190 VAL C O     
3998  C CB    . VAL C 189 ? 0.5135 0.4938 0.4416 0.0116  0.0423  -0.0548 190 VAL C CB    
3999  C CG1   . VAL C 189 ? 0.5453 0.5297 0.4722 0.0137  0.0459  -0.0536 190 VAL C CG1   
4000  C CG2   . VAL C 189 ? 0.5196 0.5024 0.4536 0.0098  0.0419  -0.0539 190 VAL C CG2   
4001  N N     . GLU C 190 ? 0.4827 0.4545 0.3992 0.0133  0.0398  -0.0576 191 GLU C N     
4002  C CA    . GLU C 190 ? 0.5262 0.4953 0.4360 0.0155  0.0401  -0.0584 191 GLU C CA    
4003  C C     . GLU C 190 ? 0.5111 0.4801 0.4206 0.0132  0.0391  -0.0577 191 GLU C C     
4004  O O     . GLU C 190 ? 0.5430 0.5123 0.4487 0.0142  0.0408  -0.0568 191 GLU C O     
4005  C CB    . GLU C 190 ? 0.5410 0.5042 0.4458 0.0181  0.0376  -0.0612 191 GLU C CB    
4006  C CG    . GLU C 190 ? 0.5776 0.5403 0.4819 0.0208  0.0386  -0.0621 191 GLU C CG    
4007  C CD    . GLU C 190 ? 0.6305 0.5867 0.5298 0.0231  0.0360  -0.0650 191 GLU C CD    
4008  O OE1   . GLU C 190 ? 0.6668 0.6191 0.5634 0.0224  0.0332  -0.0666 191 GLU C OE1   
4009  O OE2   . GLU C 190 ? 0.6880 0.6429 0.5861 0.0258  0.0368  -0.0659 191 GLU C OE2   
4010  N N     . GLN C 191 ? 0.5061 0.4745 0.4195 0.0103  0.0366  -0.0579 192 GLN C N     
4011  C CA    . GLN C 191 ? 0.5009 0.4691 0.4146 0.0082  0.0354  -0.0574 192 GLN C CA    
4012  C C     . GLN C 191 ? 0.4765 0.4492 0.3927 0.0065  0.0384  -0.0546 192 GLN C C     
4013  O O     . GLN C 191 ? 0.5277 0.5003 0.4410 0.0065  0.0391  -0.0537 192 GLN C O     
4014  C CB    . GLN C 191 ? 0.5003 0.4674 0.4184 0.0054  0.0323  -0.0582 192 GLN C CB    
4015  C CG    . GLN C 191 ? 0.5182 0.4850 0.4367 0.0035  0.0308  -0.0579 192 GLN C CG    
4016  C CD    . GLN C 191 ? 0.5224 0.4890 0.4460 0.0006  0.0283  -0.0585 192 GLN C CD    
4017  O OE1   . GLN C 191 ? 0.5329 0.4995 0.4598 -0.0002 0.0279  -0.0589 192 GLN C OE1   
4018  N NE2   . GLN C 191 ? 0.5100 0.4763 0.4341 -0.0008 0.0267  -0.0585 192 GLN C NE2   
4019  N N     . LEU C 192 ? 0.4127 0.3894 0.3342 0.0051  0.0400  -0.0533 193 LEU C N     
4020  C CA    . LEU C 192 ? 0.4324 0.4135 0.3570 0.0031  0.0427  -0.0508 193 LEU C CA    
4021  C C     . LEU C 192 ? 0.4530 0.4359 0.3741 0.0052  0.0460  -0.0497 193 LEU C C     
4022  O O     . LEU C 192 ? 0.4387 0.4244 0.3609 0.0037  0.0483  -0.0477 193 LEU C O     
4023  C CB    . LEU C 192 ? 0.3959 0.3807 0.3269 0.0012  0.0431  -0.0499 193 LEU C CB    
4024  C CG    . LEU C 192 ? 0.4242 0.4080 0.3591 -0.0015 0.0405  -0.0503 193 LEU C CG    
4025  C CD1   . LEU C 192 ? 0.4326 0.4198 0.3730 -0.0028 0.0412  -0.0494 193 LEU C CD1   
4026  C CD2   . LEU C 192 ? 0.4397 0.4234 0.3752 -0.0039 0.0401  -0.0494 193 LEU C CD2   
4027  N N     . ASN C 193 ? 0.5175 0.4985 0.4344 0.0085  0.0463  -0.0511 194 ASN C N     
4028  C CA    . ASN C 193 ? 0.6020 0.5848 0.5158 0.0108  0.0498  -0.0501 194 ASN C CA    
4029  C C     . ASN C 193 ? 0.6246 0.6054 0.5331 0.0111  0.0506  -0.0494 194 ASN C C     
4030  O O     . ASN C 193 ? 0.6390 0.6212 0.5446 0.0125  0.0539  -0.0482 194 ASN C O     
4031  C CB    . ASN C 193 ? 0.6244 0.6052 0.5345 0.0146  0.0499  -0.0519 194 ASN C CB    
4032  C CG    . ASN C 193 ? 0.6357 0.6194 0.5436 0.0170  0.0539  -0.0509 194 ASN C CG    
4033  O OD1   . ASN C 193 ? 0.6357 0.6249 0.5483 0.0160  0.0566  -0.0491 194 ASN C OD1   
4034  N ND2   . ASN C 193 ? 0.6508 0.6309 0.5515 0.0202  0.0544  -0.0519 194 ASN C ND2   
4035  N N     . GLN C 194 ? 0.6348 0.6124 0.5421 0.0098  0.0478  -0.0501 195 GLN C N     
4036  C CA    . GLN C 194 ? 0.6562 0.6314 0.5584 0.0101  0.0481  -0.0494 195 GLN C CA    
4037  C C     . GLN C 194 ? 0.6575 0.6362 0.5624 0.0076  0.0511  -0.0466 195 GLN C C     
4038  O O     . GLN C 194 ? 0.6326 0.6104 0.5330 0.0083  0.0531  -0.0453 195 GLN C O     
4039  C CB    . GLN C 194 ? 0.6608 0.6322 0.5620 0.0094  0.0441  -0.0508 195 GLN C CB    
4040  C CG    . GLN C 194 ? 0.6690 0.6364 0.5673 0.0115  0.0408  -0.0537 195 GLN C CG    
4041  C CD    . GLN C 194 ? 0.6766 0.6411 0.5748 0.0104  0.0368  -0.0551 195 GLN C CD    
4042  O OE1   . GLN C 194 ? 0.6031 0.5656 0.4974 0.0109  0.0361  -0.0548 195 GLN C OE1   
4043  N NE2   . GLN C 194 ? 0.6964 0.6606 0.5989 0.0090  0.0342  -0.0566 195 GLN C NE2   
4044  N N     . TRP C 195 ? 0.5907 0.5731 0.5026 0.0047  0.0513  -0.0457 196 TRP C N     
4045  C CA    . TRP C 195 ? 0.5706 0.5560 0.4856 0.0018  0.0534  -0.0433 196 TRP C CA    
4046  C C     . TRP C 195 ? 0.5860 0.5770 0.5064 0.0007  0.0561  -0.0421 196 TRP C C     
4047  O O     . TRP C 195 ? 0.6640 0.6580 0.5862 -0.0011 0.0589  -0.0400 196 TRP C O     
4048  C CB    . TRP C 195 ? 0.5550 0.5395 0.4734 -0.0011 0.0508  -0.0433 196 TRP C CB    
4049  C CG    . TRP C 195 ? 0.5123 0.4919 0.4264 0.0000  0.0477  -0.0447 196 TRP C CG    
4050  C CD1   . TRP C 195 ? 0.5487 0.5254 0.4578 0.0006  0.0478  -0.0441 196 TRP C CD1   
4051  C CD2   . TRP C 195 ? 0.5042 0.4814 0.4189 0.0005  0.0440  -0.0470 196 TRP C CD2   
4052  N NE1   . TRP C 195 ? 0.5226 0.4956 0.4292 0.0017  0.0443  -0.0459 196 TRP C NE1   
4053  C CE2   . TRP C 195 ? 0.5387 0.5121 0.4490 0.0014  0.0419  -0.0478 196 TRP C CE2   
4054  C CE3   . TRP C 195 ? 0.4623 0.4401 0.3808 0.0002  0.0422  -0.0485 196 TRP C CE3   
4055  C CZ2   . TRP C 195 ? 0.5347 0.5054 0.4447 0.0019  0.0380  -0.0500 196 TRP C CZ2   
4056  C CZ3   . TRP C 195 ? 0.4674 0.4420 0.3853 0.0006  0.0386  -0.0506 196 TRP C CZ3   
4057  C CH2   . TRP C 195 ? 0.4953 0.4667 0.4094 0.0013  0.0365  -0.0514 196 TRP C CH2   
4058  N N     . TYR C 196 ? 0.5712 0.5636 0.4942 0.0019  0.0553  -0.0433 197 TYR C N     
4059  C CA    . TYR C 196 ? 0.5403 0.5382 0.4689 0.0010  0.0572  -0.0424 197 TYR C CA    
4060  C C     . TYR C 196 ? 0.5155 0.5145 0.4424 0.0046  0.0586  -0.0432 197 TYR C C     
4061  O O     . TYR C 196 ? 0.5176 0.5130 0.4416 0.0070  0.0566  -0.0452 197 TYR C O     
4062  C CB    . TYR C 196 ? 0.4953 0.4943 0.4296 -0.0012 0.0547  -0.0428 197 TYR C CB    
4063  C CG    . TYR C 196 ? 0.5164 0.5141 0.4524 -0.0045 0.0532  -0.0422 197 TYR C CG    
4064  C CD1   . TYR C 196 ? 0.4937 0.4947 0.4331 -0.0074 0.0551  -0.0402 197 TYR C CD1   
4065  C CD2   . TYR C 196 ? 0.4958 0.4891 0.4301 -0.0046 0.0501  -0.0435 197 TYR C CD2   
4066  C CE1   . TYR C 196 ? 0.4786 0.4782 0.4192 -0.0102 0.0538  -0.0397 197 TYR C CE1   
4067  C CE2   . TYR C 196 ? 0.4736 0.4660 0.4095 -0.0073 0.0489  -0.0430 197 TYR C CE2   
4068  C CZ    . TYR C 196 ? 0.4726 0.4679 0.4114 -0.0100 0.0508  -0.0410 197 TYR C CZ    
4069  O OH    . TYR C 196 ? 0.4755 0.4696 0.4156 -0.0125 0.0497  -0.0405 197 TYR C OH    
4070  N N     . PRO C 197 ? 0.6041 0.6080 0.5328 0.0049  0.0622  -0.0418 198 PRO C N     
4071  C CA    . PRO C 197 ? 0.6116 0.6175 0.5396 0.0083  0.0638  -0.0425 198 PRO C CA    
4072  C C     . PRO C 197 ? 0.6601 0.6664 0.5918 0.0091  0.0614  -0.0439 198 PRO C C     
4073  O O     . PRO C 197 ? 0.6396 0.6459 0.5752 0.0065  0.0591  -0.0439 198 PRO C O     
4074  C CB    . PRO C 197 ? 0.6191 0.6314 0.5506 0.0074  0.0679  -0.0404 198 PRO C CB    
4075  C CG    . PRO C 197 ? 0.6342 0.6458 0.5650 0.0042  0.0689  -0.0387 198 PRO C CG    
4076  C CD    . PRO C 197 ? 0.6038 0.6116 0.5352 0.0021  0.0650  -0.0395 198 PRO C CD    
4077  N N     . LEU C 198 ? 0.6761 0.6826 0.6061 0.0127  0.0622  -0.0450 199 LEU C N     
4078  C CA    . LEU C 198 ? 0.6522 0.6582 0.5847 0.0139  0.0601  -0.0463 199 LEU C CA    
4079  C C     . LEU C 198 ? 0.6055 0.6184 0.5454 0.0124  0.0612  -0.0449 199 LEU C C     
4080  O O     . LEU C 198 ? 0.6069 0.6199 0.5502 0.0121  0.0591  -0.0454 199 LEU C O     
4081  C CB    . LEU C 198 ? 0.6667 0.6702 0.5944 0.0186  0.0606  -0.0480 199 LEU C CB    
4082  C CG    . LEU C 198 ? 0.6926 0.6889 0.6127 0.0204  0.0588  -0.0499 199 LEU C CG    
4083  C CD1   . LEU C 198 ? 0.7007 0.6943 0.6163 0.0249  0.0590  -0.0517 199 LEU C CD1   
4084  C CD2   . LEU C 198 ? 0.7099 0.7016 0.6303 0.0180  0.0547  -0.0510 199 LEU C CD2   
4085  N N     . ASP C 199 ? 0.5567 0.5752 0.4991 0.0115  0.0646  -0.0431 200 ASP C N     
4086  C CA    . ASP C 199 ? 0.5676 0.5933 0.5171 0.0102  0.0658  -0.0418 200 ASP C CA    
4087  C C     . ASP C 199 ? 0.5541 0.5816 0.5077 0.0054  0.0652  -0.0404 200 ASP C C     
4088  O O     . ASP C 199 ? 0.5287 0.5624 0.4879 0.0036  0.0666  -0.0390 200 ASP C O     
4089  C CB    . ASP C 199 ? 0.6066 0.6380 0.5570 0.0120  0.0699  -0.0408 200 ASP C CB    
4090  C CG    . ASP C 199 ? 0.6507 0.6826 0.5987 0.0105  0.0729  -0.0394 200 ASP C CG    
4091  O OD1   . ASP C 199 ? 0.6755 0.7029 0.6206 0.0082  0.0715  -0.0392 200 ASP C OD1   
4092  O OD2   . ASP C 199 ? 0.7049 0.7415 0.6536 0.0117  0.0765  -0.0384 200 ASP C OD2   
4093  N N     . HIS C 200 ? 0.5447 0.5668 0.4953 0.0036  0.0631  -0.0407 201 HIS C N     
4094  C CA    . HIS C 200 ? 0.5708 0.5938 0.5245 -0.0007 0.0624  -0.0396 201 HIS C CA    
4095  C C     . HIS C 200 ? 0.4996 0.5239 0.4582 -0.0021 0.0599  -0.0398 201 HIS C C     
4096  O O     . HIS C 200 ? 0.5127 0.5332 0.4702 -0.0009 0.0573  -0.0412 201 HIS C O     
4097  C CB    . HIS C 200 ? 0.5992 0.6161 0.5481 -0.0017 0.0610  -0.0399 201 HIS C CB    
4098  C CG    . HIS C 200 ? 0.5865 0.6037 0.5380 -0.0058 0.0604  -0.0388 201 HIS C CG    
4099  N ND1   . HIS C 200 ? 0.5959 0.6161 0.5488 -0.0081 0.0629  -0.0370 201 HIS C ND1   
4100  C CD2   . HIS C 200 ? 0.5213 0.5362 0.4744 -0.0079 0.0576  -0.0392 201 HIS C CD2   
4101  C CE1   . HIS C 200 ? 0.5386 0.5579 0.4935 -0.0114 0.0616  -0.0364 201 HIS C CE1   
4102  N NE2   . HIS C 200 ? 0.5525 0.5688 0.5075 -0.0113 0.0585  -0.0377 201 HIS C NE2   
4103  N N     . GLU C 201 ? 0.4480 0.4777 0.4121 -0.0049 0.0608  -0.0384 202 GLU C N     
4104  C CA    . GLU C 201 ? 0.5034 0.5350 0.4722 -0.0062 0.0587  -0.0385 202 GLU C CA    
4105  C C     . GLU C 201 ? 0.4543 0.4810 0.4221 -0.0086 0.0560  -0.0389 202 GLU C C     
4106  O O     . GLU C 201 ? 0.4138 0.4395 0.3812 -0.0114 0.0563  -0.0381 202 GLU C O     
4107  C CB    . GLU C 201 ? 0.5183 0.5569 0.4929 -0.0087 0.0603  -0.0370 202 GLU C CB    
4108  C CG    . GLU C 201 ? 0.5472 0.5878 0.5264 -0.0102 0.0581  -0.0369 202 GLU C CG    
4109  C CD    . GLU C 201 ? 0.5697 0.6173 0.5546 -0.0128 0.0592  -0.0356 202 GLU C CD    
4110  O OE1   . GLU C 201 ? 0.6721 0.7254 0.6598 -0.0114 0.0613  -0.0352 202 GLU C OE1   
4111  O OE2   . GLU C 201 ? 0.6415 0.6888 0.6282 -0.0163 0.0581  -0.0351 202 GLU C OE2   
4112  N N     . VAL C 202 ? 0.4399 0.4633 0.4072 -0.0075 0.0534  -0.0401 203 VAL C N     
4113  C CA    . VAL C 202 ? 0.3967 0.4160 0.3638 -0.0097 0.0509  -0.0405 203 VAL C CA    
4114  C C     . VAL C 202 ? 0.3910 0.4127 0.3625 -0.0107 0.0495  -0.0402 203 VAL C C     
4115  O O     . VAL C 202 ? 0.3497 0.3752 0.3235 -0.0091 0.0501  -0.0400 203 VAL C O     
4116  C CB    . VAL C 202 ? 0.3898 0.4028 0.3525 -0.0079 0.0490  -0.0422 203 VAL C CB    
4117  C CG1   . VAL C 202 ? 0.4108 0.4213 0.3688 -0.0067 0.0500  -0.0425 203 VAL C CG1   
4118  C CG2   . VAL C 202 ? 0.3864 0.3983 0.3487 -0.0048 0.0480  -0.0433 203 VAL C CG2   
4119  N N     . VAL C 203 ? 0.3731 0.3925 0.3454 -0.0133 0.0477  -0.0402 204 VAL C N     
4120  C CA    . VAL C 203 ? 0.3554 0.3765 0.3312 -0.0145 0.0465  -0.0398 204 VAL C CA    
4121  C C     . VAL C 203 ? 0.3704 0.3862 0.3448 -0.0146 0.0440  -0.0408 204 VAL C C     
4122  O O     . VAL C 203 ? 0.4162 0.4282 0.3888 -0.0160 0.0432  -0.0412 204 VAL C O     
4123  C CB    . VAL C 203 ? 0.3594 0.3837 0.3383 -0.0181 0.0470  -0.0386 204 VAL C CB    
4124  C CG1   . VAL C 203 ? 0.3616 0.3874 0.3436 -0.0194 0.0455  -0.0382 204 VAL C CG1   
4125  C CG2   . VAL C 203 ? 0.3609 0.3904 0.3415 -0.0185 0.0495  -0.0376 204 VAL C CG2   
4126  N N     . ILE C 204 ? 0.3681 0.3837 0.3434 -0.0130 0.0429  -0.0411 205 ILE C N     
4127  C CA    . ILE C 204 ? 0.4136 0.4246 0.3882 -0.0135 0.0408  -0.0417 205 ILE C CA    
4128  C C     . ILE C 204 ? 0.3997 0.4126 0.3772 -0.0162 0.0402  -0.0406 205 ILE C C     
4129  O O     . ILE C 204 ? 0.4253 0.4420 0.4053 -0.0157 0.0403  -0.0399 205 ILE C O     
4130  C CB    . ILE C 204 ? 0.3985 0.4074 0.3719 -0.0103 0.0400  -0.0425 205 ILE C CB    
4131  C CG1   . ILE C 204 ? 0.4118 0.4183 0.3816 -0.0076 0.0406  -0.0437 205 ILE C CG1   
4132  C CG2   . ILE C 204 ? 0.3987 0.4029 0.3716 -0.0111 0.0380  -0.0429 205 ILE C CG2   
4133  C CD1   . ILE C 204 ? 0.4449 0.4491 0.4132 -0.0041 0.0399  -0.0446 205 ILE C CD1   
4134  N N     . TYR C 205 ? 0.4034 0.4138 0.3807 -0.0188 0.0395  -0.0406 206 TYR C N     
4135  C CA    . TYR C 205 ? 0.3715 0.3833 0.3510 -0.0215 0.0391  -0.0397 206 TYR C CA    
4136  C C     . TYR C 205 ? 0.3502 0.3577 0.3290 -0.0220 0.0374  -0.0400 206 TYR C C     
4137  O O     . TYR C 205 ? 0.3905 0.3936 0.3674 -0.0220 0.0368  -0.0409 206 TYR C O     
4138  C CB    . TYR C 205 ? 0.3447 0.3571 0.3244 -0.0242 0.0399  -0.0392 206 TYR C CB    
4139  C CG    . TYR C 205 ? 0.3759 0.3886 0.3572 -0.0270 0.0393  -0.0386 206 TYR C CG    
4140  C CD1   . TYR C 205 ? 0.3778 0.3947 0.3616 -0.0279 0.0394  -0.0377 206 TYR C CD1   
4141  C CD2   . TYR C 205 ? 0.3866 0.3956 0.3670 -0.0288 0.0386  -0.0388 206 TYR C CD2   
4142  C CE1   . TYR C 205 ? 0.3552 0.3721 0.3400 -0.0304 0.0388  -0.0372 206 TYR C CE1   
4143  C CE2   . TYR C 205 ? 0.4052 0.4143 0.3867 -0.0311 0.0382  -0.0383 206 TYR C CE2   
4144  C CZ    . TYR C 205 ? 0.3632 0.3761 0.3466 -0.0319 0.0383  -0.0375 206 TYR C CZ    
4145  O OH    . TYR C 205 ? 0.4025 0.4151 0.3865 -0.0342 0.0378  -0.0370 206 TYR C OH    
4146  N N     . GLU C 206 ? 0.3247 0.3336 0.3051 -0.0226 0.0368  -0.0393 207 GLU C N     
4147  C CA    . GLU C 206 ? 0.3324 0.3375 0.3122 -0.0235 0.0356  -0.0393 207 GLU C CA    
4148  C C     . GLU C 206 ? 0.3523 0.3598 0.3338 -0.0257 0.0354  -0.0383 207 GLU C C     
4149  O O     . GLU C 206 ? 0.3296 0.3408 0.3126 -0.0251 0.0353  -0.0376 207 GLU C O     
4150  C CB    . GLU C 206 ? 0.3724 0.3752 0.3511 -0.0209 0.0347  -0.0395 207 GLU C CB    
4151  C CG    . GLU C 206 ? 0.3948 0.3944 0.3714 -0.0188 0.0346  -0.0408 207 GLU C CG    
4152  C CD    . GLU C 206 ? 0.4488 0.4456 0.4240 -0.0161 0.0338  -0.0411 207 GLU C CD    
4153  O OE1   . GLU C 206 ? 0.4695 0.4668 0.4453 -0.0158 0.0333  -0.0402 207 GLU C OE1   
4154  O OE2   . GLU C 206 ? 0.4773 0.4710 0.4505 -0.0143 0.0337  -0.0422 207 GLU C OE2   
4155  N N     . ALA C 207 ? 0.3532 0.3586 0.3344 -0.0283 0.0353  -0.0382 208 ALA C N     
4156  C CA    . ALA C 207 ? 0.3694 0.3762 0.3515 -0.0305 0.0351  -0.0374 208 ALA C CA    
4157  C C     . ALA C 207 ? 0.3447 0.3496 0.3262 -0.0299 0.0340  -0.0370 208 ALA C C     
4158  O O     . ALA C 207 ? 0.3664 0.3672 0.3465 -0.0290 0.0336  -0.0373 208 ALA C O     
4159  C CB    . ALA C 207 ? 0.3917 0.3964 0.3734 -0.0329 0.0355  -0.0375 208 ALA C CB    
4160  N N     . ALA C 208 ? 0.3156 0.3235 0.2981 -0.0304 0.0336  -0.0362 209 ALA C N     
4161  C CA    . ALA C 208 ? 0.3300 0.3363 0.3115 -0.0297 0.0325  -0.0357 209 ALA C CA    
4162  C C     . ALA C 208 ? 0.3542 0.3560 0.3340 -0.0317 0.0324  -0.0355 209 ALA C C     
4163  O O     . ALA C 208 ? 0.3628 0.3644 0.3428 -0.0339 0.0331  -0.0357 209 ALA C O     
4164  C CB    . ALA C 208 ? 0.3314 0.3423 0.3144 -0.0297 0.0318  -0.0350 209 ALA C CB    
4165  N N     . ASN C 209 ? 0.3422 0.3404 0.3202 -0.0307 0.0318  -0.0352 210 ASN C N     
4166  C CA    . ASN C 209 ? 0.3297 0.3237 0.3062 -0.0324 0.0320  -0.0349 210 ASN C CA    
4167  C C     . ASN C 209 ? 0.3093 0.3035 0.2845 -0.0328 0.0313  -0.0339 210 ASN C C     
4168  O O     . ASN C 209 ? 0.3153 0.3069 0.2891 -0.0345 0.0316  -0.0336 210 ASN C O     
4169  C CB    . ASN C 209 ? 0.3593 0.3482 0.3343 -0.0315 0.0320  -0.0352 210 ASN C CB    
4170  C CG    . ASN C 209 ? 0.3706 0.3591 0.3466 -0.0312 0.0324  -0.0363 210 ASN C CG    
4171  O OD1   . ASN C 209 ? 0.3867 0.3758 0.3636 -0.0329 0.0331  -0.0368 210 ASN C OD1   
4172  N ND2   . ASN C 209 ? 0.4001 0.3874 0.3755 -0.0289 0.0320  -0.0368 210 ASN C ND2   
4173  N N     . LEU C 210 ? 0.3118 0.3092 0.2875 -0.0311 0.0303  -0.0335 211 LEU C N     
4174  C CA    . LEU C 210 ? 0.3483 0.3464 0.3228 -0.0311 0.0292  -0.0327 211 LEU C CA    
4175  C C     . LEU C 210 ? 0.3576 0.3616 0.3342 -0.0319 0.0287  -0.0327 211 LEU C C     
4176  O O     . LEU C 210 ? 0.3569 0.3649 0.3361 -0.0314 0.0291  -0.0332 211 LEU C O     
4177  C CB    . LEU C 210 ? 0.3293 0.3257 0.3022 -0.0282 0.0282  -0.0321 211 LEU C CB    
4178  C CG    . LEU C 210 ? 0.3621 0.3519 0.3325 -0.0276 0.0287  -0.0320 211 LEU C CG    
4179  C CD1   . LEU C 210 ? 0.3974 0.3852 0.3659 -0.0246 0.0276  -0.0313 211 LEU C CD1   
4180  C CD2   . LEU C 210 ? 0.3799 0.3659 0.3484 -0.0300 0.0294  -0.0316 211 LEU C CD2   
4181  N N     . PRO C 211 ? 0.3968 0.4015 0.3724 -0.0331 0.0279  -0.0323 212 PRO C N     
4182  C CA    . PRO C 211 ? 0.4369 0.4470 0.4147 -0.0343 0.0273  -0.0325 212 PRO C CA    
4183  C C     . PRO C 211 ? 0.4793 0.4944 0.4590 -0.0321 0.0259  -0.0323 212 PRO C C     
4184  O O     . PRO C 211 ? 0.5758 0.5961 0.5581 -0.0331 0.0254  -0.0325 212 PRO C O     
4185  C CB    . PRO C 211 ? 0.4151 0.4229 0.3902 -0.0363 0.0268  -0.0322 212 PRO C CB    
4186  C CG    . PRO C 211 ? 0.4281 0.4310 0.3998 -0.0347 0.0265  -0.0314 212 PRO C CG    
4187  C CD    . PRO C 211 ? 0.4441 0.4442 0.4162 -0.0335 0.0276  -0.0316 212 PRO C CD    
4188  N N     . ILE C 212 ? 0.5135 0.5269 0.4922 -0.0292 0.0254  -0.0319 213 ILE C N     
4189  C CA    . ILE C 212 ? 0.4928 0.5107 0.4733 -0.0265 0.0241  -0.0317 213 ILE C CA    
4190  C C     . ILE C 212 ? 0.5151 0.5344 0.4977 -0.0245 0.0251  -0.0321 213 ILE C C     
4191  O O     . ILE C 212 ? 0.4955 0.5187 0.4800 -0.0219 0.0245  -0.0321 213 ILE C O     
4192  C CB    . ILE C 212 ? 0.4912 0.5060 0.4686 -0.0241 0.0226  -0.0308 213 ILE C CB    
4193  C CG1   . ILE C 212 ? 0.5217 0.5293 0.4958 -0.0231 0.0235  -0.0305 213 ILE C CG1   
4194  C CG2   . ILE C 212 ? 0.4886 0.5030 0.4639 -0.0258 0.0213  -0.0303 213 ILE C CG2   
4195  C CD1   . ILE C 212 ? 0.5192 0.5265 0.4947 -0.0212 0.0244  -0.0311 213 ILE C CD1   
4196  N N     . GLN C 213 ? 0.5362 0.5525 0.5184 -0.0257 0.0267  -0.0327 214 GLN C N     
4197  C CA    . GLN C 213 ? 0.5148 0.5313 0.4981 -0.0239 0.0278  -0.0332 214 GLN C CA    
4198  C C     . GLN C 213 ? 0.5000 0.5212 0.4863 -0.0254 0.0290  -0.0337 214 GLN C C     
4199  O O     . GLN C 213 ? 0.5840 0.6046 0.5703 -0.0283 0.0297  -0.0339 214 GLN C O     
4200  C CB    . GLN C 213 ? 0.5496 0.5593 0.5301 -0.0240 0.0285  -0.0335 214 GLN C CB    
4201  C CG    . GLN C 213 ? 0.6256 0.6348 0.6066 -0.0222 0.0294  -0.0343 214 GLN C CG    
4202  C CD    . GLN C 213 ? 0.6439 0.6471 0.6228 -0.0231 0.0301  -0.0348 214 GLN C CD    
4203  O OE1   . GLN C 213 ? 0.6936 0.6933 0.6710 -0.0252 0.0301  -0.0346 214 GLN C OE1   
4204  N NE2   . GLN C 213 ? 0.6819 0.6839 0.6607 -0.0215 0.0306  -0.0356 214 GLN C NE2   
4205  N N     . ALA C 214 ? 0.5005 0.5261 0.4891 -0.0233 0.0293  -0.0339 215 ALA C N     
4206  C CA    . ALA C 214 ? 0.4809 0.5107 0.4722 -0.0243 0.0308  -0.0343 215 ALA C CA    
4207  C C     . ALA C 214 ? 0.4289 0.4546 0.4185 -0.0239 0.0321  -0.0350 215 ALA C C     
4208  O O     . ALA C 214 ? 0.4037 0.4252 0.3911 -0.0218 0.0319  -0.0352 215 ALA C O     
4209  C CB    . ALA C 214 ? 0.5223 0.5586 0.5169 -0.0222 0.0308  -0.0342 215 ALA C CB    
4210  N N     . PRO C 215 ? 0.4724 0.4989 0.4626 -0.0260 0.0335  -0.0353 216 PRO C N     
4211  C CA    . PRO C 215 ? 0.4697 0.4926 0.4581 -0.0255 0.0346  -0.0359 216 PRO C CA    
4212  C C     . PRO C 215 ? 0.4181 0.4429 0.4070 -0.0223 0.0353  -0.0363 216 PRO C C     
4213  O O     . PRO C 215 ? 0.4373 0.4672 0.4286 -0.0210 0.0354  -0.0360 216 PRO C O     
4214  C CB    . PRO C 215 ? 0.4489 0.4730 0.4381 -0.0284 0.0358  -0.0359 216 PRO C CB    
4215  C CG    . PRO C 215 ? 0.4561 0.4862 0.4484 -0.0296 0.0358  -0.0353 216 PRO C CG    
4216  C CD    . PRO C 215 ? 0.4926 0.5232 0.4851 -0.0288 0.0340  -0.0350 216 PRO C CD    
4217  N N     . ARG C 216 ? 0.4125 0.4330 0.3990 -0.0211 0.0357  -0.0370 217 ARG C N     
4218  C CA    . ARG C 216 ? 0.4455 0.4669 0.4316 -0.0181 0.0365  -0.0376 217 ARG C CA    
4219  C C     . ARG C 216 ? 0.4014 0.4250 0.3880 -0.0191 0.0382  -0.0377 217 ARG C C     
4220  O O     . ARG C 216 ? 0.3517 0.3721 0.3366 -0.0208 0.0385  -0.0381 217 ARG C O     
4221  C CB    . ARG C 216 ? 0.4509 0.4661 0.4339 -0.0162 0.0358  -0.0384 217 ARG C CB    
4222  C CG    . ARG C 216 ? 0.5251 0.5406 0.5071 -0.0129 0.0366  -0.0392 217 ARG C CG    
4223  C CD    . ARG C 216 ? 0.5334 0.5423 0.5120 -0.0113 0.0358  -0.0402 217 ARG C CD    
4224  N NE    . ARG C 216 ? 0.5784 0.5872 0.5556 -0.0078 0.0365  -0.0410 217 ARG C NE    
4225  C CZ    . ARG C 216 ? 0.6224 0.6258 0.5965 -0.0060 0.0359  -0.0422 217 ARG C CZ    
4226  N NH1   . ARG C 216 ? 0.6184 0.6162 0.5908 -0.0075 0.0347  -0.0426 217 ARG C NH1   
4227  N NH2   . ARG C 216 ? 0.5831 0.5867 0.5558 -0.0027 0.0366  -0.0429 217 ARG C NH2   
4228  N N     . ILE C 217 ? 0.4296 0.4588 0.4185 -0.0179 0.0394  -0.0374 218 ILE C N     
4229  C CA    . ILE C 217 ? 0.4994 0.5308 0.4885 -0.0186 0.0414  -0.0374 218 ILE C CA    
4230  C C     . ILE C 217 ? 0.5288 0.5631 0.5182 -0.0152 0.0426  -0.0377 218 ILE C C     
4231  O O     . ILE C 217 ? 0.5696 0.6101 0.5623 -0.0148 0.0436  -0.0371 218 ILE C O     
4232  C CB    . ILE C 217 ? 0.5048 0.5409 0.4969 -0.0218 0.0420  -0.0365 218 ILE C CB    
4233  C CG1   . ILE C 217 ? 0.5201 0.5534 0.5118 -0.0248 0.0408  -0.0363 218 ILE C CG1   
4234  C CG2   . ILE C 217 ? 0.5162 0.5539 0.5082 -0.0226 0.0443  -0.0363 218 ILE C CG2   
4235  C CD1   . ILE C 217 ? 0.5493 0.5864 0.5436 -0.0280 0.0413  -0.0356 218 ILE C CD1   
4236  N N     . GLU C 218 ? 0.5290 0.5588 0.5151 -0.0127 0.0425  -0.0386 219 GLU C N     
4237  C CA    . GLU C 218 ? 0.5541 0.5854 0.5395 -0.0091 0.0436  -0.0391 219 GLU C CA    
4238  C C     . GLU C 218 ? 0.5121 0.5438 0.4959 -0.0091 0.0457  -0.0392 219 GLU C C     
4239  O O     . GLU C 218 ? 0.5099 0.5366 0.4903 -0.0097 0.0454  -0.0399 219 GLU C O     
4240  C CB    . GLU C 218 ? 0.6000 0.6258 0.5823 -0.0062 0.0422  -0.0401 219 GLU C CB    
4241  C CG    . GLU C 218 ? 0.6522 0.6790 0.6333 -0.0021 0.0433  -0.0408 219 GLU C CG    
4242  C CD    . GLU C 218 ? 0.6607 0.6815 0.6385 0.0008  0.0419  -0.0419 219 GLU C CD    
4243  O OE1   . GLU C 218 ? 0.7034 0.7193 0.6800 -0.0006 0.0401  -0.0421 219 GLU C OE1   
4244  O OE2   . GLU C 218 ? 0.7804 0.8014 0.7569 0.0044  0.0427  -0.0425 219 GLU C OE2   
4245  N N     . ARG C 219 ? 0.5000 0.5377 0.4862 -0.0084 0.0477  -0.0386 220 ARG C N     
4246  C CA    . ARG C 219 ? 0.5041 0.5424 0.4886 -0.0080 0.0500  -0.0386 220 ARG C CA    
4247  C C     . ARG C 219 ? 0.5005 0.5382 0.4827 -0.0036 0.0509  -0.0395 220 ARG C C     
4248  O O     . ARG C 219 ? 0.5330 0.5736 0.5172 -0.0011 0.0508  -0.0396 220 ARG C O     
4249  C CB    . ARG C 219 ? 0.4807 0.5259 0.4692 -0.0101 0.0521  -0.0374 220 ARG C CB    
4250  C CG    . ARG C 219 ? 0.5030 0.5488 0.4936 -0.0144 0.0513  -0.0366 220 ARG C CG    
4251  C CD    . ARG C 219 ? 0.5365 0.5894 0.5316 -0.0165 0.0531  -0.0354 220 ARG C CD    
4252  N NE    . ARG C 219 ? 0.5672 0.6201 0.5640 -0.0206 0.0523  -0.0348 220 ARG C NE    
4253  C CZ    . ARG C 219 ? 0.6338 0.6826 0.6281 -0.0231 0.0524  -0.0347 220 ARG C CZ    
4254  N NH1   . ARG C 219 ? 0.6616 0.7062 0.6517 -0.0220 0.0534  -0.0350 220 ARG C NH1   
4255  N NH2   . ARG C 219 ? 0.5862 0.6350 0.5820 -0.0266 0.0516  -0.0342 220 ARG C NH2   
4256  N N     . LEU C 220 ? 0.4792 0.5126 0.4567 -0.0026 0.0516  -0.0403 221 LEU C N     
4257  C CA    . LEU C 220 ? 0.4652 0.4971 0.4397 0.0016  0.0525  -0.0413 221 LEU C CA    
4258  C C     . LEU C 220 ? 0.4630 0.4917 0.4328 0.0019  0.0538  -0.0417 221 LEU C C     
4259  O O     . LEU C 220 ? 0.4478 0.4738 0.4162 -0.0008 0.0533  -0.0415 221 LEU C O     
4260  C CB    . LEU C 220 ? 0.4775 0.5041 0.4498 0.0037  0.0500  -0.0425 221 LEU C CB    
4261  C CG    . LEU C 220 ? 0.4806 0.4998 0.4492 0.0023  0.0479  -0.0435 221 LEU C CG    
4262  C CD1   . LEU C 220 ? 0.5058 0.5199 0.4725 0.0043  0.0458  -0.0448 221 LEU C CD1   
4263  C CD2   . LEU C 220 ? 0.4752 0.4946 0.4460 -0.0020 0.0470  -0.0427 221 LEU C CD2   
4264  N N     . PRO C 221 ? 0.5106 0.5394 0.4776 0.0054  0.0555  -0.0423 222 PRO C N     
4265  C CA    . PRO C 221 ? 0.5279 0.5529 0.4896 0.0062  0.0566  -0.0429 222 PRO C CA    
4266  C C     . PRO C 221 ? 0.5282 0.5454 0.4854 0.0063  0.0538  -0.0445 222 PRO C C     
4267  O O     . PRO C 221 ? 0.5595 0.5737 0.5165 0.0075  0.0517  -0.0455 222 PRO C O     
4268  C CB    . PRO C 221 ? 0.5403 0.5676 0.5004 0.0103  0.0590  -0.0433 222 PRO C CB    
4269  C CG    . PRO C 221 ? 0.5441 0.5733 0.5072 0.0125  0.0580  -0.0437 222 PRO C CG    
4270  C CD    . PRO C 221 ? 0.5029 0.5353 0.4715 0.0090  0.0566  -0.0426 222 PRO C CD    
4271  N N     . LEU C 222 ? 0.5352 0.5492 0.4888 0.0051  0.0539  -0.0446 223 LEU C N     
4272  C CA    . LEU C 222 ? 0.5444 0.5515 0.4941 0.0049  0.0512  -0.0460 223 LEU C CA    
4273  C C     . LEU C 222 ? 0.5387 0.5416 0.4848 0.0085  0.0501  -0.0480 223 LEU C C     
4274  O O     . LEU C 222 ? 0.6026 0.6003 0.5471 0.0083  0.0474  -0.0493 223 LEU C O     
4275  C CB    . LEU C 222 ? 0.5849 0.5900 0.5309 0.0040  0.0519  -0.0458 223 LEU C CB    
4276  C CG    . LEU C 222 ? 0.6116 0.6101 0.5535 0.0039  0.0491  -0.0475 223 LEU C CG    
4277  C CD1   . LEU C 222 ? 0.6239 0.6212 0.5691 0.0007  0.0466  -0.0474 223 LEU C CD1   
4278  C CD2   . LEU C 222 ? 0.6193 0.6160 0.5568 0.0039  0.0500  -0.0473 223 LEU C CD2   
4279  N N     . ALA C 223 ? 0.5511 0.5562 0.4959 0.0118  0.0522  -0.0481 224 ALA C N     
4280  C CA    . ALA C 223 ? 0.5071 0.5080 0.4476 0.0157  0.0516  -0.0500 224 ALA C CA    
4281  C C     . ALA C 223 ? 0.4799 0.4794 0.4227 0.0164  0.0496  -0.0506 224 ALA C C     
4282  O O     . ALA C 223 ? 0.4256 0.4194 0.3649 0.0184  0.0478  -0.0524 224 ALA C O     
4283  C CB    . ALA C 223 ? 0.5425 0.5466 0.4813 0.0191  0.0548  -0.0497 224 ALA C CB    
4284  N N     . ASN C 224 ? 0.4580 0.4624 0.4065 0.0148  0.0498  -0.0491 225 ASN C N     
4285  C CA    . ASN C 224 ? 0.4482 0.4520 0.3990 0.0158  0.0483  -0.0494 225 ASN C CA    
4286  C C     . ASN C 224 ? 0.4610 0.4606 0.4126 0.0127  0.0454  -0.0497 225 ASN C C     
4287  O O     . ASN C 224 ? 0.4451 0.4432 0.3982 0.0129  0.0440  -0.0497 225 ASN C O     
4288  C CB    . ASN C 224 ? 0.4591 0.4703 0.4154 0.0160  0.0499  -0.0478 225 ASN C CB    
4289  C CG    . ASN C 224 ? 0.4684 0.4838 0.4243 0.0196  0.0527  -0.0477 225 ASN C CG    
4290  O OD1   . ASN C 224 ? 0.5250 0.5373 0.4760 0.0221  0.0536  -0.0489 225 ASN C OD1   
4291  N ND2   . ASN C 224 ? 0.4590 0.4817 0.4201 0.0199  0.0541  -0.0464 225 ASN C ND2   
4292  N N     . LEU C 225 ? 0.5110 0.5086 0.4614 0.0099  0.0447  -0.0497 226 LEU C N     
4293  C CA    . LEU C 225 ? 0.5081 0.5023 0.4596 0.0068  0.0423  -0.0499 226 LEU C CA    
4294  C C     . LEU C 225 ? 0.5587 0.5467 0.5078 0.0083  0.0401  -0.0515 226 LEU C C     
4295  O O     . LEU C 225 ? 0.5747 0.5614 0.5260 0.0071  0.0387  -0.0512 226 LEU C O     
4296  C CB    . LEU C 225 ? 0.5385 0.5311 0.4883 0.0045  0.0419  -0.0500 226 LEU C CB    
4297  C CG    . LEU C 225 ? 0.5187 0.5080 0.4697 0.0013  0.0396  -0.0503 226 LEU C CG    
4298  C CD1   . LEU C 225 ? 0.5322 0.5252 0.4882 -0.0014 0.0397  -0.0486 226 LEU C CD1   
4299  C CD2   . LEU C 225 ? 0.5004 0.4879 0.4492 -0.0002 0.0391  -0.0507 226 LEU C CD2   
4300  N N     . PRO C 226 ? 0.5632 0.5469 0.5075 0.0110  0.0398  -0.0533 227 PRO C N     
4301  C CA    . PRO C 226 ? 0.5582 0.5352 0.4998 0.0122  0.0376  -0.0551 227 PRO C CA    
4302  C C     . PRO C 226 ? 0.5494 0.5261 0.4927 0.0137  0.0374  -0.0548 227 PRO C C     
4303  O O     . PRO C 226 ? 0.5825 0.5537 0.5248 0.0135  0.0354  -0.0557 227 PRO C O     
4304  C CB    . PRO C 226 ? 0.5629 0.5367 0.4989 0.0155  0.0380  -0.0569 227 PRO C CB    
4305  C CG    . PRO C 226 ? 0.5622 0.5397 0.4976 0.0147  0.0397  -0.0561 227 PRO C CG    
4306  C CD    . PRO C 226 ? 0.5705 0.5551 0.5113 0.0130  0.0416  -0.0537 227 PRO C CD    
4307  N N     . GLN C 227 ? 0.6017 0.5842 0.5476 0.0154  0.0393  -0.0534 228 GLN C N     
4308  C CA    . GLN C 227 ? 0.6105 0.5933 0.5579 0.0175  0.0392  -0.0530 228 GLN C CA    
4309  C C     . GLN C 227 ? 0.5186 0.5052 0.4710 0.0146  0.0388  -0.0511 228 GLN C C     
4310  O O     . GLN C 227 ? 0.4752 0.4625 0.4293 0.0159  0.0384  -0.0505 228 GLN C O     
4311  C CB    . GLN C 227 ? 0.6539 0.6410 0.6011 0.0215  0.0414  -0.0528 228 GLN C CB    
4312  C CG    . GLN C 227 ? 0.7407 0.7233 0.6823 0.0252  0.0418  -0.0548 228 GLN C CG    
4313  C CD    . GLN C 227 ? 0.7980 0.7803 0.7368 0.0243  0.0426  -0.0554 228 GLN C CD    
4314  O OE1   . GLN C 227 ? 0.8608 0.8490 0.8014 0.0236  0.0447  -0.0542 228 GLN C OE1   
4315  N NE2   . GLN C 227 ? 0.8472 0.8225 0.7813 0.0244  0.0408  -0.0573 228 GLN C NE2   
4316  N N     . ALA C 228 ? 0.5063 0.4953 0.4609 0.0108  0.0388  -0.0503 229 ALA C N     
4317  C CA    . ALA C 228 ? 0.5133 0.5062 0.4724 0.0080  0.0386  -0.0485 229 ALA C CA    
4318  C C     . ALA C 228 ? 0.5032 0.4908 0.4621 0.0063  0.0365  -0.0487 229 ALA C C     
4319  O O     . ALA C 228 ? 0.4984 0.4801 0.4546 0.0057  0.0351  -0.0501 229 ALA C O     
4320  C CB    . ALA C 228 ? 0.5453 0.5419 0.5062 0.0048  0.0395  -0.0477 229 ALA C CB    
4321  N N     . HIS C 229 ? 0.5034 0.4934 0.4653 0.0055  0.0361  -0.0474 230 HIS C N     
4322  C CA    . HIS C 229 ? 0.5427 0.5283 0.5047 0.0037  0.0344  -0.0471 230 HIS C CA    
4323  C C     . HIS C 229 ? 0.4936 0.4796 0.4573 -0.0006 0.0341  -0.0466 230 HIS C C     
4324  O O     . HIS C 229 ? 0.5305 0.5216 0.4972 -0.0025 0.0347  -0.0453 230 HIS C O     
4325  C CB    . HIS C 229 ? 0.6163 0.6041 0.5803 0.0049  0.0342  -0.0459 230 HIS C CB    
4326  C CG    . HIS C 229 ? 0.7417 0.7245 0.7051 0.0035  0.0326  -0.0455 230 HIS C CG    
4327  N ND1   . HIS C 229 ? 0.7847 0.7616 0.7453 0.0057  0.0317  -0.0461 230 HIS C ND1   
4328  C CD2   . HIS C 229 ? 0.7809 0.7635 0.7458 0.0001  0.0320  -0.0445 230 HIS C CD2   
4329  C CE1   . HIS C 229 ? 0.8382 0.8115 0.7988 0.0036  0.0306  -0.0454 230 HIS C CE1   
4330  N NE2   . HIS C 229 ? 0.8267 0.8035 0.7899 0.0002  0.0308  -0.0445 230 HIS C NE2   
4331  N N     . LEU C 230 ? 0.4600 0.4406 0.4217 -0.0022 0.0330  -0.0477 231 LEU C N     
4332  C CA    . LEU C 230 ? 0.4352 0.4160 0.3984 -0.0059 0.0326  -0.0474 231 LEU C CA    
4333  C C     . LEU C 230 ? 0.4410 0.4179 0.4047 -0.0080 0.0314  -0.0471 231 LEU C C     
4334  O O     . LEU C 230 ? 0.4687 0.4406 0.4305 -0.0067 0.0305  -0.0478 231 LEU C O     
4335  C CB    . LEU C 230 ? 0.4172 0.3958 0.3783 -0.0063 0.0324  -0.0489 231 LEU C CB    
4336  C CG    . LEU C 230 ? 0.4451 0.4271 0.4051 -0.0044 0.0338  -0.0491 231 LEU C CG    
4337  C CD1   . LEU C 230 ? 0.4312 0.4105 0.3887 -0.0048 0.0332  -0.0506 231 LEU C CD1   
4338  C CD2   . LEU C 230 ? 0.4176 0.4061 0.3806 -0.0058 0.0353  -0.0475 231 LEU C CD2   
4339  N N     . MET C 231 ? 0.4453 0.4242 0.4114 -0.0111 0.0315  -0.0461 232 MET C N     
4340  C CA    . MET C 231 ? 0.4631 0.4386 0.4297 -0.0133 0.0306  -0.0457 232 MET C CA    
4341  C C     . MET C 231 ? 0.4539 0.4290 0.4216 -0.0164 0.0305  -0.0461 232 MET C C     
4342  O O     . MET C 231 ? 0.4362 0.4144 0.4044 -0.0170 0.0311  -0.0461 232 MET C O     
4343  C CB    . MET C 231 ? 0.4939 0.4722 0.4623 -0.0140 0.0309  -0.0439 232 MET C CB    
4344  C CG    . MET C 231 ? 0.5336 0.5121 0.5013 -0.0108 0.0308  -0.0434 232 MET C CG    
4345  S SD    . MET C 231 ? 0.6530 0.6235 0.6173 -0.0091 0.0298  -0.0444 232 MET C SD    
4346  C CE    . MET C 231 ? 0.7843 0.7508 0.7492 -0.0129 0.0292  -0.0438 232 MET C CE    
4347  N N     . PRO C 232 ? 0.4654 0.4364 0.4332 -0.0185 0.0297  -0.0462 233 PRO C N     
4348  C CA    . PRO C 232 ? 0.4723 0.4431 0.4415 -0.0212 0.0295  -0.0467 233 PRO C CA    
4349  C C     . PRO C 232 ? 0.4895 0.4651 0.4606 -0.0228 0.0304  -0.0457 233 PRO C C     
4350  O O     . PRO C 232 ? 0.5861 0.5626 0.5578 -0.0241 0.0304  -0.0462 233 PRO C O     
4351  C CB    . PRO C 232 ? 0.4644 0.4311 0.4341 -0.0231 0.0290  -0.0464 233 PRO C CB    
4352  C CG    . PRO C 232 ? 0.4800 0.4428 0.4474 -0.0209 0.0285  -0.0467 233 PRO C CG    
4353  C CD    . PRO C 232 ? 0.4822 0.4487 0.4490 -0.0181 0.0291  -0.0460 233 PRO C CD    
4354  N N     . ILE C 233 ? 0.4263 0.4050 0.3983 -0.0227 0.0311  -0.0442 234 ILE C N     
4355  C CA    . ILE C 233 ? 0.4061 0.3888 0.3798 -0.0245 0.0319  -0.0432 234 ILE C CA    
4356  C C     . ILE C 233 ? 0.4004 0.3874 0.3742 -0.0232 0.0328  -0.0431 234 ILE C C     
4357  O O     . ILE C 233 ? 0.3829 0.3735 0.3581 -0.0245 0.0336  -0.0422 234 ILE C O     
4358  C CB    . ILE C 233 ? 0.3849 0.3686 0.3596 -0.0254 0.0321  -0.0418 234 ILE C CB    
4359  C CG1   . ILE C 233 ? 0.3746 0.3600 0.3488 -0.0230 0.0321  -0.0412 234 ILE C CG1   
4360  C CG2   . ILE C 233 ? 0.4020 0.3813 0.3764 -0.0269 0.0316  -0.0417 234 ILE C CG2   
4361  C CD1   . ILE C 233 ? 0.3646 0.3513 0.3394 -0.0236 0.0320  -0.0398 234 ILE C CD1   
4362  N N     . SER C 234 ? 0.3770 0.3633 0.3492 -0.0208 0.0327  -0.0441 235 SER C N     
4363  C CA    . SER C 234 ? 0.3726 0.3628 0.3447 -0.0193 0.0338  -0.0439 235 SER C CA    
4364  C C     . SER C 234 ? 0.3688 0.3595 0.3403 -0.0203 0.0342  -0.0444 235 SER C C     
4365  O O     . SER C 234 ? 0.3867 0.3741 0.3568 -0.0204 0.0333  -0.0455 235 SER C O     
4366  C CB    . SER C 234 ? 0.3681 0.3574 0.3383 -0.0160 0.0338  -0.0447 235 SER C CB    
4367  O OG    . SER C 234 ? 0.3195 0.3093 0.2903 -0.0148 0.0336  -0.0440 235 SER C OG    
4368  N N     . THR C 235 ? 0.3756 0.3703 0.3481 -0.0211 0.0354  -0.0434 236 THR C N     
4369  C CA    . THR C 235 ? 0.3664 0.3616 0.3379 -0.0217 0.0361  -0.0436 236 THR C CA    
4370  C C     . THR C 235 ? 0.3823 0.3805 0.3529 -0.0197 0.0375  -0.0434 236 THR C C     
4371  O O     . THR C 235 ? 0.4005 0.4022 0.3726 -0.0190 0.0383  -0.0426 236 THR C O     
4372  C CB    . THR C 235 ? 0.3737 0.3705 0.3469 -0.0245 0.0365  -0.0426 236 THR C CB    
4373  O OG1   . THR C 235 ? 0.3621 0.3560 0.3360 -0.0260 0.0353  -0.0430 236 THR C OG1   
4374  C CG2   . THR C 235 ? 0.3779 0.3752 0.3499 -0.0250 0.0373  -0.0426 236 THR C CG2   
4375  N N     . LEU C 236 ? 0.4026 0.3996 0.3707 -0.0187 0.0378  -0.0441 237 LEU C N     
4376  C CA    . LEU C 236 ? 0.4275 0.4268 0.3941 -0.0167 0.0393  -0.0439 237 LEU C CA    
4377  C C     . LEU C 236 ? 0.4003 0.4018 0.3670 -0.0183 0.0408  -0.0429 237 LEU C C     
4378  O O     . LEU C 236 ? 0.3951 0.3942 0.3602 -0.0192 0.0403  -0.0432 237 LEU C O     
4379  C CB    . LEU C 236 ? 0.4443 0.4401 0.4073 -0.0141 0.0387  -0.0455 237 LEU C CB    
4380  C CG    . LEU C 236 ? 0.4797 0.4772 0.4402 -0.0117 0.0405  -0.0454 237 LEU C CG    
4381  C CD1   . LEU C 236 ? 0.4635 0.4644 0.4256 -0.0100 0.0417  -0.0449 237 LEU C CD1   
4382  C CD2   . LEU C 236 ? 0.5152 0.5085 0.4714 -0.0095 0.0395  -0.0471 237 LEU C CD2   
4383  N N     . LEU C 237 ? 0.4140 0.4200 0.3826 -0.0186 0.0426  -0.0417 238 LEU C N     
4384  C CA    A LEU C 237 ? 0.3772 0.3853 0.3458 -0.0202 0.0443  -0.0406 238 LEU C CA    
4385  C CA    B LEU C 237 ? 0.3931 0.4011 0.3616 -0.0202 0.0442  -0.0406 238 LEU C CA    
4386  C C     . LEU C 237 ? 0.3852 0.3945 0.3514 -0.0180 0.0461  -0.0405 238 LEU C C     
4387  O O     . LEU C 237 ? 0.3859 0.3977 0.3528 -0.0161 0.0470  -0.0406 238 LEU C O     
4388  C CB    A LEU C 237 ? 0.3840 0.3962 0.3564 -0.0225 0.0450  -0.0394 238 LEU C CB    
4389  C CB    B LEU C 237 ? 0.4017 0.4138 0.3741 -0.0225 0.0450  -0.0394 238 LEU C CB    
4390  C CG    A LEU C 237 ? 0.3984 0.4132 0.3713 -0.0243 0.0470  -0.0381 238 LEU C CG    
4391  C CG    B LEU C 237 ? 0.4157 0.4294 0.3885 -0.0249 0.0465  -0.0382 238 LEU C CG    
4392  C CD1   A LEU C 237 ? 0.4008 0.4123 0.3719 -0.0262 0.0467  -0.0380 238 LEU C CD1   
4393  C CD1   B LEU C 237 ? 0.4313 0.4494 0.4079 -0.0270 0.0471  -0.0372 238 LEU C CD1   
4394  C CD2   A LEU C 237 ? 0.4366 0.4562 0.4136 -0.0261 0.0476  -0.0372 238 LEU C CD2   
4395  C CD2   B LEU C 237 ? 0.4198 0.4342 0.3901 -0.0235 0.0485  -0.0379 238 LEU C CD2   
4396  N N     . ILE C 238 ? 0.3958 0.4032 0.3590 -0.0182 0.0468  -0.0404 239 ILE C N     
4397  C CA    . ILE C 238 ? 0.3876 0.3956 0.3479 -0.0162 0.0488  -0.0402 239 ILE C CA    
4398  C C     . ILE C 238 ? 0.3875 0.3974 0.3480 -0.0183 0.0509  -0.0386 239 ILE C C     
4399  O O     . ILE C 238 ? 0.3830 0.3899 0.3409 -0.0192 0.0508  -0.0385 239 ILE C O     
4400  C CB    . ILE C 238 ? 0.3877 0.3909 0.3431 -0.0140 0.0476  -0.0416 239 ILE C CB    
4401  C CG1   . ILE C 238 ? 0.3856 0.3865 0.3408 -0.0122 0.0455  -0.0432 239 ILE C CG1   
4402  C CG2   . ILE C 238 ? 0.4170 0.4205 0.3686 -0.0119 0.0498  -0.0413 239 ILE C CG2   
4403  C CD1   . ILE C 238 ? 0.4091 0.4053 0.3597 -0.0101 0.0440  -0.0449 239 ILE C CD1   
4404  N N     . PRO C 239 ? 0.3893 0.4042 0.3530 -0.0193 0.0529  -0.0375 240 PRO C N     
4405  C CA    . PRO C 239 ? 0.4084 0.4252 0.3726 -0.0216 0.0551  -0.0359 240 PRO C CA    
4406  C C     . PRO C 239 ? 0.4091 0.4233 0.3684 -0.0204 0.0567  -0.0356 240 PRO C C     
4407  O O     . PRO C 239 ? 0.4535 0.4653 0.4091 -0.0175 0.0564  -0.0365 240 PRO C O     
4408  C CB    . PRO C 239 ? 0.4391 0.4622 0.4077 -0.0220 0.0569  -0.0351 240 PRO C CB    
4409  C CG    . PRO C 239 ? 0.4261 0.4503 0.3973 -0.0208 0.0548  -0.0361 240 PRO C CG    
4410  C CD    . PRO C 239 ? 0.4059 0.4250 0.3730 -0.0181 0.0532  -0.0376 240 PRO C CD    
4411  N N     . PRO C 240 ? 0.4158 0.4300 0.3745 -0.0226 0.0585  -0.0342 241 PRO C N     
4412  C CA    . PRO C 240 ? 0.4606 0.4718 0.4141 -0.0216 0.0602  -0.0336 241 PRO C CA    
4413  C C     . PRO C 240 ? 0.4771 0.4905 0.4289 -0.0189 0.0625  -0.0335 241 PRO C C     
4414  O O     . PRO C 240 ? 0.4545 0.4732 0.4101 -0.0193 0.0643  -0.0328 241 PRO C O     
4415  C CB    . PRO C 240 ? 0.4396 0.4513 0.3941 -0.0249 0.0620  -0.0319 241 PRO C CB    
4416  C CG    . PRO C 240 ? 0.4112 0.4242 0.3703 -0.0276 0.0601  -0.0321 241 PRO C CG    
4417  C CD    . PRO C 240 ? 0.4306 0.4470 0.3932 -0.0263 0.0589  -0.0331 241 PRO C CD    
4418  N N     . ALA C 241 ? 0.5068 0.5163 0.4529 -0.0161 0.0624  -0.0341 242 ALA C N     
4419  C CA    . ALA C 241 ? 0.5174 0.5280 0.4607 -0.0132 0.0647  -0.0341 242 ALA C CA    
4420  C C     . ALA C 241 ? 0.5477 0.5582 0.4882 -0.0141 0.0681  -0.0322 242 ALA C C     
4421  O O     . ALA C 241 ? 0.5147 0.5274 0.4537 -0.0124 0.0709  -0.0317 242 ALA C O     
4422  C CB    . ALA C 241 ? 0.5061 0.5123 0.4442 -0.0098 0.0628  -0.0359 242 ALA C CB    
4423  N N     . LYS C 242 ? 0.5239 0.5319 0.4636 -0.0167 0.0679  -0.0312 243 LYS C N     
4424  C CA    . LYS C 242 ? 0.5885 0.5954 0.5252 -0.0178 0.0710  -0.0293 243 LYS C CA    
4425  C C     . LYS C 242 ? 0.6380 0.6455 0.5782 -0.0220 0.0712  -0.0281 243 LYS C C     
4426  O O     . LYS C 242 ? 0.6192 0.6258 0.5619 -0.0234 0.0684  -0.0289 243 LYS C O     
4427  C CB    . LYS C 242 ? 0.6176 0.6182 0.5465 -0.0155 0.0704  -0.0295 243 LYS C CB    
4428  C CG    . LYS C 242 ? 0.6785 0.6775 0.6031 -0.0113 0.0697  -0.0311 243 LYS C CG    
4429  C CD    . LYS C 242 ? 0.7605 0.7532 0.6773 -0.0090 0.0687  -0.0314 243 LYS C CD    
4430  C CE    . LYS C 242 ? 0.8490 0.8399 0.7612 -0.0095 0.0720  -0.0293 243 LYS C CE    
4431  N NZ    . LYS C 242 ? 0.8820 0.8667 0.7863 -0.0069 0.0708  -0.0296 243 LYS C NZ    
4432  N N     . LYS C 243 ? 0.5848 0.5935 0.5249 -0.0240 0.0746  -0.0262 244 LYS C N     
4433  C CA    . LYS C 243 ? 0.6210 0.6296 0.5637 -0.0280 0.0750  -0.0250 244 LYS C CA    
4434  C C     . LYS C 243 ? 0.6275 0.6292 0.5642 -0.0281 0.0746  -0.0243 244 LYS C C     
4435  O O     . LYS C 243 ? 0.5456 0.5434 0.4762 -0.0252 0.0747  -0.0245 244 LYS C O     
4436  C CB    . LYS C 243 ? 0.6786 0.6920 0.6246 -0.0305 0.0789  -0.0233 244 LYS C CB    
4437  C CG    . LYS C 243 ? 0.7109 0.7319 0.6639 -0.0309 0.0792  -0.0238 244 LYS C CG    
4438  C CD    . LYS C 243 ? 0.7997 0.8260 0.7570 -0.0340 0.0826  -0.0222 244 LYS C CD    
4439  C CE    . LYS C 243 ? 0.8509 0.8768 0.8043 -0.0329 0.0867  -0.0207 244 LYS C CE    
4440  N NZ    . LYS C 243 ? 0.8948 0.9228 0.8467 -0.0287 0.0873  -0.0216 244 LYS C NZ    
4441  N N     . LEU C 244 ? 0.6542 0.6543 0.5926 -0.0313 0.0741  -0.0237 245 LEU C N     
4442  C CA    . LEU C 244 ? 0.6537 0.6473 0.5869 -0.0314 0.0735  -0.0231 245 LEU C CA    
4443  C C     . LEU C 244 ? 0.6569 0.6479 0.5849 -0.0313 0.0771  -0.0211 245 LEU C C     
4444  O O     . LEU C 244 ? 0.6340 0.6281 0.5644 -0.0337 0.0802  -0.0197 245 LEU C O     
4445  C CB    . LEU C 244 ? 0.6555 0.6483 0.5920 -0.0350 0.0724  -0.0228 245 LEU C CB    
4446  C CG    . LEU C 244 ? 0.6755 0.6705 0.6169 -0.0354 0.0691  -0.0246 245 LEU C CG    
4447  C CD1   . LEU C 244 ? 0.7092 0.7028 0.6529 -0.0388 0.0684  -0.0243 245 LEU C CD1   
4448  C CD2   . LEU C 244 ? 0.6652 0.6574 0.6039 -0.0321 0.0660  -0.0262 245 LEU C CD2   
4449  N N     . GLU C 245 ? 0.6835 0.6689 0.6045 -0.0285 0.0765  -0.0211 246 GLU C N     
4450  C CA    . GLU C 245 ? 0.6906 0.6724 0.6054 -0.0279 0.0797  -0.0191 246 GLU C CA    
4451  C C     . GLU C 245 ? 0.6533 0.6284 0.5637 -0.0286 0.0788  -0.0183 246 GLU C C     
4452  O O     . GLU C 245 ? 0.6098 0.5822 0.5193 -0.0272 0.0753  -0.0196 246 GLU C O     
4453  C CB    . GLU C 245 ? 0.7014 0.6822 0.6108 -0.0237 0.0800  -0.0197 246 GLU C CB    
4454  C CG    . GLU C 245 ? 0.7427 0.7298 0.6561 -0.0227 0.0812  -0.0205 246 GLU C CG    
4455  C CD    . GLU C 245 ? 0.7490 0.7347 0.6565 -0.0184 0.0816  -0.0211 246 GLU C CD    
4456  O OE1   . GLU C 245 ? 0.7956 0.7782 0.6970 -0.0173 0.0844  -0.0196 246 GLU C OE1   
4457  O OE2   . GLU C 245 ? 0.7414 0.7287 0.6502 -0.0160 0.0792  -0.0232 246 GLU C OE2   
4458  N N     . TYR C 246 ? 0.6514 0.6239 0.5591 -0.0306 0.0821  -0.0160 247 TYR C N     
4459  C CA    . TYR C 246 ? 0.6811 0.6471 0.5848 -0.0315 0.0816  -0.0150 247 TYR C CA    
4460  C C     . TYR C 246 ? 0.6421 0.6025 0.5384 -0.0273 0.0794  -0.0155 247 TYR C C     
4461  O O     . TYR C 246 ? 0.6647 0.6249 0.5568 -0.0242 0.0800  -0.0157 247 TYR C O     
4462  C CB    . TYR C 246 ? 0.7001 0.6639 0.6016 -0.0343 0.0859  -0.0124 247 TYR C CB    
4463  C CG    . TYR C 246 ? 0.7045 0.6736 0.6134 -0.0389 0.0878  -0.0119 247 TYR C CG    
4464  C CD1   . TYR C 246 ? 0.7337 0.7027 0.6469 -0.0420 0.0862  -0.0124 247 TYR C CD1   
4465  C CD2   . TYR C 246 ? 0.7496 0.7240 0.6613 -0.0401 0.0913  -0.0110 247 TYR C CD2   
4466  C CE1   . TYR C 246 ? 0.7654 0.7391 0.6852 -0.0462 0.0876  -0.0120 247 TYR C CE1   
4467  C CE2   . TYR C 246 ? 0.7870 0.7666 0.7058 -0.0443 0.0929  -0.0106 247 TYR C CE2   
4468  C CZ    . TYR C 246 ? 0.8069 0.7861 0.7297 -0.0475 0.0909  -0.0112 247 TYR C CZ    
4469  O OH    . TYR C 246 ? 0.8589 0.8433 0.7886 -0.0517 0.0921  -0.0110 247 TYR C OH    
4470  N N     . ASN C 247 ? 0.5697 0.5256 0.4644 -0.0271 0.0769  -0.0159 248 ASN C N     
4471  C CA    . ASN C 247 ? 0.5351 0.4858 0.4233 -0.0233 0.0744  -0.0164 248 ASN C CA    
4472  C C     . ASN C 247 ? 0.5336 0.4773 0.4147 -0.0233 0.0765  -0.0140 248 ASN C C     
4473  O O     . ASN C 247 ? 0.5141 0.4539 0.3945 -0.0242 0.0753  -0.0137 248 ASN C O     
4474  C CB    . ASN C 247 ? 0.5434 0.4942 0.4348 -0.0227 0.0700  -0.0184 248 ASN C CB    
4475  C CG    . ASN C 247 ? 0.5404 0.4868 0.4259 -0.0186 0.0671  -0.0193 248 ASN C CG    
4476  O OD1   . ASN C 247 ? 0.6051 0.5477 0.4835 -0.0162 0.0683  -0.0182 248 ASN C OD1   
4477  N ND2   . ASN C 247 ? 0.5430 0.4901 0.4315 -0.0178 0.0633  -0.0212 248 ASN C ND2   
4478  N N     . TYR C 248 ? 0.5197 0.4618 0.3955 -0.0222 0.0797  -0.0124 249 TYR C N     
4479  C CA    . TYR C 248 ? 0.5289 0.4645 0.3978 -0.0225 0.0825  -0.0098 249 TYR C CA    
4480  C C     . TYR C 248 ? 0.5283 0.4572 0.3909 -0.0194 0.0794  -0.0100 249 TYR C C     
4481  O O     . TYR C 248 ? 0.4993 0.4222 0.3576 -0.0201 0.0805  -0.0083 249 TYR C O     
4482  C CB    . TYR C 248 ? 0.5246 0.4599 0.3885 -0.0214 0.0864  -0.0082 249 TYR C CB    
4483  C CG    . TYR C 248 ? 0.5239 0.4654 0.3938 -0.0249 0.0901  -0.0075 249 TYR C CG    
4484  C CD1   . TYR C 248 ? 0.5370 0.4776 0.4084 -0.0291 0.0936  -0.0054 249 TYR C CD1   
4485  C CD2   . TYR C 248 ? 0.5278 0.4759 0.4017 -0.0239 0.0902  -0.0089 249 TYR C CD2   
4486  C CE1   . TYR C 248 ? 0.5554 0.5022 0.4328 -0.0324 0.0969  -0.0047 249 TYR C CE1   
4487  C CE2   . TYR C 248 ? 0.5266 0.4808 0.4063 -0.0269 0.0936  -0.0082 249 TYR C CE2   
4488  C CZ    . TYR C 248 ? 0.5853 0.5391 0.4669 -0.0312 0.0969  -0.0061 249 TYR C CZ    
4489  O OH    . TYR C 248 ? 0.6220 0.5824 0.5098 -0.0341 0.1001  -0.0055 249 TYR C OH    
4490  N N     . ALA C 249 ? 0.5118 0.4417 0.3738 -0.0158 0.0756  -0.0122 250 ALA C N     
4491  C CA    . ALA C 249 ? 0.5249 0.4494 0.3814 -0.0125 0.0723  -0.0127 250 ALA C CA    
4492  C C     . ALA C 249 ? 0.5279 0.4503 0.3873 -0.0145 0.0709  -0.0126 250 ALA C C     
4493  O O     . ALA C 249 ? 0.5638 0.4798 0.4175 -0.0133 0.0708  -0.0113 250 ALA C O     
4494  C CB    . ALA C 249 ? 0.5125 0.4398 0.3700 -0.0092 0.0683  -0.0154 250 ALA C CB    
4495  N N     . ILE C 250 ? 0.5529 0.4804 0.4208 -0.0173 0.0699  -0.0140 251 ILE C N     
4496  C CA    . ILE C 250 ? 0.5635 0.4895 0.4346 -0.0190 0.0683  -0.0143 251 ILE C CA    
4497  C C     . ILE C 250 ? 0.6083 0.5315 0.4790 -0.0228 0.0719  -0.0120 251 ILE C C     
4498  O O     . ILE C 250 ? 0.6552 0.5732 0.5236 -0.0231 0.0717  -0.0112 251 ILE C O     
4499  C CB    . ILE C 250 ? 0.5592 0.4915 0.4390 -0.0204 0.0657  -0.0167 251 ILE C CB    
4500  C CG1   . ILE C 250 ? 0.5572 0.4924 0.4374 -0.0170 0.0625  -0.0189 251 ILE C CG1   
4501  C CG2   . ILE C 250 ? 0.5471 0.4777 0.4297 -0.0218 0.0641  -0.0171 251 ILE C CG2   
4502  C CD1   . ILE C 250 ? 0.5660 0.4967 0.4408 -0.0131 0.0595  -0.0194 251 ILE C CD1   
4503  N N     . LEU C 251 ? 0.5872 0.5139 0.4606 -0.0256 0.0753  -0.0111 252 LEU C N     
4504  C CA    . LEU C 251 ? 0.6342 0.5590 0.5080 -0.0296 0.0789  -0.0091 252 LEU C CA    
4505  C C     . LEU C 251 ? 0.6967 0.6129 0.5615 -0.0283 0.0806  -0.0068 252 LEU C C     
4506  O O     . LEU C 251 ? 0.7011 0.6127 0.5649 -0.0307 0.0818  -0.0055 252 LEU C O     
4507  C CB    . LEU C 251 ? 0.6517 0.5819 0.5289 -0.0321 0.0822  -0.0084 252 LEU C CB    
4508  C CG    . LEU C 251 ? 0.6393 0.5779 0.5257 -0.0339 0.0810  -0.0104 252 LEU C CG    
4509  C CD1   . LEU C 251 ? 0.6213 0.5652 0.5108 -0.0361 0.0845  -0.0096 252 LEU C CD1   
4510  C CD2   . LEU C 251 ? 0.6655 0.6047 0.5573 -0.0371 0.0795  -0.0112 252 LEU C CD2   
4511  N N     . ALA C 252 ? 0.7578 0.6715 0.6158 -0.0245 0.0806  -0.0063 253 ALA C N     
4512  C CA    . ALA C 252 ? 0.7604 0.6658 0.6090 -0.0227 0.0822  -0.0040 253 ALA C CA    
4513  C C     . ALA C 252 ? 0.7662 0.6660 0.6123 -0.0210 0.0792  -0.0043 253 ALA C C     
4514  O O     . ALA C 252 ? 0.8019 0.6948 0.6431 -0.0217 0.0809  -0.0023 253 ALA C O     
4515  C CB    . ALA C 252 ? 0.7575 0.6619 0.5995 -0.0185 0.0823  -0.0037 253 ALA C CB    
4516  N N     . LYS C 253 ? 0.7510 0.6539 0.6005 -0.0187 0.0748  -0.0068 254 LYS C N     
4517  C CA    . LYS C 253 ? 0.7327 0.6315 0.5808 -0.0168 0.0717  -0.0074 254 LYS C CA    
4518  C C     . LYS C 253 ? 0.7441 0.6419 0.5965 -0.0208 0.0726  -0.0071 254 LYS C C     
4519  O O     . LYS C 253 ? 0.7824 0.6739 0.6311 -0.0202 0.0723  -0.0062 254 LYS C O     
4520  C CB    . LYS C 253 ? 0.7167 0.6201 0.5685 -0.0139 0.0671  -0.0103 254 LYS C CB    
4521  C CG    . LYS C 253 ? 0.7543 0.6578 0.6011 -0.0096 0.0655  -0.0109 254 LYS C CG    
4522  C CD    . LYS C 253 ? 0.7600 0.6676 0.6106 -0.0069 0.0608  -0.0138 254 LYS C CD    
4523  C CE    . LYS C 253 ? 0.7704 0.6781 0.6161 -0.0030 0.0592  -0.0145 254 LYS C CE    
4524  N NZ    . LYS C 253 ? 0.7715 0.6719 0.6074 0.0003  0.0594  -0.0128 254 LYS C NZ    
4525  N N     . LEU C 254 ? 0.7364 0.6404 0.5965 -0.0247 0.0737  -0.0079 255 LEU C N     
4526  C CA    . LEU C 254 ? 0.7430 0.6465 0.6074 -0.0289 0.0747  -0.0077 255 LEU C CA    
4527  C C     . LEU C 254 ? 0.7472 0.6452 0.6072 -0.0316 0.0789  -0.0050 255 LEU C C     
4528  O O     . LEU C 254 ? 0.7643 0.6597 0.6259 -0.0350 0.0800  -0.0045 255 LEU C O     
4529  C CB    . LEU C 254 ? 0.7525 0.6644 0.6261 -0.0319 0.0743  -0.0095 255 LEU C CB    
4530  C CG    . LEU C 254 ? 0.7095 0.6266 0.5881 -0.0299 0.0703  -0.0122 255 LEU C CG    
4531  C CD1   . LEU C 254 ? 0.7289 0.6534 0.6160 -0.0332 0.0703  -0.0135 255 LEU C CD1   
4532  C CD2   . LEU C 254 ? 0.7204 0.6338 0.5982 -0.0281 0.0675  -0.0130 255 LEU C CD2   
4533  N N     . GLY C 255 ? 0.7644 0.6604 0.6187 -0.0303 0.0813  -0.0033 256 GLY C N     
4534  C CA    . GLY C 255 ? 0.6761 0.5666 0.5255 -0.0327 0.0856  -0.0004 256 GLY C CA    
4535  C C     . GLY C 255 ? 0.6378 0.5331 0.4939 -0.0382 0.0886  -0.0001 256 GLY C C     
4536  O O     . GLY C 255 ? 0.6691 0.5600 0.5237 -0.0417 0.0915  0.0017  256 GLY C O     
4537  N N     . ILE C 256 ? 0.5913 0.4955 0.4545 -0.0390 0.0878  -0.0018 257 ILE C N     
4538  C CA    . ILE C 256 ? 0.5872 0.4971 0.4575 -0.0439 0.0902  -0.0018 257 ILE C CA    
4539  C C     . ILE C 256 ? 0.6240 0.5406 0.4962 -0.0431 0.0918  -0.0018 257 ILE C C     
4540  O O     . ILE C 256 ? 0.5734 0.4900 0.4417 -0.0389 0.0907  -0.0022 257 ILE C O     
4541  C CB    . ILE C 256 ? 0.5475 0.4621 0.4258 -0.0460 0.0874  -0.0041 257 ILE C CB    
4542  C CG1   . ILE C 256 ? 0.4953 0.4162 0.3776 -0.0430 0.0838  -0.0065 257 ILE C CG1   
4543  C CG2   . ILE C 256 ? 0.5695 0.4774 0.4456 -0.0465 0.0859  -0.0041 257 ILE C CG2   
4544  C CD1   . ILE C 256 ? 0.4677 0.3934 0.3577 -0.0450 0.0813  -0.0087 257 ILE C CD1   
4545  N N     . GLY C 257 ? 0.6835 0.6057 0.5618 -0.0472 0.0943  -0.0016 258 GLY C N     
4546  C CA    . GLY C 257 ? 0.7138 0.6431 0.5951 -0.0468 0.0961  -0.0017 258 GLY C CA    
4547  C C     . GLY C 257 ? 0.7738 0.7120 0.6651 -0.0497 0.0950  -0.0035 258 GLY C C     
4548  O O     . GLY C 257 ? 0.8105 0.7491 0.7061 -0.0524 0.0934  -0.0044 258 GLY C O     
4549  N N     . PRO C 258 ? 0.7777 0.7233 0.6728 -0.0489 0.0960  -0.0041 259 PRO C N     
4550  C CA    . PRO C 258 ? 0.8095 0.7637 0.7139 -0.0511 0.0949  -0.0058 259 PRO C CA    
4551  C C     . PRO C 258 ? 0.8385 0.7942 0.7481 -0.0567 0.0965  -0.0051 259 PRO C C     
4552  O O     . PRO C 258 ? 0.8422 0.8020 0.7582 -0.0587 0.0943  -0.0067 259 PRO C O     
4553  C CB    . PRO C 258 ? 0.8271 0.7872 0.7327 -0.0494 0.0970  -0.0056 259 PRO C CB    
4554  C CG    . PRO C 258 ? 0.8318 0.7864 0.7284 -0.0448 0.0971  -0.0050 259 PRO C CG    
4555  C CD    . PRO C 258 ? 0.8286 0.7741 0.7186 -0.0456 0.0980  -0.0032 259 PRO C CD    
4556  N N     . GLU C 259 ? 0.8455 0.7977 0.7521 -0.0593 0.1005  -0.0028 260 GLU C N     
4557  C CA    . GLU C 259 ? 0.8761 0.8299 0.7876 -0.0649 0.1025  -0.0020 260 GLU C CA    
4558  C C     . GLU C 259 ? 0.8308 0.7785 0.7412 -0.0667 0.1003  -0.0025 260 GLU C C     
4559  O O     . GLU C 259 ? 0.7863 0.7350 0.7011 -0.0713 0.1008  -0.0025 260 GLU C O     
4560  C CB    . GLU C 259 ? 0.8561 0.8079 0.7647 -0.0671 0.1076  0.0007  260 GLU C CB    
4561  C CG    . GLU C 259 ? 0.9111 0.8523 0.8093 -0.0652 0.1090  0.0027  260 GLU C CG    
4562  C CD    . GLU C 259 ? 0.9504 0.8895 0.8421 -0.0592 0.1079  0.0025  260 GLU C CD    
4563  O OE1   . GLU C 259 ? 0.9822 0.9277 0.8772 -0.0566 0.1061  0.0008  260 GLU C OE1   
4564  O OE2   . GLU C 259 ? 0.9333 0.8639 0.8162 -0.0572 0.1088  0.0041  260 GLU C OE2   
4565  N N     . ASP C 260 ? 0.7838 0.7251 0.6883 -0.0630 0.0977  -0.0029 261 ASP C N     
4566  C CA    . ASP C 260 ? 0.7261 0.6612 0.6288 -0.0640 0.0956  -0.0034 261 ASP C CA    
4567  C C     . ASP C 260 ? 0.7508 0.6907 0.6597 -0.0638 0.0916  -0.0061 261 ASP C C     
4568  O O     . ASP C 260 ? 0.7208 0.6575 0.6303 -0.0655 0.0899  -0.0068 261 ASP C O     
4569  C CB    . ASP C 260 ? 0.7335 0.6596 0.6271 -0.0602 0.0950  -0.0025 261 ASP C CB    
4570  C CG    . ASP C 260 ? 0.7116 0.6316 0.5981 -0.0604 0.0990  0.0004  261 ASP C CG    
4571  O OD1   . ASP C 260 ? 0.6964 0.6137 0.5832 -0.0648 0.1018  0.0019  261 ASP C OD1   
4572  O OD2   . ASP C 260 ? 0.7088 0.6264 0.5893 -0.0563 0.0993  0.0011  261 ASP C OD2   
4573  N N     . LEU C 261 ? 0.7484 0.6956 0.6613 -0.0617 0.0902  -0.0075 262 LEU C N     
4574  C CA    . LEU C 261 ? 0.7236 0.6755 0.6422 -0.0613 0.0866  -0.0099 262 LEU C CA    
4575  C C     . LEU C 261 ? 0.7407 0.6960 0.6656 -0.0663 0.0868  -0.0103 262 LEU C C     
4576  O O     . LEU C 261 ? 0.7530 0.7123 0.6813 -0.0695 0.0894  -0.0094 262 LEU C O     
4577  C CB    . LEU C 261 ? 0.7580 0.7170 0.6796 -0.0585 0.0856  -0.0110 262 LEU C CB    
4578  C CG    . LEU C 261 ? 0.7821 0.7384 0.6978 -0.0534 0.0850  -0.0109 262 LEU C CG    
4579  C CD1   . LEU C 261 ? 0.7665 0.7296 0.6858 -0.0509 0.0836  -0.0124 262 LEU C CD1   
4580  C CD2   . LEU C 261 ? 0.7708 0.7207 0.6821 -0.0510 0.0821  -0.0116 262 LEU C CD2   
4581  N N     . GLY C 262 ? 0.7100 0.6636 0.6364 -0.0670 0.0839  -0.0118 263 GLY C N     
4582  C CA    . GLY C 262 ? 0.7011 0.6572 0.6327 -0.0715 0.0836  -0.0125 263 GLY C CA    
4583  C C     . GLY C 262 ? 0.6952 0.6609 0.6344 -0.0722 0.0826  -0.0138 263 GLY C C     
4584  O O     . GLY C 262 ? 0.7134 0.6828 0.6576 -0.0763 0.0832  -0.0140 263 GLY C O     
4585  O OXT   . GLY C 262 ? 0.6915 0.6609 0.6314 -0.0686 0.0813  -0.0146 263 GLY C OXT   
4646  N N     . LEU D 9   ? 0.3950 0.3554 0.3492 -0.0506 0.0448  -0.0334 11  LEU D N     
4647  C CA    . LEU D 9   ? 0.4205 0.3770 0.3773 -0.0497 0.0453  -0.0340 11  LEU D CA    
4648  C C     . LEU D 9   ? 0.4172 0.3738 0.3762 -0.0490 0.0464  -0.0329 11  LEU D C     
4649  O O     . LEU D 9   ? 0.4344 0.3898 0.3974 -0.0483 0.0467  -0.0330 11  LEU D O     
4650  C CB    . LEU D 9   ? 0.4359 0.3898 0.3908 -0.0502 0.0442  -0.0333 11  LEU D CB    
4651  C CG    . LEU D 9   ? 0.4548 0.4080 0.4118 -0.0492 0.0448  -0.0333 11  LEU D CG    
4652  C CD1   . LEU D 9   ? 0.4538 0.4069 0.4142 -0.0490 0.0452  -0.0345 11  LEU D CD1   
4653  C CD2   . LEU D 9   ? 0.4717 0.4242 0.4264 -0.0486 0.0430  -0.0338 11  LEU D CD2   
4654  N N     . GLY D 10  ? 0.4114 0.3694 0.3683 -0.0496 0.0465  -0.0312 12  GLY D N     
4655  C CA    . GLY D 10  ? 0.3930 0.3516 0.3515 -0.0490 0.0475  -0.0297 12  GLY D CA    
4656  C C     . GLY D 10  ? 0.3701 0.3301 0.3319 -0.0476 0.0479  -0.0309 12  GLY D C     
4657  O O     . GLY D 10  ? 0.3521 0.3114 0.3169 -0.0469 0.0482  -0.0297 12  GLY D O     
4658  N N     . GLN D 11  ? 0.3812 0.3438 0.3426 -0.0468 0.0474  -0.0335 13  GLN D N     
4659  C CA    . GLN D 11  ? 0.4474 0.4126 0.4115 -0.0443 0.0469  -0.0361 13  GLN D CA    
4660  C C     . GLN D 11  ? 0.4544 0.4168 0.4230 -0.0425 0.0452  -0.0395 13  GLN D C     
4661  O O     . GLN D 11  ? 0.4567 0.4176 0.4300 -0.0403 0.0435  -0.0415 13  GLN D O     
4662  C CB    . GLN D 11  ? 0.4929 0.4663 0.4539 -0.0438 0.0470  -0.0372 13  GLN D CB    
4663  C CG    . GLN D 11  ? 0.5166 0.4932 0.4744 -0.0458 0.0479  -0.0336 13  GLN D CG    
4664  C CD    . GLN D 11  ? 0.5358 0.5227 0.4910 -0.0461 0.0478  -0.0333 13  GLN D CD    
4665  O OE1   . GLN D 11  ? 0.6127 0.6058 0.5680 -0.0449 0.0482  -0.0334 13  GLN D OE1   
4666  N NE2   . GLN D 11  ? 0.5444 0.5346 0.4976 -0.0477 0.0472  -0.0326 13  GLN D NE2   
4667  N N     . ASP D 12  ? 0.4579 0.4193 0.4255 -0.0435 0.0450  -0.0403 14  ASP D N     
4668  C CA    . ASP D 12  ? 0.4493 0.4089 0.4209 -0.0418 0.0430  -0.0441 14  ASP D CA    
4669  C C     . ASP D 12  ? 0.4625 0.4159 0.4383 -0.0435 0.0423  -0.0417 14  ASP D C     
4670  O O     . ASP D 12  ? 0.4808 0.4333 0.4544 -0.0455 0.0435  -0.0394 14  ASP D O     
4671  C CB    . ASP D 12  ? 0.4752 0.4391 0.4434 -0.0417 0.0431  -0.0464 14  ASP D CB    
4672  C CG    . ASP D 12  ? 0.5489 0.5119 0.5209 -0.0397 0.0408  -0.0510 14  ASP D CG    
4673  O OD1   . ASP D 12  ? 0.5224 0.4801 0.5005 -0.0388 0.0386  -0.0524 14  ASP D OD1   
4674  O OD2   . ASP D 12  ? 0.6231 0.5909 0.5925 -0.0393 0.0409  -0.0530 14  ASP D OD2   
4675  N N     . ALA D 13  ? 0.4183 0.3680 0.4008 -0.0425 0.0399  -0.0422 15  ALA D N     
4676  C CA    . ALA D 13  ? 0.4501 0.3956 0.4379 -0.0447 0.0387  -0.0385 15  ALA D CA    
4677  C C     . ALA D 13  ? 0.4816 0.4258 0.4710 -0.0454 0.0375  -0.0404 15  ALA D C     
4678  O O     . ALA D 13  ? 0.4160 0.3597 0.4070 -0.0479 0.0378  -0.0367 15  ALA D O     
4679  C CB    . ALA D 13  ? 0.4392 0.3807 0.4346 -0.0440 0.0352  -0.0377 15  ALA D CB    
4680  N N     . GLN D 14  ? 0.5030 0.4482 0.4919 -0.0428 0.0360  -0.0463 16  GLN D N     
4681  C CA    . GLN D 14  ? 0.5635 0.5081 0.5536 -0.0430 0.0348  -0.0488 16  GLN D CA    
4682  C C     . GLN D 14  ? 0.5085 0.4556 0.4922 -0.0450 0.0381  -0.0463 16  GLN D C     
4683  O O     . GLN D 14  ? 0.4690 0.4151 0.4543 -0.0468 0.0379  -0.0446 16  GLN D O     
4684  C CB    . GLN D 14  ? 0.6142 0.5617 0.6042 -0.0391 0.0328  -0.0561 16  GLN D CB    
4685  C CG    . GLN D 14  ? 0.7080 0.6558 0.6990 -0.0389 0.0314  -0.0594 16  GLN D CG    
4686  C CD    . GLN D 14  ? 0.7971 0.7382 0.7963 -0.0407 0.0279  -0.0582 16  GLN D CD    
4687  O OE1   . GLN D 14  ? 0.8591 0.7955 0.8659 -0.0395 0.0234  -0.0598 16  GLN D OE1   
4688  N NE2   . GLN D 14  ? 0.8003 0.7412 0.7985 -0.0437 0.0294  -0.0550 16  GLN D NE2   
4689  N N     . LEU D 15  ? 0.4904 0.4413 0.4675 -0.0447 0.0404  -0.0461 17  LEU D N     
4690  C CA    . LEU D 15  ? 0.4395 0.3918 0.4111 -0.0463 0.0422  -0.0441 17  LEU D CA    
4691  C C     . LEU D 15  ? 0.4122 0.3631 0.3841 -0.0480 0.0433  -0.0398 17  LEU D C     
4692  O O     . LEU D 15  ? 0.4111 0.3624 0.3812 -0.0488 0.0436  -0.0390 17  LEU D O     
4693  C CB    . LEU D 15  ? 0.4848 0.4411 0.4508 -0.0461 0.0433  -0.0439 17  LEU D CB    
4694  C CG    . LEU D 15  ? 0.5075 0.4642 0.4686 -0.0477 0.0436  -0.0419 17  LEU D CG    
4695  C CD1   . LEU D 15  ? 0.5309 0.4885 0.4916 -0.0475 0.0428  -0.0441 17  LEU D CD1   
4696  C CD2   . LEU D 15  ? 0.4776 0.4380 0.4348 -0.0486 0.0438  -0.0399 17  LEU D CD2   
4697  N N     . MET D 16  ? 0.3966 0.3470 0.3707 -0.0482 0.0436  -0.0373 18  MET D N     
4698  C CA    . MET D 16  ? 0.4253 0.3771 0.3997 -0.0494 0.0446  -0.0332 18  MET D CA    
4699  C C     . MET D 16  ? 0.4438 0.3964 0.4226 -0.0507 0.0437  -0.0315 18  MET D C     
4700  O O     . MET D 16  ? 0.4011 0.3571 0.3779 -0.0510 0.0446  -0.0304 18  MET D O     
4701  C CB    . MET D 16  ? 0.4341 0.3861 0.4112 -0.0495 0.0447  -0.0305 18  MET D CB    
4702  C CG    . MET D 16  ? 0.4637 0.4197 0.4416 -0.0505 0.0457  -0.0259 18  MET D CG    
4703  S SD    . MET D 16  ? 0.5552 0.5147 0.5257 -0.0495 0.0472  -0.0265 18  MET D SD    
4704  C CE    . MET D 16  ? 0.4653 0.4235 0.4332 -0.0489 0.0478  -0.0268 18  MET D CE    
4705  N N     . GLU D 17  ? 0.4540 0.4039 0.4395 -0.0513 0.0415  -0.0316 19  GLU D N     
4706  C CA    . GLU D 17  ? 0.4705 0.4214 0.4616 -0.0533 0.0400  -0.0290 19  GLU D CA    
4707  C C     . GLU D 17  ? 0.4638 0.4159 0.4518 -0.0530 0.0405  -0.0318 19  GLU D C     
4708  O O     . GLU D 17  ? 0.4641 0.4204 0.4537 -0.0544 0.0406  -0.0292 19  GLU D O     
4709  C CB    . GLU D 17  ? 0.4630 0.4089 0.4626 -0.0539 0.0361  -0.0292 19  GLU D CB    
4710  C CG    . GLU D 17  ? 0.4941 0.4389 0.4984 -0.0548 0.0348  -0.0249 19  GLU D CG    
4711  C CD    . GLU D 17  ? 0.5236 0.4750 0.5297 -0.0576 0.0361  -0.0171 19  GLU D CD    
4712  O OE1   . GLU D 17  ? 0.5882 0.5426 0.5994 -0.0604 0.0347  -0.0131 19  GLU D OE1   
4713  O OE2   . GLU D 17  ? 0.5989 0.5538 0.6013 -0.0570 0.0385  -0.0150 19  GLU D OE2   
4714  N N     . ASP D 18  ? 0.4739 0.4238 0.4577 -0.0512 0.0406  -0.0367 20  ASP D N     
4715  C CA    . ASP D 18  ? 0.4961 0.4471 0.4766 -0.0507 0.0409  -0.0393 20  ASP D CA    
4716  C C     . ASP D 18  ? 0.4662 0.4206 0.4415 -0.0505 0.0426  -0.0376 20  ASP D C     
4717  O O     . ASP D 18  ? 0.4190 0.3760 0.3939 -0.0506 0.0425  -0.0376 20  ASP D O     
4718  C CB    . ASP D 18  ? 0.5966 0.5465 0.5736 -0.0489 0.0405  -0.0439 20  ASP D CB    
4719  C CG    . ASP D 18  ? 0.6957 0.6439 0.6777 -0.0477 0.0381  -0.0477 20  ASP D CG    
4720  O OD1   . ASP D 18  ? 0.6881 0.6337 0.6772 -0.0487 0.0359  -0.0466 20  ASP D OD1   
4721  O OD2   . ASP D 18  ? 0.8486 0.7988 0.8278 -0.0457 0.0378  -0.0516 20  ASP D OD2   
4722  N N     . TYR D 19  ? 0.4791 0.4336 0.4507 -0.0499 0.0436  -0.0367 21  TYR D N     
4723  C CA    . TYR D 19  ? 0.4565 0.4134 0.4235 -0.0490 0.0440  -0.0363 21  TYR D CA    
4724  C C     . TYR D 19  ? 0.4797 0.4429 0.4491 -0.0490 0.0445  -0.0338 21  TYR D C     
4725  O O     . TYR D 19  ? 0.4560 0.4225 0.4233 -0.0477 0.0440  -0.0351 21  TYR D O     
4726  C CB    . TYR D 19  ? 0.4350 0.3907 0.3989 -0.0485 0.0444  -0.0357 21  TYR D CB    
4727  C CG    . TYR D 19  ? 0.4224 0.3802 0.3827 -0.0471 0.0438  -0.0359 21  TYR D CG    
4728  C CD1   . TYR D 19  ? 0.3888 0.3439 0.3453 -0.0462 0.0417  -0.0381 21  TYR D CD1   
4729  C CD2   . TYR D 19  ? 0.4129 0.3757 0.3741 -0.0463 0.0445  -0.0339 21  TYR D CD2   
4730  C CE1   . TYR D 19  ? 0.4002 0.3563 0.3542 -0.0442 0.0397  -0.0393 21  TYR D CE1   
4731  C CE2   . TYR D 19  ? 0.3993 0.3650 0.3575 -0.0440 0.0432  -0.0354 21  TYR D CE2   
4732  C CZ    . TYR D 19  ? 0.3928 0.3543 0.3476 -0.0427 0.0405  -0.0386 21  TYR D CZ    
4733  O OH    . TYR D 19  ? 0.4082 0.3716 0.3608 -0.0398 0.0379  -0.0411 21  TYR D OH    
4734  N N     . LYS D 20  ? 0.5149 0.4807 0.4889 -0.0504 0.0450  -0.0300 22  LYS D N     
4735  C CA    . LYS D 20  ? 0.5460 0.5208 0.5225 -0.0509 0.0455  -0.0262 22  LYS D CA    
4736  C C     . LYS D 20  ? 0.5510 0.5293 0.5309 -0.0520 0.0447  -0.0256 22  LYS D C     
4737  O O     . LYS D 20  ? 0.5331 0.5212 0.5136 -0.0517 0.0451  -0.0235 22  LYS D O     
4738  C CB    . LYS D 20  ? 0.5623 0.5393 0.5439 -0.0528 0.0457  -0.0209 22  LYS D CB    
4739  C CG    . LYS D 20  ? 0.5679 0.5437 0.5464 -0.0516 0.0466  -0.0209 22  LYS D CG    
4740  C CD    . LYS D 20  ? 0.5496 0.5312 0.5326 -0.0531 0.0470  -0.0149 22  LYS D CD    
4741  C CE    . LYS D 20  ? 0.5814 0.5594 0.5724 -0.0562 0.0450  -0.0110 22  LYS D CE    
4742  N NZ    . LYS D 20  ? 0.5980 0.5827 0.5942 -0.0582 0.0447  -0.0037 22  LYS D NZ    
4743  N N     . GLN D 21  ? 0.5640 0.5353 0.5460 -0.0531 0.0435  -0.0278 23  GLN D N     
4744  C CA    . GLN D 21  ? 0.5397 0.5132 0.5249 -0.0542 0.0425  -0.0279 23  GLN D CA    
4745  C C     . GLN D 21  ? 0.4809 0.4574 0.4603 -0.0516 0.0430  -0.0316 23  GLN D C     
4746  O O     . GLN D 21  ? 0.4070 0.3915 0.3876 -0.0516 0.0430  -0.0304 23  GLN D O     
4747  C CB    . GLN D 21  ? 0.5427 0.5081 0.5314 -0.0552 0.0406  -0.0305 23  GLN D CB    
4748  C CG    . GLN D 21  ? 0.6113 0.5736 0.6081 -0.0576 0.0384  -0.0272 23  GLN D CG    
4749  C CD    . GLN D 21  ? 0.6741 0.6427 0.6785 -0.0612 0.0369  -0.0209 23  GLN D CD    
4750  O OE1   . GLN D 21  ? 0.7604 0.7386 0.7642 -0.0619 0.0385  -0.0162 23  GLN D OE1   
4751  N NE2   . GLN D 21  ? 0.6635 0.6277 0.6754 -0.0633 0.0333  -0.0207 23  GLN D NE2   
4752  N N     . ASN D 22  ? 0.4689 0.4396 0.4424 -0.0495 0.0430  -0.0356 24  ASN D N     
4753  C CA    . ASN D 22  ? 0.4813 0.4525 0.4499 -0.0470 0.0422  -0.0392 24  ASN D CA    
4754  C C     . ASN D 22  ? 0.4459 0.4121 0.4092 -0.0453 0.0415  -0.0412 24  ASN D C     
4755  O O     . ASN D 22  ? 0.5298 0.4901 0.4909 -0.0456 0.0407  -0.0429 24  ASN D O     
4756  C CB    . ASN D 22  ? 0.4597 0.4280 0.4291 -0.0476 0.0413  -0.0416 24  ASN D CB    
4757  C CG    . ASN D 22  ? 0.4878 0.4575 0.4531 -0.0451 0.0401  -0.0447 24  ASN D CG    
4758  O OD1   . ASN D 22  ? 0.5642 0.5354 0.5259 -0.0426 0.0392  -0.0458 24  ASN D OD1   
4759  N ND2   . ASN D 22  ? 0.4921 0.4609 0.4580 -0.0453 0.0394  -0.0465 24  ASN D ND2   
4760  N N     . PRO D 23  ? 0.4071 0.3767 0.3686 -0.0436 0.0414  -0.0408 25  PRO D N     
4761  C CA    . PRO D 23  ? 0.4085 0.3730 0.3660 -0.0425 0.0399  -0.0422 25  PRO D CA    
4762  C C     . PRO D 23  ? 0.4185 0.3772 0.3727 -0.0416 0.0371  -0.0450 25  PRO D C     
4763  O O     . PRO D 23  ? 0.3948 0.3480 0.3477 -0.0432 0.0364  -0.0443 25  PRO D O     
4764  C CB    . PRO D 23  ? 0.4006 0.3720 0.3572 -0.0396 0.0394  -0.0427 25  PRO D CB    
4765  C CG    . PRO D 23  ? 0.3830 0.3634 0.3439 -0.0409 0.0420  -0.0390 25  PRO D CG    
4766  C CD    . PRO D 23  ? 0.3915 0.3713 0.3552 -0.0429 0.0424  -0.0385 25  PRO D CD    
4767  N N     . GLU D 24  ? 0.4457 0.4069 0.3990 -0.0391 0.0352  -0.0476 26  GLU D N     
4768  C CA    . GLU D 24  ? 0.5231 0.4787 0.4738 -0.0380 0.0315  -0.0499 26  GLU D CA    
4769  C C     . GLU D 24  ? 0.5105 0.4621 0.4613 -0.0408 0.0323  -0.0487 26  GLU D C     
4770  O O     . GLU D 24  ? 0.5072 0.4538 0.4562 -0.0418 0.0298  -0.0480 26  GLU D O     
4771  C CB    . GLU D 24  ? 0.5995 0.5594 0.5496 -0.0342 0.0292  -0.0536 26  GLU D CB    
4772  C CG    . GLU D 24  ? 0.7102 0.6731 0.6591 -0.0299 0.0261  -0.0567 26  GLU D CG    
4773  C CD    . GLU D 24  ? 0.7901 0.7568 0.7381 -0.0250 0.0224  -0.0617 26  GLU D CD    
4774  O OE1   . GLU D 24  ? 0.9550 0.9327 0.9033 -0.0212 0.0228  -0.0641 26  GLU D OE1   
4775  O OE2   . GLU D 24  ? 0.7889 0.7487 0.7359 -0.0247 0.0190  -0.0631 26  GLU D OE2   
4776  N N     . ALA D 25  ? 0.4897 0.4446 0.4432 -0.0422 0.0352  -0.0481 27  ALA D N     
4777  C CA    . ALA D 25  ? 0.4876 0.4407 0.4417 -0.0439 0.0357  -0.0481 27  ALA D CA    
4778  C C     . ALA D 25  ? 0.4360 0.3865 0.3893 -0.0458 0.0362  -0.0463 27  ALA D C     
4779  O O     . ALA D 25  ? 0.4035 0.3528 0.3549 -0.0466 0.0350  -0.0460 27  ALA D O     
4780  C CB    . ALA D 25  ? 0.4836 0.4402 0.4418 -0.0448 0.0378  -0.0483 27  ALA D CB    
4781  N N     . VAL D 26  ? 0.3958 0.3468 0.3505 -0.0463 0.0379  -0.0449 28  VAL D N     
4782  C CA    . VAL D 26  ? 0.4034 0.3537 0.3577 -0.0477 0.0386  -0.0435 28  VAL D CA    
4783  C C     . VAL D 26  ? 0.4380 0.3860 0.3890 -0.0482 0.0362  -0.0419 28  VAL D C     
4784  O O     . VAL D 26  ? 0.4435 0.3924 0.3933 -0.0497 0.0358  -0.0404 28  VAL D O     
4785  C CB    . VAL D 26  ? 0.4156 0.3669 0.3727 -0.0480 0.0406  -0.0424 28  VAL D CB    
4786  C CG1   . VAL D 26  ? 0.4245 0.3756 0.3806 -0.0488 0.0410  -0.0412 28  VAL D CG1   
4787  C CG2   . VAL D 26  ? 0.4411 0.3937 0.4030 -0.0482 0.0416  -0.0430 28  VAL D CG2   
4788  N N     . MET D 27  ? 0.4136 0.3594 0.3634 -0.0470 0.0342  -0.0422 29  MET D N     
4789  C CA    . MET D 27  ? 0.4428 0.3849 0.3906 -0.0476 0.0306  -0.0407 29  MET D CA    
4790  C C     . MET D 27  ? 0.4202 0.3603 0.3669 -0.0486 0.0274  -0.0397 29  MET D C     
4791  O O     . MET D 27  ? 0.4662 0.4056 0.4122 -0.0512 0.0254  -0.0363 29  MET D O     
4792  C CB    . MET D 27  ? 0.3998 0.3404 0.3474 -0.0449 0.0282  -0.0427 29  MET D CB    
4793  C CG    . MET D 27  ? 0.4243 0.3672 0.3725 -0.0446 0.0303  -0.0421 29  MET D CG    
4794  S SD    . MET D 27  ? 0.4582 0.4018 0.4059 -0.0406 0.0269  -0.0453 29  MET D SD    
4795  C CE    . MET D 27  ? 0.4893 0.4396 0.4378 -0.0374 0.0283  -0.0484 29  MET D CE    
4796  N N     . ARG D 28  ? 0.4464 0.3865 0.3931 -0.0469 0.0267  -0.0422 30  ARG D N     
4797  C CA    . ARG D 28  ? 0.4913 0.4299 0.4371 -0.0477 0.0236  -0.0411 30  ARG D CA    
4798  C C     . ARG D 28  ? 0.4650 0.4084 0.4106 -0.0503 0.0259  -0.0386 30  ARG D C     
4799  O O     . ARG D 28  ? 0.5342 0.4783 0.4791 -0.0524 0.0232  -0.0352 30  ARG D O     
4800  C CB    . ARG D 28  ? 0.5022 0.4411 0.4481 -0.0451 0.0231  -0.0447 30  ARG D CB    
4801  C CG    . ARG D 28  ? 0.5787 0.5142 0.5244 -0.0417 0.0189  -0.0476 30  ARG D CG    
4802  C CD    . ARG D 28  ? 0.6423 0.5792 0.5879 -0.0390 0.0178  -0.0508 30  ARG D CD    
4803  N NE    . ARG D 28  ? 0.6954 0.6292 0.6407 -0.0351 0.0123  -0.0543 30  ARG D NE    
4804  C CZ    . ARG D 28  ? 0.7889 0.7252 0.7344 -0.0315 0.0117  -0.0577 30  ARG D CZ    
4805  N NH1   . ARG D 28  ? 0.7674 0.7014 0.7128 -0.0270 0.0057  -0.0619 30  ARG D NH1   
4806  N NH2   . ARG D 28  ? 0.8130 0.7550 0.7591 -0.0322 0.0167  -0.0570 30  ARG D NH2   
4807  N N     . ALA D 29  ? 0.4402 0.3877 0.3871 -0.0499 0.0303  -0.0403 31  ALA D N     
4808  C CA    . ALA D 29  ? 0.4485 0.4021 0.3955 -0.0509 0.0322  -0.0399 31  ALA D CA    
4809  C C     . ALA D 29  ? 0.4354 0.3922 0.3814 -0.0532 0.0316  -0.0358 31  ALA D C     
4810  O O     . ALA D 29  ? 0.4567 0.4210 0.4021 -0.0542 0.0319  -0.0343 31  ALA D O     
4811  C CB    . ALA D 29  ? 0.4545 0.4102 0.4041 -0.0495 0.0355  -0.0433 31  ALA D CB    
4812  N N     . HIS D 30  ? 0.4305 0.3834 0.3764 -0.0539 0.0307  -0.0341 32  HIS D N     
4813  C CA    . HIS D 30  ? 0.4247 0.3808 0.3701 -0.0564 0.0300  -0.0300 32  HIS D CA    
4814  C C     . HIS D 30  ? 0.4234 0.3755 0.3684 -0.0590 0.0247  -0.0254 32  HIS D C     
4815  O O     . HIS D 30  ? 0.4331 0.3873 0.3782 -0.0619 0.0229  -0.0207 32  HIS D O     
4816  C CB    . HIS D 30  ? 0.4235 0.3786 0.3697 -0.0556 0.0324  -0.0310 32  HIS D CB    
4817  C CG    . HIS D 30  ? 0.4123 0.3723 0.3599 -0.0539 0.0363  -0.0341 32  HIS D CG    
4818  N ND1   . HIS D 30  ? 0.3905 0.3485 0.3400 -0.0517 0.0380  -0.0380 32  HIS D ND1   
4819  C CD2   . HIS D 30  ? 0.4058 0.3729 0.3536 -0.0538 0.0379  -0.0340 32  HIS D CD2   
4820  C CE1   . HIS D 30  ? 0.3935 0.3554 0.3449 -0.0505 0.0399  -0.0403 32  HIS D CE1   
4821  N NE2   . HIS D 30  ? 0.4087 0.3765 0.3589 -0.0512 0.0400  -0.0384 32  HIS D NE2   
4822  N N     . GLY D 31  ? 0.4309 0.3770 0.3759 -0.0579 0.0215  -0.0267 33  GLY D N     
4823  C CA    . GLY D 31  ? 0.4688 0.4106 0.4143 -0.0602 0.0152  -0.0224 33  GLY D CA    
4824  C C     . GLY D 31  ? 0.4787 0.4117 0.4254 -0.0597 0.0105  -0.0227 33  GLY D C     
4825  O O     . GLY D 31  ? 0.4695 0.3986 0.4178 -0.0626 0.0043  -0.0180 33  GLY D O     
4826  N N     . LEU D 32  ? 0.5166 0.4471 0.4630 -0.0561 0.0128  -0.0281 34  LEU D N     
4827  C CA    . LEU D 32  ? 0.5284 0.4521 0.4758 -0.0544 0.0083  -0.0301 34  LEU D CA    
4828  C C     . LEU D 32  ? 0.5352 0.4523 0.4833 -0.0517 0.0021  -0.0328 34  LEU D C     
4829  O O     . LEU D 32  ? 0.4894 0.4082 0.4367 -0.0494 0.0038  -0.0358 34  LEU D O     
4830  C CB    . LEU D 32  ? 0.5598 0.4858 0.5067 -0.0511 0.0128  -0.0346 34  LEU D CB    
4831  C CG    . LEU D 32  ? 0.5735 0.5037 0.5204 -0.0531 0.0170  -0.0321 34  LEU D CG    
4832  C CD1   . LEU D 32  ? 0.5740 0.5110 0.5203 -0.0548 0.0223  -0.0305 34  LEU D CD1   
4833  C CD2   . LEU D 32  ? 0.5610 0.4924 0.5079 -0.0500 0.0195  -0.0358 34  LEU D CD2   
4834  N N     . THR D 33  ? 0.5480 0.4575 0.4983 -0.0520 -0.0058 -0.0320 35  THR D N     
4835  C CA    . THR D 33  ? 0.5288 0.4309 0.4806 -0.0489 -0.0134 -0.0352 35  THR D CA    
4836  C C     . THR D 33  ? 0.5153 0.4191 0.4659 -0.0421 -0.0120 -0.0439 35  THR D C     
4837  O O     . THR D 33  ? 0.4551 0.3650 0.4043 -0.0405 -0.0059 -0.0462 35  THR D O     
4838  C CB    . THR D 33  ? 0.5169 0.4098 0.4723 -0.0510 -0.0233 -0.0323 35  THR D CB    
4839  O OG1   . THR D 33  ? 0.5107 0.4036 0.4663 -0.0490 -0.0227 -0.0355 35  THR D OG1   
4840  C CG2   . THR D 33  ? 0.5013 0.3951 0.4585 -0.0585 -0.0250 -0.0221 35  THR D CG2   
4841  N N     . ASP D 34  ? 0.6015 0.5009 0.5529 -0.0379 -0.0180 -0.0484 36  ASP D N     
4842  C CA    . ASP D 34  ? 0.6302 0.5337 0.5806 -0.0308 -0.0174 -0.0568 36  ASP D CA    
4843  C C     . ASP D 34  ? 0.5686 0.4718 0.5199 -0.0274 -0.0203 -0.0610 36  ASP D C     
4844  O O     . ASP D 34  ? 0.5050 0.4171 0.4548 -0.0239 -0.0154 -0.0650 36  ASP D O     
4845  C CB    . ASP D 34  ? 0.6946 0.5941 0.6459 -0.0267 -0.0240 -0.0610 36  ASP D CB    
4846  C CG    . ASP D 34  ? 0.7632 0.6642 0.7134 -0.0293 -0.0211 -0.0576 36  ASP D CG    
4847  O OD1   . ASP D 34  ? 0.8387 0.7447 0.7875 -0.0340 -0.0138 -0.0526 36  ASP D OD1   
4848  O OD2   . ASP D 34  ? 0.8141 0.7116 0.7650 -0.0261 -0.0266 -0.0606 36  ASP D OD2   
4849  N N     . GLU D 35  ? 0.5815 0.4750 0.5357 -0.0288 -0.0288 -0.0596 37  GLU D N     
4850  C CA    . GLU D 35  ? 0.6106 0.5027 0.5662 -0.0256 -0.0330 -0.0639 37  GLU D CA    
4851  C C     . GLU D 35  ? 0.5362 0.4359 0.4898 -0.0284 -0.0242 -0.0608 37  GLU D C     
4852  O O     . GLU D 35  ? 0.5176 0.4238 0.4704 -0.0241 -0.0222 -0.0657 37  GLU D O     
4853  C CB    . GLU D 35  ? 0.6816 0.5607 0.6418 -0.0279 -0.0445 -0.0616 37  GLU D CB    
4854  C CG    . GLU D 35  ? 0.7768 0.6528 0.7383 -0.0372 -0.0432 -0.0505 37  GLU D CG    
4855  C CD    . GLU D 35  ? 0.9148 0.7785 0.8820 -0.0408 -0.0554 -0.0463 37  GLU D CD    
4856  O OE1   . GLU D 35  ? 0.9443 0.8028 0.9144 -0.0382 -0.0622 -0.0505 37  GLU D OE1   
4857  O OE2   . GLU D 35  ? 0.9987 0.8585 0.9679 -0.0463 -0.0585 -0.0386 37  GLU D OE2   
4858  N N     . GLN D 36  ? 0.5339 0.4339 0.4870 -0.0354 -0.0192 -0.0527 38  GLN D N     
4859  C CA    . GLN D 36  ? 0.4999 0.4064 0.4516 -0.0382 -0.0115 -0.0495 38  GLN D CA    
4860  C C     . GLN D 36  ? 0.4647 0.3814 0.4139 -0.0348 -0.0034 -0.0530 38  GLN D C     
4861  O O     . GLN D 36  ? 0.4834 0.4058 0.4321 -0.0333 0.0002  -0.0543 38  GLN D O     
4862  C CB    . GLN D 36  ? 0.4785 0.3852 0.4301 -0.0453 -0.0082 -0.0411 38  GLN D CB    
4863  C CG    . GLN D 36  ? 0.4808 0.3801 0.4355 -0.0500 -0.0159 -0.0355 38  GLN D CG    
4864  C CD    . GLN D 36  ? 0.4801 0.3835 0.4345 -0.0566 -0.0127 -0.0270 38  GLN D CD    
4865  O OE1   . GLN D 36  ? 0.4272 0.3382 0.3791 -0.0571 -0.0050 -0.0264 38  GLN D OE1   
4866  N NE2   . GLN D 36  ? 0.4615 0.3609 0.4190 -0.0617 -0.0191 -0.0204 38  GLN D NE2   
4867  N N     . ILE D 37  ? 0.4510 0.3703 0.3993 -0.0339 -0.0010 -0.0539 39  ILE D N     
4868  C CA    . ILE D 37  ? 0.4627 0.3919 0.4097 -0.0315 0.0058  -0.0561 39  ILE D CA    
4869  C C     . ILE D 37  ? 0.4680 0.4030 0.4150 -0.0250 0.0036  -0.0626 39  ILE D C     
4870  O O     . ILE D 37  ? 0.5336 0.4779 0.4802 -0.0237 0.0086  -0.0629 39  ILE D O     
4871  C CB    . ILE D 37  ? 0.4473 0.3777 0.3939 -0.0320 0.0077  -0.0558 39  ILE D CB    
4872  C CG1   . ILE D 37  ? 0.4515 0.3792 0.3980 -0.0377 0.0104  -0.0498 39  ILE D CG1   
4873  C CG2   . ILE D 37  ? 0.4522 0.3930 0.3985 -0.0295 0.0133  -0.0580 39  ILE D CG2   
4874  C CD1   . ILE D 37  ? 0.4460 0.3756 0.3921 -0.0382 0.0125  -0.0498 39  ILE D CD1   
4875  N N     . ASN D 38  ? 0.5093 0.4396 0.4570 -0.0206 -0.0044 -0.0678 40  ASN D N     
4876  C CA    . ASN D 38  ? 0.5340 0.4713 0.4817 -0.0131 -0.0078 -0.0755 40  ASN D CA    
4877  C C     . ASN D 38  ? 0.5063 0.4470 0.4541 -0.0125 -0.0070 -0.0759 40  ASN D C     
4878  O O     . ASN D 38  ? 0.4763 0.4297 0.4233 -0.0084 -0.0039 -0.0789 40  ASN D O     
4879  C CB    . ASN D 38  ? 0.6325 0.5616 0.5817 -0.0083 -0.0184 -0.0815 40  ASN D CB    
4880  C CG    . ASN D 38  ? 0.7076 0.6448 0.6570 0.0006  -0.0230 -0.0909 40  ASN D CG    
4881  O OD1   . ASN D 38  ? 0.8001 0.7517 0.7480 0.0051  -0.0191 -0.0946 40  ASN D OD1   
4882  N ND2   . ASN D 38  ? 0.7465 0.6760 0.6982 0.0032  -0.0317 -0.0949 40  ASN D ND2   
4883  N N     . ALA D 39  ? 0.4880 0.4187 0.4371 -0.0167 -0.0100 -0.0722 41  ALA D N     
4884  C CA    . ALA D 39  ? 0.4657 0.3983 0.4151 -0.0165 -0.0098 -0.0723 41  ALA D CA    
4885  C C     . ALA D 39  ? 0.4544 0.3982 0.4022 -0.0184 0.0001  -0.0686 41  ALA D C     
4886  O O     . ALA D 39  ? 0.4771 0.4295 0.4246 -0.0154 0.0016  -0.0708 41  ALA D O     
4887  C CB    . ALA D 39  ? 0.4640 0.3847 0.4153 -0.0222 -0.0139 -0.0674 41  ALA D CB    
4888  N N     . VAL D 40  ? 0.4256 0.3694 0.3728 -0.0233 0.0062  -0.0630 42  VAL D N     
4889  C CA    . VAL D 40  ? 0.4306 0.3827 0.3775 -0.0257 0.0145  -0.0588 42  VAL D CA    
4890  C C     . VAL D 40  ? 0.4378 0.4034 0.3846 -0.0213 0.0172  -0.0617 42  VAL D C     
4891  O O     . VAL D 40  ? 0.4113 0.3864 0.3584 -0.0207 0.0210  -0.0602 42  VAL D O     
4892  C CB    . VAL D 40  ? 0.4383 0.3867 0.3854 -0.0313 0.0189  -0.0533 42  VAL D CB    
4893  C CG1   . VAL D 40  ? 0.4286 0.3850 0.3765 -0.0329 0.0260  -0.0501 42  VAL D CG1   
4894  C CG2   . VAL D 40  ? 0.4441 0.3838 0.3913 -0.0360 0.0173  -0.0493 42  VAL D CG2   
4895  N N     . MET D 41  ? 0.4243 0.3918 0.3708 -0.0183 0.0151  -0.0652 43  MET D N     
4896  C CA    . MET D 41  ? 0.4823 0.4646 0.4289 -0.0146 0.0178  -0.0670 43  MET D CA    
4897  C C     . MET D 41  ? 0.4553 0.4482 0.4014 -0.0078 0.0145  -0.0730 43  MET D C     
4898  O O     . MET D 41  ? 0.4361 0.4452 0.3824 -0.0056 0.0181  -0.0725 43  MET D O     
4899  C CB    . MET D 41  ? 0.5248 0.5067 0.4712 -0.0131 0.0162  -0.0695 43  MET D CB    
4900  C CG    . MET D 41  ? 0.5449 0.5190 0.4919 -0.0192 0.0196  -0.0642 43  MET D CG    
4901  S SD    . MET D 41  ? 0.6633 0.6431 0.6123 -0.0247 0.0276  -0.0568 43  MET D SD    
4902  C CE    . MET D 41  ? 0.6931 0.6928 0.6434 -0.0209 0.0299  -0.0575 43  MET D CE    
4903  N N     . THR D 42  ? 0.4296 0.4141 0.3754 -0.0044 0.0072  -0.0785 44  THR D N     
4904  C CA    . THR D 42  ? 0.4608 0.4546 0.4064 0.0031  0.0026  -0.0859 44  THR D CA    
4905  C C     . THR D 42  ? 0.4589 0.4554 0.4046 0.0014  0.0051  -0.0831 44  THR D C     
4906  O O     . THR D 42  ? 0.5009 0.5088 0.4462 0.0073  0.0031  -0.0881 44  THR D O     
4907  C CB    . THR D 42  ? 0.4953 0.4773 0.4416 0.0076  -0.0078 -0.0934 44  THR D CB    
4908  O OG1   . THR D 42  ? 0.4905 0.4554 0.4380 0.0014  -0.0099 -0.0887 44  THR D OG1   
4909  C CG2   . THR D 42  ? 0.5008 0.4806 0.4471 0.0099  -0.0108 -0.0966 44  THR D CG2   
4910  N N     . GLY D 43  ? 0.4895 0.4765 0.4355 -0.0061 0.0093  -0.0755 45  GLY D N     
4911  C CA    . GLY D 43  ? 0.4701 0.4586 0.4163 -0.0082 0.0118  -0.0723 45  GLY D CA    
4912  C C     . GLY D 43  ? 0.4956 0.4760 0.4422 -0.0057 0.0043  -0.0773 45  GLY D C     
4913  O O     . GLY D 43  ? 0.5382 0.5259 0.4848 -0.0029 0.0039  -0.0793 45  GLY D O     
4914  N N     . ASP D 44  ? 0.5096 0.4753 0.4573 -0.0068 -0.0023 -0.0789 46  ASP D N     
4915  C CA    . ASP D 44  ? 0.5625 0.5181 0.5120 -0.0056 -0.0109 -0.0825 46  ASP D CA    
4916  C C     . ASP D 44  ? 0.5955 0.5401 0.5458 -0.0138 -0.0093 -0.0746 46  ASP D C     
4917  O O     . ASP D 44  ? 0.5949 0.5281 0.5465 -0.0183 -0.0122 -0.0710 46  ASP D O     
4918  C CB    . ASP D 44  ? 0.6120 0.5586 0.5633 -0.0017 -0.0206 -0.0887 46  ASP D CB    
4919  C CG    . ASP D 44  ? 0.6620 0.5967 0.6165 -0.0004 -0.0316 -0.0928 46  ASP D CG    
4920  O OD1   . ASP D 44  ? 0.6722 0.6062 0.6274 -0.0026 -0.0312 -0.0907 46  ASP D OD1   
4921  O OD2   . ASP D 44  ? 0.7121 0.6381 0.6691 0.0029  -0.0410 -0.0979 46  ASP D OD2   
4922  N N     . MET D 45  ? 0.6139 0.5637 0.5637 -0.0156 -0.0047 -0.0716 47  MET D N     
4923  C CA    . MET D 45  ? 0.6425 0.5855 0.5929 -0.0228 -0.0023 -0.0642 47  MET D CA    
4924  C C     . MET D 45  ? 0.6824 0.6127 0.6356 -0.0248 -0.0115 -0.0645 47  MET D C     
4925  O O     . MET D 45  ? 0.7494 0.6724 0.7036 -0.0314 -0.0116 -0.0579 47  MET D O     
4926  C CB    . MET D 45  ? 0.6574 0.6090 0.6069 -0.0231 0.0033  -0.0621 47  MET D CB    
4927  C CG    . MET D 45  ? 0.6338 0.5973 0.5818 -0.0225 0.0119  -0.0596 47  MET D CG    
4928  S SD    . MET D 45  ? 0.6457 0.6054 0.5934 -0.0281 0.0177  -0.0534 47  MET D SD    
4929  C CE    . MET D 45  ? 0.6551 0.6149 0.6026 -0.0242 0.0141  -0.0584 47  MET D CE    
4930  N N     . GLU D 46  ? 0.7217 0.6505 0.6767 -0.0190 -0.0199 -0.0722 48  GLU D N     
4931  C CA    . GLU D 46  ? 0.7665 0.6830 0.7254 -0.0208 -0.0302 -0.0728 48  GLU D CA    
4932  C C     . GLU D 46  ? 0.7722 0.6769 0.7334 -0.0251 -0.0353 -0.0688 48  GLU D C     
4933  O O     . GLU D 46  ? 0.9079 0.8037 0.8721 -0.0316 -0.0394 -0.0625 48  GLU D O     
4934  C CB    . GLU D 46  ? 0.8101 0.7274 0.7710 -0.0124 -0.0393 -0.0834 48  GLU D CB    
4935  C CG    . GLU D 46  ? 0.8912 0.7949 0.8576 -0.0143 -0.0512 -0.0842 48  GLU D CG    
4936  C CD    . GLU D 46  ? 0.8840 0.7868 0.8513 -0.0208 -0.0487 -0.0773 48  GLU D CD    
4937  O OE1   . GLU D 46  ? 1.0068 0.9197 0.9718 -0.0180 -0.0437 -0.0795 48  GLU D OE1   
4938  O OE2   . GLU D 46  ? 0.8862 0.7792 0.8564 -0.0287 -0.0518 -0.0693 48  GLU D OE2   
4939  N N     . LYS D 47  ? 0.8045 0.7103 0.7644 -0.0217 -0.0351 -0.0721 49  LYS D N     
4940  C CA    . LYS D 47  ? 0.7844 0.6799 0.7464 -0.0250 -0.0402 -0.0689 49  LYS D CA    
4941  C C     . LYS D 47  ? 0.7576 0.6534 0.7182 -0.0336 -0.0327 -0.0583 49  LYS D C     
4942  O O     . LYS D 47  ? 0.7746 0.6622 0.7380 -0.0394 -0.0374 -0.0521 49  LYS D O     
4943  C CB    . LYS D 47  ? 0.7823 0.6805 0.7430 -0.0188 -0.0411 -0.0753 49  LYS D CB    
4944  C CG    . LYS D 47  ? 0.7854 0.6720 0.7490 -0.0208 -0.0489 -0.0735 49  LYS D CG    
4945  C CD    . LYS D 47  ? 0.7981 0.6716 0.7675 -0.0191 -0.0635 -0.0772 49  LYS D CD    
4946  C CE    . LYS D 47  ? 0.8057 0.6672 0.7788 -0.0223 -0.0715 -0.0734 49  LYS D CE    
4947  N NZ    . LYS D 47  ? 0.8231 0.6888 0.7933 -0.0180 -0.0686 -0.0771 49  LYS D NZ    
4948  N N     . LEU D 48  ? 0.6882 0.5944 0.6450 -0.0342 -0.0216 -0.0563 50  LEU D N     
4949  C CA    . LEU D 48  ? 0.6722 0.5805 0.6277 -0.0408 -0.0145 -0.0480 50  LEU D CA    
4950  C C     . LEU D 48  ? 0.6797 0.5836 0.6376 -0.0470 -0.0177 -0.0415 50  LEU D C     
4951  O O     . LEU D 48  ? 0.6107 0.5134 0.5692 -0.0529 -0.0172 -0.0343 50  LEU D O     
4952  C CB    . LEU D 48  ? 0.6553 0.5744 0.6076 -0.0398 -0.0040 -0.0478 50  LEU D CB    
4953  C CG    . LEU D 48  ? 0.6601 0.5855 0.6105 -0.0352 0.0000  -0.0520 50  LEU D CG    
4954  C CD1   . LEU D 48  ? 0.6275 0.5623 0.5762 -0.0358 0.0093  -0.0498 50  LEU D CD1   
4955  C CD2   . LEU D 48  ? 0.6789 0.5999 0.6293 -0.0366 -0.0014 -0.0508 50  LEU D CD2   
4956  N N     . LYS D 49  ? 0.6942 0.5974 0.6536 -0.0456 -0.0210 -0.0439 51  LYS D N     
4957  C CA    . LYS D 49  ? 0.7705 0.6708 0.7326 -0.0514 -0.0241 -0.0379 51  LYS D CA    
4958  C C     . LYS D 49  ? 0.7746 0.6639 0.7417 -0.0549 -0.0356 -0.0348 51  LYS D C     
4959  O O     . LYS D 49  ? 0.8638 0.7521 0.8331 -0.0622 -0.0370 -0.0260 51  LYS D O     
4960  C CB    . LYS D 49  ? 0.7938 0.6968 0.7561 -0.0483 -0.0246 -0.0420 51  LYS D CB    
4961  C CG    . LYS D 49  ? 0.8066 0.7209 0.7647 -0.0456 -0.0140 -0.0434 51  LYS D CG    
4962  C CD    . LYS D 49  ? 0.8597 0.7780 0.8181 -0.0426 -0.0145 -0.0470 51  LYS D CD    
4963  C CE    . LYS D 49  ? 0.8445 0.7738 0.7994 -0.0406 -0.0045 -0.0470 51  LYS D CE    
4964  N NZ    . LYS D 49  ? 0.8360 0.7701 0.7910 -0.0377 -0.0049 -0.0500 51  LYS D NZ    
4965  N N     . THR D 50  ? 0.7630 0.6448 0.7324 -0.0495 -0.0441 -0.0421 52  THR D N     
4966  C CA    . THR D 50  ? 0.7796 0.6491 0.7548 -0.0520 -0.0566 -0.0400 52  THR D CA    
4967  C C     . THR D 50  ? 0.7610 0.6304 0.7360 -0.0579 -0.0546 -0.0316 52  THR D C     
4968  O O     . THR D 50  ? 0.7366 0.6003 0.7162 -0.0647 -0.0615 -0.0233 52  THR D O     
4969  C CB    . THR D 50  ? 0.7970 0.6602 0.7739 -0.0434 -0.0652 -0.0511 52  THR D CB    
4970  O OG1   . THR D 50  ? 0.8339 0.6987 0.8118 -0.0387 -0.0679 -0.0579 52  THR D OG1   
4971  C CG2   . THR D 50  ? 0.8497 0.6989 0.8332 -0.0453 -0.0789 -0.0494 52  THR D CG2   
4972  N N     . LEU D 51  ? 0.7760 0.6526 0.7459 -0.0553 -0.0454 -0.0335 53  LEU D N     
4973  C CA    . LEU D 51  ? 0.7742 0.6521 0.7433 -0.0595 -0.0431 -0.0271 53  LEU D CA    
4974  C C     . LEU D 51  ? 0.7714 0.6579 0.7392 -0.0667 -0.0361 -0.0176 53  LEU D C     
4975  O O     . LEU D 51  ? 0.7075 0.5965 0.6755 -0.0715 -0.0355 -0.0106 53  LEU D O     
4976  C CB    . LEU D 51  ? 0.7795 0.6621 0.7441 -0.0539 -0.0364 -0.0332 53  LEU D CB    
4977  C CG    . LEU D 51  ? 0.8209 0.6970 0.7867 -0.0468 -0.0436 -0.0419 53  LEU D CG    
4978  C CD1   . LEU D 51  ? 0.7507 0.6339 0.7123 -0.0423 -0.0362 -0.0465 53  LEU D CD1   
4979  C CD2   . LEU D 51  ? 0.8566 0.7210 0.8277 -0.0496 -0.0555 -0.0384 53  LEU D CD2   
4980  N N     . SER D 52  ? 0.7868 0.6789 0.7532 -0.0669 -0.0311 -0.0179 54  SER D N     
4981  C CA    . SER D 52  ? 0.8218 0.7234 0.7870 -0.0726 -0.0248 -0.0101 54  SER D CA    
4982  C C     . SER D 52  ? 0.8163 0.7155 0.7863 -0.0786 -0.0320 -0.0033 54  SER D C     
4983  O O     . SER D 52  ? 0.7953 0.7034 0.7651 -0.0838 -0.0283 0.0039  54  SER D O     
4984  C CB    . SER D 52  ? 0.7923 0.7024 0.7531 -0.0692 -0.0146 -0.0140 54  SER D CB    
4985  O OG    . SER D 52  ? 0.8137 0.7337 0.7733 -0.0737 -0.0087 -0.0076 54  SER D OG    
4986  N N     . GLY D 53  ? 0.8592 0.7469 0.8339 -0.0775 -0.0428 -0.0059 55  GLY D N     
4987  C CA    . GLY D 53  ? 0.8401 0.7233 0.8210 -0.0837 -0.0520 0.0008  55  GLY D CA    
4988  C C     . GLY D 53  ? 0.8423 0.7288 0.8229 -0.0830 -0.0497 -0.0013 55  GLY D C     
4989  O O     . GLY D 53  ? 0.8892 0.7702 0.8753 -0.0864 -0.0584 0.0016  55  GLY D O     
4990  N N     . ASP D 54  ? 0.8339 0.7292 0.8084 -0.0786 -0.0386 -0.0062 56  ASP D N     
4991  C CA    . ASP D 54  ? 0.8826 0.7827 0.8562 -0.0777 -0.0352 -0.0078 56  ASP D CA    
4992  C C     . ASP D 54  ? 0.8635 0.7584 0.8368 -0.0698 -0.0378 -0.0187 56  ASP D C     
4993  O O     . ASP D 54  ? 0.8176 0.7180 0.7863 -0.0640 -0.0302 -0.0249 56  ASP D O     
4994  C CB    . ASP D 54  ? 0.9357 0.8487 0.9041 -0.0779 -0.0228 -0.0060 56  ASP D CB    
4995  C CG    . ASP D 54  ? 0.9840 0.9057 0.9525 -0.0847 -0.0199 0.0038  56  ASP D CG    
4996  O OD1   . ASP D 54  ? 1.0466 0.9651 1.0192 -0.0901 -0.0272 0.0105  56  ASP D OD1   
4997  O OD2   . ASP D 54  ? 0.8982 0.8306 0.8631 -0.0843 -0.0109 0.0046  56  ASP D OD2   
4998  N N     . SER D 55  ? 0.7637 0.6490 0.7425 -0.0697 -0.0493 -0.0208 57  SER D N     
4999  C CA    . SER D 55  ? 0.7626 0.6444 0.7416 -0.0616 -0.0534 -0.0318 57  SER D CA    
5000  C C     . SER D 55  ? 0.7758 0.6692 0.7492 -0.0572 -0.0423 -0.0359 57  SER D C     
5001  O O     . SER D 55  ? 0.8615 0.7590 0.8353 -0.0599 -0.0404 -0.0329 57  SER D O     
5002  C CB    . SER D 55  ? 0.7556 0.6285 0.7415 -0.0633 -0.0658 -0.0323 57  SER D CB    
5003  O OG    . SER D 55  ? 0.7565 0.6179 0.7488 -0.0678 -0.0772 -0.0277 57  SER D OG    
5004  N N     . ALA D 60  ? 0.8283 0.7760 0.7924 -0.0461 -0.0146 -0.0443 62  ALA D N     
5005  C CA    . ALA D 60  ? 0.8009 0.7591 0.7624 -0.0405 -0.0101 -0.0484 62  ALA D CA    
5006  C C     . ALA D 60  ? 0.7845 0.7510 0.7423 -0.0418 0.0011  -0.0428 62  ALA D C     
5007  O O     . ALA D 60  ? 0.7586 0.7260 0.7166 -0.0468 0.0042  -0.0367 62  ALA D O     
5008  C CB    . ALA D 60  ? 0.7677 0.7259 0.7322 -0.0410 -0.0157 -0.0499 62  ALA D CB    
5009  N N     . LEU D 61  ? 0.8091 0.7823 0.7642 -0.0372 0.0065  -0.0451 63  LEU D N     
5010  C CA    . LEU D 61  ? 0.8232 0.8032 0.7758 -0.0379 0.0159  -0.0403 63  LEU D CA    
5011  C C     . LEU D 61  ? 0.7481 0.7377 0.7000 -0.0354 0.0189  -0.0403 63  LEU D C     
5012  O O     . LEU D 61  ? 0.7996 0.7951 0.7502 -0.0357 0.0257  -0.0363 63  LEU D O     
5013  C CB    . LEU D 61  ? 0.8460 0.8289 0.7970 -0.0348 0.0193  -0.0416 63  LEU D CB    
5014  C CG    . LEU D 61  ? 0.9801 0.9548 0.9314 -0.0377 0.0184  -0.0402 63  LEU D CG    
5015  C CD1   . LEU D 61  ? 1.0233 1.0024 0.9732 -0.0372 0.0254  -0.0375 63  LEU D CD1   
5016  C CD2   . LEU D 61  ? 0.9696 0.9370 0.9222 -0.0440 0.0167  -0.0354 63  LEU D CD2   
5017  N N     . VAL D 62  ? 0.7125 0.7033 0.6656 -0.0329 0.0132  -0.0450 64  VAL D N     
5018  C CA    . VAL D 62  ? 0.6913 0.6923 0.6437 -0.0297 0.0154  -0.0461 64  VAL D CA    
5019  C C     . VAL D 62  ? 0.6533 0.6534 0.6062 -0.0345 0.0174  -0.0407 64  VAL D C     
5020  O O     . VAL D 62  ? 0.5460 0.5392 0.5012 -0.0384 0.0122  -0.0400 64  VAL D O     
5021  C CB    . VAL D 62  ? 0.7046 0.7081 0.6582 -0.0242 0.0077  -0.0545 64  VAL D CB    
5022  C CG1   . VAL D 62  ? 0.7074 0.7242 0.6599 -0.0199 0.0101  -0.0561 64  VAL D CG1   
5023  C CG2   . VAL D 62  ? 0.7283 0.7323 0.6816 -0.0192 0.0043  -0.0608 64  VAL D CG2   
5024  N N     . ILE D 63  ? 0.6756 0.6831 0.6270 -0.0343 0.0245  -0.0365 65  ILE D N     
5025  C CA    . ILE D 63  ? 0.6176 0.6258 0.5694 -0.0381 0.0270  -0.0317 65  ILE D CA    
5026  C C     . ILE D 63  ? 0.6063 0.6251 0.5572 -0.0347 0.0304  -0.0314 65  ILE D C     
5027  O O     . ILE D 63  ? 0.6075 0.6290 0.5583 -0.0365 0.0345  -0.0269 65  ILE D O     
5028  C CB    . ILE D 63  ? 0.5679 0.5732 0.5192 -0.0418 0.0320  -0.0262 65  ILE D CB    
5029  C CG1   . ILE D 63  ? 0.5573 0.5573 0.5083 -0.0419 0.0321  -0.0268 65  ILE D CG1   
5030  C CG2   . ILE D 63  ? 0.5824 0.5850 0.5348 -0.0470 0.0306  -0.0227 65  ILE D CG2   
5031  C CD1   . ILE D 63  ? 0.5371 0.5357 0.4877 -0.0443 0.0370  -0.0225 65  ILE D CD1   
5032  N N     . SER D 64  ? 0.6217 0.6475 0.5723 -0.0295 0.0283  -0.0363 66  SER D N     
5033  C CA    . SER D 64  ? 0.5585 0.5963 0.5083 -0.0260 0.0315  -0.0356 66  SER D CA    
5034  C C     . SER D 64  ? 0.5814 0.6270 0.5310 -0.0203 0.0266  -0.0429 66  SER D C     
5035  O O     . SER D 64  ? 0.5933 0.6363 0.5433 -0.0178 0.0218  -0.0486 66  SER D O     
5036  C CB    . SER D 64  ? 0.5294 0.5735 0.4784 -0.0251 0.0379  -0.0307 66  SER D CB    
5037  O OG    . SER D 64  ? 0.5285 0.5745 0.4771 -0.0225 0.0374  -0.0330 66  SER D OG    
5038  N N     . HIS D 65  ? 0.5388 0.5948 0.4881 -0.0177 0.0277  -0.0430 67  HIS D N     
5039  C CA    . HIS D 65  ? 0.6448 0.7118 0.5938 -0.0112 0.0237  -0.0502 67  HIS D CA    
5040  C C     . HIS D 65  ? 0.6279 0.7122 0.5756 -0.0077 0.0293  -0.0466 67  HIS D C     
5041  O O     . HIS D 65  ? 0.6118 0.6971 0.5593 -0.0107 0.0354  -0.0386 67  HIS D O     
5042  C CB    . HIS D 65  ? 0.6770 0.7396 0.6279 -0.0114 0.0168  -0.0552 67  HIS D CB    
5043  C CG    . HIS D 65  ? 0.7379 0.7981 0.6893 -0.0162 0.0194  -0.0496 67  HIS D CG    
5044  N ND1   . HIS D 65  ? 0.7741 0.8458 0.7244 -0.0146 0.0241  -0.0464 67  HIS D ND1   
5045  C CD2   . HIS D 65  ? 0.8161 0.8651 0.7693 -0.0225 0.0178  -0.0463 67  HIS D CD2   
5046  C CE1   . HIS D 65  ? 0.8614 0.9282 0.8125 -0.0193 0.0252  -0.0421 67  HIS D CE1   
5047  N NE2   . HIS D 65  ? 0.8297 0.8837 0.7825 -0.0242 0.0215  -0.0419 67  HIS D NE2   
5048  N N     . GLY D 66  ? 0.6449 0.7432 0.5920 -0.0012 0.0264  -0.0528 68  GLY D N     
5049  C CA    . GLY D 66  ? 0.6101 0.7277 0.5560 0.0024  0.0311  -0.0492 68  GLY D CA    
5050  C C     . GLY D 66  ? 0.6257 0.7561 0.5713 0.0083  0.0270  -0.0562 68  GLY D C     
5051  O O     . GLY D 66  ? 0.4962 0.6466 0.4408 0.0140  0.0283  -0.0572 68  GLY D O     
5052  N N     . ASN D 67  ? 0.6279 0.7476 0.5748 0.0069  0.0218  -0.0608 69  ASN D N     
5053  C CA    . ASN D 67  ? 0.6396 0.7694 0.5869 0.0121  0.0171  -0.0680 69  ASN D CA    
5054  C C     . ASN D 67  ? 0.6152 0.7486 0.5622 0.0093  0.0214  -0.0615 69  ASN D C     
5055  O O     . ASN D 67  ? 0.5846 0.7222 0.5324 0.0116  0.0175  -0.0663 69  ASN D O     
5056  C CB    . ASN D 67  ? 0.6492 0.7658 0.5992 0.0125  0.0071  -0.0774 69  ASN D CB    
5057  C CG    . ASN D 67  ? 0.6565 0.7700 0.6071 0.0164  0.0017  -0.0850 69  ASN D CG    
5058  O OD1   . ASN D 67  ? 0.7125 0.8335 0.6611 0.0182  0.0061  -0.0827 69  ASN D OD1   
5059  N ND2   . ASN D 67  ? 0.7312 0.8336 0.6850 0.0177  -0.0085 -0.0938 69  ASN D ND2   
5060  N N     . GLY D 68  ? 0.6401 0.7718 0.5866 0.0046  0.0288  -0.0510 70  GLY D N     
5061  C CA    . GLY D 68  ? 0.6593 0.7934 0.6058 0.0020  0.0329  -0.0445 70  GLY D CA    
5062  C C     . GLY D 68  ? 0.6282 0.7446 0.5760 -0.0048 0.0325  -0.0417 70  GLY D C     
5063  O O     . GLY D 68  ? 0.6553 0.7587 0.6036 -0.0085 0.0319  -0.0409 70  GLY D O     
5064  N N     . GLY E 1   ? 0.5304 0.5411 0.5448 -0.0398 0.0208  -0.0516 2   GLY E N     
5065  C CA    . GLY E 1   ? 0.4975 0.5052 0.5083 -0.0410 0.0234  -0.0501 2   GLY E CA    
5066  C C     . GLY E 1   ? 0.4798 0.4867 0.4901 -0.0400 0.0248  -0.0492 2   GLY E C     
5067  O O     . GLY E 1   ? 0.4882 0.4981 0.5020 -0.0390 0.0247  -0.0502 2   GLY E O     
5068  N N     . SER E 2   ? 0.4152 0.4183 0.4212 -0.0402 0.0260  -0.0475 3   SER E N     
5069  C CA    . SER E 2   ? 0.4272 0.4292 0.4323 -0.0394 0.0272  -0.0466 3   SER E CA    
5070  C C     . SER E 2   ? 0.4186 0.4179 0.4205 -0.0407 0.0294  -0.0453 3   SER E C     
5071  O O     . SER E 2   ? 0.3593 0.3574 0.3594 -0.0418 0.0298  -0.0451 3   SER E O     
5072  C CB    . SER E 2   ? 0.4599 0.4597 0.4630 -0.0376 0.0252  -0.0458 3   SER E CB    
5073  O OG    . SER E 2   ? 0.4794 0.4760 0.4781 -0.0378 0.0244  -0.0444 3   SER E OG    
5074  N N     . LEU E 3   ? 0.3893 0.3878 0.3906 -0.0403 0.0308  -0.0445 4   LEU E N     
5075  C CA    . LEU E 3   ? 0.3745 0.3706 0.3730 -0.0413 0.0327  -0.0433 4   LEU E CA    
5076  C C     . LEU E 3   ? 0.3613 0.3550 0.3573 -0.0402 0.0326  -0.0419 4   LEU E C     
5077  O O     . LEU E 3   ? 0.3906 0.3849 0.3880 -0.0390 0.0320  -0.0422 4   LEU E O     
5078  C CB    . LEU E 3   ? 0.4119 0.4098 0.4125 -0.0425 0.0349  -0.0439 4   LEU E CB    
5079  C CG    . LEU E 3   ? 0.4316 0.4270 0.4295 -0.0434 0.0368  -0.0427 4   LEU E CG    
5080  C CD1   . LEU E 3   ? 0.4660 0.4590 0.4613 -0.0442 0.0367  -0.0422 4   LEU E CD1   
5081  C CD2   . LEU E 3   ? 0.4320 0.4290 0.4315 -0.0446 0.0387  -0.0431 4   LEU E CD2   
5082  N N     . VAL E 4   ? 0.3515 0.3426 0.3442 -0.0406 0.0330  -0.0406 5   VAL E N     
5083  C CA    . VAL E 4   ? 0.3817 0.3707 0.3721 -0.0400 0.0332  -0.0392 5   VAL E CA    
5084  C C     . VAL E 4   ? 0.3918 0.3794 0.3803 -0.0409 0.0350  -0.0385 5   VAL E C     
5085  O O     . VAL E 4   ? 0.4251 0.4120 0.4119 -0.0415 0.0352  -0.0384 5   VAL E O     
5086  C CB    . VAL E 4   ? 0.3741 0.3615 0.3620 -0.0394 0.0314  -0.0382 5   VAL E CB    
5087  C CG1   . VAL E 4   ? 0.4111 0.3964 0.3967 -0.0393 0.0318  -0.0365 5   VAL E CG1   
5088  C CG2   . VAL E 4   ? 0.3830 0.3711 0.3726 -0.0383 0.0292  -0.0388 5   VAL E CG2   
5089  N N     . CYS E 5   ? 0.3651 0.3524 0.3539 -0.0410 0.0363  -0.0382 6   CYS E N     
5090  C CA    . CYS E 5   ? 0.3605 0.3464 0.3475 -0.0417 0.0378  -0.0375 6   CYS E CA    
5091  C C     . CYS E 5   ? 0.3176 0.3019 0.3025 -0.0412 0.0375  -0.0361 6   CYS E C     
5092  O O     . CYS E 5   ? 0.2768 0.2608 0.2621 -0.0406 0.0368  -0.0357 6   CYS E O     
5093  C CB    . CYS E 5   ? 0.4017 0.3881 0.3900 -0.0422 0.0392  -0.0379 6   CYS E CB    
5094  S SG    . CYS E 5   ? 0.5088 0.4974 0.4995 -0.0433 0.0398  -0.0393 6   CYS E SG    
5095  N N     . VAL E 6   ? 0.3192 0.3027 0.3021 -0.0415 0.0380  -0.0354 7   VAL E N     
5096  C CA    . VAL E 6   ? 0.3264 0.3089 0.3074 -0.0413 0.0379  -0.0341 7   VAL E CA    
5097  C C     . VAL E 6   ? 0.3154 0.2974 0.2955 -0.0415 0.0392  -0.0338 7   VAL E C     
5098  O O     . VAL E 6   ? 0.2784 0.2601 0.2587 -0.0418 0.0400  -0.0346 7   VAL E O     
5099  C CB    . VAL E 6   ? 0.3440 0.3267 0.3233 -0.0412 0.0369  -0.0336 7   VAL E CB    
5100  C CG1   . VAL E 6   ? 0.3338 0.3169 0.3139 -0.0408 0.0352  -0.0339 7   VAL E CG1   
5101  C CG2   . VAL E 6   ? 0.3668 0.3498 0.3449 -0.0413 0.0375  -0.0343 7   VAL E CG2   
5102  N N     . GLY E 7   ? 0.2800 0.2617 0.2592 -0.0415 0.0393  -0.0327 8   GLY E N     
5103  C CA    . GLY E 7   ? 0.2932 0.2746 0.2715 -0.0415 0.0403  -0.0325 8   GLY E CA    
5104  C C     . GLY E 7   ? 0.2990 0.2813 0.2758 -0.0414 0.0404  -0.0319 8   GLY E C     
5105  O O     . GLY E 7   ? 0.3185 0.3013 0.2946 -0.0416 0.0397  -0.0312 8   GLY E O     
5106  N N     . THR E 8   ? 0.3102 0.2927 0.2864 -0.0411 0.0412  -0.0323 9   THR E N     
5107  C CA    . THR E 8   ? 0.3499 0.3339 0.3248 -0.0409 0.0415  -0.0321 9   THR E CA    
5108  C C     . THR E 8   ? 0.3929 0.3778 0.3681 -0.0408 0.0421  -0.0314 9   THR E C     
5109  O O     . THR E 8   ? 0.4387 0.4254 0.4133 -0.0405 0.0427  -0.0314 9   THR E O     
5110  C CB    . THR E 8   ? 0.3368 0.3207 0.3109 -0.0403 0.0417  -0.0335 9   THR E CB    
5111  O OG1   . THR E 8   ? 0.2912 0.2738 0.2660 -0.0400 0.0421  -0.0341 9   THR E OG1   
5112  C CG2   . THR E 8   ? 0.3482 0.3315 0.3223 -0.0405 0.0410  -0.0342 9   THR E CG2   
5113  N N     . GLY E 9   ? 0.4550 0.4388 0.4313 -0.0410 0.0420  -0.0310 10  GLY E N     
5114  C CA    . GLY E 9   ? 0.4316 0.4160 0.4085 -0.0409 0.0424  -0.0304 10  GLY E CA    
5115  C C     . GLY E 9   ? 0.4284 0.4128 0.4051 -0.0400 0.0429  -0.0314 10  GLY E C     
5116  O O     . GLY E 9   ? 0.4631 0.4463 0.4393 -0.0396 0.0430  -0.0325 10  GLY E O     
5117  N N     . LEU E 10  ? 0.4501 0.4358 0.4273 -0.0397 0.0432  -0.0312 11  LEU E N     
5118  C CA    . LEU E 10  ? 0.4501 0.4356 0.4274 -0.0385 0.0434  -0.0322 11  LEU E CA    
5119  C C     . LEU E 10  ? 0.3905 0.3790 0.3677 -0.0377 0.0440  -0.0328 11  LEU E C     
5120  O O     . LEU E 10  ? 0.3860 0.3742 0.3628 -0.0365 0.0440  -0.0341 11  LEU E O     
5121  C CB    . LEU E 10  ? 0.5203 0.5050 0.4984 -0.0383 0.0431  -0.0318 11  LEU E CB    
5122  C CG    . LEU E 10  ? 0.4978 0.4791 0.4752 -0.0382 0.0428  -0.0322 11  LEU E CG    
5123  C CD1   . LEU E 10  ? 0.5517 0.5316 0.5287 -0.0391 0.0428  -0.0321 11  LEU E CD1   
5124  C CD2   . LEU E 10  ? 0.4748 0.4551 0.4526 -0.0382 0.0423  -0.0316 11  LEU E CD2   
5125  N N     . GLN E 11  ? 0.4176 0.4091 0.3951 -0.0385 0.0443  -0.0319 12  GLN E N     
5126  C CA    . GLN E 11  ? 0.4693 0.4643 0.4465 -0.0380 0.0451  -0.0324 12  GLN E CA    
5127  C C     . GLN E 11  ? 0.4917 0.4865 0.4671 -0.0379 0.0452  -0.0330 12  GLN E C     
5128  O O     . GLN E 11  ? 0.5112 0.5038 0.4858 -0.0387 0.0447  -0.0326 12  GLN E O     
5129  C CB    . GLN E 11  ? 0.4500 0.4484 0.4281 -0.0392 0.0456  -0.0309 12  GLN E CB    
5130  C CG    . GLN E 11  ? 0.4842 0.4846 0.4644 -0.0387 0.0457  -0.0310 12  GLN E CG    
5131  C CD    . GLN E 11  ? 0.4887 0.4921 0.4695 -0.0370 0.0464  -0.0327 12  GLN E CD    
5132  O OE1   . GLN E 11  ? 0.3798 0.3838 0.3591 -0.0362 0.0469  -0.0338 12  GLN E OE1   
5133  N NE2   . GLN E 11  ? 0.5525 0.5580 0.5354 -0.0363 0.0464  -0.0330 12  GLN E NE2   
5134  N N     . LEU E 12  ? 0.5284 0.5257 0.5031 -0.0369 0.0459  -0.0342 13  LEU E N     
5135  C CA    . LEU E 12  ? 0.4740 0.4711 0.4467 -0.0365 0.0459  -0.0352 13  LEU E CA    
5136  C C     . LEU E 12  ? 0.4072 0.4062 0.3785 -0.0379 0.0462  -0.0338 13  LEU E C     
5137  O O     . LEU E 12  ? 0.4194 0.4220 0.3907 -0.0385 0.0471  -0.0331 13  LEU E O     
5138  C CB    . LEU E 12  ? 0.4506 0.4496 0.4230 -0.0346 0.0464  -0.0372 13  LEU E CB    
5139  C CG    . LEU E 12  ? 0.3878 0.3876 0.3578 -0.0340 0.0466  -0.0385 13  LEU E CG    
5140  C CD1   . LEU E 12  ? 0.3555 0.3510 0.3243 -0.0341 0.0454  -0.0391 13  LEU E CD1   
5141  C CD2   . LEU E 12  ? 0.3754 0.3777 0.3453 -0.0320 0.0472  -0.0406 13  LEU E CD2   
5142  N N     . ALA E 13  ? 0.3842 0.3807 0.3544 -0.0386 0.0453  -0.0334 14  ALA E N     
5143  C CA    . ALA E 13  ? 0.4048 0.4022 0.3729 -0.0396 0.0452  -0.0325 14  ALA E CA    
5144  C C     . ALA E 13  ? 0.4142 0.4122 0.3826 -0.0413 0.0450  -0.0302 14  ALA E C     
5145  O O     . ALA E 13  ? 0.4354 0.4324 0.4023 -0.0423 0.0442  -0.0291 14  ALA E O     
5146  C CB    . ALA E 13  ? 0.4307 0.4314 0.3970 -0.0388 0.0462  -0.0336 14  ALA E CB    
5147  N N     . GLY E 14  ? 0.4231 0.4226 0.3934 -0.0416 0.0456  -0.0295 15  GLY E N     
5148  C CA    . GLY E 14  ? 0.4168 0.4173 0.3872 -0.0434 0.0455  -0.0273 15  GLY E CA    
5149  C C     . GLY E 14  ? 0.4143 0.4115 0.3861 -0.0441 0.0443  -0.0263 15  GLY E C     
5150  O O     . GLY E 14  ? 0.3755 0.3721 0.3469 -0.0456 0.0436  -0.0245 15  GLY E O     
5151  N N     . GLN E 15  ? 0.4266 0.4216 0.3998 -0.0430 0.0440  -0.0275 16  GLN E N     
5152  C CA    . GLN E 15  ? 0.4154 0.4079 0.3900 -0.0434 0.0431  -0.0268 16  GLN E CA    
5153  C C     . GLN E 15  ? 0.4391 0.4286 0.4133 -0.0433 0.0420  -0.0270 16  GLN E C     
5154  O O     . GLN E 15  ? 0.5102 0.4976 0.4854 -0.0433 0.0413  -0.0270 16  GLN E O     
5155  C CB    . GLN E 15  ? 0.3837 0.3760 0.3599 -0.0424 0.0435  -0.0278 16  GLN E CB    
5156  C CG    . GLN E 15  ? 0.4260 0.4168 0.4035 -0.0430 0.0428  -0.0270 16  GLN E CG    
5157  C CD    . GLN E 15  ? 0.4286 0.4197 0.4074 -0.0421 0.0431  -0.0278 16  GLN E CD    
5158  O OE1   . GLN E 15  ? 0.4988 0.4884 0.4775 -0.0410 0.0432  -0.0290 16  GLN E OE1   
5159  N NE2   . GLN E 15  ? 0.4371 0.4301 0.4172 -0.0427 0.0431  -0.0270 16  GLN E NE2   
5160  N N     . ILE E 16  ? 0.3605 0.3500 0.3331 -0.0431 0.0418  -0.0274 17  ILE E N     
5161  C CA    . ILE E 16  ? 0.3385 0.3258 0.3110 -0.0431 0.0406  -0.0276 17  ILE E CA    
5162  C C     . ILE E 16  ? 0.3232 0.3097 0.2946 -0.0441 0.0394  -0.0259 17  ILE E C     
5163  O O     . ILE E 16  ? 0.2933 0.2814 0.2634 -0.0450 0.0397  -0.0247 17  ILE E O     
5164  C CB    . ILE E 16  ? 0.3479 0.3353 0.3193 -0.0423 0.0406  -0.0290 17  ILE E CB    
5165  C CG1   . ILE E 16  ? 0.3657 0.3511 0.3376 -0.0422 0.0394  -0.0295 17  ILE E CG1   
5166  C CG2   . ILE E 16  ? 0.3523 0.3415 0.3213 -0.0426 0.0408  -0.0286 17  ILE E CG2   
5167  C CD1   . ILE E 16  ? 0.3931 0.3786 0.3644 -0.0416 0.0392  -0.0310 17  ILE E CD1   
5168  N N     A SER E 17  ? 0.3293 0.3135 0.3015 -0.0440 0.0381  -0.0259 18  SER E N     
5169  N N     B SER E 17  ? 0.3111 0.2953 0.2832 -0.0440 0.0381  -0.0259 18  SER E N     
5170  C CA    A SER E 17  ? 0.3550 0.3378 0.3262 -0.0447 0.0365  -0.0244 18  SER E CA    
5171  C CA    B SER E 17  ? 0.3221 0.3048 0.2933 -0.0447 0.0365  -0.0244 18  SER E CA    
5172  C C     A SER E 17  ? 0.3435 0.3266 0.3124 -0.0449 0.0359  -0.0241 18  SER E C     
5173  C C     B SER E 17  ? 0.3261 0.3092 0.2949 -0.0449 0.0359  -0.0241 18  SER E C     
5174  O O     A SER E 17  ? 0.3432 0.3272 0.3117 -0.0441 0.0364  -0.0255 18  SER E O     
5175  O O     B SER E 17  ? 0.3259 0.3098 0.2944 -0.0441 0.0364  -0.0255 18  SER E O     
5176  C CB    A SER E 17  ? 0.3826 0.3630 0.3553 -0.0441 0.0352  -0.0249 18  SER E CB    
5177  C CB    B SER E 17  ? 0.3242 0.3046 0.2970 -0.0441 0.0352  -0.0249 18  SER E CB    
5178  O OG    A SER E 17  ? 0.4153 0.3954 0.3898 -0.0440 0.0357  -0.0253 18  SER E OG    
5179  O OG    B SER E 17  ? 0.3121 0.2924 0.2855 -0.0431 0.0348  -0.0264 18  SER E OG    
5180  N N     . VAL E 18  ? 0.3256 0.3077 0.2926 -0.0459 0.0348  -0.0223 19  VAL E N     
5181  C CA    . VAL E 18  ? 0.3431 0.3252 0.3073 -0.0463 0.0340  -0.0216 19  VAL E CA    
5182  C C     . VAL E 18  ? 0.3804 0.3611 0.3451 -0.0450 0.0326  -0.0230 19  VAL E C     
5183  O O     . VAL E 18  ? 0.3865 0.3681 0.3499 -0.0445 0.0326  -0.0239 19  VAL E O     
5184  C CB    . VAL E 18  ? 0.3714 0.3520 0.3333 -0.0478 0.0328  -0.0191 19  VAL E CB    
5185  C CG1   . VAL E 18  ? 0.4080 0.3882 0.3665 -0.0482 0.0317  -0.0183 19  VAL E CG1   
5186  C CG2   . VAL E 18  ? 0.3538 0.3365 0.3155 -0.0494 0.0343  -0.0177 19  VAL E CG2   
5187  N N     . LEU E 19  ? 0.3657 0.3444 0.3325 -0.0443 0.0313  -0.0234 20  LEU E N     
5188  C CA    . LEU E 19  ? 0.3665 0.3443 0.3345 -0.0431 0.0298  -0.0248 20  LEU E CA    
5189  C C     . LEU E 19  ? 0.3497 0.3294 0.3195 -0.0423 0.0312  -0.0269 20  LEU E C     
5190  O O     . LEU E 19  ? 0.3578 0.3379 0.3275 -0.0418 0.0305  -0.0280 20  LEU E O     
5191  C CB    . LEU E 19  ? 0.3674 0.3431 0.3374 -0.0425 0.0283  -0.0248 20  LEU E CB    
5192  C CG    . LEU E 19  ? 0.3826 0.3579 0.3544 -0.0411 0.0267  -0.0264 20  LEU E CG    
5193  C CD1   . LEU E 19  ? 0.4099 0.3841 0.3794 -0.0410 0.0246  -0.0258 20  LEU E CD1   
5194  C CD2   . LEU E 19  ? 0.3925 0.3661 0.3665 -0.0403 0.0255  -0.0269 20  LEU E CD2   
5195  N N     . SER E 20  ? 0.3372 0.3178 0.3086 -0.0424 0.0329  -0.0275 21  SER E N     
5196  C CA    . SER E 20  ? 0.3628 0.3445 0.3357 -0.0418 0.0341  -0.0293 21  SER E CA    
5197  C C     . SER E 20  ? 0.3929 0.3759 0.3640 -0.0419 0.0347  -0.0298 21  SER E C     
5198  O O     . SER E 20  ? 0.4009 0.3843 0.3727 -0.0414 0.0347  -0.0313 21  SER E O     
5199  C CB    . SER E 20  ? 0.3472 0.3292 0.3216 -0.0419 0.0356  -0.0295 21  SER E CB    
5200  O OG    . SER E 20  ? 0.3771 0.3580 0.3533 -0.0416 0.0351  -0.0297 21  SER E OG    
5201  N N     . ARG E 21  ? 0.4069 0.3906 0.3755 -0.0424 0.0353  -0.0287 22  ARG E N     
5202  C CA    . ARG E 21  ? 0.3856 0.3707 0.3521 -0.0423 0.0358  -0.0292 22  ARG E CA    
5203  C C     . ARG E 21  ? 0.3451 0.3295 0.3101 -0.0421 0.0341  -0.0295 22  ARG E C     
5204  O O     . ARG E 21  ? 0.3241 0.3090 0.2883 -0.0416 0.0341  -0.0309 22  ARG E O     
5205  C CB    . ARG E 21  ? 0.4398 0.4264 0.4041 -0.0431 0.0369  -0.0278 22  ARG E CB    
5206  C CG    . ARG E 21  ? 0.4641 0.4527 0.4260 -0.0428 0.0378  -0.0286 22  ARG E CG    
5207  C CD    . ARG E 21  ? 0.5107 0.5016 0.4709 -0.0436 0.0391  -0.0273 22  ARG E CD    
5208  N NE    . ARG E 21  ? 0.5075 0.5007 0.4655 -0.0431 0.0402  -0.0284 22  ARG E NE    
5209  C CZ    . ARG E 21  ? 0.5904 0.5838 0.5454 -0.0429 0.0396  -0.0288 22  ARG E CZ    
5210  N NH1   . ARG E 21  ? 0.5723 0.5636 0.5261 -0.0433 0.0377  -0.0279 22  ARG E NH1   
5211  N NH2   . ARG E 21  ? 0.6277 0.6234 0.5809 -0.0423 0.0407  -0.0300 22  ARG E NH2   
5212  N N     . SER E 22  ? 0.3422 0.3251 0.3068 -0.0424 0.0325  -0.0282 23  SER E N     
5213  C CA    . SER E 22  ? 0.3899 0.3720 0.3530 -0.0421 0.0304  -0.0283 23  SER E CA    
5214  C C     . SER E 22  ? 0.4155 0.3976 0.3813 -0.0412 0.0296  -0.0303 23  SER E C     
5215  O O     . SER E 22  ? 0.3722 0.3545 0.3370 -0.0408 0.0285  -0.0312 23  SER E O     
5216  C CB    . SER E 22  ? 0.4356 0.4157 0.3978 -0.0425 0.0286  -0.0264 23  SER E CB    
5217  O OG    . SER E 22  ? 0.4546 0.4337 0.4149 -0.0421 0.0264  -0.0263 23  SER E OG    
5218  N N     . TYR E 23  ? 0.3936 0.3759 0.3628 -0.0409 0.0303  -0.0311 24  TYR E N     
5219  C CA    . TYR E 23  ? 0.3676 0.3504 0.3397 -0.0404 0.0298  -0.0329 24  TYR E CA    
5220  C C     . TYR E 23  ? 0.3690 0.3527 0.3407 -0.0405 0.0308  -0.0344 24  TYR E C     
5221  O O     . TYR E 23  ? 0.3696 0.3537 0.3419 -0.0403 0.0298  -0.0356 24  TYR E O     
5222  C CB    . TYR E 23  ? 0.3776 0.3605 0.3530 -0.0403 0.0306  -0.0334 24  TYR E CB    
5223  C CG    . TYR E 23  ? 0.3622 0.3443 0.3392 -0.0397 0.0290  -0.0331 24  TYR E CG    
5224  C CD1   . TYR E 23  ? 0.3668 0.3496 0.3457 -0.0389 0.0274  -0.0343 24  TYR E CD1   
5225  C CD2   . TYR E 23  ? 0.3700 0.3508 0.3466 -0.0397 0.0290  -0.0318 24  TYR E CD2   
5226  C CE1   . TYR E 23  ? 0.3997 0.3818 0.3802 -0.0380 0.0257  -0.0343 24  TYR E CE1   
5227  C CE2   . TYR E 23  ? 0.4144 0.3941 0.3924 -0.0389 0.0272  -0.0317 24  TYR E CE2   
5228  C CZ    . TYR E 23  ? 0.4214 0.4018 0.4013 -0.0380 0.0256  -0.0331 24  TYR E CZ    
5229  O OH    . TYR E 23  ? 0.4448 0.4242 0.4261 -0.0369 0.0238  -0.0333 24  TYR E OH    
5230  N N     . ILE E 24  ? 0.3461 0.3301 0.3169 -0.0407 0.0326  -0.0342 25  ILE E N     
5231  C CA    . ILE E 24  ? 0.3779 0.3622 0.3481 -0.0407 0.0335  -0.0356 25  ILE E CA    
5232  C C     . ILE E 24  ? 0.3988 0.3834 0.3663 -0.0404 0.0323  -0.0361 25  ILE E C     
5233  O O     . ILE E 24  ? 0.3788 0.3633 0.3465 -0.0403 0.0318  -0.0376 25  ILE E O     
5234  C CB    . ILE E 24  ? 0.3819 0.3665 0.3514 -0.0407 0.0353  -0.0353 25  ILE E CB    
5235  C CG1   . ILE E 24  ? 0.3809 0.3651 0.3530 -0.0409 0.0363  -0.0351 25  ILE E CG1   
5236  C CG2   . ILE E 24  ? 0.3994 0.3841 0.3678 -0.0403 0.0358  -0.0369 25  ILE E CG2   
5237  C CD1   . ILE E 24  ? 0.3754 0.3596 0.3470 -0.0408 0.0378  -0.0349 25  ILE E CD1   
5238  N N     . GLU E 25  ? 0.4266 0.4113 0.3913 -0.0405 0.0320  -0.0346 26  GLU E N     
5239  C CA    . GLU E 25  ? 0.4625 0.4475 0.4237 -0.0404 0.0312  -0.0348 26  GLU E CA    
5240  C C     . GLU E 25  ? 0.4618 0.4462 0.4235 -0.0401 0.0289  -0.0357 26  GLU E C     
5241  O O     . GLU E 25  ? 0.4612 0.4457 0.4212 -0.0398 0.0282  -0.0370 26  GLU E O     
5242  C CB    . GLU E 25  ? 0.4956 0.4807 0.4536 -0.0409 0.0312  -0.0326 26  GLU E CB    
5243  C CG    . GLU E 25  ? 0.5861 0.5716 0.5398 -0.0409 0.0304  -0.0326 26  GLU E CG    
5244  C CD    . GLU E 25  ? 0.6714 0.6571 0.6217 -0.0418 0.0305  -0.0302 26  GLU E CD    
5245  O OE1   . GLU E 25  ? 0.7782 0.7635 0.7297 -0.0425 0.0309  -0.0285 26  GLU E OE1   
5246  O OE2   . GLU E 25  ? 0.7784 0.7645 0.7247 -0.0419 0.0300  -0.0299 26  GLU E OE2   
5247  N N     . HIS E 26  ? 0.5050 0.4888 0.4691 -0.0401 0.0276  -0.0352 27  HIS E N     
5248  C CA    . HIS E 26  ? 0.4799 0.4635 0.4448 -0.0396 0.0252  -0.0360 27  HIS E CA    
5249  C C     . HIS E 26  ? 0.4551 0.4396 0.4245 -0.0396 0.0252  -0.0378 27  HIS E C     
5250  O O     . HIS E 26  ? 0.4336 0.4185 0.4050 -0.0392 0.0233  -0.0386 27  HIS E O     
5251  C CB    . HIS E 26  ? 0.4993 0.4818 0.4637 -0.0394 0.0235  -0.0344 27  HIS E CB    
5252  C CG    . HIS E 26  ? 0.5242 0.5056 0.4838 -0.0398 0.0231  -0.0324 27  HIS E CG    
5253  N ND1   . HIS E 26  ? 0.5698 0.5507 0.5283 -0.0405 0.0241  -0.0304 27  HIS E ND1   
5254  C CD2   . HIS E 26  ? 0.5753 0.5563 0.5310 -0.0398 0.0218  -0.0321 27  HIS E CD2   
5255  C CE1   . HIS E 26  ? 0.5646 0.5448 0.5186 -0.0411 0.0236  -0.0288 27  HIS E CE1   
5256  N NE2   . HIS E 26  ? 0.5572 0.5375 0.5093 -0.0406 0.0223  -0.0298 27  HIS E NE2   
5257  N N     . ALA E 27  ? 0.4240 0.4088 0.3950 -0.0400 0.0272  -0.0384 28  ALA E N     
5258  C CA    . ALA E 27  ? 0.4109 0.3965 0.3858 -0.0403 0.0274  -0.0399 28  ALA E CA    
5259  C C     . ALA E 27  ? 0.3940 0.3798 0.3686 -0.0405 0.0264  -0.0416 28  ALA E C     
5260  O O     . ALA E 27  ? 0.4463 0.4314 0.4177 -0.0403 0.0265  -0.0419 28  ALA E O     
5261  C CB    . ALA E 27  ? 0.3751 0.3605 0.3511 -0.0408 0.0297  -0.0397 28  ALA E CB    
5262  N N     . ASP E 28  ? 0.3793 0.3663 0.3576 -0.0408 0.0255  -0.0428 29  ASP E N     
5263  C CA    . ASP E 28  ? 0.3802 0.3674 0.3590 -0.0413 0.0245  -0.0446 29  ASP E CA    
5264  C C     . ASP E 28  ? 0.3655 0.3516 0.3442 -0.0421 0.0262  -0.0452 29  ASP E C     
5265  O O     . ASP E 28  ? 0.3876 0.3726 0.3644 -0.0422 0.0256  -0.0463 29  ASP E O     
5266  C CB    . ASP E 28  ? 0.3903 0.3796 0.3735 -0.0417 0.0231  -0.0457 29  ASP E CB    
5267  C CG    . ASP E 28  ? 0.4622 0.4524 0.4455 -0.0406 0.0207  -0.0456 29  ASP E CG    
5268  O OD1   . ASP E 28  ? 0.4991 0.4878 0.4785 -0.0398 0.0198  -0.0445 29  ASP E OD1   
5269  O OD2   . ASP E 28  ? 0.5237 0.5161 0.5112 -0.0406 0.0196  -0.0466 29  ASP E OD2   
5270  N N     . ILE E 29  ? 0.3518 0.3379 0.3322 -0.0426 0.0280  -0.0445 30  ILE E N     
5271  C CA    . ILE E 29  ? 0.3306 0.3154 0.3110 -0.0434 0.0295  -0.0449 30  ILE E CA    
5272  C C     . ILE E 29  ? 0.3275 0.3119 0.3080 -0.0433 0.0314  -0.0435 30  ILE E C     
5273  O O     . ILE E 29  ? 0.3228 0.3085 0.3051 -0.0431 0.0316  -0.0428 30  ILE E O     
5274  C CB    . ILE E 29  ? 0.3655 0.3507 0.3490 -0.0448 0.0291  -0.0461 30  ILE E CB    
5275  C CG1   . ILE E 29  ? 0.3871 0.3700 0.3698 -0.0457 0.0301  -0.0465 30  ILE E CG1   
5276  C CG2   . ILE E 29  ? 0.3686 0.3563 0.3562 -0.0454 0.0297  -0.0458 30  ILE E CG2   
5277  C CD1   . ILE E 29  ? 0.4252 0.4081 0.4107 -0.0475 0.0296  -0.0475 30  ILE E CD1   
5278  N N     . VAL E 30  ? 0.3398 0.3224 0.3184 -0.0432 0.0326  -0.0434 31  VAL E N     
5279  C CA    . VAL E 30  ? 0.3629 0.3451 0.3414 -0.0430 0.0342  -0.0422 31  VAL E CA    
5280  C C     . VAL E 30  ? 0.3896 0.3701 0.3687 -0.0439 0.0351  -0.0426 31  VAL E C     
5281  O O     . VAL E 30  ? 0.3986 0.3774 0.3765 -0.0440 0.0348  -0.0435 31  VAL E O     
5282  C CB    . VAL E 30  ? 0.3779 0.3598 0.3533 -0.0419 0.0347  -0.0414 31  VAL E CB    
5283  C CG1   . VAL E 30  ? 0.4052 0.3868 0.3808 -0.0418 0.0362  -0.0403 31  VAL E CG1   
5284  C CG2   . VAL E 30  ? 0.3550 0.3381 0.3292 -0.0414 0.0337  -0.0408 31  VAL E CG2   
5285  N N     . PHE E 31  ? 0.3817 0.3626 0.3627 -0.0446 0.0362  -0.0418 32  PHE E N     
5286  C CA    . PHE E 31  ? 0.3636 0.3427 0.3447 -0.0454 0.0372  -0.0417 32  PHE E CA    
5287  C C     . PHE E 31  ? 0.3960 0.3741 0.3754 -0.0445 0.0383  -0.0406 32  PHE E C     
5288  O O     . PHE E 31  ? 0.4068 0.3863 0.3868 -0.0441 0.0387  -0.0397 32  PHE E O     
5289  C CB    . PHE E 31  ? 0.3589 0.3392 0.3428 -0.0469 0.0377  -0.0416 32  PHE E CB    
5290  C CG    . PHE E 31  ? 0.3756 0.3569 0.3615 -0.0481 0.0367  -0.0428 32  PHE E CG    
5291  C CD1   . PHE E 31  ? 0.4060 0.3899 0.3935 -0.0477 0.0356  -0.0434 32  PHE E CD1   
5292  C CD2   . PHE E 31  ? 0.4060 0.3856 0.3921 -0.0497 0.0367  -0.0433 32  PHE E CD2   
5293  C CE1   . PHE E 31  ? 0.4240 0.4092 0.4137 -0.0488 0.0346  -0.0445 32  PHE E CE1   
5294  C CE2   . PHE E 31  ? 0.3959 0.3766 0.3841 -0.0511 0.0357  -0.0443 32  PHE E CE2   
5295  C CZ    . PHE E 31  ? 0.4037 0.3874 0.3938 -0.0506 0.0347  -0.0450 32  PHE E CZ    
5296  N N     . SER E 32  ? 0.3924 0.3683 0.3700 -0.0441 0.0384  -0.0409 33  SER E N     
5297  C CA    . SER E 32  ? 0.3990 0.3746 0.3751 -0.0429 0.0391  -0.0402 33  SER E CA    
5298  C C     . SER E 32  ? 0.3774 0.3506 0.3532 -0.0433 0.0398  -0.0398 33  SER E C     
5299  O O     . SER E 32  ? 0.3957 0.3668 0.3715 -0.0442 0.0394  -0.0403 33  SER E O     
5300  C CB    . SER E 32  ? 0.3522 0.3276 0.3262 -0.0416 0.0387  -0.0409 33  SER E CB    
5301  O OG    . SER E 32  ? 0.3787 0.3518 0.3518 -0.0417 0.0380  -0.0423 33  SER E OG    
5302  N N     . LEU E 33  ? 0.3483 0.3219 0.3239 -0.0426 0.0405  -0.0388 34  LEU E N     
5303  C CA    . LEU E 33  ? 0.3693 0.3405 0.3440 -0.0426 0.0409  -0.0384 34  LEU E CA    
5304  C C     . LEU E 33  ? 0.3959 0.3681 0.3699 -0.0411 0.0413  -0.0379 34  LEU E C     
5305  O O     . LEU E 33  ? 0.4257 0.3990 0.4005 -0.0412 0.0418  -0.0369 34  LEU E O     
5306  C CB    . LEU E 33  ? 0.3743 0.3452 0.3500 -0.0439 0.0415  -0.0376 34  LEU E CB    
5307  C CG    . LEU E 33  ? 0.4149 0.3824 0.3893 -0.0444 0.0416  -0.0372 34  LEU E CG    
5308  C CD1   . LEU E 33  ? 0.4576 0.4254 0.4326 -0.0457 0.0425  -0.0363 34  LEU E CD1   
5309  C CD2   . LEU E 33  ? 0.4366 0.4029 0.4096 -0.0428 0.0414  -0.0371 34  LEU E CD2   
5310  N N     . LEU E 34  ? 0.3985 0.3705 0.3714 -0.0398 0.0409  -0.0388 35  LEU E N     
5311  C CA    . LEU E 34  ? 0.4300 0.4039 0.4026 -0.0385 0.0413  -0.0385 35  LEU E CA    
5312  C C     . LEU E 34  ? 0.4504 0.4224 0.4223 -0.0375 0.0412  -0.0389 35  LEU E C     
5313  O O     . LEU E 34  ? 0.4280 0.3969 0.3992 -0.0375 0.0405  -0.0395 35  LEU E O     
5314  C CB    . LEU E 34  ? 0.4441 0.4202 0.4159 -0.0378 0.0412  -0.0393 35  LEU E CB    
5315  C CG    . LEU E 34  ? 0.5084 0.4866 0.4807 -0.0386 0.0412  -0.0387 35  LEU E CG    
5316  C CD1   . LEU E 34  ? 0.5696 0.5464 0.5427 -0.0398 0.0407  -0.0388 35  LEU E CD1   
5317  C CD2   . LEU E 34  ? 0.5108 0.4907 0.4816 -0.0379 0.0410  -0.0394 35  LEU E CD2   
5318  N N     . PRO E 35  ? 0.5269 0.5007 0.4992 -0.0365 0.0416  -0.0384 36  PRO E N     
5319  C CA    . PRO E 35  ? 0.5634 0.5356 0.5354 -0.0354 0.0412  -0.0387 36  PRO E CA    
5320  C C     . PRO E 35  ? 0.5831 0.5539 0.5540 -0.0338 0.0405  -0.0404 36  PRO E C     
5321  O O     . PRO E 35  ? 0.6069 0.5742 0.5770 -0.0333 0.0396  -0.0408 36  PRO E O     
5322  C CB    . PRO E 35  ? 0.5764 0.5519 0.5495 -0.0348 0.0419  -0.0379 36  PRO E CB    
5323  C CG    . PRO E 35  ? 0.5614 0.5391 0.5352 -0.0362 0.0425  -0.0368 36  PRO E CG    
5324  C CD    . PRO E 35  ? 0.5027 0.4801 0.4758 -0.0366 0.0423  -0.0375 36  PRO E CD    
5325  N N     . ASP E 36  ? 0.5803 0.5537 0.5509 -0.0329 0.0408  -0.0414 37  ASP E N     
5326  C CA    . ASP E 36  ? 0.6080 0.5809 0.5777 -0.0310 0.0402  -0.0434 37  ASP E CA    
5327  C C     . ASP E 36  ? 0.5417 0.5155 0.5104 -0.0310 0.0401  -0.0445 37  ASP E C     
5328  O O     . ASP E 36  ? 0.5427 0.5171 0.5114 -0.0326 0.0403  -0.0437 37  ASP E O     
5329  C CB    . ASP E 36  ? 0.6255 0.6018 0.5961 -0.0292 0.0407  -0.0438 37  ASP E CB    
5330  C CG    . ASP E 36  ? 0.6746 0.6560 0.6461 -0.0298 0.0420  -0.0428 37  ASP E CG    
5331  O OD1   . ASP E 36  ? 0.7038 0.6872 0.6745 -0.0301 0.0425  -0.0432 37  ASP E OD1   
5332  O OD2   . ASP E 36  ? 0.7241 0.7073 0.6971 -0.0301 0.0425  -0.0416 37  ASP E OD2   
5333  N N     . GLY E 37  ? 0.5588 0.5326 0.5264 -0.0291 0.0396  -0.0466 38  GLY E N     
5334  C CA    . GLY E 37  ? 0.5192 0.4934 0.4853 -0.0288 0.0393  -0.0480 38  GLY E CA    
5335  C C     . GLY E 37  ? 0.4870 0.4665 0.4529 -0.0286 0.0406  -0.0478 38  GLY E C     
5336  O O     . GLY E 37  ? 0.4751 0.4553 0.4398 -0.0292 0.0405  -0.0481 38  GLY E O     
5337  N N     . PHE E 38  ? 0.4467 0.4297 0.4137 -0.0280 0.0417  -0.0472 39  PHE E N     
5338  C CA    . PHE E 38  ? 0.4216 0.4097 0.3883 -0.0282 0.0430  -0.0466 39  PHE E CA    
5339  C C     . PHE E 38  ? 0.4354 0.4235 0.4022 -0.0305 0.0432  -0.0446 39  PHE E C     
5340  O O     . PHE E 38  ? 0.4251 0.4154 0.3906 -0.0311 0.0436  -0.0443 39  PHE E O     
5341  C CB    . PHE E 38  ? 0.4387 0.4306 0.4072 -0.0275 0.0441  -0.0461 39  PHE E CB    
5342  C CG    . PHE E 38  ? 0.4430 0.4363 0.4117 -0.0249 0.0441  -0.0484 39  PHE E CG    
5343  C CD1   . PHE E 38  ? 0.4287 0.4255 0.3961 -0.0235 0.0448  -0.0502 39  PHE E CD1   
5344  C CD2   . PHE E 38  ? 0.4578 0.4490 0.4280 -0.0237 0.0433  -0.0488 39  PHE E CD2   
5345  C CE1   . PHE E 38  ? 0.4660 0.4644 0.4339 -0.0207 0.0447  -0.0526 39  PHE E CE1   
5346  C CE2   . PHE E 38  ? 0.4580 0.4504 0.4286 -0.0209 0.0430  -0.0511 39  PHE E CE2   
5347  C CZ    . PHE E 38  ? 0.4331 0.4293 0.4027 -0.0194 0.0438  -0.0531 39  PHE E CZ    
5348  N N     . SER E 39  ? 0.4251 0.4107 0.3933 -0.0318 0.0428  -0.0432 40  SER E N     
5349  C CA    . SER E 39  ? 0.4609 0.4463 0.4295 -0.0337 0.0428  -0.0414 40  SER E CA    
5350  C C     . SER E 39  ? 0.4220 0.4052 0.3896 -0.0343 0.0418  -0.0422 40  SER E C     
5351  O O     . SER E 39  ? 0.3868 0.3709 0.3541 -0.0353 0.0416  -0.0413 40  SER E O     
5352  C CB    . SER E 39  ? 0.4800 0.4637 0.4503 -0.0346 0.0427  -0.0401 40  SER E CB    
5353  O OG    . SER E 39  ? 0.5908 0.5748 0.5617 -0.0361 0.0427  -0.0386 40  SER E OG    
5354  N N     . GLN E 40  ? 0.4759 0.4562 0.4430 -0.0336 0.0409  -0.0437 41  GLN E N     
5355  C CA    . GLN E 40  ? 0.5047 0.4827 0.4711 -0.0343 0.0399  -0.0446 41  GLN E CA    
5356  C C     . GLN E 40  ? 0.4459 0.4259 0.4102 -0.0336 0.0397  -0.0456 41  GLN E C     
5357  O O     . GLN E 40  ? 0.5184 0.4984 0.4823 -0.0345 0.0390  -0.0455 41  GLN E O     
5358  C CB    . GLN E 40  ? 0.5884 0.5623 0.5546 -0.0339 0.0388  -0.0459 41  GLN E CB    
5359  C CG    . GLN E 40  ? 0.6335 0.6050 0.5998 -0.0353 0.0377  -0.0463 41  GLN E CG    
5360  C CD    . GLN E 40  ? 0.6722 0.6439 0.6404 -0.0372 0.0380  -0.0446 41  GLN E CD    
5361  O OE1   . GLN E 40  ? 0.7985 0.7715 0.7678 -0.0375 0.0389  -0.0431 41  GLN E OE1   
5362  N NE2   . GLN E 40  ? 0.6791 0.6497 0.6479 -0.0386 0.0372  -0.0449 41  GLN E NE2   
5363  N N     . ARG E 41  ? 0.4548 0.4368 0.4180 -0.0319 0.0403  -0.0468 42  ARG E N     
5364  C CA    A ARG E 41  ? 0.4394 0.4237 0.4002 -0.0312 0.0404  -0.0479 42  ARG E CA    
5365  C CA    B ARG E 41  ? 0.4287 0.4130 0.3895 -0.0312 0.0404  -0.0479 42  ARG E CA    
5366  C C     . ARG E 41  ? 0.4185 0.4057 0.3789 -0.0325 0.0411  -0.0459 42  ARG E C     
5367  O O     . ARG E 41  ? 0.4387 0.4263 0.3974 -0.0329 0.0405  -0.0460 42  ARG E O     
5368  C CB    A ARG E 41  ? 0.4527 0.4393 0.4126 -0.0290 0.0412  -0.0494 42  ARG E CB    
5369  C CB    B ARG E 41  ? 0.4269 0.4132 0.3868 -0.0290 0.0411  -0.0496 42  ARG E CB    
5370  C CG    A ARG E 41  ? 0.4680 0.4514 0.4278 -0.0273 0.0403  -0.0517 42  ARG E CG    
5371  C CG    B ARG E 41  ? 0.4302 0.4132 0.3890 -0.0274 0.0398  -0.0523 42  ARG E CG    
5372  C CD    A ARG E 41  ? 0.5037 0.4840 0.4617 -0.0271 0.0386  -0.0535 42  ARG E CD    
5373  C CD    B ARG E 41  ? 0.4421 0.4268 0.4005 -0.0248 0.0403  -0.0542 42  ARG E CD    
5374  N NE    A ARG E 41  ? 0.5206 0.4981 0.4780 -0.0250 0.0376  -0.0560 42  ARG E NE    
5375  N NE    B ARG E 41  ? 0.4629 0.4459 0.4235 -0.0242 0.0402  -0.0539 42  ARG E NE    
5376  C CZ    A ARG E 41  ? 0.5798 0.5579 0.5379 -0.0232 0.0380  -0.0567 42  ARG E CZ    
5377  C CZ    B ARG E 41  ? 0.4691 0.4553 0.4311 -0.0234 0.0413  -0.0535 42  ARG E CZ    
5378  N NH1   A ARG E 41  ? 0.5647 0.5464 0.5245 -0.0234 0.0396  -0.0551 42  ARG E NH1   
5379  N NH1   B ARG E 41  ? 0.4707 0.4624 0.4326 -0.0233 0.0430  -0.0531 42  ARG E NH1   
5380  N NH2   A ARG E 41  ? 0.6189 0.5939 0.5763 -0.0212 0.0367  -0.0591 42  ARG E NH2   
5381  N NH2   B ARG E 41  ? 0.4731 0.4571 0.4368 -0.0227 0.0408  -0.0533 42  ARG E NH2   
5382  N N     . TRP E 42  ? 0.3843 0.3735 0.3462 -0.0330 0.0422  -0.0441 43  TRP E N     
5383  C CA    . TRP E 42  ? 0.3450 0.3364 0.3065 -0.0344 0.0426  -0.0420 43  TRP E CA    
5384  C C     . TRP E 42  ? 0.3341 0.3234 0.2957 -0.0357 0.0414  -0.0413 43  TRP E C     
5385  O O     . TRP E 42  ? 0.2566 0.2469 0.2165 -0.0363 0.0410  -0.0406 43  TRP E O     
5386  C CB    . TRP E 42  ? 0.3749 0.3677 0.3385 -0.0350 0.0436  -0.0403 43  TRP E CB    
5387  C CG    . TRP E 42  ? 0.3675 0.3610 0.3312 -0.0367 0.0435  -0.0380 43  TRP E CG    
5388  C CD1   . TRP E 42  ? 0.3835 0.3796 0.3455 -0.0374 0.0440  -0.0367 43  TRP E CD1   
5389  C CD2   . TRP E 42  ? 0.3915 0.3827 0.3570 -0.0378 0.0427  -0.0367 43  TRP E CD2   
5390  N NE1   . TRP E 42  ? 0.3683 0.3634 0.3308 -0.0389 0.0434  -0.0347 43  TRP E NE1   
5391  C CE2   . TRP E 42  ? 0.3999 0.3922 0.3647 -0.0390 0.0426  -0.0348 43  TRP E CE2   
5392  C CE3   . TRP E 42  ? 0.4016 0.3901 0.3690 -0.0379 0.0422  -0.0370 43  TRP E CE3   
5393  C CZ2   . TRP E 42  ? 0.4002 0.3909 0.3664 -0.0399 0.0418  -0.0335 43  TRP E CZ2   
5394  C CZ3   . TRP E 42  ? 0.4441 0.4315 0.4128 -0.0389 0.0417  -0.0357 43  TRP E CZ3   
5395  C CH2   . TRP E 42  ? 0.4027 0.3911 0.3709 -0.0398 0.0414  -0.0341 43  TRP E CH2   
5396  N N     . LEU E 43  ? 0.3518 0.3383 0.3155 -0.0361 0.0407  -0.0414 44  LEU E N     
5397  C CA    . LEU E 43  ? 0.3622 0.3472 0.3268 -0.0372 0.0396  -0.0409 44  LEU E CA    
5398  C C     . LEU E 43  ? 0.3443 0.3288 0.3071 -0.0370 0.0384  -0.0423 44  LEU E C     
5399  O O     . LEU E 43  ? 0.3165 0.3013 0.2787 -0.0376 0.0375  -0.0417 44  LEU E O     
5400  C CB    . LEU E 43  ? 0.3938 0.3764 0.3608 -0.0377 0.0394  -0.0409 44  LEU E CB    
5401  C CG    . LEU E 43  ? 0.4053 0.3869 0.3738 -0.0389 0.0384  -0.0407 44  LEU E CG    
5402  C CD1   . LEU E 43  ? 0.4124 0.3955 0.3814 -0.0395 0.0383  -0.0391 44  LEU E CD1   
5403  C CD2   . LEU E 43  ? 0.4105 0.3901 0.3810 -0.0395 0.0385  -0.0408 44  LEU E CD2   
5404  N N     . THR E 44  ? 0.3771 0.3605 0.3388 -0.0360 0.0382  -0.0443 45  THR E N     
5405  C CA    . THR E 44  ? 0.3828 0.3651 0.3428 -0.0357 0.0368  -0.0459 45  THR E CA    
5406  C C     . THR E 44  ? 0.4439 0.4285 0.4011 -0.0354 0.0368  -0.0457 45  THR E C     
5407  O O     . THR E 44  ? 0.4173 0.4014 0.3732 -0.0357 0.0354  -0.0463 45  THR E O     
5408  C CB    . THR E 44  ? 0.4209 0.4013 0.3802 -0.0345 0.0366  -0.0481 45  THR E CB    
5409  O OG1   . THR E 44  ? 0.4769 0.4549 0.4386 -0.0350 0.0366  -0.0478 45  THR E OG1   
5410  C CG2   . THR E 44  ? 0.4260 0.4048 0.3836 -0.0342 0.0349  -0.0501 45  THR E CG2   
5411  N N     . LYS E 45  ? 0.4836 0.4709 0.4396 -0.0350 0.0382  -0.0448 46  LYS E N     
5412  C CA    . LYS E 45  ? 0.5222 0.5120 0.4750 -0.0350 0.0385  -0.0443 46  LYS E CA    
5413  C C     . LYS E 45  ? 0.5466 0.5364 0.4995 -0.0364 0.0377  -0.0421 46  LYS E C     
5414  O O     . LYS E 45  ? 0.4520 0.4424 0.4022 -0.0366 0.0370  -0.0418 46  LYS E O     
5415  C CB    . LYS E 45  ? 0.6116 0.6046 0.5634 -0.0343 0.0404  -0.0441 46  LYS E CB    
5416  C CG    . LYS E 45  ? 0.6702 0.6635 0.6216 -0.0324 0.0410  -0.0466 46  LYS E CG    
5417  C CD    . LYS E 45  ? 0.7302 0.7278 0.6806 -0.0316 0.0429  -0.0467 46  LYS E CD    
5418  C CE    . LYS E 45  ? 0.8256 0.8260 0.7722 -0.0319 0.0434  -0.0463 46  LYS E CE    
5419  N NZ    . LYS E 45  ? 0.8936 0.8988 0.8394 -0.0312 0.0455  -0.0465 46  LYS E NZ    
5420  N N     . LEU E 46  ? 0.5107 0.4998 0.4667 -0.0373 0.0379  -0.0406 47  LEU E N     
5421  C CA    . LEU E 46  ? 0.5012 0.4898 0.4578 -0.0384 0.0369  -0.0388 47  LEU E CA    
5422  C C     . LEU E 46  ? 0.5016 0.4884 0.4586 -0.0385 0.0350  -0.0398 47  LEU E C     
5423  O O     . LEU E 46  ? 0.4715 0.4584 0.4270 -0.0388 0.0336  -0.0392 47  LEU E O     
5424  C CB    . LEU E 46  ? 0.5251 0.5132 0.4847 -0.0390 0.0375  -0.0374 47  LEU E CB    
5425  C CG    . LEU E 46  ? 0.5249 0.5150 0.4842 -0.0394 0.0389  -0.0357 47  LEU E CG    
5426  C CD1   . LEU E 46  ? 0.5019 0.4910 0.4641 -0.0400 0.0390  -0.0344 47  LEU E CD1   
5427  C CD2   . LEU E 46  ? 0.5451 0.5362 0.5013 -0.0401 0.0385  -0.0341 47  LEU E CD2   
5428  N N     . ASN E 47  ? 0.4749 0.4603 0.4343 -0.0383 0.0347  -0.0413 48  ASN E N     
5429  C CA    . ASN E 47  ? 0.4569 0.4410 0.4175 -0.0386 0.0330  -0.0424 48  ASN E CA    
5430  C C     . ASN E 47  ? 0.4675 0.4501 0.4284 -0.0383 0.0329  -0.0445 48  ASN E C     
5431  O O     . ASN E 47  ? 0.5044 0.4860 0.4671 -0.0383 0.0338  -0.0447 48  ASN E O     
5432  C CB    . ASN E 47  ? 0.5334 0.5172 0.4975 -0.0395 0.0326  -0.0414 48  ASN E CB    
5433  C CG    . ASN E 47  ? 0.4990 0.4825 0.4646 -0.0398 0.0307  -0.0423 48  ASN E CG    
5434  O OD1   . ASN E 47  ? 0.5364 0.5190 0.5022 -0.0399 0.0300  -0.0440 48  ASN E OD1   
5435  N ND2   . ASN E 47  ? 0.4872 0.4713 0.4538 -0.0400 0.0297  -0.0413 48  ASN E ND2   
5436  N N     . PRO E 48  ? 0.4681 0.4501 0.4271 -0.0379 0.0315  -0.0462 49  PRO E N     
5437  C CA    . PRO E 48  ? 0.4916 0.4717 0.4505 -0.0375 0.0311  -0.0483 49  PRO E CA    
5438  C C     . PRO E 48  ? 0.4965 0.4748 0.4589 -0.0387 0.0303  -0.0488 49  PRO E C     
5439  O O     . PRO E 48  ? 0.4825 0.4586 0.4452 -0.0387 0.0303  -0.0500 49  PRO E O     
5440  C CB    . PRO E 48  ? 0.4888 0.4690 0.4443 -0.0368 0.0297  -0.0497 49  PRO E CB    
5441  C CG    . PRO E 48  ? 0.4891 0.4705 0.4447 -0.0374 0.0286  -0.0484 49  PRO E CG    
5442  C CD    . PRO E 48  ? 0.4752 0.4580 0.4319 -0.0378 0.0301  -0.0461 49  PRO E CD    
5443  N N     . ASN E 49  ? 0.5144 0.4937 0.4792 -0.0397 0.0297  -0.0478 50  ASN E N     
5444  C CA    . ASN E 49  ? 0.5139 0.4924 0.4822 -0.0410 0.0291  -0.0482 50  ASN E CA    
5445  C C     . ASN E 49  ? 0.4729 0.4513 0.4436 -0.0417 0.0307  -0.0470 50  ASN E C     
5446  O O     . ASN E 49  ? 0.4254 0.4053 0.3985 -0.0422 0.0310  -0.0459 50  ASN E O     
5447  C CB    . ASN E 49  ? 0.5321 0.5122 0.5022 -0.0416 0.0275  -0.0482 50  ASN E CB    
5448  C CG    . ASN E 49  ? 0.5652 0.5452 0.5392 -0.0432 0.0269  -0.0489 50  ASN E CG    
5449  O OD1   . ASN E 49  ? 0.6063 0.5846 0.5811 -0.0440 0.0276  -0.0493 50  ASN E OD1   
5450  N ND2   . ASN E 49  ? 0.5143 0.4961 0.4906 -0.0436 0.0256  -0.0490 50  ASN E ND2   
5451  N N     . VAL E 50  ? 0.4578 0.4342 0.4277 -0.0414 0.0317  -0.0473 51  VAL E N     
5452  C CA    . VAL E 50  ? 0.4784 0.4544 0.4500 -0.0419 0.0331  -0.0461 51  VAL E CA    
5453  C C     . VAL E 50  ? 0.4479 0.4215 0.4209 -0.0431 0.0329  -0.0468 51  VAL E C     
5454  O O     . VAL E 50  ? 0.4923 0.4636 0.4640 -0.0431 0.0318  -0.0482 51  VAL E O     
5455  C CB    . VAL E 50  ? 0.5189 0.4949 0.4885 -0.0405 0.0344  -0.0456 51  VAL E CB    
5456  C CG1   . VAL E 50  ? 0.5270 0.5020 0.4980 -0.0409 0.0356  -0.0446 51  VAL E CG1   
5457  C CG2   . VAL E 50  ? 0.5332 0.5117 0.5015 -0.0398 0.0348  -0.0445 51  VAL E CG2   
5458  N N     . ILE E 51  ? 0.4469 0.4207 0.4222 -0.0443 0.0338  -0.0457 52  ILE E N     
5459  C CA    . ILE E 51  ? 0.4190 0.3903 0.3952 -0.0458 0.0339  -0.0458 52  ILE E CA    
5460  C C     . ILE E 51  ? 0.4098 0.3801 0.3857 -0.0455 0.0353  -0.0446 52  ILE E C     
5461  O O     . ILE E 51  ? 0.3747 0.3471 0.3517 -0.0455 0.0364  -0.0434 52  ILE E O     
5462  C CB    . ILE E 51  ? 0.4608 0.4336 0.4402 -0.0478 0.0335  -0.0459 52  ILE E CB    
5463  C CG1   . ILE E 51  ? 0.4628 0.4363 0.4426 -0.0480 0.0318  -0.0473 52  ILE E CG1   
5464  C CG2   . ILE E 51  ? 0.4592 0.4297 0.4394 -0.0497 0.0340  -0.0455 52  ILE E CG2   
5465  C CD1   . ILE E 51  ? 0.5033 0.4788 0.4867 -0.0501 0.0313  -0.0476 52  ILE E CD1   
5466  N N     . ASN E 52  ? 0.3805 0.3475 0.3547 -0.0453 0.0352  -0.0449 53  ASN E N     
5467  C CA    . ASN E 52  ? 0.4065 0.3723 0.3801 -0.0448 0.0363  -0.0438 53  ASN E CA    
5468  C C     . ASN E 52  ? 0.3878 0.3523 0.3627 -0.0468 0.0368  -0.0429 53  ASN E C     
5469  O O     . ASN E 52  ? 0.3643 0.3262 0.3391 -0.0483 0.0360  -0.0433 53  ASN E O     
5470  C CB    . ASN E 52  ? 0.4434 0.4063 0.4146 -0.0432 0.0357  -0.0447 53  ASN E CB    
5471  C CG    . ASN E 52  ? 0.5021 0.4643 0.4726 -0.0423 0.0366  -0.0437 53  ASN E CG    
5472  O OD1   . ASN E 52  ? 0.5249 0.4885 0.4966 -0.0430 0.0377  -0.0423 53  ASN E OD1   
5473  N ND2   . ASN E 52  ? 0.5255 0.4858 0.4944 -0.0405 0.0361  -0.0446 53  ASN E ND2   
5474  N N     . LEU E 53  ? 0.3693 0.3357 0.3452 -0.0470 0.0381  -0.0416 54  LEU E N     
5475  C CA    . LEU E 53  ? 0.4035 0.3694 0.3804 -0.0489 0.0389  -0.0406 54  LEU E CA    
5476  C C     . LEU E 53  ? 0.4052 0.3668 0.3799 -0.0491 0.0388  -0.0401 54  LEU E C     
5477  O O     . LEU E 53  ? 0.4586 0.4186 0.4333 -0.0509 0.0391  -0.0393 54  LEU E O     
5478  C CB    . LEU E 53  ? 0.4102 0.3792 0.3885 -0.0487 0.0402  -0.0396 54  LEU E CB    
5479  C CG    . LEU E 53  ? 0.4208 0.3937 0.4013 -0.0486 0.0401  -0.0400 54  LEU E CG    
5480  C CD1   . LEU E 53  ? 0.4039 0.3791 0.3853 -0.0481 0.0411  -0.0391 54  LEU E CD1   
5481  C CD2   . LEU E 53  ? 0.4466 0.4206 0.4292 -0.0505 0.0397  -0.0407 54  LEU E CD2   
5482  N N     . GLN E 54  ? 0.3910 0.3510 0.3639 -0.0470 0.0382  -0.0405 55  GLN E N     
5483  C CA    . GLN E 54  ? 0.4343 0.3901 0.4051 -0.0466 0.0378  -0.0402 55  GLN E CA    
5484  C C     . GLN E 54  ? 0.4231 0.3748 0.3931 -0.0484 0.0367  -0.0404 55  GLN E C     
5485  O O     . GLN E 54  ? 0.3659 0.3138 0.3343 -0.0490 0.0363  -0.0396 55  GLN E O     
5486  C CB    . GLN E 54  ? 0.4492 0.4046 0.4186 -0.0439 0.0371  -0.0413 55  GLN E CB    
5487  C CG    . GLN E 54  ? 0.5044 0.4564 0.4721 -0.0427 0.0366  -0.0410 55  GLN E CG    
5488  C CD    . GLN E 54  ? 0.6663 0.6197 0.6343 -0.0425 0.0377  -0.0395 55  GLN E CD    
5489  O OE1   . GLN E 54  ? 0.7650 0.7156 0.7320 -0.0434 0.0377  -0.0385 55  GLN E OE1   
5490  N NE2   . GLN E 54  ? 0.6775 0.6350 0.6466 -0.0414 0.0386  -0.0394 55  GLN E NE2   
5491  N N     . GLN E 55  ? 0.4554 0.4079 0.4265 -0.0495 0.0360  -0.0414 56  GLN E N     
5492  C CA    . GLN E 55  ? 0.4671 0.4155 0.4375 -0.0512 0.0346  -0.0418 56  GLN E CA    
5493  C C     . GLN E 55  ? 0.5079 0.4556 0.4790 -0.0543 0.0354  -0.0403 56  GLN E C     
5494  O O     . GLN E 55  ? 0.5230 0.4669 0.4932 -0.0563 0.0344  -0.0402 56  GLN E O     
5495  C CB    . GLN E 55  ? 0.4992 0.4492 0.4709 -0.0516 0.0337  -0.0434 56  GLN E CB    
5496  C CG    . GLN E 55  ? 0.4842 0.4388 0.4589 -0.0534 0.0346  -0.0430 56  GLN E CG    
5497  C CD    . GLN E 55  ? 0.5048 0.4612 0.4807 -0.0533 0.0334  -0.0446 56  GLN E CD    
5498  O OE1   . GLN E 55  ? 0.4961 0.4540 0.4713 -0.0511 0.0330  -0.0456 56  GLN E OE1   
5499  N NE2   . GLN E 55  ? 0.5001 0.4567 0.4778 -0.0559 0.0329  -0.0448 56  GLN E NE2   
5500  N N     . PHE E 56  ? 0.5379 0.4892 0.5103 -0.0548 0.0372  -0.0392 57  PHE E N     
5501  C CA    . PHE E 56  ? 0.5483 0.5001 0.5215 -0.0577 0.0383  -0.0379 57  PHE E CA    
5502  C C     . PHE E 56  ? 0.5532 0.5017 0.5238 -0.0579 0.0387  -0.0363 57  PHE E C     
5503  O O     . PHE E 56  ? 0.4784 0.4267 0.4488 -0.0603 0.0397  -0.0350 57  PHE E O     
5504  C CB    . PHE E 56  ? 0.5351 0.4930 0.5114 -0.0581 0.0399  -0.0378 57  PHE E CB    
5505  C CG    . PHE E 56  ? 0.5261 0.4871 0.5051 -0.0584 0.0392  -0.0392 57  PHE E CG    
5506  C CD1   . PHE E 56  ? 0.5647 0.5255 0.5451 -0.0611 0.0387  -0.0395 57  PHE E CD1   
5507  C CD2   . PHE E 56  ? 0.5379 0.5021 0.5180 -0.0562 0.0391  -0.0401 57  PHE E CD2   
5508  C CE1   . PHE E 56  ? 0.5354 0.4992 0.5184 -0.0614 0.0379  -0.0408 57  PHE E CE1   
5509  C CE2   . PHE E 56  ? 0.5520 0.5189 0.5343 -0.0565 0.0382  -0.0413 57  PHE E CE2   
5510  C CZ    . PHE E 56  ? 0.5450 0.5117 0.5288 -0.0589 0.0376  -0.0418 57  PHE E CZ    
5511  N N     . TYR E 57  ? 0.5640 0.5100 0.5325 -0.0553 0.0380  -0.0365 58  TYR E N     
5512  C CA    . TYR E 57  ? 0.5708 0.5133 0.5367 -0.0551 0.0380  -0.0351 58  TYR E CA    
5513  C C     . TYR E 57  ? 0.6262 0.5623 0.5896 -0.0565 0.0363  -0.0348 58  TYR E C     
5514  O O     . TYR E 57  ? 0.5684 0.5025 0.5319 -0.0564 0.0348  -0.0361 58  TYR E O     
5515  C CB    . TYR E 57  ? 0.5535 0.4962 0.5186 -0.0518 0.0377  -0.0355 58  TYR E CB    
5516  C CG    . TYR E 57  ? 0.5211 0.4689 0.4878 -0.0509 0.0394  -0.0352 58  TYR E CG    
5517  C CD1   . TYR E 57  ? 0.4520 0.4003 0.4182 -0.0517 0.0405  -0.0338 58  TYR E CD1   
5518  C CD2   . TYR E 57  ? 0.5138 0.4656 0.4825 -0.0493 0.0396  -0.0363 58  TYR E CD2   
5519  C CE1   . TYR E 57  ? 0.5023 0.4547 0.4698 -0.0508 0.0417  -0.0337 58  TYR E CE1   
5520  C CE2   . TYR E 57  ? 0.5134 0.4692 0.4834 -0.0485 0.0408  -0.0359 58  TYR E CE2   
5521  C CZ    . TYR E 57  ? 0.4825 0.4386 0.4521 -0.0493 0.0418  -0.0347 58  TYR E CZ    
5522  O OH    . TYR E 57  ? 0.6115 0.5711 0.5823 -0.0485 0.0427  -0.0344 58  TYR E OH    
5523  N N     . ALA E 58  ? 0.5959 0.5286 0.5569 -0.0577 0.0364  -0.0331 59  ALA E N     
5524  C CA    . ALA E 58  ? 0.6263 0.5522 0.5844 -0.0592 0.0346  -0.0324 59  ALA E CA    
5525  C C     . ALA E 58  ? 0.6663 0.5886 0.6236 -0.0568 0.0322  -0.0342 59  ALA E C     
5526  O O     . ALA E 58  ? 0.5600 0.4833 0.5174 -0.0534 0.0319  -0.0353 59  ALA E O     
5527  C CB    . ALA E 58  ? 0.6832 0.6056 0.6382 -0.0594 0.0346  -0.0306 59  ALA E CB    
5528  N N     . GLN E 59  ? 0.6976 0.6160 0.6544 -0.0585 0.0306  -0.0346 60  GLN E N     
5529  C CA    . GLN E 59  ? 0.7868 0.7014 0.7427 -0.0563 0.0283  -0.0366 60  GLN E CA    
5530  C C     . GLN E 59  ? 0.7791 0.6853 0.7315 -0.0575 0.0259  -0.0358 60  GLN E C     
5531  O O     . GLN E 59  ? 0.8132 0.7169 0.7652 -0.0612 0.0256  -0.0347 60  GLN E O     
5532  C CB    . GLN E 59  ? 0.8598 0.7772 0.8181 -0.0569 0.0280  -0.0383 60  GLN E CB    
5533  C CG    . GLN E 59  ? 0.8781 0.8033 0.8395 -0.0559 0.0301  -0.0390 60  GLN E CG    
5534  C CD    . GLN E 59  ? 0.9149 0.8424 0.8763 -0.0519 0.0303  -0.0402 60  GLN E CD    
5535  O OE1   . GLN E 59  ? 0.8362 0.7612 0.7964 -0.0495 0.0286  -0.0419 60  GLN E OE1   
5536  N NE2   . GLN E 59  ? 0.8870 0.8196 0.8499 -0.0512 0.0322  -0.0395 60  GLN E NE2   
5537  N N     . ASN E 60  ? 0.8337 0.7357 0.7839 -0.0545 0.0241  -0.0365 61  ASN E N     
5538  C CA    . ASN E 60  ? 0.8611 0.7544 0.8079 -0.0549 0.0212  -0.0361 61  ASN E CA    
5539  C C     . ASN E 60  ? 0.7770 0.6668 0.7211 -0.0574 0.0215  -0.0332 61  ASN E C     
5540  O O     . ASN E 60  ? 0.8827 0.7690 0.8256 -0.0613 0.0211  -0.0315 61  ASN E O     
5541  C CB    . ASN E 60  ? 0.9184 0.8084 0.8653 -0.0572 0.0196  -0.0370 61  ASN E CB    
5542  C CG    . ASN E 60  ? 1.0152 0.9089 0.9645 -0.0549 0.0194  -0.0399 61  ASN E CG    
5543  O OD1   . ASN E 60  ? 1.0628 0.9558 1.0115 -0.0510 0.0182  -0.0419 61  ASN E OD1   
5544  N ND2   . ASN E 60  ? 1.0804 0.9781 1.0321 -0.0573 0.0205  -0.0401 61  ASN E ND2   
5545  N N     . GLY E 61  ? 0.6304 0.5212 0.5737 -0.0552 0.0220  -0.0325 62  GLY E N     
5546  C CA    . GLY E 61  ? 0.6080 0.4951 0.5481 -0.0570 0.0220  -0.0298 62  GLY E CA    
5547  C C     . GLY E 61  ? 0.5781 0.4665 0.5182 -0.0619 0.0239  -0.0276 62  GLY E C     
5548  O O     . GLY E 61  ? 0.6345 0.5178 0.5713 -0.0647 0.0232  -0.0253 62  GLY E O     
5549  N N     . GLU E 62  ? 0.6001 0.4957 0.5440 -0.0630 0.0263  -0.0284 63  GLU E N     
5550  C CA    . GLU E 62  ? 0.5861 0.4845 0.5309 -0.0675 0.0283  -0.0268 63  GLU E CA    
5551  C C     . GLU E 62  ? 0.5793 0.4819 0.5239 -0.0681 0.0309  -0.0252 63  GLU E C     
5552  O O     . GLU E 62  ? 0.5656 0.4723 0.5114 -0.0651 0.0318  -0.0260 63  GLU E O     
5553  C CB    . GLU E 62  ? 0.6003 0.5046 0.5496 -0.0679 0.0293  -0.0286 63  GLU E CB    
5554  C CG    . GLU E 62  ? 0.6212 0.5315 0.5729 -0.0713 0.0321  -0.0276 63  GLU E CG    
5555  C CD    . GLU E 62  ? 0.7216 0.6383 0.6778 -0.0710 0.0330  -0.0295 63  GLU E CD    
5556  O OE1   . GLU E 62  ? 0.7854 0.7019 0.7425 -0.0682 0.0316  -0.0316 63  GLU E OE1   
5557  O OE2   . GLU E 62  ? 0.8201 0.7421 0.7789 -0.0736 0.0351  -0.0290 63  GLU E OE2   
5558  N N     . VAL E 63  ? 0.5515 0.4532 0.4945 -0.0721 0.0320  -0.0229 64  VAL E N     
5559  C CA    . VAL E 63  ? 0.5620 0.4680 0.5045 -0.0731 0.0346  -0.0215 64  VAL E CA    
5560  C C     . VAL E 63  ? 0.5771 0.4915 0.5242 -0.0745 0.0373  -0.0223 64  VAL E C     
5561  O O     . VAL E 63  ? 0.5809 0.4965 0.5292 -0.0781 0.0381  -0.0218 64  VAL E O     
5562  C CB    . VAL E 63  ? 0.6012 0.5024 0.5393 -0.0768 0.0347  -0.0185 64  VAL E CB    
5563  C CG1   . VAL E 63  ? 0.6415 0.5477 0.5791 -0.0780 0.0376  -0.0173 64  VAL E CG1   
5564  C CG2   . VAL E 63  ? 0.6202 0.5125 0.5535 -0.0753 0.0316  -0.0176 64  VAL E CG2   
5565  N N     . LYS E 64  ? 0.5506 0.4708 0.5004 -0.0715 0.0386  -0.0238 65  LYS E N     
5566  C CA    . LYS E 64  ? 0.5654 0.4934 0.5197 -0.0720 0.0408  -0.0249 65  LYS E CA    
5567  C C     . LYS E 64  ? 0.5516 0.4846 0.5065 -0.0702 0.0427  -0.0249 65  LYS E C     
5568  O O     . LYS E 64  ? 0.5040 0.4368 0.4586 -0.0669 0.0421  -0.0256 65  LYS E O     
5569  C CB    . LYS E 64  ? 0.5918 0.5215 0.5492 -0.0699 0.0396  -0.0272 65  LYS E CB    
5570  C CG    . LYS E 64  ? 0.5855 0.5227 0.5476 -0.0703 0.0413  -0.0284 65  LYS E CG    
5571  C CD    . LYS E 64  ? 0.6176 0.5559 0.5821 -0.0683 0.0400  -0.0306 65  LYS E CD    
5572  C CE    . LYS E 64  ? 0.5826 0.5272 0.5515 -0.0694 0.0411  -0.0316 65  LYS E CE    
5573  N NZ    . LYS E 64  ? 0.5760 0.5213 0.5467 -0.0675 0.0396  -0.0336 65  LYS E NZ    
5574  N N     . ASN E 65  ? 0.6003 0.5377 0.5562 -0.0726 0.0451  -0.0242 66  ASN E N     
5575  C CA    . ASN E 65  ? 0.6005 0.5429 0.5572 -0.0711 0.0470  -0.0244 66  ASN E CA    
5576  C C     . ASN E 65  ? 0.5885 0.5357 0.5494 -0.0682 0.0470  -0.0266 66  ASN E C     
5577  O O     . ASN E 65  ? 0.6263 0.5761 0.5903 -0.0688 0.0470  -0.0277 66  ASN E O     
5578  C CB    . ASN E 65  ? 0.6173 0.5638 0.5743 -0.0742 0.0495  -0.0236 66  ASN E CB    
5579  C CG    . ASN E 65  ? 0.6227 0.5732 0.5796 -0.0725 0.0512  -0.0238 66  ASN E CG    
5580  O OD1   . ASN E 65  ? 0.5837 0.5381 0.5436 -0.0698 0.0514  -0.0254 66  ASN E OD1   
5581  N ND2   . ASN E 65  ? 0.5995 0.5489 0.5529 -0.0741 0.0524  -0.0223 66  ASN E ND2   
5582  N N     . ARG E 66  ? 0.5826 0.5308 0.5432 -0.0652 0.0470  -0.0270 67  ARG E N     
5583  C CA    . ARG E 66  ? 0.6162 0.5681 0.5800 -0.0625 0.0468  -0.0287 67  ARG E CA    
5584  C C     . ARG E 66  ? 0.6060 0.5644 0.5735 -0.0632 0.0485  -0.0296 67  ARG E C     
5585  O O     . ARG E 66  ? 0.6358 0.5973 0.6063 -0.0618 0.0482  -0.0310 67  ARG E O     
5586  C CB    . ARG E 66  ? 0.6572 0.6086 0.6198 -0.0595 0.0464  -0.0287 67  ARG E CB    
5587  C CG    . ARG E 66  ? 0.6782 0.6240 0.6380 -0.0581 0.0444  -0.0283 67  ARG E CG    
5588  C CD    . ARG E 66  ? 0.6485 0.5954 0.6090 -0.0548 0.0437  -0.0291 67  ARG E CD    
5589  N NE    . ARG E 66  ? 0.6807 0.6294 0.6405 -0.0541 0.0447  -0.0286 67  ARG E NE    
5590  C CZ    . ARG E 66  ? 0.6814 0.6271 0.6380 -0.0543 0.0444  -0.0273 67  ARG E CZ    
5591  N NH1   . ARG E 66  ? 0.6590 0.5994 0.6126 -0.0552 0.0432  -0.0264 67  ARG E NH1   
5592  N NH2   . ARG E 66  ? 0.7082 0.6558 0.6644 -0.0537 0.0452  -0.0271 67  ARG E NH2   
5593  N N     . ARG E 67  ? 0.5660 0.5264 0.5330 -0.0655 0.0503  -0.0288 68  ARG E N     
5594  C CA    . ARG E 67  ? 0.5552 0.5220 0.5257 -0.0661 0.0520  -0.0298 68  ARG E CA    
5595  C C     . ARG E 67  ? 0.5336 0.5022 0.5074 -0.0677 0.0516  -0.0307 68  ARG E C     
5596  O O     . ARG E 67  ? 0.4798 0.4535 0.4575 -0.0670 0.0521  -0.0321 68  ARG E O     
5597  C CB    . ARG E 67  ? 0.6023 0.5708 0.5713 -0.0683 0.0541  -0.0289 68  ARG E CB    
5598  C CG    . ARG E 67  ? 0.6814 0.6478 0.6468 -0.0669 0.0543  -0.0280 68  ARG E CG    
5599  C CD    . ARG E 67  ? 0.7565 0.7246 0.7198 -0.0691 0.0565  -0.0271 68  ARG E CD    
5600  N NE    . ARG E 67  ? 0.7754 0.7506 0.7423 -0.0689 0.0584  -0.0286 68  ARG E NE    
5601  C CZ    . ARG E 67  ? 0.8108 0.7885 0.7768 -0.0676 0.0596  -0.0291 68  ARG E CZ    
5602  N NH1   . ARG E 67  ? 0.8167 0.7905 0.7784 -0.0667 0.0591  -0.0281 68  ARG E NH1   
5603  N NH2   . ARG E 67  ? 0.8000 0.7840 0.7695 -0.0672 0.0611  -0.0308 68  ARG E NH2   
5604  N N     . ASP E 68  ? 0.4893 0.4535 0.4615 -0.0696 0.0505  -0.0299 69  ASP E N     
5605  C CA    . ASP E 68  ? 0.4881 0.4531 0.4629 -0.0712 0.0497  -0.0306 69  ASP E CA    
5606  C C     . ASP E 68  ? 0.5312 0.4956 0.5074 -0.0683 0.0479  -0.0321 69  ASP E C     
5607  O O     . ASP E 68  ? 0.5457 0.5135 0.5252 -0.0682 0.0476  -0.0335 69  ASP E O     
5608  C CB    . ASP E 68  ? 0.5267 0.4865 0.4990 -0.0743 0.0489  -0.0293 69  ASP E CB    
5609  C CG    . ASP E 68  ? 0.5189 0.4795 0.4899 -0.0779 0.0508  -0.0277 69  ASP E CG    
5610  O OD1   . ASP E 68  ? 0.5636 0.5303 0.5381 -0.0797 0.0525  -0.0282 69  ASP E OD1   
5611  O OD2   . ASP E 68  ? 0.5648 0.5202 0.5314 -0.0788 0.0506  -0.0259 69  ASP E OD2   
5612  N N     . THR E 69  ? 0.4777 0.4380 0.4511 -0.0659 0.0467  -0.0318 70  THR E N     
5613  C CA    . THR E 69  ? 0.4652 0.4249 0.4393 -0.0631 0.0452  -0.0331 70  THR E CA    
5614  C C     . THR E 69  ? 0.4659 0.4314 0.4433 -0.0614 0.0459  -0.0343 70  THR E C     
5615  O O     . THR E 69  ? 0.4134 0.3808 0.3930 -0.0608 0.0451  -0.0355 70  THR E O     
5616  C CB    . THR E 69  ? 0.5064 0.4618 0.4773 -0.0609 0.0442  -0.0326 70  THR E CB    
5617  O OG1   . THR E 69  ? 0.5230 0.4728 0.4912 -0.0623 0.0431  -0.0318 70  THR E OG1   
5618  C CG2   . THR E 69  ? 0.5311 0.4871 0.5027 -0.0579 0.0431  -0.0339 70  THR E CG2   
5619  N N     . TYR E 70  ? 0.4393 0.4070 0.4165 -0.0606 0.0473  -0.0339 71  TYR E N     
5620  C CA    . TYR E 70  ? 0.4444 0.4169 0.4243 -0.0589 0.0477  -0.0348 71  TYR E CA    
5621  C C     . TYR E 70  ? 0.4360 0.4130 0.4196 -0.0602 0.0482  -0.0359 71  TYR E C     
5622  O O     . TYR E 70  ? 0.4441 0.4236 0.4300 -0.0589 0.0474  -0.0370 71  TYR E O     
5623  C CB    . TYR E 70  ? 0.4889 0.4624 0.4677 -0.0581 0.0490  -0.0342 71  TYR E CB    
5624  C CG    . TYR E 70  ? 0.5280 0.4974 0.5034 -0.0567 0.0484  -0.0333 71  TYR E CG    
5625  C CD1   . TYR E 70  ? 0.4954 0.4623 0.4700 -0.0550 0.0469  -0.0335 71  TYR E CD1   
5626  C CD2   . TYR E 70  ? 0.5533 0.5217 0.5264 -0.0571 0.0493  -0.0323 71  TYR E CD2   
5627  C CE1   . TYR E 70  ? 0.5207 0.4844 0.4927 -0.0536 0.0463  -0.0328 71  TYR E CE1   
5628  C CE2   . TYR E 70  ? 0.5514 0.5162 0.5216 -0.0557 0.0485  -0.0315 71  TYR E CE2   
5629  C CZ    . TYR E 70  ? 0.5277 0.4903 0.4977 -0.0540 0.0470  -0.0318 71  TYR E CZ    
5630  O OH    . TYR E 70  ? 0.5696 0.5292 0.5372 -0.0525 0.0462  -0.0312 71  TYR E OH    
5631  N N     . GLU E 71  ? 0.4692 0.4473 0.4533 -0.0631 0.0493  -0.0354 72  GLU E N     
5632  C CA    . GLU E 71  ? 0.4889 0.4717 0.4769 -0.0647 0.0499  -0.0364 72  GLU E CA    
5633  C C     . GLU E 71  ? 0.5110 0.4933 0.5006 -0.0646 0.0480  -0.0374 72  GLU E C     
5634  O O     . GLU E 71  ? 0.4588 0.4452 0.4519 -0.0641 0.0477  -0.0387 72  GLU E O     
5635  C CB    . GLU E 71  ? 0.4914 0.4749 0.4792 -0.0682 0.0514  -0.0355 72  GLU E CB    
5636  C CG    . GLU E 71  ? 0.5150 0.5040 0.5073 -0.0702 0.0520  -0.0366 72  GLU E CG    
5637  C CD    . GLU E 71  ? 0.5466 0.5420 0.5426 -0.0683 0.0528  -0.0381 72  GLU E CD    
5638  O OE1   . GLU E 71  ? 0.6577 0.6530 0.6526 -0.0656 0.0528  -0.0383 72  GLU E OE1   
5639  O OE2   . GLU E 71  ? 0.5645 0.5650 0.5648 -0.0696 0.0531  -0.0393 72  GLU E OE2   
5640  N N     . GLN E 72  ? 0.4650 0.4419 0.4519 -0.0651 0.0467  -0.0368 73  GLN E N     
5641  C CA    . GLN E 72  ? 0.5320 0.5077 0.5199 -0.0651 0.0449  -0.0378 73  GLN E CA    
5642  C C     . GLN E 72  ? 0.4659 0.4426 0.4541 -0.0619 0.0438  -0.0388 73  GLN E C     
5643  O O     . GLN E 72  ? 0.4483 0.4269 0.4387 -0.0615 0.0427  -0.0400 73  GLN E O     
5644  C CB    . GLN E 72  ? 0.5686 0.5379 0.5531 -0.0662 0.0437  -0.0370 73  GLN E CB    
5645  C CG    . GLN E 72  ? 0.6235 0.5913 0.6075 -0.0699 0.0443  -0.0359 73  GLN E CG    
5646  C CD    . GLN E 72  ? 0.6912 0.6518 0.6716 -0.0708 0.0428  -0.0351 73  GLN E CD    
5647  O OE1   . GLN E 72  ? 0.7765 0.7335 0.7549 -0.0683 0.0412  -0.0356 73  GLN E OE1   
5648  N NE2   . GLN E 72  ? 0.7393 0.6979 0.7189 -0.0743 0.0431  -0.0339 73  GLN E NE2   
5649  N N     . MET E 73  ? 0.4614 0.4369 0.4476 -0.0597 0.0442  -0.0383 74  MET E N     
5650  C CA    . MET E 73  ? 0.4146 0.3912 0.4009 -0.0569 0.0434  -0.0389 74  MET E CA    
5651  C C     . MET E 73  ? 0.3975 0.3793 0.3873 -0.0565 0.0436  -0.0398 74  MET E C     
5652  O O     . MET E 73  ? 0.4098 0.3929 0.4008 -0.0555 0.0424  -0.0408 74  MET E O     
5653  C CB    . MET E 73  ? 0.4122 0.3871 0.3961 -0.0551 0.0439  -0.0380 74  MET E CB    
5654  C CG    . MET E 73  ? 0.4243 0.3942 0.4049 -0.0546 0.0432  -0.0375 74  MET E CG    
5655  S SD    . MET E 73  ? 0.4183 0.3870 0.3967 -0.0525 0.0436  -0.0366 74  MET E SD    
5656  C CE    . MET E 73  ? 0.4562 0.4194 0.4314 -0.0520 0.0425  -0.0364 74  MET E CE    
5657  N N     . VAL E 74  ? 0.4071 0.3917 0.3983 -0.0571 0.0452  -0.0395 75  VAL E N     
5658  C CA    . VAL E 74  ? 0.4124 0.4019 0.4069 -0.0563 0.0454  -0.0405 75  VAL E CA    
5659  C C     . VAL E 74  ? 0.4403 0.4326 0.4381 -0.0575 0.0445  -0.0417 75  VAL E C     
5660  O O     . VAL E 74  ? 0.4471 0.4418 0.4469 -0.0561 0.0434  -0.0427 75  VAL E O     
5661  C CB    . VAL E 74  ? 0.3841 0.3762 0.3794 -0.0570 0.0473  -0.0403 75  VAL E CB    
5662  C CG1   . VAL E 74  ? 0.3835 0.3811 0.3828 -0.0562 0.0475  -0.0416 75  VAL E CG1   
5663  C CG2   . VAL E 74  ? 0.4283 0.4179 0.4206 -0.0556 0.0479  -0.0392 75  VAL E CG2   
5664  N N     . ASN E 75  ? 0.4676 0.4591 0.4656 -0.0602 0.0448  -0.0415 76  ASN E N     
5665  C CA    . ASN E 75  ? 0.4582 0.4525 0.4596 -0.0618 0.0440  -0.0426 76  ASN E CA    
5666  C C     . ASN E 75  ? 0.4296 0.4221 0.4305 -0.0604 0.0417  -0.0434 76  ASN E C     
5667  O O     . ASN E 75  ? 0.4072 0.4030 0.4110 -0.0599 0.0406  -0.0447 76  ASN E O     
5668  C CB    . ASN E 75  ? 0.4775 0.4705 0.4788 -0.0653 0.0447  -0.0420 76  ASN E CB    
5669  C CG    . ASN E 75  ? 0.5442 0.5401 0.5492 -0.0671 0.0437  -0.0432 76  ASN E CG    
5670  O OD1   . ASN E 75  ? 0.6812 0.6736 0.6850 -0.0684 0.0423  -0.0432 76  ASN E OD1   
5671  N ND2   . ASN E 75  ? 0.6228 0.6249 0.6321 -0.0671 0.0442  -0.0443 76  ASN E ND2   
5672  N N     . ALA E 76  ? 0.3969 0.3844 0.3940 -0.0596 0.0410  -0.0428 77  ALA E N     
5673  C CA    . ALA E 76  ? 0.3878 0.3733 0.3836 -0.0582 0.0390  -0.0436 77  ALA E CA    
5674  C C     . ALA E 76  ? 0.3670 0.3551 0.3636 -0.0557 0.0384  -0.0441 77  ALA E C     
5675  O O     . ALA E 76  ? 0.3206 0.3097 0.3181 -0.0551 0.0367  -0.0452 77  ALA E O     
5676  C CB    . ALA E 76  ? 0.3760 0.3562 0.3677 -0.0576 0.0387  -0.0430 77  ALA E CB    
5677  N N     . ILE E 77  ? 0.3492 0.3380 0.3453 -0.0543 0.0395  -0.0434 78  ILE E N     
5678  C CA    . ILE E 77  ? 0.3301 0.3205 0.3264 -0.0520 0.0388  -0.0436 78  ILE E CA    
5679  C C     . ILE E 77  ? 0.3252 0.3202 0.3255 -0.0521 0.0381  -0.0447 78  ILE E C     
5680  O O     . ILE E 77  ? 0.3099 0.3058 0.3107 -0.0507 0.0365  -0.0453 78  ILE E O     
5681  C CB    . ILE E 77  ? 0.3371 0.3270 0.3320 -0.0508 0.0400  -0.0425 78  ILE E CB    
5682  C CG1   . ILE E 77  ? 0.3200 0.3057 0.3111 -0.0505 0.0404  -0.0415 78  ILE E CG1   
5683  C CG2   . ILE E 77  ? 0.3480 0.3395 0.3434 -0.0487 0.0391  -0.0426 78  ILE E CG2   
5684  C CD1   . ILE E 77  ? 0.2861 0.2713 0.2760 -0.0495 0.0415  -0.0405 78  ILE E CD1   
5685  N N     . LEU E 78  ? 0.3345 0.3325 0.3378 -0.0537 0.0394  -0.0450 79  LEU E N     
5686  C CA    . LEU E 78  ? 0.3537 0.3567 0.3613 -0.0536 0.0390  -0.0463 79  LEU E CA    
5687  C C     . LEU E 78  ? 0.3582 0.3623 0.3678 -0.0547 0.0373  -0.0474 79  LEU E C     
5688  O O     . LEU E 78  ? 0.3987 0.4060 0.4112 -0.0537 0.0359  -0.0486 79  LEU E O     
5689  C CB    . LEU E 78  ? 0.3748 0.3812 0.3849 -0.0550 0.0411  -0.0464 79  LEU E CB    
5690  C CG    . LEU E 78  ? 0.4138 0.4216 0.4239 -0.0532 0.0421  -0.0463 79  LEU E CG    
5691  C CD1   . LEU E 78  ? 0.4268 0.4357 0.4380 -0.0505 0.0402  -0.0471 79  LEU E CD1   
5692  C CD2   . LEU E 78  ? 0.4398 0.4433 0.4457 -0.0528 0.0432  -0.0447 79  LEU E CD2   
5693  N N     . ASP E 79  ? 0.3549 0.3561 0.3629 -0.0566 0.0372  -0.0471 80  ASP E N     
5694  C CA    . ASP E 79  ? 0.4067 0.4083 0.4163 -0.0578 0.0354  -0.0482 80  ASP E CA    
5695  C C     . ASP E 79  ? 0.4152 0.4163 0.4238 -0.0554 0.0331  -0.0489 80  ASP E C     
5696  O O     . ASP E 79  ? 0.4022 0.4058 0.4134 -0.0555 0.0314  -0.0502 80  ASP E O     
5697  C CB    . ASP E 79  ? 0.4562 0.4537 0.4635 -0.0599 0.0354  -0.0478 80  ASP E CB    
5698  C CG    . ASP E 79  ? 0.4841 0.4827 0.4933 -0.0631 0.0371  -0.0473 80  ASP E CG    
5699  O OD1   . ASP E 79  ? 0.6100 0.6133 0.6224 -0.0636 0.0385  -0.0475 80  ASP E OD1   
5700  O OD2   . ASP E 79  ? 0.5736 0.5684 0.5809 -0.0651 0.0368  -0.0468 80  ASP E OD2   
5701  N N     . ALA E 80  ? 0.3940 0.3918 0.3986 -0.0535 0.0331  -0.0480 81  ALA E N     
5702  C CA    . ALA E 80  ? 0.3804 0.3773 0.3832 -0.0514 0.0311  -0.0484 81  ALA E CA    
5703  C C     . ALA E 80  ? 0.3694 0.3699 0.3748 -0.0499 0.0304  -0.0488 81  ALA E C     
5704  O O     . ALA E 80  ? 0.3209 0.3225 0.3270 -0.0490 0.0282  -0.0496 81  ALA E O     
5705  C CB    . ALA E 80  ? 0.3887 0.3817 0.3867 -0.0501 0.0316  -0.0472 81  ALA E CB    
5706  N N     . VAL E 81  ? 0.3988 0.4008 0.4054 -0.0494 0.0319  -0.0482 82  VAL E N     
5707  C CA    . VAL E 81  ? 0.3814 0.3864 0.3903 -0.0477 0.0312  -0.0487 82  VAL E CA    
5708  C C     . VAL E 81  ? 0.3644 0.3740 0.3783 -0.0483 0.0301  -0.0504 82  VAL E C     
5709  O O     . VAL E 81  ? 0.3261 0.3374 0.3415 -0.0468 0.0280  -0.0512 82  VAL E O     
5710  C CB    . VAL E 81  ? 0.3555 0.3612 0.3648 -0.0471 0.0331  -0.0480 82  VAL E CB    
5711  C CG1   . VAL E 81  ? 0.3304 0.3391 0.3425 -0.0452 0.0321  -0.0489 82  VAL E CG1   
5712  C CG2   . VAL E 81  ? 0.3605 0.3620 0.3653 -0.0465 0.0340  -0.0464 82  VAL E CG2   
5713  N N     . ARG E 82  ? 0.4270 0.4387 0.4434 -0.0507 0.0315  -0.0509 83  ARG E N     
5714  C CA    . ARG E 82  ? 0.4230 0.4398 0.4447 -0.0518 0.0309  -0.0525 83  ARG E CA    
5715  C C     . ARG E 82  ? 0.4381 0.4545 0.4601 -0.0517 0.0282  -0.0534 83  ARG E C     
5716  O O     . ARG E 82  ? 0.4037 0.4242 0.4298 -0.0515 0.0266  -0.0549 83  ARG E O     
5717  C CB    . ARG E 82  ? 0.4558 0.4743 0.4794 -0.0549 0.0332  -0.0524 83  ARG E CB    
5718  C CG    . ARG E 82  ? 0.4499 0.4696 0.4736 -0.0550 0.0359  -0.0517 83  ARG E CG    
5719  C CD    . ARG E 82  ? 0.4914 0.5107 0.5149 -0.0583 0.0381  -0.0509 83  ARG E CD    
5720  N NE    . ARG E 82  ? 0.4769 0.4966 0.4994 -0.0583 0.0406  -0.0501 83  ARG E NE    
5721  C CZ    . ARG E 82  ? 0.5183 0.5365 0.5391 -0.0607 0.0426  -0.0489 83  ARG E CZ    
5722  N NH1   . ARG E 82  ? 0.5737 0.5894 0.5936 -0.0633 0.0424  -0.0484 83  ARG E NH1   
5723  N NH2   . ARG E 82  ? 0.5372 0.5559 0.5569 -0.0604 0.0448  -0.0482 83  ARG E NH2   
5724  N N     . ALA E 83  ? 0.4452 0.4567 0.4626 -0.0519 0.0275  -0.0526 84  ALA E N     
5725  C CA    . ALA E 83  ? 0.4661 0.4766 0.4828 -0.0519 0.0249  -0.0535 84  ALA E CA    
5726  C C     . ALA E 83  ? 0.4222 0.4326 0.4377 -0.0491 0.0227  -0.0537 84  ALA E C     
5727  O O     . ALA E 83  ? 0.4401 0.4510 0.4561 -0.0487 0.0201  -0.0547 84  ALA E O     
5728  C CB    . ALA E 83  ? 0.5033 0.5085 0.5153 -0.0528 0.0250  -0.0529 84  ALA E CB    
5729  N N     . GLY E 84  ? 0.3886 0.3981 0.4025 -0.0473 0.0235  -0.0526 85  GLY E N     
5730  C CA    . GLY E 84  ? 0.4082 0.4175 0.4210 -0.0448 0.0214  -0.0525 85  GLY E CA    
5731  C C     . GLY E 84  ? 0.4132 0.4176 0.4199 -0.0438 0.0212  -0.0510 85  GLY E C     
5732  O O     . GLY E 84  ? 0.4528 0.4562 0.4575 -0.0422 0.0190  -0.0507 85  GLY E O     
5733  N N     . LYS E 85  ? 0.4135 0.4153 0.4175 -0.0447 0.0233  -0.0499 86  LYS E N     
5734  C CA    . LYS E 85  ? 0.4336 0.4315 0.4322 -0.0439 0.0235  -0.0486 86  LYS E CA    
5735  C C     . LYS E 85  ? 0.4006 0.3977 0.3981 -0.0427 0.0246  -0.0471 86  LYS E C     
5736  O O     . LYS E 85  ? 0.3230 0.3212 0.3225 -0.0432 0.0265  -0.0469 86  LYS E O     
5737  C CB    . LYS E 85  ? 0.4689 0.4643 0.4652 -0.0452 0.0250  -0.0484 86  LYS E CB    
5738  C CG    . LYS E 85  ? 0.5278 0.5229 0.5244 -0.0464 0.0237  -0.0498 86  LYS E CG    
5739  C CD    . LYS E 85  ? 0.5567 0.5490 0.5514 -0.0477 0.0251  -0.0497 86  LYS E CD    
5740  C CE    . LYS E 85  ? 0.5918 0.5839 0.5877 -0.0493 0.0238  -0.0512 86  LYS E CE    
5741  N NZ    . LYS E 85  ? 0.6509 0.6423 0.6446 -0.0483 0.0214  -0.0521 86  LYS E NZ    
5742  N N     . LYS E 86  ? 0.3922 0.3874 0.3863 -0.0414 0.0235  -0.0461 87  LYS E N     
5743  C CA    . LYS E 86  ? 0.3927 0.3864 0.3850 -0.0406 0.0245  -0.0445 87  LYS E CA    
5744  C C     . LYS E 86  ? 0.3956 0.3875 0.3857 -0.0415 0.0269  -0.0438 87  LYS E C     
5745  O O     . LYS E 86  ? 0.4032 0.3931 0.3897 -0.0415 0.0270  -0.0432 87  LYS E O     
5746  C CB    . LYS E 86  ? 0.3753 0.3671 0.3640 -0.0394 0.0226  -0.0434 87  LYS E CB    
5747  C CG    . LYS E 86  ? 0.3937 0.3837 0.3803 -0.0388 0.0234  -0.0416 87  LYS E CG    
5748  C CD    . LYS E 86  ? 0.3838 0.3720 0.3673 -0.0379 0.0213  -0.0404 87  LYS E CD    
5749  C CE    . LYS E 86  ? 0.3974 0.3847 0.3772 -0.0381 0.0204  -0.0403 87  LYS E CE    
5750  N NZ    . LYS E 86  ? 0.4203 0.4056 0.3964 -0.0375 0.0187  -0.0387 87  LYS E NZ    
5751  N N     . THR E 87  ? 0.3889 0.3817 0.3813 -0.0422 0.0287  -0.0438 88  THR E N     
5752  C CA    . THR E 87  ? 0.3769 0.3681 0.3679 -0.0431 0.0307  -0.0433 88  THR E CA    
5753  C C     . THR E 87  ? 0.3645 0.3543 0.3537 -0.0425 0.0319  -0.0419 88  THR E C     
5754  O O     . THR E 87  ? 0.3920 0.3828 0.3827 -0.0418 0.0318  -0.0416 88  THR E O     
5755  C CB    . THR E 87  ? 0.3621 0.3549 0.3563 -0.0445 0.0320  -0.0442 88  THR E CB    
5756  O OG1   . THR E 87  ? 0.4063 0.4006 0.4024 -0.0452 0.0306  -0.0455 88  THR E OG1   
5757  C CG2   . THR E 87  ? 0.3620 0.3526 0.3545 -0.0456 0.0337  -0.0436 88  THR E CG2   
5758  N N     . VAL E 88  ? 0.3625 0.3503 0.3487 -0.0426 0.0328  -0.0411 89  VAL E N     
5759  C CA    . VAL E 88  ? 0.3741 0.3607 0.3588 -0.0422 0.0340  -0.0398 89  VAL E CA    
5760  C C     . VAL E 88  ? 0.3815 0.3671 0.3658 -0.0430 0.0357  -0.0397 89  VAL E C     
5761  O O     . VAL E 88  ? 0.4283 0.4128 0.4113 -0.0433 0.0357  -0.0403 89  VAL E O     
5762  C CB    . VAL E 88  ? 0.3751 0.3607 0.3565 -0.0415 0.0334  -0.0387 89  VAL E CB    
5763  C CG1   . VAL E 88  ? 0.4027 0.3873 0.3826 -0.0415 0.0348  -0.0375 89  VAL E CG1   
5764  C CG2   . VAL E 88  ? 0.3903 0.3762 0.3718 -0.0408 0.0317  -0.0382 89  VAL E CG2   
5765  N N     . CYS E 89  ? 0.4340 0.4194 0.4190 -0.0431 0.0368  -0.0392 90  CYS E N     
5766  C CA    . CYS E 89  ? 0.4364 0.4205 0.4207 -0.0437 0.0383  -0.0389 90  CYS E CA    
5767  C C     . CYS E 89  ? 0.4579 0.4408 0.4400 -0.0429 0.0388  -0.0378 90  CYS E C     
5768  O O     . CYS E 89  ? 0.4000 0.3832 0.3822 -0.0424 0.0387  -0.0370 90  CYS E O     
5769  C CB    . CYS E 89  ? 0.5008 0.4856 0.4872 -0.0444 0.0393  -0.0390 90  CYS E CB    
5770  S SG    . CYS E 89  ? 0.6336 0.6162 0.6185 -0.0452 0.0408  -0.0385 90  CYS E SG    
5771  N N     . ALA E 90  ? 0.4490 0.4306 0.4292 -0.0428 0.0391  -0.0378 91  ALA E N     
5772  C CA    . ALA E 90  ? 0.4416 0.4227 0.4201 -0.0421 0.0396  -0.0369 91  ALA E CA    
5773  C C     . ALA E 90  ? 0.4769 0.4565 0.4550 -0.0422 0.0406  -0.0367 91  ALA E C     
5774  O O     . ALA E 90  ? 0.4766 0.4550 0.4538 -0.0422 0.0407  -0.0374 91  ALA E O     
5775  C CB    . ALA E 90  ? 0.4372 0.4185 0.4137 -0.0416 0.0391  -0.0372 91  ALA E CB    
5776  N N     . LEU E 91  ? 0.4835 0.4632 0.4623 -0.0423 0.0412  -0.0360 92  LEU E N     
5777  C CA    . LEU E 91  ? 0.4871 0.4653 0.4653 -0.0423 0.0419  -0.0356 92  LEU E CA    
5778  C C     . LEU E 91  ? 0.4637 0.4422 0.4411 -0.0416 0.0421  -0.0348 92  LEU E C     
5779  O O     . LEU E 91  ? 0.5233 0.5031 0.5009 -0.0414 0.0418  -0.0342 92  LEU E O     
5780  C CB    . LEU E 91  ? 0.4873 0.4652 0.4666 -0.0431 0.0424  -0.0355 92  LEU E CB    
5781  C CG    . LEU E 91  ? 0.5482 0.5267 0.5288 -0.0441 0.0424  -0.0363 92  LEU E CG    
5782  C CD1   . LEU E 91  ? 0.5943 0.5728 0.5756 -0.0449 0.0433  -0.0361 92  LEU E CD1   
5783  C CD2   . LEU E 91  ? 0.5533 0.5305 0.5333 -0.0446 0.0421  -0.0370 92  LEU E CD2   
5784  N N     . TYR E 92  ? 0.4251 0.4025 0.4016 -0.0412 0.0424  -0.0348 93  TYR E N     
5785  C CA    . TYR E 92  ? 0.4557 0.4339 0.4318 -0.0405 0.0426  -0.0342 93  TYR E CA    
5786  C C     . TYR E 92  ? 0.5348 0.5131 0.5117 -0.0408 0.0427  -0.0332 93  TYR E C     
5787  O O     . TYR E 92  ? 0.5915 0.5687 0.5687 -0.0413 0.0428  -0.0333 93  TYR E O     
5788  C CB    . TYR E 92  ? 0.4143 0.3913 0.3897 -0.0397 0.0427  -0.0346 93  TYR E CB    
5789  C CG    . TYR E 92  ? 0.4007 0.3753 0.3758 -0.0400 0.0427  -0.0344 93  TYR E CG    
5790  C CD1   . TYR E 92  ? 0.4106 0.3829 0.3852 -0.0407 0.0427  -0.0349 93  TYR E CD1   
5791  C CD2   . TYR E 92  ? 0.4283 0.4028 0.4035 -0.0396 0.0428  -0.0337 93  TYR E CD2   
5792  C CE1   . TYR E 92  ? 0.4142 0.3842 0.3880 -0.0412 0.0427  -0.0345 93  TYR E CE1   
5793  C CE2   . TYR E 92  ? 0.4039 0.3760 0.3782 -0.0399 0.0427  -0.0335 93  TYR E CE2   
5794  C CZ    . TYR E 92  ? 0.4077 0.3776 0.3813 -0.0407 0.0428  -0.0338 93  TYR E CZ    
5795  O OH    . TYR E 92  ? 0.4876 0.4549 0.4599 -0.0411 0.0427  -0.0333 93  TYR E OH    
5796  N N     . GLY E 93  ? 0.5192 0.4989 0.4962 -0.0406 0.0426  -0.0324 94  GLY E N     
5797  C CA    . GLY E 93  ? 0.4983 0.4778 0.4759 -0.0409 0.0424  -0.0316 94  GLY E CA    
5798  C C     . GLY E 93  ? 0.4369 0.4164 0.4152 -0.0413 0.0419  -0.0316 94  GLY E C     
5799  O O     . GLY E 93  ? 0.4366 0.4169 0.4149 -0.0414 0.0415  -0.0315 94  GLY E O     
5800  N N     . HIS E 94  ? 0.3568 0.3353 0.3355 -0.0414 0.0419  -0.0316 95  HIS E N     
5801  C CA    . HIS E 94  ? 0.3598 0.3384 0.3393 -0.0415 0.0415  -0.0319 95  HIS E CA    
5802  C C     . HIS E 94  ? 0.3753 0.3539 0.3553 -0.0418 0.0421  -0.0329 95  HIS E C     
5803  O O     . HIS E 94  ? 0.4056 0.3834 0.3851 -0.0420 0.0428  -0.0331 95  HIS E O     
5804  C CB    . HIS E 94  ? 0.3513 0.3292 0.3310 -0.0414 0.0411  -0.0315 95  HIS E CB    
5805  C CG    . HIS E 94  ? 0.3284 0.3064 0.3090 -0.0411 0.0404  -0.0320 95  HIS E CG    
5806  N ND1   . HIS E 94  ? 0.3038 0.2826 0.2854 -0.0410 0.0406  -0.0330 95  HIS E ND1   
5807  C CD2   . HIS E 94  ? 0.2896 0.2669 0.2704 -0.0408 0.0393  -0.0316 95  HIS E CD2   
5808  C CE1   . HIS E 94  ? 0.3077 0.2866 0.2902 -0.0405 0.0397  -0.0334 95  HIS E CE1   
5809  N NE2   . HIS E 94  ? 0.2966 0.2742 0.2785 -0.0403 0.0389  -0.0326 95  HIS E NE2   
5810  N N     . PRO E 95  ? 0.4153 0.3949 0.3962 -0.0418 0.0417  -0.0335 96  PRO E N     
5811  C CA    . PRO E 95  ? 0.4231 0.4032 0.4048 -0.0423 0.0422  -0.0344 96  PRO E CA    
5812  C C     . PRO E 95  ? 0.4116 0.3920 0.3940 -0.0426 0.0430  -0.0349 96  PRO E C     
5813  O O     . PRO E 95  ? 0.4373 0.4181 0.4202 -0.0434 0.0437  -0.0355 96  PRO E O     
5814  C CB    . PRO E 95  ? 0.4050 0.3864 0.3878 -0.0422 0.0413  -0.0349 96  PRO E CB    
5815  C CG    . PRO E 95  ? 0.3899 0.3713 0.3727 -0.0415 0.0403  -0.0343 96  PRO E CG    
5816  C CD    . PRO E 95  ? 0.4114 0.3917 0.3927 -0.0415 0.0406  -0.0332 96  PRO E CD    
5817  N N     . GLY E 96  ? 0.3745 0.3547 0.3569 -0.0421 0.0428  -0.0347 97  GLY E N     
5818  C CA    . GLY E 96  ? 0.3917 0.3725 0.3746 -0.0421 0.0434  -0.0354 97  GLY E CA    
5819  C C     . GLY E 96  ? 0.3857 0.3649 0.3668 -0.0422 0.0440  -0.0348 97  GLY E C     
5820  O O     . GLY E 96  ? 0.3459 0.3254 0.3267 -0.0424 0.0447  -0.0353 97  GLY E O     
5821  N N     . VAL E 97  ? 0.4261 0.4038 0.4059 -0.0422 0.0437  -0.0339 98  VAL E N     
5822  C CA    . VAL E 97  ? 0.4531 0.4292 0.4313 -0.0421 0.0438  -0.0333 98  VAL E CA    
5823  C C     . VAL E 97  ? 0.4901 0.4650 0.4669 -0.0428 0.0446  -0.0331 98  VAL E C     
5824  O O     . VAL E 97  ? 0.5253 0.4995 0.5018 -0.0429 0.0445  -0.0329 98  VAL E O     
5825  C CB    . VAL E 97  ? 0.4984 0.4739 0.4763 -0.0416 0.0429  -0.0325 98  VAL E CB    
5826  C CG1   . VAL E 97  ? 0.4972 0.4712 0.4736 -0.0415 0.0429  -0.0320 98  VAL E CG1   
5827  C CG2   . VAL E 97  ? 0.4728 0.4488 0.4517 -0.0411 0.0419  -0.0325 98  VAL E CG2   
5828  N N     . PHE E 98  ? 0.4917 0.4660 0.4673 -0.0433 0.0454  -0.0333 99  PHE E N     
5829  C CA    . PHE E 98  ? 0.4453 0.4179 0.4192 -0.0443 0.0460  -0.0329 99  PHE E CA    
5830  C C     . PHE E 98  ? 0.4468 0.4198 0.4216 -0.0450 0.0462  -0.0331 99  PHE E C     
5831  O O     . PHE E 98  ? 0.4455 0.4164 0.4191 -0.0454 0.0461  -0.0327 99  PHE E O     
5832  C CB    . PHE E 98  ? 0.4686 0.4388 0.4406 -0.0437 0.0453  -0.0321 99  PHE E CB    
5833  C CG    . PHE E 98  ? 0.4242 0.3936 0.3948 -0.0433 0.0451  -0.0318 99  PHE E CG    
5834  C CD1   . PHE E 98  ? 0.4019 0.3722 0.3735 -0.0424 0.0444  -0.0320 99  PHE E CD1   
5835  C CD2   . PHE E 98  ? 0.4328 0.4002 0.4008 -0.0439 0.0455  -0.0313 99  PHE E CD2   
5836  C CE1   . PHE E 98  ? 0.4298 0.3991 0.3999 -0.0421 0.0441  -0.0319 99  PHE E CE1   
5837  C CE2   . PHE E 98  ? 0.4434 0.4099 0.4098 -0.0435 0.0452  -0.0312 99  PHE E CE2   
5838  C CZ    . PHE E 98  ? 0.4419 0.4095 0.4095 -0.0425 0.0445  -0.0316 99  PHE E CZ    
5839  N N     . ALA E 99  ? 0.4779 0.4533 0.4549 -0.0451 0.0464  -0.0339 100 ALA E N     
5840  C CA    . ALA E 99  ? 0.4809 0.4569 0.4590 -0.0459 0.0464  -0.0343 100 ALA E CA    
5841  C C     . ALA E 99  ? 0.5056 0.4844 0.4856 -0.0466 0.0471  -0.0352 100 ALA E C     
5842  O O     . ALA E 99  ? 0.5446 0.5255 0.5265 -0.0457 0.0467  -0.0359 100 ALA E O     
5843  C CB    . ALA E 99  ? 0.5127 0.4891 0.4916 -0.0449 0.0454  -0.0344 100 ALA E CB    
5844  N N     . CYS E 100 ? 0.4962 0.4751 0.4760 -0.0482 0.0481  -0.0352 101 CYS E N     
5845  C CA    . CYS E 100 ? 0.5401 0.5222 0.5220 -0.0491 0.0490  -0.0361 101 CYS E CA    
5846  C C     . CYS E 100 ? 0.5064 0.4904 0.4909 -0.0494 0.0485  -0.0369 101 CYS E C     
5847  O O     . CYS E 100 ? 0.4971 0.4846 0.4843 -0.0494 0.0487  -0.0379 101 CYS E O     
5848  C CB    . CYS E 100 ? 0.5618 0.5434 0.5422 -0.0510 0.0505  -0.0356 101 CYS E CB    
5849  S SG    . CYS E 100 ? 0.5848 0.5629 0.5634 -0.0529 0.0501  -0.0346 101 CYS E SG    
5850  N N     . VAL E 101 ? 0.5499 0.5316 0.5335 -0.0497 0.0476  -0.0365 102 VAL E N     
5851  C CA    . VAL E 101 ? 0.5201 0.5031 0.5057 -0.0502 0.0470  -0.0373 102 VAL E CA    
5852  C C     . VAL E 101 ? 0.4492 0.4353 0.4374 -0.0489 0.0462  -0.0382 102 VAL E C     
5853  O O     . VAL E 101 ? 0.4252 0.4143 0.4160 -0.0495 0.0463  -0.0392 102 VAL E O     
5854  C CB    . VAL E 101 ? 0.5934 0.5734 0.5773 -0.0500 0.0459  -0.0369 102 VAL E CB    
5855  C CG1   . VAL E 101 ? 0.6513 0.6325 0.6370 -0.0502 0.0449  -0.0379 102 VAL E CG1   
5856  C CG2   . VAL E 101 ? 0.6349 0.6114 0.6164 -0.0513 0.0462  -0.0361 102 VAL E CG2   
5857  N N     . SER E 102 ? 0.4050 0.3902 0.3923 -0.0472 0.0454  -0.0379 103 SER E N     
5858  C CA    . SER E 102 ? 0.4953 0.4825 0.4844 -0.0459 0.0443  -0.0385 103 SER E CA    
5859  C C     . SER E 102 ? 0.4903 0.4804 0.4816 -0.0455 0.0448  -0.0395 103 SER E C     
5860  O O     . SER E 102 ? 0.5551 0.5479 0.5491 -0.0453 0.0442  -0.0405 103 SER E O     
5861  C CB    . SER E 102 ? 0.5512 0.5366 0.5387 -0.0445 0.0434  -0.0377 103 SER E CB    
5862  O OG    . SER E 102 ? 0.5485 0.5320 0.5343 -0.0446 0.0430  -0.0372 103 SER E OG    
5863  N N     . HIS E 103 ? 0.5196 0.5093 0.5099 -0.0454 0.0458  -0.0392 104 HIS E N     
5864  C CA    . HIS E 103 ? 0.4382 0.4309 0.4303 -0.0449 0.0465  -0.0403 104 HIS E CA    
5865  C C     . HIS E 103 ? 0.3997 0.3958 0.3944 -0.0463 0.0474  -0.0413 104 HIS E C     
5866  O O     . HIS E 103 ? 0.3395 0.3391 0.3371 -0.0456 0.0472  -0.0428 104 HIS E O     
5867  C CB    . HIS E 103 ? 0.4483 0.4397 0.4383 -0.0449 0.0475  -0.0399 104 HIS E CB    
5868  C CG    . HIS E 103 ? 0.4547 0.4435 0.4429 -0.0435 0.0465  -0.0391 104 HIS E CG    
5869  N ND1   . HIS E 103 ? 0.4173 0.4065 0.4064 -0.0418 0.0453  -0.0398 104 HIS E ND1   
5870  C CD2   . HIS E 103 ? 0.4465 0.4321 0.4320 -0.0436 0.0463  -0.0379 104 HIS E CD2   
5871  C CE1   . HIS E 103 ? 0.4009 0.3873 0.3881 -0.0412 0.0445  -0.0388 104 HIS E CE1   
5872  N NE2   . HIS E 103 ? 0.4284 0.4129 0.4135 -0.0422 0.0451  -0.0377 104 HIS E NE2   
5873  N N     . MET E 104 ? 0.3826 0.3777 0.3762 -0.0484 0.0484  -0.0406 105 MET E N     
5874  C CA    . MET E 104 ? 0.3716 0.3698 0.3675 -0.0502 0.0494  -0.0413 105 MET E CA    
5875  C C     . MET E 104 ? 0.3468 0.3471 0.3457 -0.0500 0.0480  -0.0423 105 MET E C     
5876  O O     . MET E 104 ? 0.3261 0.3307 0.3284 -0.0504 0.0484  -0.0436 105 MET E O     
5877  C CB    . MET E 104 ? 0.4196 0.4153 0.4132 -0.0526 0.0503  -0.0401 105 MET E CB    
5878  C CG    . MET E 104 ? 0.4825 0.4767 0.4732 -0.0533 0.0519  -0.0392 105 MET E CG    
5879  S SD    . MET E 104 ? 0.5846 0.5745 0.5720 -0.0558 0.0523  -0.0375 105 MET E SD    
5880  C CE    . MET E 104 ? 0.6326 0.6260 0.6230 -0.0587 0.0532  -0.0381 105 MET E CE    
5881  N N     . ALA E 105 ? 0.3097 0.3072 0.3073 -0.0493 0.0465  -0.0418 106 ALA E N     
5882  C CA    . ALA E 105 ? 0.3148 0.3136 0.3145 -0.0491 0.0449  -0.0426 106 ALA E CA    
5883  C C     . ALA E 105 ? 0.3454 0.3471 0.3477 -0.0472 0.0439  -0.0438 106 ALA E C     
5884  O O     . ALA E 105 ? 0.3332 0.3386 0.3390 -0.0473 0.0434  -0.0451 106 ALA E O     
5885  C CB    . ALA E 105 ? 0.3335 0.3285 0.3306 -0.0486 0.0436  -0.0417 106 ALA E CB    
5886  N N     . ILE E 106 ? 0.3532 0.3534 0.3541 -0.0453 0.0434  -0.0434 107 ILE E N     
5887  C CA    . ILE E 106 ? 0.3684 0.3703 0.3712 -0.0433 0.0421  -0.0444 107 ILE E CA    
5888  C C     . ILE E 106 ? 0.3589 0.3654 0.3651 -0.0432 0.0431  -0.0460 107 ILE E C     
5889  O O     . ILE E 106 ? 0.3804 0.3901 0.3899 -0.0422 0.0420  -0.0475 107 ILE E O     
5890  C CB    . ILE E 106 ? 0.3744 0.3733 0.3748 -0.0417 0.0414  -0.0435 107 ILE E CB    
5891  C CG1   . ILE E 106 ? 0.3821 0.3774 0.3796 -0.0417 0.0403  -0.0420 107 ILE E CG1   
5892  C CG2   . ILE E 106 ? 0.3871 0.3875 0.3894 -0.0396 0.0400  -0.0446 107 ILE E CG2   
5893  C CD1   . ILE E 106 ? 0.3833 0.3759 0.3787 -0.0405 0.0395  -0.0410 107 ILE E CD1   
5894  N N     . THR E 107 ? 0.3621 0.3691 0.3674 -0.0442 0.0452  -0.0458 108 THR E N     
5895  C CA    . THR E 107 ? 0.3690 0.3808 0.3772 -0.0443 0.0467  -0.0474 108 THR E CA    
5896  C C     . THR E 107 ? 0.3981 0.4142 0.4102 -0.0456 0.0468  -0.0485 108 THR E C     
5897  O O     . THR E 107 ? 0.4145 0.4350 0.4303 -0.0445 0.0463  -0.0504 108 THR E O     
5898  C CB    . THR E 107 ? 0.3802 0.3914 0.3859 -0.0458 0.0491  -0.0466 108 THR E CB    
5899  O OG1   . THR E 107 ? 0.3855 0.3931 0.3882 -0.0443 0.0486  -0.0459 108 THR E OG1   
5900  C CG2   . THR E 107 ? 0.3996 0.4161 0.4079 -0.0463 0.0510  -0.0482 108 THR E CG2   
5901  N N     . ARG E 108 ? 0.3921 0.4068 0.4032 -0.0480 0.0472  -0.0475 109 ARG E N     
5902  C CA    . ARG E 108 ? 0.3938 0.4123 0.4083 -0.0499 0.0474  -0.0483 109 ARG E CA    
5903  C C     . ARG E 108 ? 0.4088 0.4286 0.4260 -0.0483 0.0449  -0.0495 109 ARG E C     
5904  O O     . ARG E 108 ? 0.4256 0.4504 0.4472 -0.0486 0.0447  -0.0511 109 ARG E O     
5905  C CB    . ARG E 108 ? 0.4190 0.4345 0.4312 -0.0527 0.0481  -0.0468 109 ARG E CB    
5906  C CG    . ARG E 108 ? 0.4493 0.4684 0.4647 -0.0553 0.0487  -0.0475 109 ARG E CG    
5907  C CD    . ARG E 108 ? 0.4750 0.4904 0.4877 -0.0582 0.0493  -0.0459 109 ARG E CD    
5908  N NE    . ARG E 108 ? 0.5047 0.5176 0.5139 -0.0591 0.0512  -0.0446 109 ARG E NE    
5909  C CZ    . ARG E 108 ? 0.5373 0.5466 0.5436 -0.0615 0.0519  -0.0430 109 ARG E CZ    
5910  N NH1   . ARG E 108 ? 0.5503 0.5579 0.5568 -0.0633 0.0508  -0.0428 109 ARG E NH1   
5911  N NH2   . ARG E 108 ? 0.5212 0.5283 0.5242 -0.0621 0.0534  -0.0418 109 ARG E NH2   
5912  N N     . ALA E 109 ? 0.3881 0.4038 0.4028 -0.0468 0.0430  -0.0486 110 ALA E N     
5913  C CA    . ALA E 109 ? 0.3750 0.3911 0.3913 -0.0454 0.0404  -0.0494 110 ALA E CA    
5914  C C     . ALA E 109 ? 0.3999 0.4197 0.4196 -0.0431 0.0395  -0.0512 110 ALA E C     
5915  O O     . ALA E 109 ? 0.3746 0.3977 0.3979 -0.0425 0.0380  -0.0526 110 ALA E O     
5916  C CB    . ALA E 109 ? 0.4027 0.4135 0.4149 -0.0443 0.0389  -0.0479 110 ALA E CB    
5917  N N     . LYS E 110 ? 0.4496 0.4688 0.4683 -0.0416 0.0402  -0.0512 111 LYS E N     
5918  C CA    . LYS E 110 ? 0.4864 0.5087 0.5080 -0.0391 0.0392  -0.0530 111 LYS E CA    
5919  C C     . LYS E 110 ? 0.4920 0.5211 0.5186 -0.0398 0.0406  -0.0550 111 LYS E C     
5920  O O     . LYS E 110 ? 0.4829 0.5158 0.5135 -0.0382 0.0391  -0.0569 111 LYS E O     
5921  C CB    . LYS E 110 ? 0.4980 0.5179 0.5172 -0.0377 0.0398  -0.0526 111 LYS E CB    
5922  C CG    . LYS E 110 ? 0.5380 0.5519 0.5530 -0.0366 0.0381  -0.0509 111 LYS E CG    
5923  C CD    . LYS E 110 ? 0.5666 0.5782 0.5794 -0.0354 0.0387  -0.0506 111 LYS E CD    
5924  C CE    . LYS E 110 ? 0.6375 0.6438 0.6470 -0.0344 0.0367  -0.0490 111 LYS E CE    
5925  N NZ    . LYS E 110 ? 0.6811 0.6871 0.6920 -0.0324 0.0338  -0.0497 111 LYS E NZ    
5926  N N     . ALA E 111 ? 0.5130 0.5437 0.5392 -0.0423 0.0434  -0.0546 112 ALA E N     
5927  C CA    . ALA E 111 ? 0.4833 0.5208 0.5139 -0.0435 0.0453  -0.0563 112 ALA E CA    
5928  C C     . ALA E 111 ? 0.4815 0.5227 0.5163 -0.0443 0.0440  -0.0573 112 ALA E C     
5929  O O     . ALA E 111 ? 0.6079 0.6557 0.6478 -0.0442 0.0444  -0.0594 112 ALA E O     
5930  C CB    . ALA E 111 ? 0.4438 0.4813 0.4723 -0.0465 0.0484  -0.0551 112 ALA E CB    
5931  N N     . GLU E 112 ? 0.4535 0.4905 0.4862 -0.0452 0.0423  -0.0560 113 GLU E N     
5932  C CA    . GLU E 112 ? 0.4593 0.4989 0.4954 -0.0462 0.0408  -0.0568 113 GLU E CA    
5933  C C     . GLU E 112 ? 0.4417 0.4808 0.4790 -0.0431 0.0374  -0.0578 113 GLU E C     
5934  O O     . GLU E 112 ? 0.3939 0.4344 0.4334 -0.0433 0.0355  -0.0585 113 GLU E O     
5935  C CB    . GLU E 112 ? 0.5313 0.5668 0.5644 -0.0489 0.0409  -0.0550 113 GLU E CB    
5936  C CG    . GLU E 112 ? 0.5322 0.5679 0.5641 -0.0521 0.0439  -0.0540 113 GLU E CG    
5937  C CD    . GLU E 112 ? 0.5566 0.5883 0.5860 -0.0548 0.0438  -0.0525 113 GLU E CD    
5938  O OE1   . GLU E 112 ? 0.5556 0.5848 0.5843 -0.0542 0.0414  -0.0525 113 GLU E OE1   
5939  O OE2   . GLU E 112 ? 0.5683 0.5994 0.5964 -0.0576 0.0459  -0.0515 113 GLU E OE2   
5940  N N     . GLY E 113 ? 0.4201 0.4569 0.4556 -0.0403 0.0366  -0.0578 114 GLY E N     
5941  C CA    . GLY E 113 ? 0.4172 0.4534 0.4538 -0.0372 0.0333  -0.0587 114 GLY E CA    
5942  C C     . GLY E 113 ? 0.4380 0.4682 0.4704 -0.0371 0.0310  -0.0569 114 GLY E C     
5943  O O     . GLY E 113 ? 0.4172 0.4474 0.4507 -0.0356 0.0282  -0.0575 114 GLY E O     
5944  N N     . PHE E 114 ? 0.4789 0.5042 0.5064 -0.0385 0.0323  -0.0548 115 PHE E N     
5945  C CA    . PHE E 114 ? 0.4584 0.4784 0.4817 -0.0383 0.0306  -0.0531 115 PHE E CA    
5946  C C     . PHE E 114 ? 0.4663 0.4818 0.4858 -0.0367 0.0303  -0.0517 115 PHE E C     
5947  O O     . PHE E 114 ? 0.4913 0.5068 0.5102 -0.0367 0.0321  -0.0516 115 PHE E O     
5948  C CB    . PHE E 114 ? 0.4301 0.4477 0.4507 -0.0410 0.0320  -0.0517 115 PHE E CB    
5949  C CG    . PHE E 114 ? 0.4718 0.4928 0.4956 -0.0429 0.0319  -0.0528 115 PHE E CG    
5950  C CD1   . PHE E 114 ? 0.4637 0.4853 0.4886 -0.0424 0.0292  -0.0535 115 PHE E CD1   
5951  C CD2   . PHE E 114 ? 0.4454 0.4686 0.4706 -0.0455 0.0344  -0.0529 115 PHE E CD2   
5952  C CE1   . PHE E 114 ? 0.4610 0.4855 0.4889 -0.0442 0.0290  -0.0546 115 PHE E CE1   
5953  C CE2   . PHE E 114 ? 0.4373 0.4634 0.4655 -0.0475 0.0342  -0.0538 115 PHE E CE2   
5954  C CZ    . PHE E 114 ? 0.4347 0.4615 0.4643 -0.0469 0.0315  -0.0547 115 PHE E CZ    
5955  N N     . SER E 115 ? 0.4385 0.4504 0.4553 -0.0355 0.0279  -0.0508 116 SER E N     
5956  C CA    . SER E 115 ? 0.4613 0.4686 0.4741 -0.0345 0.0274  -0.0491 116 SER E CA    
5957  C C     . SER E 115 ? 0.4338 0.4383 0.4430 -0.0364 0.0296  -0.0474 116 SER E C     
5958  O O     . SER E 115 ? 0.4075 0.4111 0.4152 -0.0378 0.0299  -0.0468 116 SER E O     
5959  C CB    . SER E 115 ? 0.4471 0.4515 0.4579 -0.0332 0.0244  -0.0483 116 SER E CB    
5960  O OG    . SER E 115 ? 0.4426 0.4426 0.4495 -0.0327 0.0240  -0.0466 116 SER E OG    
5961  N N     . ALA E 116 ? 0.3696 0.3728 0.3775 -0.0361 0.0310  -0.0468 117 ALA E N     
5962  C CA    . ALA E 116 ? 0.3553 0.3558 0.3600 -0.0376 0.0330  -0.0453 117 ALA E CA    
5963  C C     . ALA E 116 ? 0.3783 0.3761 0.3808 -0.0366 0.0330  -0.0443 117 ALA E C     
5964  O O     . ALA E 116 ? 0.3563 0.3552 0.3605 -0.0354 0.0329  -0.0453 117 ALA E O     
5965  C CB    . ALA E 116 ? 0.3897 0.3927 0.3959 -0.0393 0.0355  -0.0459 117 ALA E CB    
5966  N N     . LYS E 117 ? 0.3764 0.3707 0.3754 -0.0372 0.0332  -0.0425 118 LYS E N     
5967  C CA    . LYS E 117 ? 0.3813 0.3729 0.3781 -0.0367 0.0331  -0.0414 118 LYS E CA    
5968  C C     . LYS E 117 ? 0.3757 0.3652 0.3695 -0.0380 0.0345  -0.0398 118 LYS E C     
5969  O O     . LYS E 117 ? 0.3631 0.3527 0.3562 -0.0390 0.0352  -0.0396 118 LYS E O     
5970  C CB    . LYS E 117 ? 0.4450 0.4344 0.4408 -0.0353 0.0305  -0.0408 118 LYS E CB    
5971  C CG    . LYS E 117 ? 0.4867 0.4744 0.4801 -0.0359 0.0294  -0.0395 118 LYS E CG    
5972  C CD    . LYS E 117 ? 0.5098 0.4948 0.5016 -0.0349 0.0268  -0.0384 118 LYS E CD    
5973  C CE    . LYS E 117 ? 0.5214 0.5051 0.5105 -0.0355 0.0259  -0.0371 118 LYS E CE    
5974  N NZ    . LYS E 117 ? 0.5412 0.5220 0.5283 -0.0349 0.0235  -0.0358 118 LYS E NZ    
5975  N N     . MET E 118 ? 0.4148 0.4023 0.4071 -0.0378 0.0349  -0.0390 119 MET E N     
5976  C CA    . MET E 118 ? 0.3762 0.3619 0.3660 -0.0388 0.0360  -0.0376 119 MET E CA    
5977  C C     . MET E 118 ? 0.3596 0.3428 0.3474 -0.0385 0.0348  -0.0361 119 MET E C     
5978  O O     . MET E 118 ? 0.3494 0.3316 0.3374 -0.0376 0.0338  -0.0361 119 MET E O     
5979  C CB    . MET E 118 ? 0.3755 0.3614 0.3654 -0.0392 0.0378  -0.0379 119 MET E CB    
5980  C CG    . MET E 118 ? 0.4282 0.4121 0.4156 -0.0399 0.0387  -0.0365 119 MET E CG    
5981  S SD    . MET E 118 ? 0.4596 0.4435 0.4467 -0.0403 0.0405  -0.0368 119 MET E SD    
5982  C CE    . MET E 118 ? 0.4419 0.4281 0.4306 -0.0413 0.0418  -0.0380 119 MET E CE    
5983  N N     . GLU E 119 ? 0.3833 0.3656 0.3689 -0.0392 0.0350  -0.0349 120 GLU E N     
5984  C CA    . GLU E 119 ? 0.3555 0.3359 0.3391 -0.0394 0.0342  -0.0333 120 GLU E CA    
5985  C C     . GLU E 119 ? 0.3118 0.2917 0.2945 -0.0400 0.0356  -0.0326 120 GLU E C     
5986  O O     . GLU E 119 ? 0.2804 0.2610 0.2628 -0.0405 0.0370  -0.0328 120 GLU E O     
5987  C CB    . GLU E 119 ? 0.3609 0.3412 0.3428 -0.0398 0.0335  -0.0324 120 GLU E CB    
5988  C CG    . GLU E 119 ? 0.4105 0.3907 0.3928 -0.0391 0.0315  -0.0327 120 GLU E CG    
5989  C CD    . GLU E 119 ? 0.4361 0.4143 0.4182 -0.0385 0.0296  -0.0320 120 GLU E CD    
5990  O OE1   . GLU E 119 ? 0.5619 0.5388 0.5435 -0.0387 0.0298  -0.0313 120 GLU E OE1   
5991  O OE2   . GLU E 119 ? 0.4803 0.4581 0.4626 -0.0378 0.0276  -0.0322 120 GLU E OE2   
5992  N N     . PRO E 120 ? 0.2691 0.2476 0.2514 -0.0399 0.0351  -0.0318 121 PRO E N     
5993  C CA    . PRO E 120 ? 0.2966 0.2746 0.2782 -0.0405 0.0362  -0.0312 121 PRO E CA    
5994  C C     . PRO E 120 ? 0.3219 0.3005 0.3021 -0.0412 0.0369  -0.0301 121 PRO E C     
5995  O O     . PRO E 120 ? 0.3494 0.3281 0.3286 -0.0415 0.0362  -0.0294 121 PRO E O     
5996  C CB    . PRO E 120 ? 0.2753 0.2515 0.2568 -0.0402 0.0350  -0.0307 121 PRO E CB    
5997  C CG    . PRO E 120 ? 0.2840 0.2593 0.2654 -0.0399 0.0331  -0.0303 121 PRO E CG    
5998  C CD    . PRO E 120 ? 0.2768 0.2536 0.2592 -0.0394 0.0332  -0.0315 121 PRO E CD    
5999  N N     . GLY E 121 ? 0.3151 0.2939 0.2951 -0.0415 0.0381  -0.0302 122 GLY E N     
6000  C CA    . GLY E 121 ? 0.3496 0.3293 0.3286 -0.0419 0.0388  -0.0294 122 GLY E CA    
6001  C C     . GLY E 121 ? 0.3621 0.3416 0.3411 -0.0421 0.0392  -0.0289 122 GLY E C     
6002  O O     . GLY E 121 ? 0.3675 0.3459 0.3470 -0.0419 0.0389  -0.0290 122 GLY E O     
6003  N N     . ILE E 122 ? 0.3923 0.3730 0.3708 -0.0423 0.0399  -0.0284 123 ILE E N     
6004  C CA    . ILE E 122 ? 0.3795 0.3605 0.3583 -0.0425 0.0401  -0.0280 123 ILE E CA    
6005  C C     . ILE E 122 ? 0.4038 0.3844 0.3827 -0.0418 0.0409  -0.0289 123 ILE E C     
6006  O O     . ILE E 122 ? 0.3999 0.3812 0.3784 -0.0414 0.0416  -0.0295 123 ILE E O     
6007  C CB    . ILE E 122 ? 0.3974 0.3806 0.3761 -0.0430 0.0404  -0.0270 123 ILE E CB    
6008  C CG1   . ILE E 122 ? 0.4228 0.4059 0.4010 -0.0440 0.0395  -0.0258 123 ILE E CG1   
6009  C CG2   . ILE E 122 ? 0.4147 0.3986 0.3941 -0.0431 0.0405  -0.0267 123 ILE E CG2   
6010  C CD1   . ILE E 122 ? 0.4278 0.4134 0.4055 -0.0449 0.0400  -0.0247 123 ILE E CD1   
6011  N N     . SER E 123 ? 0.3445 0.3237 0.3235 -0.0417 0.0407  -0.0291 124 SER E N     
6012  C CA    . SER E 123 ? 0.3629 0.3411 0.3414 -0.0412 0.0413  -0.0298 124 SER E CA    
6013  C C     . SER E 123 ? 0.3344 0.3132 0.3130 -0.0409 0.0413  -0.0295 124 SER E C     
6014  O O     . SER E 123 ? 0.3245 0.3048 0.3038 -0.0412 0.0410  -0.0288 124 SER E O     
6015  C CB    . SER E 123 ? 0.3807 0.3573 0.3590 -0.0412 0.0412  -0.0302 124 SER E CB    
6016  O OG    . SER E 123 ? 0.4163 0.3925 0.3948 -0.0413 0.0404  -0.0297 124 SER E OG    
6017  N N     . ALA E 124 ? 0.3519 0.3294 0.3298 -0.0404 0.0416  -0.0300 125 ALA E N     
6018  C CA    . ALA E 124 ? 0.3443 0.3220 0.3222 -0.0398 0.0413  -0.0300 125 ALA E CA    
6019  C C     . ALA E 124 ? 0.3421 0.3196 0.3204 -0.0400 0.0406  -0.0294 125 ALA E C     
6020  O O     . ALA E 124 ? 0.3420 0.3207 0.3211 -0.0398 0.0401  -0.0292 125 ALA E O     
6021  C CB    . ALA E 124 ? 0.3753 0.3509 0.3519 -0.0392 0.0415  -0.0305 125 ALA E CB    
6022  N N     . GLU E 125 ? 0.3374 0.3135 0.3152 -0.0405 0.0403  -0.0293 126 GLU E N     
6023  C CA    . GLU E 125 ? 0.3834 0.3589 0.3614 -0.0407 0.0394  -0.0290 126 GLU E CA    
6024  C C     . GLU E 125 ? 0.3687 0.3459 0.3481 -0.0414 0.0388  -0.0282 126 GLU E C     
6025  O O     . GLU E 125 ? 0.4467 0.4246 0.4269 -0.0416 0.0381  -0.0278 126 GLU E O     
6026  C CB    . GLU E 125 ? 0.4554 0.4292 0.4325 -0.0408 0.0394  -0.0295 126 GLU E CB    
6027  C CG    . GLU E 125 ? 0.4898 0.4625 0.4667 -0.0409 0.0383  -0.0293 126 GLU E CG    
6028  C CD    . GLU E 125 ? 0.5653 0.5369 0.5416 -0.0407 0.0382  -0.0301 126 GLU E CD    
6029  O OE1   . GLU E 125 ? 0.5684 0.5393 0.5434 -0.0404 0.0391  -0.0307 126 GLU E OE1   
6030  O OE2   . GLU E 125 ? 0.5717 0.5431 0.5488 -0.0409 0.0373  -0.0300 126 GLU E OE2   
6031  N N     . ALA E 126 ? 0.4000 0.3780 0.3797 -0.0418 0.0391  -0.0280 127 ALA E N     
6032  C CA    . ALA E 126 ? 0.3632 0.3425 0.3439 -0.0427 0.0386  -0.0270 127 ALA E CA    
6033  C C     . ALA E 126 ? 0.3469 0.3290 0.3286 -0.0429 0.0389  -0.0265 127 ALA E C     
6034  O O     . ALA E 126 ? 0.3124 0.2957 0.2951 -0.0438 0.0383  -0.0257 127 ALA E O     
6035  C CB    . ALA E 126 ? 0.3419 0.3214 0.3222 -0.0430 0.0387  -0.0268 127 ALA E CB    
6036  N N     . CYS E 127 ? 0.3167 0.2999 0.2982 -0.0420 0.0399  -0.0272 128 CYS E N     
6037  C CA    . CYS E 127 ? 0.2906 0.2768 0.2732 -0.0418 0.0403  -0.0272 128 CYS E CA    
6038  C C     . CYS E 127 ? 0.3125 0.2989 0.2961 -0.0415 0.0396  -0.0273 128 CYS E C     
6039  O O     . CYS E 127 ? 0.3587 0.3482 0.3441 -0.0419 0.0395  -0.0269 128 CYS E O     
6040  C CB    . CYS E 127 ? 0.3012 0.2878 0.2832 -0.0406 0.0412  -0.0283 128 CYS E CB    
6041  S SG    . CYS E 127 ? 0.3045 0.2912 0.2854 -0.0409 0.0419  -0.0284 128 CYS E SG    
6042  N N     . LEU E 128 ? 0.3617 0.3452 0.3443 -0.0409 0.0390  -0.0277 129 LEU E N     
6043  C CA    . LEU E 128 ? 0.3623 0.3456 0.3454 -0.0405 0.0381  -0.0279 129 LEU E CA    
6044  C C     . LEU E 128 ? 0.3502 0.3345 0.3347 -0.0417 0.0372  -0.0270 129 LEU E C     
6045  O O     . LEU E 128 ? 0.3626 0.3495 0.3489 -0.0418 0.0368  -0.0269 129 LEU E O     
6046  C CB    . LEU E 128 ? 0.3702 0.3498 0.3511 -0.0399 0.0378  -0.0284 129 LEU E CB    
6047  C CG    . LEU E 128 ? 0.3934 0.3719 0.3740 -0.0392 0.0367  -0.0285 129 LEU E CG    
6048  C CD1   . LEU E 128 ? 0.4548 0.4298 0.4328 -0.0387 0.0367  -0.0289 129 LEU E CD1   
6049  C CD2   . LEU E 128 ? 0.4541 0.4332 0.4359 -0.0401 0.0355  -0.0280 129 LEU E CD2   
6050  N N     . TRP E 129 ? 0.3347 0.3171 0.3185 -0.0426 0.0367  -0.0265 130 TRP E N     
6051  C CA    . TRP E 129 ? 0.3196 0.3020 0.3044 -0.0438 0.0355  -0.0258 130 TRP E CA    
6052  C C     . TRP E 129 ? 0.3459 0.3322 0.3329 -0.0450 0.0357  -0.0248 130 TRP E C     
6053  O O     . TRP E 129 ? 0.2995 0.2871 0.2880 -0.0458 0.0348  -0.0244 130 TRP E O     
6054  C CB    . TRP E 129 ? 0.3162 0.2960 0.2998 -0.0444 0.0349  -0.0255 130 TRP E CB    
6055  C CG    . TRP E 129 ? 0.3076 0.2843 0.2894 -0.0434 0.0349  -0.0265 130 TRP E CG    
6056  C CD1   . TRP E 129 ? 0.3171 0.2923 0.2978 -0.0431 0.0353  -0.0269 130 TRP E CD1   
6057  C CD2   . TRP E 129 ? 0.3114 0.2864 0.2920 -0.0425 0.0345  -0.0273 130 TRP E CD2   
6058  N NE1   . TRP E 129 ? 0.3298 0.3030 0.3090 -0.0422 0.0353  -0.0279 130 TRP E NE1   
6059  C CE2   . TRP E 129 ? 0.3416 0.3144 0.3205 -0.0419 0.0349  -0.0280 130 TRP E CE2   
6060  C CE3   . TRP E 129 ? 0.3021 0.2774 0.2831 -0.0422 0.0337  -0.0274 130 TRP E CE3   
6061  C CZ2   . TRP E 129 ? 0.3158 0.2867 0.2929 -0.0411 0.0348  -0.0288 130 TRP E CZ2   
6062  C CZ3   . TRP E 129 ? 0.3134 0.2863 0.2923 -0.0414 0.0334  -0.0281 130 TRP E CZ3   
6063  C CH2   . TRP E 129 ? 0.2983 0.2691 0.2752 -0.0409 0.0340  -0.0288 130 TRP E CH2   
6064  N N     . ALA E 130 ? 0.3721 0.3604 0.3590 -0.0451 0.0370  -0.0246 131 ALA E N     
6065  C CA    . ALA E 130 ? 0.3522 0.3446 0.3409 -0.0464 0.0375  -0.0237 131 ALA E CA    
6066  C C     . ALA E 130 ? 0.3676 0.3638 0.3581 -0.0455 0.0381  -0.0244 131 ALA E C     
6067  O O     . ALA E 130 ? 0.3560 0.3558 0.3488 -0.0467 0.0380  -0.0238 131 ALA E O     
6068  C CB    . ALA E 130 ? 0.3578 0.3507 0.3452 -0.0467 0.0386  -0.0233 131 ALA E CB    
6069  N N     . ASP E 131 ? 0.3841 0.3796 0.3739 -0.0436 0.0385  -0.0257 132 ASP E N     
6070  C CA    . ASP E 131 ? 0.3480 0.3468 0.3395 -0.0422 0.0389  -0.0267 132 ASP E CA    
6071  C C     . ASP E 131 ? 0.3801 0.3790 0.3731 -0.0419 0.0375  -0.0269 132 ASP E C     
6072  O O     . ASP E 131 ? 0.4217 0.4246 0.4172 -0.0415 0.0375  -0.0273 132 ASP E O     
6073  C CB    . ASP E 131 ? 0.3423 0.3395 0.3322 -0.0403 0.0396  -0.0280 132 ASP E CB    
6074  C CG    . ASP E 131 ? 0.3969 0.3951 0.3858 -0.0403 0.0409  -0.0281 132 ASP E CG    
6075  O OD1   . ASP E 131 ? 0.5268 0.5272 0.5161 -0.0418 0.0415  -0.0271 132 ASP E OD1   
6076  O OD2   . ASP E 131 ? 0.4332 0.4296 0.4206 -0.0389 0.0413  -0.0292 132 ASP E OD2   
6077  N N     . LEU E 132 ? 0.3769 0.3717 0.3685 -0.0421 0.0363  -0.0267 133 LEU E N     
6078  C CA    . LEU E 132 ? 0.4117 0.4060 0.4042 -0.0418 0.0348  -0.0269 133 LEU E CA    
6079  C C     . LEU E 132 ? 0.4117 0.4065 0.4055 -0.0439 0.0337  -0.0258 133 LEU E C     
6080  O O     . LEU E 132 ? 0.4180 0.4132 0.4132 -0.0441 0.0323  -0.0258 133 LEU E O     
6081  C CB    . LEU E 132 ? 0.4303 0.4197 0.4200 -0.0406 0.0340  -0.0275 133 LEU E CB    
6082  C CG    . LEU E 132 ? 0.4740 0.4624 0.4624 -0.0386 0.0345  -0.0285 133 LEU E CG    
6083  C CD1   . LEU E 132 ? 0.5495 0.5378 0.5369 -0.0385 0.0361  -0.0286 133 LEU E CD1   
6084  C CD2   . LEU E 132 ? 0.4796 0.4636 0.4653 -0.0378 0.0335  -0.0288 133 LEU E CD2   
6085  N N     . GLY E 133 ? 0.4088 0.4033 0.4021 -0.0455 0.0343  -0.0248 134 GLY E N     
6086  C CA    . GLY E 133 ? 0.4489 0.4430 0.4430 -0.0476 0.0331  -0.0236 134 GLY E CA    
6087  C C     . GLY E 133 ? 0.4529 0.4424 0.4455 -0.0473 0.0313  -0.0240 134 GLY E C     
6088  O O     . GLY E 133 ? 0.5110 0.5007 0.5049 -0.0482 0.0298  -0.0237 134 GLY E O     
6089  N N     . ILE E 134 ? 0.4356 0.4213 0.4253 -0.0461 0.0316  -0.0246 135 ILE E N     
6090  C CA    . ILE E 134 ? 0.4267 0.4082 0.4145 -0.0456 0.0303  -0.0252 135 ILE E CA    
6091  C C     . ILE E 134 ? 0.4064 0.3849 0.3925 -0.0460 0.0303  -0.0250 135 ILE E C     
6092  O O     . ILE E 134 ? 0.4358 0.4144 0.4211 -0.0456 0.0316  -0.0251 135 ILE E O     
6093  C CB    . ILE E 134 ? 0.4268 0.4069 0.4129 -0.0437 0.0306  -0.0263 135 ILE E CB    
6094  C CG1   . ILE E 134 ? 0.4507 0.4334 0.4385 -0.0429 0.0302  -0.0266 135 ILE E CG1   
6095  C CG2   . ILE E 134 ? 0.4348 0.4108 0.4184 -0.0432 0.0294  -0.0270 135 ILE E CG2   
6096  C CD1   . ILE E 134 ? 0.5180 0.4986 0.5036 -0.0411 0.0302  -0.0275 135 ILE E CD1   
6097  N N     . ASP E 135 ? 0.3726 0.3486 0.3583 -0.0467 0.0286  -0.0250 136 ASP E N     
6098  C CA    . ASP E 135 ? 0.4004 0.3732 0.3846 -0.0467 0.0281  -0.0251 136 ASP E CA    
6099  C C     . ASP E 135 ? 0.4056 0.3754 0.3873 -0.0451 0.0280  -0.0266 136 ASP E C     
6100  O O     . ASP E 135 ? 0.3974 0.3660 0.3786 -0.0447 0.0268  -0.0272 136 ASP E O     
6101  C CB    . ASP E 135 ? 0.4294 0.4008 0.4143 -0.0485 0.0262  -0.0242 136 ASP E CB    
6102  C CG    . ASP E 135 ? 0.4451 0.4131 0.4287 -0.0484 0.0254  -0.0243 136 ASP E CG    
6103  O OD1   . ASP E 135 ? 0.4900 0.4569 0.4720 -0.0469 0.0264  -0.0253 136 ASP E OD1   
6104  O OD2   . ASP E 135 ? 0.4263 0.3926 0.4103 -0.0499 0.0237  -0.0234 136 ASP E OD2   
6105  N N     . PRO E 136 ? 0.4032 0.3722 0.3835 -0.0441 0.0293  -0.0272 137 PRO E N     
6106  C CA    . PRO E 136 ? 0.4251 0.3920 0.4032 -0.0427 0.0295  -0.0286 137 PRO E CA    
6107  C C     . PRO E 136 ? 0.4627 0.4266 0.4398 -0.0425 0.0277  -0.0294 137 PRO E C     
6108  O O     . PRO E 136 ? 0.5276 0.4900 0.5027 -0.0415 0.0276  -0.0306 137 PRO E O     
6109  C CB    . PRO E 136 ? 0.4042 0.3715 0.3818 -0.0421 0.0311  -0.0289 137 PRO E CB    
6110  C CG    . PRO E 136 ? 0.3998 0.3681 0.3790 -0.0432 0.0309  -0.0278 137 PRO E CG    
6111  C CD    . PRO E 136 ? 0.3682 0.3385 0.3490 -0.0444 0.0305  -0.0267 137 PRO E CD    
6112  N N     . GLY E 137 ? 0.4586 0.4216 0.4368 -0.0436 0.0262  -0.0287 138 GLY E N     
6113  C CA    . GLY E 137 ? 0.4557 0.4155 0.4330 -0.0434 0.0242  -0.0295 138 GLY E CA    
6114  C C     . GLY E 137 ? 0.4331 0.3922 0.4107 -0.0440 0.0224  -0.0295 138 GLY E C     
6115  O O     . GLY E 137 ? 0.4142 0.3704 0.3906 -0.0435 0.0206  -0.0305 138 GLY E O     
6116  N N     . ASN E 138 ? 0.3890 0.3508 0.3681 -0.0448 0.0228  -0.0285 139 ASN E N     
6117  C CA    . ASN E 138 ? 0.3919 0.3537 0.3718 -0.0456 0.0211  -0.0283 139 ASN E CA    
6118  C C     . ASN E 138 ? 0.3753 0.3347 0.3526 -0.0441 0.0202  -0.0299 139 ASN E C     
6119  O O     . ASN E 138 ? 0.3168 0.2738 0.2936 -0.0444 0.0180  -0.0305 139 ASN E O     
6120  C CB    . ASN E 138 ? 0.4165 0.3823 0.3986 -0.0462 0.0219  -0.0274 139 ASN E CB    
6121  C CG    . ASN E 138 ? 0.4787 0.4450 0.4623 -0.0473 0.0199  -0.0271 139 ASN E CG    
6122  O OD1   . ASN E 138 ? 0.5088 0.4747 0.4940 -0.0490 0.0184  -0.0263 139 ASN E OD1   
6123  N ND2   . ASN E 138 ? 0.5129 0.4800 0.4961 -0.0463 0.0197  -0.0277 139 ASN E ND2   
6124  N N     . SER E 139 ? 0.3521 0.3118 0.3274 -0.0427 0.0219  -0.0307 140 SER E N     
6125  C CA    . SER E 139 ? 0.3537 0.3113 0.3260 -0.0414 0.0215  -0.0321 140 SER E CA    
6126  C C     . SER E 139 ? 0.3253 0.2827 0.2954 -0.0401 0.0236  -0.0329 140 SER E C     
6127  O O     . SER E 139 ? 0.3475 0.3040 0.3148 -0.0392 0.0240  -0.0338 140 SER E O     
6128  C CB    . SER E 139 ? 0.3458 0.3042 0.3179 -0.0413 0.0209  -0.0319 140 SER E CB    
6129  O OG    . SER E 139 ? 0.3378 0.2985 0.3102 -0.0409 0.0227  -0.0312 140 SER E OG    
6130  N N     . GLY E 140 ? 0.3093 0.2676 0.2805 -0.0403 0.0249  -0.0326 141 GLY E N     
6131  C CA    . GLY E 140 ? 0.3517 0.3103 0.3215 -0.0393 0.0269  -0.0334 141 GLY E CA    
6132  C C     . GLY E 140 ? 0.3573 0.3180 0.3272 -0.0394 0.0289  -0.0326 141 GLY E C     
6133  O O     . GLY E 140 ? 0.3787 0.3404 0.3494 -0.0398 0.0287  -0.0317 141 GLY E O     
6134  N N     . HIS E 141 ? 0.3754 0.3368 0.3448 -0.0390 0.0307  -0.0330 142 HIS E N     
6135  C CA    . HIS E 141 ? 0.3690 0.3320 0.3386 -0.0392 0.0325  -0.0323 142 HIS E CA    
6136  C C     . HIS E 141 ? 0.3838 0.3466 0.3511 -0.0387 0.0341  -0.0332 142 HIS E C     
6137  O O     . HIS E 141 ? 0.3674 0.3301 0.3344 -0.0382 0.0345  -0.0342 142 HIS E O     
6138  C CB    . HIS E 141 ? 0.3773 0.3421 0.3495 -0.0398 0.0329  -0.0315 142 HIS E CB    
6139  C CG    . HIS E 141 ? 0.3782 0.3443 0.3504 -0.0398 0.0348  -0.0314 142 HIS E CG    
6140  N ND1   . HIS E 141 ? 0.4066 0.3737 0.3801 -0.0399 0.0355  -0.0314 142 HIS E ND1   
6141  C CD2   . HIS E 141 ? 0.3836 0.3498 0.3546 -0.0396 0.0359  -0.0312 142 HIS E CD2   
6142  C CE1   . HIS E 141 ? 0.4114 0.3795 0.3847 -0.0399 0.0370  -0.0313 142 HIS E CE1   
6143  N NE2   . HIS E 141 ? 0.4012 0.3686 0.3729 -0.0398 0.0372  -0.0312 142 HIS E NE2   
6144  N N     . GLN E 142 ? 0.4164 0.3791 0.3822 -0.0388 0.0351  -0.0327 143 GLN E N     
6145  C CA    . GLN E 142 ? 0.4027 0.3654 0.3665 -0.0387 0.0368  -0.0331 143 GLN E CA    
6146  C C     . GLN E 142 ? 0.3744 0.3378 0.3387 -0.0392 0.0379  -0.0322 143 GLN E C     
6147  O O     . GLN E 142 ? 0.3808 0.3440 0.3455 -0.0393 0.0373  -0.0314 143 GLN E O     
6148  C CB    . GLN E 142 ? 0.4152 0.3760 0.3753 -0.0385 0.0366  -0.0334 143 GLN E CB    
6149  C CG    . GLN E 142 ? 0.4465 0.4064 0.4056 -0.0378 0.0354  -0.0346 143 GLN E CG    
6150  C CD    . GLN E 142 ? 0.4877 0.4458 0.4428 -0.0376 0.0352  -0.0349 143 GLN E CD    
6151  O OE1   . GLN E 142 ? 0.4614 0.4194 0.4143 -0.0372 0.0359  -0.0361 143 GLN E OE1   
6152  N NE2   . GLN E 142 ? 0.5299 0.4867 0.4838 -0.0377 0.0342  -0.0339 143 GLN E NE2   
6153  N N     . SER E 143 ? 0.3528 0.3172 0.3172 -0.0396 0.0395  -0.0325 144 SER E N     
6154  C CA    . SER E 143 ? 0.3881 0.3529 0.3529 -0.0401 0.0405  -0.0318 144 SER E CA    
6155  C C     . SER E 143 ? 0.3736 0.3380 0.3360 -0.0408 0.0421  -0.0320 144 SER E C     
6156  O O     . SER E 143 ? 0.4190 0.3846 0.3814 -0.0409 0.0430  -0.0329 144 SER E O     
6157  C CB    . SER E 143 ? 0.3781 0.3448 0.3458 -0.0403 0.0408  -0.0318 144 SER E CB    
6158  O OG    . SER E 143 ? 0.4549 0.4221 0.4244 -0.0400 0.0396  -0.0314 144 SER E OG    
6159  N N     . PHE E 144 ? 0.3861 0.3489 0.3467 -0.0413 0.0423  -0.0312 145 PHE E N     
6160  C CA    . PHE E 144 ? 0.3715 0.3335 0.3297 -0.0423 0.0437  -0.0310 145 PHE E CA    
6161  C C     . PHE E 144 ? 0.3585 0.3195 0.3169 -0.0429 0.0438  -0.0301 145 PHE E C     
6162  O O     . PHE E 144 ? 0.4178 0.3777 0.3767 -0.0422 0.0426  -0.0296 145 PHE E O     
6163  C CB    . PHE E 144 ? 0.3603 0.3202 0.3145 -0.0425 0.0435  -0.0306 145 PHE E CB    
6164  C CG    . PHE E 144 ? 0.3585 0.3190 0.3118 -0.0418 0.0433  -0.0317 145 PHE E CG    
6165  C CD1   . PHE E 144 ? 0.3578 0.3202 0.3109 -0.0420 0.0447  -0.0328 145 PHE E CD1   
6166  C CD2   . PHE E 144 ? 0.3713 0.3305 0.3241 -0.0408 0.0414  -0.0317 145 PHE E CD2   
6167  C CE1   . PHE E 144 ? 0.3779 0.3408 0.3302 -0.0411 0.0444  -0.0340 145 PHE E CE1   
6168  C CE2   . PHE E 144 ? 0.3744 0.3337 0.3263 -0.0401 0.0410  -0.0327 145 PHE E CE2   
6169  C CZ    . PHE E 144 ? 0.3862 0.3473 0.3377 -0.0402 0.0424  -0.0339 145 PHE E CZ    
6170  N N     . GLU E 145 ? 0.3772 0.3386 0.3352 -0.0442 0.0453  -0.0301 146 GLU E N     
6171  C CA    . GLU E 145 ? 0.3881 0.3476 0.3454 -0.0450 0.0453  -0.0293 146 GLU E CA    
6172  C C     . GLU E 145 ? 0.3917 0.3476 0.3450 -0.0453 0.0447  -0.0282 146 GLU E C     
6173  O O     . GLU E 145 ? 0.3943 0.3498 0.3448 -0.0459 0.0453  -0.0281 146 GLU E O     
6174  C CB    . GLU E 145 ? 0.4238 0.3849 0.3820 -0.0464 0.0469  -0.0295 146 GLU E CB    
6175  C CG    . GLU E 145 ? 0.4726 0.4321 0.4311 -0.0472 0.0466  -0.0290 146 GLU E CG    
6176  C CD    . GLU E 145 ? 0.5359 0.4914 0.4908 -0.0482 0.0463  -0.0278 146 GLU E CD    
6177  O OE1   . GLU E 145 ? 0.5706 0.5248 0.5224 -0.0485 0.0464  -0.0272 146 GLU E OE1   
6178  O OE2   . GLU E 145 ? 0.6053 0.5588 0.5601 -0.0487 0.0458  -0.0274 146 GLU E OE2   
6179  N N     . ALA E 146 ? 0.3942 0.3475 0.3469 -0.0447 0.0432  -0.0276 147 ALA E N     
6180  C CA    . ALA E 146 ? 0.4002 0.3498 0.3492 -0.0445 0.0420  -0.0267 147 ALA E CA    
6181  C C     . ALA E 146 ? 0.3865 0.3340 0.3317 -0.0464 0.0430  -0.0257 147 ALA E C     
6182  O O     . ALA E 146 ? 0.3713 0.3172 0.3130 -0.0465 0.0428  -0.0252 147 ALA E O     
6183  C CB    . ALA E 146 ? 0.4081 0.3555 0.3576 -0.0434 0.0404  -0.0264 147 ALA E CB    
6184  N N     . SER E 147 ? 0.3828 0.3302 0.3283 -0.0479 0.0441  -0.0255 148 SER E N     
6185  C CA    . SER E 147 ? 0.3951 0.3404 0.3370 -0.0502 0.0451  -0.0243 148 SER E CA    
6186  C C     . SER E 147 ? 0.3755 0.3239 0.3166 -0.0511 0.0471  -0.0248 148 SER E C     
6187  O O     . SER E 147 ? 0.3466 0.2932 0.2835 -0.0524 0.0476  -0.0238 148 SER E O     
6188  C CB    . SER E 147 ? 0.4173 0.3621 0.3603 -0.0517 0.0457  -0.0241 148 SER E CB    
6189  O OG    . SER E 147 ? 0.4147 0.3562 0.3579 -0.0507 0.0438  -0.0238 148 SER E OG    
6190  N N     . GLN E 148 ? 0.3656 0.3184 0.3104 -0.0504 0.0480  -0.0262 149 GLN E N     
6191  C CA    . GLN E 148 ? 0.4064 0.3626 0.3511 -0.0509 0.0498  -0.0271 149 GLN E CA    
6192  C C     . GLN E 148 ? 0.4221 0.3771 0.3638 -0.0498 0.0490  -0.0272 149 GLN E C     
6193  O O     . GLN E 148 ? 0.4611 0.4172 0.4002 -0.0505 0.0503  -0.0274 149 GLN E O     
6194  C CB    . GLN E 148 ? 0.3900 0.3506 0.3395 -0.0499 0.0504  -0.0288 149 GLN E CB    
6195  C CG    . GLN E 148 ? 0.4096 0.3740 0.3594 -0.0501 0.0521  -0.0300 149 GLN E CG    
6196  C CD    . GLN E 148 ? 0.4143 0.3823 0.3686 -0.0487 0.0521  -0.0317 149 GLN E CD    
6197  O OE1   . GLN E 148 ? 0.3748 0.3437 0.3297 -0.0471 0.0515  -0.0327 149 GLN E OE1   
6198  N NE2   . GLN E 148 ? 0.4117 0.3817 0.3692 -0.0494 0.0526  -0.0319 149 GLN E NE2   
6199  N N     . PHE E 149 ? 0.3736 0.3265 0.3155 -0.0480 0.0469  -0.0270 150 PHE E N     
6200  C CA    . PHE E 149 ? 0.3824 0.3340 0.3218 -0.0469 0.0458  -0.0272 150 PHE E CA    
6201  C C     . PHE E 149 ? 0.4411 0.3888 0.3749 -0.0480 0.0455  -0.0257 150 PHE E C     
6202  O O     . PHE E 149 ? 0.3889 0.3356 0.3196 -0.0475 0.0449  -0.0257 150 PHE E O     
6203  C CB    . PHE E 149 ? 0.4011 0.3522 0.3430 -0.0450 0.0436  -0.0274 150 PHE E CB    
6204  C CG    . PHE E 149 ? 0.4279 0.3777 0.3677 -0.0438 0.0420  -0.0277 150 PHE E CG    
6205  C CD1   . PHE E 149 ? 0.4158 0.3619 0.3521 -0.0435 0.0404  -0.0266 150 PHE E CD1   
6206  C CD2   . PHE E 149 ? 0.4466 0.3988 0.3880 -0.0428 0.0420  -0.0290 150 PHE E CD2   
6207  C CE1   . PHE E 149 ? 0.4515 0.3965 0.3860 -0.0424 0.0388  -0.0269 150 PHE E CE1   
6208  C CE2   . PHE E 149 ? 0.4467 0.3975 0.3862 -0.0418 0.0404  -0.0293 150 PHE E CE2   
6209  C CZ    . PHE E 149 ? 0.4334 0.3808 0.3695 -0.0417 0.0388  -0.0282 150 PHE E CZ    
6210  N N     . MET E 150 ? 0.4769 0.4223 0.4094 -0.0495 0.0457  -0.0244 151 MET E N     
6211  C CA    . MET E 150 ? 0.4665 0.4074 0.3935 -0.0507 0.0451  -0.0226 151 MET E CA    
6212  C C     . MET E 150 ? 0.4566 0.3985 0.3807 -0.0533 0.0476  -0.0220 151 MET E C     
6213  O O     . MET E 150 ? 0.4481 0.3877 0.3669 -0.0543 0.0477  -0.0210 151 MET E O     
6214  C CB    . MET E 150 ? 0.5017 0.4385 0.4284 -0.0507 0.0434  -0.0214 151 MET E CB    
6215  C CG    . MET E 150 ? 0.5071 0.4426 0.4357 -0.0482 0.0408  -0.0218 151 MET E CG    
6216  S SD    . MET E 150 ? 0.5406 0.4712 0.4688 -0.0478 0.0387  -0.0208 151 MET E SD    
6217  C CE    . MET E 150 ? 0.5364 0.4609 0.4572 -0.0493 0.0377  -0.0186 151 MET E CE    
6218  N N     . PHE E 151 ? 0.4751 0.4205 0.4026 -0.0544 0.0495  -0.0227 152 PHE E N     
6219  C CA    . PHE E 151 ? 0.5028 0.4497 0.4285 -0.0572 0.0519  -0.0221 152 PHE E CA    
6220  C C     . PHE E 151 ? 0.5045 0.4562 0.4301 -0.0570 0.0539  -0.0235 152 PHE E C     
6221  O O     . PHE E 151 ? 0.4796 0.4323 0.4020 -0.0591 0.0559  -0.0230 152 PHE E O     
6222  C CB    . PHE E 151 ? 0.5335 0.4824 0.4632 -0.0586 0.0529  -0.0222 152 PHE E CB    
6223  C CG    . PHE E 151 ? 0.5500 0.4942 0.4796 -0.0589 0.0510  -0.0209 152 PHE E CG    
6224  C CD1   . PHE E 151 ? 0.5621 0.5005 0.4872 -0.0590 0.0491  -0.0192 152 PHE E CD1   
6225  C CD2   . PHE E 151 ? 0.5556 0.5012 0.4896 -0.0590 0.0510  -0.0216 152 PHE E CD2   
6226  C CE1   . PHE E 151 ? 0.5713 0.5053 0.4964 -0.0589 0.0472  -0.0184 152 PHE E CE1   
6227  C CE2   . PHE E 151 ? 0.5379 0.4793 0.4718 -0.0591 0.0492  -0.0207 152 PHE E CE2   
6228  C CZ    . PHE E 151 ? 0.5530 0.4885 0.4824 -0.0590 0.0473  -0.0192 152 PHE E CZ    
6229  N N     . PHE E 152 ? 0.4500 0.4044 0.3791 -0.0546 0.0534  -0.0254 153 PHE E N     
6230  C CA    . PHE E 152 ? 0.4450 0.4038 0.3745 -0.0540 0.0550  -0.0273 153 PHE E CA    
6231  C C     . PHE E 152 ? 0.4601 0.4174 0.3879 -0.0517 0.0533  -0.0280 153 PHE E C     
6232  O O     . PHE E 152 ? 0.4330 0.3864 0.3597 -0.0507 0.0510  -0.0271 153 PHE E O     
6233  C CB    . PHE E 152 ? 0.4726 0.4362 0.4081 -0.0533 0.0560  -0.0290 153 PHE E CB    
6234  C CG    . PHE E 152 ? 0.5237 0.4890 0.4613 -0.0556 0.0575  -0.0284 153 PHE E CG    
6235  C CD1   . PHE E 152 ? 0.5797 0.5480 0.5160 -0.0579 0.0601  -0.0283 153 PHE E CD1   
6236  C CD2   . PHE E 152 ? 0.5664 0.5306 0.5073 -0.0555 0.0563  -0.0280 153 PHE E CD2   
6237  C CE1   . PHE E 152 ? 0.5844 0.5542 0.5228 -0.0602 0.0613  -0.0277 153 PHE E CE1   
6238  C CE2   . PHE E 152 ? 0.5674 0.5329 0.5102 -0.0576 0.0575  -0.0275 153 PHE E CE2   
6239  C CZ    . PHE E 152 ? 0.5966 0.5648 0.5382 -0.0601 0.0599  -0.0273 153 PHE E CZ    
6240  N N     . ASN E 153 ? 0.4924 0.4530 0.4201 -0.0508 0.0544  -0.0299 154 ASN E N     
6241  C CA    . ASN E 153 ? 0.5351 0.4943 0.4606 -0.0489 0.0528  -0.0307 154 ASN E CA    
6242  C C     . ASN E 153 ? 0.5012 0.4618 0.4316 -0.0465 0.0513  -0.0324 154 ASN E C     
6243  O O     . ASN E 153 ? 0.4895 0.4539 0.4229 -0.0457 0.0523  -0.0343 154 ASN E O     
6244  C CB    . ASN E 153 ? 0.5731 0.5345 0.4948 -0.0492 0.0547  -0.0318 154 ASN E CB    
6245  C CG    . ASN E 153 ? 0.6561 0.6152 0.5718 -0.0515 0.0557  -0.0298 154 ASN E CG    
6246  O OD1   . ASN E 153 ? 0.7280 0.6825 0.6393 -0.0514 0.0539  -0.0285 154 ASN E OD1   
6247  N ND2   . ASN E 153 ? 0.6334 0.5956 0.5487 -0.0537 0.0586  -0.0296 154 ASN E ND2   
6248  N N     . HIS E 154 ? 0.4494 0.4069 0.3805 -0.0455 0.0488  -0.0316 155 HIS E N     
6249  C CA    . HIS E 154 ? 0.4791 0.4373 0.4143 -0.0437 0.0471  -0.0327 155 HIS E CA    
6250  C C     . HIS E 154 ? 0.4546 0.4098 0.3875 -0.0424 0.0447  -0.0327 155 HIS E C     
6251  O O     . HIS E 154 ? 0.4574 0.4094 0.3877 -0.0428 0.0435  -0.0312 155 HIS E O     
6252  C CB    . HIS E 154 ? 0.4927 0.4510 0.4322 -0.0438 0.0465  -0.0320 155 HIS E CB    
6253  C CG    . HIS E 154 ? 0.4977 0.4594 0.4406 -0.0445 0.0484  -0.0326 155 HIS E CG    
6254  N ND1   . HIS E 154 ? 0.5159 0.4811 0.4611 -0.0438 0.0493  -0.0344 155 HIS E ND1   
6255  C CD2   . HIS E 154 ? 0.5062 0.4682 0.4508 -0.0457 0.0492  -0.0317 155 HIS E CD2   
6256  C CE1   . HIS E 154 ? 0.5035 0.4712 0.4517 -0.0446 0.0507  -0.0346 155 HIS E CE1   
6257  N NE2   . HIS E 154 ? 0.4626 0.4284 0.4104 -0.0459 0.0506  -0.0329 155 HIS E NE2   
6258  N N     . VAL E 155 ? 0.5188 0.4750 0.4527 -0.0410 0.0439  -0.0344 156 VAL E N     
6259  C CA    . VAL E 155 ? 0.5305 0.4842 0.4626 -0.0399 0.0414  -0.0345 156 VAL E CA    
6260  C C     . VAL E 155 ? 0.5623 0.5164 0.4992 -0.0388 0.0396  -0.0350 156 VAL E C     
6261  O O     . VAL E 155 ? 0.4838 0.4399 0.4235 -0.0381 0.0396  -0.0364 156 VAL E O     
6262  C CB    . VAL E 155 ? 0.5667 0.5205 0.4952 -0.0391 0.0416  -0.0361 156 VAL E CB    
6263  C CG1   . VAL E 155 ? 0.5969 0.5482 0.5240 -0.0379 0.0387  -0.0365 156 VAL E CG1   
6264  C CG2   . VAL E 155 ? 0.5439 0.4975 0.4672 -0.0404 0.0436  -0.0355 156 VAL E CG2   
6265  N N     . PRO E 156 ? 0.5337 0.4862 0.4718 -0.0387 0.0378  -0.0337 157 PRO E N     
6266  C CA    . PRO E 156 ? 0.4797 0.4330 0.4224 -0.0381 0.0362  -0.0339 157 PRO E CA    
6267  C C     . PRO E 156 ? 0.5055 0.4578 0.4480 -0.0372 0.0339  -0.0348 157 PRO E C     
6268  O O     . PRO E 156 ? 0.5348 0.4850 0.4734 -0.0368 0.0330  -0.0350 157 PRO E O     
6269  C CB    . PRO E 156 ? 0.4909 0.4432 0.4346 -0.0384 0.0355  -0.0323 157 PRO E CB    
6270  C CG    . PRO E 156 ? 0.5404 0.4899 0.4790 -0.0386 0.0350  -0.0315 157 PRO E CG    
6271  C CD    . PRO E 156 ? 0.5289 0.4788 0.4641 -0.0392 0.0371  -0.0321 157 PRO E CD    
6272  N N     . ASP E 157 ? 0.4653 0.4187 0.4117 -0.0368 0.0330  -0.0354 158 ASP E N     
6273  C CA    . ASP E 157 ? 0.4880 0.4403 0.4349 -0.0362 0.0306  -0.0361 158 ASP E CA    
6274  C C     . ASP E 157 ? 0.4561 0.4081 0.4050 -0.0364 0.0288  -0.0348 158 ASP E C     
6275  O O     . ASP E 157 ? 0.4325 0.3861 0.3853 -0.0369 0.0288  -0.0341 158 ASP E O     
6276  C CB    . ASP E 157 ? 0.4670 0.4202 0.4167 -0.0359 0.0302  -0.0372 158 ASP E CB    
6277  C CG    . ASP E 157 ? 0.4865 0.4382 0.4368 -0.0355 0.0276  -0.0380 158 ASP E CG    
6278  O OD1   . ASP E 157 ? 0.6103 0.5606 0.5592 -0.0355 0.0259  -0.0377 158 ASP E OD1   
6279  O OD2   . ASP E 157 ? 0.4581 0.4099 0.4103 -0.0351 0.0270  -0.0390 158 ASP E OD2   
6280  N N     . PRO E 158 ? 0.4190 0.3691 0.3653 -0.0361 0.0271  -0.0346 159 PRO E N     
6281  C CA    . PRO E 158 ? 0.4330 0.3833 0.3812 -0.0362 0.0255  -0.0336 159 PRO E CA    
6282  C C     . PRO E 158 ? 0.4692 0.4208 0.4218 -0.0364 0.0237  -0.0337 159 PRO E C     
6283  O O     . PRO E 158 ? 0.4584 0.4108 0.4131 -0.0364 0.0223  -0.0330 159 PRO E O     
6284  C CB    . PRO E 158 ? 0.4756 0.4232 0.4193 -0.0356 0.0241  -0.0336 159 PRO E CB    
6285  C CG    . PRO E 158 ? 0.4405 0.3869 0.3809 -0.0353 0.0241  -0.0350 159 PRO E CG    
6286  C CD    . PRO E 158 ? 0.4319 0.3799 0.3732 -0.0356 0.0267  -0.0355 159 PRO E CD    
6287  N N     . THR E 159 ? 0.4566 0.4085 0.4106 -0.0366 0.0237  -0.0345 160 THR E N     
6288  C CA    . THR E 159 ? 0.4423 0.3951 0.4000 -0.0372 0.0220  -0.0345 160 THR E CA    
6289  C C     . THR E 159 ? 0.4151 0.3703 0.3766 -0.0379 0.0234  -0.0336 160 THR E C     
6290  O O     . THR E 159 ? 0.4288 0.3853 0.3938 -0.0387 0.0223  -0.0331 160 THR E O     
6291  C CB    . THR E 159 ? 0.4838 0.4347 0.4403 -0.0369 0.0207  -0.0359 160 THR E CB    
6292  O OG1   . THR E 159 ? 0.4513 0.4023 0.4071 -0.0365 0.0226  -0.0366 160 THR E OG1   
6293  C CG2   . THR E 159 ? 0.4774 0.4258 0.4297 -0.0361 0.0192  -0.0369 160 THR E CG2   
6294  N N     . THR E 160 ? 0.3865 0.3424 0.3473 -0.0377 0.0257  -0.0334 161 THR E N     
6295  C CA    . THR E 160 ? 0.4061 0.3641 0.3700 -0.0383 0.0270  -0.0328 161 THR E CA    
6296  C C     . THR E 160 ? 0.4149 0.3747 0.3803 -0.0385 0.0278  -0.0317 161 THR E C     
6297  O O     . THR E 160 ? 0.4958 0.4550 0.4599 -0.0381 0.0273  -0.0314 161 THR E O     
6298  C CB    . THR E 160 ? 0.4089 0.3667 0.3715 -0.0380 0.0289  -0.0336 161 THR E CB    
6299  O OG1   . THR E 160 ? 0.4140 0.3718 0.3744 -0.0378 0.0305  -0.0333 161 THR E OG1   
6300  C CG2   . THR E 160 ? 0.4357 0.3918 0.3964 -0.0374 0.0282  -0.0351 161 THR E CG2   
6301  N N     . HIS E 161 ? 0.4156 0.3773 0.3835 -0.0390 0.0290  -0.0312 162 HIS E N     
6302  C CA    . HIS E 161 ? 0.3964 0.3599 0.3656 -0.0390 0.0301  -0.0304 162 HIS E CA    
6303  C C     . HIS E 161 ? 0.3732 0.3359 0.3402 -0.0387 0.0320  -0.0306 162 HIS E C     
6304  O O     . HIS E 161 ? 0.3210 0.2842 0.2885 -0.0390 0.0331  -0.0309 162 HIS E O     
6305  C CB    . HIS E 161 ? 0.3865 0.3527 0.3593 -0.0397 0.0302  -0.0298 162 HIS E CB    
6306  C CG    . HIS E 161 ? 0.4086 0.3765 0.3838 -0.0401 0.0288  -0.0293 162 HIS E CG    
6307  N ND1   . HIS E 161 ? 0.3848 0.3528 0.3615 -0.0410 0.0273  -0.0291 162 HIS E ND1   
6308  C CD2   . HIS E 161 ? 0.3812 0.3509 0.3578 -0.0398 0.0285  -0.0290 162 HIS E CD2   
6309  C CE1   . HIS E 161 ? 0.3733 0.3435 0.3524 -0.0414 0.0263  -0.0287 162 HIS E CE1   
6310  N NE2   . HIS E 161 ? 0.3848 0.3563 0.3640 -0.0405 0.0270  -0.0287 162 HIS E NE2   
6311  N N     . LEU E 162 ? 0.3799 0.3414 0.3448 -0.0383 0.0321  -0.0304 163 LEU E N     
6312  C CA    . LEU E 162 ? 0.3728 0.3332 0.3353 -0.0383 0.0338  -0.0304 163 LEU E CA    
6313  C C     . LEU E 162 ? 0.3575 0.3190 0.3215 -0.0384 0.0347  -0.0299 163 LEU E C     
6314  O O     . LEU E 162 ? 0.3800 0.3418 0.3449 -0.0379 0.0338  -0.0295 163 LEU E O     
6315  C CB    . LEU E 162 ? 0.3578 0.3156 0.3163 -0.0380 0.0333  -0.0303 163 LEU E CB    
6316  C CG    . LEU E 162 ? 0.3691 0.3255 0.3248 -0.0385 0.0349  -0.0301 163 LEU E CG    
6317  C CD1   . LEU E 162 ? 0.3963 0.3537 0.3517 -0.0390 0.0366  -0.0308 163 LEU E CD1   
6318  C CD2   . LEU E 162 ? 0.3824 0.3359 0.3338 -0.0383 0.0342  -0.0297 163 LEU E CD2   
6319  N N     . LEU E 163 ? 0.4045 0.3666 0.3688 -0.0389 0.0363  -0.0300 164 LEU E N     
6320  C CA    . LEU E 163 ? 0.3982 0.3610 0.3635 -0.0389 0.0371  -0.0297 164 LEU E CA    
6321  C C     . LEU E 163 ? 0.3651 0.3259 0.3275 -0.0394 0.0382  -0.0296 164 LEU E C     
6322  O O     . LEU E 163 ? 0.3598 0.3206 0.3212 -0.0400 0.0393  -0.0299 164 LEU E O     
6323  C CB    . LEU E 163 ? 0.4055 0.3707 0.3736 -0.0393 0.0379  -0.0298 164 LEU E CB    
6324  C CG    . LEU E 163 ? 0.4525 0.4197 0.4233 -0.0392 0.0369  -0.0297 164 LEU E CG    
6325  C CD1   . LEU E 163 ? 0.4627 0.4319 0.4356 -0.0396 0.0377  -0.0296 164 LEU E CD1   
6326  C CD2   . LEU E 163 ? 0.5216 0.4894 0.4933 -0.0386 0.0360  -0.0293 164 LEU E CD2   
6327  N N     . LEU E 164 ? 0.3685 0.3278 0.3299 -0.0392 0.0380  -0.0291 165 LEU E N     
6328  C CA    . LEU E 164 ? 0.3754 0.3325 0.3342 -0.0399 0.0389  -0.0287 165 LEU E CA    
6329  C C     . LEU E 164 ? 0.3482 0.3060 0.3088 -0.0400 0.0394  -0.0288 165 LEU E C     
6330  O O     . LEU E 164 ? 0.3771 0.3342 0.3383 -0.0391 0.0385  -0.0287 165 LEU E O     
6331  C CB    . LEU E 164 ? 0.3977 0.3514 0.3531 -0.0397 0.0378  -0.0281 165 LEU E CB    
6332  C CG    . LEU E 164 ? 0.4197 0.3724 0.3726 -0.0396 0.0372  -0.0280 165 LEU E CG    
6333  C CD1   . LEU E 164 ? 0.4792 0.4280 0.4279 -0.0397 0.0363  -0.0272 165 LEU E CD1   
6334  C CD2   . LEU E 164 ? 0.4203 0.3743 0.3725 -0.0405 0.0388  -0.0286 165 LEU E CD2   
6335  N N     . TRP E 165 ? 0.3290 0.2883 0.2907 -0.0409 0.0408  -0.0291 166 TRP E N     
6336  C CA    . TRP E 165 ? 0.3525 0.3125 0.3158 -0.0410 0.0412  -0.0293 166 TRP E CA    
6337  C C     . TRP E 165 ? 0.3641 0.3210 0.3250 -0.0417 0.0413  -0.0289 166 TRP E C     
6338  O O     . TRP E 165 ? 0.3758 0.3305 0.3339 -0.0424 0.0415  -0.0283 166 TRP E O     
6339  C CB    . TRP E 165 ? 0.3392 0.3018 0.3046 -0.0416 0.0424  -0.0299 166 TRP E CB    
6340  C CG    . TRP E 165 ? 0.3332 0.2981 0.3006 -0.0411 0.0421  -0.0302 166 TRP E CG    
6341  C CD1   . TRP E 165 ? 0.3486 0.3135 0.3155 -0.0408 0.0415  -0.0302 166 TRP E CD1   
6342  C CD2   . TRP E 165 ? 0.3379 0.3052 0.3079 -0.0409 0.0421  -0.0305 166 TRP E CD2   
6343  N NE1   . TRP E 165 ? 0.3275 0.2944 0.2967 -0.0405 0.0411  -0.0304 166 TRP E NE1   
6344  C CE2   . TRP E 165 ? 0.3419 0.3103 0.3129 -0.0406 0.0415  -0.0305 166 TRP E CE2   
6345  C CE3   . TRP E 165 ? 0.3366 0.3051 0.3080 -0.0410 0.0425  -0.0307 166 TRP E CE3   
6346  C CZ2   . TRP E 165 ? 0.3319 0.3023 0.3050 -0.0406 0.0413  -0.0305 166 TRP E CZ2   
6347  C CZ3   . TRP E 165 ? 0.3247 0.2953 0.2980 -0.0409 0.0423  -0.0308 166 TRP E CZ3   
6348  C CH2   . TRP E 165 ? 0.3395 0.3110 0.3137 -0.0407 0.0417  -0.0306 166 TRP E CH2   
6349  N N     . GLN E 166 ? 0.3537 0.3103 0.3156 -0.0414 0.0411  -0.0291 167 GLN E N     
6350  C CA    . GLN E 166 ? 0.3589 0.3123 0.3188 -0.0421 0.0409  -0.0287 167 GLN E CA    
6351  C C     . GLN E 166 ? 0.3606 0.3103 0.3173 -0.0419 0.0398  -0.0279 167 GLN E C     
6352  O O     . GLN E 166 ? 0.3515 0.2985 0.3052 -0.0433 0.0402  -0.0271 167 GLN E O     
6353  C CB    . GLN E 166 ? 0.3926 0.3463 0.3522 -0.0440 0.0424  -0.0287 167 GLN E CB    
6354  C CG    . GLN E 166 ? 0.4184 0.3753 0.3811 -0.0441 0.0431  -0.0295 167 GLN E CG    
6355  C CD    . GLN E 166 ? 0.4668 0.4245 0.4297 -0.0460 0.0444  -0.0296 167 GLN E CD    
6356  O OE1   . GLN E 166 ? 0.5953 0.5516 0.5560 -0.0474 0.0451  -0.0289 167 GLN E OE1   
6357  N NE2   . GLN E 166 ? 0.4900 0.4502 0.4554 -0.0461 0.0448  -0.0304 167 GLN E NE2   
6358  N N     . ILE E 167 ? 0.3626 0.3122 0.3197 -0.0402 0.0384  -0.0280 168 ILE E N     
6359  C CA    . ILE E 167 ? 0.3551 0.3012 0.3093 -0.0396 0.0369  -0.0273 168 ILE E CA    
6360  C C     . ILE E 167 ? 0.4016 0.3436 0.3539 -0.0394 0.0358  -0.0270 168 ILE E C     
6361  O O     . ILE E 167 ? 0.3627 0.3006 0.3116 -0.0395 0.0346  -0.0261 168 ILE E O     
6362  C CB    . ILE E 167 ? 0.3411 0.2890 0.2970 -0.0378 0.0356  -0.0277 168 ILE E CB    
6363  C CG1   . ILE E 167 ? 0.3338 0.2783 0.2867 -0.0371 0.0339  -0.0271 168 ILE E CG1   
6364  C CG2   . ILE E 167 ? 0.3315 0.2816 0.2906 -0.0362 0.0351  -0.0287 168 ILE E CG2   
6365  C CD1   . ILE E 167 ? 0.3489 0.2918 0.2984 -0.0385 0.0344  -0.0262 168 ILE E CD1   
6366  N N     . ALA E 168 ? 0.3796 0.3224 0.3339 -0.0391 0.0360  -0.0278 169 ALA E N     
6367  C CA    . ALA E 168 ? 0.4222 0.3611 0.3751 -0.0386 0.0347  -0.0279 169 ALA E CA    
6368  C C     . ALA E 168 ? 0.4066 0.3411 0.3559 -0.0408 0.0349  -0.0267 169 ALA E C     
6369  O O     . ALA E 168 ? 0.4091 0.3387 0.3558 -0.0406 0.0333  -0.0261 169 ALA E O     
6370  C CB    . ALA E 168 ? 0.4669 0.4080 0.4227 -0.0378 0.0350  -0.0292 169 ALA E CB    
6371  N N     . ILE E 169 ? 0.4262 0.3626 0.3754 -0.0430 0.0369  -0.0262 170 ILE E N     
6372  C CA    . ILE E 169 ? 0.4451 0.3784 0.3914 -0.0455 0.0375  -0.0250 170 ILE E CA    
6373  C C     . ILE E 169 ? 0.4302 0.3639 0.3740 -0.0468 0.0385  -0.0240 170 ILE E C     
6374  O O     . ILE E 169 ? 0.4110 0.3453 0.3537 -0.0491 0.0401  -0.0234 170 ILE E O     
6375  C CB    . ILE E 169 ? 0.4830 0.4185 0.4314 -0.0471 0.0390  -0.0256 170 ILE E CB    
6376  C CG1   . ILE E 169 ? 0.4978 0.4391 0.4495 -0.0470 0.0407  -0.0265 170 ILE E CG1   
6377  C CG2   . ILE E 169 ? 0.4685 0.4024 0.4182 -0.0461 0.0377  -0.0265 170 ILE E CG2   
6378  C CD1   . ILE E 169 ? 0.5223 0.4662 0.4764 -0.0485 0.0420  -0.0271 170 ILE E CD1   
6379  N N     . ALA E 170 ? 0.3980 0.3316 0.3410 -0.0452 0.0375  -0.0240 171 ALA E N     
6380  C CA    . ALA E 170 ? 0.3945 0.3284 0.3350 -0.0460 0.0382  -0.0233 171 ALA E CA    
6381  C C     . ALA E 170 ? 0.3995 0.3286 0.3349 -0.0479 0.0379  -0.0215 171 ALA E C     
6382  O O     . ALA E 170 ? 0.3937 0.3179 0.3263 -0.0472 0.0358  -0.0208 171 ALA E O     
6383  C CB    . ALA E 170 ? 0.3848 0.3194 0.3258 -0.0438 0.0367  -0.0237 171 ALA E CB    
6384  N N     . GLY E 171 ? 0.4028 0.3331 0.3368 -0.0503 0.0400  -0.0210 172 GLY E N     
6385  C CA    . GLY E 171 ? 0.4133 0.3396 0.3421 -0.0526 0.0402  -0.0192 172 GLY E CA    
6386  C C     . GLY E 171 ? 0.4282 0.3522 0.3567 -0.0549 0.0405  -0.0184 172 GLY E C     
6387  O O     . GLY E 171 ? 0.3712 0.2915 0.2955 -0.0573 0.0406  -0.0167 172 GLY E O     
6388  N N     . GLU E 172 ? 0.4570 0.3828 0.3897 -0.0542 0.0405  -0.0197 173 GLU E N     
6389  C CA    . GLU E 172 ? 0.5043 0.4282 0.4373 -0.0561 0.0406  -0.0193 173 GLU E CA    
6390  C C     . GLU E 172 ? 0.5247 0.4527 0.4588 -0.0589 0.0434  -0.0193 173 GLU E C     
6391  O O     . GLU E 172 ? 0.5402 0.4736 0.4787 -0.0584 0.0447  -0.0208 173 GLU E O     
6392  C CB    . GLU E 172 ? 0.5368 0.4612 0.4736 -0.0541 0.0394  -0.0208 173 GLU E CB    
6393  C CG    . GLU E 172 ? 0.6045 0.5244 0.5404 -0.0554 0.0382  -0.0204 173 GLU E CG    
6394  C CD    . GLU E 172 ? 0.6732 0.5940 0.6089 -0.0591 0.0400  -0.0196 173 GLU E CD    
6395  O OE1   . GLU E 172 ? 0.7292 0.6553 0.6687 -0.0596 0.0418  -0.0207 173 GLU E OE1   
6396  O OE2   . GLU E 172 ? 0.6245 0.5405 0.5561 -0.0615 0.0395  -0.0178 173 GLU E OE2   
6397  N N     . HIS E 173 ? 0.5191 0.4448 0.4493 -0.0619 0.0442  -0.0175 174 HIS E N     
6398  C CA    . HIS E 173 ? 0.5007 0.4311 0.4316 -0.0645 0.0471  -0.0174 174 HIS E CA    
6399  C C     . HIS E 173 ? 0.4812 0.4127 0.4147 -0.0668 0.0479  -0.0176 174 HIS E C     
6400  O O     . HIS E 173 ? 0.5324 0.4695 0.4687 -0.0682 0.0501  -0.0184 174 HIS E O     
6401  C CB    . HIS E 173 ? 0.5222 0.4501 0.4474 -0.0667 0.0478  -0.0155 174 HIS E CB    
6402  C CG    . HIS E 173 ? 0.5331 0.4539 0.4538 -0.0689 0.0462  -0.0133 174 HIS E CG    
6403  N ND1   . HIS E 173 ? 0.5543 0.4686 0.4714 -0.0674 0.0434  -0.0123 174 HIS E ND1   
6404  C CD2   . HIS E 173 ? 0.5223 0.4415 0.4417 -0.0725 0.0470  -0.0119 174 HIS E CD2   
6405  C CE1   . HIS E 173 ? 0.5635 0.4720 0.4769 -0.0699 0.0423  -0.0103 174 HIS E CE1   
6406  N NE2   . HIS E 173 ? 0.5328 0.4441 0.4475 -0.0732 0.0445  -0.0100 174 HIS E NE2   
6407  N N     . THR E 174 ? 0.5430 0.4693 0.4756 -0.0673 0.0459  -0.0170 175 THR E N     
6408  C CA    . THR E 174 ? 0.5495 0.4758 0.4838 -0.0699 0.0463  -0.0168 175 THR E CA    
6409  C C     . THR E 174 ? 0.4846 0.4158 0.4247 -0.0683 0.0466  -0.0191 175 THR E C     
6410  O O     . THR E 174 ? 0.5078 0.4420 0.4506 -0.0704 0.0478  -0.0195 175 THR E O     
6411  C CB    . THR E 174 ? 0.6042 0.5225 0.5352 -0.0707 0.0436  -0.0155 175 THR E CB    
6412  O OG1   . THR E 174 ? 0.5634 0.4801 0.4961 -0.0670 0.0414  -0.0170 175 THR E OG1   
6413  C CG2   . THR E 174 ? 0.6269 0.5396 0.5517 -0.0721 0.0429  -0.0131 175 THR E CG2   
6414  N N     . LEU E 175 ? 0.5226 0.4547 0.4646 -0.0647 0.0455  -0.0205 176 LEU E N     
6415  C CA    . LEU E 175 ? 0.5271 0.4633 0.4739 -0.0630 0.0456  -0.0225 176 LEU E CA    
6416  C C     . LEU E 175 ? 0.5101 0.4430 0.4576 -0.0635 0.0440  -0.0228 176 LEU E C     
6417  O O     . LEU E 175 ? 0.4807 0.4168 0.4319 -0.0636 0.0444  -0.0241 176 LEU E O     
6418  C CB    . LEU E 175 ? 0.5817 0.5246 0.5318 -0.0643 0.0481  -0.0233 176 LEU E CB    
6419  C CG    . LEU E 175 ? 0.6176 0.5642 0.5674 -0.0636 0.0497  -0.0234 176 LEU E CG    
6420  C CD1   . LEU E 175 ? 0.6154 0.5686 0.5690 -0.0644 0.0518  -0.0246 176 LEU E CD1   
6421  C CD2   . LEU E 175 ? 0.6546 0.6011 0.6046 -0.0602 0.0485  -0.0241 176 LEU E CD2   
6422  N N     . THR E 176 ? 0.5107 0.4369 0.4547 -0.0637 0.0420  -0.0217 177 THR E N     
6423  C CA    . THR E 176 ? 0.5139 0.4360 0.4580 -0.0640 0.0400  -0.0221 177 THR E CA    
6424  C C     . THR E 176 ? 0.5353 0.4532 0.4781 -0.0606 0.0375  -0.0228 177 THR E C     
6425  O O     . THR E 176 ? 0.5819 0.4963 0.5248 -0.0599 0.0356  -0.0236 177 THR E O     
6426  C CB    . THR E 176 ? 0.4989 0.4163 0.4398 -0.0678 0.0398  -0.0202 177 THR E CB    
6427  O OG1   . THR E 176 ? 0.5077 0.4197 0.4438 -0.0676 0.0386  -0.0185 177 THR E OG1   
6428  C CG2   . THR E 176 ? 0.4923 0.4145 0.4345 -0.0713 0.0425  -0.0196 177 THR E CG2   
6429  N N     . GLN E 177 ? 0.5731 0.4915 0.5149 -0.0584 0.0374  -0.0226 178 GLN E N     
6430  C CA    . GLN E 177 ? 0.5894 0.5050 0.5306 -0.0550 0.0352  -0.0233 178 GLN E CA    
6431  C C     . GLN E 177 ? 0.6049 0.5262 0.5500 -0.0522 0.0359  -0.0252 178 GLN E C     
6432  O O     . GLN E 177 ? 0.5948 0.5216 0.5423 -0.0527 0.0379  -0.0255 178 GLN E O     
6433  C CB    . GLN E 177 ? 0.5755 0.4873 0.5127 -0.0546 0.0342  -0.0218 178 GLN E CB    
6434  C CG    . GLN E 177 ? 0.6075 0.5126 0.5398 -0.0574 0.0332  -0.0196 178 GLN E CG    
6435  C CD    . GLN E 177 ? 0.6677 0.5668 0.5991 -0.0572 0.0306  -0.0199 178 GLN E CD    
6436  O OE1   . GLN E 177 ? 0.7644 0.6644 0.6986 -0.0548 0.0297  -0.0219 178 GLN E OE1   
6437  N NE2   . GLN E 177 ? 0.6421 0.5346 0.5691 -0.0597 0.0294  -0.0179 178 GLN E NE2   
6438  N N     . PHE E 178 ? 0.6507 0.5708 0.5966 -0.0492 0.0341  -0.0265 179 PHE E N     
6439  C CA    . PHE E 178 ? 0.6736 0.5990 0.6230 -0.0466 0.0346  -0.0281 179 PHE E CA    
6440  C C     . PHE E 178 ? 0.5914 0.5172 0.5403 -0.0443 0.0339  -0.0280 179 PHE E C     
6441  O O     . PHE E 178 ? 0.5947 0.5249 0.5463 -0.0424 0.0344  -0.0290 179 PHE E O     
6442  C CB    . PHE E 178 ? 0.7678 0.6925 0.7187 -0.0449 0.0333  -0.0299 179 PHE E CB    
6443  C CG    . PHE E 178 ? 0.8646 0.7888 0.8162 -0.0470 0.0337  -0.0302 179 PHE E CG    
6444  C CD1   . PHE E 178 ? 0.8901 0.8188 0.8437 -0.0491 0.0358  -0.0301 179 PHE E CD1   
6445  C CD2   . PHE E 178 ? 0.9957 0.9149 0.9459 -0.0470 0.0317  -0.0308 179 PHE E CD2   
6446  C CE1   . PHE E 178 ? 0.9317 0.8602 0.8862 -0.0511 0.0360  -0.0305 179 PHE E CE1   
6447  C CE2   . PHE E 178 ? 1.0266 0.9454 0.9775 -0.0491 0.0319  -0.0312 179 PHE E CE2   
6448  C CZ    . PHE E 178 ? 0.9711 0.8947 0.9242 -0.0512 0.0340  -0.0310 179 PHE E CZ    
6449  N N     . HIS E 179 ? 0.5542 0.4752 0.4995 -0.0447 0.0327  -0.0266 180 HIS E N     
6450  C CA    . HIS E 179 ? 0.5562 0.4772 0.5007 -0.0427 0.0318  -0.0263 180 HIS E CA    
6451  C C     . HIS E 179 ? 0.5446 0.4612 0.4845 -0.0445 0.0313  -0.0242 180 HIS E C     
6452  O O     . HIS E 179 ? 0.5482 0.4610 0.4856 -0.0470 0.0314  -0.0230 180 HIS E O     
6453  C CB    . HIS E 179 ? 0.5604 0.4796 0.5056 -0.0395 0.0294  -0.0276 180 HIS E CB    
6454  C CG    . HIS E 179 ? 0.6094 0.5216 0.5515 -0.0395 0.0271  -0.0273 180 HIS E CG    
6455  N ND1   . HIS E 179 ? 0.7079 0.6144 0.6461 -0.0395 0.0252  -0.0259 180 HIS E ND1   
6456  C CD2   . HIS E 179 ? 0.5812 0.4907 0.5234 -0.0396 0.0262  -0.0281 180 HIS E CD2   
6457  C CE1   . HIS E 179 ? 0.7227 0.6231 0.6587 -0.0395 0.0231  -0.0258 180 HIS E CE1   
6458  N NE2   . HIS E 179 ? 0.7005 0.6026 0.6389 -0.0396 0.0237  -0.0273 180 HIS E NE2   
6459  N N     . THR E 180 ? 0.5900 0.5072 0.5290 -0.0434 0.0309  -0.0238 181 THR E N     
6460  C CA    . THR E 180 ? 0.6641 0.5774 0.5985 -0.0448 0.0304  -0.0219 181 THR E CA    
6461  C C     . THR E 180 ? 0.6955 0.6032 0.6273 -0.0427 0.0273  -0.0216 181 THR E C     
6462  O O     . THR E 180 ? 0.6465 0.5528 0.5798 -0.0407 0.0256  -0.0228 181 THR E O     
6463  C CB    . THR E 180 ? 0.6459 0.5634 0.5806 -0.0450 0.0320  -0.0217 181 THR E CB    
6464  O OG1   . THR E 180 ? 0.6581 0.5717 0.5877 -0.0468 0.0318  -0.0198 181 THR E OG1   
6465  C CG2   . THR E 180 ? 0.6466 0.5669 0.5838 -0.0420 0.0310  -0.0228 181 THR E CG2   
6466  N N     . SER E 181 ? 0.7893 0.6942 0.7172 -0.0431 0.0264  -0.0201 182 SER E N     
6467  C CA    . SER E 181 ? 0.7790 0.6785 0.7041 -0.0410 0.0232  -0.0197 182 SER E CA    
6468  C C     . SER E 181 ? 0.7963 0.6983 0.7217 -0.0392 0.0226  -0.0199 182 SER E C     
6469  O O     . SER E 181 ? 0.7147 0.6214 0.6413 -0.0401 0.0247  -0.0200 182 SER E O     
6470  C CB    . SER E 181 ? 0.8702 0.7622 0.7894 -0.0433 0.0219  -0.0174 182 SER E CB    
6471  O OG    . SER E 181 ? 0.9158 0.8084 0.8317 -0.0461 0.0238  -0.0157 182 SER E OG    
6472  N N     . SER E 182 ? 0.7504 0.6490 0.6747 -0.0366 0.0195  -0.0201 183 SER E N     
6473  C CA    . SER E 182 ? 0.7725 0.6732 0.6972 -0.0347 0.0184  -0.0204 183 SER E CA    
6474  C C     . SER E 182 ? 0.7187 0.6173 0.6384 -0.0369 0.0189  -0.0184 183 SER E C     
6475  O O     . SER E 182 ? 0.6839 0.5859 0.6043 -0.0364 0.0194  -0.0187 183 SER E O     
6476  C CB    . SER E 182 ? 0.7787 0.6762 0.7035 -0.0314 0.0148  -0.0211 183 SER E CB    
6477  O OG    . SER E 182 ? 0.7863 0.6755 0.7055 -0.0321 0.0125  -0.0194 183 SER E OG    
6478  N N     . ASP E 183 ? 0.6555 0.5484 0.5700 -0.0393 0.0188  -0.0165 184 ASP E N     
6479  C CA    . ASP E 183 ? 0.6818 0.5722 0.5907 -0.0416 0.0193  -0.0145 184 ASP E CA    
6480  C C     . ASP E 183 ? 0.6202 0.5168 0.5308 -0.0435 0.0230  -0.0148 184 ASP E C     
6481  O O     . ASP E 183 ? 0.5368 0.4347 0.4452 -0.0440 0.0236  -0.0143 184 ASP E O     
6482  C CB    . ASP E 183 ? 0.7761 0.6591 0.6791 -0.0441 0.0184  -0.0122 184 ASP E CB    
6483  C CG    . ASP E 183 ? 0.8939 0.7770 0.7982 -0.0466 0.0204  -0.0120 184 ASP E CG    
6484  O OD1   . ASP E 183 ? 0.9621 0.8462 0.8706 -0.0451 0.0199  -0.0136 184 ASP E OD1   
6485  O OD2   . ASP E 183 ? 0.9723 0.8547 0.8733 -0.0502 0.0224  -0.0103 184 ASP E OD2   
6486  N N     . ARG E 184 ? 0.5668 0.4672 0.4814 -0.0446 0.0253  -0.0157 185 ARG E N     
6487  C CA    . ARG E 184 ? 0.5993 0.5057 0.5161 -0.0461 0.0286  -0.0163 185 ARG E CA    
6488  C C     . ARG E 184 ? 0.5856 0.4972 0.5061 -0.0438 0.0286  -0.0179 185 ARG E C     
6489  O O     . ARG E 184 ? 0.5012 0.4158 0.4213 -0.0445 0.0302  -0.0180 185 ARG E O     
6490  C CB    . ARG E 184 ? 0.6580 0.5671 0.5785 -0.0473 0.0305  -0.0170 185 ARG E CB    
6491  C CG    . ARG E 184 ? 0.7559 0.6605 0.6731 -0.0502 0.0308  -0.0155 185 ARG E CG    
6492  C CD    . ARG E 184 ? 0.8396 0.7442 0.7527 -0.0534 0.0329  -0.0138 185 ARG E CD    
6493  N NE    . ARG E 184 ? 0.8818 0.7831 0.7924 -0.0567 0.0335  -0.0123 185 ARG E NE    
6494  C CZ    . ARG E 184 ? 0.9725 0.8684 0.8770 -0.0590 0.0330  -0.0100 185 ARG E CZ    
6495  N NH1   . ARG E 184 ? 0.9892 0.8823 0.8893 -0.0583 0.0317  -0.0089 185 ARG E NH1   
6496  N NH2   . ARG E 184 ? 0.9834 0.8765 0.8862 -0.0622 0.0336  -0.0086 185 ARG E NH2   
6497  N N     . LEU E 185 ? 0.5957 0.5082 0.5199 -0.0410 0.0269  -0.0192 186 LEU E N     
6498  C CA    . LEU E 185 ? 0.5624 0.4799 0.4906 -0.0390 0.0267  -0.0207 186 LEU E CA    
6499  C C     . LEU E 185 ? 0.5177 0.4334 0.4428 -0.0382 0.0250  -0.0201 186 LEU E C     
6500  O O     . LEU E 185 ? 0.4855 0.4050 0.4123 -0.0377 0.0255  -0.0209 186 LEU E O     
6501  C CB    . LEU E 185 ? 0.5897 0.5087 0.5225 -0.0365 0.0254  -0.0221 186 LEU E CB    
6502  C CG    . LEU E 185 ? 0.5703 0.4915 0.5064 -0.0370 0.0269  -0.0230 186 LEU E CG    
6503  C CD1   . LEU E 185 ? 0.5383 0.4611 0.4783 -0.0343 0.0255  -0.0246 186 LEU E CD1   
6504  C CD2   . LEU E 185 ? 0.5531 0.4797 0.4919 -0.0384 0.0298  -0.0235 186 LEU E CD2   
6505  N N     . GLN E 186 ? 0.5095 0.4192 0.4298 -0.0381 0.0228  -0.0188 187 GLN E N     
6506  C CA    . GLN E 186 ? 0.5426 0.4499 0.4592 -0.0373 0.0208  -0.0181 187 GLN E CA    
6507  C C     . GLN E 186 ? 0.5544 0.4627 0.4676 -0.0395 0.0229  -0.0173 187 GLN E C     
6508  O O     . GLN E 186 ? 0.5470 0.4564 0.4592 -0.0388 0.0221  -0.0176 187 GLN E O     
6509  C CB    . GLN E 186 ? 0.5681 0.4680 0.4798 -0.0369 0.0178  -0.0166 187 GLN E CB    
6510  C CG    . GLN E 186 ? 0.6133 0.5100 0.5203 -0.0363 0.0155  -0.0157 187 GLN E CG    
6511  C CD    . GLN E 186 ? 0.6526 0.5533 0.5634 -0.0336 0.0140  -0.0173 187 GLN E CD    
6512  O OE1   . GLN E 186 ? 0.6788 0.5811 0.5941 -0.0311 0.0124  -0.0186 187 GLN E OE1   
6513  N NE2   . GLN E 186 ? 0.6726 0.5750 0.5817 -0.0342 0.0146  -0.0173 187 GLN E NE2   
6514  N N     . ILE E 187 ? 0.5644 0.4725 0.4758 -0.0422 0.0254  -0.0165 188 ILE E N     
6515  C CA    . ILE E 187 ? 0.5625 0.4721 0.4708 -0.0444 0.0277  -0.0160 188 ILE E CA    
6516  C C     . ILE E 187 ? 0.5170 0.4331 0.4301 -0.0436 0.0295  -0.0178 188 ILE E C     
6517  O O     . ILE E 187 ? 0.4859 0.4035 0.3971 -0.0438 0.0301  -0.0181 188 ILE E O     
6518  C CB    . ILE E 187 ? 0.5738 0.4820 0.4796 -0.0475 0.0300  -0.0147 188 ILE E CB    
6519  C CG1   . ILE E 187 ? 0.5862 0.4870 0.4862 -0.0486 0.0281  -0.0124 188 ILE E CG1   
6520  C CG2   . ILE E 187 ? 0.5683 0.4800 0.4724 -0.0495 0.0330  -0.0147 188 ILE E CG2   
6521  C CD1   . ILE E 187 ? 0.5988 0.4981 0.4965 -0.0520 0.0301  -0.0110 188 ILE E CD1   
6522  N N     . LEU E 188 ? 0.4597 0.3794 0.3787 -0.0428 0.0301  -0.0191 189 LEU E N     
6523  C CA    . LEU E 188 ? 0.4550 0.3804 0.3787 -0.0421 0.0315  -0.0208 189 LEU E CA    
6524  C C     . LEU E 188 ? 0.4338 0.3600 0.3582 -0.0401 0.0294  -0.0215 189 LEU E C     
6525  O O     . LEU E 188 ? 0.4161 0.3452 0.3413 -0.0400 0.0301  -0.0223 189 LEU E O     
6526  C CB    . LEU E 188 ? 0.4420 0.3704 0.3712 -0.0416 0.0322  -0.0217 189 LEU E CB    
6527  C CG    . LEU E 188 ? 0.4547 0.3886 0.3889 -0.0409 0.0333  -0.0233 189 LEU E CG    
6528  C CD1   . LEU E 188 ? 0.4663 0.4027 0.3998 -0.0424 0.0357  -0.0236 189 LEU E CD1   
6529  C CD2   . LEU E 188 ? 0.4807 0.4170 0.4197 -0.0403 0.0337  -0.0241 189 LEU E CD2   
6530  N N     . VAL E 189 ? 0.4335 0.3571 0.3579 -0.0384 0.0267  -0.0213 190 VAL E N     
6531  C CA    . VAL E 189 ? 0.4683 0.3927 0.3939 -0.0364 0.0244  -0.0220 190 VAL E CA    
6532  C C     . VAL E 189 ? 0.5249 0.4472 0.4452 -0.0370 0.0239  -0.0214 190 VAL E C     
6533  O O     . VAL E 189 ? 0.5101 0.4349 0.4316 -0.0364 0.0235  -0.0223 190 VAL E O     
6534  C CB    . VAL E 189 ? 0.4556 0.3775 0.3819 -0.0344 0.0214  -0.0219 190 VAL E CB    
6535  C CG1   . VAL E 189 ? 0.4658 0.3877 0.3921 -0.0326 0.0187  -0.0223 190 VAL E CG1   
6536  C CG2   . VAL E 189 ? 0.4433 0.3682 0.3753 -0.0334 0.0218  -0.0229 190 VAL E CG2   
6537  N N     . GLU E 190 ? 0.5187 0.4365 0.4331 -0.0384 0.0240  -0.0198 191 GLU E N     
6538  C CA    . GLU E 190 ? 0.5920 0.5075 0.5006 -0.0391 0.0236  -0.0191 191 GLU E CA    
6539  C C     . GLU E 190 ? 0.5200 0.4397 0.4292 -0.0402 0.0264  -0.0201 191 GLU E C     
6540  O O     . GLU E 190 ? 0.4889 0.4091 0.3961 -0.0398 0.0258  -0.0207 191 GLU E O     
6541  C CB    . GLU E 190 ? 0.6748 0.5847 0.5767 -0.0408 0.0235  -0.0170 191 GLU E CB    
6542  C CG    . GLU E 190 ? 0.7652 0.6701 0.6657 -0.0395 0.0202  -0.0160 191 GLU E CG    
6543  C CD    . GLU E 190 ? 0.8248 0.7233 0.7183 -0.0413 0.0197  -0.0137 191 GLU E CD    
6544  O OE1   . GLU E 190 ? 0.8917 0.7902 0.7814 -0.0439 0.0223  -0.0127 191 GLU E OE1   
6545  O OE2   . GLU E 190 ? 0.8591 0.7527 0.7507 -0.0401 0.0167  -0.0128 191 GLU E OE2   
6546  N N     . GLN E 191 ? 0.4707 0.3932 0.3826 -0.0415 0.0292  -0.0205 192 GLN E N     
6547  C CA    . GLN E 191 ? 0.4793 0.4058 0.3922 -0.0424 0.0318  -0.0216 192 GLN E CA    
6548  C C     . GLN E 191 ? 0.5019 0.4320 0.4194 -0.0407 0.0309  -0.0233 192 GLN E C     
6549  O O     . GLN E 191 ? 0.4982 0.4297 0.4145 -0.0406 0.0313  -0.0243 192 GLN E O     
6550  C CB    . GLN E 191 ? 0.4934 0.4224 0.4091 -0.0439 0.0345  -0.0216 192 GLN E CB    
6551  C CG    . GLN E 191 ? 0.5088 0.4422 0.4259 -0.0447 0.0371  -0.0229 192 GLN E CG    
6552  C CD    . GLN E 191 ? 0.5034 0.4395 0.4240 -0.0459 0.0394  -0.0231 192 GLN E CD    
6553  O OE1   . GLN E 191 ? 0.5218 0.4565 0.4439 -0.0462 0.0391  -0.0224 192 GLN E OE1   
6554  N NE2   . GLN E 191 ? 0.4610 0.4010 0.3831 -0.0464 0.0416  -0.0244 192 GLN E NE2   
6555  N N     . LEU E 192 ? 0.4848 0.4164 0.4074 -0.0395 0.0298  -0.0238 193 LEU E N     
6556  C CA    . LEU E 192 ? 0.4519 0.3870 0.3793 -0.0382 0.0290  -0.0252 193 LEU E CA    
6557  C C     . LEU E 192 ? 0.4388 0.3723 0.3641 -0.0370 0.0264  -0.0254 193 LEU E C     
6558  O O     . LEU E 192 ? 0.3710 0.3068 0.2988 -0.0364 0.0258  -0.0266 193 LEU E O     
6559  C CB    . LEU E 192 ? 0.4639 0.4009 0.3967 -0.0374 0.0286  -0.0254 193 LEU E CB    
6560  C CG    . LEU E 192 ? 0.4789 0.4180 0.4145 -0.0383 0.0310  -0.0256 193 LEU E CG    
6561  C CD1   . LEU E 192 ? 0.4480 0.3890 0.3885 -0.0373 0.0303  -0.0259 193 LEU E CD1   
6562  C CD2   . LEU E 192 ? 0.5027 0.4450 0.4398 -0.0390 0.0329  -0.0265 193 LEU E CD2   
6563  N N     . ASN E 193 ? 0.4621 0.3915 0.3829 -0.0368 0.0247  -0.0243 194 ASN E N     
6564  C CA    . ASN E 193 ? 0.5055 0.4331 0.4244 -0.0356 0.0218  -0.0244 194 ASN E CA    
6565  C C     . ASN E 193 ? 0.5330 0.4608 0.4485 -0.0360 0.0223  -0.0252 194 ASN E C     
6566  O O     . ASN E 193 ? 0.4802 0.4071 0.3943 -0.0351 0.0199  -0.0256 194 ASN E O     
6567  C CB    . ASN E 193 ? 0.5395 0.4622 0.4538 -0.0352 0.0197  -0.0230 194 ASN E CB    
6568  C CG    . ASN E 193 ? 0.5799 0.5010 0.4928 -0.0336 0.0163  -0.0232 194 ASN E CG    
6569  O OD1   . ASN E 193 ? 0.6391 0.5630 0.5571 -0.0323 0.0148  -0.0243 194 ASN E OD1   
6570  N ND2   . ASN E 193 ? 0.6095 0.5263 0.5157 -0.0339 0.0151  -0.0222 194 ASN E ND2   
6571  N N     . GLN E 194 ? 0.5297 0.4591 0.4443 -0.0373 0.0252  -0.0255 195 GLN E N     
6572  C CA    . GLN E 194 ? 0.5553 0.4854 0.4670 -0.0376 0.0260  -0.0266 195 GLN E CA    
6573  C C     . GLN E 194 ? 0.5927 0.5258 0.5092 -0.0365 0.0249  -0.0283 195 GLN E C     
6574  O O     . GLN E 194 ? 0.5994 0.5322 0.5137 -0.0360 0.0240  -0.0294 195 GLN E O     
6575  C CB    . GLN E 194 ? 0.5812 0.5130 0.4916 -0.0391 0.0294  -0.0267 195 GLN E CB    
6576  C CG    . GLN E 194 ? 0.5683 0.4972 0.4737 -0.0407 0.0307  -0.0249 195 GLN E CG    
6577  C CD    . GLN E 194 ? 0.5480 0.4795 0.4529 -0.0424 0.0343  -0.0252 195 GLN E CD    
6578  O OE1   . GLN E 194 ? 0.5759 0.5094 0.4792 -0.0424 0.0356  -0.0265 195 GLN E OE1   
6579  N NE2   . GLN E 194 ? 0.5308 0.4624 0.4372 -0.0436 0.0357  -0.0241 195 GLN E NE2   
6580  N N     . TRP E 195 ? 0.5712 0.5069 0.4938 -0.0362 0.0250  -0.0285 196 TRP E N     
6581  C CA    . TRP E 195 ? 0.5337 0.4722 0.4610 -0.0357 0.0243  -0.0299 196 TRP E CA    
6582  C C     . TRP E 195 ? 0.4815 0.4209 0.4132 -0.0348 0.0220  -0.0297 196 TRP E C     
6583  O O     . TRP E 195 ? 0.4466 0.3873 0.3810 -0.0343 0.0204  -0.0305 196 TRP E O     
6584  C CB    . TRP E 195 ? 0.5630 0.5045 0.4938 -0.0363 0.0269  -0.0305 196 TRP E CB    
6585  C CG    . TRP E 195 ? 0.5328 0.4744 0.4601 -0.0371 0.0294  -0.0309 196 TRP E CG    
6586  C CD1   . TRP E 195 ? 0.5535 0.4956 0.4790 -0.0369 0.0297  -0.0324 196 TRP E CD1   
6587  C CD2   . TRP E 195 ? 0.5124 0.4538 0.4377 -0.0383 0.0318  -0.0300 196 TRP E CD2   
6588  N NE1   . TRP E 195 ? 0.5715 0.5142 0.4942 -0.0377 0.0324  -0.0326 196 TRP E NE1   
6589  C CE2   . TRP E 195 ? 0.5103 0.4527 0.4329 -0.0387 0.0337  -0.0310 196 TRP E CE2   
6590  C CE3   . TRP E 195 ? 0.5383 0.4788 0.4639 -0.0390 0.0324  -0.0286 196 TRP E CE3   
6591  C CZ2   . TRP E 195 ? 0.4950 0.4379 0.4154 -0.0401 0.0363  -0.0305 196 TRP E CZ2   
6592  C CZ3   . TRP E 195 ? 0.4799 0.4203 0.4032 -0.0404 0.0349  -0.0280 196 TRP E CZ3   
6593  C CH2   . TRP E 195 ? 0.4711 0.4130 0.3920 -0.0411 0.0369  -0.0288 196 TRP E CH2   
6594  N N     . TYR E 196 ? 0.4470 0.3859 0.3797 -0.0346 0.0219  -0.0286 197 TYR E N     
6595  C CA    . TYR E 196 ? 0.4451 0.3857 0.3825 -0.0337 0.0202  -0.0286 197 TYR E CA    
6596  C C     . TYR E 196 ? 0.4529 0.3907 0.3879 -0.0326 0.0178  -0.0278 197 TYR E C     
6597  O O     . TYR E 196 ? 0.4789 0.4135 0.4099 -0.0328 0.0182  -0.0268 197 TYR E O     
6598  C CB    . TYR E 196 ? 0.4005 0.3436 0.3420 -0.0340 0.0221  -0.0283 197 TYR E CB    
6599  C CG    . TYR E 196 ? 0.4064 0.3522 0.3503 -0.0350 0.0243  -0.0290 197 TYR E CG    
6600  C CD1   . TYR E 196 ? 0.4100 0.3587 0.3583 -0.0350 0.0239  -0.0297 197 TYR E CD1   
6601  C CD2   . TYR E 196 ? 0.4023 0.3475 0.3439 -0.0359 0.0268  -0.0288 197 TYR E CD2   
6602  C CE1   . TYR E 196 ? 0.4177 0.3683 0.3679 -0.0358 0.0256  -0.0302 197 TYR E CE1   
6603  C CE2   . TYR E 196 ? 0.4167 0.3643 0.3606 -0.0366 0.0285  -0.0296 197 TYR E CE2   
6604  C CZ    . TYR E 196 ? 0.4022 0.3522 0.3502 -0.0364 0.0278  -0.0302 197 TYR E CZ    
6605  O OH    . TYR E 196 ? 0.4956 0.4475 0.4456 -0.0369 0.0293  -0.0309 197 TYR E OH    
6606  N N     . PRO E 197 ? 0.4706 0.4093 0.4080 -0.0316 0.0150  -0.0283 198 PRO E N     
6607  C CA    . PRO E 197 ? 0.5049 0.4413 0.4408 -0.0302 0.0124  -0.0278 198 PRO E CA    
6608  C C     . PRO E 197 ? 0.5118 0.4482 0.4496 -0.0296 0.0130  -0.0272 198 PRO E C     
6609  O O     . PRO E 197 ? 0.5411 0.4802 0.4823 -0.0302 0.0152  -0.0273 198 PRO E O     
6610  C CB    . PRO E 197 ? 0.5416 0.4808 0.4818 -0.0293 0.0098  -0.0287 198 PRO E CB    
6611  C CG    . PRO E 197 ? 0.5498 0.4908 0.4909 -0.0305 0.0107  -0.0295 198 PRO E CG    
6612  C CD    . PRO E 197 ? 0.4961 0.4380 0.4375 -0.0316 0.0142  -0.0294 198 PRO E CD    
6613  N N     . LEU E 198 ? 0.5528 0.4858 0.4879 -0.0284 0.0108  -0.0265 199 LEU E N     
6614  C CA    . LEU E 198 ? 0.5806 0.5126 0.5168 -0.0277 0.0109  -0.0261 199 LEU E CA    
6615  C C     . LEU E 198 ? 0.6095 0.5464 0.5528 -0.0263 0.0102  -0.0272 199 LEU E C     
6616  O O     . LEU E 198 ? 0.6075 0.5453 0.5531 -0.0258 0.0111  -0.0273 199 LEU E O     
6617  C CB    . LEU E 198 ? 0.6123 0.5386 0.5430 -0.0267 0.0085  -0.0250 199 LEU E CB    
6618  C CG    . LEU E 198 ? 0.6339 0.5553 0.5571 -0.0284 0.0095  -0.0236 199 LEU E CG    
6619  C CD1   . LEU E 198 ? 0.5923 0.5076 0.5101 -0.0276 0.0069  -0.0223 199 LEU E CD1   
6620  C CD2   . LEU E 198 ? 0.6529 0.5749 0.5758 -0.0303 0.0131  -0.0232 199 LEU E CD2   
6621  N N     . ASP E 199 ? 0.6143 0.5544 0.5608 -0.0258 0.0086  -0.0280 200 ASP E N     
6622  C CA    . ASP E 199 ? 0.6382 0.5835 0.5915 -0.0246 0.0078  -0.0291 200 ASP E CA    
6623  C C     . ASP E 199 ? 0.6222 0.5723 0.5799 -0.0262 0.0102  -0.0295 200 ASP E C     
6624  O O     . ASP E 199 ? 0.5756 0.5308 0.5390 -0.0258 0.0099  -0.0303 200 ASP E O     
6625  C CB    . ASP E 199 ? 0.6482 0.5943 0.6029 -0.0232 0.0043  -0.0297 200 ASP E CB    
6626  C CG    . ASP E 199 ? 0.6722 0.6187 0.6260 -0.0243 0.0035  -0.0299 200 ASP E CG    
6627  O OD1   . ASP E 199 ? 0.6900 0.6363 0.6423 -0.0261 0.0057  -0.0297 200 ASP E OD1   
6628  O OD2   . ASP E 199 ? 0.7256 0.6724 0.6801 -0.0233 0.0005  -0.0304 200 ASP E OD2   
6629  N N     . HIS E 200 ? 0.5608 0.5095 0.5158 -0.0279 0.0125  -0.0291 201 HIS E N     
6630  C CA    . HIS E 200 ? 0.5468 0.4993 0.5053 -0.0293 0.0147  -0.0294 201 HIS E CA    
6631  C C     . HIS E 200 ? 0.4989 0.4545 0.4613 -0.0291 0.0164  -0.0296 201 HIS E C     
6632  O O     . HIS E 200 ? 0.4749 0.4283 0.4353 -0.0288 0.0174  -0.0292 201 HIS E O     
6633  C CB    . HIS E 200 ? 0.5638 0.5140 0.5184 -0.0308 0.0165  -0.0291 201 HIS E CB    
6634  C CG    . HIS E 200 ? 0.5368 0.4902 0.4946 -0.0321 0.0184  -0.0294 201 HIS E CG    
6635  N ND1   . HIS E 200 ? 0.5348 0.4902 0.4949 -0.0327 0.0174  -0.0300 201 HIS E ND1   
6636  C CD2   . HIS E 200 ? 0.5230 0.4778 0.4822 -0.0329 0.0209  -0.0293 201 HIS E CD2   
6637  C CE1   . HIS E 200 ? 0.5560 0.5135 0.5184 -0.0338 0.0192  -0.0301 201 HIS E CE1   
6638  N NE2   . HIS E 200 ? 0.5383 0.4956 0.5002 -0.0339 0.0213  -0.0297 201 HIS E NE2   
6639  N N     . GLU E 201 ? 0.4614 0.4221 0.4293 -0.0293 0.0166  -0.0301 202 GLU E N     
6640  C CA    . GLU E 201 ? 0.4767 0.4410 0.4484 -0.0291 0.0182  -0.0304 202 GLU E CA    
6641  C C     . GLU E 201 ? 0.3935 0.3572 0.3641 -0.0305 0.0210  -0.0300 202 GLU E C     
6642  O O     . GLU E 201 ? 0.3290 0.2935 0.2998 -0.0320 0.0218  -0.0298 202 GLU E O     
6643  C CB    . GLU E 201 ? 0.4737 0.4439 0.4512 -0.0292 0.0177  -0.0309 202 GLU E CB    
6644  C CG    . GLU E 201 ? 0.5516 0.5259 0.5329 -0.0289 0.0194  -0.0313 202 GLU E CG    
6645  C CD    . GLU E 201 ? 0.5846 0.5653 0.5716 -0.0295 0.0194  -0.0317 202 GLU E CD    
6646  O OE1   . GLU E 201 ? 0.6007 0.5850 0.5911 -0.0280 0.0187  -0.0325 202 GLU E OE1   
6647  O OE2   . GLU E 201 ? 0.5730 0.5550 0.5610 -0.0314 0.0199  -0.0312 202 GLU E OE2   
6648  N N     . VAL E 202 ? 0.4027 0.3651 0.3721 -0.0300 0.0221  -0.0299 203 VAL E N     
6649  C CA    . VAL E 202 ? 0.3858 0.3481 0.3547 -0.0312 0.0246  -0.0296 203 VAL E CA    
6650  C C     . VAL E 202 ? 0.3757 0.3419 0.3485 -0.0307 0.0257  -0.0301 203 VAL E C     
6651  O O     . VAL E 202 ? 0.3853 0.3538 0.3607 -0.0293 0.0246  -0.0307 203 VAL E O     
6652  C CB    . VAL E 202 ? 0.4343 0.3918 0.3984 -0.0314 0.0253  -0.0291 203 VAL E CB    
6653  C CG1   . VAL E 202 ? 0.4878 0.4422 0.4478 -0.0322 0.0249  -0.0286 203 VAL E CG1   
6654  C CG2   . VAL E 202 ? 0.4367 0.3917 0.3995 -0.0299 0.0241  -0.0291 203 VAL E CG2   
6655  N N     . VAL E 203 ? 0.3402 0.3072 0.3133 -0.0318 0.0278  -0.0300 204 VAL E N     
6656  C CA    . VAL E 203 ? 0.3064 0.2772 0.2828 -0.0315 0.0289  -0.0305 204 VAL E CA    
6657  C C     . VAL E 203 ? 0.3174 0.2861 0.2919 -0.0317 0.0305  -0.0305 204 VAL E C     
6658  O O     . VAL E 203 ? 0.3348 0.3019 0.3075 -0.0330 0.0316  -0.0300 204 VAL E O     
6659  C CB    . VAL E 203 ? 0.3163 0.2912 0.2958 -0.0329 0.0298  -0.0303 204 VAL E CB    
6660  C CG1   . VAL E 203 ? 0.3418 0.3207 0.3241 -0.0328 0.0312  -0.0306 204 VAL E CG1   
6661  C CG2   . VAL E 203 ? 0.3086 0.2855 0.2902 -0.0330 0.0281  -0.0303 204 VAL E CG2   
6662  N N     . ILE E 204 ? 0.3223 0.2912 0.2974 -0.0303 0.0303  -0.0311 205 ILE E N     
6663  C CA    . ILE E 204 ? 0.3253 0.2928 0.2993 -0.0305 0.0316  -0.0313 205 ILE E CA    
6664  C C     . ILE E 204 ? 0.3280 0.3002 0.3051 -0.0308 0.0330  -0.0318 205 ILE E C     
6665  O O     . ILE E 204 ? 0.3795 0.3552 0.3593 -0.0296 0.0328  -0.0326 205 ILE E O     
6666  C CB    . ILE E 204 ? 0.3084 0.2729 0.2809 -0.0288 0.0304  -0.0319 205 ILE E CB    
6667  C CG1   . ILE E 204 ? 0.3072 0.2665 0.2759 -0.0287 0.0289  -0.0311 205 ILE E CG1   
6668  C CG2   . ILE E 204 ? 0.3063 0.2696 0.2780 -0.0290 0.0316  -0.0322 205 ILE E CG2   
6669  C CD1   . ILE E 204 ? 0.3380 0.2935 0.3049 -0.0270 0.0273  -0.0315 205 ILE E CD1   
6670  N N     . TYR E 205 ? 0.3407 0.3132 0.3174 -0.0324 0.0345  -0.0313 206 TYR E N     
6671  C CA    . TYR E 205 ? 0.3385 0.3150 0.3176 -0.0330 0.0358  -0.0315 206 TYR E CA    
6672  C C     . TYR E 205 ? 0.3419 0.3174 0.3200 -0.0329 0.0368  -0.0319 206 TYR E C     
6673  O O     . TYR E 205 ? 0.3769 0.3489 0.3526 -0.0335 0.0371  -0.0317 206 TYR E O     
6674  C CB    . TYR E 205 ? 0.3239 0.3014 0.3035 -0.0347 0.0363  -0.0306 206 TYR E CB    
6675  C CG    . TYR E 205 ? 0.3484 0.3290 0.3296 -0.0356 0.0375  -0.0305 206 TYR E CG    
6676  C CD1   . TYR E 205 ? 0.3756 0.3606 0.3595 -0.0355 0.0377  -0.0305 206 TYR E CD1   
6677  C CD2   . TYR E 205 ? 0.3404 0.3197 0.3203 -0.0365 0.0385  -0.0302 206 TYR E CD2   
6678  C CE1   . TYR E 205 ? 0.3587 0.3464 0.3435 -0.0365 0.0389  -0.0302 206 TYR E CE1   
6679  C CE2   . TYR E 205 ? 0.3451 0.3269 0.3262 -0.0373 0.0394  -0.0300 206 TYR E CE2   
6680  C CZ    . TYR E 205 ? 0.3724 0.3582 0.3556 -0.0373 0.0396  -0.0299 206 TYR E CZ    
6681  O OH    . TYR E 205 ? 0.4508 0.4389 0.4346 -0.0382 0.0404  -0.0296 206 TYR E OH    
6682  N N     . GLU E 206 ? 0.3411 0.3200 0.3211 -0.0323 0.0375  -0.0326 207 GLU E N     
6683  C CA    . GLU E 206 ? 0.3346 0.3132 0.3138 -0.0323 0.0384  -0.0332 207 GLU E CA    
6684  C C     . GLU E 206 ? 0.3491 0.3324 0.3303 -0.0329 0.0396  -0.0332 207 GLU E C     
6685  O O     . GLU E 206 ? 0.3602 0.3472 0.3433 -0.0319 0.0397  -0.0339 207 GLU E O     
6686  C CB    . GLU E 206 ? 0.3446 0.3216 0.3232 -0.0305 0.0377  -0.0344 207 GLU E CB    
6687  C CG    . GLU E 206 ? 0.3876 0.3593 0.3636 -0.0301 0.0365  -0.0341 207 GLU E CG    
6688  C CD    . GLU E 206 ? 0.4220 0.3913 0.3971 -0.0283 0.0354  -0.0353 207 GLU E CD    
6689  O OE1   . GLU E 206 ? 0.4118 0.3838 0.3884 -0.0270 0.0358  -0.0366 207 GLU E OE1   
6690  O OE2   . GLU E 206 ? 0.4024 0.3669 0.3751 -0.0281 0.0342  -0.0350 207 GLU E OE2   
6691  N N     . ALA E 207 ? 0.3758 0.3590 0.3565 -0.0344 0.0404  -0.0325 208 ALA E N     
6692  C CA    . ALA E 207 ? 0.4146 0.4015 0.3965 -0.0351 0.0413  -0.0323 208 ALA E CA    
6693  C C     . ALA E 207 ? 0.3670 0.3553 0.3487 -0.0339 0.0419  -0.0335 208 ALA E C     
6694  O O     . ALA E 207 ? 0.3987 0.3840 0.3789 -0.0331 0.0416  -0.0344 208 ALA E O     
6695  C CB    . ALA E 207 ? 0.4037 0.3892 0.3846 -0.0367 0.0417  -0.0314 208 ALA E CB    
6696  N N     . ALA E 208 ? 0.3569 0.3498 0.3401 -0.0339 0.0426  -0.0337 209 ALA E N     
6697  C CA    . ALA E 208 ? 0.3568 0.3517 0.3398 -0.0327 0.0432  -0.0350 209 ALA E CA    
6698  C C     . ALA E 208 ? 0.3281 0.3214 0.3091 -0.0335 0.0438  -0.0350 209 ALA E C     
6699  O O     . ALA E 208 ? 0.3588 0.3518 0.3395 -0.0352 0.0440  -0.0337 209 ALA E O     
6700  C CB    . ALA E 208 ? 0.3653 0.3660 0.3502 -0.0326 0.0441  -0.0351 209 ALA E CB    
6701  N N     . ASN E 209 ? 0.3095 0.3018 0.2894 -0.0322 0.0437  -0.0365 210 ASN E N     
6702  C CA    . ASN E 209 ? 0.3339 0.3249 0.3120 -0.0328 0.0440  -0.0367 210 ASN E CA    
6703  C C     . ASN E 209 ? 0.3169 0.3121 0.2949 -0.0324 0.0450  -0.0373 210 ASN E C     
6704  O O     . ASN E 209 ? 0.3618 0.3571 0.3385 -0.0333 0.0453  -0.0372 210 ASN E O     
6705  C CB    . ASN E 209 ? 0.3285 0.3152 0.3052 -0.0320 0.0432  -0.0378 210 ASN E CB    
6706  C CG    . ASN E 209 ? 0.3255 0.3083 0.3019 -0.0329 0.0425  -0.0368 210 ASN E CG    
6707  O OD1   . ASN E 209 ? 0.3457 0.3278 0.3220 -0.0344 0.0427  -0.0357 210 ASN E OD1   
6708  N ND2   . ASN E 209 ? 0.3535 0.3335 0.3295 -0.0318 0.0417  -0.0374 210 ASN E ND2   
6709  N N     . LEU E 210 ? 0.3194 0.3184 0.2988 -0.0312 0.0454  -0.0382 211 LEU E N     
6710  C CA    . LEU E 210 ? 0.3475 0.3511 0.3267 -0.0307 0.0466  -0.0391 211 LEU E CA    
6711  C C     . LEU E 210 ? 0.3111 0.3197 0.2921 -0.0319 0.0475  -0.0378 211 LEU E C     
6712  O O     . LEU E 210 ? 0.2812 0.2903 0.2642 -0.0321 0.0472  -0.0370 211 LEU E O     
6713  C CB    . LEU E 210 ? 0.3880 0.3922 0.3672 -0.0280 0.0463  -0.0416 211 LEU E CB    
6714  C CG    . LEU E 210 ? 0.4220 0.4211 0.3991 -0.0269 0.0453  -0.0429 211 LEU E CG    
6715  C CD1   . LEU E 210 ? 0.4529 0.4526 0.4301 -0.0241 0.0449  -0.0456 211 LEU E CD1   
6716  C CD2   . LEU E 210 ? 0.4825 0.4809 0.4575 -0.0282 0.0456  -0.0426 211 LEU E CD2   
6717  N N     . PRO E 211 ? 0.2681 0.2807 0.2483 -0.0327 0.0488  -0.0374 212 PRO E N     
6718  C CA    . PRO E 211 ? 0.2846 0.3021 0.2664 -0.0344 0.0498  -0.0359 212 PRO E CA    
6719  C C     . PRO E 211 ? 0.3277 0.3505 0.3121 -0.0330 0.0505  -0.0372 212 PRO E C     
6720  O O     . PRO E 211 ? 0.3431 0.3700 0.3295 -0.0344 0.0512  -0.0359 212 PRO E O     
6721  C CB    . PRO E 211 ? 0.2926 0.3120 0.2719 -0.0356 0.0508  -0.0353 212 PRO E CB    
6722  C CG    . PRO E 211 ? 0.2850 0.3032 0.2624 -0.0335 0.0508  -0.0376 212 PRO E CG    
6723  C CD    . PRO E 211 ? 0.2972 0.3096 0.2747 -0.0323 0.0492  -0.0384 212 PRO E CD    
6724  N N     . ILE E 212 ? 0.3487 0.3714 0.3333 -0.0302 0.0502  -0.0397 213 ILE E N     
6725  C CA    . ILE E 212 ? 0.3568 0.3845 0.3442 -0.0284 0.0507  -0.0413 213 ILE E CA    
6726  C C     . ILE E 212 ? 0.3350 0.3592 0.3241 -0.0270 0.0490  -0.0417 213 ILE E C     
6727  O O     . ILE E 212 ? 0.3316 0.3589 0.3232 -0.0250 0.0487  -0.0433 213 ILE E O     
6728  C CB    . ILE E 212 ? 0.3927 0.4228 0.3791 -0.0258 0.0514  -0.0440 213 ILE E CB    
6729  C CG1   . ILE E 212 ? 0.4133 0.4370 0.3974 -0.0240 0.0499  -0.0456 213 ILE E CG1   
6730  C CG2   . ILE E 212 ? 0.4443 0.4788 0.4289 -0.0273 0.0533  -0.0435 213 ILE E CG2   
6731  C CD1   . ILE E 212 ? 0.4348 0.4541 0.4201 -0.0225 0.0480  -0.0462 213 ILE E CD1   
6732  N N     . GLN E 213 ? 0.3700 0.3881 0.3578 -0.0280 0.0477  -0.0404 214 GLN E N     
6733  C CA    . GLN E 213 ? 0.3827 0.3967 0.3712 -0.0269 0.0460  -0.0406 214 GLN E CA    
6734  C C     . GLN E 213 ? 0.4166 0.4313 0.4070 -0.0288 0.0457  -0.0387 214 GLN E C     
6735  O O     . GLN E 213 ? 0.5107 0.5251 0.5004 -0.0312 0.0461  -0.0368 214 GLN E O     
6736  C CB    . GLN E 213 ? 0.4342 0.4413 0.4199 -0.0269 0.0450  -0.0406 214 GLN E CB    
6737  C CG    . GLN E 213 ? 0.4646 0.4669 0.4503 -0.0260 0.0433  -0.0406 214 GLN E CG    
6738  C CD    . GLN E 213 ? 0.4551 0.4510 0.4380 -0.0267 0.0425  -0.0402 214 GLN E CD    
6739  O OE1   . GLN E 213 ? 0.4430 0.4380 0.4243 -0.0277 0.0432  -0.0399 214 GLN E OE1   
6740  N NE2   . GLN E 213 ? 0.4769 0.4685 0.4593 -0.0261 0.0411  -0.0400 214 GLN E NE2   
6741  N N     . ALA E 214 ? 0.4749 0.4901 0.4674 -0.0275 0.0446  -0.0393 215 ALA E N     
6742  C CA    . ALA E 214 ? 0.4646 0.4797 0.4587 -0.0289 0.0439  -0.0377 215 ALA E CA    
6743  C C     . ALA E 214 ? 0.4420 0.4501 0.4340 -0.0290 0.0424  -0.0370 215 ALA E C     
6744  O O     . ALA E 214 ? 0.4105 0.4147 0.4009 -0.0273 0.0415  -0.0381 215 ALA E O     
6745  C CB    . ALA E 214 ? 0.5146 0.5343 0.5122 -0.0275 0.0434  -0.0387 215 ALA E CB    
6746  N N     . PRO E 215 ? 0.4203 0.4265 0.4121 -0.0311 0.0420  -0.0352 216 PRO E N     
6747  C CA    . PRO E 215 ? 0.4509 0.4510 0.4406 -0.0312 0.0408  -0.0346 216 PRO E CA    
6748  C C     . PRO E 215 ? 0.3970 0.3956 0.3873 -0.0295 0.0392  -0.0354 216 PRO E C     
6749  O O     . PRO E 215 ? 0.4125 0.4152 0.4056 -0.0286 0.0388  -0.0359 216 PRO E O     
6750  C CB    . PRO E 215 ? 0.4183 0.4182 0.4080 -0.0337 0.0408  -0.0328 216 PRO E CB    
6751  C CG    . PRO E 215 ? 0.4151 0.4208 0.4078 -0.0345 0.0414  -0.0324 216 PRO E CG    
6752  C CD    . PRO E 215 ? 0.3962 0.4059 0.3895 -0.0334 0.0426  -0.0337 216 PRO E CD    
6753  N N     . ARG E 216 ? 0.4002 0.3932 0.3880 -0.0290 0.0382  -0.0353 217 ARG E N     
6754  C CA    . ARG E 216 ? 0.3683 0.3587 0.3558 -0.0276 0.0364  -0.0357 217 ARG E CA    
6755  C C     . ARG E 216 ? 0.3566 0.3458 0.3440 -0.0290 0.0357  -0.0343 217 ARG E C     
6756  O O     . ARG E 216 ? 0.3056 0.2917 0.2909 -0.0306 0.0360  -0.0333 217 ARG E O     
6757  C CB    . ARG E 216 ? 0.3563 0.3409 0.3407 -0.0266 0.0356  -0.0361 217 ARG E CB    
6758  C CG    . ARG E 216 ? 0.3764 0.3577 0.3599 -0.0251 0.0336  -0.0363 217 ARG E CG    
6759  C CD    . ARG E 216 ? 0.3755 0.3503 0.3553 -0.0249 0.0328  -0.0362 217 ARG E CD    
6760  N NE    . ARG E 216 ? 0.3958 0.3670 0.3743 -0.0234 0.0306  -0.0363 217 ARG E NE    
6761  C CZ    . ARG E 216 ? 0.4068 0.3719 0.3818 -0.0232 0.0296  -0.0359 217 ARG E CZ    
6762  N NH1   . ARG E 216 ? 0.4202 0.3824 0.3929 -0.0247 0.0306  -0.0355 217 ARG E NH1   
6763  N NH2   . ARG E 216 ? 0.3992 0.3610 0.3729 -0.0218 0.0274  -0.0360 217 ARG E NH2   
6764  N N     . ILE E 217 ? 0.3998 0.3917 0.3896 -0.0284 0.0346  -0.0345 218 ILE E N     
6765  C CA    . ILE E 217 ? 0.4405 0.4312 0.4302 -0.0295 0.0335  -0.0334 218 ILE E CA    
6766  C C     . ILE E 217 ? 0.4704 0.4599 0.4604 -0.0276 0.0315  -0.0341 218 ILE E C     
6767  O O     . ILE E 217 ? 0.5012 0.4948 0.4944 -0.0271 0.0307  -0.0345 218 ILE E O     
6768  C CB    . ILE E 217 ? 0.4715 0.4669 0.4641 -0.0313 0.0342  -0.0327 218 ILE E CB    
6769  C CG1   . ILE E 217 ? 0.4929 0.4893 0.4850 -0.0330 0.0360  -0.0320 218 ILE E CG1   
6770  C CG2   . ILE E 217 ? 0.4938 0.4874 0.4860 -0.0325 0.0328  -0.0318 218 ILE E CG2   
6771  C CD1   . ILE E 217 ? 0.5431 0.5435 0.5375 -0.0351 0.0365  -0.0310 218 ILE E CD1   
6772  N N     . GLU E 218 ? 0.4883 0.4722 0.4749 -0.0268 0.0305  -0.0341 219 GLU E N     
6773  C CA    . GLU E 218 ? 0.5078 0.4895 0.4938 -0.0248 0.0283  -0.0346 219 GLU E CA    
6774  C C     . GLU E 218 ? 0.4881 0.4669 0.4723 -0.0258 0.0270  -0.0336 219 GLU E C     
6775  O O     . GLU E 218 ? 0.4675 0.4419 0.4481 -0.0270 0.0273  -0.0326 219 GLU E O     
6776  C CB    . GLU E 218 ? 0.5782 0.5551 0.5613 -0.0233 0.0277  -0.0352 219 GLU E CB    
6777  C CG    . GLU E 218 ? 0.6138 0.5877 0.5959 -0.0211 0.0251  -0.0357 219 GLU E CG    
6778  C CD    . GLU E 218 ? 0.7064 0.6749 0.6853 -0.0198 0.0242  -0.0361 219 GLU E CD    
6779  O OE1   . GLU E 218 ? 0.7365 0.7040 0.7143 -0.0205 0.0257  -0.0361 219 GLU E OE1   
6780  O OE2   . GLU E 218 ? 0.8131 0.7782 0.7906 -0.0180 0.0218  -0.0363 219 GLU E OE2   
6781  N N     . ARG E 219 ? 0.4267 0.4082 0.4134 -0.0252 0.0254  -0.0338 220 ARG E N     
6782  C CA    . ARG E 219 ? 0.4344 0.4134 0.4194 -0.0259 0.0239  -0.0331 220 ARG E CA    
6783  C C     . ARG E 219 ? 0.4480 0.4230 0.4307 -0.0238 0.0215  -0.0334 220 ARG E C     
6784  O O     . ARG E 219 ? 0.4610 0.4378 0.4459 -0.0216 0.0203  -0.0345 220 ARG E O     
6785  C CB    . ARG E 219 ? 0.4637 0.4478 0.4528 -0.0267 0.0234  -0.0331 220 ARG E CB    
6786  C CG    . ARG E 219 ? 0.4898 0.4774 0.4809 -0.0290 0.0255  -0.0325 220 ARG E CG    
6787  C CD    . ARG E 219 ? 0.5679 0.5609 0.5633 -0.0300 0.0250  -0.0325 220 ARG E CD    
6788  N NE    . ARG E 219 ? 0.5532 0.5492 0.5503 -0.0322 0.0268  -0.0317 220 ARG E NE    
6789  C CZ    . ARG E 219 ? 0.6348 0.6280 0.6296 -0.0340 0.0275  -0.0307 220 ARG E CZ    
6790  N NH1   . ARG E 219 ? 0.6240 0.6119 0.6151 -0.0340 0.0266  -0.0305 220 ARG E NH1   
6791  N NH2   . ARG E 219 ? 0.6816 0.6774 0.6779 -0.0359 0.0289  -0.0301 220 ARG E NH2   
6792  N N     . LEU E 220 ? 0.4207 0.3902 0.3989 -0.0245 0.0206  -0.0325 221 LEU E N     
6793  C CA    . LEU E 220 ? 0.4430 0.4079 0.4181 -0.0228 0.0182  -0.0324 221 LEU E CA    
6794  C C     . LEU E 220 ? 0.4691 0.4296 0.4397 -0.0241 0.0175  -0.0313 221 LEU E C     
6795  O O     . LEU E 220 ? 0.4850 0.4452 0.4543 -0.0261 0.0193  -0.0306 221 LEU E O     
6796  C CB    . LEU E 220 ? 0.4749 0.4359 0.4475 -0.0218 0.0184  -0.0325 221 LEU E CB    
6797  C CG    . LEU E 220 ? 0.4875 0.4447 0.4562 -0.0238 0.0204  -0.0315 221 LEU E CG    
6798  C CD1   . LEU E 220 ? 0.5645 0.5179 0.5310 -0.0228 0.0203  -0.0317 221 LEU E CD1   
6799  C CD2   . LEU E 220 ? 0.4943 0.4555 0.4653 -0.0256 0.0231  -0.0314 221 LEU E CD2   
6800  N N     . PRO E 221 ? 0.4967 0.4539 0.4649 -0.0229 0.0149  -0.0311 222 PRO E N     
6801  C CA    . PRO E 221 ? 0.4917 0.4444 0.4548 -0.0240 0.0142  -0.0301 222 PRO E CA    
6802  C C     . PRO E 221 ? 0.4993 0.4471 0.4574 -0.0253 0.0158  -0.0291 222 PRO E C     
6803  O O     . PRO E 221 ? 0.4932 0.4389 0.4504 -0.0246 0.0161  -0.0290 222 PRO E O     
6804  C CB    . PRO E 221 ? 0.5145 0.4647 0.4762 -0.0221 0.0107  -0.0302 222 PRO E CB    
6805  C CG    . PRO E 221 ? 0.5447 0.4960 0.5092 -0.0198 0.0098  -0.0311 222 PRO E CG    
6806  C CD    . PRO E 221 ? 0.5097 0.4673 0.4797 -0.0203 0.0123  -0.0320 222 PRO E CD    
6807  N N     . LEU E 222 ? 0.4631 0.4094 0.4182 -0.0271 0.0169  -0.0283 223 LEU E N     
6808  C CA    . LEU E 222 ? 0.4936 0.4362 0.4443 -0.0286 0.0188  -0.0274 223 LEU E CA    
6809  C C     . LEU E 222 ? 0.5010 0.4382 0.4475 -0.0278 0.0174  -0.0266 223 LEU E C     
6810  O O     . LEU E 222 ? 0.5235 0.4582 0.4677 -0.0288 0.0188  -0.0260 223 LEU E O     
6811  C CB    . LEU E 222 ? 0.4968 0.4384 0.4443 -0.0301 0.0194  -0.0270 223 LEU E CB    
6812  C CG    . LEU E 222 ? 0.5305 0.4692 0.4736 -0.0318 0.0215  -0.0262 223 LEU E CG    
6813  C CD1   . LEU E 222 ? 0.5316 0.4732 0.4777 -0.0328 0.0242  -0.0265 223 LEU E CD1   
6814  C CD2   . LEU E 222 ? 0.5423 0.4799 0.4819 -0.0328 0.0217  -0.0260 223 LEU E CD2   
6815  N N     . ALA E 223 ? 0.5258 0.4610 0.4711 -0.0262 0.0144  -0.0266 224 ALA E N     
6816  C CA    . ALA E 223 ? 0.5298 0.4589 0.4702 -0.0255 0.0125  -0.0257 224 ALA E CA    
6817  C C     . ALA E 223 ? 0.5406 0.4688 0.4826 -0.0243 0.0123  -0.0260 224 ALA E C     
6818  O O     . ALA E 223 ? 0.4949 0.4174 0.4326 -0.0244 0.0115  -0.0251 224 ALA E O     
6819  C CB    . ALA E 223 ? 0.5770 0.5046 0.5162 -0.0238 0.0091  -0.0258 224 ALA E CB    
6820  N N     . ASN E 224 ? 0.5173 0.4508 0.4653 -0.0233 0.0131  -0.0275 225 ASN E N     
6821  C CA    . ASN E 224 ? 0.5126 0.4458 0.4626 -0.0217 0.0126  -0.0283 225 ASN E CA    
6822  C C     . ASN E 224 ? 0.4965 0.4301 0.4467 -0.0233 0.0155  -0.0281 225 ASN E C     
6823  O O     . ASN E 224 ? 0.5432 0.4763 0.4946 -0.0223 0.0155  -0.0288 225 ASN E O     
6824  C CB    . ASN E 224 ? 0.5300 0.4690 0.4861 -0.0194 0.0117  -0.0301 225 ASN E CB    
6825  C CG    . ASN E 224 ? 0.5526 0.4909 0.5088 -0.0174 0.0083  -0.0304 225 ASN E CG    
6826  O OD1   . ASN E 224 ? 0.6254 0.5585 0.5766 -0.0176 0.0066  -0.0292 225 ASN E OD1   
6827  N ND2   . ASN E 224 ? 0.6259 0.5697 0.5877 -0.0154 0.0074  -0.0320 225 ASN E ND2   
6828  N N     . LEU E 225 ? 0.4397 0.3741 0.3886 -0.0258 0.0179  -0.0274 226 LEU E N     
6829  C CA    . LEU E 225 ? 0.4273 0.3628 0.3768 -0.0275 0.0206  -0.0273 226 LEU E CA    
6830  C C     . LEU E 225 ? 0.4335 0.3636 0.3798 -0.0276 0.0202  -0.0267 226 LEU E C     
6831  O O     . LEU E 225 ? 0.4547 0.3857 0.4029 -0.0274 0.0211  -0.0275 226 LEU E O     
6832  C CB    . LEU E 225 ? 0.4280 0.3641 0.3757 -0.0299 0.0228  -0.0265 226 LEU E CB    
6833  C CG    . LEU E 225 ? 0.3931 0.3303 0.3413 -0.0317 0.0255  -0.0264 226 LEU E CG    
6834  C CD1   . LEU E 225 ? 0.3995 0.3421 0.3530 -0.0311 0.0267  -0.0277 226 LEU E CD1   
6835  C CD2   . LEU E 225 ? 0.3909 0.3280 0.3366 -0.0338 0.0272  -0.0257 226 LEU E CD2   
6836  N N     . PRO E 226 ? 0.4438 0.3679 0.3847 -0.0281 0.0187  -0.0254 227 PRO E N     
6837  C CA    . PRO E 226 ? 0.4815 0.3998 0.4187 -0.0288 0.0182  -0.0245 227 PRO E CA    
6838  C C     . PRO E 226 ? 0.4938 0.4110 0.4332 -0.0263 0.0164  -0.0257 227 PRO E C     
6839  O O     . PRO E 226 ? 0.5588 0.4724 0.4966 -0.0269 0.0164  -0.0254 227 PRO E O     
6840  C CB    . PRO E 226 ? 0.4683 0.3808 0.3995 -0.0294 0.0164  -0.0227 227 PRO E CB    
6841  C CG    . PRO E 226 ? 0.4566 0.3724 0.3878 -0.0301 0.0173  -0.0226 227 PRO E CG    
6842  C CD    . PRO E 226 ? 0.4504 0.3728 0.3881 -0.0283 0.0174  -0.0245 227 PRO E CD    
6843  N N     . GLN E 227 ? 0.5432 0.4636 0.4863 -0.0236 0.0147  -0.0271 228 GLN E N     
6844  C CA    . GLN E 227 ? 0.5819 0.5016 0.5271 -0.0208 0.0128  -0.0286 228 GLN E CA    
6845  C C     . GLN E 227 ? 0.5709 0.4976 0.5219 -0.0199 0.0147  -0.0305 228 GLN E C     
6846  O O     . GLN E 227 ? 0.5811 0.5090 0.5348 -0.0174 0.0136  -0.0322 228 GLN E O     
6847  C CB    . GLN E 227 ? 0.6435 0.5624 0.5890 -0.0180 0.0095  -0.0291 228 GLN E CB    
6848  C CG    . GLN E 227 ? 0.7145 0.6255 0.6537 -0.0182 0.0068  -0.0274 228 GLN E CG    
6849  C CD    . GLN E 227 ? 0.7285 0.6385 0.6640 -0.0209 0.0079  -0.0255 228 GLN E CD    
6850  O OE1   . GLN E 227 ? 0.7646 0.6788 0.7020 -0.0208 0.0082  -0.0258 228 GLN E OE1   
6851  N NE2   . GLN E 227 ? 0.7952 0.6996 0.7251 -0.0234 0.0085  -0.0236 228 GLN E NE2   
6852  N N     . ALA E 228 ? 0.5117 0.4429 0.4645 -0.0220 0.0176  -0.0302 229 ALA E N     
6853  C CA    . ALA E 228 ? 0.4940 0.4319 0.4519 -0.0216 0.0195  -0.0317 229 ALA E CA    
6854  C C     . ALA E 228 ? 0.4835 0.4201 0.4411 -0.0222 0.0208  -0.0321 229 ALA E C     
6855  O O     . ALA E 228 ? 0.4780 0.4095 0.4318 -0.0239 0.0209  -0.0310 229 ALA E O     
6856  C CB    . ALA E 228 ? 0.5048 0.4471 0.4642 -0.0236 0.0216  -0.0311 229 ALA E CB    
6857  N N     . HIS E 229 ? 0.4708 0.4123 0.4325 -0.0209 0.0216  -0.0338 230 HIS E N     
6858  C CA    . HIS E 229 ? 0.4727 0.4138 0.4345 -0.0213 0.0228  -0.0345 230 HIS E CA    
6859  C C     . HIS E 229 ? 0.4418 0.3863 0.4046 -0.0239 0.0257  -0.0339 230 HIS E C     
6860  O O     . HIS E 229 ? 0.4816 0.4320 0.4478 -0.0239 0.0270  -0.0344 230 HIS E O     
6861  C CB    . HIS E 229 ? 0.5619 0.5064 0.5272 -0.0184 0.0222  -0.0368 230 HIS E CB    
6862  C CG    . HIS E 229 ? 0.6023 0.5466 0.5677 -0.0185 0.0233  -0.0378 230 HIS E CG    
6863  N ND1   . HIS E 229 ? 0.6216 0.5596 0.5840 -0.0181 0.0218  -0.0381 230 HIS E ND1   
6864  C CD2   . HIS E 229 ? 0.5714 0.5205 0.5391 -0.0192 0.0255  -0.0386 230 HIS E CD2   
6865  C CE1   . HIS E 229 ? 0.6120 0.5514 0.5753 -0.0184 0.0231  -0.0392 230 HIS E CE1   
6866  N NE2   . HIS E 229 ? 0.5594 0.5055 0.5258 -0.0190 0.0253  -0.0395 230 HIS E NE2   
6867  N N     . LEU E 230 ? 0.4146 0.3554 0.3744 -0.0262 0.0266  -0.0328 231 LEU E N     
6868  C CA    . LEU E 230 ? 0.4028 0.3463 0.3632 -0.0285 0.0290  -0.0322 231 LEU E CA    
6869  C C     . LEU E 230 ? 0.4680 0.4113 0.4287 -0.0291 0.0300  -0.0329 231 LEU E C     
6870  O O     . LEU E 230 ? 0.4984 0.4372 0.4572 -0.0287 0.0288  -0.0331 231 LEU E O     
6871  C CB    . LEU E 230 ? 0.3936 0.3340 0.3507 -0.0308 0.0295  -0.0304 231 LEU E CB    
6872  C CG    . LEU E 230 ? 0.3844 0.3250 0.3407 -0.0305 0.0286  -0.0297 231 LEU E CG    
6873  C CD1   . LEU E 230 ? 0.4011 0.3391 0.3539 -0.0328 0.0294  -0.0281 231 LEU E CD1   
6874  C CD2   . LEU E 230 ? 0.3697 0.3164 0.3299 -0.0300 0.0294  -0.0304 231 LEU E CD2   
6875  N N     . MET E 231 ? 0.4325 0.3804 0.3956 -0.0300 0.0319  -0.0332 232 MET E N     
6876  C CA    . MET E 231 ? 0.4624 0.4105 0.4258 -0.0307 0.0329  -0.0339 232 MET E CA    
6877  C C     . MET E 231 ? 0.4465 0.3958 0.4097 -0.0333 0.0347  -0.0329 232 MET E C     
6878  O O     . MET E 231 ? 0.3921 0.3431 0.3556 -0.0341 0.0354  -0.0320 232 MET E O     
6879  C CB    . MET E 231 ? 0.5305 0.4833 0.4970 -0.0291 0.0334  -0.0355 232 MET E CB    
6880  C CG    . MET E 231 ? 0.6172 0.5694 0.5842 -0.0263 0.0317  -0.0369 232 MET E CG    
6881  S SD    . MET E 231 ? 0.7945 0.7396 0.7584 -0.0257 0.0298  -0.0375 232 MET E SD    
6882  C CE    . MET E 231 ? 0.8661 0.8119 0.8301 -0.0275 0.0314  -0.0379 232 MET E CE    
6883  N N     . PRO E 232 ? 0.4476 0.3960 0.4105 -0.0346 0.0355  -0.0331 233 PRO E N     
6884  C CA    . PRO E 232 ? 0.4439 0.3937 0.4069 -0.0369 0.0371  -0.0323 233 PRO E CA    
6885  C C     . PRO E 232 ? 0.4725 0.4273 0.4380 -0.0369 0.0382  -0.0323 233 PRO E C     
6886  O O     . PRO E 232 ? 0.4960 0.4517 0.4614 -0.0383 0.0392  -0.0316 233 PRO E O     
6887  C CB    . PRO E 232 ? 0.4257 0.3748 0.3889 -0.0375 0.0373  -0.0331 233 PRO E CB    
6888  C CG    . PRO E 232 ? 0.4436 0.3884 0.4052 -0.0363 0.0355  -0.0337 233 PRO E CG    
6889  C CD    . PRO E 232 ? 0.4473 0.3932 0.4096 -0.0338 0.0346  -0.0342 233 PRO E CD    
6890  N N     . ILE E 233 ? 0.4318 0.3898 0.3994 -0.0353 0.0381  -0.0332 234 ILE E N     
6891  C CA    . ILE E 233 ? 0.4567 0.4192 0.4265 -0.0355 0.0391  -0.0331 234 ILE E CA    
6892  C C     . ILE E 233 ? 0.4604 0.4240 0.4307 -0.0350 0.0386  -0.0325 234 ILE E C     
6893  O O     . ILE E 233 ? 0.5212 0.4882 0.4933 -0.0351 0.0391  -0.0324 234 ILE E O     
6894  C CB    . ILE E 233 ? 0.4842 0.4500 0.4558 -0.0344 0.0394  -0.0342 234 ILE E CB    
6895  C CG1   . ILE E 233 ? 0.4649 0.4312 0.4370 -0.0323 0.0384  -0.0351 234 ILE E CG1   
6896  C CG2   . ILE E 233 ? 0.5187 0.4834 0.4897 -0.0350 0.0397  -0.0348 234 ILE E CG2   
6897  C CD1   . ILE E 233 ? 0.4808 0.4511 0.4547 -0.0312 0.0389  -0.0362 234 ILE E CD1   
6898  N N     . SER E 234 ? 0.4321 0.3924 0.4005 -0.0346 0.0375  -0.0321 235 SER E N     
6899  C CA    . SER E 234 ? 0.4275 0.3884 0.3962 -0.0340 0.0368  -0.0317 235 SER E CA    
6900  C C     . SER E 234 ? 0.4006 0.3615 0.3685 -0.0355 0.0374  -0.0308 235 SER E C     
6901  O O     . SER E 234 ? 0.3776 0.3362 0.3436 -0.0368 0.0380  -0.0303 235 SER E O     
6902  C CB    . SER E 234 ? 0.4283 0.3856 0.3951 -0.0328 0.0351  -0.0316 235 SER E CB    
6903  O OG    . SER E 234 ? 0.4050 0.3630 0.3731 -0.0309 0.0342  -0.0328 235 SER E OG    
6904  N N     . THR E 235 ? 0.4389 0.4025 0.4085 -0.0354 0.0373  -0.0306 236 THR E N     
6905  C CA    . THR E 235 ? 0.4200 0.3835 0.3889 -0.0364 0.0376  -0.0300 236 THR E CA    
6906  C C     . THR E 235 ? 0.3765 0.3396 0.3451 -0.0357 0.0362  -0.0298 236 THR E C     
6907  O O     . THR E 235 ? 0.3533 0.3185 0.3240 -0.0346 0.0353  -0.0301 236 THR E O     
6908  C CB    . THR E 235 ? 0.5006 0.4674 0.4717 -0.0372 0.0385  -0.0301 236 THR E CB    
6909  O OG1   . THR E 235 ? 0.5039 0.4707 0.4750 -0.0378 0.0395  -0.0303 236 THR E OG1   
6910  C CG2   . THR E 235 ? 0.4956 0.4620 0.4660 -0.0380 0.0386  -0.0297 236 THR E CG2   
6911  N N     . LEU E 236 ? 0.3585 0.3191 0.3246 -0.0363 0.0359  -0.0293 237 LEU E N     
6912  C CA    . LEU E 236 ? 0.3390 0.2987 0.3042 -0.0356 0.0343  -0.0291 237 LEU E CA    
6913  C C     . LEU E 236 ? 0.3595 0.3211 0.3258 -0.0362 0.0344  -0.0290 237 LEU E C     
6914  O O     . LEU E 236 ? 0.3201 0.2809 0.2849 -0.0372 0.0352  -0.0290 237 LEU E O     
6915  C CB    . LEU E 236 ? 0.3489 0.3043 0.3100 -0.0357 0.0338  -0.0285 237 LEU E CB    
6916  C CG    . LEU E 236 ? 0.3670 0.3209 0.3265 -0.0351 0.0320  -0.0283 237 LEU E CG    
6917  C CD1   . LEU E 236 ? 0.3624 0.3174 0.3241 -0.0334 0.0303  -0.0287 237 LEU E CD1   
6918  C CD2   . LEU E 236 ? 0.4098 0.3591 0.3644 -0.0356 0.0317  -0.0275 237 LEU E CD2   
6919  N N     . LEU E 237 ? 0.3784 0.3425 0.3473 -0.0356 0.0333  -0.0292 238 LEU E N     
6920  C CA    . LEU E 237 ? 0.3686 0.3340 0.3385 -0.0363 0.0329  -0.0292 238 LEU E CA    
6921  C C     . LEU E 237 ? 0.3621 0.3257 0.3304 -0.0357 0.0311  -0.0291 238 LEU E C     
6922  O O     . LEU E 237 ? 0.3689 0.3329 0.3380 -0.0347 0.0298  -0.0292 238 LEU E O     
6923  C CB    . LEU E 237 ? 0.3653 0.3348 0.3392 -0.0364 0.0329  -0.0292 238 LEU E CB    
6924  C CG    . LEU E 237 ? 0.3728 0.3434 0.3480 -0.0372 0.0319  -0.0291 238 LEU E CG    
6925  C CD1   . LEU E 237 ? 0.4076 0.3772 0.3819 -0.0381 0.0326  -0.0290 238 LEU E CD1   
6926  C CD2   . LEU E 237 ? 0.3529 0.3276 0.3320 -0.0374 0.0317  -0.0289 238 LEU E CD2   
6927  N N     . ILE E 238 ? 0.4106 0.3723 0.3764 -0.0363 0.0310  -0.0291 239 ILE E N     
6928  C CA    . ILE E 238 ? 0.3733 0.3331 0.3371 -0.0359 0.0293  -0.0292 239 ILE E CA    
6929  C C     . ILE E 238 ? 0.3846 0.3460 0.3502 -0.0364 0.0284  -0.0295 239 ILE E C     
6930  O O     . ILE E 238 ? 0.3843 0.3448 0.3487 -0.0370 0.0290  -0.0298 239 ILE E O     
6931  C CB    . ILE E 238 ? 0.3808 0.3369 0.3397 -0.0361 0.0297  -0.0290 239 ILE E CB    
6932  C CG1   . ILE E 238 ? 0.3737 0.3280 0.3309 -0.0359 0.0304  -0.0285 239 ILE E CG1   
6933  C CG2   . ILE E 238 ? 0.3906 0.3447 0.3470 -0.0356 0.0278  -0.0290 239 ILE E CG2   
6934  C CD1   . ILE E 238 ? 0.4010 0.3519 0.3533 -0.0365 0.0310  -0.0280 239 ILE E CD1   
6935  N N     . PRO E 239 ? 0.3712 0.3348 0.3399 -0.0362 0.0269  -0.0295 240 PRO E N     
6936  C CA    . PRO E 239 ? 0.3621 0.3270 0.3327 -0.0369 0.0259  -0.0296 240 PRO E CA    
6937  C C     . PRO E 239 ? 0.3399 0.3018 0.3073 -0.0368 0.0245  -0.0301 240 PRO E C     
6938  O O     . PRO E 239 ? 0.3592 0.3185 0.3231 -0.0361 0.0241  -0.0301 240 PRO E O     
6939  C CB    . PRO E 239 ? 0.3452 0.3133 0.3196 -0.0367 0.0246  -0.0295 240 PRO E CB    
6940  C CG    . PRO E 239 ? 0.3593 0.3286 0.3345 -0.0357 0.0256  -0.0295 240 PRO E CG    
6941  C CD    . PRO E 239 ? 0.3579 0.3232 0.3286 -0.0352 0.0262  -0.0294 240 PRO E CD    
6942  N N     . PRO E 240 ? 0.3085 0.2705 0.2768 -0.0376 0.0237  -0.0304 241 PRO E N     
6943  C CA    . PRO E 240 ? 0.3304 0.2896 0.2955 -0.0374 0.0223  -0.0311 241 PRO E CA    
6944  C C     . PRO E 240 ? 0.3452 0.3031 0.3086 -0.0365 0.0203  -0.0311 241 PRO E C     
6945  O O     . PRO E 240 ? 0.3840 0.3440 0.3503 -0.0363 0.0192  -0.0308 241 PRO E O     
6946  C CB    . PRO E 240 ? 0.3204 0.2804 0.2881 -0.0383 0.0210  -0.0314 241 PRO E CB    
6947  C CG    . PRO E 240 ? 0.3253 0.2877 0.2961 -0.0392 0.0227  -0.0307 241 PRO E CG    
6948  C CD    . PRO E 240 ? 0.3234 0.2879 0.2954 -0.0387 0.0239  -0.0301 241 PRO E CD    
6949  N N     . ALA E 241 ? 0.3926 0.3473 0.3513 -0.0360 0.0200  -0.0316 242 ALA E N     
6950  C CA    . ALA E 241 ? 0.4141 0.3669 0.3702 -0.0352 0.0179  -0.0316 242 ALA E CA    
6951  C C     . ALA E 241 ? 0.4785 0.4304 0.4342 -0.0353 0.0157  -0.0325 242 ALA E C     
6952  O O     . ALA E 241 ? 0.5207 0.4717 0.4754 -0.0348 0.0133  -0.0327 242 ALA E O     
6953  C CB    . ALA E 241 ? 0.4149 0.3646 0.3657 -0.0346 0.0188  -0.0314 242 ALA E CB    
6954  N N     . LYS E 242 ? 0.5351 0.4870 0.4915 -0.0360 0.0162  -0.0331 243 LYS E N     
6955  C CA    . LYS E 242 ? 0.5895 0.5402 0.5455 -0.0362 0.0140  -0.0341 243 LYS E CA    
6956  C C     . LYS E 242 ? 0.5711 0.5236 0.5314 -0.0374 0.0139  -0.0341 243 LYS E C     
6957  O O     . LYS E 242 ? 0.5958 0.5497 0.5580 -0.0379 0.0160  -0.0336 243 LYS E O     
6958  C CB    . LYS E 242 ? 0.6349 0.5824 0.5857 -0.0357 0.0145  -0.0353 243 LYS E CB    
6959  C CG    . LYS E 242 ? 0.6858 0.6307 0.6314 -0.0348 0.0134  -0.0356 243 LYS E CG    
6960  C CD    . LYS E 242 ? 0.7116 0.6540 0.6523 -0.0343 0.0136  -0.0370 243 LYS E CD    
6961  C CE    . LYS E 242 ? 0.7303 0.6735 0.6715 -0.0344 0.0160  -0.0377 243 LYS E CE    
6962  N NZ    . LYS E 242 ? 0.7451 0.6884 0.6893 -0.0347 0.0147  -0.0386 243 LYS E NZ    
6963  N N     . LYS E 243 ? 0.5757 0.5278 0.5375 -0.0380 0.0114  -0.0346 244 LYS E N     
6964  C CA    . LYS E 243 ? 0.6368 0.5895 0.6019 -0.0393 0.0108  -0.0346 244 LYS E CA    
6965  C C     . LYS E 243 ? 0.5228 0.4723 0.4848 -0.0388 0.0107  -0.0359 244 LYS E C     
6966  O O     . LYS E 243 ? 0.6282 0.5753 0.5857 -0.0376 0.0105  -0.0370 244 LYS E O     
6967  C CB    . LYS E 243 ? 0.7192 0.6733 0.6879 -0.0405 0.0081  -0.0343 244 LYS E CB    
6968  C CG    . LYS E 243 ? 0.7993 0.7538 0.7675 -0.0398 0.0062  -0.0344 244 LYS E CG    
6969  C CD    . LYS E 243 ? 0.8302 0.7854 0.8014 -0.0409 0.0030  -0.0346 244 LYS E CD    
6970  C CE    . LYS E 243 ? 0.8645 0.8200 0.8388 -0.0429 0.0026  -0.0343 244 LYS E CE    
6971  N NZ    . LYS E 243 ? 0.8859 0.8369 0.8569 -0.0427 0.0013  -0.0356 244 LYS E NZ    
6972  N N     . LEU E 244 ? 0.5080 0.4575 0.4723 -0.0397 0.0107  -0.0359 245 LEU E N     
6973  C CA    . LEU E 244 ? 0.5193 0.4659 0.4813 -0.0391 0.0105  -0.0373 245 LEU E CA    
6974  C C     . LEU E 244 ? 0.5382 0.4817 0.4978 -0.0387 0.0076  -0.0388 245 LEU E C     
6975  O O     . LEU E 244 ? 0.5804 0.5237 0.5423 -0.0399 0.0051  -0.0385 245 LEU E O     
6976  C CB    . LEU E 244 ? 0.4600 0.4070 0.4252 -0.0403 0.0107  -0.0366 245 LEU E CB    
6977  C CG    . LEU E 244 ? 0.4446 0.3945 0.4117 -0.0406 0.0135  -0.0353 245 LEU E CG    
6978  C CD1   . LEU E 244 ? 0.4383 0.3883 0.4083 -0.0419 0.0132  -0.0345 245 LEU E CD1   
6979  C CD2   . LEU E 244 ? 0.4257 0.3752 0.3896 -0.0390 0.0159  -0.0362 245 LEU E CD2   
6980  N N     . GLU E 245 ? 0.5737 0.5149 0.5287 -0.0371 0.0080  -0.0405 246 GLU E N     
6981  C CA    . GLU E 245 ? 0.6051 0.5431 0.5571 -0.0364 0.0054  -0.0423 246 GLU E CA    
6982  C C     . GLU E 245 ? 0.5772 0.5128 0.5286 -0.0358 0.0049  -0.0439 246 GLU E C     
6983  O O     . GLU E 245 ? 0.5278 0.4642 0.4793 -0.0352 0.0072  -0.0440 246 GLU E O     
6984  C CB    . GLU E 245 ? 0.6611 0.5982 0.6079 -0.0350 0.0060  -0.0432 246 GLU E CB    
6985  C CG    . GLU E 245 ? 0.7171 0.6557 0.6641 -0.0353 0.0058  -0.0417 246 GLU E CG    
6986  C CD    . GLU E 245 ? 0.7677 0.7049 0.7091 -0.0341 0.0062  -0.0423 246 GLU E CD    
6987  O OE1   . GLU E 245 ? 0.8229 0.7575 0.7607 -0.0334 0.0041  -0.0439 246 GLU E OE1   
6988  O OE2   . GLU E 245 ? 0.8007 0.7392 0.7408 -0.0339 0.0083  -0.0412 246 GLU E OE2   
6989  N N     . TYR E 246 ? 0.5958 0.5283 0.5464 -0.0357 0.0018  -0.0453 247 TYR E N     
6990  C CA    . TYR E 246 ? 0.5689 0.4985 0.5192 -0.0351 0.0006  -0.0470 247 TYR E CA    
6991  C C     . TYR E 246 ? 0.5458 0.4744 0.4914 -0.0327 0.0021  -0.0493 247 TYR E C     
6992  O O     . TYR E 246 ? 0.5560 0.4845 0.4976 -0.0317 0.0024  -0.0502 247 TYR E O     
6993  C CB    . TYR E 246 ? 0.5579 0.4841 0.5088 -0.0359 -0.0035 -0.0477 247 TYR E CB    
6994  C CG    . TYR E 246 ? 0.5288 0.4561 0.4848 -0.0386 -0.0050 -0.0454 247 TYR E CG    
6995  C CD1   . TYR E 246 ? 0.5188 0.4460 0.4780 -0.0397 -0.0047 -0.0443 247 TYR E CD1   
6996  C CD2   . TYR E 246 ? 0.5259 0.4544 0.4835 -0.0400 -0.0067 -0.0445 247 TYR E CD2   
6997  C CE1   . TYR E 246 ? 0.5408 0.4694 0.5045 -0.0424 -0.0059 -0.0421 247 TYR E CE1   
6998  C CE2   . TYR E 246 ? 0.5372 0.4674 0.4997 -0.0425 -0.0078 -0.0424 247 TYR E CE2   
6999  C CZ    . TYR E 246 ? 0.5425 0.4728 0.5079 -0.0439 -0.0073 -0.0412 247 TYR E CZ    
7000  O OH    . TYR E 246 ? 0.5200 0.4522 0.4899 -0.0467 -0.0082 -0.0391 247 TYR E OH    
7001  N N     . ASN E 247 ? 0.5600 0.4882 0.5060 -0.0317 0.0030  -0.0504 248 ASN E N     
7002  C CA    . ASN E 247 ? 0.5682 0.4960 0.5105 -0.0294 0.0045  -0.0530 248 ASN E CA    
7003  C C     . ASN E 247 ? 0.5422 0.4659 0.4829 -0.0281 0.0013  -0.0556 248 ASN E C     
7004  O O     . ASN E 247 ? 0.4978 0.4200 0.4403 -0.0275 0.0005  -0.0565 248 ASN E O     
7005  C CB    . ASN E 247 ? 0.5785 0.5091 0.5225 -0.0289 0.0075  -0.0527 248 ASN E CB    
7006  C CG    . ASN E 247 ? 0.6207 0.5523 0.5611 -0.0267 0.0097  -0.0551 248 ASN E CG    
7007  O OD1   . ASN E 247 ? 0.6676 0.5978 0.6038 -0.0255 0.0090  -0.0570 248 ASN E OD1   
7008  N ND2   . ASN E 247 ? 0.7246 0.6588 0.6665 -0.0262 0.0123  -0.0551 248 ASN E ND2   
7009  N N     . TYR E 248 ? 0.5514 0.4729 0.4886 -0.0275 -0.0007 -0.0570 249 TYR E N     
7010  C CA    . TYR E 248 ? 0.5778 0.4950 0.5134 -0.0264 -0.0042 -0.0596 249 TYR E CA    
7011  C C     . TYR E 248 ? 0.5698 0.4865 0.5032 -0.0237 -0.0031 -0.0627 249 TYR E C     
7012  O O     . TYR E 248 ? 0.5361 0.4494 0.4701 -0.0227 -0.0056 -0.0645 249 TYR E O     
7013  C CB    . TYR E 248 ? 0.6125 0.5279 0.5443 -0.0263 -0.0063 -0.0605 249 TYR E CB    
7014  C CG    . TYR E 248 ? 0.6450 0.5610 0.5795 -0.0288 -0.0079 -0.0579 249 TYR E CG    
7015  C CD1   . TYR E 248 ? 0.6685 0.5821 0.6065 -0.0306 -0.0112 -0.0571 249 TYR E CD1   
7016  C CD2   . TYR E 248 ? 0.6850 0.6038 0.6183 -0.0293 -0.0061 -0.0563 249 TYR E CD2   
7017  C CE1   . TYR E 248 ? 0.6758 0.5907 0.6167 -0.0328 -0.0126 -0.0549 249 TYR E CE1   
7018  C CE2   . TYR E 248 ? 0.6755 0.5952 0.6116 -0.0313 -0.0076 -0.0541 249 TYR E CE2   
7019  C CZ    . TYR E 248 ? 0.7056 0.6237 0.6456 -0.0330 -0.0108 -0.0535 249 TYR E CZ    
7020  O OH    . TYR E 248 ? 0.6713 0.5911 0.6144 -0.0350 -0.0122 -0.0515 249 TYR E OH    
7021  N N     . ALA E 249 ? 0.5712 0.4913 0.5019 -0.0225 0.0005  -0.0632 250 ALA E N     
7022  C CA    . ALA E 249 ? 0.5518 0.4726 0.4805 -0.0198 0.0020  -0.0663 250 ALA E CA    
7023  C C     . ALA E 249 ? 0.5157 0.4356 0.4485 -0.0193 0.0012  -0.0667 250 ALA E C     
7024  O O     . ALA E 249 ? 0.5679 0.4850 0.4999 -0.0172 -0.0008 -0.0696 250 ALA E O     
7025  C CB    . ALA E 249 ? 0.5801 0.5057 0.5069 -0.0195 0.0065  -0.0659 250 ALA E CB    
7026  N N     . ILE E 250 ? 0.5307 0.4527 0.4676 -0.0211 0.0026  -0.0637 251 ILE E N     
7027  C CA    . ILE E 250 ? 0.5242 0.4456 0.4648 -0.0208 0.0021  -0.0637 251 ILE E CA    
7028  C C     . ILE E 250 ? 0.5046 0.4209 0.4471 -0.0218 -0.0023 -0.0633 251 ILE E C     
7029  O O     . ILE E 250 ? 0.4761 0.3894 0.4194 -0.0204 -0.0043 -0.0650 251 ILE E O     
7030  C CB    . ILE E 250 ? 0.5446 0.4700 0.4886 -0.0225 0.0051  -0.0607 251 ILE E CB    
7031  C CG1   . ILE E 250 ? 0.5850 0.5153 0.5272 -0.0218 0.0093  -0.0610 251 ILE E CG1   
7032  C CG2   . ILE E 250 ? 0.5598 0.4844 0.5074 -0.0222 0.0044  -0.0605 251 ILE E CG2   
7033  C CD1   . ILE E 250 ? 0.6191 0.5507 0.5596 -0.0189 0.0107  -0.0644 251 ILE E CD1   
7034  N N     . LEU E 251 ? 0.5321 0.4474 0.4754 -0.0243 -0.0038 -0.0611 252 LEU E N     
7035  C CA    . LEU E 251 ? 0.5577 0.4685 0.5029 -0.0259 -0.0079 -0.0603 252 LEU E CA    
7036  C C     . LEU E 251 ? 0.5411 0.4469 0.4835 -0.0236 -0.0113 -0.0639 252 LEU E C     
7037  O O     . LEU E 251 ? 0.5201 0.4215 0.4639 -0.0238 -0.0144 -0.0643 252 LEU E O     
7038  C CB    . LEU E 251 ? 0.5858 0.4971 0.5318 -0.0285 -0.0089 -0.0580 252 LEU E CB    
7039  C CG    . LEU E 251 ? 0.5902 0.5059 0.5394 -0.0308 -0.0062 -0.0544 252 LEU E CG    
7040  C CD1   . LEU E 251 ? 0.5530 0.4694 0.5032 -0.0331 -0.0075 -0.0526 252 LEU E CD1   
7041  C CD2   . LEU E 251 ? 0.6001 0.5156 0.5531 -0.0321 -0.0063 -0.0526 252 LEU E CD2   
7042  N N     . ALA E 252 ? 0.5269 0.4332 0.4650 -0.0216 -0.0106 -0.0665 253 ALA E N     
7043  C CA    . ALA E 252 ? 0.5377 0.4396 0.4725 -0.0192 -0.0136 -0.0703 253 ALA E CA    
7044  C C     . ALA E 252 ? 0.5564 0.4573 0.4916 -0.0164 -0.0135 -0.0728 253 ALA E C     
7045  O O     . ALA E 252 ? 0.6032 0.4990 0.5380 -0.0152 -0.0172 -0.0750 253 ALA E O     
7046  C CB    . ALA E 252 ? 0.5319 0.4353 0.4617 -0.0177 -0.0123 -0.0723 253 ALA E CB    
7047  N N     . LYS E 253 ? 0.5375 0.4434 0.4737 -0.0155 -0.0095 -0.0725 254 LYS E N     
7048  C CA    . LYS E 253 ? 0.5595 0.4654 0.4968 -0.0129 -0.0092 -0.0748 254 LYS E CA    
7049  C C     . LYS E 253 ? 0.5773 0.4796 0.5186 -0.0143 -0.0119 -0.0729 254 LYS E C     
7050  O O     . LYS E 253 ? 0.5599 0.4588 0.5017 -0.0122 -0.0143 -0.0751 254 LYS E O     
7051  C CB    . LYS E 253 ? 0.5661 0.4786 0.5039 -0.0121 -0.0042 -0.0746 254 LYS E CB    
7052  C CG    . LYS E 253 ? 0.5724 0.4884 0.5059 -0.0102 -0.0015 -0.0772 254 LYS E CG    
7053  C CD    . LYS E 253 ? 0.6006 0.5231 0.5347 -0.0099 0.0034  -0.0766 254 LYS E CD    
7054  C CE    . LYS E 253 ? 0.6125 0.5383 0.5422 -0.0079 0.0060  -0.0795 254 LYS E CE    
7055  N NZ    . LYS E 253 ? 0.6003 0.5249 0.5259 -0.0091 0.0056  -0.0788 254 LYS E NZ    
7056  N N     . LEU E 254 ? 0.5559 0.4590 0.4999 -0.0178 -0.0116 -0.0688 255 LEU E N     
7057  C CA    . LEU E 254 ? 0.5496 0.4495 0.4970 -0.0197 -0.0140 -0.0664 255 LEU E CA    
7058  C C     . LEU E 254 ? 0.5672 0.4604 0.5138 -0.0206 -0.0190 -0.0670 255 LEU E C     
7059  O O     . LEU E 254 ? 0.4940 0.3829 0.4426 -0.0219 -0.0220 -0.0657 255 LEU E O     
7060  C CB    . LEU E 254 ? 0.5167 0.4203 0.4670 -0.0231 -0.0117 -0.0621 255 LEU E CB    
7061  C CG    . LEU E 254 ? 0.4920 0.4015 0.4435 -0.0226 -0.0072 -0.0612 255 LEU E CG    
7062  C CD1   . LEU E 254 ? 0.4624 0.3751 0.4166 -0.0259 -0.0053 -0.0572 255 LEU E CD1   
7063  C CD2   . LEU E 254 ? 0.4901 0.3990 0.4431 -0.0206 -0.0074 -0.0624 255 LEU E CD2   
7064  N N     . GLY E 255 ? 0.5641 0.4563 0.5075 -0.0200 -0.0200 -0.0688 256 GLY E N     
7065  C CA    . GLY E 255 ? 0.5829 0.4688 0.5252 -0.0207 -0.0249 -0.0698 256 GLY E CA    
7066  C C     . GLY E 255 ? 0.6242 0.5093 0.5694 -0.0250 -0.0265 -0.0659 256 GLY E C     
7067  O O     . GLY E 255 ? 0.6396 0.5191 0.5854 -0.0265 -0.0308 -0.0657 256 GLY E O     
7068  N N     . ILE E 256 ? 0.6381 0.5288 0.5852 -0.0271 -0.0231 -0.0628 257 ILE E N     
7069  C CA    . ILE E 256 ? 0.6436 0.5349 0.5938 -0.0312 -0.0240 -0.0591 257 ILE E CA    
7070  C C     . ILE E 256 ? 0.6667 0.5620 0.6161 -0.0321 -0.0222 -0.0584 257 ILE E C     
7071  O O     . ILE E 256 ? 0.6775 0.5744 0.6235 -0.0297 -0.0207 -0.0607 257 ILE E O     
7072  C CB    . ILE E 256 ? 0.6484 0.5423 0.6022 -0.0330 -0.0218 -0.0559 257 ILE E CB    
7073  C CG1   . ILE E 256 ? 0.6335 0.5340 0.5875 -0.0321 -0.0168 -0.0552 257 ILE E CG1   
7074  C CG2   . ILE E 256 ? 0.6931 0.5826 0.6474 -0.0319 -0.0238 -0.0566 257 ILE E CG2   
7075  C CD1   . ILE E 256 ? 0.6369 0.5401 0.5941 -0.0337 -0.0147 -0.0522 257 ILE E CD1   
7076  N N     . GLY E 257 ? 0.7017 0.5987 0.6542 -0.0355 -0.0226 -0.0553 258 GLY E N     
7077  C CA    . GLY E 257 ? 0.6697 0.5707 0.6221 -0.0365 -0.0213 -0.0543 258 GLY E CA    
7078  C C     . GLY E 257 ? 0.6370 0.5420 0.5938 -0.0398 -0.0199 -0.0505 258 GLY E C     
7079  O O     . GLY E 257 ? 0.5804 0.4849 0.5401 -0.0415 -0.0201 -0.0485 258 GLY E O     
7080  N N     . PRO E 258 ? 0.6130 0.5223 0.5704 -0.0406 -0.0184 -0.0493 259 PRO E N     
7081  C CA    . PRO E 258 ? 0.6649 0.5787 0.6265 -0.0433 -0.0168 -0.0460 259 PRO E CA    
7082  C C     . PRO E 258 ? 0.6674 0.5794 0.6327 -0.0466 -0.0195 -0.0441 259 PRO E C     
7083  O O     . PRO E 258 ? 0.6167 0.5311 0.5851 -0.0484 -0.0179 -0.0416 259 PRO E O     
7084  C CB    . PRO E 258 ? 0.6538 0.5704 0.6148 -0.0434 -0.0167 -0.0460 259 PRO E CB    
7085  C CG    . PRO E 258 ? 0.6331 0.5482 0.5888 -0.0401 -0.0160 -0.0489 259 PRO E CG    
7086  C CD    . PRO E 258 ? 0.6391 0.5488 0.5927 -0.0388 -0.0182 -0.0512 259 PRO E CD    
7087  N N     . GLU E 259 ? 0.7387 0.6466 0.7036 -0.0475 -0.0235 -0.0451 260 GLU E N     
7088  C CA    . GLU E 259 ? 0.7764 0.6825 0.7447 -0.0510 -0.0264 -0.0432 260 GLU E CA    
7089  C C     . GLU E 259 ? 0.7061 0.6086 0.6748 -0.0515 -0.0269 -0.0425 260 GLU E C     
7090  O O     . GLU E 259 ? 0.6506 0.5523 0.6222 -0.0548 -0.0284 -0.0401 260 GLU E O     
7091  C CB    . GLU E 259 ? 0.8616 0.7634 0.8289 -0.0517 -0.0309 -0.0448 260 GLU E CB    
7092  C CG    . GLU E 259 ? 1.0099 0.9053 0.9728 -0.0488 -0.0333 -0.0482 260 GLU E CG    
7093  C CD    . GLU E 259 ? 1.1160 1.0125 1.0745 -0.0447 -0.0309 -0.0509 260 GLU E CD    
7094  O OE1   . GLU E 259 ? 1.1410 1.0429 1.0997 -0.0443 -0.0275 -0.0500 260 GLU E OE1   
7095  O OE2   . GLU E 259 ? 1.1671 1.0591 1.1219 -0.0421 -0.0324 -0.0540 260 GLU E OE2   
7096  N N     . ASP E 260 ? 0.6416 0.5421 0.6072 -0.0482 -0.0257 -0.0445 261 ASP E N     
7097  C CA    . ASP E 260 ? 0.6285 0.5252 0.5941 -0.0480 -0.0265 -0.0443 261 ASP E CA    
7098  C C     . ASP E 260 ? 0.6362 0.5375 0.6039 -0.0487 -0.0227 -0.0418 261 ASP E C     
7099  O O     . ASP E 260 ? 0.6296 0.5286 0.5979 -0.0492 -0.0232 -0.0407 261 ASP E O     
7100  C CB    . ASP E 260 ? 0.6630 0.5555 0.6246 -0.0440 -0.0274 -0.0479 261 ASP E CB    
7101  C CG    . ASP E 260 ? 0.6668 0.5537 0.6259 -0.0431 -0.0316 -0.0507 261 ASP E CG    
7102  O OD1   . ASP E 260 ? 0.7063 0.5885 0.6666 -0.0454 -0.0354 -0.0499 261 ASP E OD1   
7103  O OD2   . ASP E 260 ? 0.6922 0.5795 0.6481 -0.0401 -0.0310 -0.0536 261 ASP E OD2   
7104  N N     . LEU E 261 ? 0.6354 0.5429 0.6039 -0.0485 -0.0192 -0.0409 262 LEU E N     
7105  C CA    . LEU E 261 ? 0.6480 0.5602 0.6185 -0.0490 -0.0155 -0.0388 262 LEU E CA    
7106  C C     . LEU E 261 ? 0.6457 0.5585 0.6196 -0.0529 -0.0164 -0.0355 262 LEU E C     
7107  O O     . LEU E 261 ? 0.6797 0.5936 0.6558 -0.0556 -0.0178 -0.0342 262 LEU E O     
7108  C CB    . LEU E 261 ? 0.6505 0.5686 0.6211 -0.0482 -0.0121 -0.0387 262 LEU E CB    
7109  C CG    . LEU E 261 ? 0.6956 0.6135 0.6624 -0.0447 -0.0110 -0.0416 262 LEU E CG    
7110  C CD1   . LEU E 261 ? 0.7055 0.6289 0.6724 -0.0442 -0.0074 -0.0409 262 LEU E CD1   
7111  C CD2   . LEU E 261 ? 0.6798 0.5951 0.6444 -0.0421 -0.0104 -0.0434 262 LEU E CD2   
7112  N N     . GLY E 262 ? 0.6411 0.5533 0.6155 -0.0533 -0.0155 -0.0341 263 GLY E N     
7113  C CA    . GLY E 262 ? 0.6849 0.5977 0.6620 -0.0571 -0.0160 -0.0308 263 GLY E CA    
7114  C C     . GLY E 262 ? 0.7117 0.6318 0.6915 -0.0587 -0.0125 -0.0286 263 GLY E C     
7115  O O     . GLY E 262 ? 0.6197 0.5437 0.5989 -0.0564 -0.0095 -0.0297 263 GLY E O     
7116  O OXT   . GLY E 262 ? 0.7611 0.6829 0.7436 -0.0623 -0.0129 -0.0259 263 GLY E OXT   
7172  N N     . GLN F 8   ? 0.4593 0.5212 0.4670 -0.0377 0.0443  -0.0376 10  GLN F N     
7173  C CA    . GLN F 8   ? 0.4940 0.5617 0.5036 -0.0321 0.0452  -0.0273 10  GLN F CA    
7174  C C     . GLN F 8   ? 0.4651 0.5145 0.4790 -0.0331 0.0453  -0.0216 10  GLN F C     
7175  O O     . GLN F 8   ? 0.5220 0.5690 0.5403 -0.0299 0.0469  -0.0139 10  GLN F O     
7176  C CB    . GLN F 8   ? 0.6106 0.6940 0.6196 -0.0294 0.0464  -0.0269 10  GLN F CB    
7177  C CG    . GLN F 8   ? 0.7580 0.8501 0.7694 -0.0224 0.0488  -0.0145 10  GLN F CG    
7178  C CD    . GLN F 8   ? 0.8805 0.9922 0.8903 -0.0186 0.0500  -0.0139 10  GLN F CD    
7179  O OE1   . GLN F 8   ? 0.9613 1.0942 0.9676 -0.0171 0.0494  -0.0207 10  GLN F OE1   
7180  N NE2   . GLN F 8   ? 0.9308 1.0376 0.9441 -0.0171 0.0519  -0.0068 10  GLN F NE2   
7181  N N     . LEU F 9   ? 0.4178 0.4556 0.4318 -0.0372 0.0442  -0.0258 11  LEU F N     
7182  C CA    . LEU F 9   ? 0.4806 0.5053 0.4991 -0.0383 0.0439  -0.0228 11  LEU F CA    
7183  C C     . LEU F 9   ? 0.5041 0.5207 0.5248 -0.0389 0.0431  -0.0226 11  LEU F C     
7184  O O     . LEU F 9   ? 0.5575 0.5685 0.5851 -0.0382 0.0440  -0.0190 11  LEU F O     
7185  C CB    . LEU F 9   ? 0.5008 0.5183 0.5177 -0.0414 0.0428  -0.0277 11  LEU F CB    
7186  C CG    . LEU F 9   ? 0.4950 0.5027 0.5161 -0.0424 0.0417  -0.0266 11  LEU F CG    
7187  C CD1   . LEU F 9   ? 0.4980 0.5078 0.5260 -0.0408 0.0433  -0.0211 11  LEU F CD1   
7188  C CD2   . LEU F 9   ? 0.4888 0.4919 0.5072 -0.0438 0.0411  -0.0303 11  LEU F CD2   
7189  N N     . GLY F 10  ? 0.5168 0.5331 0.5329 -0.0403 0.0418  -0.0274 12  GLY F N     
7190  C CA    . GLY F 10  ? 0.4865 0.4960 0.5037 -0.0410 0.0408  -0.0284 12  GLY F CA    
7191  C C     . GLY F 10  ? 0.4882 0.5018 0.5091 -0.0376 0.0425  -0.0234 12  GLY F C     
7192  O O     . GLY F 10  ? 0.5488 0.5565 0.5730 -0.0377 0.0424  -0.0238 12  GLY F O     
7193  N N     . GLN F 11  ? 0.4735 0.4987 0.4942 -0.0338 0.0445  -0.0184 13  GLN F N     
7194  C CA    . GLN F 11  ? 0.4937 0.5254 0.5174 -0.0287 0.0471  -0.0117 13  GLN F CA    
7195  C C     . GLN F 11  ? 0.4457 0.4766 0.4782 -0.0248 0.0514  -0.0021 13  GLN F C     
7196  O O     . GLN F 11  ? 0.4623 0.4901 0.5022 -0.0213 0.0552  0.0042  13  GLN F O     
7197  C CB    . GLN F 11  ? 0.5530 0.6033 0.5704 -0.0255 0.0469  -0.0122 13  GLN F CB    
7198  C CG    . GLN F 11  ? 0.5826 0.6346 0.5941 -0.0296 0.0441  -0.0219 13  GLN F CG    
7199  C CD    . GLN F 11  ? 0.6387 0.7121 0.6463 -0.0267 0.0442  -0.0243 13  GLN F CD    
7200  O OE1   . GLN F 11  ? 0.6761 0.7609 0.6841 -0.0209 0.0456  -0.0186 13  GLN F OE1   
7201  N NE2   . GLN F 11  ? 0.7317 0.8121 0.7365 -0.0306 0.0433  -0.0335 13  GLN F NE2   
7202  N N     . ASP F 12  ? 0.4011 0.4343 0.4337 -0.0251 0.0519  -0.0008 14  ASP F N     
7203  C CA    . ASP F 12  ? 0.4103 0.4451 0.4513 -0.0210 0.0569  0.0092  14  ASP F CA    
7204  C C     . ASP F 12  ? 0.3732 0.3925 0.4239 -0.0254 0.0578  0.0073  14  ASP F C     
7205  O O     . ASP F 12  ? 0.4173 0.4335 0.4655 -0.0295 0.0548  0.0016  14  ASP F O     
7206  C CB    . ASP F 12  ? 0.4366 0.4870 0.4724 -0.0178 0.0573  0.0122  14  ASP F CB    
7207  C CG    . ASP F 12  ? 0.4825 0.5375 0.5262 -0.0122 0.0634  0.0244  14  ASP F CG    
7208  O OD1   . ASP F 12  ? 0.4380 0.4819 0.4935 -0.0113 0.0684  0.0307  14  ASP F OD1   
7209  O OD2   . ASP F 12  ? 0.5891 0.6592 0.6282 -0.0087 0.0639  0.0271  14  ASP F OD2   
7210  N N     . ALA F 13  ? 0.3851 0.3962 0.4482 -0.0243 0.0626  0.0117  15  ALA F N     
7211  C CA    . ALA F 13  ? 0.4111 0.4099 0.4866 -0.0289 0.0642  0.0078  15  ALA F CA    
7212  C C     . ALA F 13  ? 0.4496 0.4504 0.5302 -0.0286 0.0670  0.0123  15  ALA F C     
7213  O O     . ALA F 13  ? 0.5057 0.5010 0.5911 -0.0334 0.0654  0.0060  15  ALA F O     
7214  C CB    . ALA F 13  ? 0.4198 0.4104 0.5102 -0.0277 0.0702  0.0106  15  ALA F CB    
7215  N N     . GLN F 14  ? 0.4231 0.4340 0.5027 -0.0223 0.0713  0.0235  16  GLN F N     
7216  C CA    . GLN F 14  ? 0.4460 0.4608 0.5301 -0.0210 0.0747  0.0295  16  GLN F CA    
7217  C C     . GLN F 14  ? 0.3854 0.4029 0.4590 -0.0253 0.0679  0.0207  16  GLN F C     
7218  O O     . GLN F 14  ? 0.3899 0.4019 0.4697 -0.0292 0.0678  0.0173  16  GLN F O     
7219  C CB    . GLN F 14  ? 0.5226 0.5524 0.6043 -0.0119 0.0799  0.0432  16  GLN F CB    
7220  C CG    . GLN F 14  ? 0.5822 0.6172 0.6701 -0.0092 0.0851  0.0517  16  GLN F CG    
7221  C CD    . GLN F 14  ? 0.6694 0.6902 0.7779 -0.0112 0.0932  0.0561  16  GLN F CD    
7222  O OE1   . GLN F 14  ? 0.7450 0.7525 0.8643 -0.0148 0.0951  0.0518  16  GLN F OE1   
7223  N NE2   . GLN F 14  ? 0.7378 0.7623 0.8533 -0.0091 0.0985  0.0639  16  GLN F NE2   
7224  N N     . LEU F 15  ? 0.3467 0.3732 0.4058 -0.0246 0.0629  0.0167  17  LEU F N     
7225  C CA    . LEU F 15  ? 0.3452 0.3739 0.3955 -0.0280 0.0578  0.0088  17  LEU F CA    
7226  C C     . LEU F 15  ? 0.3321 0.3480 0.3838 -0.0340 0.0540  -0.0003 17  LEU F C     
7227  O O     . LEU F 15  ? 0.3075 0.3218 0.3582 -0.0365 0.0520  -0.0043 17  LEU F O     
7228  C CB    . LEU F 15  ? 0.3760 0.4161 0.4141 -0.0266 0.0548  0.0049  17  LEU F CB    
7229  C CG    . LEU F 15  ? 0.3977 0.4396 0.4284 -0.0300 0.0512  -0.0038 17  LEU F CG    
7230  C CD1   . LEU F 15  ? 0.4216 0.4701 0.4539 -0.0284 0.0529  -0.0007 17  LEU F CD1   
7231  C CD2   . LEU F 15  ? 0.3868 0.4394 0.4094 -0.0296 0.0494  -0.0097 17  LEU F CD2   
7232  N N     . MET F 16  ? 0.3556 0.3646 0.4097 -0.0355 0.0533  -0.0034 18  MET F N     
7233  C CA    . MET F 16  ? 0.3876 0.3885 0.4424 -0.0399 0.0496  -0.0121 18  MET F CA    
7234  C C     . MET F 16  ? 0.4026 0.3999 0.4690 -0.0422 0.0512  -0.0134 18  MET F C     
7235  O O     . MET F 16  ? 0.3081 0.3052 0.3724 -0.0445 0.0479  -0.0192 18  MET F O     
7236  C CB    . MET F 16  ? 0.4186 0.4147 0.4756 -0.0405 0.0493  -0.0149 18  MET F CB    
7237  C CG    . MET F 16  ? 0.4616 0.4531 0.5202 -0.0441 0.0459  -0.0239 18  MET F CG    
7238  S SD    . MET F 16  ? 0.5979 0.5913 0.6422 -0.0449 0.0407  -0.0289 18  MET F SD    
7239  C CE    . MET F 16  ? 0.5050 0.4986 0.5406 -0.0440 0.0398  -0.0293 18  MET F CE    
7240  N N     . GLU F 17  ? 0.4159 0.4112 0.4957 -0.0412 0.0571  -0.0078 19  GLU F N     
7241  C CA    . GLU F 17  ? 0.4749 0.4673 0.5692 -0.0441 0.0600  -0.0098 19  GLU F CA    
7242  C C     . GLU F 17  ? 0.4747 0.4724 0.5657 -0.0436 0.0596  -0.0072 19  GLU F C     
7243  O O     . GLU F 17  ? 0.4053 0.4030 0.5033 -0.0466 0.0590  -0.0121 19  GLU F O     
7244  C CB    . GLU F 17  ? 0.5259 0.5135 0.6376 -0.0429 0.0685  -0.0034 19  GLU F CB    
7245  C CG    . GLU F 17  ? 0.5947 0.5759 0.7138 -0.0443 0.0696  -0.0084 19  GLU F CG    
7246  C CD    . GLU F 17  ? 0.6956 0.6752 0.8207 -0.0500 0.0657  -0.0228 19  GLU F CD    
7247  O OE1   . GLU F 17  ? 0.7891 0.7683 0.9296 -0.0536 0.0688  -0.0275 19  GLU F OE1   
7248  O OE2   . GLU F 17  ? 0.7983 0.7794 0.9132 -0.0507 0.0598  -0.0295 19  GLU F OE2   
7249  N N     . ASP F 18  ? 0.5100 0.5143 0.5908 -0.0395 0.0598  -0.0003 20  ASP F N     
7250  C CA    . ASP F 18  ? 0.4832 0.4938 0.5597 -0.0386 0.0593  0.0016  20  ASP F CA    
7251  C C     . ASP F 18  ? 0.3869 0.3970 0.4540 -0.0412 0.0531  -0.0072 20  ASP F C     
7252  O O     . ASP F 18  ? 0.3171 0.3287 0.3860 -0.0424 0.0523  -0.0092 20  ASP F O     
7253  C CB    . ASP F 18  ? 0.5359 0.5570 0.6046 -0.0334 0.0612  0.0095  20  ASP F CB    
7254  C CG    . ASP F 18  ? 0.6321 0.6567 0.7098 -0.0285 0.0685  0.0213  20  ASP F CG    
7255  O OD1   . ASP F 18  ? 0.6931 0.7090 0.7854 -0.0300 0.0732  0.0234  20  ASP F OD1   
7256  O OD2   . ASP F 18  ? 0.7287 0.7660 0.7997 -0.0229 0.0701  0.0281  20  ASP F OD2   
7257  N N     . TYR F 19  ? 0.4157 0.4239 0.4735 -0.0416 0.0495  -0.0116 21  TYR F N     
7258  C CA    . TYR F 19  ? 0.3970 0.4040 0.4465 -0.0429 0.0452  -0.0181 21  TYR F CA    
7259  C C     . TYR F 19  ? 0.4440 0.4489 0.5000 -0.0451 0.0434  -0.0233 21  TYR F C     
7260  O O     . TYR F 19  ? 0.3846 0.3916 0.4381 -0.0449 0.0416  -0.0257 21  TYR F O     
7261  C CB    . TYR F 19  ? 0.4087 0.4138 0.4495 -0.0428 0.0432  -0.0209 21  TYR F CB    
7262  C CG    . TYR F 19  ? 0.3622 0.3648 0.3962 -0.0433 0.0406  -0.0258 21  TYR F CG    
7263  C CD1   . TYR F 19  ? 0.3516 0.3556 0.3797 -0.0426 0.0412  -0.0265 21  TYR F CD1   
7264  C CD2   . TYR F 19  ? 0.3705 0.3704 0.4049 -0.0440 0.0384  -0.0296 21  TYR F CD2   
7265  C CE1   . TYR F 19  ? 0.3551 0.3557 0.3789 -0.0421 0.0407  -0.0292 21  TYR F CE1   
7266  C CE2   . TYR F 19  ? 0.3540 0.3531 0.3823 -0.0428 0.0372  -0.0318 21  TYR F CE2   
7267  C CZ    . TYR F 19  ? 0.3509 0.3492 0.3743 -0.0417 0.0388  -0.0308 21  TYR F CZ    
7268  O OH    . TYR F 19  ? 0.3611 0.3575 0.3804 -0.0396 0.0394  -0.0312 21  TYR F OH    
7269  N N     . LYS F 20  ? 0.5303 0.5325 0.5953 -0.0468 0.0442  -0.0256 22  LYS F N     
7270  C CA    . LYS F 20  ? 0.5609 0.5649 0.6336 -0.0491 0.0424  -0.0331 22  LYS F CA    
7271  C C     . LYS F 20  ? 0.4994 0.5079 0.5799 -0.0499 0.0436  -0.0334 22  LYS F C     
7272  O O     . LYS F 20  ? 0.5347 0.5491 0.6154 -0.0502 0.0406  -0.0392 22  LYS F O     
7273  C CB    . LYS F 20  ? 0.6121 0.6131 0.6971 -0.0513 0.0447  -0.0366 22  LYS F CB    
7274  C CG    . LYS F 20  ? 0.6865 0.6844 0.7648 -0.0506 0.0430  -0.0381 22  LYS F CG    
7275  C CD    . LYS F 20  ? 0.6647 0.6670 0.7335 -0.0500 0.0378  -0.0444 22  LYS F CD    
7276  C CE    . LYS F 20  ? 0.7743 0.7739 0.8378 -0.0494 0.0366  -0.0459 22  LYS F CE    
7277  N NZ    . LYS F 20  ? 0.7550 0.7601 0.8100 -0.0479 0.0326  -0.0506 22  LYS F NZ    
7278  N N     . GLN F 21  ? 0.5089 0.5162 0.5957 -0.0497 0.0483  -0.0265 23  GLN F N     
7279  C CA    . GLN F 21  ? 0.5088 0.5200 0.6048 -0.0508 0.0505  -0.0260 23  GLN F CA    
7280  C C     . GLN F 21  ? 0.4372 0.4532 0.5219 -0.0486 0.0471  -0.0258 23  GLN F C     
7281  O O     . GLN F 21  ? 0.3421 0.3635 0.4308 -0.0494 0.0456  -0.0302 23  GLN F O     
7282  C CB    . GLN F 21  ? 0.6038 0.6132 0.7088 -0.0498 0.0573  -0.0167 23  GLN F CB    
7283  C CG    . GLN F 21  ? 0.6821 0.6860 0.8043 -0.0520 0.0632  -0.0165 23  GLN F CG    
7284  C CD    . GLN F 21  ? 0.8309 0.8362 0.9703 -0.0571 0.0642  -0.0266 23  GLN F CD    
7285  O OE1   . GLN F 21  ? 0.9670 0.9712 1.1132 -0.0600 0.0631  -0.0358 23  GLN F OE1   
7286  N NE2   . GLN F 21  ? 0.8701 0.8798 1.0173 -0.0582 0.0665  -0.0261 23  GLN F NE2   
7287  N N     . ASN F 22  ? 0.3580 0.3729 0.4300 -0.0459 0.0465  -0.0213 24  ASN F N     
7288  C CA    . ASN F 22  ? 0.3544 0.3726 0.4179 -0.0438 0.0450  -0.0208 24  ASN F CA    
7289  C C     . ASN F 22  ? 0.3304 0.3461 0.3813 -0.0421 0.0435  -0.0212 24  ASN F C     
7290  O O     . ASN F 22  ? 0.3434 0.3610 0.3900 -0.0409 0.0452  -0.0182 24  ASN F O     
7291  C CB    . ASN F 22  ? 0.3793 0.4020 0.4462 -0.0427 0.0484  -0.0152 24  ASN F CB    
7292  C CG    . ASN F 22  ? 0.3914 0.4181 0.4540 -0.0412 0.0472  -0.0164 24  ASN F CG    
7293  O OD1   . ASN F 22  ? 0.4598 0.4851 0.5128 -0.0396 0.0455  -0.0186 24  ASN F OD1   
7294  N ND2   . ASN F 22  ? 0.3695 0.4007 0.4402 -0.0417 0.0489  -0.0152 24  ASN F ND2   
7295  N N     . PRO F 23  ? 0.3181 0.3311 0.3639 -0.0418 0.0408  -0.0253 25  PRO F N     
7296  C CA    . PRO F 23  ? 0.3553 0.3647 0.3917 -0.0408 0.0407  -0.0259 25  PRO F CA    
7297  C C     . PRO F 23  ? 0.3652 0.3758 0.3972 -0.0395 0.0428  -0.0253 25  PRO F C     
7298  O O     . PRO F 23  ? 0.3973 0.4088 0.4261 -0.0398 0.0442  -0.0257 25  PRO F O     
7299  C CB    . PRO F 23  ? 0.3404 0.3486 0.3740 -0.0394 0.0386  -0.0288 25  PRO F CB    
7300  C CG    . PRO F 23  ? 0.3292 0.3417 0.3709 -0.0407 0.0366  -0.0315 25  PRO F CG    
7301  C CD    . PRO F 23  ? 0.3314 0.3469 0.3812 -0.0421 0.0383  -0.0297 25  PRO F CD    
7302  N N     . GLU F 24  ? 0.3987 0.4110 0.4316 -0.0379 0.0431  -0.0252 26  GLU F N     
7303  C CA    . GLU F 24  ? 0.4892 0.5022 0.5195 -0.0366 0.0456  -0.0259 26  GLU F CA    
7304  C C     . GLU F 24  ? 0.4882 0.5079 0.5196 -0.0372 0.0471  -0.0249 26  GLU F C     
7305  O O     . GLU F 24  ? 0.4843 0.5067 0.5129 -0.0373 0.0489  -0.0277 26  GLU F O     
7306  C CB    . GLU F 24  ? 0.5672 0.5816 0.5992 -0.0341 0.0460  -0.0252 26  GLU F CB    
7307  C CG    . GLU F 24  ? 0.6678 0.6785 0.6972 -0.0312 0.0458  -0.0251 26  GLU F CG    
7308  C CD    . GLU F 24  ? 0.7352 0.7478 0.7653 -0.0271 0.0475  -0.0235 26  GLU F CD    
7309  O OE1   . GLU F 24  ? 0.8734 0.8930 0.9073 -0.0266 0.0458  -0.0230 26  GLU F OE1   
7310  O OE2   . GLU F 24  ? 0.7687 0.7758 0.7968 -0.0242 0.0514  -0.0226 26  GLU F OE2   
7311  N N     . ALA F 25  ? 0.4369 0.4611 0.4736 -0.0374 0.0468  -0.0210 27  ALA F N     
7312  C CA    . ALA F 25  ? 0.4736 0.5065 0.5118 -0.0365 0.0489  -0.0176 27  ALA F CA    
7313  C C     . ALA F 25  ? 0.4842 0.5207 0.5184 -0.0362 0.0495  -0.0177 27  ALA F C     
7314  O O     . ALA F 25  ? 0.4324 0.4788 0.4637 -0.0346 0.0509  -0.0188 27  ALA F O     
7315  C CB    . ALA F 25  ? 0.4850 0.5198 0.5317 -0.0367 0.0500  -0.0122 27  ALA F CB    
7316  N N     . VAL F 26  ? 0.4766 0.5070 0.5109 -0.0374 0.0482  -0.0174 28  VAL F N     
7317  C CA    . VAL F 26  ? 0.4315 0.4660 0.4627 -0.0368 0.0486  -0.0171 28  VAL F CA    
7318  C C     . VAL F 26  ? 0.4280 0.4639 0.4532 -0.0377 0.0484  -0.0244 28  VAL F C     
7319  O O     . VAL F 26  ? 0.4432 0.4901 0.4659 -0.0366 0.0494  -0.0265 28  VAL F O     
7320  C CB    . VAL F 26  ? 0.4524 0.4793 0.4861 -0.0380 0.0476  -0.0156 28  VAL F CB    
7321  C CG1   . VAL F 26  ? 0.4240 0.4550 0.4537 -0.0371 0.0478  -0.0157 28  VAL F CG1   
7322  C CG2   . VAL F 26  ? 0.4521 0.4775 0.4953 -0.0377 0.0495  -0.0097 28  VAL F CG2   
7323  N N     . MET F 27  ? 0.4125 0.4385 0.4366 -0.0394 0.0479  -0.0285 29  MET F N     
7324  C CA    . MET F 27  ? 0.4006 0.4247 0.4222 -0.0407 0.0495  -0.0353 29  MET F CA    
7325  C C     . MET F 27  ? 0.4175 0.4504 0.4401 -0.0403 0.0520  -0.0400 29  MET F C     
7326  O O     . MET F 27  ? 0.4064 0.4468 0.4287 -0.0414 0.0536  -0.0467 29  MET F O     
7327  C CB    . MET F 27  ? 0.3721 0.3839 0.3936 -0.0410 0.0499  -0.0360 29  MET F CB    
7328  C CG    . MET F 27  ? 0.3693 0.3749 0.3890 -0.0416 0.0478  -0.0344 29  MET F CG    
7329  S SD    . MET F 27  ? 0.3434 0.3390 0.3620 -0.0400 0.0489  -0.0337 29  MET F SD    
7330  C CE    . MET F 27  ? 0.3767 0.3749 0.3977 -0.0374 0.0468  -0.0300 29  MET F CE    
7331  N N     . ARG F 28  ? 0.4257 0.4594 0.4502 -0.0388 0.0523  -0.0375 30  ARG F N     
7332  C CA    . ARG F 28  ? 0.4696 0.5118 0.4956 -0.0381 0.0548  -0.0424 30  ARG F CA    
7333  C C     . ARG F 28  ? 0.4301 0.4907 0.4548 -0.0367 0.0547  -0.0430 30  ARG F C     
7334  O O     . ARG F 28  ? 0.4302 0.5028 0.4556 -0.0366 0.0566  -0.0505 30  ARG F O     
7335  C CB    . ARG F 28  ? 0.5320 0.5721 0.5602 -0.0364 0.0550  -0.0387 30  ARG F CB    
7336  C CG    . ARG F 28  ? 0.6433 0.6700 0.6721 -0.0360 0.0541  -0.0354 30  ARG F CG    
7337  C CD    . ARG F 28  ? 0.6859 0.7124 0.7173 -0.0339 0.0549  -0.0336 30  ARG F CD    
7338  N NE    . ARG F 28  ? 0.7471 0.7713 0.7803 -0.0331 0.0591  -0.0389 30  ARG F NE    
7339  C CZ    . ARG F 28  ? 0.8573 0.8723 0.8921 -0.0310 0.0616  -0.0380 30  ARG F CZ    
7340  N NH1   . ARG F 28  ? 0.7889 0.7992 0.8221 -0.0290 0.0593  -0.0324 30  ARG F NH1   
7341  N NH2   . ARG F 28  ? 0.9705 0.9822 1.0091 -0.0303 0.0670  -0.0428 30  ARG F NH2   
7342  N N     . ALA F 29  ? 0.3602 0.4243 0.3837 -0.0350 0.0529  -0.0350 31  ALA F N     
7343  C CA    . ALA F 29  ? 0.3778 0.4608 0.3999 -0.0315 0.0535  -0.0322 31  ALA F CA    
7344  C C     . ALA F 29  ? 0.3465 0.4384 0.3657 -0.0321 0.0532  -0.0386 31  ALA F C     
7345  O O     . ALA F 29  ? 0.3329 0.4456 0.3503 -0.0286 0.0538  -0.0390 31  ALA F O     
7346  C CB    . ALA F 29  ? 0.3775 0.4592 0.4018 -0.0289 0.0536  -0.0201 31  ALA F CB    
7347  N N     . HIS F 30  ? 0.3330 0.4111 0.3522 -0.0359 0.0526  -0.0434 32  HIS F N     
7348  C CA    . HIS F 30  ? 0.3652 0.4503 0.3831 -0.0374 0.0527  -0.0505 32  HIS F CA    
7349  C C     . HIS F 30  ? 0.3620 0.4455 0.3835 -0.0415 0.0554  -0.0636 32  HIS F C     
7350  O O     . HIS F 30  ? 0.3840 0.4694 0.4068 -0.0443 0.0564  -0.0716 32  HIS F O     
7351  C CB    . HIS F 30  ? 0.3913 0.4636 0.4078 -0.0385 0.0510  -0.0457 32  HIS F CB    
7352  C CG    . HIS F 30  ? 0.3929 0.4703 0.4084 -0.0344 0.0499  -0.0351 32  HIS F CG    
7353  N ND1   . HIS F 30  ? 0.3923 0.4619 0.4106 -0.0329 0.0500  -0.0257 32  HIS F ND1   
7354  C CD2   . HIS F 30  ? 0.4021 0.4921 0.4158 -0.0312 0.0498  -0.0321 32  HIS F CD2   
7355  C CE1   . HIS F 30  ? 0.3950 0.4702 0.4144 -0.0292 0.0508  -0.0172 32  HIS F CE1   
7356  N NE2   . HIS F 30  ? 0.4130 0.5007 0.4289 -0.0275 0.0506  -0.0201 32  HIS F NE2   
7357  N N     . GLY F 31  ? 0.3784 0.4579 0.4029 -0.0418 0.0574  -0.0658 33  GLY F N     
7358  C CA    . GLY F 31  ? 0.3678 0.4485 0.3982 -0.0449 0.0616  -0.0787 33  GLY F CA    
7359  C C     . GLY F 31  ? 0.3796 0.4386 0.4142 -0.0484 0.0649  -0.0810 33  GLY F C     
7360  O O     . GLY F 31  ? 0.3752 0.4335 0.4170 -0.0519 0.0699  -0.0923 33  GLY F O     
7361  N N     . LEU F 32  ? 0.4040 0.4466 0.4351 -0.0472 0.0629  -0.0704 34  LEU F N     
7362  C CA    . LEU F 32  ? 0.4158 0.4399 0.4499 -0.0486 0.0664  -0.0698 34  LEU F CA    
7363  C C     . LEU F 32  ? 0.4341 0.4502 0.4732 -0.0473 0.0707  -0.0702 34  LEU F C     
7364  O O     . LEU F 32  ? 0.3838 0.4022 0.4208 -0.0445 0.0685  -0.0650 34  LEU F O     
7365  C CB    . LEU F 32  ? 0.4147 0.4289 0.4433 -0.0469 0.0625  -0.0596 34  LEU F CB    
7366  C CG    . LEU F 32  ? 0.4178 0.4346 0.4433 -0.0484 0.0601  -0.0598 34  LEU F CG    
7367  C CD1   . LEU F 32  ? 0.4380 0.4711 0.4604 -0.0473 0.0564  -0.0590 34  LEU F CD1   
7368  C CD2   . LEU F 32  ? 0.4202 0.4257 0.4423 -0.0471 0.0576  -0.0519 34  LEU F CD2   
7369  N N     . THR F 33  ? 0.4844 0.4907 0.5313 -0.0491 0.0779  -0.0760 35  THR F N     
7370  C CA    . THR F 33  ? 0.5078 0.5054 0.5614 -0.0474 0.0839  -0.0764 35  THR F CA    
7371  C C     . THR F 33  ? 0.5102 0.4966 0.5589 -0.0423 0.0822  -0.0632 35  THR F C     
7372  O O     . THR F 33  ? 0.4776 0.4623 0.5195 -0.0412 0.0773  -0.0561 35  THR F O     
7373  C CB    . THR F 33  ? 0.5204 0.5091 0.5860 -0.0506 0.0937  -0.0853 35  THR F CB    
7374  O OG1   . THR F 33  ? 0.5555 0.5324 0.6195 -0.0501 0.0949  -0.0785 35  THR F OG1   
7375  C CG2   . THR F 33  ? 0.4904 0.4938 0.5625 -0.0561 0.0953  -0.1012 35  THR F CG2   
7376  N N     . ASP F 34  ? 0.4966 0.4773 0.5497 -0.0390 0.0866  -0.0609 36  ASP F N     
7377  C CA    . ASP F 34  ? 0.5790 0.5536 0.6281 -0.0332 0.0852  -0.0494 36  ASP F CA    
7378  C C     . ASP F 34  ? 0.5565 0.5198 0.6059 -0.0308 0.0891  -0.0431 36  ASP F C     
7379  O O     . ASP F 34  ? 0.4968 0.4603 0.5397 -0.0266 0.0850  -0.0343 36  ASP F O     
7380  C CB    . ASP F 34  ? 0.6323 0.6051 0.6867 -0.0295 0.0897  -0.0486 36  ASP F CB    
7381  C CG    . ASP F 34  ? 0.7172 0.7025 0.7713 -0.0311 0.0862  -0.0540 36  ASP F CG    
7382  O OD1   . ASP F 34  ? 0.7778 0.7718 0.8248 -0.0306 0.0786  -0.0496 36  ASP F OD1   
7383  O OD2   . ASP F 34  ? 0.7598 0.7464 0.8217 -0.0327 0.0919  -0.0628 36  ASP F OD2   
7384  N N     . GLU F 35  ? 0.5819 0.5369 0.6399 -0.0333 0.0975  -0.0485 37  GLU F N     
7385  C CA    . GLU F 35  ? 0.6016 0.5456 0.6615 -0.0307 0.1032  -0.0420 37  GLU F CA    
7386  C C     . GLU F 35  ? 0.5862 0.5343 0.6379 -0.0331 0.0963  -0.0410 37  GLU F C     
7387  O O     . GLU F 35  ? 0.5885 0.5330 0.6359 -0.0291 0.0962  -0.0324 37  GLU F O     
7388  C CB    . GLU F 35  ? 0.6345 0.5678 0.7090 -0.0336 0.1157  -0.0489 37  GLU F CB    
7389  C CG    . GLU F 35  ? 0.7004 0.6407 0.7799 -0.0423 0.1152  -0.0641 37  GLU F CG    
7390  C CD    . GLU F 35  ? 0.7347 0.6659 0.8318 -0.0465 0.1282  -0.0741 37  GLU F CD    
7391  O OE1   . GLU F 35  ? 0.8635 0.7819 0.9667 -0.0450 0.1365  -0.0685 37  GLU F OE1   
7392  O OE2   . GLU F 35  ? 0.7554 0.6933 0.8614 -0.0511 0.1308  -0.0879 37  GLU F OE2   
7393  N N     . GLN F 36  ? 0.5658 0.5231 0.6155 -0.0391 0.0910  -0.0498 38  GLN F N     
7394  C CA    . GLN F 36  ? 0.5182 0.4801 0.5609 -0.0413 0.0847  -0.0495 38  GLN F CA    
7395  C C     . GLN F 36  ? 0.5040 0.4709 0.5373 -0.0378 0.0761  -0.0413 38  GLN F C     
7396  O O     . GLN F 36  ? 0.5218 0.4883 0.5500 -0.0369 0.0728  -0.0372 38  GLN F O     
7397  C CB    . GLN F 36  ? 0.4973 0.4703 0.5409 -0.0471 0.0820  -0.0600 38  GLN F CB    
7398  C CG    . GLN F 36  ? 0.5333 0.5049 0.5881 -0.0518 0.0902  -0.0715 38  GLN F CG    
7399  C CD    . GLN F 36  ? 0.5523 0.5407 0.6077 -0.0563 0.0870  -0.0830 38  GLN F CD    
7400  O OE1   . GLN F 36  ? 0.5431 0.5436 0.5904 -0.0551 0.0793  -0.0807 38  GLN F OE1   
7401  N NE2   . GLN F 36  ? 0.5494 0.5402 0.6155 -0.0612 0.0935  -0.0955 38  GLN F NE2   
7402  N N     . ILE F 37  ? 0.4595 0.4317 0.4917 -0.0361 0.0732  -0.0400 39  ILE F N     
7403  C CA    . ILE F 37  ? 0.4484 0.4264 0.4749 -0.0336 0.0660  -0.0343 39  ILE F CA    
7404  C C     . ILE F 37  ? 0.4416 0.4160 0.4664 -0.0277 0.0672  -0.0266 39  ILE F C     
7405  O O     . ILE F 37  ? 0.4465 0.4252 0.4670 -0.0262 0.0621  -0.0235 39  ILE F O     
7406  C CB    . ILE F 37  ? 0.4336 0.4189 0.4610 -0.0336 0.0636  -0.0353 39  ILE F CB    
7407  C CG1   . ILE F 37  ? 0.4466 0.4399 0.4744 -0.0378 0.0621  -0.0414 39  ILE F CG1   
7408  C CG2   . ILE F 37  ? 0.4352 0.4257 0.4599 -0.0312 0.0579  -0.0300 39  ILE F CG2   
7409  C CD1   . ILE F 37  ? 0.4715 0.4737 0.5002 -0.0372 0.0603  -0.0414 39  ILE F CD1   
7410  N N     . ASN F 38  ? 0.5055 0.4736 0.5347 -0.0239 0.0744  -0.0240 40  ASN F N     
7411  C CA    . ASN F 38  ? 0.5476 0.5148 0.5752 -0.0163 0.0768  -0.0151 40  ASN F CA    
7412  C C     . ASN F 38  ? 0.5343 0.4996 0.5587 -0.0151 0.0772  -0.0119 40  ASN F C     
7413  O O     . ASN F 38  ? 0.5584 0.5311 0.5776 -0.0102 0.0735  -0.0066 40  ASN F O     
7414  C CB    . ASN F 38  ? 0.5568 0.5161 0.5914 -0.0118 0.0865  -0.0118 40  ASN F CB    
7415  C CG    . ASN F 38  ? 0.5906 0.5513 0.6233 -0.0020 0.0899  -0.0005 40  ASN F CG    
7416  O OD1   . ASN F 38  ? 0.5899 0.5622 0.6176 0.0027  0.0841  0.0034  40  ASN F OD1   
7417  N ND2   . ASN F 38  ? 0.5339 0.4846 0.5714 0.0017  0.0998  0.0050  40  ASN F ND2   
7418  N N     . ALA F 39  ? 0.4951 0.4523 0.5230 -0.0196 0.0819  -0.0160 41  ALA F N     
7419  C CA    . ALA F 39  ? 0.5110 0.4658 0.5366 -0.0191 0.0831  -0.0133 41  ALA F CA    
7420  C C     . ALA F 39  ? 0.4479 0.4123 0.4657 -0.0205 0.0731  -0.0145 41  ALA F C     
7421  O O     . ALA F 39  ? 0.5051 0.4735 0.5186 -0.0164 0.0717  -0.0098 41  ALA F O     
7422  C CB    . ALA F 39  ? 0.5052 0.4517 0.5375 -0.0252 0.0891  -0.0200 41  ALA F CB    
7423  N N     . VAL F 40  ? 0.4246 0.3936 0.4418 -0.0259 0.0670  -0.0208 42  VAL F N     
7424  C CA    . VAL F 40  ? 0.4243 0.4006 0.4372 -0.0278 0.0590  -0.0226 42  VAL F CA    
7425  C C     . VAL F 40  ? 0.3941 0.3791 0.4047 -0.0229 0.0548  -0.0189 42  VAL F C     
7426  O O     . VAL F 40  ? 0.3638 0.3548 0.3715 -0.0216 0.0510  -0.0188 42  VAL F O     
7427  C CB    . VAL F 40  ? 0.4137 0.3930 0.4279 -0.0333 0.0554  -0.0281 42  VAL F CB    
7428  C CG1   . VAL F 40  ? 0.4021 0.3879 0.4148 -0.0344 0.0487  -0.0286 42  VAL F CG1   
7429  C CG2   . VAL F 40  ? 0.4256 0.4018 0.4416 -0.0378 0.0583  -0.0332 42  VAL F CG2   
7430  N N     . MET F 41  ? 0.4150 0.4024 0.4275 -0.0201 0.0557  -0.0170 43  MET F N     
7431  C CA    . MET F 41  ? 0.4414 0.4402 0.4530 -0.0158 0.0515  -0.0153 43  MET F CA    
7432  C C     . MET F 41  ? 0.4357 0.4401 0.4439 -0.0078 0.0536  -0.0091 43  MET F C     
7433  O O     . MET F 41  ? 0.4206 0.4386 0.4270 -0.0046 0.0489  -0.0097 43  MET F O     
7434  C CB    . MET F 41  ? 0.4725 0.4732 0.4873 -0.0147 0.0522  -0.0147 43  MET F CB    
7435  C CG    . MET F 41  ? 0.5078 0.5076 0.5258 -0.0212 0.0497  -0.0197 43  MET F CG    
7436  S SD    . MET F 41  ? 0.6144 0.6207 0.6339 -0.0259 0.0430  -0.0240 43  MET F SD    
7437  C CE    . MET F 41  ? 0.6276 0.6477 0.6479 -0.0209 0.0394  -0.0240 43  MET F CE    
7438  N N     . THR F 42  ? 0.4776 0.4728 0.4860 -0.0044 0.0615  -0.0034 44  THR F N     
7439  C CA    . THR F 42  ? 0.5003 0.5008 0.5057 0.0047  0.0654  0.0050  44  THR F CA    
7440  C C     . THR F 42  ? 0.4999 0.4996 0.5021 0.0033  0.0648  0.0044  44  THR F C     
7441  O O     . THR F 42  ? 0.5559 0.5638 0.5543 0.0107  0.0665  0.0107  44  THR F O     
7442  C CB    . THR F 42  ? 0.5339 0.5239 0.5436 0.0099  0.0761  0.0129  44  THR F CB    
7443  O OG1   . THR F 42  ? 0.5603 0.5345 0.5750 0.0025  0.0810  0.0084  44  THR F OG1   
7444  C CG2   . THR F 42  ? 0.5488 0.5409 0.5616 0.0125  0.0768  0.0139  44  THR F CG2   
7445  N N     . GLY F 43  ? 0.4963 0.4880 0.4999 -0.0057 0.0626  -0.0028 45  GLY F N     
7446  C CA    . GLY F 43  ? 0.5191 0.5101 0.5200 -0.0079 0.0615  -0.0046 45  GLY F CA    
7447  C C     . GLY F 43  ? 0.5867 0.5682 0.5891 -0.0051 0.0709  0.0017  45  GLY F C     
7448  O O     . GLY F 43  ? 0.4896 0.4746 0.4886 -0.0022 0.0715  0.0048  45  GLY F O     
7449  N N     . ASP F 44  ? 0.5831 0.5527 0.5919 -0.0060 0.0788  0.0032  46  ASP F N     
7450  C CA    . ASP F 44  ? 0.6032 0.5614 0.6175 -0.0047 0.0898  0.0079  46  ASP F CA    
7451  C C     . ASP F 44  ? 0.6280 0.5787 0.6459 -0.0143 0.0900  -0.0012 46  ASP F C     
7452  O O     . ASP F 44  ? 0.6328 0.5763 0.6577 -0.0201 0.0932  -0.0079 46  ASP F O     
7453  C CB    . ASP F 44  ? 0.6909 0.6403 0.7132 -0.0010 0.0996  0.0128  46  ASP F CB    
7454  C CG    . ASP F 44  ? 0.7430 0.6787 0.7749 0.0003  0.1135  0.0178  46  ASP F CG    
7455  O OD1   . ASP F 44  ? 0.7238 0.6574 0.7556 -0.0020 0.1152  0.0174  46  ASP F OD1   
7456  O OD2   . ASP F 44  ? 0.7654 0.6923 0.8062 0.0036  0.1232  0.0219  46  ASP F OD2   
7457  N N     . MET F 45  ? 0.5988 0.5534 0.6120 -0.0154 0.0865  -0.0019 47  MET F N     
7458  C CA    . MET F 45  ? 0.5932 0.5438 0.6087 -0.0237 0.0858  -0.0103 47  MET F CA    
7459  C C     . MET F 45  ? 0.6304 0.5690 0.6568 -0.0264 0.0976  -0.0114 47  MET F C     
7460  O O     . MET F 45  ? 0.5873 0.5233 0.6194 -0.0340 0.0984  -0.0212 47  MET F O     
7461  C CB    . MET F 45  ? 0.6065 0.5633 0.6156 -0.0230 0.0813  -0.0096 47  MET F CB    
7462  C CG    . MET F 45  ? 0.5959 0.5644 0.5975 -0.0220 0.0703  -0.0116 47  MET F CG    
7463  S SD    . MET F 45  ? 0.6171 0.5870 0.6199 -0.0294 0.0629  -0.0209 47  MET F SD    
7464  C CE    . MET F 45  ? 0.6054 0.5759 0.6103 -0.0262 0.0637  -0.0182 47  MET F CE    
7465  N N     . GLU F 46  ? 0.6879 0.6207 0.7182 -0.0196 0.1074  -0.0012 48  GLU F N     
7466  C CA    . GLU F 46  ? 0.7443 0.6641 0.7879 -0.0218 0.1210  -0.0013 48  GLU F CA    
7467  C C     . GLU F 46  ? 0.7175 0.6315 0.7713 -0.0284 0.1241  -0.0118 48  GLU F C     
7468  O O     . GLU F 46  ? 0.7452 0.6554 0.8085 -0.0364 0.1283  -0.0224 48  GLU F O     
7469  C CB    . GLU F 46  ? 0.8362 0.7509 0.8834 -0.0114 0.1322  0.0138  48  GLU F CB    
7470  C CG    . GLU F 46  ? 0.9009 0.8231 0.9396 -0.0044 0.1313  0.0239  48  GLU F CG    
7471  C CD    . GLU F 46  ? 0.9850 0.9037 1.0270 -0.0106 0.1338  0.0191  48  GLU F CD    
7472  O OE1   . GLU F 46  ? 1.0927 1.0185 1.1277 -0.0055 0.1327  0.0262  48  GLU F OE1   
7473  O OE2   . GLU F 46  ? 1.0414 0.9522 1.0932 -0.0204 0.1367  0.0075  48  GLU F OE2   
7474  N N     . LYS F 47  ? 0.7239 0.6397 0.7761 -0.0248 0.1220  -0.0095 49  LYS F N     
7475  C CA    . LYS F 47  ? 0.6786 0.5903 0.7404 -0.0297 0.1255  -0.0186 49  LYS F CA    
7476  C C     . LYS F 47  ? 0.6260 0.5462 0.6857 -0.0388 0.1168  -0.0329 49  LYS F C     
7477  O O     . LYS F 47  ? 0.6337 0.5525 0.7039 -0.0452 0.1215  -0.0444 49  LYS F O     
7478  C CB    . LYS F 47  ? 0.7562 0.6703 0.8145 -0.0233 0.1233  -0.0126 49  LYS F CB    
7479  C CG    . LYS F 47  ? 0.8519 0.7626 0.9198 -0.0273 0.1271  -0.0216 49  LYS F CG    
7480  C CD    . LYS F 47  ? 0.9490 0.8628 1.0133 -0.0209 0.1247  -0.0154 49  LYS F CD    
7481  C CE    . LYS F 47  ? 1.0020 0.9099 1.0684 -0.0102 0.1334  -0.0004 49  LYS F CE    
7482  N NZ    . LYS F 47  ? 1.0294 0.9218 1.1127 -0.0101 0.1498  0.0003  49  LYS F NZ    
7483  N N     . LEU F 48  ? 0.5837 0.5142 0.6306 -0.0387 0.1048  -0.0323 50  LEU F N     
7484  C CA    . LEU F 48  ? 0.5862 0.5263 0.6300 -0.0452 0.0968  -0.0427 50  LEU F CA    
7485  C C     . LEU F 48  ? 0.6062 0.5458 0.6582 -0.0519 0.1017  -0.0524 50  LEU F C     
7486  O O     . LEU F 48  ? 0.5563 0.5035 0.6126 -0.0575 0.1006  -0.0638 50  LEU F O     
7487  C CB    . LEU F 48  ? 0.6112 0.5598 0.6427 -0.0434 0.0856  -0.0388 50  LEU F CB    
7488  C CG    . LEU F 48  ? 0.6420 0.5948 0.6671 -0.0385 0.0796  -0.0328 50  LEU F CG    
7489  C CD1   . LEU F 48  ? 0.6525 0.6137 0.6695 -0.0387 0.0698  -0.0323 50  LEU F CD1   
7490  C CD2   . LEU F 48  ? 0.6482 0.6028 0.6771 -0.0400 0.0799  -0.0371 50  LEU F CD2   
7491  N N     . LYS F 49  ? 0.6761 0.6089 0.7304 -0.0509 0.1073  -0.0478 51  LYS F N     
7492  C CA    . LYS F 49  ? 0.7992 0.7318 0.8621 -0.0573 0.1125  -0.0567 51  LYS F CA    
7493  C C     . LYS F 49  ? 0.7936 0.7198 0.8741 -0.0618 0.1243  -0.0659 51  LYS F C     
7494  O O     . LYS F 49  ? 0.8663 0.7999 0.9548 -0.0690 0.1254  -0.0803 51  LYS F O     
7495  C CB    . LYS F 49  ? 0.8546 0.7815 0.9158 -0.0543 0.1161  -0.0480 51  LYS F CB    
7496  C CG    . LYS F 49  ? 0.8945 0.8291 0.9402 -0.0505 0.1049  -0.0416 51  LYS F CG    
7497  C CD    . LYS F 49  ? 0.9844 0.9161 1.0279 -0.0473 0.1082  -0.0339 51  LYS F CD    
7498  C CE    . LYS F 49  ? 1.0169 0.9576 1.0468 -0.0442 0.0972  -0.0302 51  LYS F CE    
7499  N NZ    . LYS F 49  ? 1.0626 1.0027 1.0901 -0.0407 0.1003  -0.0234 51  LYS F NZ    
7500  N N     . THR F 50  ? 0.7225 0.6364 0.8097 -0.0570 0.1334  -0.0580 52  THR F N     
7501  C CA    . THR F 50  ? 0.7682 0.6736 0.8744 -0.0607 0.1463  -0.0661 52  THR F CA    
7502  C C     . THR F 50  ? 0.7493 0.6665 0.8575 -0.0660 0.1411  -0.0808 52  THR F C     
7503  O O     . THR F 50  ? 0.7469 0.6677 0.8697 -0.0734 0.1472  -0.0966 52  THR F O     
7504  C CB    . THR F 50  ? 0.7800 0.6716 0.8906 -0.0524 0.1557  -0.0522 52  THR F CB    
7505  O OG1   . THR F 50  ? 0.8767 0.7612 0.9855 -0.0470 0.1609  -0.0389 52  THR F OG1   
7506  C CG2   . THR F 50  ? 0.8264 0.7072 0.9588 -0.0556 0.1704  -0.0602 52  THR F CG2   
7507  N N     . LEU F 51  ? 0.7213 0.6464 0.8155 -0.0620 0.1301  -0.0760 53  LEU F N     
7508  C CA    . LEU F 51  ? 0.7008 0.6378 0.7953 -0.0649 0.1253  -0.0868 53  LEU F CA    
7509  C C     . LEU F 51  ? 0.7454 0.7002 0.8372 -0.0710 0.1183  -0.0994 53  LEU F C     
7510  O O     . LEU F 51  ? 0.7633 0.7324 0.8565 -0.0737 0.1151  -0.1102 53  LEU F O     
7511  C CB    . LEU F 51  ? 0.6464 0.5864 0.7273 -0.0586 0.1164  -0.0764 53  LEU F CB    
7512  C CG    . LEU F 51  ? 0.6245 0.5514 0.7075 -0.0515 0.1226  -0.0645 53  LEU F CG    
7513  C CD1   . LEU F 51  ? 0.5667 0.5001 0.6377 -0.0465 0.1132  -0.0574 53  LEU F CD1   
7514  C CD2   . LEU F 51  ? 0.6511 0.5690 0.7522 -0.0536 0.1357  -0.0719 53  LEU F CD2   
7515  N N     . SER F 52  ? 0.8089 0.7646 0.8967 -0.0722 0.1162  -0.0975 54  SER F N     
7516  C CA    . SER F 52  ? 0.8153 0.7890 0.8998 -0.0765 0.1095  -0.1075 54  SER F CA    
7517  C C     . SER F 52  ? 0.8671 0.8415 0.9664 -0.0833 0.1182  -0.1199 54  SER F C     
7518  O O     . SER F 52  ? 0.8823 0.8746 0.9830 -0.0877 0.1148  -0.1320 54  SER F O     
7519  C CB    . SER F 52  ? 0.8000 0.7770 0.8683 -0.0726 0.0992  -0.0968 54  SER F CB    
7520  O OG    . SER F 52  ? 0.8099 0.8056 0.8743 -0.0752 0.0927  -0.1046 54  SER F OG    
7521  N N     . GLY F 53  ? 0.9198 0.8757 1.0310 -0.0838 0.1301  -0.1164 55  GLY F N     
7522  C CA    . GLY F 53  ? 0.9633 0.9166 1.0908 -0.0903 0.1402  -0.1264 55  GLY F CA    
7523  C C     . GLY F 53  ? 0.9192 0.8644 1.0399 -0.0877 0.1399  -0.1145 55  GLY F C     
7524  O O     . GLY F 53  ? 0.8409 0.7719 0.9738 -0.0886 0.1518  -0.1113 55  GLY F O     
7525  N N     . ASP F 54  ? 0.9500 0.9048 1.0522 -0.0843 0.1269  -0.1079 56  ASP F N     
7526  C CA    . ASP F 54  ? 1.0212 0.9704 1.1144 -0.0808 0.1247  -0.0961 56  ASP F CA    
7527  C C     . ASP F 54  ? 1.0514 0.9815 1.1546 -0.0783 0.1378  -0.0867 56  ASP F C     
7528  O O     . ASP F 54  ? 1.0725 0.9929 1.1708 -0.0713 0.1390  -0.0738 56  ASP F O     
7529  C CB    . ASP F 54  ? 1.1244 1.0769 1.1980 -0.0740 0.1122  -0.0840 56  ASP F CB    
7530  C CG    . ASP F 54  ? 1.3027 1.2517 1.3665 -0.0698 0.1090  -0.0729 56  ASP F CG    
7531  O OD1   . ASP F 54  ? 1.5403 1.4835 1.6113 -0.0715 0.1167  -0.0726 56  ASP F OD1   
7532  O OD2   . ASP F 54  ? 1.3397 1.2924 1.3898 -0.0651 0.0993  -0.0654 56  ASP F OD2   
7533  N N     . LEU F 61  ? 0.6888 0.6557 0.7003 -0.0365 0.1066  -0.0122 63  LEU F N     
7534  C CA    . LEU F 61  ? 0.6894 0.6658 0.6911 -0.0373 0.0931  -0.0192 63  LEU F CA    
7535  C C     . LEU F 61  ? 0.6116 0.5974 0.6066 -0.0332 0.0907  -0.0168 63  LEU F C     
7536  O O     . LEU F 61  ? 0.6320 0.6256 0.6205 -0.0331 0.0811  -0.0221 63  LEU F O     
7537  C CB    . LEU F 61  ? 0.6220 0.6016 0.6171 -0.0333 0.0857  -0.0178 63  LEU F CB    
7538  C CG    . LEU F 61  ? 0.7509 0.7240 0.7507 -0.0378 0.0847  -0.0226 63  LEU F CG    
7539  C CD1   . LEU F 61  ? 0.7496 0.7288 0.7430 -0.0376 0.0734  -0.0271 63  LEU F CD1   
7540  C CD2   . LEU F 61  ? 0.7185 0.6868 0.7276 -0.0462 0.0886  -0.0310 63  LEU F CD2   
7541  N N     . VAL F 62  ? 0.6266 0.6115 0.6246 -0.0298 0.1004  -0.0087 64  VAL F N     
7542  C CA    . VAL F 62  ? 0.6580 0.6536 0.6494 -0.0246 0.0990  -0.0052 64  VAL F CA    
7543  C C     . VAL F 62  ? 0.6078 0.6045 0.6019 -0.0312 0.0975  -0.0135 64  VAL F C     
7544  O O     . VAL F 62  ? 0.5998 0.5895 0.6040 -0.0365 0.1062  -0.0147 64  VAL F O     
7545  C CB    . VAL F 62  ? 0.6914 0.6875 0.6846 -0.0167 0.1109  0.0090  64  VAL F CB    
7546  C CG1   . VAL F 62  ? 0.7051 0.7172 0.6887 -0.0087 0.1081  0.0137  64  VAL F CG1   
7547  C CG2   . VAL F 62  ? 0.7143 0.7071 0.7080 -0.0106 0.1151  0.0181  64  VAL F CG2   
7548  N N     . IML F 63  ? 0.5674 0.5733 0.5541 -0.0312 0.0873  -0.0200 65  IML F N     
7549  C CA    . IML F 63  ? 0.5312 0.5395 0.5201 -0.0364 0.0856  -0.0274 65  IML F CA    
7550  C C     . IML F 63  ? 0.5763 0.5958 0.5585 -0.0313 0.0831  -0.0259 65  IML F C     
7551  O O     . IML F 63  ? 0.5181 0.5420 0.4996 -0.0341 0.0785  -0.0328 65  IML F O     
7552  C CB    . IML F 63  ? 0.4783 0.4865 0.4672 -0.0416 0.0768  -0.0375 65  IML F CB    
7553  C CN    . IML F 63  ? 0.5596 0.5736 0.5379 -0.0261 0.0781  -0.0209 65  IML F CN    
7554  C CG2   . IML F 63  ? 0.4937 0.5045 0.4875 -0.0474 0.0773  -0.0447 65  IML F CG2   
7555  C CG1   . IML F 63  ? 0.4753 0.4761 0.4679 -0.0444 0.0770  -0.0385 65  IML F CG1   
7556  C CD1   . IML F 63  ? 0.4418 0.4442 0.4346 -0.0484 0.0696  -0.0465 65  IML F CD1   
7557  N N     . SER F 64  ? 0.6008 0.6267 0.5781 -0.0231 0.0864  -0.0167 66  SER F N     
7558  C CA    . SER F 64  ? 0.6141 0.6537 0.5849 -0.0173 0.0845  -0.0153 66  SER F CA    
7559  C C     . SER F 64  ? 0.6341 0.6806 0.6021 -0.0079 0.0927  -0.0020 66  SER F C     
7560  O O     . SER F 64  ? 0.7452 0.7857 0.7158 -0.0053 0.0988  0.0062  66  SER F O     
7561  C CB    . SER F 64  ? 0.6166 0.6662 0.5808 -0.0154 0.0729  -0.0235 66  SER F CB    
7562  O OG    . SER F 64  ? 0.6026 0.6564 0.5632 -0.0106 0.0698  -0.0213 66  SER F OG    
7563  N N     . HIS F 65  ? 0.6648 0.7253 0.6274 -0.0021 0.0931  0.0007  67  HIS F N     
7564  C CA    . HIS F 65  ? 0.7273 0.7992 0.6861 0.0088  0.1008  0.0145  67  HIS F CA    
7565  C C     . HIS F 65  ? 0.7295 0.8251 0.6777 0.0167  0.0930  0.0112  67  HIS F C     
7566  O O     . HIS F 65  ? 0.6736 0.7734 0.6196 0.0128  0.0826  -0.0022 67  HIS F O     
7567  C CB    . HIS F 65  ? 0.7826 0.8476 0.7490 0.0082  0.1144  0.0239  67  HIS F CB    
7568  C CG    . HIS F 65  ? 0.8478 0.9142 0.8159 0.0024  0.1126  0.0159  67  HIS F CG    
7569  N ND1   . HIS F 65  ? 0.8227 0.9069 0.7830 0.0082  0.1090  0.0152  67  HIS F ND1   
7570  C CD2   . HIS F 65  ? 0.8946 0.9490 0.8714 -0.0082 0.1136  0.0076  67  HIS F CD2   
7571  C CE1   . HIS F 65  ? 0.9126 0.9936 0.8768 0.0013  0.1083  0.0076  67  HIS F CE1   
7572  N NE2   . HIS F 65  ? 0.9186 0.9824 0.8927 -0.0085 0.1109  0.0030  67  HIS F NE2   
7573  N N     . GLY F 66  ? 0.8310 0.9430 0.7738 0.0284  0.0988  0.0234  68  GLY F N     
7574  C CA    . GLY F 66  ? 0.8425 0.9818 0.7755 0.0373  0.0922  0.0200  68  GLY F CA    
7575  C C     . GLY F 66  ? 0.8714 1.0247 0.8014 0.0460  0.1011  0.0318  68  GLY F C     
7576  O O     . GLY F 66  ? 0.8300 1.0101 0.7513 0.0575  0.0995  0.0352  68  GLY F O     
7577  N N     . ASN F 67  ? 0.8477 0.9843 0.7855 0.0405  0.1108  0.0375  69  ASN F N     
7578  C CA    . ASN F 67  ? 0.8097 0.9566 0.7469 0.0476  0.1209  0.0494  69  ASN F CA    
7579  C C     . ASN F 67  ? 0.8177 0.9700 0.7536 0.0424  0.1149  0.0374  69  ASN F C     
7580  O O     . ASN F 67  ? 0.7294 0.8897 0.6653 0.0464  0.1222  0.0446  69  ASN F O     
7581  C CB    . ASN F 67  ? 0.7769 0.9035 0.7261 0.0454  0.1374  0.0638  69  ASN F CB    
7582  C CG    . ASN F 67  ? 0.7768 0.9000 0.7276 0.0530  0.1453  0.0781  69  ASN F CG    
7583  O OD1   . ASN F 67  ? 0.7542 0.8920 0.6960 0.0601  0.1375  0.0772  69  ASN F OD1   
7584  N ND2   . ASN F 67  ? 0.7966 0.9015 0.7602 0.0517  0.1612  0.0907  69  ASN F ND2   
7585  N N     . GLY F 68  ? 0.8392 0.9869 0.7747 0.0339  0.1024  0.0198  70  GLY F N     
7586  C CA    . GLY F 68  ? 0.8567 1.0086 0.7918 0.0291  0.0962  0.0076  70  GLY F CA    
7587  C C     . GLY F 68  ? 0.8033 0.9352 0.7482 0.0187  0.1020  0.0065  70  GLY F C     
7588  O O     . GLY F 68  ? 0.7719 0.8925 0.7240 0.0180  0.1140  0.0182  70  GLY F O     
7589  N N     . GLY G 1   ? 0.4754 0.5165 0.5018 -0.0512 0.0674  -0.0429 2   GLY G N     
7590  C CA    . GLY G 1   ? 0.4549 0.4921 0.4786 -0.0515 0.0655  -0.0413 2   GLY G CA    
7591  C C     . GLY G 1   ? 0.4963 0.5329 0.5175 -0.0494 0.0615  -0.0420 2   GLY G C     
7592  O O     . GLY G 1   ? 0.4874 0.5270 0.5103 -0.0478 0.0601  -0.0441 2   GLY G O     
7593  N N     . SER G 2   ? 0.4530 0.4855 0.4699 -0.0492 0.0600  -0.0400 3   SER G N     
7594  C CA    . SER G 2   ? 0.4374 0.4687 0.4517 -0.0474 0.0567  -0.0404 3   SER G CA    
7595  C C     . SER G 2   ? 0.4231 0.4510 0.4355 -0.0480 0.0555  -0.0386 3   SER G C     
7596  O O     . SER G 2   ? 0.3554 0.3812 0.3671 -0.0493 0.0573  -0.0366 3   SER G O     
7597  C CB    . SER G 2   ? 0.4642 0.4943 0.4734 -0.0459 0.0561  -0.0399 3   SER G CB    
7598  O OG    . SER G 2   ? 0.5069 0.5342 0.5115 -0.0465 0.0574  -0.0374 3   SER G OG    
7599  N N     . LEU G 3   ? 0.4107 0.4377 0.4221 -0.0468 0.0527  -0.0392 4   LEU G N     
7600  C CA    . LEU G 3   ? 0.4115 0.4355 0.4214 -0.0471 0.0516  -0.0377 4   LEU G CA    
7601  C C     . LEU G 3   ? 0.4019 0.4238 0.4072 -0.0456 0.0494  -0.0371 4   LEU G C     
7602  O O     . LEU G 3   ? 0.3804 0.4031 0.3851 -0.0442 0.0479  -0.0386 4   LEU G O     
7603  C CB    . LEU G 3   ? 0.4249 0.4499 0.4390 -0.0475 0.0507  -0.0394 4   LEU G CB    
7604  C CG    . LEU G 3   ? 0.4032 0.4251 0.4158 -0.0476 0.0495  -0.0382 4   LEU G CG    
7605  C CD1   . LEU G 3   ? 0.4095 0.4288 0.4213 -0.0489 0.0515  -0.0357 4   LEU G CD1   
7606  C CD2   . LEU G 3   ? 0.4375 0.4604 0.4536 -0.0478 0.0483  -0.0404 4   LEU G CD2   
7607  N N     . VAL G 4   ? 0.3911 0.4104 0.3933 -0.0460 0.0494  -0.0348 5   VAL G N     
7608  C CA    . VAL G 4   ? 0.3879 0.4054 0.3865 -0.0450 0.0474  -0.0342 5   VAL G CA    
7609  C C     . VAL G 4   ? 0.3753 0.3907 0.3737 -0.0454 0.0469  -0.0325 5   VAL G C     
7610  O O     . VAL G 4   ? 0.3545 0.3690 0.3523 -0.0461 0.0482  -0.0305 5   VAL G O     
7611  C CB    . VAL G 4   ? 0.3704 0.3873 0.3648 -0.0448 0.0477  -0.0332 5   VAL G CB    
7612  C CG1   . VAL G 4   ? 0.3857 0.4008 0.3767 -0.0443 0.0459  -0.0326 5   VAL G CG1   
7613  C CG2   . VAL G 4   ? 0.3760 0.3945 0.3702 -0.0441 0.0483  -0.0350 5   VAL G CG2   
7614  N N     . CYS G 5   ? 0.3987 0.4133 0.3974 -0.0447 0.0453  -0.0333 6   CYS G N     
7615  C CA    . CYS G 5   ? 0.3741 0.3868 0.3727 -0.0449 0.0448  -0.0319 6   CYS G CA    
7616  C C     . CYS G 5   ? 0.3624 0.3739 0.3576 -0.0443 0.0435  -0.0308 6   CYS G C     
7617  O O     . CYS G 5   ? 0.3716 0.3828 0.3652 -0.0436 0.0424  -0.0320 6   CYS G O     
7618  C CB    . CYS G 5   ? 0.4018 0.4143 0.4029 -0.0446 0.0439  -0.0335 6   CYS G CB    
7619  S SG    . CYS G 5   ? 0.4543 0.4689 0.4601 -0.0456 0.0452  -0.0354 6   CYS G SG    
7620  N N     . VAL G 6   ? 0.3652 0.3760 0.3593 -0.0447 0.0439  -0.0286 7   VAL G N     
7621  C CA    . VAL G 6   ? 0.3773 0.3877 0.3687 -0.0444 0.0427  -0.0276 7   VAL G CA    
7622  C C     . VAL G 6   ? 0.4266 0.4360 0.4189 -0.0442 0.0424  -0.0262 7   VAL G C     
7623  O O     . VAL G 6   ? 0.4973 0.5060 0.4916 -0.0443 0.0434  -0.0255 7   VAL G O     
7624  C CB    . VAL G 6   ? 0.3662 0.3776 0.3550 -0.0447 0.0431  -0.0264 7   VAL G CB    
7625  C CG1   . VAL G 6   ? 0.3273 0.3395 0.3152 -0.0448 0.0438  -0.0279 7   VAL G CG1   
7626  C CG2   . VAL G 6   ? 0.3507 0.3620 0.3398 -0.0448 0.0444  -0.0241 7   VAL G CG2   
7627  N N     . GLY G 7   ? 0.4634 0.4728 0.4543 -0.0440 0.0412  -0.0258 8   GLY G N     
7628  C CA    . GLY G 7   ? 0.4505 0.4594 0.4422 -0.0436 0.0410  -0.0243 8   GLY G CA    
7629  C C     . GLY G 7   ? 0.4400 0.4505 0.4303 -0.0436 0.0405  -0.0224 8   GLY G C     
7630  O O     . GLY G 7   ? 0.4086 0.4203 0.3967 -0.0440 0.0398  -0.0229 8   GLY G O     
7631  N N     . THR G 8   ? 0.4471 0.4576 0.4383 -0.0430 0.0409  -0.0204 9   THR G N     
7632  C CA    . THR G 8   ? 0.5165 0.5289 0.5065 -0.0426 0.0404  -0.0184 9   THR G CA    
7633  C C     . THR G 8   ? 0.4146 0.4281 0.4056 -0.0422 0.0392  -0.0180 9   THR G C     
7634  O O     . THR G 8   ? 0.4017 0.4174 0.3923 -0.0417 0.0385  -0.0164 9   THR G O     
7635  C CB    . THR G 8   ? 0.5293 0.5408 0.5195 -0.0419 0.0418  -0.0162 9   THR G CB    
7636  O OG1   . THR G 8   ? 0.5745 0.5841 0.5671 -0.0414 0.0425  -0.0158 9   THR G OG1   
7637  C CG2   . THR G 8   ? 0.5601 0.5705 0.5496 -0.0425 0.0433  -0.0166 9   THR G CG2   
7638  N N     . GLY G 9   ? 0.3722 0.3844 0.3645 -0.0425 0.0391  -0.0195 10  GLY G N     
7639  C CA    . GLY G 9   ? 0.3109 0.3240 0.3045 -0.0422 0.0385  -0.0192 10  GLY G CA    
7640  C C     . GLY G 9   ? 0.3151 0.3277 0.3107 -0.0410 0.0392  -0.0173 10  GLY G C     
7641  O O     . GLY G 9   ? 0.3241 0.3348 0.3201 -0.0406 0.0404  -0.0166 10  GLY G O     
7642  N N     . LEU G 10  ? 0.3311 0.3454 0.3282 -0.0405 0.0387  -0.0166 11  LEU G N     
7643  C CA    . LEU G 10  ? 0.3080 0.3221 0.3071 -0.0391 0.0395  -0.0147 11  LEU G CA    
7644  C C     . LEU G 10  ? 0.3152 0.3325 0.3142 -0.0380 0.0387  -0.0124 11  LEU G C     
7645  O O     . LEU G 10  ? 0.3085 0.3249 0.3078 -0.0366 0.0396  -0.0104 11  LEU G O     
7646  C CB    . LEU G 10  ? 0.2960 0.3099 0.2971 -0.0389 0.0396  -0.0153 11  LEU G CB    
7647  C CG    . LEU G 10  ? 0.2887 0.2987 0.2897 -0.0392 0.0407  -0.0169 11  LEU G CG    
7648  C CD1   . LEU G 10  ? 0.3134 0.3207 0.3148 -0.0385 0.0420  -0.0163 11  LEU G CD1   
7649  C CD2   . LEU G 10  ? 0.2962 0.3053 0.2953 -0.0404 0.0402  -0.0192 11  LEU G CD2   
7650  N N     . GLN G 11  ? 0.3125 0.3334 0.3108 -0.0387 0.0370  -0.0129 12  GLN G N     
7651  C CA    . GLN G 11  ? 0.3391 0.3640 0.3372 -0.0377 0.0358  -0.0111 12  GLN G CA    
7652  C C     . GLN G 11  ? 0.3207 0.3451 0.3156 -0.0374 0.0359  -0.0101 12  GLN G C     
7653  O O     . GLN G 11  ? 0.3706 0.3933 0.3636 -0.0387 0.0362  -0.0115 12  GLN G O     
7654  C CB    . GLN G 11  ? 0.3443 0.3735 0.3430 -0.0388 0.0340  -0.0123 12  GLN G CB    
7655  C CG    . GLN G 11  ? 0.3842 0.4156 0.3866 -0.0384 0.0338  -0.0122 12  GLN G CG    
7656  C CD    . GLN G 11  ? 0.3741 0.4085 0.3782 -0.0360 0.0334  -0.0095 12  GLN G CD    
7657  O OE1   . GLN G 11  ? 0.3595 0.3933 0.3618 -0.0345 0.0336  -0.0075 12  GLN G OE1   
7658  N NE2   . GLN G 11  ? 0.4051 0.4426 0.4128 -0.0356 0.0331  -0.0094 12  GLN G NE2   
7659  N N     . LEU G 12  ? 0.3200 0.3462 0.3144 -0.0356 0.0356  -0.0075 13  LEU G N     
7660  C CA    . LEU G 12  ? 0.3180 0.3434 0.3090 -0.0349 0.0360  -0.0060 13  LEU G CA    
7661  C C     . LEU G 12  ? 0.3181 0.3463 0.3062 -0.0362 0.0343  -0.0074 13  LEU G C     
7662  O O     . LEU G 12  ? 0.3100 0.3426 0.2981 -0.0361 0.0323  -0.0075 13  LEU G O     
7663  C CB    . LEU G 12  ? 0.3270 0.3537 0.3180 -0.0322 0.0359  -0.0027 13  LEU G CB    
7664  C CG    . LEU G 12  ? 0.3479 0.3743 0.3348 -0.0310 0.0362  -0.0005 13  LEU G CG    
7665  C CD1   . LEU G 12  ? 0.3419 0.3628 0.3275 -0.0314 0.0390  0.0000  13  LEU G CD1   
7666  C CD2   . LEU G 12  ? 0.3458 0.3745 0.3325 -0.0280 0.0355  0.0027  13  LEU G CD2   
7667  N N     . ALA G 13  ? 0.3307 0.3562 0.3166 -0.0375 0.0353  -0.0086 14  ALA G N     
7668  C CA    . ALA G 13  ? 0.3496 0.3767 0.3318 -0.0382 0.0344  -0.0093 14  ALA G CA    
7669  C C     . ALA G 13  ? 0.3528 0.3817 0.3350 -0.0402 0.0330  -0.0123 14  ALA G C     
7670  O O     . ALA G 13  ? 0.4076 0.4352 0.3875 -0.0414 0.0333  -0.0140 14  ALA G O     
7671  C CB    . ALA G 13  ? 0.3852 0.4155 0.3652 -0.0364 0.0332  -0.0069 14  ALA G CB    
7672  N N     . GLY G 14  ? 0.3182 0.3498 0.3030 -0.0405 0.0316  -0.0130 15  GLY G N     
7673  C CA    . GLY G 14  ? 0.3147 0.3484 0.2993 -0.0424 0.0301  -0.0156 15  GLY G CA    
7674  C C     . GLY G 14  ? 0.3654 0.3960 0.3516 -0.0438 0.0311  -0.0179 15  GLY G C     
7675  O O     . GLY G 14  ? 0.3431 0.3744 0.3290 -0.0455 0.0304  -0.0201 15  GLY G O     
7676  N N     . GLN G 15  ? 0.3672 0.3944 0.3550 -0.0432 0.0328  -0.0173 16  GLN G N     
7677  C CA    . GLN G 15  ? 0.4005 0.4249 0.3897 -0.0441 0.0336  -0.0191 16  GLN G CA    
7678  C C     . GLN G 15  ? 0.4088 0.4298 0.3963 -0.0444 0.0348  -0.0202 16  GLN G C     
7679  O O     . GLN G 15  ? 0.3931 0.4115 0.3813 -0.0448 0.0354  -0.0217 16  GLN G O     
7680  C CB    . GLN G 15  ? 0.4278 0.4514 0.4202 -0.0431 0.0343  -0.0180 16  GLN G CB    
7681  C CG    . GLN G 15  ? 0.4770 0.4994 0.4710 -0.0440 0.0346  -0.0197 16  GLN G CG    
7682  C CD    . GLN G 15  ? 0.4940 0.5165 0.4911 -0.0429 0.0352  -0.0185 16  GLN G CD    
7683  O OE1   . GLN G 15  ? 0.4891 0.5092 0.4870 -0.0418 0.0364  -0.0176 16  GLN G OE1   
7684  N NE2   . GLN G 15  ? 0.5235 0.5489 0.5225 -0.0434 0.0345  -0.0187 16  GLN G NE2   
7685  N N     . ILE G 16  ? 0.3494 0.3704 0.3346 -0.0442 0.0351  -0.0196 17  ILE G N     
7686  C CA    . ILE G 16  ? 0.3284 0.3470 0.3122 -0.0446 0.0361  -0.0209 17  ILE G CA    
7687  C C     . ILE G 16  ? 0.2973 0.3162 0.2787 -0.0458 0.0354  -0.0231 17  ILE G C     
7688  O O     . ILE G 16  ? 0.2984 0.3197 0.2786 -0.0463 0.0341  -0.0233 17  ILE G O     
7689  C CB    . ILE G 16  ? 0.3447 0.3629 0.3272 -0.0439 0.0373  -0.0194 17  ILE G CB    
7690  C CG1   . ILE G 16  ? 0.3316 0.3478 0.3136 -0.0443 0.0386  -0.0208 17  ILE G CG1   
7691  C CG2   . ILE G 16  ? 0.3499 0.3707 0.3295 -0.0437 0.0363  -0.0183 17  ILE G CG2   
7692  C CD1   . ILE G 16  ? 0.3111 0.3263 0.2933 -0.0438 0.0403  -0.0194 17  ILE G CD1   
7693  N N     . SER G 17  ? 0.3163 0.3328 0.2972 -0.0461 0.0362  -0.0248 18  SER G N     
7694  C CA    . SER G 17  ? 0.3552 0.3712 0.3336 -0.0470 0.0359  -0.0269 18  SER G CA    
7695  C C     . SER G 17  ? 0.3557 0.3730 0.3311 -0.0471 0.0360  -0.0266 18  SER G C     
7696  O O     . SER G 17  ? 0.3060 0.3238 0.2814 -0.0463 0.0367  -0.0250 18  SER G O     
7697  C CB    . SER G 17  ? 0.3497 0.3628 0.3282 -0.0468 0.0368  -0.0286 18  SER G CB    
7698  O OG    . SER G 17  ? 0.3779 0.3906 0.3562 -0.0462 0.0379  -0.0285 18  SER G OG    
7699  N N     . VAL G 18  ? 0.3672 0.3848 0.3398 -0.0480 0.0354  -0.0283 19  VAL G N     
7700  C CA    . VAL G 18  ? 0.3923 0.4111 0.3615 -0.0482 0.0354  -0.0283 19  VAL G CA    
7701  C C     . VAL G 18  ? 0.4061 0.4231 0.3747 -0.0475 0.0372  -0.0284 19  VAL G C     
7702  O O     . VAL G 18  ? 0.4302 0.4479 0.3972 -0.0470 0.0379  -0.0272 19  VAL G O     
7703  C CB    . VAL G 18  ? 0.4546 0.4737 0.4210 -0.0495 0.0344  -0.0305 19  VAL G CB    
7704  C CG1   . VAL G 18  ? 0.4817 0.5013 0.4439 -0.0495 0.0347  -0.0309 19  VAL G CG1   
7705  C CG2   . VAL G 18  ? 0.4240 0.4457 0.3913 -0.0504 0.0326  -0.0305 19  VAL G CG2   
7706  N N     . LEU G 19  ? 0.3650 0.3796 0.3348 -0.0474 0.0379  -0.0300 20  LEU G N     
7707  C CA    . LEU G 19  ? 0.4057 0.4193 0.3756 -0.0467 0.0396  -0.0306 20  LEU G CA    
7708  C C     . LEU G 19  ? 0.3845 0.3986 0.3572 -0.0460 0.0405  -0.0287 20  LEU G C     
7709  O O     . LEU G 19  ? 0.3910 0.4055 0.3631 -0.0458 0.0419  -0.0281 20  LEU G O     
7710  C CB    . LEU G 19  ? 0.4147 0.4259 0.3853 -0.0464 0.0398  -0.0326 20  LEU G CB    
7711  C CG    . LEU G 19  ? 0.4225 0.4332 0.3936 -0.0455 0.0413  -0.0335 20  LEU G CG    
7712  C CD1   . LEU G 19  ? 0.4659 0.4769 0.4338 -0.0457 0.0422  -0.0342 20  LEU G CD1   
7713  C CD2   . LEU G 19  ? 0.4546 0.4632 0.4266 -0.0448 0.0413  -0.0352 20  LEU G CD2   
7714  N N     . SER G 20  ? 0.3642 0.3780 0.3398 -0.0458 0.0400  -0.0280 21  SER G N     
7715  C CA    . SER G 20  ? 0.3795 0.3933 0.3580 -0.0454 0.0410  -0.0266 21  SER G CA    
7716  C C     . SER G 20  ? 0.3430 0.3578 0.3201 -0.0452 0.0416  -0.0243 21  SER G C     
7717  O O     . SER G 20  ? 0.3477 0.3621 0.3258 -0.0451 0.0433  -0.0235 21  SER G O     
7718  C CB    . SER G 20  ? 0.3544 0.3675 0.3355 -0.0451 0.0403  -0.0262 21  SER G CB    
7719  O OG    . SER G 20  ? 0.3967 0.4085 0.3787 -0.0450 0.0400  -0.0280 21  SER G OG    
7720  N N     . ARG G 21  ? 0.3124 0.3286 0.2874 -0.0453 0.0404  -0.0233 22  ARG G N     
7721  C CA    . ARG G 21  ? 0.3338 0.3510 0.3068 -0.0447 0.0407  -0.0210 22  ARG G CA    
7722  C C     . ARG G 21  ? 0.3522 0.3690 0.3225 -0.0449 0.0423  -0.0213 22  ARG G C     
7723  O O     . ARG G 21  ? 0.3477 0.3640 0.3177 -0.0444 0.0440  -0.0196 22  ARG G O     
7724  C CB    . ARG G 21  ? 0.3680 0.3874 0.3389 -0.0447 0.0387  -0.0204 22  ARG G CB    
7725  C CG    . ARG G 21  ? 0.3980 0.4188 0.3665 -0.0437 0.0387  -0.0178 22  ARG G CG    
7726  C CD    . ARG G 21  ? 0.4433 0.4672 0.4102 -0.0436 0.0362  -0.0175 22  ARG G CD    
7727  N NE    . ARG G 21  ? 0.4606 0.4859 0.4253 -0.0420 0.0360  -0.0146 22  ARG G NE    
7728  C CZ    . ARG G 21  ? 0.5229 0.5479 0.4835 -0.0414 0.0369  -0.0135 22  ARG G CZ    
7729  N NH1   . ARG G 21  ? 0.6006 0.6243 0.5589 -0.0423 0.0381  -0.0151 22  ARG G NH1   
7730  N NH2   . ARG G 21  ? 0.5228 0.5488 0.4813 -0.0397 0.0367  -0.0106 22  ARG G NH2   
7731  N N     . SER G 22  ? 0.3837 0.4006 0.3522 -0.0454 0.0420  -0.0236 23  SER G N     
7732  C CA    . SER G 22  ? 0.3680 0.3846 0.3338 -0.0455 0.0436  -0.0242 23  SER G CA    
7733  C C     . SER G 22  ? 0.3843 0.3999 0.3530 -0.0453 0.0459  -0.0241 23  SER G C     
7734  O O     . SER G 22  ? 0.4375 0.4531 0.4048 -0.0452 0.0478  -0.0231 23  SER G O     
7735  C CB    . SER G 22  ? 0.3525 0.3687 0.3163 -0.0460 0.0430  -0.0269 23  SER G CB    
7736  O OG    . SER G 22  ? 0.3518 0.3677 0.3129 -0.0459 0.0446  -0.0276 23  SER G OG    
7737  N N     . TYR G 23  ? 0.3545 0.3696 0.3273 -0.0454 0.0458  -0.0252 24  TYR G N     
7738  C CA    . TYR G 23  ? 0.3473 0.3621 0.3236 -0.0455 0.0476  -0.0256 24  TYR G CA    
7739  C C     . TYR G 23  ? 0.3297 0.3441 0.3068 -0.0455 0.0492  -0.0231 24  TYR G C     
7740  O O     . TYR G 23  ? 0.3530 0.3672 0.3307 -0.0458 0.0515  -0.0228 24  TYR G O     
7741  C CB    . TYR G 23  ? 0.3407 0.3552 0.3208 -0.0454 0.0468  -0.0271 24  TYR G CB    
7742  C CG    . TYR G 23  ? 0.3762 0.3907 0.3563 -0.0450 0.0464  -0.0296 24  TYR G CG    
7743  C CD1   . TYR G 23  ? 0.4214 0.4368 0.4028 -0.0448 0.0479  -0.0309 24  TYR G CD1   
7744  C CD2   . TYR G 23  ? 0.4392 0.4527 0.4181 -0.0448 0.0446  -0.0307 24  TYR G CD2   
7745  C CE1   . TYR G 23  ? 0.4275 0.4429 0.4088 -0.0441 0.0476  -0.0331 24  TYR G CE1   
7746  C CE2   . TYR G 23  ? 0.4281 0.4411 0.4067 -0.0442 0.0444  -0.0329 24  TYR G CE2   
7747  C CZ    . TYR G 23  ? 0.4469 0.4608 0.4266 -0.0437 0.0459  -0.0340 24  TYR G CZ    
7748  O OH    . TYR G 23  ? 0.4567 0.4700 0.4360 -0.0427 0.0457  -0.0360 24  TYR G OH    
7749  N N     . ILE G 24  ? 0.3274 0.3414 0.3047 -0.0452 0.0481  -0.0213 25  ILE G N     
7750  C CA    . ILE G 24  ? 0.3457 0.3585 0.3235 -0.0450 0.0496  -0.0188 25  ILE G CA    
7751  C C     . ILE G 24  ? 0.3790 0.3917 0.3528 -0.0447 0.0512  -0.0171 25  ILE G C     
7752  O O     . ILE G 24  ? 0.3773 0.3887 0.3515 -0.0448 0.0536  -0.0155 25  ILE G O     
7753  C CB    . ILE G 24  ? 0.3416 0.3542 0.3199 -0.0443 0.0480  -0.0172 25  ILE G CB    
7754  C CG1   . ILE G 24  ? 0.3067 0.3189 0.2889 -0.0446 0.0471  -0.0187 25  ILE G CG1   
7755  C CG2   . ILE G 24  ? 0.3595 0.3706 0.3374 -0.0437 0.0497  -0.0141 25  ILE G CG2   
7756  C CD1   . ILE G 24  ? 0.2838 0.2958 0.2668 -0.0439 0.0458  -0.0172 25  ILE G CD1   
7757  N N     . GLU G 25  ? 0.3997 0.4137 0.3694 -0.0444 0.0498  -0.0175 26  GLU G N     
7758  C CA    . GLU G 25  ? 0.4597 0.4737 0.4245 -0.0439 0.0507  -0.0158 26  GLU G CA    
7759  C C     . GLU G 25  ? 0.4464 0.4597 0.4109 -0.0445 0.0536  -0.0165 26  GLU G C     
7760  O O     . GLU G 25  ? 0.4683 0.4806 0.4305 -0.0442 0.0559  -0.0145 26  GLU G O     
7761  C CB    . GLU G 25  ? 0.4710 0.4868 0.4317 -0.0437 0.0483  -0.0166 26  GLU G CB    
7762  C CG    . GLU G 25  ? 0.5058 0.5219 0.4607 -0.0429 0.0488  -0.0149 26  GLU G CG    
7763  C CD    . GLU G 25  ? 0.5666 0.5846 0.5174 -0.0429 0.0462  -0.0161 26  GLU G CD    
7764  O OE1   . GLU G 25  ? 0.5042 0.5233 0.4570 -0.0436 0.0441  -0.0181 26  GLU G OE1   
7765  O OE2   . GLU G 25  ? 0.6266 0.6451 0.5722 -0.0423 0.0464  -0.0151 26  GLU G OE2   
7766  N N     . HIS G 26  ? 0.4263 0.4404 0.3932 -0.0451 0.0537  -0.0193 27  HIS G N     
7767  C CA    . HIS G 26  ? 0.4518 0.4659 0.4186 -0.0455 0.0563  -0.0204 27  HIS G CA    
7768  C C     . HIS G 26  ? 0.4304 0.4445 0.4030 -0.0463 0.0583  -0.0210 27  HIS G C     
7769  O O     . HIS G 26  ? 0.4534 0.4682 0.4276 -0.0467 0.0603  -0.0225 27  HIS G O     
7770  C CB    . HIS G 26  ? 0.4760 0.4911 0.4415 -0.0455 0.0552  -0.0232 27  HIS G CB    
7771  C CG    . HIS G 26  ? 0.5055 0.5208 0.4651 -0.0451 0.0538  -0.0231 27  HIS G CG    
7772  N ND1   . HIS G 26  ? 0.5228 0.5386 0.4814 -0.0451 0.0508  -0.0240 27  HIS G ND1   
7773  C CD2   . HIS G 26  ? 0.5337 0.5489 0.4882 -0.0449 0.0549  -0.0223 27  HIS G CD2   
7774  C CE1   . HIS G 26  ? 0.5737 0.5898 0.5269 -0.0450 0.0500  -0.0240 27  HIS G CE1   
7775  N NE2   . HIS G 26  ? 0.5710 0.5867 0.5214 -0.0447 0.0524  -0.0230 27  HIS G NE2   
7776  N N     . ALA G 27  ? 0.4682 0.4815 0.4440 -0.0465 0.0577  -0.0201 28  ALA G N     
7777  C CA    . ALA G 27  ? 0.4244 0.4376 0.4058 -0.0474 0.0594  -0.0210 28  ALA G CA    
7778  C C     . ALA G 27  ? 0.4124 0.4242 0.3938 -0.0480 0.0629  -0.0191 28  ALA G C     
7779  O O     . ALA G 27  ? 0.3689 0.3788 0.3464 -0.0475 0.0637  -0.0163 28  ALA G O     
7780  C CB    . ALA G 27  ? 0.4406 0.4530 0.4248 -0.0473 0.0576  -0.0208 28  ALA G CB    
7781  N N     . ASP G 28  ? 0.4033 0.4160 0.3890 -0.0492 0.0652  -0.0207 29  ASP G N     
7782  C CA    . ASP G 28  ? 0.4266 0.4378 0.4133 -0.0502 0.0690  -0.0193 29  ASP G CA    
7783  C C     . ASP G 28  ? 0.4354 0.4439 0.4238 -0.0506 0.0695  -0.0174 29  ASP G C     
7784  O O     . ASP G 28  ? 0.4083 0.4139 0.3944 -0.0506 0.0719  -0.0147 29  ASP G O     
7785  C CB    . ASP G 28  ? 0.4594 0.4730 0.4514 -0.0516 0.0712  -0.0218 29  ASP G CB    
7786  C CG    . ASP G 28  ? 0.4726 0.4887 0.4633 -0.0512 0.0716  -0.0235 29  ASP G CG    
7787  O OD1   . ASP G 28  ? 0.5529 0.5684 0.5379 -0.0500 0.0706  -0.0225 29  ASP G OD1   
7788  O OD2   . ASP G 28  ? 0.4990 0.5178 0.4946 -0.0520 0.0729  -0.0259 29  ASP G OD2   
7789  N N     . ILE G 29  ? 0.3968 0.4059 0.3888 -0.0507 0.0672  -0.0190 30  ILE G N     
7790  C CA    . ILE G 29  ? 0.4231 0.4296 0.4172 -0.0511 0.0675  -0.0179 30  ILE G CA    
7791  C C     . ILE G 29  ? 0.4130 0.4202 0.4079 -0.0503 0.0639  -0.0189 30  ILE G C     
7792  O O     . ILE G 29  ? 0.4063 0.4160 0.4027 -0.0501 0.0618  -0.0214 30  ILE G O     
7793  C CB    . ILE G 29  ? 0.4038 0.4102 0.4036 -0.0532 0.0703  -0.0194 30  ILE G CB    
7794  C CG1   . ILE G 29  ? 0.4411 0.4437 0.4423 -0.0538 0.0716  -0.0179 30  ILE G CG1   
7795  C CG2   . ILE G 29  ? 0.3872 0.3974 0.3918 -0.0538 0.0684  -0.0233 30  ILE G CG2   
7796  C CD1   . ILE G 29  ? 0.4437 0.4459 0.4504 -0.0562 0.0747  -0.0196 30  ILE G CD1   
7797  N N     . VAL G 30  ? 0.4172 0.4219 0.4111 -0.0496 0.0634  -0.0168 31  VAL G N     
7798  C CA    . VAL G 30  ? 0.4003 0.4052 0.3946 -0.0487 0.0603  -0.0174 31  VAL G CA    
7799  C C     . VAL G 30  ? 0.4055 0.4080 0.4032 -0.0493 0.0612  -0.0173 31  VAL G C     
7800  O O     . VAL G 30  ? 0.3932 0.3927 0.3904 -0.0494 0.0635  -0.0151 31  VAL G O     
7801  C CB    . VAL G 30  ? 0.4161 0.4210 0.4059 -0.0470 0.0584  -0.0151 31  VAL G CB    
7802  C CG1   . VAL G 30  ? 0.4075 0.4128 0.3981 -0.0462 0.0555  -0.0157 31  VAL G CG1   
7803  C CG2   . VAL G 30  ? 0.4236 0.4306 0.4096 -0.0466 0.0577  -0.0153 31  VAL G CG2   
7804  N N     . PHE G 31  ? 0.3980 0.4017 0.3989 -0.0496 0.0594  -0.0199 32  PHE G N     
7805  C CA    . PHE G 31  ? 0.3746 0.3760 0.3782 -0.0500 0.0596  -0.0202 32  PHE G CA    
7806  C C     . PHE G 31  ? 0.3974 0.3985 0.3993 -0.0484 0.0571  -0.0194 32  PHE G C     
7807  O O     . PHE G 31  ? 0.4773 0.4805 0.4788 -0.0479 0.0546  -0.0209 32  PHE G O     
7808  C CB    . PHE G 31  ? 0.3661 0.3692 0.3743 -0.0515 0.0595  -0.0237 32  PHE G CB    
7809  C CG    . PHE G 31  ? 0.3633 0.3668 0.3743 -0.0534 0.0624  -0.0247 32  PHE G CG    
7810  C CD1   . PHE G 31  ? 0.3707 0.3774 0.3819 -0.0537 0.0628  -0.0257 32  PHE G CD1   
7811  C CD2   . PHE G 31  ? 0.3424 0.3433 0.3562 -0.0550 0.0651  -0.0248 32  PHE G CD2   
7812  C CE1   . PHE G 31  ? 0.3669 0.3744 0.3811 -0.0555 0.0657  -0.0267 32  PHE G CE1   
7813  C CE2   . PHE G 31  ? 0.3409 0.3425 0.3579 -0.0570 0.0680  -0.0258 32  PHE G CE2   
7814  C CZ    . PHE G 31  ? 0.3536 0.3586 0.3708 -0.0573 0.0683  -0.0267 32  PHE G CZ    
7815  N N     . SER G 32  ? 0.3936 0.3918 0.3945 -0.0476 0.0579  -0.0169 33  SER G N     
7816  C CA    . SER G 32  ? 0.4032 0.4014 0.4023 -0.0459 0.0559  -0.0155 33  SER G CA    
7817  C C     . SER G 32  ? 0.3990 0.3950 0.4004 -0.0459 0.0558  -0.0162 33  SER G C     
7818  O O     . SER G 32  ? 0.3933 0.3869 0.3971 -0.0469 0.0578  -0.0168 33  SER G O     
7819  C CB    . SER G 32  ? 0.3669 0.3640 0.3626 -0.0445 0.0565  -0.0120 33  SER G CB    
7820  O OG    . SER G 32  ? 0.3742 0.3675 0.3704 -0.0445 0.0593  -0.0101 33  SER G OG    
7821  N N     . LEU G 33  ? 0.4333 0.4303 0.4342 -0.0447 0.0535  -0.0164 34  LEU G N     
7822  C CA    . LEU G 33  ? 0.4620 0.4570 0.4644 -0.0442 0.0535  -0.0165 34  LEU G CA    
7823  C C     . LEU G 33  ? 0.4605 0.4567 0.4612 -0.0424 0.0516  -0.0149 34  LEU G C     
7824  O O     . LEU G 33  ? 0.5221 0.5199 0.5229 -0.0423 0.0497  -0.0164 34  LEU G O     
7825  C CB    . LEU G 33  ? 0.4928 0.4881 0.4975 -0.0452 0.0527  -0.0199 34  LEU G CB    
7826  C CG    . LEU G 33  ? 0.5557 0.5480 0.5620 -0.0451 0.0534  -0.0205 34  LEU G CG    
7827  C CD1   . LEU G 33  ? 0.5926 0.5857 0.6003 -0.0458 0.0520  -0.0239 34  LEU G CD1   
7828  C CD2   . LEU G 33  ? 0.5575 0.5487 0.5626 -0.0433 0.0530  -0.0182 34  LEU G CD2   
7829  N N     . LEU G 34  ? 0.4652 0.4607 0.4643 -0.0411 0.0523  -0.0118 35  LEU G N     
7830  C CA    . LEU G 34  ? 0.4938 0.4916 0.4916 -0.0395 0.0505  -0.0102 35  LEU G CA    
7831  C C     . LEU G 34  ? 0.5079 0.5039 0.5069 -0.0380 0.0510  -0.0088 35  LEU G C     
7832  O O     . LEU G 34  ? 0.5416 0.5338 0.5416 -0.0380 0.0532  -0.0083 35  LEU G O     
7833  C CB    . LEU G 34  ? 0.5322 0.5315 0.5272 -0.0387 0.0505  -0.0078 35  LEU G CB    
7834  C CG    . LEU G 34  ? 0.5543 0.5552 0.5476 -0.0400 0.0503  -0.0091 35  LEU G CG    
7835  C CD1   . LEU G 34  ? 0.5600 0.5624 0.5499 -0.0390 0.0501  -0.0067 35  LEU G CD1   
7836  C CD2   . LEU G 34  ? 0.5535 0.5570 0.5474 -0.0409 0.0482  -0.0119 35  LEU G CD2   
7837  N N     . PRO G 35  ? 0.5515 0.5499 0.5505 -0.0367 0.0493  -0.0081 36  PRO G N     
7838  C CA    . PRO G 35  ? 0.5556 0.5527 0.5562 -0.0352 0.0498  -0.0071 36  PRO G CA    
7839  C C     . PRO G 35  ? 0.5380 0.5331 0.5380 -0.0332 0.0513  -0.0038 36  PRO G C     
7840  O O     . PRO G 35  ? 0.5508 0.5431 0.5521 -0.0322 0.0527  -0.0031 36  PRO G O     
7841  C CB    . PRO G 35  ? 0.5647 0.5658 0.5656 -0.0347 0.0474  -0.0075 36  PRO G CB    
7842  C CG    . PRO G 35  ? 0.5695 0.5731 0.5691 -0.0364 0.0459  -0.0094 36  PRO G CG    
7843  C CD    . PRO G 35  ? 0.5517 0.5543 0.5496 -0.0369 0.0469  -0.0087 36  PRO G CD    
7844  N N     . ASP G 36  ? 0.4947 0.4913 0.4924 -0.0325 0.0511  -0.0017 37  ASP G N     
7845  C CA    . ASP G 36  ? 0.5147 0.5100 0.5113 -0.0300 0.0522  0.0018  37  ASP G CA    
7846  C C     . ASP G 36  ? 0.4627 0.4576 0.4560 -0.0300 0.0529  0.0036  37  ASP G C     
7847  O O     . ASP G 36  ? 0.4722 0.4679 0.4646 -0.0320 0.0527  0.0019  37  ASP G O     
7848  C CB    . ASP G 36  ? 0.5725 0.5718 0.5696 -0.0278 0.0502  0.0033  37  ASP G CB    
7849  C CG    . ASP G 36  ? 0.6299 0.6350 0.6262 -0.0284 0.0472  0.0024  37  ASP G CG    
7850  O OD1   . ASP G 36  ? 0.6620 0.6684 0.6554 -0.0286 0.0467  0.0032  37  ASP G OD1   
7851  O OD2   . ASP G 36  ? 0.7741 0.7821 0.7724 -0.0288 0.0456  0.0008  37  ASP G OD2   
7852  N N     . GLY G 37  ? 0.4584 0.4521 0.4499 -0.0275 0.0539  0.0071  38  GLY G N     
7853  C CA    . GLY G 37  ? 0.4685 0.4610 0.4563 -0.0270 0.0551  0.0093  38  GLY G CA    
7854  C C     . GLY G 37  ? 0.4728 0.4707 0.4579 -0.0262 0.0522  0.0099  38  GLY G C     
7855  O O     . GLY G 37  ? 0.4273 0.4251 0.4090 -0.0265 0.0527  0.0108  38  GLY G O     
7856  N N     . PHE G 38  ? 0.4849 0.4876 0.4714 -0.0254 0.0493  0.0094  39  PHE G N     
7857  C CA    . PHE G 38  ? 0.4705 0.4789 0.4550 -0.0251 0.0464  0.0092  39  PHE G CA    
7858  C C     . PHE G 38  ? 0.4326 0.4420 0.4166 -0.0282 0.0458  0.0060  39  PHE G C     
7859  O O     . PHE G 38  ? 0.4151 0.4263 0.3958 -0.0285 0.0450  0.0062  39  PHE G O     
7860  C CB    . PHE G 38  ? 0.4727 0.4861 0.4597 -0.0239 0.0437  0.0090  39  PHE G CB    
7861  C CG    . PHE G 38  ? 0.4632 0.4770 0.4505 -0.0204 0.0438  0.0124  39  PHE G CG    
7862  C CD1   . PHE G 38  ? 0.4908 0.5068 0.4746 -0.0178 0.0428  0.0153  39  PHE G CD1   
7863  C CD2   . PHE G 38  ? 0.4530 0.4650 0.4439 -0.0193 0.0449  0.0126  39  PHE G CD2   
7864  C CE1   . PHE G 38  ? 0.5018 0.5184 0.4859 -0.0141 0.0428  0.0185  39  PHE G CE1   
7865  C CE2   . PHE G 38  ? 0.4830 0.4953 0.4742 -0.0158 0.0451  0.0158  39  PHE G CE2   
7866  C CZ    . PHE G 38  ? 0.5085 0.5233 0.4965 -0.0131 0.0440  0.0187  39  PHE G CZ    
7867  N N     . SER G 39  ? 0.4258 0.4339 0.4129 -0.0302 0.0461  0.0032  40  SER G N     
7868  C CA    . SER G 39  ? 0.4153 0.4240 0.4023 -0.0328 0.0457  0.0002  40  SER G CA    
7869  C C     . SER G 39  ? 0.3960 0.4014 0.3812 -0.0337 0.0482  0.0004  40  SER G C     
7870  O O     . SER G 39  ? 0.3574 0.3639 0.3411 -0.0352 0.0479  -0.0012 40  SER G O     
7871  C CB    . SER G 39  ? 0.4000 0.4080 0.3905 -0.0342 0.0456  -0.0026 40  SER G CB    
7872  O OG    . SER G 39  ? 0.4562 0.4643 0.4464 -0.0364 0.0453  -0.0054 40  SER G OG    
7873  N N     . GLN G 40  ? 0.4123 0.4134 0.3976 -0.0329 0.0508  0.0025  41  GLN G N     
7874  C CA    . GLN G 40  ? 0.4315 0.4291 0.4157 -0.0340 0.0537  0.0027  41  GLN G CA    
7875  C C     . GLN G 40  ? 0.4404 0.4389 0.4199 -0.0330 0.0538  0.0050  41  GLN G C     
7876  O O     . GLN G 40  ? 0.4672 0.4654 0.4452 -0.0344 0.0549  0.0041  41  GLN G O     
7877  C CB    . GLN G 40  ? 0.4633 0.4557 0.4490 -0.0335 0.0566  0.0042  41  GLN G CB    
7878  C CG    . GLN G 40  ? 0.4458 0.4346 0.4322 -0.0356 0.0598  0.0033  41  GLN G CG    
7879  C CD    . GLN G 40  ? 0.4407 0.4310 0.4302 -0.0382 0.0591  -0.0008 41  GLN G CD    
7880  O OE1   . GLN G 40  ? 0.4555 0.4460 0.4478 -0.0387 0.0580  -0.0028 41  GLN G OE1   
7881  N NE2   . GLN G 40  ? 0.4409 0.4321 0.4296 -0.0398 0.0598  -0.0020 41  GLN G NE2   
7882  N N     A ARG G 41  ? 0.4475 0.4472 0.4247 -0.0303 0.0527  0.0079  42  ARG G N     
7883  N N     B ARG G 41  ? 0.4439 0.4437 0.4211 -0.0303 0.0527  0.0079  42  ARG G N     
7884  C CA    A ARG G 41  ? 0.5010 0.5020 0.4732 -0.0289 0.0525  0.0102  42  ARG G CA    
7885  C CA    B ARG G 41  ? 0.4944 0.4953 0.4665 -0.0289 0.0525  0.0102  42  ARG G CA    
7886  C C     A ARG G 41  ? 0.4569 0.4623 0.4276 -0.0303 0.0500  0.0077  42  ARG G C     
7887  C C     B ARG G 41  ? 0.4534 0.4589 0.4241 -0.0303 0.0500  0.0078  42  ARG G C     
7888  O O     A ARG G 41  ? 0.4295 0.4346 0.3969 -0.0310 0.0510  0.0077  42  ARG G O     
7889  O O     B ARG G 41  ? 0.4273 0.4325 0.3945 -0.0309 0.0509  0.0078  42  ARG G O     
7890  C CB    A ARG G 41  ? 0.5423 0.5447 0.5126 -0.0254 0.0511  0.0135  42  ARG G CB    
7891  C CB    B ARG G 41  ? 0.5289 0.5310 0.4991 -0.0254 0.0513  0.0136  42  ARG G CB    
7892  C CG    A ARG G 41  ? 0.6078 0.6049 0.5776 -0.0234 0.0541  0.0169  42  ARG G CG    
7893  C CG    B ARG G 41  ? 0.5876 0.5841 0.5571 -0.0235 0.0546  0.0170  42  ARG G CG    
7894  C CD    A ARG G 41  ? 0.6528 0.6517 0.6198 -0.0195 0.0528  0.0205  42  ARG G CD    
7895  C CD    B ARG G 41  ? 0.6225 0.6204 0.5893 -0.0196 0.0533  0.0207  42  ARG G CD    
7896  N NE    A ARG G 41  ? 0.6649 0.6579 0.6304 -0.0172 0.0560  0.0241  42  ARG G NE    
7897  N NE    B ARG G 41  ? 0.6126 0.6139 0.5832 -0.0183 0.0509  0.0202  42  ARG G NE    
7898  C CZ    A ARG G 41  ? 0.6919 0.6840 0.6587 -0.0143 0.0560  0.0264  42  ARG G CZ    
7899  C CZ    B ARG G 41  ? 0.6120 0.6106 0.5868 -0.0185 0.0522  0.0196  42  ARG G CZ    
7900  N NH1   A ARG G 41  ? 0.7038 0.7012 0.6738 -0.0135 0.0528  0.0253  42  ARG G NH1   
7901  N NH1   B ARG G 41  ? 0.5920 0.5940 0.5700 -0.0173 0.0502  0.0193  42  ARG G NH1   
7902  N NH2   A ARG G 41  ? 0.6943 0.6802 0.6594 -0.0123 0.0594  0.0296  42  ARG G NH2   
7903  N NH2   B ARG G 41  ? 0.6247 0.6172 0.6005 -0.0201 0.0557  0.0192  42  ARG G NH2   
7904  N N     . TRP G 42  ? 0.4425 0.4518 0.4156 -0.0308 0.0471  0.0056  43  TRP G N     
7905  C CA    . TRP G 42  ? 0.4149 0.4281 0.3868 -0.0322 0.0448  0.0031  43  TRP G CA    
7906  C C     . TRP G 42  ? 0.4216 0.4329 0.3932 -0.0345 0.0465  0.0009  43  TRP G C     
7907  O O     . TRP G 42  ? 0.4525 0.4651 0.4207 -0.0349 0.0462  0.0004  43  TRP G O     
7908  C CB    . TRP G 42  ? 0.3981 0.4144 0.3737 -0.0329 0.0423  0.0008  43  TRP G CB    
7909  C CG    . TRP G 42  ? 0.3645 0.3831 0.3397 -0.0350 0.0407  -0.0025 43  TRP G CG    
7910  C CD1   . TRP G 42  ? 0.3549 0.3773 0.3273 -0.0352 0.0385  -0.0032 43  TRP G CD1   
7911  C CD2   . TRP G 42  ? 0.3591 0.3764 0.3367 -0.0371 0.0413  -0.0055 43  TRP G CD2   
7912  N NE1   . TRP G 42  ? 0.3558 0.3786 0.3285 -0.0373 0.0379  -0.0064 43  TRP G NE1   
7913  C CE2   . TRP G 42  ? 0.3519 0.3717 0.3278 -0.0383 0.0395  -0.0077 43  TRP G CE2   
7914  C CE3   . TRP G 42  ? 0.3382 0.3525 0.3190 -0.0380 0.0429  -0.0066 43  TRP G CE3   
7915  C CZ2   . TRP G 42  ? 0.3537 0.3729 0.3309 -0.0401 0.0396  -0.0107 43  TRP G CZ2   
7916  C CZ3   . TRP G 42  ? 0.3678 0.3819 0.3499 -0.0397 0.0427  -0.0096 43  TRP G CZ3   
7917  C CH2   . TRP G 42  ? 0.3609 0.3773 0.3412 -0.0406 0.0411  -0.0115 43  TRP G CH2   
7918  N N     . LEU G 43  ? 0.3973 0.4057 0.3726 -0.0358 0.0483  -0.0004 44  LEU G N     
7919  C CA    . LEU G 43  ? 0.4036 0.4108 0.3796 -0.0379 0.0499  -0.0027 44  LEU G CA    
7920  C C     . LEU G 43  ? 0.3931 0.3982 0.3659 -0.0377 0.0525  -0.0010 44  LEU G C     
7921  O O     . LEU G 43  ? 0.3335 0.3393 0.3045 -0.0388 0.0530  -0.0023 44  LEU G O     
7922  C CB    . LEU G 43  ? 0.4076 0.4125 0.3883 -0.0391 0.0511  -0.0044 44  LEU G CB    
7923  C CG    . LEU G 43  ? 0.4257 0.4298 0.4080 -0.0411 0.0527  -0.0069 44  LEU G CG    
7924  C CD1   . LEU G 43  ? 0.4518 0.4589 0.4338 -0.0419 0.0506  -0.0096 44  LEU G CD1   
7925  C CD2   . LEU G 43  ? 0.4401 0.4419 0.4268 -0.0420 0.0540  -0.0082 44  LEU G CD2   
7926  N N     . THR G 44  ? 0.4283 0.4303 0.4001 -0.0363 0.0545  0.0021  45  THR G N     
7927  C CA    . THR G 44  ? 0.4942 0.4932 0.4630 -0.0362 0.0577  0.0042  45  THR G CA    
7928  C C     . THR G 44  ? 0.4783 0.4795 0.4415 -0.0353 0.0567  0.0051  45  THR G C     
7929  O O     . THR G 44  ? 0.4883 0.4884 0.4492 -0.0361 0.0588  0.0051  45  THR G O     
7930  C CB    . THR G 44  ? 0.5100 0.5049 0.4784 -0.0345 0.0599  0.0076  45  THR G CB    
7931  O OG1   . THR G 44  ? 0.5383 0.5309 0.5119 -0.0359 0.0611  0.0060  45  THR G OG1   
7932  C CG2   . THR G 44  ? 0.5278 0.5191 0.4923 -0.0340 0.0634  0.0102  45  THR G CG2   
7933  N N     . LYS G 45  ? 0.5125 0.5172 0.4737 -0.0336 0.0534  0.0058  46  LYS G N     
7934  C CA    . LYS G 45  ? 0.5206 0.5278 0.4762 -0.0326 0.0520  0.0065  46  LYS G CA    
7935  C C     . LYS G 45  ? 0.4720 0.4816 0.4277 -0.0348 0.0509  0.0029  46  LYS G C     
7936  O O     . LYS G 45  ? 0.4810 0.4915 0.4321 -0.0347 0.0510  0.0028  46  LYS G O     
7937  C CB    . LYS G 45  ? 0.5957 0.6064 0.5498 -0.0304 0.0486  0.0080  46  LYS G CB    
7938  C CG    . LYS G 45  ? 0.6949 0.7035 0.6483 -0.0276 0.0495  0.0119  46  LYS G CG    
7939  C CD    . LYS G 45  ? 0.8024 0.8154 0.7542 -0.0251 0.0460  0.0134  46  LYS G CD    
7940  C CE    . LYS G 45  ? 0.8813 0.8972 0.8269 -0.0242 0.0443  0.0138  46  LYS G CE    
7941  N NZ    . LYS G 45  ? 0.9179 0.9388 0.8625 -0.0217 0.0407  0.0151  46  LYS G NZ    
7942  N N     . LEU G 46  ? 0.4370 0.4474 0.3976 -0.0365 0.0500  -0.0001 47  LEU G N     
7943  C CA    . LEU G 46  ? 0.4550 0.4672 0.4160 -0.0383 0.0491  -0.0035 47  LEU G CA    
7944  C C     . LEU G 46  ? 0.4929 0.5028 0.4542 -0.0396 0.0523  -0.0044 47  LEU G C     
7945  O O     . LEU G 46  ? 0.5427 0.5536 0.5017 -0.0403 0.0526  -0.0059 47  LEU G O     
7946  C CB    . LEU G 46  ? 0.4953 0.5088 0.4610 -0.0392 0.0472  -0.0060 47  LEU G CB    
7947  C CG    . LEU G 46  ? 0.5038 0.5198 0.4691 -0.0404 0.0452  -0.0092 47  LEU G CG    
7948  C CD1   . LEU G 46  ? 0.5079 0.5240 0.4778 -0.0414 0.0441  -0.0113 47  LEU G CD1   
7949  C CD2   . LEU G 46  ? 0.5551 0.5704 0.5183 -0.0414 0.0468  -0.0106 47  LEU G CD2   
7950  N N     . ASN G 47  ? 0.5022 0.5092 0.4668 -0.0400 0.0549  -0.0035 48  ASN G N     
7951  C CA    . ASN G 47  ? 0.4661 0.4712 0.4321 -0.0414 0.0582  -0.0043 48  ASN G CA    
7952  C C     . ASN G 47  ? 0.5407 0.5419 0.5082 -0.0412 0.0612  -0.0019 48  ASN G C     
7953  O O     . ASN G 47  ? 0.5123 0.5125 0.4837 -0.0414 0.0610  -0.0022 48  ASN G O     
7954  C CB    . ASN G 47  ? 0.4431 0.4496 0.4136 -0.0431 0.0577  -0.0080 48  ASN G CB    
7955  C CG    . ASN G 47  ? 0.4043 0.4100 0.3763 -0.0445 0.0608  -0.0091 48  ASN G CG    
7956  O OD1   . ASN G 47  ? 0.4020 0.4051 0.3751 -0.0449 0.0639  -0.0077 48  ASN G OD1   
7957  N ND2   . ASN G 47  ? 0.3509 0.3588 0.3231 -0.0452 0.0603  -0.0118 48  ASN G ND2   
7958  N N     . PRO G 48  ? 0.5791 0.5779 0.5433 -0.0409 0.0643  0.0004  49  PRO G N     
7959  C CA    . PRO G 48  ? 0.6102 0.6046 0.5752 -0.0406 0.0675  0.0030  49  PRO G CA    
7960  C C     . PRO G 48  ? 0.6237 0.6163 0.5946 -0.0429 0.0701  0.0010  49  PRO G C     
7961  O O     . PRO G 48  ? 0.5975 0.5868 0.5706 -0.0430 0.0718  0.0023  49  PRO G O     
7962  C CB    . PRO G 48  ? 0.6353 0.6278 0.5943 -0.0396 0.0701  0.0058  49  PRO G CB    
7963  C CG    . PRO G 48  ? 0.6334 0.6289 0.5911 -0.0407 0.0697  0.0033  49  PRO G CG    
7964  C CD    . PRO G 48  ? 0.6504 0.6500 0.6098 -0.0407 0.0652  0.0006  49  PRO G CD    
7965  N N     . ASN G 49  ? 0.5821 0.5771 0.5557 -0.0448 0.0703  -0.0022 50  ASN G N     
7966  C CA    . ASN G 49  ? 0.6045 0.5987 0.5838 -0.0471 0.0725  -0.0044 50  ASN G CA    
7967  C C     . ASN G 49  ? 0.5472 0.5427 0.5312 -0.0475 0.0699  -0.0067 50  ASN G C     
7968  O O     . ASN G 49  ? 0.4816 0.4804 0.4681 -0.0482 0.0678  -0.0098 50  ASN G O     
7969  C CB    . ASN G 49  ? 0.6719 0.6687 0.6525 -0.0486 0.0738  -0.0069 50  ASN G CB    
7970  C CG    . ASN G 49  ? 0.7407 0.7371 0.7273 -0.0510 0.0766  -0.0090 50  ASN G CG    
7971  O OD1   . ASN G 49  ? 0.7908 0.7844 0.7802 -0.0518 0.0779  -0.0084 50  ASN G OD1   
7972  N ND2   . ASN G 49  ? 0.7578 0.7572 0.7467 -0.0523 0.0775  -0.0115 50  ASN G ND2   
7973  N N     . VAL G 50  ? 0.5608 0.5534 0.5457 -0.0469 0.0701  -0.0051 51  VAL G N     
7974  C CA    . VAL G 50  ? 0.5124 0.5057 0.5008 -0.0470 0.0677  -0.0069 51  VAL G CA    
7975  C C     . VAL G 50  ? 0.4940 0.4838 0.4864 -0.0483 0.0703  -0.0073 51  VAL G C     
7976  O O     . VAL G 50  ? 0.4972 0.4828 0.4882 -0.0480 0.0732  -0.0046 51  VAL G O     
7977  C CB    . VAL G 50  ? 0.5388 0.5325 0.5245 -0.0446 0.0649  -0.0050 51  VAL G CB    
7978  C CG1   . VAL G 50  ? 0.5558 0.5494 0.5450 -0.0446 0.0631  -0.0064 51  VAL G CG1   
7979  C CG2   . VAL G 50  ? 0.5364 0.5338 0.5186 -0.0437 0.0621  -0.0052 51  VAL G CG2   
7980  N N     . ILE G 51  ? 0.5037 0.4950 0.5008 -0.0498 0.0692  -0.0107 52  ILE G N     
7981  C CA    . ILE G 51  ? 0.4855 0.4739 0.4865 -0.0511 0.0708  -0.0116 52  ILE G CA    
7982  C C     . ILE G 51  ? 0.4485 0.4374 0.4505 -0.0501 0.0678  -0.0126 52  ILE G C     
7983  O O     . ILE G 51  ? 0.3921 0.3845 0.3949 -0.0499 0.0649  -0.0148 52  ILE G O     
7984  C CB    . ILE G 51  ? 0.5229 0.5129 0.5288 -0.0538 0.0724  -0.0150 52  ILE G CB    
7985  C CG1   . ILE G 51  ? 0.5546 0.5440 0.5599 -0.0550 0.0759  -0.0141 52  ILE G CG1   
7986  C CG2   . ILE G 51  ? 0.4942 0.4816 0.5042 -0.0554 0.0735  -0.0167 52  ILE G CG2   
7987  C CD1   . ILE G 51  ? 0.6149 0.6073 0.6165 -0.0539 0.0749  -0.0134 52  ILE G CD1   
7988  N N     . ASN G 52  ? 0.4130 0.3978 0.4147 -0.0493 0.0689  -0.0107 53  ASN G N     
7989  C CA    . ASN G 52  ? 0.4146 0.3994 0.4170 -0.0481 0.0665  -0.0112 53  ASN G CA    
7990  C C     . ASN G 52  ? 0.4287 0.4128 0.4355 -0.0500 0.0668  -0.0147 53  ASN G C     
7991  O O     . ASN G 52  ? 0.4438 0.4246 0.4526 -0.0515 0.0697  -0.0150 53  ASN G O     
7992  C CB    . ASN G 52  ? 0.4256 0.4068 0.4254 -0.0459 0.0674  -0.0076 53  ASN G CB    
7993  C CG    . ASN G 52  ? 0.4102 0.3918 0.4107 -0.0445 0.0650  -0.0079 53  ASN G CG    
7994  O OD1   . ASN G 52  ? 0.4267 0.4104 0.4295 -0.0453 0.0631  -0.0110 53  ASN G OD1   
7995  N ND2   . ASN G 52  ? 0.4638 0.4434 0.4623 -0.0421 0.0653  -0.0048 53  ASN G ND2   
7996  N N     . LEU G 53  ? 0.4209 0.4082 0.4289 -0.0499 0.0637  -0.0172 54  LEU G N     
7997  C CA    . LEU G 53  ? 0.4351 0.4225 0.4467 -0.0514 0.0634  -0.0207 54  LEU G CA    
7998  C C     . LEU G 53  ? 0.4566 0.4399 0.4687 -0.0508 0.0642  -0.0202 54  LEU G C     
7999  O O     . LEU G 53  ? 0.4193 0.4016 0.4341 -0.0522 0.0645  -0.0229 54  LEU G O     
8000  C CB    . LEU G 53  ? 0.4277 0.4194 0.4396 -0.0509 0.0600  -0.0232 54  LEU G CB    
8001  C CG    . LEU G 53  ? 0.4461 0.4418 0.4579 -0.0514 0.0592  -0.0243 54  LEU G CG    
8002  C CD1   . LEU G 53  ? 0.4446 0.4436 0.4562 -0.0506 0.0559  -0.0265 54  LEU G CD1   
8003  C CD2   . LEU G 53  ? 0.4446 0.4410 0.4599 -0.0537 0.0614  -0.0262 54  LEU G CD2   
8004  N N     . GLN G 54  ? 0.4852 0.4663 0.4945 -0.0487 0.0645  -0.0167 55  GLN G N     
8005  C CA    . GLN G 54  ? 0.6116 0.5889 0.6209 -0.0477 0.0651  -0.0158 55  GLN G CA    
8006  C C     . GLN G 54  ? 0.5734 0.5460 0.5847 -0.0494 0.0686  -0.0165 55  GLN G C     
8007  O O     . GLN G 54  ? 0.6233 0.5924 0.6355 -0.0493 0.0694  -0.0171 55  GLN G O     
8008  C CB    . GLN G 54  ? 0.7179 0.6943 0.7239 -0.0449 0.0651  -0.0117 55  GLN G CB    
8009  C CG    . GLN G 54  ? 0.7812 0.7553 0.7872 -0.0431 0.0648  -0.0108 55  GLN G CG    
8010  C CD    . GLN G 54  ? 0.8492 0.8267 0.8557 -0.0425 0.0617  -0.0128 55  GLN G CD    
8011  O OE1   . GLN G 54  ? 0.8785 0.8546 0.8865 -0.0430 0.0615  -0.0150 55  GLN G OE1   
8012  N NE2   . GLN G 54  ? 0.9063 0.8880 0.9112 -0.0416 0.0593  -0.0120 55  GLN G NE2   
8013  N N     . GLN G 55  ? 0.5288 0.5010 0.5409 -0.0513 0.0708  -0.0165 56  GLN G N     
8014  C CA    . GLN G 55  ? 0.5239 0.4911 0.5378 -0.0532 0.0747  -0.0167 56  GLN G CA    
8015  C C     . GLN G 55  ? 0.5038 0.4714 0.5218 -0.0558 0.0746  -0.0213 56  GLN G C     
8016  O O     . GLN G 55  ? 0.4204 0.3835 0.4403 -0.0575 0.0775  -0.0221 56  GLN G O     
8017  C CB    . GLN G 55  ? 0.5667 0.5339 0.5803 -0.0544 0.0773  -0.0154 56  GLN G CB    
8018  C CG    . GLN G 55  ? 0.5855 0.5585 0.6012 -0.0561 0.0757  -0.0183 56  GLN G CG    
8019  C CD    . GLN G 55  ? 0.6483 0.6211 0.6638 -0.0574 0.0786  -0.0171 56  GLN G CD    
8020  O OE1   . GLN G 55  ? 0.6235 0.5929 0.6411 -0.0596 0.0823  -0.0175 56  GLN G OE1   
8021  N NE2   . GLN G 55  ? 0.6718 0.6481 0.6846 -0.0561 0.0772  -0.0157 56  GLN G NE2   
8022  N N     . PHE G 56  ? 0.4403 0.4131 0.4596 -0.0560 0.0712  -0.0242 57  PHE G N     
8023  C CA    . PHE G 56  ? 0.4608 0.4350 0.4839 -0.0583 0.0706  -0.0288 57  PHE G CA    
8024  C C     . PHE G 56  ? 0.4578 0.4300 0.4804 -0.0574 0.0692  -0.0301 57  PHE G C     
8025  O O     . PHE G 56  ? 0.4114 0.3846 0.4365 -0.0589 0.0683  -0.0339 57  PHE G O     
8026  C CB    . PHE G 56  ? 0.4727 0.4535 0.4973 -0.0588 0.0678  -0.0313 57  PHE G CB    
8027  C CG    . PHE G 56  ? 0.4906 0.4735 0.5162 -0.0601 0.0695  -0.0307 57  PHE G CG    
8028  C CD1   . PHE G 56  ? 0.5138 0.4960 0.5433 -0.0631 0.0724  -0.0327 57  PHE G CD1   
8029  C CD2   . PHE G 56  ? 0.5290 0.5146 0.5518 -0.0585 0.0684  -0.0285 57  PHE G CD2   
8030  C CE1   . PHE G 56  ? 0.5127 0.4969 0.5433 -0.0644 0.0743  -0.0321 57  PHE G CE1   
8031  C CE2   . PHE G 56  ? 0.5177 0.5050 0.5413 -0.0597 0.0702  -0.0281 57  PHE G CE2   
8032  C CZ    . PHE G 56  ? 0.5204 0.5071 0.5478 -0.0625 0.0732  -0.0298 57  PHE G CZ    
8033  N N     . TYR G 57  ? 0.4691 0.4387 0.4887 -0.0548 0.0691  -0.0269 58  TYR G N     
8034  C CA    . TYR G 57  ? 0.4697 0.4370 0.4886 -0.0536 0.0682  -0.0277 58  TYR G CA    
8035  C C     . TYR G 57  ? 0.5091 0.4701 0.5291 -0.0548 0.0717  -0.0280 58  TYR G C     
8036  O O     . TYR G 57  ? 0.4949 0.4528 0.5155 -0.0559 0.0748  -0.0266 58  TYR G O     
8037  C CB    . TYR G 57  ? 0.4687 0.4363 0.4845 -0.0504 0.0668  -0.0244 58  TYR G CB    
8038  C CG    . TYR G 57  ? 0.4649 0.4378 0.4796 -0.0493 0.0632  -0.0252 58  TYR G CG    
8039  C CD1   . TYR G 57  ? 0.4592 0.4335 0.4741 -0.0491 0.0610  -0.0280 58  TYR G CD1   
8040  C CD2   . TYR G 57  ? 0.4667 0.4430 0.4798 -0.0483 0.0620  -0.0231 58  TYR G CD2   
8041  C CE1   . TYR G 57  ? 0.5005 0.4791 0.5142 -0.0481 0.0580  -0.0285 58  TYR G CE1   
8042  C CE2   . TYR G 57  ? 0.5168 0.4974 0.5289 -0.0475 0.0590  -0.0238 58  TYR G CE2   
8043  C CZ    . TYR G 57  ? 0.5041 0.4856 0.5165 -0.0474 0.0571  -0.0265 58  TYR G CZ    
8044  O OH    . TYR G 57  ? 0.5182 0.5034 0.5294 -0.0465 0.0544  -0.0271 58  TYR G OH    
8045  N N     . ALA G 58  ? 0.5306 0.4895 0.5507 -0.0545 0.0712  -0.0300 59  ALA G N     
8046  C CA    . ALA G 58  ? 0.5738 0.5262 0.5945 -0.0554 0.0744  -0.0305 59  ALA G CA    
8047  C C     . ALA G 58  ? 0.5624 0.5100 0.5816 -0.0542 0.0777  -0.0260 59  ALA G C     
8048  O O     . ALA G 58  ? 0.4719 0.4196 0.4884 -0.0511 0.0771  -0.0223 59  ALA G O     
8049  C CB    . ALA G 58  ? 0.5930 0.5435 0.6124 -0.0539 0.0733  -0.0316 59  ALA G CB    
8050  N N     . GLN G 59  ? 0.6155 0.5588 0.6363 -0.0566 0.0813  -0.0265 60  GLN G N     
8051  C CA    . GLN G 59  ? 0.7450 0.6834 0.7641 -0.0557 0.0849  -0.0223 60  GLN G CA    
8052  C C     . GLN G 59  ? 0.8403 0.7732 0.8569 -0.0526 0.0862  -0.0194 60  GLN G C     
8053  O O     . GLN G 59  ? 0.9082 0.8426 0.9222 -0.0492 0.0848  -0.0159 60  GLN G O     
8054  C CB    . GLN G 59  ? 0.8298 0.7644 0.8516 -0.0595 0.0887  -0.0242 60  GLN G CB    
8055  C CG    . GLN G 59  ? 0.8627 0.7927 0.8828 -0.0591 0.0927  -0.0200 60  GLN G CG    
8056  C CD    . GLN G 59  ? 0.8744 0.7997 0.8974 -0.0630 0.0970  -0.0221 60  GLN G CD    
8057  O OE1   . GLN G 59  ? 0.9319 0.8583 0.9560 -0.0650 0.0987  -0.0218 60  GLN G OE1   
8058  N NE2   . GLN G 59  ? 0.8809 0.8006 0.9050 -0.0643 0.0989  -0.0243 60  GLN G NE2   
8059  N N     . ASN G 60  ? 0.8627 0.7893 0.8802 -0.0538 0.0890  -0.0211 61  ASN G N     
8060  C CA    . ASN G 60  ? 0.8752 0.7959 0.8906 -0.0509 0.0909  -0.0186 61  ASN G CA    
8061  C C     . ASN G 60  ? 0.7957 0.7127 0.8125 -0.0526 0.0916  -0.0227 61  ASN G C     
8062  O O     . ASN G 60  ? 0.8602 0.7729 0.8789 -0.0558 0.0945  -0.0253 61  ASN G O     
8063  C CB    . ASN G 60  ? 0.9221 0.8364 0.9357 -0.0499 0.0951  -0.0143 61  ASN G CB    
8064  C CG    . ASN G 60  ? 0.9514 0.8632 0.9668 -0.0538 0.0983  -0.0158 61  ASN G CG    
8065  O OD1   . ASN G 60  ? 0.9878 0.9023 1.0066 -0.0575 0.0974  -0.0205 61  ASN G OD1   
8066  N ND2   . ASN G 60  ? 0.8944 0.8013 0.9079 -0.0530 0.1019  -0.0118 61  ASN G ND2   
8067  N N     . GLY G 61  ? 0.6502 0.5689 0.6659 -0.0503 0.0892  -0.0234 62  GLY G N     
8068  C CA    . GLY G 61  ? 0.6100 0.5257 0.6264 -0.0515 0.0895  -0.0273 62  GLY G CA    
8069  C C     . GLY G 61  ? 0.5395 0.4575 0.5588 -0.0559 0.0886  -0.0327 62  GLY G C     
8070  O O     . GLY G 61  ? 0.5626 0.4772 0.5828 -0.0578 0.0897  -0.0365 62  GLY G O     
8071  N N     . GLU G 62  ? 0.5708 0.4949 0.5917 -0.0574 0.0867  -0.0331 63  GLU G N     
8072  C CA    . GLU G 62  ? 0.5493 0.4767 0.5735 -0.0614 0.0858  -0.0380 63  GLU G CA    
8073  C C     . GLU G 62  ? 0.4862 0.4193 0.5103 -0.0611 0.0814  -0.0415 63  GLU G C     
8074  O O     . GLU G 62  ? 0.4302 0.3676 0.4523 -0.0584 0.0785  -0.0395 63  GLU G O     
8075  C CB    . GLU G 62  ? 0.5997 0.5312 0.6256 -0.0629 0.0858  -0.0369 63  GLU G CB    
8076  C CG    . GLU G 62  ? 0.6635 0.5995 0.6935 -0.0669 0.0848  -0.0419 63  GLU G CG    
8077  C CD    . GLU G 62  ? 0.7422 0.6840 0.7737 -0.0677 0.0839  -0.0410 63  GLU G CD    
8078  O OE1   . GLU G 62  ? 0.7600 0.7021 0.7890 -0.0653 0.0841  -0.0365 63  GLU G OE1   
8079  O OE2   . GLU G 62  ? 0.7897 0.7359 0.8249 -0.0707 0.0829  -0.0450 63  GLU G OE2   
8080  N N     . VAL G 63  ? 0.4634 0.3967 0.4895 -0.0640 0.0809  -0.0466 64  VAL G N     
8081  C CA    . VAL G 63  ? 0.4547 0.3934 0.4805 -0.0638 0.0768  -0.0502 64  VAL G CA    
8082  C C     . VAL G 63  ? 0.4365 0.3827 0.4649 -0.0655 0.0742  -0.0519 64  VAL G C     
8083  O O     . VAL G 63  ? 0.3861 0.3336 0.4183 -0.0689 0.0751  -0.0551 64  VAL G O     
8084  C CB    . VAL G 63  ? 0.4715 0.4071 0.4978 -0.0658 0.0772  -0.0552 64  VAL G CB    
8085  C CG1   . VAL G 63  ? 0.4745 0.4162 0.5004 -0.0657 0.0727  -0.0591 64  VAL G CG1   
8086  C CG2   . VAL G 63  ? 0.4572 0.3852 0.4806 -0.0639 0.0797  -0.0536 64  VAL G CG2   
8087  N N     . LYS G 64  ? 0.4230 0.3744 0.4498 -0.0630 0.0713  -0.0497 65  LYS G N     
8088  C CA    . LYS G 64  ? 0.4367 0.3950 0.4654 -0.0638 0.0690  -0.0506 65  LYS G CA    
8089  C C     . LYS G 64  ? 0.4424 0.4058 0.4688 -0.0614 0.0647  -0.0510 65  LYS G C     
8090  O O     . LYS G 64  ? 0.3864 0.3489 0.4096 -0.0585 0.0640  -0.0480 65  LYS G O     
8091  C CB    . LYS G 64  ? 0.4615 0.4198 0.4903 -0.0634 0.0708  -0.0463 65  LYS G CB    
8092  C CG    . LYS G 64  ? 0.4750 0.4400 0.5059 -0.0643 0.0691  -0.0469 65  LYS G CG    
8093  C CD    . LYS G 64  ? 0.4732 0.4376 0.5038 -0.0640 0.0713  -0.0428 65  LYS G CD    
8094  C CE    . LYS G 64  ? 0.4688 0.4392 0.5019 -0.0654 0.0702  -0.0440 65  LYS G CE    
8095  N NZ    . LYS G 64  ? 0.4885 0.4579 0.5210 -0.0652 0.0727  -0.0402 65  LYS G NZ    
8096  N N     . ASN G 65  ? 0.4639 0.4328 0.4922 -0.0627 0.0620  -0.0548 66  ASN G N     
8097  C CA    . ASN G 65  ? 0.5157 0.4892 0.5417 -0.0605 0.0581  -0.0554 66  ASN G CA    
8098  C C     . ASN G 65  ? 0.5074 0.4845 0.5328 -0.0590 0.0572  -0.0522 66  ASN G C     
8099  O O     . ASN G 65  ? 0.5408 0.5201 0.5690 -0.0606 0.0583  -0.0518 66  ASN G O     
8100  C CB    . ASN G 65  ? 0.5256 0.5035 0.5535 -0.0620 0.0556  -0.0605 66  ASN G CB    
8101  C CG    . ASN G 65  ? 0.5349 0.5162 0.5595 -0.0593 0.0518  -0.0612 66  ASN G CG    
8102  O OD1   . ASN G 65  ? 0.5813 0.5655 0.6045 -0.0574 0.0504  -0.0589 66  ASN G OD1   
8103  N ND2   . ASN G 65  ? 0.5587 0.5392 0.5817 -0.0592 0.0504  -0.0645 66  ASN G ND2   
8104  N N     . ARG G 66  ? 0.5199 0.4977 0.5418 -0.0561 0.0555  -0.0499 67  ARG G N     
8105  C CA    . ARG G 66  ? 0.5524 0.5331 0.5733 -0.0547 0.0546  -0.0468 67  ARG G CA    
8106  C C     . ARG G 66  ? 0.4999 0.4865 0.5225 -0.0553 0.0524  -0.0491 67  ARG G C     
8107  O O     . ARG G 66  ? 0.4835 0.4727 0.5063 -0.0550 0.0522  -0.0472 67  ARG G O     
8108  C CB    . ARG G 66  ? 0.5664 0.5464 0.5834 -0.0518 0.0533  -0.0443 67  ARG G CB    
8109  C CG    . ARG G 66  ? 0.6070 0.5821 0.6226 -0.0507 0.0556  -0.0414 67  ARG G CG    
8110  C CD    . ARG G 66  ? 0.6280 0.6040 0.6410 -0.0481 0.0546  -0.0381 67  ARG G CD    
8111  N NE    . ARG G 66  ? 0.6622 0.6401 0.6729 -0.0468 0.0521  -0.0395 67  ARG G NE    
8112  C CZ    . ARG G 66  ? 0.6638 0.6394 0.6730 -0.0461 0.0519  -0.0411 67  ARG G CZ    
8113  N NH1   . ARG G 66  ? 0.6973 0.6686 0.7070 -0.0467 0.0540  -0.0417 67  ARG G NH1   
8114  N NH2   . ARG G 66  ? 0.6781 0.6553 0.6848 -0.0448 0.0498  -0.0421 67  ARG G NH2   
8115  N N     . ARG G 67  ? 0.5224 0.5112 0.5462 -0.0562 0.0506  -0.0532 68  ARG G N     
8116  C CA    . ARG G 67  ? 0.5503 0.5450 0.5763 -0.0567 0.0485  -0.0557 68  ARG G CA    
8117  C C     . ARG G 67  ? 0.4960 0.4922 0.5262 -0.0591 0.0506  -0.0555 68  ARG G C     
8118  O O     . ARG G 67  ? 0.4704 0.4708 0.5017 -0.0588 0.0498  -0.0551 68  ARG G O     
8119  C CB    . ARG G 67  ? 0.5996 0.5963 0.6265 -0.0573 0.0463  -0.0603 68  ARG G CB    
8120  C CG    . ARG G 67  ? 0.6185 0.6146 0.6407 -0.0546 0.0438  -0.0607 68  ARG G CG    
8121  C CD    . ARG G 67  ? 0.6717 0.6700 0.6945 -0.0551 0.0416  -0.0653 68  ARG G CD    
8122  N NE    . ARG G 67  ? 0.6888 0.6864 0.7066 -0.0523 0.0393  -0.0656 68  ARG G NE    
8123  C CZ    . ARG G 67  ? 0.7702 0.7702 0.7851 -0.0497 0.0371  -0.0644 68  ARG G CZ    
8124  N NH1   . ARG G 67  ? 0.7551 0.7586 0.7718 -0.0495 0.0368  -0.0630 68  ARG G NH1   
8125  N NH2   . ARG G 67  ? 0.8055 0.8041 0.8156 -0.0473 0.0355  -0.0646 68  ARG G NH2   
8126  N N     . ASP G 68  ? 0.4677 0.4601 0.5001 -0.0614 0.0537  -0.0558 69  ASP G N     
8127  C CA    . ASP G 68  ? 0.4665 0.4595 0.5029 -0.0640 0.0564  -0.0557 69  ASP G CA    
8128  C C     . ASP G 68  ? 0.3931 0.3845 0.4274 -0.0628 0.0580  -0.0510 69  ASP G C     
8129  O O     . ASP G 68  ? 0.3937 0.3880 0.4300 -0.0636 0.0589  -0.0504 69  ASP G O     
8130  C CB    . ASP G 68  ? 0.5383 0.5270 0.5772 -0.0668 0.0593  -0.0574 69  ASP G CB    
8131  C CG    . ASP G 68  ? 0.5996 0.5898 0.6406 -0.0684 0.0577  -0.0626 69  ASP G CG    
8132  O OD1   . ASP G 68  ? 0.5678 0.5643 0.6120 -0.0694 0.0557  -0.0658 69  ASP G OD1   
8133  O OD2   . ASP G 68  ? 0.6918 0.6773 0.7313 -0.0685 0.0585  -0.0633 69  ASP G OD2   
8134  N N     . THR G 69  ? 0.3737 0.3609 0.4042 -0.0607 0.0585  -0.0477 70  THR G N     
8135  C CA    . THR G 69  ? 0.3959 0.3818 0.4241 -0.0593 0.0597  -0.0432 70  THR G CA    
8136  C C     . THR G 69  ? 0.3760 0.3671 0.4033 -0.0581 0.0574  -0.0428 70  THR G C     
8137  O O     . THR G 69  ? 0.3767 0.3690 0.4043 -0.0583 0.0586  -0.0409 70  THR G O     
8138  C CB    . THR G 69  ? 0.3808 0.3625 0.4052 -0.0570 0.0598  -0.0404 70  THR G CB    
8139  O OG1   . THR G 69  ? 0.3829 0.3593 0.4082 -0.0582 0.0626  -0.0406 70  THR G OG1   
8140  C CG2   . THR G 69  ? 0.3822 0.3636 0.4040 -0.0551 0.0603  -0.0360 70  THR G CG2   
8141  N N     . TYR G 70  ? 0.3311 0.3251 0.3572 -0.0566 0.0542  -0.0446 71  TYR G N     
8142  C CA    . TYR G 70  ? 0.3430 0.3412 0.3678 -0.0551 0.0520  -0.0442 71  TYR G CA    
8143  C C     . TYR G 70  ? 0.3788 0.3816 0.4074 -0.0568 0.0520  -0.0466 71  TYR G C     
8144  O O     . TYR G 70  ? 0.3943 0.3998 0.4226 -0.0562 0.0517  -0.0455 71  TYR G O     
8145  C CB    . TYR G 70  ? 0.3182 0.3174 0.3404 -0.0531 0.0489  -0.0454 71  TYR G CB    
8146  C CG    . TYR G 70  ? 0.3058 0.3009 0.3246 -0.0515 0.0491  -0.0432 71  TYR G CG    
8147  C CD1   . TYR G 70  ? 0.3067 0.2990 0.3242 -0.0511 0.0509  -0.0396 71  TYR G CD1   
8148  C CD2   . TYR G 70  ? 0.3073 0.3016 0.3242 -0.0504 0.0474  -0.0448 71  TYR G CD2   
8149  C CE1   . TYR G 70  ? 0.3033 0.2926 0.3184 -0.0495 0.0510  -0.0377 71  TYR G CE1   
8150  C CE2   . TYR G 70  ? 0.3172 0.3080 0.3314 -0.0489 0.0477  -0.0428 71  TYR G CE2   
8151  C CZ    . TYR G 70  ? 0.3092 0.2977 0.3227 -0.0485 0.0495  -0.0393 71  TYR G CZ    
8152  O OH    . TYR G 70  ? 0.3237 0.3095 0.3352 -0.0470 0.0499  -0.0375 71  TYR G OH    
8153  N N     . GLU G 71  ? 0.4002 0.4039 0.4325 -0.0589 0.0524  -0.0499 72  GLU G N     
8154  C CA    . GLU G 71  ? 0.4150 0.4236 0.4519 -0.0606 0.0525  -0.0526 72  GLU G CA    
8155  C C     . GLU G 71  ? 0.3859 0.3936 0.4245 -0.0623 0.0559  -0.0505 72  GLU G C     
8156  O O     . GLU G 71  ? 0.4103 0.4220 0.4507 -0.0626 0.0561  -0.0508 72  GLU G O     
8157  C CB    . GLU G 71  ? 0.4296 0.4393 0.4703 -0.0627 0.0522  -0.0569 72  GLU G CB    
8158  C CG    . GLU G 71  ? 0.4662 0.4814 0.5127 -0.0650 0.0527  -0.0599 72  GLU G CG    
8159  C CD    . GLU G 71  ? 0.5075 0.5288 0.5543 -0.0631 0.0501  -0.0606 72  GLU G CD    
8160  O OE1   . GLU G 71  ? 0.5433 0.5667 0.5881 -0.0609 0.0467  -0.0620 72  GLU G OE1   
8161  O OE2   . GLU G 71  ? 0.5585 0.5821 0.6072 -0.0637 0.0517  -0.0596 72  GLU G OE2   
8162  N N     . GLN G 72  ? 0.3815 0.3836 0.4192 -0.0632 0.0588  -0.0483 73  GLN G N     
8163  C CA    . GLN G 72  ? 0.3964 0.3966 0.4348 -0.0645 0.0624  -0.0459 73  GLN G CA    
8164  C C     . GLN G 72  ? 0.3889 0.3894 0.4233 -0.0623 0.0620  -0.0423 73  GLN G C     
8165  O O     . GLN G 72  ? 0.3582 0.3600 0.3933 -0.0630 0.0638  -0.0411 73  GLN G O     
8166  C CB    . GLN G 72  ? 0.4134 0.4070 0.4513 -0.0656 0.0656  -0.0443 73  GLN G CB    
8167  C CG    . GLN G 72  ? 0.4010 0.3936 0.4431 -0.0685 0.0667  -0.0482 73  GLN G CG    
8168  C CD    . GLN G 72  ? 0.4350 0.4203 0.4761 -0.0693 0.0699  -0.0466 73  GLN G CD    
8169  O OE1   . GLN G 72  ? 0.4359 0.4169 0.4730 -0.0673 0.0709  -0.0425 73  GLN G OE1   
8170  N NE2   . GLN G 72  ? 0.4245 0.4083 0.4692 -0.0723 0.0714  -0.0499 73  GLN G NE2   
8171  N N     . MET G 73  ? 0.4100 0.4096 0.4403 -0.0597 0.0597  -0.0406 74  MET G N     
8172  C CA    . MET G 73  ? 0.4219 0.4222 0.4485 -0.0576 0.0588  -0.0377 74  MET G CA    
8173  C C     . MET G 73  ? 0.3892 0.3949 0.4170 -0.0575 0.0574  -0.0394 74  MET G C     
8174  O O     . MET G 73  ? 0.3781 0.3849 0.4053 -0.0575 0.0587  -0.0378 74  MET G O     
8175  C CB    . MET G 73  ? 0.4750 0.4741 0.4979 -0.0552 0.0564  -0.0364 74  MET G CB    
8176  C CG    . MET G 73  ? 0.5102 0.5041 0.5312 -0.0547 0.0580  -0.0338 74  MET G CG    
8177  S SD    . MET G 73  ? 0.5962 0.5893 0.6135 -0.0520 0.0554  -0.0325 74  MET G SD    
8178  C CE    . MET G 73  ? 0.5834 0.5708 0.5998 -0.0515 0.0579  -0.0297 74  MET G CE    
8179  N N     . VAL G 74  ? 0.3667 0.3757 0.3962 -0.0572 0.0549  -0.0426 75  VAL G N     
8180  C CA    . VAL G 74  ? 0.3925 0.4066 0.4231 -0.0565 0.0532  -0.0443 75  VAL G CA    
8181  C C     . VAL G 74  ? 0.3832 0.3999 0.4179 -0.0586 0.0557  -0.0452 75  VAL G C     
8182  O O     . VAL G 74  ? 0.3357 0.3550 0.3700 -0.0580 0.0558  -0.0448 75  VAL G O     
8183  C CB    . VAL G 74  ? 0.3545 0.3716 0.3863 -0.0557 0.0501  -0.0476 75  VAL G CB    
8184  C CG1   . VAL G 74  ? 0.3348 0.3573 0.3684 -0.0550 0.0487  -0.0496 75  VAL G CG1   
8185  C CG2   . VAL G 74  ? 0.3733 0.3878 0.4006 -0.0535 0.0479  -0.0466 75  VAL G CG2   
8186  N N     . ASN G 75  ? 0.4024 0.4180 0.4408 -0.0611 0.0578  -0.0466 76  ASN G N     
8187  C CA    . ASN G 75  ? 0.4409 0.4591 0.4841 -0.0636 0.0604  -0.0480 76  ASN G CA    
8188  C C     . ASN G 75  ? 0.4520 0.4677 0.4929 -0.0637 0.0635  -0.0444 76  ASN G C     
8189  O O     . ASN G 75  ? 0.5233 0.5420 0.5661 -0.0645 0.0650  -0.0448 76  ASN G O     
8190  C CB    . ASN G 75  ? 0.4847 0.5017 0.5323 -0.0665 0.0621  -0.0505 76  ASN G CB    
8191  C CG    . ASN G 75  ? 0.4769 0.4972 0.5302 -0.0693 0.0649  -0.0523 76  ASN G CG    
8192  O OD1   . ASN G 75  ? 0.5333 0.5598 0.5899 -0.0692 0.0636  -0.0547 76  ASN G OD1   
8193  N ND2   . ASN G 75  ? 0.5647 0.5808 0.6192 -0.0718 0.0689  -0.0512 76  ASN G ND2   
8194  N N     . ALA G 76  ? 0.4834 0.4936 0.5200 -0.0629 0.0645  -0.0410 77  ALA G N     
8195  C CA    . ALA G 76  ? 0.5166 0.5240 0.5501 -0.0627 0.0672  -0.0373 77  ALA G CA    
8196  C C     . ALA G 76  ? 0.4841 0.4946 0.5147 -0.0607 0.0656  -0.0363 77  ALA G C     
8197  O O     . ALA G 76  ? 0.4163 0.4273 0.4462 -0.0611 0.0678  -0.0350 77  ALA G O     
8198  C CB    . ALA G 76  ? 0.5243 0.5259 0.5538 -0.0617 0.0679  -0.0341 77  ALA G CB    
8199  N N     . ILE G 77  ? 0.4806 0.4927 0.5091 -0.0587 0.0620  -0.0370 78  ILE G N     
8200  C CA    . ILE G 77  ? 0.4462 0.4606 0.4716 -0.0568 0.0603  -0.0362 78  ILE G CA    
8201  C C     . ILE G 77  ? 0.4765 0.4958 0.5053 -0.0573 0.0606  -0.0388 78  ILE G C     
8202  O O     . ILE G 77  ? 0.4825 0.5030 0.5097 -0.0569 0.0615  -0.0378 78  ILE G O     
8203  C CB    . ILE G 77  ? 0.4805 0.4949 0.5031 -0.0546 0.0568  -0.0364 78  ILE G CB    
8204  C CG1   . ILE G 77  ? 0.4995 0.5095 0.5190 -0.0539 0.0567  -0.0339 78  ILE G CG1   
8205  C CG2   . ILE G 77  ? 0.4688 0.4853 0.4884 -0.0529 0.0552  -0.0361 78  ILE G CG2   
8206  C CD1   . ILE G 77  ? 0.4856 0.4954 0.5027 -0.0521 0.0536  -0.0341 78  ILE G CD1   
8207  N N     . LEU G 78  ? 0.4509 0.4733 0.4845 -0.0583 0.0597  -0.0422 79  LEU G N     
8208  C CA    . LEU G 78  ? 0.4549 0.4828 0.4925 -0.0585 0.0595  -0.0449 79  LEU G CA    
8209  C C     . LEU G 78  ? 0.4554 0.4841 0.4960 -0.0607 0.0634  -0.0446 79  LEU G C     
8210  O O     . LEU G 78  ? 0.5070 0.5393 0.5489 -0.0604 0.0642  -0.0453 79  LEU G O     
8211  C CB    . LEU G 78  ? 0.4886 0.5200 0.5307 -0.0589 0.0573  -0.0487 79  LEU G CB    
8212  C CG    . LEU G 78  ? 0.5246 0.5573 0.5643 -0.0562 0.0533  -0.0497 79  LEU G CG    
8213  C CD1   . LEU G 78  ? 0.5542 0.5899 0.5924 -0.0541 0.0524  -0.0496 79  LEU G CD1   
8214  C CD2   . LEU G 78  ? 0.5745 0.6020 0.6088 -0.0549 0.0521  -0.0473 79  LEU G CD2   
8215  N N     . ASP G 79  ? 0.4204 0.4454 0.4620 -0.0629 0.0663  -0.0435 80  ASP G N     
8216  C CA    . ASP G 79  ? 0.4291 0.4539 0.4733 -0.0652 0.0705  -0.0430 80  ASP G CA    
8217  C C     . ASP G 79  ? 0.4157 0.4397 0.4552 -0.0638 0.0719  -0.0401 80  ASP G C     
8218  O O     . ASP G 79  ? 0.4290 0.4557 0.4707 -0.0647 0.0743  -0.0406 80  ASP G O     
8219  C CB    . ASP G 79  ? 0.4142 0.4338 0.4589 -0.0674 0.0735  -0.0417 80  ASP G CB    
8220  C CG    . ASP G 79  ? 0.4598 0.4809 0.5107 -0.0699 0.0736  -0.0454 80  ASP G CG    
8221  O OD1   . ASP G 79  ? 0.4572 0.4840 0.5120 -0.0698 0.0710  -0.0489 80  ASP G OD1   
8222  O OD2   . ASP G 79  ? 0.4638 0.4803 0.5154 -0.0718 0.0763  -0.0446 80  ASP G OD2   
8223  N N     . ALA G 80  ? 0.3727 0.3932 0.4059 -0.0617 0.0704  -0.0372 81  ALA G N     
8224  C CA    . ALA G 80  ? 0.3900 0.4096 0.4182 -0.0603 0.0712  -0.0346 81  ALA G CA    
8225  C C     . ALA G 80  ? 0.3737 0.3982 0.4024 -0.0590 0.0695  -0.0365 81  ALA G C     
8226  O O     . ALA G 80  ? 0.3850 0.4104 0.4123 -0.0589 0.0715  -0.0358 81  ALA G O     
8227  C CB    . ALA G 80  ? 0.4140 0.4297 0.4361 -0.0584 0.0694  -0.0316 81  ALA G CB    
8228  N N     . VAL G 81  ? 0.3295 0.3567 0.3599 -0.0579 0.0661  -0.0389 82  VAL G N     
8229  C CA    . VAL G 81  ? 0.3520 0.3832 0.3825 -0.0562 0.0642  -0.0407 82  VAL G CA    
8230  C C     . VAL G 81  ? 0.3514 0.3876 0.3879 -0.0574 0.0662  -0.0433 82  VAL G C     
8231  O O     . VAL G 81  ? 0.3760 0.4146 0.4121 -0.0566 0.0670  -0.0436 82  VAL G O     
8232  C CB    . VAL G 81  ? 0.3502 0.3824 0.3803 -0.0544 0.0602  -0.0423 82  VAL G CB    
8233  C CG1   . VAL G 81  ? 0.3362 0.3723 0.3667 -0.0524 0.0584  -0.0442 82  VAL G CG1   
8234  C CG2   . VAL G 81  ? 0.3328 0.3605 0.3574 -0.0532 0.0584  -0.0399 82  VAL G CG2   
8235  N N     . ARG G 82  ? 0.3766 0.4143 0.4188 -0.0596 0.0671  -0.0452 83  ARG G N     
8236  C CA    . ARG G 82  ? 0.4043 0.4474 0.4534 -0.0612 0.0689  -0.0480 83  ARG G CA    
8237  C C     . ARG G 82  ? 0.4268 0.4686 0.4757 -0.0629 0.0736  -0.0462 83  ARG G C     
8238  O O     . ARG G 82  ? 0.4536 0.4998 0.5067 -0.0635 0.0755  -0.0479 83  ARG G O     
8239  C CB    . ARG G 82  ? 0.4394 0.4843 0.4946 -0.0634 0.0685  -0.0508 83  ARG G CB    
8240  C CG    . ARG G 82  ? 0.4632 0.5111 0.5194 -0.0616 0.0639  -0.0534 83  ARG G CG    
8241  C CD    . ARG G 82  ? 0.5239 0.5739 0.5860 -0.0638 0.0634  -0.0565 83  ARG G CD    
8242  N NE    . ARG G 82  ? 0.5531 0.5970 0.6132 -0.0655 0.0645  -0.0549 83  ARG G NE    
8243  C CZ    . ARG G 82  ? 0.5825 0.6247 0.6418 -0.0651 0.0619  -0.0558 83  ARG G CZ    
8244  N NH1   . ARG G 82  ? 0.5736 0.6196 0.6335 -0.0632 0.0580  -0.0582 83  ARG G NH1   
8245  N NH2   . ARG G 82  ? 0.5632 0.5997 0.6207 -0.0666 0.0634  -0.0543 83  ARG G NH2   
8246  N N     . ALA G 83  ? 0.4773 0.5130 0.5213 -0.0633 0.0754  -0.0428 84  ALA G N     
8247  C CA    . ALA G 83  ? 0.4888 0.5223 0.5312 -0.0646 0.0799  -0.0405 84  ALA G CA    
8248  C C     . ALA G 83  ? 0.4639 0.4987 0.5022 -0.0625 0.0800  -0.0396 84  ALA G C     
8249  O O     . ALA G 83  ? 0.5073 0.5428 0.5461 -0.0633 0.0836  -0.0391 84  ALA G O     
8250  C CB    . ALA G 83  ? 0.5013 0.5280 0.5390 -0.0650 0.0814  -0.0370 84  ALA G CB    
8251  N N     . GLY G 84  ? 0.4567 0.4915 0.4909 -0.0599 0.0761  -0.0395 85  GLY G N     
8252  C CA    . GLY G 84  ? 0.4052 0.4410 0.4354 -0.0578 0.0758  -0.0391 85  GLY G CA    
8253  C C     . GLY G 84  ? 0.4145 0.4455 0.4365 -0.0563 0.0748  -0.0358 85  GLY G C     
8254  O O     . GLY G 84  ? 0.3720 0.4028 0.3896 -0.0550 0.0749  -0.0351 85  GLY G O     
8255  N N     . LYS G 85  ? 0.4337 0.4609 0.4539 -0.0566 0.0736  -0.0341 86  LYS G N     
8256  C CA    . LYS G 85  ? 0.4429 0.4661 0.4560 -0.0553 0.0726  -0.0311 86  LYS G CA    
8257  C C     . LYS G 85  ? 0.4354 0.4592 0.4460 -0.0533 0.0684  -0.0319 86  LYS G C     
8258  O O     . LYS G 85  ? 0.3961 0.4216 0.4101 -0.0530 0.0660  -0.0340 86  LYS G O     
8259  C CB    . LYS G 85  ? 0.4697 0.4888 0.4823 -0.0562 0.0733  -0.0289 86  LYS G CB    
8260  C CG    . LYS G 85  ? 0.4966 0.5140 0.5116 -0.0584 0.0778  -0.0279 86  LYS G CG    
8261  C CD    . LYS G 85  ? 0.5422 0.5549 0.5564 -0.0590 0.0786  -0.0257 86  LYS G CD    
8262  C CE    . LYS G 85  ? 0.5744 0.5850 0.5911 -0.0613 0.0833  -0.0249 86  LYS G CE    
8263  N NZ    . LYS G 85  ? 0.6010 0.6102 0.6137 -0.0611 0.0866  -0.0226 86  LYS G NZ    
8264  N N     . LYS G 86  ? 0.4281 0.4504 0.4327 -0.0519 0.0675  -0.0304 87  LYS G N     
8265  C CA    . LYS G 86  ? 0.4673 0.4892 0.4689 -0.0503 0.0639  -0.0308 87  LYS G CA    
8266  C C     . LYS G 86  ? 0.4515 0.4708 0.4522 -0.0503 0.0623  -0.0291 87  LYS G C     
8267  O O     . LYS G 86  ? 0.3845 0.4013 0.3810 -0.0500 0.0625  -0.0265 87  LYS G O     
8268  C CB    . LYS G 86  ? 0.4934 0.5147 0.4891 -0.0492 0.0638  -0.0299 87  LYS G CB    
8269  C CG    . LYS G 86  ? 0.5687 0.5897 0.5615 -0.0478 0.0604  -0.0307 87  LYS G CG    
8270  C CD    . LYS G 86  ? 0.6267 0.6472 0.6141 -0.0469 0.0604  -0.0306 87  LYS G CD    
8271  C CE    . LYS G 86  ? 0.6793 0.6980 0.6619 -0.0472 0.0616  -0.0279 87  LYS G CE    
8272  N NZ    . LYS G 86  ? 0.7354 0.7537 0.7126 -0.0465 0.0614  -0.0282 87  LYS G NZ    
8273  N N     . THR G 87  ? 0.4137 0.4337 0.4183 -0.0505 0.0607  -0.0307 88  THR G N     
8274  C CA    . THR G 87  ? 0.4140 0.4316 0.4189 -0.0508 0.0599  -0.0294 88  THR G CA    
8275  C C     . THR G 87  ? 0.4068 0.4236 0.4089 -0.0493 0.0566  -0.0293 88  THR G C     
8276  O O     . THR G 87  ? 0.4339 0.4523 0.4365 -0.0485 0.0547  -0.0313 88  THR G O     
8277  C CB    . THR G 87  ? 0.4172 0.4357 0.4278 -0.0520 0.0604  -0.0314 88  THR G CB    
8278  O OG1   . THR G 87  ? 0.3768 0.3963 0.3901 -0.0536 0.0637  -0.0315 88  THR G OG1   
8279  C CG2   . THR G 87  ? 0.4129 0.4285 0.4239 -0.0524 0.0600  -0.0302 88  THR G CG2   
8280  N N     . VAL G 88  ? 0.4359 0.4501 0.4354 -0.0490 0.0561  -0.0269 89  VAL G N     
8281  C CA    . VAL G 88  ? 0.4576 0.4710 0.4550 -0.0480 0.0534  -0.0266 89  VAL G CA    
8282  C C     . VAL G 88  ? 0.4709 0.4825 0.4703 -0.0482 0.0532  -0.0259 89  VAL G C     
8283  O O     . VAL G 88  ? 0.5360 0.5457 0.5356 -0.0487 0.0551  -0.0240 89  VAL G O     
8284  C CB    . VAL G 88  ? 0.5099 0.5228 0.5024 -0.0472 0.0527  -0.0247 89  VAL G CB    
8285  C CG1   . VAL G 88  ? 0.5168 0.5290 0.5078 -0.0464 0.0502  -0.0241 89  VAL G CG1   
8286  C CG2   . VAL G 88  ? 0.5154 0.5298 0.5055 -0.0469 0.0527  -0.0258 89  VAL G CG2   
8287  N N     . CYS G 89  ? 0.5177 0.5293 0.5181 -0.0477 0.0511  -0.0272 90  CYS G N     
8288  C CA    . CYS G 89  ? 0.5598 0.5695 0.5616 -0.0477 0.0508  -0.0267 90  CYS G CA    
8289  C C     . CYS G 89  ? 0.5312 0.5400 0.5301 -0.0465 0.0490  -0.0252 90  CYS G C     
8290  O O     . CYS G 89  ? 0.6439 0.6534 0.6420 -0.0459 0.0471  -0.0265 90  CYS G O     
8291  C CB    . CYS G 89  ? 0.6161 0.6266 0.6212 -0.0479 0.0500  -0.0294 90  CYS G CB    
8292  S SG    . CYS G 89  ? 0.7015 0.7093 0.7080 -0.0480 0.0497  -0.0291 90  CYS G SG    
8293  N N     . ALA G 90  ? 0.4572 0.4645 0.4548 -0.0463 0.0497  -0.0226 91  ALA G N     
8294  C CA    . ALA G 90  ? 0.4373 0.4445 0.4327 -0.0452 0.0481  -0.0211 91  ALA G CA    
8295  C C     . ALA G 90  ? 0.4345 0.4399 0.4318 -0.0448 0.0480  -0.0208 91  ALA G C     
8296  O O     . ALA G 90  ? 0.3774 0.3809 0.3753 -0.0447 0.0495  -0.0191 91  ALA G O     
8297  C CB    . ALA G 90  ? 0.4435 0.4508 0.4361 -0.0447 0.0487  -0.0184 91  ALA G CB    
8298  N N     . LEU G 91  ? 0.4851 0.4907 0.4828 -0.0445 0.0463  -0.0223 92  LEU G N     
8299  C CA    . LEU G 91  ? 0.4872 0.4912 0.4862 -0.0440 0.0461  -0.0222 92  LEU G CA    
8300  C C     . LEU G 91  ? 0.5269 0.5317 0.5243 -0.0431 0.0447  -0.0210 92  LEU G C     
8301  O O     . LEU G 91  ? 0.4596 0.4661 0.4552 -0.0431 0.0435  -0.0213 92  LEU G O     
8302  C CB    . LEU G 91  ? 0.5044 0.5081 0.5051 -0.0443 0.0455  -0.0249 92  LEU G CB    
8303  C CG    . LEU G 91  ? 0.5476 0.5515 0.5504 -0.0454 0.0466  -0.0266 92  LEU G CG    
8304  C CD1   . LEU G 91  ? 0.5453 0.5491 0.5497 -0.0454 0.0457  -0.0292 92  LEU G CD1   
8305  C CD2   . LEU G 91  ? 0.5365 0.5388 0.5408 -0.0461 0.0489  -0.0252 92  LEU G CD2   
8306  N N     . TYR G 92  ? 0.4692 0.4727 0.4676 -0.0424 0.0449  -0.0197 93  TYR G N     
8307  C CA    . TYR G 92  ? 0.4338 0.4385 0.4315 -0.0415 0.0438  -0.0186 93  TYR G CA    
8308  C C     . TYR G 92  ? 0.4561 0.4609 0.4536 -0.0417 0.0426  -0.0206 93  TYR G C     
8309  O O     . TYR G 92  ? 0.3796 0.3830 0.3777 -0.0419 0.0427  -0.0224 93  TYR G O     
8310  C CB    . TYR G 92  ? 0.4791 0.4824 0.4780 -0.0404 0.0447  -0.0166 93  TYR G CB    
8311  C CG    . TYR G 92  ? 0.4783 0.4792 0.4789 -0.0403 0.0453  -0.0178 93  TYR G CG    
8312  C CD1   . TYR G 92  ? 0.4992 0.5003 0.4999 -0.0399 0.0444  -0.0186 93  TYR G CD1   
8313  C CD2   . TYR G 92  ? 0.4799 0.4781 0.4817 -0.0407 0.0469  -0.0182 93  TYR G CD2   
8314  C CE1   . TYR G 92  ? 0.5244 0.5232 0.5261 -0.0397 0.0450  -0.0197 93  TYR G CE1   
8315  C CE2   . TYR G 92  ? 0.5063 0.5022 0.5092 -0.0406 0.0474  -0.0195 93  TYR G CE2   
8316  C CZ    . TYR G 92  ? 0.5110 0.5072 0.5137 -0.0400 0.0464  -0.0202 93  TYR G CZ    
8317  O OH    . TYR G 92  ? 0.5709 0.5647 0.5742 -0.0398 0.0469  -0.0216 93  TYR G OH    
8318  N N     . GLY G 93  ? 0.3910 0.3976 0.3875 -0.0416 0.0414  -0.0203 94  GLY G N     
8319  C CA    . GLY G 93  ? 0.4068 0.4131 0.4027 -0.0418 0.0406  -0.0219 94  GLY G CA    
8320  C C     . GLY G 93  ? 0.3974 0.4035 0.3920 -0.0423 0.0402  -0.0239 94  GLY G C     
8321  O O     . GLY G 93  ? 0.3765 0.3839 0.3699 -0.0428 0.0400  -0.0239 94  GLY G O     
8322  N N     . HIS G 94  ? 0.3438 0.3482 0.3383 -0.0421 0.0401  -0.0256 95  HIS G N     
8323  C CA    . HIS G 94  ? 0.3412 0.3452 0.3344 -0.0422 0.0397  -0.0275 95  HIS G CA    
8324  C C     . HIS G 94  ? 0.3593 0.3629 0.3540 -0.0421 0.0402  -0.0284 95  HIS G C     
8325  O O     . HIS G 94  ? 0.3522 0.3545 0.3481 -0.0418 0.0405  -0.0288 95  HIS G O     
8326  C CB    . HIS G 94  ? 0.2951 0.2975 0.2867 -0.0417 0.0392  -0.0286 95  HIS G CB    
8327  C CG    . HIS G 94  ? 0.2706 0.2724 0.2606 -0.0413 0.0387  -0.0303 95  HIS G CG    
8328  N ND1   . HIS G 94  ? 0.2484 0.2509 0.2393 -0.0410 0.0387  -0.0315 95  HIS G ND1   
8329  C CD2   . HIS G 94  ? 0.2449 0.2455 0.2326 -0.0410 0.0384  -0.0312 95  HIS G CD2   
8330  C CE1   . HIS G 94  ? 0.2447 0.2466 0.2338 -0.0404 0.0382  -0.0328 95  HIS G CE1   
8331  N NE2   . HIS G 94  ? 0.2542 0.2545 0.2411 -0.0403 0.0381  -0.0326 95  HIS G NE2   
8332  N N     . PRO G 95  ? 0.3432 0.3481 0.3381 -0.0425 0.0404  -0.0291 96  PRO G N     
8333  C CA    . PRO G 95  ? 0.3464 0.3516 0.3436 -0.0428 0.0411  -0.0300 96  PRO G CA    
8334  C C     . PRO G 95  ? 0.3205 0.3251 0.3184 -0.0423 0.0405  -0.0321 96  PRO G C     
8335  O O     . PRO G 95  ? 0.3467 0.3515 0.3469 -0.0427 0.0410  -0.0330 96  PRO G O     
8336  C CB    . PRO G 95  ? 0.3510 0.3580 0.3479 -0.0433 0.0415  -0.0303 96  PRO G CB    
8337  C CG    . PRO G 95  ? 0.3412 0.3482 0.3353 -0.0428 0.0404  -0.0307 96  PRO G CG    
8338  C CD    . PRO G 95  ? 0.3511 0.3571 0.3441 -0.0427 0.0400  -0.0294 96  PRO G CD    
8339  N N     . GLY G 96  ? 0.2832 0.2870 0.2790 -0.0413 0.0394  -0.0330 97  GLY G N     
8340  C CA    . GLY G 96  ? 0.3357 0.3390 0.3314 -0.0404 0.0386  -0.0350 97  GLY G CA    
8341  C C     . GLY G 96  ? 0.3053 0.3062 0.2995 -0.0396 0.0383  -0.0348 97  GLY G C     
8342  O O     . GLY G 96  ? 0.3826 0.3827 0.3754 -0.0384 0.0375  -0.0362 97  GLY G O     
8343  N N     . VAL G 97  ? 0.3117 0.3116 0.3060 -0.0400 0.0390  -0.0330 98  VAL G N     
8344  C CA    . VAL G 97  ? 0.3490 0.3467 0.3421 -0.0394 0.0391  -0.0327 98  VAL G CA    
8345  C C     . VAL G 97  ? 0.3662 0.3631 0.3612 -0.0396 0.0399  -0.0326 98  VAL G C     
8346  O O     . VAL G 97  ? 0.3073 0.3045 0.3040 -0.0403 0.0408  -0.0310 98  VAL G O     
8347  C CB    . VAL G 97  ? 0.3478 0.3453 0.3399 -0.0396 0.0395  -0.0310 98  VAL G CB    
8348  C CG1   . VAL G 97  ? 0.3904 0.3860 0.3821 -0.0391 0.0400  -0.0304 98  VAL G CG1   
8349  C CG2   . VAL G 97  ? 0.3101 0.3075 0.2999 -0.0394 0.0389  -0.0314 98  VAL G CG2   
8350  N N     . PHE G 98  ? 0.4096 0.4052 0.4041 -0.0390 0.0395  -0.0343 99  PHE G N     
8351  C CA    . PHE G 98  ? 0.4078 0.4022 0.4039 -0.0393 0.0403  -0.0347 99  PHE G CA    
8352  C C     . PHE G 98  ? 0.4123 0.4080 0.4114 -0.0406 0.0411  -0.0345 99  PHE G C     
8353  O O     . PHE G 98  ? 0.4142 0.4087 0.4147 -0.0411 0.0424  -0.0333 99  PHE G O     
8354  C CB    . PHE G 98  ? 0.4376 0.4300 0.4332 -0.0388 0.0413  -0.0331 99  PHE G CB    
8355  C CG    . PHE G 98  ? 0.4538 0.4443 0.4466 -0.0376 0.0410  -0.0337 99  PHE G CG    
8356  C CD1   . PHE G 98  ? 0.4358 0.4263 0.4265 -0.0371 0.0407  -0.0330 99  PHE G CD1   
8357  C CD2   . PHE G 98  ? 0.4741 0.4625 0.4660 -0.0370 0.0413  -0.0350 99  PHE G CD2   
8358  C CE1   . PHE G 98  ? 0.4689 0.4571 0.4566 -0.0360 0.0408  -0.0334 99  PHE G CE1   
8359  C CE2   . PHE G 98  ? 0.4384 0.4248 0.4272 -0.0358 0.0412  -0.0354 99  PHE G CE2   
8360  C CZ    . PHE G 98  ? 0.4299 0.4161 0.4165 -0.0353 0.0410  -0.0345 99  PHE G CZ    
8361  N N     . ALA G 99  ? 0.4664 0.4644 0.4663 -0.0411 0.0405  -0.0355 100 ALA G N     
8362  C CA    . ALA G 99  ? 0.4153 0.4146 0.4180 -0.0424 0.0415  -0.0355 100 ALA G CA    
8363  C C     . ALA G 99  ? 0.4245 0.4262 0.4284 -0.0427 0.0405  -0.0380 100 ALA G C     
8364  O O     . ALA G 99  ? 0.4849 0.4882 0.4876 -0.0419 0.0395  -0.0385 100 ALA G O     
8365  C CB    . ALA G 99  ? 0.4045 0.4046 0.4069 -0.0428 0.0422  -0.0332 100 ALA G CB    
8366  N N     . CYS G 100 ? 0.4065 0.4086 0.4131 -0.0437 0.0410  -0.0398 101 CYS G N     
8367  C CA    . CYS G 100 ? 0.4167 0.4217 0.4251 -0.0439 0.0399  -0.0426 101 CYS G CA    
8368  C C     . CYS G 100 ? 0.4109 0.4184 0.4223 -0.0454 0.0411  -0.0426 101 CYS G C     
8369  O O     . CYS G 100 ? 0.4504 0.4611 0.4632 -0.0452 0.0402  -0.0444 101 CYS G O     
8370  C CB    . CYS G 100 ? 0.4478 0.4523 0.4577 -0.0445 0.0396  -0.0451 101 CYS G CB    
8371  S SG    . CYS G 100 ? 0.4586 0.4603 0.4712 -0.0466 0.0423  -0.0444 101 CYS G SG    
8372  N N     . VAL G 101 ? 0.3974 0.4033 0.4095 -0.0465 0.0432  -0.0404 102 VAL G N     
8373  C CA    . VAL G 101 ? 0.3854 0.3929 0.4001 -0.0480 0.0448  -0.0402 102 VAL G CA    
8374  C C     . VAL G 101 ? 0.3456 0.3561 0.3595 -0.0472 0.0440  -0.0403 102 VAL G C     
8375  O O     . VAL G 101 ? 0.3079 0.3216 0.3245 -0.0478 0.0439  -0.0423 102 VAL G O     
8376  C CB    . VAL G 101 ? 0.4016 0.4064 0.4157 -0.0487 0.0470  -0.0371 102 VAL G CB    
8377  C CG1   . VAL G 101 ? 0.4136 0.4197 0.4293 -0.0500 0.0489  -0.0364 102 VAL G CG1   
8378  C CG2   . VAL G 101 ? 0.4031 0.4045 0.4182 -0.0494 0.0483  -0.0370 102 VAL G CG2   
8379  N N     . SER G 102 ? 0.3467 0.3563 0.3572 -0.0460 0.0434  -0.0384 103 SER G N     
8380  C CA    . SER G 102 ? 0.3472 0.3588 0.3564 -0.0453 0.0429  -0.0383 103 SER G CA    
8381  C C     . SER G 102 ? 0.2890 0.3031 0.2989 -0.0443 0.0412  -0.0409 103 SER G C     
8382  O O     . SER G 102 ? 0.3192 0.3362 0.3308 -0.0444 0.0414  -0.0420 103 SER G O     
8383  C CB    . SER G 102 ? 0.4198 0.4298 0.4253 -0.0444 0.0424  -0.0362 103 SER G CB    
8384  O OG    . SER G 102 ? 0.5156 0.5242 0.5205 -0.0451 0.0438  -0.0337 103 SER G OG    
8385  N N     . HIS G 103 ? 0.2781 0.2911 0.2865 -0.0430 0.0396  -0.0419 104 HIS G N     
8386  C CA    . HIS G 103 ? 0.2611 0.2762 0.2695 -0.0415 0.0377  -0.0442 104 HIS G CA    
8387  C C     . HIS G 103 ? 0.2735 0.2923 0.2865 -0.0425 0.0378  -0.0467 104 HIS G C     
8388  O O     . HIS G 103 ? 0.2676 0.2897 0.2819 -0.0416 0.0371  -0.0482 104 HIS G O     
8389  C CB    . HIS G 103 ? 0.2619 0.2747 0.2675 -0.0400 0.0363  -0.0446 104 HIS G CB    
8390  C CG    . HIS G 103 ? 0.2557 0.2657 0.2570 -0.0388 0.0360  -0.0427 104 HIS G CG    
8391  N ND1   . HIS G 103 ? 0.2717 0.2786 0.2713 -0.0393 0.0368  -0.0408 104 HIS G ND1   
8392  C CD2   . HIS G 103 ? 0.2385 0.2481 0.2370 -0.0373 0.0353  -0.0426 104 HIS G CD2   
8393  C CE1   . HIS G 103 ? 0.2963 0.3015 0.2926 -0.0383 0.0365  -0.0397 104 HIS G CE1   
8394  N NE2   . HIS G 103 ? 0.2573 0.2638 0.2527 -0.0371 0.0356  -0.0407 104 HIS G NE2   
8395  N N     . MET G 104 ? 0.2957 0.3139 0.3113 -0.0443 0.0389  -0.0471 105 MET G N     
8396  C CA    . MET G 104 ? 0.3348 0.3564 0.3552 -0.0458 0.0392  -0.0497 105 MET G CA    
8397  C C     . MET G 104 ? 0.3328 0.3570 0.3559 -0.0469 0.0409  -0.0494 105 MET G C     
8398  O O     . MET G 104 ? 0.3416 0.3702 0.3681 -0.0469 0.0404  -0.0517 105 MET G O     
8399  C CB    . MET G 104 ? 0.3658 0.3851 0.3881 -0.0478 0.0405  -0.0500 105 MET G CB    
8400  C CG    . MET G 104 ? 0.4470 0.4644 0.4674 -0.0469 0.0388  -0.0512 105 MET G CG    
8401  S SD    . MET G 104 ? 0.6026 0.6164 0.6247 -0.0492 0.0407  -0.0514 105 MET G SD    
8402  C CE    . MET G 104 ? 0.6056 0.6236 0.6340 -0.0518 0.0415  -0.0549 105 MET G CE    
8403  N N     . ALA G 105 ? 0.3388 0.3606 0.3603 -0.0476 0.0428  -0.0466 106 ALA G N     
8404  C CA    . ALA G 105 ? 0.3265 0.3500 0.3498 -0.0487 0.0448  -0.0460 106 ALA G CA    
8405  C C     . ALA G 105 ? 0.3167 0.3433 0.3393 -0.0469 0.0437  -0.0468 106 ALA G C     
8406  O O     . ALA G 105 ? 0.2951 0.3255 0.3211 -0.0474 0.0444  -0.0483 106 ALA G O     
8407  C CB    . ALA G 105 ? 0.3369 0.3569 0.3575 -0.0493 0.0467  -0.0427 106 ALA G CB    
8408  N N     . ILE G 106 ? 0.3431 0.3678 0.3612 -0.0449 0.0421  -0.0457 107 ILE G N     
8409  C CA    . ILE G 106 ? 0.3578 0.3844 0.3744 -0.0430 0.0412  -0.0462 107 ILE G CA    
8410  C C     . ILE G 106 ? 0.3871 0.4178 0.4068 -0.0419 0.0396  -0.0492 107 ILE G C     
8411  O O     . ILE G 106 ? 0.3828 0.4169 0.4044 -0.0412 0.0399  -0.0504 107 ILE G O     
8412  C CB    . ILE G 106 ? 0.3563 0.3793 0.3675 -0.0413 0.0400  -0.0447 107 ILE G CB    
8413  C CG1   . ILE G 106 ? 0.3816 0.4018 0.3903 -0.0424 0.0414  -0.0419 107 ILE G CG1   
8414  C CG2   . ILE G 106 ? 0.3540 0.3783 0.3636 -0.0391 0.0390  -0.0456 107 ILE G CG2   
8415  C CD1   . ILE G 106 ? 0.3731 0.3904 0.3771 -0.0411 0.0404  -0.0407 107 ILE G CD1   
8416  N N     . THR G 107 ? 0.3749 0.4053 0.3949 -0.0415 0.0379  -0.0506 108 THR G N     
8417  C CA    . THR G 107 ? 0.4250 0.4595 0.4474 -0.0401 0.0359  -0.0535 108 THR G CA    
8418  C C     . THR G 107 ? 0.4255 0.4651 0.4542 -0.0418 0.0371  -0.0555 108 THR G C     
8419  O O     . THR G 107 ? 0.4457 0.4899 0.4768 -0.0405 0.0363  -0.0573 108 THR G O     
8420  C CB    . THR G 107 ? 0.4474 0.4805 0.4688 -0.0397 0.0342  -0.0545 108 THR G CB    
8421  O OG1   . THR G 107 ? 0.4715 0.5001 0.4871 -0.0379 0.0334  -0.0526 108 THR G OG1   
8422  C CG2   . THR G 107 ? 0.4702 0.5079 0.4942 -0.0384 0.0319  -0.0577 108 THR G CG2   
8423  N N     . ARG G 108 ? 0.4329 0.4717 0.4643 -0.0448 0.0391  -0.0553 109 ARG G N     
8424  C CA    . ARG G 108 ? 0.4353 0.4784 0.4730 -0.0470 0.0406  -0.0573 109 ARG G CA    
8425  C C     . ARG G 108 ? 0.4023 0.4474 0.4411 -0.0472 0.0426  -0.0564 109 ARG G C     
8426  O O     . ARG G 108 ? 0.4154 0.4657 0.4593 -0.0477 0.0432  -0.0585 109 ARG G O     
8427  C CB    . ARG G 108 ? 0.4421 0.4825 0.4816 -0.0501 0.0426  -0.0569 109 ARG G CB    
8428  C CG    . ARG G 108 ? 0.4610 0.5056 0.5074 -0.0529 0.0443  -0.0595 109 ARG G CG    
8429  C CD    . ARG G 108 ? 0.4832 0.5242 0.5310 -0.0558 0.0463  -0.0592 109 ARG G CD    
8430  N NE    . ARG G 108 ? 0.4788 0.5171 0.5243 -0.0552 0.0442  -0.0600 109 ARG G NE    
8431  C CZ    . ARG G 108 ? 0.5111 0.5458 0.5571 -0.0573 0.0455  -0.0601 109 ARG G CZ    
8432  N NH1   . ARG G 108 ? 0.4782 0.5115 0.5272 -0.0602 0.0489  -0.0595 109 ARG G NH1   
8433  N NH2   . ARG G 108 ? 0.4795 0.5119 0.5230 -0.0564 0.0436  -0.0608 109 ARG G NH2   
8434  N N     . ALA G 109 ? 0.3883 0.4294 0.4224 -0.0466 0.0437  -0.0534 110 ALA G N     
8435  C CA    . ALA G 109 ? 0.4155 0.4576 0.4494 -0.0466 0.0457  -0.0524 110 ALA G CA    
8436  C C     . ALA G 109 ? 0.4143 0.4605 0.4490 -0.0441 0.0442  -0.0541 110 ALA G C     
8437  O O     . ALA G 109 ? 0.4948 0.5450 0.5332 -0.0444 0.0457  -0.0552 110 ALA G O     
8438  C CB    . ALA G 109 ? 0.4134 0.4505 0.4416 -0.0463 0.0466  -0.0491 110 ALA G CB    
8439  N N     . LYS G 110 ? 0.4621 0.5070 0.4932 -0.0414 0.0416  -0.0542 111 LYS G N     
8440  C CA    . LYS G 110 ? 0.4906 0.5385 0.5215 -0.0384 0.0401  -0.0555 111 LYS G CA    
8441  C C     . LYS G 110 ? 0.5172 0.5717 0.5545 -0.0383 0.0391  -0.0588 111 LYS G C     
8442  O O     . LYS G 110 ? 0.5243 0.5832 0.5643 -0.0370 0.0393  -0.0600 111 LYS G O     
8443  C CB    . LYS G 110 ? 0.5220 0.5663 0.5474 -0.0357 0.0376  -0.0549 111 LYS G CB    
8444  C CG    . LYS G 110 ? 0.5627 0.6012 0.5821 -0.0356 0.0384  -0.0520 111 LYS G CG    
8445  C CD    . LYS G 110 ? 0.5868 0.6218 0.6012 -0.0330 0.0363  -0.0515 111 LYS G CD    
8446  C CE    . LYS G 110 ? 0.6245 0.6542 0.6336 -0.0333 0.0372  -0.0491 111 LYS G CE    
8447  N NZ    . LYS G 110 ? 0.6766 0.7065 0.6848 -0.0331 0.0387  -0.0486 111 LYS G NZ    
8448  N N     . ALA G 111 ? 0.5218 0.5772 0.5617 -0.0397 0.0381  -0.0602 112 ALA G N     
8449  C CA    . ALA G 111 ? 0.5191 0.5811 0.5651 -0.0399 0.0367  -0.0637 112 ALA G CA    
8450  C C     . ALA G 111 ? 0.5031 0.5699 0.5555 -0.0422 0.0394  -0.0648 112 ALA G C     
8451  O O     . ALA G 111 ? 0.4864 0.5599 0.5442 -0.0415 0.0387  -0.0675 112 ALA G O     
8452  C CB    . ALA G 111 ? 0.5196 0.5807 0.5665 -0.0415 0.0355  -0.0649 112 ALA G CB    
8453  N N     . GLU G 112 ? 0.5241 0.5873 0.5757 -0.0447 0.0427  -0.0626 113 GLU G N     
8454  C CA    . GLU G 112 ? 0.5442 0.6109 0.6012 -0.0471 0.0459  -0.0633 113 GLU G CA    
8455  C C     . GLU G 112 ? 0.5784 0.6453 0.6333 -0.0454 0.0474  -0.0619 113 GLU G C     
8456  O O     . GLU G 112 ? 0.5964 0.6651 0.6544 -0.0471 0.0505  -0.0618 113 GLU G O     
8457  C CB    . GLU G 112 ? 0.5571 0.6196 0.6143 -0.0508 0.0488  -0.0617 113 GLU G CB    
8458  C CG    . GLU G 112 ? 0.5561 0.6180 0.6154 -0.0526 0.0477  -0.0633 113 GLU G CG    
8459  C CD    . GLU G 112 ? 0.6004 0.6578 0.6600 -0.0560 0.0508  -0.0617 113 GLU G CD    
8460  O OE1   . GLU G 112 ? 0.6720 0.7272 0.7304 -0.0571 0.0539  -0.0594 113 GLU G OE1   
8461  O OE2   . GLU G 112 ? 0.5852 0.6410 0.6457 -0.0575 0.0501  -0.0628 113 GLU G OE2   
8462  N N     . GLY G 113 ? 0.5855 0.6502 0.6351 -0.0421 0.0453  -0.0609 114 GLY G N     
8463  C CA    . GLY G 113 ? 0.5971 0.6620 0.6445 -0.0400 0.0463  -0.0601 114 GLY G CA    
8464  C C     . GLY G 113 ? 0.5647 0.6243 0.6075 -0.0414 0.0491  -0.0570 114 GLY G C     
8465  O O     . GLY G 113 ? 0.6281 0.6887 0.6708 -0.0411 0.0513  -0.0566 114 GLY G O     
8466  N N     . PHE G 114 ? 0.5336 0.5878 0.5725 -0.0427 0.0489  -0.0550 115 PHE G N     
8467  C CA    . PHE G 114 ? 0.5308 0.5801 0.5647 -0.0436 0.0509  -0.0521 115 PHE G CA    
8468  C C     . PHE G 114 ? 0.5240 0.5689 0.5513 -0.0415 0.0489  -0.0506 115 PHE G C     
8469  O O     . PHE G 114 ? 0.5713 0.6156 0.5975 -0.0398 0.0463  -0.0513 115 PHE G O     
8470  C CB    . PHE G 114 ? 0.5316 0.5780 0.5658 -0.0466 0.0525  -0.0506 115 PHE G CB    
8471  C CG    . PHE G 114 ? 0.5333 0.5829 0.5735 -0.0492 0.0553  -0.0516 115 PHE G CG    
8472  C CD1   . PHE G 114 ? 0.5543 0.6047 0.5950 -0.0501 0.0585  -0.0508 115 PHE G CD1   
8473  C CD2   . PHE G 114 ? 0.5185 0.5699 0.5636 -0.0511 0.0550  -0.0534 115 PHE G CD2   
8474  C CE1   . PHE G 114 ? 0.5168 0.5697 0.5629 -0.0527 0.0616  -0.0517 115 PHE G CE1   
8475  C CE2   . PHE G 114 ? 0.4935 0.5475 0.5443 -0.0538 0.0579  -0.0545 115 PHE G CE2   
8476  C CZ    . PHE G 114 ? 0.4877 0.5424 0.5390 -0.0547 0.0613  -0.0535 115 PHE G CZ    
8477  N N     . SER G 115 ? 0.4603 0.5020 0.4830 -0.0415 0.0504  -0.0486 116 SER G N     
8478  C CA    . SER G 115 ? 0.4913 0.5285 0.5078 -0.0401 0.0489  -0.0472 116 SER G CA    
8479  C C     . SER G 115 ? 0.4661 0.4996 0.4805 -0.0415 0.0483  -0.0453 116 SER G C     
8480  O O     . SER G 115 ? 0.3730 0.4055 0.3877 -0.0435 0.0501  -0.0439 116 SER G O     
8481  C CB    . SER G 115 ? 0.5305 0.5660 0.5430 -0.0398 0.0505  -0.0461 116 SER G CB    
8482  O OG    . SER G 115 ? 0.5600 0.5915 0.5670 -0.0387 0.0491  -0.0451 116 SER G OG    
8483  N N     . ALA G 116 ? 0.4521 0.4835 0.4642 -0.0403 0.0459  -0.0453 117 ALA G N     
8484  C CA    . ALA G 116 ? 0.4302 0.4582 0.4404 -0.0413 0.0452  -0.0437 117 ALA G CA    
8485  C C     . ALA G 116 ? 0.4441 0.4690 0.4499 -0.0397 0.0433  -0.0433 117 ALA G C     
8486  O O     . ALA G 116 ? 0.4386 0.4641 0.4442 -0.0377 0.0418  -0.0447 117 ALA G O     
8487  C CB    . ALA G 116 ? 0.4234 0.4530 0.4379 -0.0423 0.0449  -0.0448 117 ALA G CB    
8488  N N     . LYS G 117 ? 0.3978 0.4195 0.4002 -0.0404 0.0434  -0.0413 118 LYS G N     
8489  C CA    . LYS G 117 ? 0.4592 0.4777 0.4577 -0.0393 0.0419  -0.0408 118 LYS G CA    
8490  C C     . LYS G 117 ? 0.3933 0.4096 0.3909 -0.0406 0.0418  -0.0389 118 LYS G C     
8491  O O     . LYS G 117 ? 0.3938 0.4105 0.3930 -0.0420 0.0429  -0.0379 118 LYS G O     
8492  C CB    . LYS G 117 ? 0.5005 0.5177 0.4953 -0.0386 0.0422  -0.0406 118 LYS G CB    
8493  C CG    . LYS G 117 ? 0.5354 0.5521 0.5284 -0.0401 0.0436  -0.0391 118 LYS G CG    
8494  C CD    . LYS G 117 ? 0.6180 0.6330 0.6069 -0.0395 0.0437  -0.0393 118 LYS G CD    
8495  C CE    . LYS G 117 ? 0.6598 0.6747 0.6465 -0.0409 0.0448  -0.0379 118 LYS G CE    
8496  N NZ    . LYS G 117 ? 0.6643 0.6774 0.6469 -0.0406 0.0448  -0.0384 118 LYS G NZ    
8497  N N     . MET G 118 ? 0.3645 0.3782 0.3593 -0.0399 0.0406  -0.0385 119 MET G N     
8498  C CA    . MET G 118 ? 0.3732 0.3850 0.3671 -0.0407 0.0404  -0.0368 119 MET G CA    
8499  C C     . MET G 118 ? 0.4281 0.4378 0.4183 -0.0407 0.0400  -0.0360 119 MET G C     
8500  O O     . MET G 118 ? 0.3735 0.3816 0.3616 -0.0396 0.0393  -0.0369 119 MET G O     
8501  C CB    . MET G 118 ? 0.3517 0.3625 0.3466 -0.0402 0.0394  -0.0374 119 MET G CB    
8502  C CG    . MET G 118 ? 0.3720 0.3807 0.3658 -0.0407 0.0392  -0.0358 119 MET G CG    
8503  S SD    . MET G 118 ? 0.4518 0.4591 0.4461 -0.0398 0.0383  -0.0366 119 MET G SD    
8504  C CE    . MET G 118 ? 0.4496 0.4593 0.4481 -0.0404 0.0387  -0.0380 119 MET G CE    
8505  N N     . GLU G 119 ? 0.4596 0.4693 0.4489 -0.0419 0.0405  -0.0344 120 GLU G N     
8506  C CA    . GLU G 119 ? 0.4452 0.4534 0.4315 -0.0422 0.0400  -0.0337 120 GLU G CA    
8507  C C     . GLU G 119 ? 0.4394 0.4465 0.4262 -0.0423 0.0394  -0.0327 120 GLU G C     
8508  O O     . GLU G 119 ? 0.4705 0.4780 0.4594 -0.0426 0.0396  -0.0318 120 GLU G O     
8509  C CB    . GLU G 119 ? 0.4847 0.4941 0.4698 -0.0432 0.0406  -0.0325 120 GLU G CB    
8510  C CG    . GLU G 119 ? 0.5700 0.5805 0.5546 -0.0430 0.0416  -0.0334 120 GLU G CG    
8511  C CD    . GLU G 119 ? 0.6518 0.6613 0.6343 -0.0422 0.0413  -0.0351 120 GLU G CD    
8512  O OE1   . GLU G 119 ? 0.6529 0.6608 0.6326 -0.0425 0.0408  -0.0352 120 GLU G OE1   
8513  O OE2   . GLU G 119 ? 0.8034 0.8135 0.7872 -0.0412 0.0418  -0.0364 120 GLU G OE2   
8514  N N     . PRO G 120 ? 0.3844 0.3896 0.3693 -0.0421 0.0388  -0.0330 121 PRO G N     
8515  C CA    . PRO G 120 ? 0.4090 0.4131 0.3942 -0.0423 0.0385  -0.0322 121 PRO G CA    
8516  C C     . PRO G 120 ? 0.4304 0.4360 0.4161 -0.0433 0.0384  -0.0305 121 PRO G C     
8517  O O     . PRO G 120 ? 0.4128 0.4196 0.3972 -0.0440 0.0384  -0.0302 121 PRO G O     
8518  C CB    . PRO G 120 ? 0.4235 0.4251 0.4063 -0.0418 0.0382  -0.0331 121 PRO G CB    
8519  C CG    . PRO G 120 ? 0.4267 0.4283 0.4074 -0.0421 0.0384  -0.0340 121 PRO G CG    
8520  C CD    . PRO G 120 ? 0.3941 0.3978 0.3762 -0.0417 0.0387  -0.0343 121 PRO G CD    
8521  N N     . GLY G 121 ? 0.4571 0.4626 0.4445 -0.0432 0.0384  -0.0294 122 GLY G N     
8522  C CA    . GLY G 121 ? 0.3842 0.3913 0.3723 -0.0438 0.0383  -0.0276 122 GLY G CA    
8523  C C     . GLY G 121 ? 0.3531 0.3595 0.3418 -0.0437 0.0381  -0.0273 122 GLY G C     
8524  O O     . GLY G 121 ? 0.3477 0.3519 0.3359 -0.0433 0.0383  -0.0283 122 GLY G O     
8525  N N     . ILE G 122 ? 0.3287 0.3370 0.3186 -0.0440 0.0379  -0.0258 123 ILE G N     
8526  C CA    . ILE G 122 ? 0.3590 0.3674 0.3501 -0.0440 0.0379  -0.0253 123 ILE G CA    
8527  C C     . ILE G 122 ? 0.3506 0.3580 0.3437 -0.0430 0.0386  -0.0244 123 ILE G C     
8528  O O     . ILE G 122 ? 0.3537 0.3622 0.3480 -0.0426 0.0388  -0.0229 123 ILE G O     
8529  C CB    . ILE G 122 ? 0.3837 0.3953 0.3754 -0.0447 0.0372  -0.0244 123 ILE G CB    
8530  C CG1   . ILE G 122 ? 0.3923 0.4045 0.3817 -0.0459 0.0365  -0.0257 123 ILE G CG1   
8531  C CG2   . ILE G 122 ? 0.3829 0.3951 0.3766 -0.0448 0.0373  -0.0240 123 ILE G CG2   
8532  C CD1   . ILE G 122 ? 0.4048 0.4208 0.3946 -0.0467 0.0354  -0.0251 123 ILE G CD1   
8533  N N     . SER G 123 ? 0.3159 0.3209 0.3089 -0.0426 0.0391  -0.0253 124 SER G N     
8534  C CA    . SER G 123 ? 0.3092 0.3127 0.3035 -0.0417 0.0398  -0.0248 124 SER G CA    
8535  C C     . SER G 123 ? 0.3363 0.3405 0.3323 -0.0414 0.0403  -0.0237 124 SER G C     
8536  O O     . SER G 123 ? 0.3236 0.3293 0.3198 -0.0420 0.0400  -0.0235 124 SER G O     
8537  C CB    . SER G 123 ? 0.3187 0.3194 0.3117 -0.0411 0.0400  -0.0265 124 SER G CB    
8538  O OG    . SER G 123 ? 0.3503 0.3495 0.3416 -0.0412 0.0401  -0.0272 124 SER G OG    
8539  N N     . ALA G 124 ? 0.3345 0.3377 0.3319 -0.0405 0.0411  -0.0230 125 ALA G N     
8540  C CA    . ALA G 124 ? 0.3727 0.3764 0.3720 -0.0399 0.0418  -0.0218 125 ALA G CA    
8541  C C     . ALA G 124 ? 0.3924 0.3952 0.3909 -0.0402 0.0421  -0.0228 125 ALA G C     
8542  O O     . ALA G 124 ? 0.3626 0.3669 0.3627 -0.0403 0.0425  -0.0220 125 ALA G O     
8543  C CB    . ALA G 124 ? 0.3681 0.3697 0.3684 -0.0389 0.0428  -0.0214 125 ALA G CB    
8544  N N     . GLU G 125 ? 0.4515 0.4516 0.4474 -0.0404 0.0421  -0.0244 126 GLU G N     
8545  C CA    . GLU G 125 ? 0.4826 0.4809 0.4770 -0.0405 0.0426  -0.0252 126 GLU G CA    
8546  C C     . GLU G 125 ? 0.4334 0.4338 0.4280 -0.0419 0.0423  -0.0252 126 GLU G C     
8547  O O     . GLU G 125 ? 0.3678 0.3683 0.3631 -0.0424 0.0431  -0.0251 126 GLU G O     
8548  C CB    . GLU G 125 ? 0.5188 0.5139 0.5100 -0.0400 0.0424  -0.0268 126 GLU G CB    
8549  C CG    . GLU G 125 ? 0.5469 0.5392 0.5355 -0.0400 0.0432  -0.0275 126 GLU G CG    
8550  C CD    . GLU G 125 ? 0.6075 0.5967 0.5926 -0.0389 0.0429  -0.0288 126 GLU G CD    
8551  O OE1   . GLU G 125 ? 0.7622 0.7502 0.7468 -0.0378 0.0428  -0.0293 126 GLU G OE1   
8552  O OE2   . GLU G 125 ? 0.7236 0.7115 0.7064 -0.0391 0.0427  -0.0295 126 GLU G OE2   
8553  N N     . ALA G 126 ? 0.4422 0.4441 0.4362 -0.0426 0.0412  -0.0254 127 ALA G N     
8554  C CA    . ALA G 126 ? 0.4071 0.4109 0.4010 -0.0441 0.0407  -0.0258 127 ALA G CA    
8555  C C     . ALA G 126 ? 0.3398 0.3477 0.3370 -0.0446 0.0405  -0.0246 127 ALA G C     
8556  O O     . ALA G 126 ? 0.3379 0.3475 0.3358 -0.0459 0.0405  -0.0250 127 ALA G O     
8557  C CB    . ALA G 126 ? 0.3717 0.3763 0.3641 -0.0445 0.0396  -0.0263 127 ALA G CB    
8558  N N     . CYS G 127 ? 0.3170 0.3265 0.3162 -0.0434 0.0404  -0.0231 128 CYS G N     
8559  C CA    . CYS G 127 ? 0.3551 0.3688 0.3575 -0.0433 0.0401  -0.0217 128 CYS G CA    
8560  C C     . CYS G 127 ? 0.3729 0.3864 0.3773 -0.0431 0.0414  -0.0216 128 CYS G C     
8561  O O     . CYS G 127 ? 0.3291 0.3463 0.3362 -0.0437 0.0413  -0.0213 128 CYS G O     
8562  C CB    . CYS G 127 ? 0.3758 0.3906 0.3793 -0.0418 0.0399  -0.0200 128 CYS G CB    
8563  S SG    . CYS G 127 ? 0.4073 0.4228 0.4086 -0.0420 0.0386  -0.0198 128 CYS G SG    
8564  N N     . LEU G 128 ? 0.3782 0.3875 0.3813 -0.0423 0.0427  -0.0220 129 LEU G N     
8565  C CA    . LEU G 128 ? 0.3706 0.3791 0.3751 -0.0419 0.0444  -0.0218 129 LEU G CA    
8566  C C     . LEU G 128 ? 0.3546 0.3635 0.3591 -0.0436 0.0450  -0.0229 129 LEU G C     
8567  O O     . LEU G 128 ? 0.3032 0.3151 0.3109 -0.0441 0.0456  -0.0225 129 LEU G O     
8568  C CB    . LEU G 128 ? 0.3883 0.3919 0.3903 -0.0407 0.0454  -0.0224 129 LEU G CB    
8569  C CG    . LEU G 128 ? 0.4037 0.4056 0.4062 -0.0400 0.0474  -0.0222 129 LEU G CG    
8570  C CD1   . LEU G 128 ? 0.4312 0.4295 0.4321 -0.0384 0.0480  -0.0224 129 LEU G CD1   
8571  C CD2   . LEU G 128 ? 0.4294 0.4290 0.4299 -0.0410 0.0485  -0.0233 129 LEU G CD2   
8572  N N     . TRP G 129 ? 0.3753 0.3812 0.3764 -0.0445 0.0448  -0.0242 130 TRP G N     
8573  C CA    . TRP G 129 ? 0.3731 0.3782 0.3736 -0.0462 0.0457  -0.0252 130 TRP G CA    
8574  C C     . TRP G 129 ? 0.3301 0.3407 0.3343 -0.0479 0.0449  -0.0252 130 TRP G C     
8575  O O     . TRP G 129 ? 0.3664 0.3781 0.3726 -0.0492 0.0461  -0.0257 130 TRP G O     
8576  C CB    . TRP G 129 ? 0.3828 0.3842 0.3791 -0.0467 0.0454  -0.0265 130 TRP G CB    
8577  C CG    . TRP G 129 ? 0.4191 0.4157 0.4117 -0.0449 0.0458  -0.0268 130 TRP G CG    
8578  C CD1   . TRP G 129 ? 0.4251 0.4200 0.4150 -0.0443 0.0447  -0.0274 130 TRP G CD1   
8579  C CD2   . TRP G 129 ? 0.4168 0.4101 0.4082 -0.0436 0.0473  -0.0266 130 TRP G CD2   
8580  N NE1   . TRP G 129 ? 0.4618 0.4531 0.4492 -0.0426 0.0452  -0.0277 130 TRP G NE1   
8581  C CE2   . TRP G 129 ? 0.4329 0.4230 0.4208 -0.0422 0.0467  -0.0272 130 TRP G CE2   
8582  C CE3   . TRP G 129 ? 0.4176 0.4107 0.4105 -0.0434 0.0490  -0.0260 130 TRP G CE3   
8583  C CZ2   . TRP G 129 ? 0.4315 0.4180 0.4171 -0.0406 0.0476  -0.0273 130 TRP G CZ2   
8584  C CZ3   . TRP G 129 ? 0.4288 0.4180 0.4191 -0.0418 0.0502  -0.0260 130 TRP G CZ3   
8585  C CH2   . TRP G 129 ? 0.4097 0.3956 0.3962 -0.0404 0.0494  -0.0267 130 TRP G CH2   
8586  N N     . ALA G 130 ? 0.3323 0.3464 0.3373 -0.0478 0.0430  -0.0247 131 ALA G N     
8587  C CA    . ALA G 130 ? 0.3168 0.3365 0.3246 -0.0492 0.0417  -0.0249 131 ALA G CA    
8588  C C     . ALA G 130 ? 0.3283 0.3527 0.3408 -0.0484 0.0417  -0.0236 131 ALA G C     
8589  O O     . ALA G 130 ? 0.3430 0.3718 0.3588 -0.0498 0.0416  -0.0241 131 ALA G O     
8590  C CB    . ALA G 130 ? 0.3214 0.3427 0.3275 -0.0491 0.0396  -0.0248 131 ALA G CB    
8591  N N     . ASP G 131 ? 0.3389 0.3626 0.3519 -0.0461 0.0420  -0.0220 132 ASP G N     
8592  C CA    . ASP G 131 ? 0.3308 0.3588 0.3481 -0.0447 0.0421  -0.0205 132 ASP G CA    
8593  C C     . ASP G 131 ? 0.3357 0.3634 0.3554 -0.0451 0.0443  -0.0208 132 ASP G C     
8594  O O     . ASP G 131 ? 0.3593 0.3922 0.3836 -0.0452 0.0443  -0.0204 132 ASP G O     
8595  C CB    . ASP G 131 ? 0.3453 0.3718 0.3620 -0.0422 0.0420  -0.0187 132 ASP G CB    
8596  C CG    . ASP G 131 ? 0.3528 0.3818 0.3688 -0.0416 0.0400  -0.0177 132 ASP G CG    
8597  O OD1   . ASP G 131 ? 0.3587 0.3919 0.3753 -0.0428 0.0384  -0.0181 132 ASP G OD1   
8598  O OD2   . ASP G 131 ? 0.3558 0.3824 0.3704 -0.0399 0.0402  -0.0165 132 ASP G OD2   
8599  N N     . LEU G 132 ? 0.3499 0.3718 0.3667 -0.0450 0.0461  -0.0214 133 LEU G N     
8600  C CA    . LEU G 132 ? 0.3887 0.4093 0.4069 -0.0451 0.0486  -0.0216 133 LEU G CA    
8601  C C     . LEU G 132 ? 0.4449 0.4647 0.4627 -0.0477 0.0496  -0.0232 133 LEU G C     
8602  O O     . LEU G 132 ? 0.4390 0.4577 0.4579 -0.0482 0.0519  -0.0235 133 LEU G O     
8603  C CB    . LEU G 132 ? 0.4124 0.4269 0.4272 -0.0434 0.0501  -0.0213 133 LEU G CB    
8604  C CG    . LEU G 132 ? 0.4132 0.4279 0.4290 -0.0409 0.0499  -0.0199 133 LEU G CG    
8605  C CD1   . LEU G 132 ? 0.4060 0.4220 0.4210 -0.0404 0.0476  -0.0193 133 LEU G CD1   
8606  C CD2   . LEU G 132 ? 0.4783 0.4872 0.4909 -0.0396 0.0516  -0.0201 133 LEU G CD2   
8607  N N     . GLY G 133 ? 0.4566 0.4768 0.4727 -0.0494 0.0480  -0.0243 134 GLY G N     
8608  C CA    . GLY G 133 ? 0.4531 0.4718 0.4683 -0.0520 0.0490  -0.0259 134 GLY G CA    
8609  C C     . GLY G 133 ? 0.4339 0.4456 0.4453 -0.0517 0.0516  -0.0263 134 GLY G C     
8610  O O     . GLY G 133 ? 0.4127 0.4235 0.4252 -0.0531 0.0539  -0.0268 134 GLY G O     
8611  N N     . ILE G 134 ? 0.4645 0.4714 0.4714 -0.0499 0.0513  -0.0260 135 ILE G N     
8612  C CA    . ILE G 134 ? 0.4136 0.4138 0.4159 -0.0492 0.0533  -0.0262 135 ILE G CA    
8613  C C     . ILE G 134 ? 0.4228 0.4191 0.4204 -0.0494 0.0524  -0.0272 135 ILE G C     
8614  O O     . ILE G 134 ? 0.3944 0.3923 0.3916 -0.0491 0.0502  -0.0273 135 ILE G O     
8615  C CB    . ILE G 134 ? 0.4214 0.4196 0.4226 -0.0465 0.0537  -0.0252 135 ILE G CB    
8616  C CG1   . ILE G 134 ? 0.4605 0.4621 0.4662 -0.0460 0.0549  -0.0243 135 ILE G CG1   
8617  C CG2   . ILE G 134 ? 0.4533 0.4446 0.4489 -0.0454 0.0552  -0.0256 135 ILE G CG2   
8618  C CD1   . ILE G 134 ? 0.4563 0.4556 0.4609 -0.0435 0.0555  -0.0235 135 ILE G CD1   
8619  N N     . ASP G 135 ? 0.4207 0.4116 0.4146 -0.0499 0.0543  -0.0278 136 ASP G N     
8620  C CA    . ASP G 135 ? 0.4509 0.4374 0.4399 -0.0496 0.0538  -0.0286 136 ASP G CA    
8621  C C     . ASP G 135 ? 0.4308 0.4120 0.4151 -0.0470 0.0544  -0.0283 136 ASP G C     
8622  O O     . ASP G 135 ? 0.4431 0.4208 0.4257 -0.0464 0.0567  -0.0279 136 ASP G O     
8623  C CB    . ASP G 135 ? 0.4598 0.4438 0.4478 -0.0519 0.0555  -0.0297 136 ASP G CB    
8624  C CG    . ASP G 135 ? 0.4542 0.4330 0.4368 -0.0514 0.0553  -0.0305 136 ASP G CG    
8625  O OD1   . ASP G 135 ? 0.4250 0.4025 0.4050 -0.0492 0.0538  -0.0302 136 ASP G OD1   
8626  O OD2   . ASP G 135 ? 0.5222 0.4982 0.5036 -0.0533 0.0568  -0.0314 136 ASP G OD2   
8627  N N     . PRO G 136 ? 0.4587 0.4394 0.4409 -0.0453 0.0524  -0.0284 137 PRO G N     
8628  C CA    . PRO G 136 ? 0.4536 0.4302 0.4317 -0.0428 0.0525  -0.0283 137 PRO G CA    
8629  C C     . PRO G 136 ? 0.4864 0.4568 0.4593 -0.0422 0.0543  -0.0286 137 PRO G C     
8630  O O     . PRO G 136 ? 0.5578 0.5246 0.5270 -0.0401 0.0550  -0.0284 137 PRO G O     
8631  C CB    . PRO G 136 ? 0.4676 0.4458 0.4453 -0.0418 0.0499  -0.0288 137 PRO G CB    
8632  C CG    . PRO G 136 ? 0.4509 0.4318 0.4304 -0.0438 0.0491  -0.0292 137 PRO G CG    
8633  C CD    . PRO G 136 ? 0.4384 0.4225 0.4219 -0.0459 0.0501  -0.0288 137 PRO G CD    
8634  N N     . GLY G 137 ? 0.4567 0.4257 0.4290 -0.0440 0.0552  -0.0291 138 GLY G N     
8635  C CA    . GLY G 137 ? 0.4609 0.4235 0.4280 -0.0434 0.0572  -0.0292 138 GLY G CA    
8636  C C     . GLY G 137 ? 0.4451 0.4051 0.4122 -0.0445 0.0605  -0.0286 138 GLY G C     
8637  O O     . GLY G 137 ? 0.5125 0.4664 0.4748 -0.0437 0.0627  -0.0284 138 GLY G O     
8638  N N     . ASN G 138 ? 0.4304 0.3953 0.4029 -0.0461 0.0608  -0.0284 139 ASN G N     
8639  C CA    . ASN G 138 ? 0.4601 0.4238 0.4339 -0.0475 0.0640  -0.0280 139 ASN G CA    
8640  C C     . ASN G 138 ? 0.4372 0.3949 0.4056 -0.0450 0.0660  -0.0272 139 ASN G C     
8641  O O     . ASN G 138 ? 0.4510 0.4032 0.4158 -0.0453 0.0689  -0.0269 139 ASN G O     
8642  C CB    . ASN G 138 ? 0.4978 0.4682 0.4783 -0.0487 0.0637  -0.0277 139 ASN G CB    
8643  C CG    . ASN G 138 ? 0.5069 0.4770 0.4897 -0.0506 0.0671  -0.0275 139 ASN G CG    
8644  O OD1   . ASN G 138 ? 0.5079 0.4788 0.4921 -0.0497 0.0685  -0.0267 139 ASN G OD1   
8645  N ND2   . ASN G 138 ? 0.5218 0.4907 0.5052 -0.0533 0.0687  -0.0283 139 ASN G ND2   
8646  N N     . SER G 139 ? 0.4490 0.4075 0.4165 -0.0426 0.0646  -0.0268 140 SER G N     
8647  C CA    . SER G 139 ? 0.4787 0.4322 0.4409 -0.0400 0.0660  -0.0262 140 SER G CA    
8648  C C     . SER G 139 ? 0.4477 0.4007 0.4067 -0.0372 0.0631  -0.0265 140 SER G C     
8649  O O     . SER G 139 ? 0.4208 0.3706 0.3754 -0.0348 0.0635  -0.0263 140 SER G O     
8650  C CB    . SER G 139 ? 0.4867 0.4415 0.4513 -0.0400 0.0680  -0.0256 140 SER G CB    
8651  O OG    . SER G 139 ? 0.4951 0.4562 0.4652 -0.0402 0.0659  -0.0256 140 SER G OG    
8652  N N     . GLY G 140 ? 0.4496 0.4061 0.4108 -0.0376 0.0603  -0.0272 141 GLY G N     
8653  C CA    . GLY G 140 ? 0.4075 0.3643 0.3665 -0.0354 0.0576  -0.0278 141 GLY G CA    
8654  C C     . GLY G 140 ? 0.3852 0.3474 0.3490 -0.0355 0.0556  -0.0280 141 GLY G C     
8655  O O     . GLY G 140 ? 0.3212 0.2863 0.2891 -0.0367 0.0566  -0.0274 141 GLY G O     
8656  N N     . HIS G 141 ? 0.3939 0.3575 0.3571 -0.0343 0.0531  -0.0287 142 HIS G N     
8657  C CA    . HIS G 141 ? 0.3623 0.3305 0.3298 -0.0345 0.0513  -0.0289 142 HIS G CA    
8658  C C     . HIS G 141 ? 0.3454 0.3130 0.3106 -0.0324 0.0496  -0.0299 142 HIS G C     
8659  O O     . HIS G 141 ? 0.3785 0.3441 0.3401 -0.0311 0.0486  -0.0306 142 HIS G O     
8660  C CB    . HIS G 141 ? 0.4171 0.3893 0.3883 -0.0363 0.0499  -0.0290 142 HIS G CB    
8661  C CG    . HIS G 141 ? 0.4200 0.3960 0.3943 -0.0362 0.0480  -0.0292 142 HIS G CG    
8662  N ND1   . HIS G 141 ? 0.4740 0.4521 0.4492 -0.0366 0.0462  -0.0297 142 HIS G ND1   
8663  C CD2   . HIS G 141 ? 0.4635 0.4410 0.4400 -0.0358 0.0477  -0.0290 142 HIS G CD2   
8664  C CE1   . HIS G 141 ? 0.4669 0.4478 0.4448 -0.0365 0.0451  -0.0298 142 HIS G CE1   
8665  N NE2   . HIS G 141 ? 0.4781 0.4586 0.4568 -0.0360 0.0460  -0.0294 142 HIS G NE2   
8666  N N     . GLN G 142 ? 0.3687 0.3379 0.3360 -0.0322 0.0493  -0.0300 143 GLN G N     
8667  C CA    . GLN G 142 ? 0.4138 0.3831 0.3799 -0.0307 0.0476  -0.0312 143 GLN G CA    
8668  C C     . GLN G 142 ? 0.4079 0.3810 0.3789 -0.0317 0.0468  -0.0313 143 GLN G C     
8669  O O     . GLN G 142 ? 0.5120 0.4865 0.4863 -0.0327 0.0479  -0.0303 143 GLN G O     
8670  C CB    . GLN G 142 ? 0.4269 0.3927 0.3890 -0.0289 0.0486  -0.0316 143 GLN G CB    
8671  C CG    . GLN G 142 ? 0.5115 0.4727 0.4678 -0.0275 0.0498  -0.0314 143 GLN G CG    
8672  C CD    . GLN G 142 ? 0.5022 0.4600 0.4540 -0.0255 0.0505  -0.0319 143 GLN G CD    
8673  O OE1   . GLN G 142 ? 0.4895 0.4449 0.4362 -0.0234 0.0495  -0.0327 143 GLN G OE1   
8674  N NE2   . GLN G 142 ? 0.5287 0.4863 0.4820 -0.0260 0.0524  -0.0314 143 GLN G NE2   
8675  N N     . SER G 143 ? 0.3708 0.3456 0.3424 -0.0314 0.0448  -0.0325 144 SER G N     
8676  C CA    . SER G 143 ? 0.3779 0.3555 0.3537 -0.0323 0.0442  -0.0326 144 SER G CA    
8677  C C     . SER G 143 ? 0.3763 0.3535 0.3511 -0.0314 0.0431  -0.0344 144 SER G C     
8678  O O     . SER G 143 ? 0.3571 0.3341 0.3296 -0.0304 0.0416  -0.0357 144 SER G O     
8679  C CB    . SER G 143 ? 0.3761 0.3569 0.3548 -0.0336 0.0432  -0.0321 144 SER G CB    
8680  O OG    . SER G 143 ? 0.4672 0.4490 0.4475 -0.0348 0.0442  -0.0307 144 SER G OG    
8681  N N     . PHE G 144 ? 0.3355 0.3126 0.3123 -0.0317 0.0438  -0.0345 145 PHE G N     
8682  C CA    . PHE G 144 ? 0.3823 0.3591 0.3588 -0.0312 0.0428  -0.0365 145 PHE G CA    
8683  C C     . PHE G 144 ? 0.3944 0.3726 0.3752 -0.0325 0.0434  -0.0363 145 PHE G C     
8684  O O     . PHE G 144 ? 0.3996 0.3782 0.3828 -0.0331 0.0448  -0.0344 145 PHE G O     
8685  C CB    . PHE G 144 ? 0.4265 0.4000 0.3991 -0.0298 0.0436  -0.0374 145 PHE G CB    
8686  C CG    . PHE G 144 ? 0.3903 0.3615 0.3577 -0.0282 0.0433  -0.0376 145 PHE G CG    
8687  C CD1   . PHE G 144 ? 0.4024 0.3738 0.3669 -0.0269 0.0413  -0.0393 145 PHE G CD1   
8688  C CD2   . PHE G 144 ? 0.4513 0.4200 0.4166 -0.0278 0.0453  -0.0360 145 PHE G CD2   
8689  C CE1   . PHE G 144 ? 0.4279 0.3967 0.3871 -0.0251 0.0412  -0.0391 145 PHE G CE1   
8690  C CE2   . PHE G 144 ? 0.4749 0.4408 0.4350 -0.0262 0.0455  -0.0359 145 PHE G CE2   
8691  C CZ    . PHE G 144 ? 0.4752 0.4409 0.4320 -0.0247 0.0434  -0.0374 145 PHE G CZ    
8692  N N     . GLU G 145 ? 0.4417 0.4208 0.4236 -0.0330 0.0423  -0.0381 146 GLU G N     
8693  C CA    . GLU G 145 ? 0.4334 0.4128 0.4189 -0.0341 0.0431  -0.0381 146 GLU G CA    
8694  C C     . GLU G 145 ? 0.4244 0.4007 0.4085 -0.0335 0.0443  -0.0389 146 GLU G C     
8695  O O     . GLU G 145 ? 0.4095 0.3844 0.3908 -0.0328 0.0435  -0.0412 146 GLU G O     
8696  C CB    . GLU G 145 ? 0.4642 0.4458 0.4518 -0.0352 0.0417  -0.0400 146 GLU G CB    
8697  C CG    . GLU G 145 ? 0.4399 0.4219 0.4315 -0.0367 0.0429  -0.0394 146 GLU G CG    
8698  C CD    . GLU G 145 ? 0.4935 0.4730 0.4855 -0.0370 0.0439  -0.0409 146 GLU G CD    
8699  O OE1   . GLU G 145 ? 0.4863 0.4639 0.4754 -0.0361 0.0435  -0.0427 146 GLU G OE1   
8700  O OE2   . GLU G 145 ? 0.4719 0.4508 0.4669 -0.0381 0.0453  -0.0402 146 GLU G OE2   
8701  N N     . ALA G 146 ? 0.4389 0.4141 0.4248 -0.0335 0.0463  -0.0371 147 ALA G N     
8702  C CA    . ALA G 146 ? 0.4240 0.3961 0.4085 -0.0326 0.0479  -0.0374 147 ALA G CA    
8703  C C     . ALA G 146 ? 0.4144 0.3847 0.3970 -0.0326 0.0472  -0.0405 147 ALA G C     
8704  O O     . ALA G 146 ? 0.4347 0.4028 0.4133 -0.0314 0.0472  -0.0418 147 ALA G O     
8705  C CB    . ALA G 146 ? 0.4417 0.4134 0.4296 -0.0329 0.0498  -0.0355 147 ALA G CB    
8706  N N     . SER G 147 ? 0.3820 0.3531 0.3673 -0.0340 0.0467  -0.0418 148 SER G N     
8707  C CA    . SER G 147 ? 0.3859 0.3555 0.3703 -0.0345 0.0462  -0.0450 148 SER G CA    
8708  C C     . SER G 147 ? 0.4023 0.3731 0.3832 -0.0337 0.0438  -0.0473 148 SER G C     
8709  O O     . SER G 147 ? 0.4076 0.3765 0.3854 -0.0330 0.0434  -0.0497 148 SER G O     
8710  C CB    . SER G 147 ? 0.3768 0.3474 0.3653 -0.0364 0.0464  -0.0459 148 SER G CB    
8711  O OG    . SER G 147 ? 0.3689 0.3374 0.3599 -0.0368 0.0488  -0.0439 148 SER G OG    
8712  N N     . GLN G 148 ? 0.3785 0.3524 0.3596 -0.0336 0.0422  -0.0467 149 GLN G N     
8713  C CA    . GLN G 148 ? 0.3890 0.3642 0.3669 -0.0324 0.0399  -0.0486 149 GLN G CA    
8714  C C     . GLN G 148 ? 0.3851 0.3573 0.3575 -0.0303 0.0402  -0.0483 149 GLN G C     
8715  O O     . GLN G 148 ? 0.3776 0.3494 0.3462 -0.0290 0.0387  -0.0504 149 GLN G O     
8716  C CB    . GLN G 148 ? 0.4241 0.4027 0.4033 -0.0325 0.0385  -0.0476 149 GLN G CB    
8717  C CG    . GLN G 148 ? 0.4642 0.4444 0.4403 -0.0310 0.0360  -0.0495 149 GLN G CG    
8718  C CD    . GLN G 148 ? 0.4932 0.4760 0.4701 -0.0307 0.0351  -0.0483 149 GLN G CD    
8719  O OE1   . GLN G 148 ? 0.4329 0.4147 0.4061 -0.0290 0.0347  -0.0473 149 GLN G OE1   
8720  N NE2   . GLN G 148 ? 0.5059 0.4917 0.4875 -0.0325 0.0349  -0.0483 149 GLN G NE2   
8721  N N     . PHE G 149 ? 0.3912 0.3616 0.3633 -0.0299 0.0423  -0.0456 150 PHE G N     
8722  C CA    . PHE G 149 ? 0.3948 0.3621 0.3620 -0.0281 0.0433  -0.0449 150 PHE G CA    
8723  C C     . PHE G 149 ? 0.4184 0.3827 0.3830 -0.0275 0.0440  -0.0469 150 PHE G C     
8724  O O     . PHE G 149 ? 0.3705 0.3324 0.3297 -0.0258 0.0440  -0.0477 150 PHE G O     
8725  C CB    . PHE G 149 ? 0.4324 0.3992 0.4012 -0.0283 0.0455  -0.0418 150 PHE G CB    
8726  C CG    . PHE G 149 ? 0.4443 0.4079 0.4087 -0.0268 0.0472  -0.0408 150 PHE G CG    
8727  C CD1   . PHE G 149 ? 0.4452 0.4059 0.4083 -0.0262 0.0492  -0.0410 150 PHE G CD1   
8728  C CD2   . PHE G 149 ? 0.4789 0.4422 0.4404 -0.0259 0.0470  -0.0397 150 PHE G CD2   
8729  C CE1   . PHE G 149 ? 0.4416 0.3994 0.4007 -0.0248 0.0510  -0.0401 150 PHE G CE1   
8730  C CE2   . PHE G 149 ? 0.4720 0.4321 0.4295 -0.0247 0.0489  -0.0387 150 PHE G CE2   
8731  C CZ    . PHE G 149 ? 0.4439 0.4014 0.4003 -0.0241 0.0510  -0.0389 150 PHE G CZ    
8732  N N     . MET G 150 ? 0.4435 0.4077 0.4116 -0.0289 0.0447  -0.0479 151 MET G N     
8733  C CA    . MET G 150 ? 0.4627 0.4236 0.4286 -0.0286 0.0457  -0.0499 151 MET G CA    
8734  C C     . MET G 150 ? 0.4598 0.4218 0.4241 -0.0289 0.0432  -0.0537 151 MET G C     
8735  O O     . MET G 150 ? 0.5341 0.4938 0.4938 -0.0277 0.0429  -0.0558 151 MET G O     
8736  C CB    . MET G 150 ? 0.4750 0.4347 0.4453 -0.0300 0.0479  -0.0492 151 MET G CB    
8737  C CG    . MET G 150 ? 0.4791 0.4379 0.4510 -0.0294 0.0505  -0.0458 151 MET G CG    
8738  S SD    . MET G 150 ? 0.5775 0.5348 0.5543 -0.0304 0.0529  -0.0447 151 MET G SD    
8739  C CE    . MET G 150 ? 0.5785 0.5310 0.5519 -0.0298 0.0544  -0.0476 151 MET G CE    
8740  N N     . PHE G 151 ? 0.4688 0.4345 0.4368 -0.0303 0.0414  -0.0547 152 PHE G N     
8741  C CA    . PHE G 151 ? 0.4228 0.3905 0.3908 -0.0310 0.0390  -0.0585 152 PHE G CA    
8742  C C     . PHE G 151 ? 0.4459 0.4152 0.4092 -0.0289 0.0363  -0.0596 152 PHE G C     
8743  O O     . PHE G 151 ? 0.4561 0.4257 0.4166 -0.0283 0.0345  -0.0628 152 PHE G O     
8744  C CB    . PHE G 151 ? 0.4035 0.3745 0.3777 -0.0334 0.0385  -0.0590 152 PHE G CB    
8745  C CG    . PHE G 151 ? 0.3900 0.3590 0.3684 -0.0353 0.0412  -0.0580 152 PHE G CG    
8746  C CD1   . PHE G 151 ? 0.4186 0.3830 0.3953 -0.0350 0.0434  -0.0580 152 PHE G CD1   
8747  C CD2   . PHE G 151 ? 0.3671 0.3383 0.3507 -0.0372 0.0416  -0.0569 152 PHE G CD2   
8748  C CE1   . PHE G 151 ? 0.4388 0.4010 0.4191 -0.0364 0.0460  -0.0569 152 PHE G CE1   
8749  C CE2   . PHE G 151 ? 0.3705 0.3394 0.3574 -0.0386 0.0442  -0.0557 152 PHE G CE2   
8750  C CZ    . PHE G 151 ? 0.3849 0.3493 0.3702 -0.0381 0.0463  -0.0557 152 PHE G CZ    
8751  N N     . PHE G 152 ? 0.4305 0.4008 0.3928 -0.0277 0.0360  -0.0570 153 PHE G N     
8752  C CA    . PHE G 152 ? 0.4451 0.4167 0.4030 -0.0254 0.0337  -0.0576 153 PHE G CA    
8753  C C     . PHE G 152 ? 0.4472 0.4149 0.3995 -0.0232 0.0352  -0.0552 153 PHE G C     
8754  O O     . PHE G 152 ? 0.4447 0.4096 0.3975 -0.0236 0.0379  -0.0530 153 PHE G O     
8755  C CB    . PHE G 152 ? 0.4661 0.4421 0.4277 -0.0259 0.0321  -0.0570 153 PHE G CB    
8756  C CG    . PHE G 152 ? 0.4688 0.4488 0.4362 -0.0282 0.0309  -0.0594 153 PHE G CG    
8757  C CD1   . PHE G 152 ? 0.5214 0.5042 0.4885 -0.0280 0.0282  -0.0631 153 PHE G CD1   
8758  C CD2   . PHE G 152 ? 0.4727 0.4537 0.4458 -0.0306 0.0324  -0.0580 153 PHE G CD2   
8759  C CE1   . PHE G 152 ? 0.4846 0.4711 0.4574 -0.0305 0.0274  -0.0655 153 PHE G CE1   
8760  C CE2   . PHE G 152 ? 0.4819 0.4661 0.4601 -0.0328 0.0318  -0.0601 153 PHE G CE2   
8761  C CZ    . PHE G 152 ? 0.4835 0.4705 0.4619 -0.0329 0.0294  -0.0639 153 PHE G CZ    
8762  N N     . ASN G 153 ? 0.4728 0.4405 0.4199 -0.0207 0.0334  -0.0555 154 ASN G N     
8763  C CA    . ASN G 153 ? 0.4647 0.4281 0.4055 -0.0184 0.0349  -0.0535 154 ASN G CA    
8764  C C     . ASN G 153 ? 0.4489 0.4124 0.3907 -0.0183 0.0359  -0.0504 154 ASN G C     
8765  O O     . ASN G 153 ? 0.4192 0.3846 0.3602 -0.0172 0.0340  -0.0504 154 ASN G O     
8766  C CB    . ASN G 153 ? 0.4462 0.4086 0.3800 -0.0155 0.0328  -0.0554 154 ASN G CB    
8767  C CG    . ASN G 153 ? 0.4582 0.4201 0.3905 -0.0157 0.0321  -0.0587 154 ASN G CG    
8768  O OD1   . ASN G 153 ? 0.4747 0.4333 0.4066 -0.0165 0.0346  -0.0585 154 ASN G OD1   
8769  N ND2   . ASN G 153 ? 0.4201 0.3854 0.3517 -0.0151 0.0288  -0.0619 154 ASN G ND2   
8770  N N     . HIS G 154 ? 0.4941 0.4555 0.4377 -0.0194 0.0388  -0.0479 155 HIS G N     
8771  C CA    . HIS G 154 ? 0.4669 0.4279 0.4112 -0.0196 0.0401  -0.0451 155 HIS G CA    
8772  C C     . HIS G 154 ? 0.4866 0.4432 0.4268 -0.0186 0.0430  -0.0432 155 HIS G C     
8773  O O     . HIS G 154 ? 0.4905 0.4453 0.4311 -0.0191 0.0450  -0.0431 155 HIS G O     
8774  C CB    . HIS G 154 ? 0.4639 0.4279 0.4154 -0.0222 0.0408  -0.0439 155 HIS G CB    
8775  C CG    . HIS G 154 ? 0.4777 0.4460 0.4331 -0.0232 0.0384  -0.0450 155 HIS G CG    
8776  N ND1   . HIS G 154 ? 0.4754 0.4450 0.4288 -0.0218 0.0364  -0.0455 155 HIS G ND1   
8777  C CD2   . HIS G 154 ? 0.4738 0.4450 0.4348 -0.0253 0.0381  -0.0456 155 HIS G CD2   
8778  C CE1   . HIS G 154 ? 0.4830 0.4568 0.4411 -0.0231 0.0349  -0.0465 155 HIS G CE1   
8779  N NE2   . HIS G 154 ? 0.4710 0.4456 0.4336 -0.0253 0.0359  -0.0465 155 HIS G NE2   
8780  N N     . VAL G 155 ? 0.4783 0.4328 0.4146 -0.0172 0.0435  -0.0416 156 VAL G N     
8781  C CA    . VAL G 155 ? 0.4670 0.4170 0.3994 -0.0164 0.0466  -0.0397 156 VAL G CA    
8782  C C     . VAL G 155 ? 0.4688 0.4194 0.4048 -0.0181 0.0483  -0.0373 156 VAL G C     
8783  O O     . VAL G 155 ? 0.4343 0.3851 0.3696 -0.0178 0.0475  -0.0367 156 VAL G O     
8784  C CB    . VAL G 155 ? 0.4953 0.4414 0.4192 -0.0134 0.0463  -0.0398 156 VAL G CB    
8785  C CG1   . VAL G 155 ? 0.5068 0.4480 0.4268 -0.0128 0.0499  -0.0376 156 VAL G CG1   
8786  C CG2   . VAL G 155 ? 0.5255 0.4713 0.4454 -0.0116 0.0443  -0.0424 156 VAL G CG2   
8787  N N     . PRO G 156 ? 0.4836 0.4345 0.4237 -0.0199 0.0507  -0.0361 157 PRO G N     
8788  C CA    . PRO G 156 ? 0.4932 0.4452 0.4370 -0.0217 0.0522  -0.0341 157 PRO G CA    
8789  C C     . PRO G 156 ? 0.4823 0.4301 0.4217 -0.0209 0.0548  -0.0326 157 PRO G C     
8790  O O     . PRO G 156 ? 0.4633 0.4071 0.3970 -0.0191 0.0561  -0.0327 157 PRO G O     
8791  C CB    . PRO G 156 ? 0.4909 0.4451 0.4405 -0.0234 0.0537  -0.0336 157 PRO G CB    
8792  C CG    . PRO G 156 ? 0.4915 0.4430 0.4378 -0.0220 0.0546  -0.0347 157 PRO G CG    
8793  C CD    . PRO G 156 ? 0.4958 0.4464 0.4373 -0.0202 0.0520  -0.0367 157 PRO G CD    
8794  N N     . ASP G 157 ? 0.4442 0.3928 0.3861 -0.0225 0.0556  -0.0312 158 ASP G N     
8795  C CA    . ASP G 157 ? 0.4292 0.3740 0.3681 -0.0225 0.0586  -0.0297 158 ASP G CA    
8796  C C     . ASP G 157 ? 0.4518 0.3983 0.3959 -0.0247 0.0612  -0.0286 158 ASP G C     
8797  O O     . ASP G 157 ? 0.4067 0.3573 0.3568 -0.0268 0.0606  -0.0283 158 ASP G O     
8798  C CB    . ASP G 157 ? 0.4283 0.3723 0.3661 -0.0227 0.0579  -0.0293 158 ASP G CB    
8799  C CG    . ASP G 157 ? 0.3988 0.3385 0.3339 -0.0232 0.0611  -0.0278 158 ASP G CG    
8800  O OD1   . ASP G 157 ? 0.3809 0.3188 0.3156 -0.0236 0.0641  -0.0270 158 ASP G OD1   
8801  O OD2   . ASP G 157 ? 0.4706 0.4087 0.4039 -0.0232 0.0609  -0.0274 158 ASP G OD2   
8802  N N     . PRO G 158 ? 0.5044 0.4481 0.4465 -0.0241 0.0641  -0.0281 159 PRO G N     
8803  C CA    . PRO G 158 ? 0.5192 0.4652 0.4668 -0.0258 0.0665  -0.0272 159 PRO G CA    
8804  C C     . PRO G 158 ? 0.5015 0.4485 0.4523 -0.0280 0.0684  -0.0260 159 PRO G C     
8805  O O     . PRO G 158 ? 0.4853 0.4348 0.4410 -0.0296 0.0704  -0.0253 159 PRO G O     
8806  C CB    . PRO G 158 ? 0.5840 0.5260 0.5272 -0.0241 0.0692  -0.0272 159 PRO G CB    
8807  C CG    . PRO G 158 ? 0.6072 0.5437 0.5418 -0.0220 0.0692  -0.0273 159 PRO G CG    
8808  C CD    . PRO G 158 ? 0.5741 0.5123 0.5083 -0.0215 0.0652  -0.0283 159 PRO G CD    
8809  N N     . THR G 159 ? 0.4614 0.4064 0.4095 -0.0282 0.0678  -0.0259 160 THR G N     
8810  C CA    . THR G 159 ? 0.4429 0.3882 0.3935 -0.0306 0.0695  -0.0251 160 THR G CA    
8811  C C     . THR G 159 ? 0.4104 0.3612 0.3668 -0.0325 0.0669  -0.0255 160 THR G C     
8812  O O     . THR G 159 ? 0.4022 0.3549 0.3623 -0.0349 0.0678  -0.0252 160 THR G O     
8813  C CB    . THR G 159 ? 0.4338 0.3730 0.3776 -0.0296 0.0710  -0.0247 160 THR G CB    
8814  O OG1   . THR G 159 ? 0.4395 0.3783 0.3804 -0.0281 0.0677  -0.0254 160 THR G OG1   
8815  C CG2   . THR G 159 ? 0.4675 0.4009 0.4048 -0.0275 0.0737  -0.0241 160 THR G CG2   
8816  N N     . THR G 160 ? 0.4063 0.3594 0.3631 -0.0315 0.0636  -0.0264 161 THR G N     
8817  C CA    . THR G 160 ? 0.3585 0.3160 0.3196 -0.0330 0.0611  -0.0267 161 THR G CA    
8818  C C     . THR G 160 ? 0.3312 0.2941 0.2987 -0.0339 0.0603  -0.0266 161 THR G C     
8819  O O     . THR G 160 ? 0.3420 0.3050 0.3102 -0.0330 0.0613  -0.0264 161 THR G O     
8820  C CB    . THR G 160 ? 0.3615 0.3183 0.3194 -0.0313 0.0582  -0.0277 161 THR G CB    
8821  O OG1   . THR G 160 ? 0.4171 0.3749 0.3751 -0.0300 0.0570  -0.0283 161 THR G OG1   
8822  C CG2   . THR G 160 ? 0.3781 0.3292 0.3290 -0.0296 0.0589  -0.0277 161 THR G CG2   
8823  N N     . HIS G 161 ? 0.3317 0.2990 0.3036 -0.0355 0.0586  -0.0266 162 HIS G N     
8824  C CA    . HIS G 161 ? 0.3141 0.2863 0.2913 -0.0359 0.0573  -0.0263 162 HIS G CA    
8825  C C     . HIS G 161 ? 0.3244 0.2963 0.3000 -0.0344 0.0551  -0.0272 162 HIS G C     
8826  O O     . HIS G 161 ? 0.3226 0.2939 0.2960 -0.0342 0.0533  -0.0279 162 HIS G O     
8827  C CB    . HIS G 161 ? 0.3201 0.2969 0.3018 -0.0380 0.0562  -0.0260 162 HIS G CB    
8828  C CG    . HIS G 161 ? 0.2981 0.2769 0.2832 -0.0397 0.0582  -0.0254 162 HIS G CG    
8829  N ND1   . HIS G 161 ? 0.2749 0.2518 0.2586 -0.0412 0.0596  -0.0256 162 HIS G ND1   
8830  C CD2   . HIS G 161 ? 0.2899 0.2726 0.2800 -0.0402 0.0591  -0.0247 162 HIS G CD2   
8831  C CE1   . HIS G 161 ? 0.2918 0.2716 0.2799 -0.0428 0.0613  -0.0252 162 HIS G CE1   
8832  N NE2   . HIS G 161 ? 0.3032 0.2869 0.2952 -0.0421 0.0609  -0.0246 162 HIS G NE2   
8833  N N     A LEU G 162 ? 0.3061 0.2783 0.2828 -0.0335 0.0554  -0.0272 163 LEU G N     
8834  N N     B LEU G 162 ? 0.3235 0.2958 0.3003 -0.0335 0.0554  -0.0272 163 LEU G N     
8835  C CA    A LEU G 162 ? 0.2973 0.2690 0.2728 -0.0323 0.0536  -0.0282 163 LEU G CA    
8836  C CA    B LEU G 162 ? 0.3253 0.2970 0.3008 -0.0323 0.0536  -0.0282 163 LEU G CA    
8837  C C     A LEU G 162 ? 0.3020 0.2777 0.2826 -0.0330 0.0526  -0.0278 163 LEU G C     
8838  C C     B LEU G 162 ? 0.3184 0.2940 0.2989 -0.0330 0.0526  -0.0278 163 LEU G C     
8839  O O     A LEU G 162 ? 0.3162 0.2936 0.3002 -0.0332 0.0538  -0.0268 163 LEU G O     
8840  O O     B LEU G 162 ? 0.3280 0.3052 0.3118 -0.0332 0.0539  -0.0268 163 LEU G O     
8841  C CB    A LEU G 162 ? 0.2846 0.2527 0.2566 -0.0306 0.0549  -0.0289 163 LEU G CB    
8842  C CB    B LEU G 162 ? 0.3322 0.3002 0.3041 -0.0306 0.0550  -0.0288 163 LEU G CB    
8843  C CG    A LEU G 162 ? 0.2908 0.2582 0.2615 -0.0296 0.0533  -0.0304 163 LEU G CG    
8844  C CG    B LEU G 162 ? 0.3557 0.3228 0.3257 -0.0295 0.0533  -0.0304 163 LEU G CG    
8845  C CD1   A LEU G 162 ? 0.2896 0.2564 0.2570 -0.0290 0.0510  -0.0316 163 LEU G CD1   
8846  C CD1   B LEU G 162 ? 0.3794 0.3420 0.3435 -0.0277 0.0541  -0.0314 163 LEU G CD1   
8847  C CD2   A LEU G 162 ? 0.2892 0.2534 0.2570 -0.0282 0.0548  -0.0310 163 LEU G CD2   
8848  C CD2   B LEU G 162 ? 0.3526 0.3217 0.3268 -0.0298 0.0532  -0.0304 163 LEU G CD2   
8849  N N     . LEU G 163 ? 0.3183 0.2952 0.2991 -0.0332 0.0505  -0.0285 164 LEU G N     
8850  C CA    . LEU G 163 ? 0.3019 0.2819 0.2868 -0.0338 0.0496  -0.0281 164 LEU G CA    
8851  C C     . LEU G 163 ? 0.2759 0.2543 0.2597 -0.0330 0.0489  -0.0294 164 LEU G C     
8852  O O     . LEU G 163 ? 0.2698 0.2470 0.2507 -0.0326 0.0476  -0.0309 164 LEU G O     
8853  C CB    . LEU G 163 ? 0.3304 0.3133 0.3169 -0.0350 0.0481  -0.0277 164 LEU G CB    
8854  C CG    . LEU G 163 ? 0.3592 0.3440 0.3471 -0.0362 0.0485  -0.0267 164 LEU G CG    
8855  C CD1   . LEU G 163 ? 0.3410 0.3288 0.3304 -0.0373 0.0469  -0.0265 164 LEU G CD1   
8856  C CD2   . LEU G 163 ? 0.3924 0.3791 0.3836 -0.0363 0.0500  -0.0254 164 LEU G CD2   
8857  N N     . LEU G 164 ? 0.2734 0.2520 0.2597 -0.0328 0.0497  -0.0290 165 LEU G N     
8858  C CA    . LEU G 164 ? 0.2738 0.2513 0.2601 -0.0326 0.0492  -0.0304 165 LEU G CA    
8859  C C     . LEU G 164 ? 0.2679 0.2479 0.2580 -0.0335 0.0487  -0.0295 165 LEU G C     
8860  O O     . LEU G 164 ? 0.2498 0.2308 0.2428 -0.0334 0.0498  -0.0278 165 LEU G O     
8861  C CB    . LEU G 164 ? 0.2843 0.2588 0.2695 -0.0315 0.0508  -0.0309 165 LEU G CB    
8862  C CG    . LEU G 164 ? 0.2978 0.2694 0.2784 -0.0304 0.0515  -0.0319 165 LEU G CG    
8863  C CD1   . LEU G 164 ? 0.2956 0.2641 0.2750 -0.0294 0.0531  -0.0327 165 LEU G CD1   
8864  C CD2   . LEU G 164 ? 0.2977 0.2686 0.2747 -0.0302 0.0495  -0.0337 165 LEU G CD2   
8865  N N     . TRP G 165 ? 0.2739 0.2550 0.2641 -0.0342 0.0471  -0.0305 166 TRP G N     
8866  C CA    . TRP G 165 ? 0.3045 0.2876 0.2978 -0.0351 0.0468  -0.0296 166 TRP G CA    
8867  C C     . TRP G 165 ? 0.3035 0.2847 0.2979 -0.0351 0.0476  -0.0305 166 TRP G C     
8868  O O     . TRP G 165 ? 0.3050 0.2839 0.2975 -0.0348 0.0476  -0.0325 166 TRP G O     
8869  C CB    . TRP G 165 ? 0.3276 0.3127 0.3206 -0.0359 0.0451  -0.0304 166 TRP G CB    
8870  C CG    . TRP G 165 ? 0.3658 0.3522 0.3573 -0.0360 0.0445  -0.0298 166 TRP G CG    
8871  C CD1   . TRP G 165 ? 0.4085 0.3934 0.3973 -0.0353 0.0447  -0.0301 166 TRP G CD1   
8872  C CD2   . TRP G 165 ? 0.3770 0.3661 0.3698 -0.0369 0.0437  -0.0288 166 TRP G CD2   
8873  N NE1   . TRP G 165 ? 0.3794 0.3657 0.3678 -0.0359 0.0442  -0.0295 166 TRP G NE1   
8874  C CE2   . TRP G 165 ? 0.4080 0.3970 0.3987 -0.0368 0.0435  -0.0288 166 TRP G CE2   
8875  C CE3   . TRP G 165 ? 0.3643 0.3556 0.3592 -0.0377 0.0434  -0.0280 166 TRP G CE3   
8876  C CZ2   . TRP G 165 ? 0.4098 0.4009 0.4008 -0.0377 0.0428  -0.0283 166 TRP G CZ2   
8877  C CZ3   . TRP G 165 ? 0.4034 0.3969 0.3982 -0.0383 0.0427  -0.0273 166 TRP G CZ3   
8878  C CH2   . TRP G 165 ? 0.3613 0.3548 0.3544 -0.0384 0.0423  -0.0276 166 TRP G CH2   
8879  N N     . GLN G 166 ? 0.3050 0.2870 0.3022 -0.0356 0.0483  -0.0290 167 GLN G N     
8880  C CA    . GLN G 166 ? 0.3744 0.3541 0.3728 -0.0358 0.0494  -0.0296 167 GLN G CA    
8881  C C     . GLN G 166 ? 0.3882 0.3647 0.3854 -0.0348 0.0508  -0.0303 167 GLN G C     
8882  O O     . GLN G 166 ? 0.4199 0.3939 0.4161 -0.0350 0.0510  -0.0326 167 GLN G O     
8883  C CB    . GLN G 166 ? 0.3828 0.3625 0.3811 -0.0371 0.0484  -0.0320 167 GLN G CB    
8884  C CG    . GLN G 166 ? 0.3961 0.3787 0.3958 -0.0381 0.0475  -0.0313 167 GLN G CG    
8885  C CD    . GLN G 166 ? 0.4452 0.4284 0.4455 -0.0393 0.0467  -0.0338 167 GLN G CD    
8886  O OE1   . GLN G 166 ? 0.4580 0.4397 0.4577 -0.0395 0.0465  -0.0362 167 GLN G OE1   
8887  N NE2   . GLN G 166 ? 0.4854 0.4710 0.4870 -0.0402 0.0462  -0.0332 167 GLN G NE2   
8888  N N     . ILE G 167 ? 0.3708 0.3475 0.3682 -0.0336 0.0518  -0.0286 168 ILE G N     
8889  C CA    . ILE G 167 ? 0.3838 0.3576 0.3801 -0.0324 0.0534  -0.0289 168 ILE G CA    
8890  C C     . ILE G 167 ? 0.4252 0.3965 0.4234 -0.0321 0.0552  -0.0285 168 ILE G C     
8891  O O     . ILE G 167 ? 0.4484 0.4163 0.4455 -0.0315 0.0566  -0.0297 168 ILE G O     
8892  C CB    . ILE G 167 ? 0.3660 0.3413 0.3627 -0.0314 0.0542  -0.0271 168 ILE G CB    
8893  C CG1   . ILE G 167 ? 0.3807 0.3531 0.3762 -0.0301 0.0561  -0.0276 168 ILE G CG1   
8894  C CG2   . ILE G 167 ? 0.3467 0.3251 0.3470 -0.0312 0.0544  -0.0244 168 ILE G CG2   
8895  C CD1   . ILE G 167 ? 0.3670 0.3365 0.3582 -0.0301 0.0557  -0.0303 168 ILE G CD1   
8896  N N     . ALA G 168 ? 0.4042 0.3768 0.4049 -0.0325 0.0553  -0.0268 169 ALA G N     
8897  C CA    . ALA G 168 ? 0.4236 0.3936 0.4261 -0.0320 0.0572  -0.0257 169 ALA G CA    
8898  C C     . ALA G 168 ? 0.4093 0.3754 0.4108 -0.0332 0.0578  -0.0285 169 ALA G C     
8899  O O     . ALA G 168 ? 0.4697 0.4322 0.4719 -0.0327 0.0598  -0.0284 169 ALA G O     
8900  C CB    . ALA G 168 ? 0.4215 0.3936 0.4261 -0.0321 0.0571  -0.0232 169 ALA G CB    
8901  N N     . ILE G 169 ? 0.3685 0.3357 0.3687 -0.0346 0.0560  -0.0310 170 ILE G N     
8902  C CA    . ILE G 169 ? 0.3677 0.3323 0.3675 -0.0360 0.0561  -0.0340 170 ILE G CA    
8903  C C     . ILE G 169 ? 0.3711 0.3353 0.3678 -0.0359 0.0548  -0.0370 170 ILE G C     
8904  O O     . ILE G 169 ? 0.3890 0.3532 0.3852 -0.0372 0.0537  -0.0399 170 ILE G O     
8905  C CB    . ILE G 169 ? 0.3916 0.3581 0.3933 -0.0379 0.0553  -0.0345 170 ILE G CB    
8906  C CG1   . ILE G 169 ? 0.4418 0.4127 0.4429 -0.0381 0.0528  -0.0344 170 ILE G CG1   
8907  C CG2   . ILE G 169 ? 0.4155 0.3810 0.4196 -0.0379 0.0571  -0.0317 170 ILE G CG2   
8908  C CD1   . ILE G 169 ? 0.4360 0.4091 0.4389 -0.0399 0.0521  -0.0349 170 ILE G CD1   
8909  N N     . ALA G 170 ? 0.3712 0.3354 0.3659 -0.0343 0.0549  -0.0362 171 ALA G N     
8910  C CA    . ALA G 170 ? 0.3535 0.3169 0.3445 -0.0338 0.0540  -0.0385 171 ALA G CA    
8911  C C     . ALA G 170 ? 0.3843 0.3438 0.3739 -0.0341 0.0549  -0.0414 171 ALA G C     
8912  O O     . ALA G 170 ? 0.3800 0.3363 0.3699 -0.0333 0.0572  -0.0408 171 ALA G O     
8913  C CB    . ALA G 170 ? 0.3564 0.3199 0.3458 -0.0321 0.0547  -0.0368 171 ALA G CB    
8914  N N     . GLY G 171 ? 0.3891 0.3491 0.3775 -0.0352 0.0531  -0.0446 172 GLY G N     
8915  C CA    . GLY G 171 ? 0.4440 0.4008 0.4307 -0.0356 0.0535  -0.0479 172 GLY G CA    
8916  C C     . GLY G 171 ? 0.4881 0.4439 0.4781 -0.0378 0.0541  -0.0494 172 GLY G C     
8917  O O     . GLY G 171 ? 0.5151 0.4684 0.5043 -0.0387 0.0545  -0.0525 172 GLY G O     
8918  N N     . GLU G 172 ? 0.4966 0.4544 0.4902 -0.0387 0.0544  -0.0471 173 GLU G N     
8919  C CA    . GLU G 172 ? 0.4784 0.4354 0.4753 -0.0409 0.0554  -0.0481 173 GLU G CA    
8920  C C     . GLU G 172 ? 0.4499 0.4102 0.4474 -0.0427 0.0529  -0.0513 173 GLU G C     
8921  O O     . GLU G 172 ? 0.4922 0.4565 0.4911 -0.0430 0.0514  -0.0504 173 GLU G O     
8922  C CB    . GLU G 172 ? 0.4981 0.4560 0.4980 -0.0409 0.0566  -0.0442 173 GLU G CB    
8923  C CG    . GLU G 172 ? 0.5555 0.5103 0.5582 -0.0425 0.0590  -0.0443 173 GLU G CG    
8924  C CD    . GLU G 172 ? 0.5969 0.5526 0.6013 -0.0453 0.0582  -0.0478 173 GLU G CD    
8925  O OE1   . GLU G 172 ? 0.5072 0.4646 0.5144 -0.0467 0.0585  -0.0469 173 GLU G OE1   
8926  O OE2   . GLU G 172 ? 0.6471 0.6021 0.6501 -0.0460 0.0573  -0.0516 173 GLU G OE2   
8927  N N     . HIS G 173 ? 0.4263 0.3850 0.4228 -0.0437 0.0525  -0.0553 174 HIS G N     
8928  C CA    . HIS G 173 ? 0.3796 0.3421 0.3761 -0.0448 0.0497  -0.0589 174 HIS G CA    
8929  C C     . HIS G 173 ? 0.3826 0.3466 0.3838 -0.0477 0.0501  -0.0605 174 HIS G C     
8930  O O     . HIS G 173 ? 0.3592 0.3275 0.3617 -0.0488 0.0478  -0.0630 174 HIS G O     
8931  C CB    . HIS G 173 ? 0.3827 0.3434 0.3755 -0.0443 0.0487  -0.0626 174 HIS G CB    
8932  C CG    . HIS G 173 ? 0.3787 0.3349 0.3723 -0.0460 0.0508  -0.0650 174 HIS G CG    
8933  N ND1   . HIS G 173 ? 0.3734 0.3241 0.3653 -0.0449 0.0537  -0.0636 174 HIS G ND1   
8934  C CD2   . HIS G 173 ? 0.3533 0.3096 0.3493 -0.0487 0.0507  -0.0688 174 HIS G CD2   
8935  C CE1   . HIS G 173 ? 0.3786 0.3257 0.3715 -0.0468 0.0553  -0.0665 174 HIS G CE1   
8936  N NE2   . HIS G 173 ? 0.3716 0.3220 0.3671 -0.0493 0.0535  -0.0698 174 HIS G NE2   
8937  N N     . THR G 174 ? 0.4039 0.3641 0.4075 -0.0490 0.0532  -0.0591 175 THR G N     
8938  C CA    . THR G 174 ? 0.4664 0.4269 0.4744 -0.0520 0.0543  -0.0607 175 THR G CA    
8939  C C     . THR G 174 ? 0.4741 0.4384 0.4846 -0.0523 0.0540  -0.0580 175 THR G C     
8940  O O     . THR G 174 ? 0.4219 0.3891 0.4359 -0.0546 0.0537  -0.0597 175 THR G O     
8941  C CB    . THR G 174 ? 0.4510 0.4051 0.4599 -0.0529 0.0581  -0.0601 175 THR G CB    
8942  O OG1   . THR G 174 ? 0.4741 0.4265 0.4826 -0.0509 0.0598  -0.0551 175 THR G OG1   
8943  C CG2   . THR G 174 ? 0.4666 0.4163 0.4725 -0.0525 0.0586  -0.0628 175 THR G CG2   
8944  N N     . LEU G 175 ? 0.4723 0.4369 0.4813 -0.0500 0.0542  -0.0538 176 LEU G N     
8945  C CA    . LEU G 175 ? 0.4467 0.4144 0.4576 -0.0501 0.0540  -0.0510 176 LEU G CA    
8946  C C     . LEU G 175 ? 0.4701 0.4349 0.4839 -0.0518 0.0572  -0.0495 176 LEU G C     
8947  O O     . LEU G 175 ? 0.4251 0.3924 0.4413 -0.0531 0.0574  -0.0488 176 LEU G O     
8948  C CB    . LEU G 175 ? 0.4176 0.3911 0.4297 -0.0509 0.0513  -0.0532 176 LEU G CB    
8949  C CG    . LEU G 175 ? 0.4355 0.4116 0.4444 -0.0492 0.0482  -0.0549 176 LEU G CG    
8950  C CD1   . LEU G 175 ? 0.4266 0.4084 0.4369 -0.0496 0.0457  -0.0565 176 LEU G CD1   
8951  C CD2   . LEU G 175 ? 0.4559 0.4309 0.4614 -0.0465 0.0481  -0.0516 176 LEU G CD2   
8952  N N     . THR G 176 ? 0.4760 0.4352 0.4893 -0.0517 0.0598  -0.0490 177 THR G N     
8953  C CA    . THR G 176 ? 0.4571 0.4123 0.4725 -0.0530 0.0632  -0.0475 177 THR G CA    
8954  C C     . THR G 176 ? 0.5000 0.4513 0.5137 -0.0505 0.0652  -0.0432 177 THR G C     
8955  O O     . THR G 176 ? 0.5287 0.4768 0.5434 -0.0506 0.0679  -0.0407 177 THR G O     
8956  C CB    . THR G 176 ? 0.4584 0.4099 0.4754 -0.0556 0.0648  -0.0514 177 THR G CB    
8957  O OG1   . THR G 176 ? 0.4949 0.4429 0.5090 -0.0541 0.0649  -0.0524 177 THR G OG1   
8958  C CG2   . THR G 176 ? 0.4391 0.3953 0.4583 -0.0582 0.0626  -0.0559 177 THR G CG2   
8959  N N     . GLN G 177 ? 0.5127 0.4645 0.5238 -0.0480 0.0639  -0.0424 178 GLN G N     
8960  C CA    . GLN G 177 ? 0.5808 0.5299 0.5906 -0.0453 0.0655  -0.0386 178 GLN G CA    
8961  C C     . GLN G 177 ? 0.5537 0.5077 0.5630 -0.0436 0.0636  -0.0354 178 GLN G C     
8962  O O     . GLN G 177 ? 0.5312 0.4898 0.5401 -0.0440 0.0610  -0.0365 178 GLN G O     
8963  C CB    . GLN G 177 ? 0.6276 0.5739 0.6352 -0.0438 0.0658  -0.0399 178 GLN G CB    
8964  C CG    . GLN G 177 ? 0.7644 0.7055 0.7721 -0.0455 0.0677  -0.0434 178 GLN G CG    
8965  C CD    . GLN G 177 ? 0.8521 0.7878 0.8614 -0.0461 0.0713  -0.0418 178 GLN G CD    
8966  O OE1   . GLN G 177 ? 0.8318 0.7677 0.8420 -0.0452 0.0724  -0.0379 178 GLN G OE1   
8967  N NE2   . GLN G 177 ? 0.9600 0.8906 0.9693 -0.0477 0.0733  -0.0448 178 GLN G NE2   
8968  N N     . PHE G 178 ? 0.5702 0.5229 0.5794 -0.0416 0.0651  -0.0314 179 PHE G N     
8969  C CA    . PHE G 178 ? 0.6537 0.6109 0.6626 -0.0400 0.0635  -0.0284 179 PHE G CA    
8970  C C     . PHE G 178 ? 0.5988 0.5569 0.6063 -0.0377 0.0627  -0.0274 179 PHE G C     
8971  O O     . PHE G 178 ? 0.6464 0.6085 0.6536 -0.0366 0.0612  -0.0255 179 PHE G O     
8972  C CB    . PHE G 178 ? 0.6854 0.6413 0.6951 -0.0393 0.0654  -0.0246 179 PHE G CB    
8973  C CG    . PHE G 178 ? 0.7902 0.7453 0.8012 -0.0416 0.0664  -0.0252 179 PHE G CG    
8974  C CD1   . PHE G 178 ? 0.8363 0.7954 0.8480 -0.0436 0.0645  -0.0273 179 PHE G CD1   
8975  C CD2   . PHE G 178 ? 0.8584 0.8085 0.8699 -0.0418 0.0696  -0.0236 179 PHE G CD2   
8976  C CE1   . PHE G 178 ? 0.8388 0.7975 0.8520 -0.0458 0.0657  -0.0278 179 PHE G CE1   
8977  C CE2   . PHE G 178 ? 0.8491 0.7984 0.8619 -0.0441 0.0710  -0.0240 179 PHE G CE2   
8978  C CZ    . PHE G 178 ? 0.8053 0.7590 0.8191 -0.0462 0.0690  -0.0262 179 PHE G CZ    
8979  N N     . HIS G 179 ? 0.5780 0.5324 0.5847 -0.0371 0.0640  -0.0289 180 HIS G N     
8980  C CA    . HIS G 179 ? 0.6003 0.5551 0.6058 -0.0349 0.0639  -0.0282 180 HIS G CA    
8981  C C     . HIS G 179 ? 0.5472 0.4987 0.5509 -0.0352 0.0644  -0.0316 180 HIS G C     
8982  O O     . HIS G 179 ? 0.5510 0.4989 0.5548 -0.0368 0.0655  -0.0340 180 HIS G O     
8983  C CB    . HIS G 179 ? 0.6240 0.5774 0.6305 -0.0325 0.0659  -0.0245 180 HIS G CB    
8984  C CG    . HIS G 179 ? 0.7119 0.6593 0.7188 -0.0323 0.0689  -0.0244 180 HIS G CG    
8985  N ND1   . HIS G 179 ? 0.7439 0.6868 0.7499 -0.0317 0.0707  -0.0261 180 HIS G ND1   
8986  C CD2   . HIS G 179 ? 0.6827 0.6274 0.6906 -0.0327 0.0707  -0.0227 180 HIS G CD2   
8987  C CE1   . HIS G 179 ? 0.7637 0.7013 0.7702 -0.0317 0.0735  -0.0256 180 HIS G CE1   
8988  N NE2   . HIS G 179 ? 0.7740 0.7124 0.7817 -0.0323 0.0736  -0.0235 180 HIS G NE2   
8989  N N     . THR G 180 ? 0.5418 0.4944 0.5438 -0.0338 0.0637  -0.0318 181 THR G N     
8990  C CA    . THR G 180 ? 0.5562 0.5059 0.5558 -0.0337 0.0641  -0.0349 181 THR G CA    
8991  C C     . THR G 180 ? 0.5700 0.5157 0.5695 -0.0316 0.0669  -0.0336 181 THR G C     
8992  O O     . THR G 180 ? 0.5616 0.5061 0.5631 -0.0306 0.0687  -0.0308 181 THR G O     
8993  C CB    . THR G 180 ? 0.6125 0.5653 0.6096 -0.0334 0.0618  -0.0360 181 THR G CB    
8994  O OG1   . THR G 180 ? 0.6941 0.6438 0.6885 -0.0334 0.0621  -0.0392 181 THR G OG1   
8995  C CG2   . THR G 180 ? 0.6104 0.5656 0.6078 -0.0314 0.0620  -0.0331 181 THR G CG2   
8996  N N     . SER G 181 ? 0.5847 0.5283 0.5815 -0.0308 0.0674  -0.0356 182 SER G N     
8997  C CA    . SER G 181 ? 0.6138 0.5536 0.6103 -0.0288 0.0702  -0.0347 182 SER G CA    
8998  C C     . SER G 181 ? 0.5859 0.5275 0.5806 -0.0270 0.0700  -0.0344 182 SER G C     
8999  O O     . SER G 181 ? 0.5154 0.4597 0.5081 -0.0277 0.0678  -0.0355 182 SER G O     
9000  C CB    . SER G 181 ? 0.7114 0.6453 0.7064 -0.0297 0.0719  -0.0379 182 SER G CB    
9001  O OG    . SER G 181 ? 0.7871 0.7210 0.7789 -0.0308 0.0703  -0.0417 182 SER G OG    
9002  N N     . SER G 182 ? 0.5792 0.5189 0.5745 -0.0248 0.0725  -0.0327 183 SER G N     
9003  C CA    . SER G 182 ? 0.5879 0.5292 0.5821 -0.0230 0.0730  -0.0320 183 SER G CA    
9004  C C     . SER G 182 ? 0.5887 0.5276 0.5783 -0.0235 0.0727  -0.0355 183 SER G C     
9005  O O     . SER G 182 ? 0.6127 0.5534 0.6004 -0.0228 0.0723  -0.0354 183 SER G O     
9006  C CB    . SER G 182 ? 0.5821 0.5219 0.5784 -0.0204 0.0760  -0.0296 183 SER G CB    
9007  O OG    . SER G 182 ? 0.6565 0.5901 0.6513 -0.0200 0.0785  -0.0315 183 SER G OG    
9008  N N     . ASP G 183 ? 0.6119 0.5464 0.5995 -0.0247 0.0730  -0.0386 184 ASP G N     
9009  C CA    . ASP G 183 ? 0.6072 0.5390 0.5899 -0.0250 0.0727  -0.0422 184 ASP G CA    
9010  C C     . ASP G 183 ? 0.5592 0.4948 0.5400 -0.0264 0.0692  -0.0436 184 ASP G C     
9011  O O     . ASP G 183 ? 0.4759 0.4112 0.4525 -0.0259 0.0685  -0.0453 184 ASP G O     
9012  C CB    . ASP G 183 ? 0.7253 0.6518 0.7069 -0.0261 0.0739  -0.0453 184 ASP G CB    
9013  C CG    . ASP G 183 ? 0.8813 0.8079 0.8653 -0.0286 0.0727  -0.0464 184 ASP G CG    
9014  O OD1   . ASP G 183 ? 0.9977 0.9254 0.9856 -0.0285 0.0734  -0.0435 184 ASP G OD1   
9015  O OD2   . ASP G 183 ? 1.0041 0.9299 0.9861 -0.0305 0.0712  -0.0501 184 ASP G OD2   
9016  N N     . ARG G 184 ? 0.5116 0.4505 0.4953 -0.0280 0.0672  -0.0428 185 ARG G N     
9017  C CA    . ARG G 184 ? 0.5456 0.4884 0.5280 -0.0291 0.0641  -0.0437 185 ARG G CA    
9018  C C     . ARG G 184 ? 0.4566 0.4026 0.4385 -0.0278 0.0636  -0.0412 185 ARG G C     
9019  O O     . ARG G 184 ? 0.4279 0.3748 0.4062 -0.0275 0.0622  -0.0424 185 ARG G O     
9020  C CB    . ARG G 184 ? 0.5642 0.5096 0.5500 -0.0311 0.0625  -0.0434 185 ARG G CB    
9021  C CG    . ARG G 184 ? 0.6820 0.6254 0.6677 -0.0331 0.0619  -0.0470 185 ARG G CG    
9022  C CD    . ARG G 184 ? 0.7595 0.6974 0.7456 -0.0331 0.0648  -0.0479 185 ARG G CD    
9023  N NE    . ARG G 184 ? 0.8348 0.7710 0.8212 -0.0355 0.0643  -0.0517 185 ARG G NE    
9024  C CZ    . ARG G 184 ? 0.8933 0.8297 0.8767 -0.0364 0.0624  -0.0556 185 ARG G CZ    
9025  N NH1   . ARG G 184 ? 0.9694 0.9070 0.9487 -0.0348 0.0610  -0.0561 185 ARG G NH1   
9026  N NH2   . ARG G 184 ? 0.8951 0.8304 0.8794 -0.0388 0.0619  -0.0591 185 ARG G NH2   
9027  N N     . LEU G 185 ? 0.4705 0.4183 0.4559 -0.0269 0.0649  -0.0378 186 LEU G N     
9028  C CA    . LEU G 185 ? 0.5289 0.4802 0.5148 -0.0261 0.0647  -0.0355 186 LEU G CA    
9029  C C     . LEU G 185 ? 0.5424 0.4915 0.5250 -0.0245 0.0664  -0.0360 186 LEU G C     
9030  O O     . LEU G 185 ? 0.5823 0.5334 0.5635 -0.0242 0.0660  -0.0352 186 LEU G O     
9031  C CB    . LEU G 185 ? 0.5644 0.5183 0.5552 -0.0255 0.0656  -0.0321 186 LEU G CB    
9032  C CG    . LEU G 185 ? 0.6119 0.5681 0.6056 -0.0268 0.0641  -0.0311 186 LEU G CG    
9033  C CD1   . LEU G 185 ? 0.6171 0.5759 0.6149 -0.0258 0.0650  -0.0276 186 LEU G CD1   
9034  C CD2   . LEU G 185 ? 0.6600 0.6194 0.6526 -0.0283 0.0613  -0.0318 186 LEU G CD2   
9035  N N     . GLN G 186 ? 0.5513 0.4961 0.5325 -0.0236 0.0685  -0.0373 187 GLN G N     
9036  C CA    . GLN G 186 ? 0.5753 0.5175 0.5529 -0.0221 0.0705  -0.0380 187 GLN G CA    
9037  C C     . GLN G 186 ? 0.5466 0.4878 0.5185 -0.0224 0.0688  -0.0405 187 GLN G C     
9038  O O     . GLN G 186 ? 0.4806 0.4214 0.4494 -0.0214 0.0695  -0.0402 187 GLN G O     
9039  C CB    . GLN G 186 ? 0.6073 0.5448 0.5847 -0.0211 0.0733  -0.0390 187 GLN G CB    
9040  C CG    . GLN G 186 ? 0.6376 0.5718 0.6107 -0.0194 0.0756  -0.0400 187 GLN G CG    
9041  C CD    . GLN G 186 ? 0.6253 0.5623 0.5999 -0.0181 0.0771  -0.0373 187 GLN G CD    
9042  O OE1   . GLN G 186 ? 0.6592 0.5989 0.6388 -0.0174 0.0783  -0.0345 187 GLN G OE1   
9043  N NE2   . GLN G 186 ? 0.6370 0.5734 0.6069 -0.0177 0.0772  -0.0381 187 GLN G NE2   
9044  N N     . ILE G 187 ? 0.5259 0.4667 0.4966 -0.0239 0.0664  -0.0431 188 ILE G N     
9045  C CA    . ILE G 187 ? 0.5081 0.4484 0.4735 -0.0240 0.0643  -0.0457 188 ILE G CA    
9046  C C     . ILE G 187 ? 0.4601 0.4042 0.4253 -0.0241 0.0623  -0.0441 188 ILE G C     
9047  O O     . ILE G 187 ? 0.4163 0.3598 0.3766 -0.0233 0.0615  -0.0449 188 ILE G O     
9048  C CB    . ILE G 187 ? 0.4883 0.4278 0.4533 -0.0256 0.0623  -0.0490 188 ILE G CB    
9049  C CG1   . ILE G 187 ? 0.5102 0.4452 0.4746 -0.0255 0.0644  -0.0511 188 ILE G CG1   
9050  C CG2   . ILE G 187 ? 0.4781 0.4186 0.4383 -0.0256 0.0593  -0.0515 188 ILE G CG2   
9051  C CD1   . ILE G 187 ? 0.5397 0.4739 0.5043 -0.0275 0.0627  -0.0547 188 ILE G CD1   
9052  N N     . LEU G 188 ? 0.4375 0.3852 0.4077 -0.0250 0.0618  -0.0417 189 LEU G N     
9053  C CA    . LEU G 188 ? 0.4661 0.4173 0.4366 -0.0253 0.0602  -0.0401 189 LEU G CA    
9054  C C     . LEU G 188 ? 0.3808 0.3314 0.3497 -0.0240 0.0622  -0.0383 189 LEU G C     
9055  O O     . LEU G 188 ? 0.3629 0.3139 0.3286 -0.0237 0.0615  -0.0381 189 LEU G O     
9056  C CB    . LEU G 188 ? 0.4833 0.4382 0.4594 -0.0266 0.0594  -0.0381 189 LEU G CB    
9057  C CG    . LEU G 188 ? 0.4940 0.4525 0.4707 -0.0271 0.0578  -0.0366 189 LEU G CG    
9058  C CD1   . LEU G 188 ? 0.4934 0.4519 0.4662 -0.0273 0.0553  -0.0387 189 LEU G CD1   
9059  C CD2   . LEU G 188 ? 0.4691 0.4310 0.4509 -0.0282 0.0571  -0.0348 189 LEU G CD2   
9060  N N     . VAL G 189 ? 0.3762 0.3260 0.3475 -0.0232 0.0650  -0.0369 190 VAL G N     
9061  C CA    . VAL G 189 ? 0.4184 0.3681 0.3892 -0.0222 0.0674  -0.0352 190 VAL G CA    
9062  C C     . VAL G 189 ? 0.4391 0.3850 0.4030 -0.0211 0.0681  -0.0369 190 VAL G C     
9063  O O     . VAL G 189 ? 0.4798 0.4260 0.4414 -0.0207 0.0685  -0.0360 190 VAL G O     
9064  C CB    . VAL G 189 ? 0.4329 0.3825 0.4077 -0.0212 0.0703  -0.0337 190 VAL G CB    
9065  C CG1   . VAL G 189 ? 0.4429 0.3921 0.4168 -0.0200 0.0732  -0.0325 190 VAL G CG1   
9066  C CG2   . VAL G 189 ? 0.4253 0.3790 0.4065 -0.0219 0.0697  -0.0315 190 VAL G CG2   
9067  N N     . GLU G 190 ? 0.3876 0.3300 0.3481 -0.0205 0.0682  -0.0394 191 GLU G N     
9068  C CA    . GLU G 190 ? 0.4533 0.3918 0.4066 -0.0192 0.0687  -0.0412 191 GLU G CA    
9069  C C     . GLU G 190 ? 0.4289 0.3683 0.3783 -0.0194 0.0659  -0.0418 191 GLU G C     
9070  O O     . GLU G 190 ? 0.4229 0.3601 0.3668 -0.0181 0.0666  -0.0418 191 GLU G O     
9071  C CB    . GLU G 190 ? 0.4911 0.4261 0.4419 -0.0189 0.0689  -0.0442 191 GLU G CB    
9072  C CG    . GLU G 190 ? 0.5193 0.4525 0.4734 -0.0184 0.0720  -0.0436 191 GLU G CG    
9073  C CD    . GLU G 190 ? 0.5753 0.5047 0.5273 -0.0184 0.0722  -0.0467 191 GLU G CD    
9074  O OE1   . GLU G 190 ? 0.6201 0.5488 0.5685 -0.0190 0.0697  -0.0496 191 GLU G OE1   
9075  O OE2   . GLU G 190 ? 0.6051 0.5323 0.5593 -0.0178 0.0750  -0.0464 191 GLU G OE2   
9076  N N     . GLN G 191 ? 0.4197 0.3622 0.3719 -0.0207 0.0629  -0.0423 192 GLN G N     
9077  C CA    . GLN G 191 ? 0.4380 0.3817 0.3871 -0.0207 0.0601  -0.0430 192 GLN G CA    
9078  C C     . GLN G 191 ? 0.4283 0.3733 0.3777 -0.0207 0.0608  -0.0403 192 GLN G C     
9079  O O     . GLN G 191 ? 0.4379 0.3817 0.3823 -0.0197 0.0601  -0.0404 192 GLN G O     
9080  C CB    . GLN G 191 ? 0.4623 0.4092 0.4151 -0.0223 0.0571  -0.0442 192 GLN G CB    
9081  C CG    . GLN G 191 ? 0.4837 0.4322 0.4336 -0.0221 0.0540  -0.0451 192 GLN G CG    
9082  C CD    . GLN G 191 ? 0.4737 0.4258 0.4279 -0.0238 0.0514  -0.0461 192 GLN G CD    
9083  O OE1   . GLN G 191 ? 0.4290 0.3823 0.3883 -0.0252 0.0520  -0.0458 192 GLN G OE1   
9084  N NE2   . GLN G 191 ? 0.5037 0.4575 0.4557 -0.0234 0.0487  -0.0472 192 GLN G NE2   
9085  N N     . LEU G 192 ? 0.4173 0.3650 0.3727 -0.0217 0.0621  -0.0380 193 LEU G N     
9086  C CA    . LEU G 192 ? 0.3935 0.3429 0.3501 -0.0221 0.0629  -0.0357 193 LEU G CA    
9087  C C     . LEU G 192 ? 0.4040 0.3503 0.3572 -0.0209 0.0661  -0.0348 193 LEU G C     
9088  O O     . LEU G 192 ? 0.3876 0.3339 0.3397 -0.0210 0.0670  -0.0334 193 LEU G O     
9089  C CB    . LEU G 192 ? 0.3766 0.3301 0.3407 -0.0235 0.0631  -0.0338 193 LEU G CB    
9090  C CG    . LEU G 192 ? 0.3469 0.3036 0.3142 -0.0248 0.0602  -0.0341 193 LEU G CG    
9091  C CD1   . LEU G 192 ? 0.3267 0.2871 0.3006 -0.0259 0.0606  -0.0320 193 LEU G CD1   
9092  C CD2   . LEU G 192 ? 0.3700 0.3274 0.3346 -0.0251 0.0581  -0.0344 193 LEU G CD2   
9093  N N     . ASN G 193 ? 0.4428 0.3864 0.3943 -0.0198 0.0681  -0.0357 194 ASN G N     
9094  C CA    . ASN G 193 ? 0.4784 0.4192 0.4273 -0.0187 0.0717  -0.0348 194 ASN G CA    
9095  C C     . ASN G 193 ? 0.4639 0.4010 0.4048 -0.0174 0.0716  -0.0354 194 ASN G C     
9096  O O     . ASN G 193 ? 0.4949 0.4292 0.4326 -0.0165 0.0747  -0.0345 194 ASN G O     
9097  C CB    . ASN G 193 ? 0.5003 0.4388 0.4491 -0.0176 0.0738  -0.0359 194 ASN G CB    
9098  C CG    . ASN G 193 ? 0.5440 0.4803 0.4913 -0.0166 0.0779  -0.0347 194 ASN G CG    
9099  O OD1   . ASN G 193 ? 0.5817 0.5207 0.5338 -0.0172 0.0798  -0.0326 194 ASN G OD1   
9100  N ND2   . ASN G 193 ? 0.5663 0.4978 0.5070 -0.0149 0.0794  -0.0363 194 ASN G ND2   
9101  N N     . GLN G 194 ? 0.5026 0.4399 0.4405 -0.0173 0.0683  -0.0366 195 GLN G N     
9102  C CA    . GLN G 194 ? 0.4918 0.4258 0.4219 -0.0158 0.0678  -0.0370 195 GLN G CA    
9103  C C     . GLN G 194 ? 0.4813 0.4155 0.4118 -0.0164 0.0690  -0.0347 195 GLN G C     
9104  O O     . GLN G 194 ? 0.4265 0.3569 0.3506 -0.0150 0.0703  -0.0341 195 GLN G O     
9105  C CB    . GLN G 194 ? 0.4894 0.4242 0.4169 -0.0154 0.0636  -0.0391 195 GLN G CB    
9106  C CG    . GLN G 194 ? 0.4951 0.4296 0.4219 -0.0151 0.0622  -0.0420 195 GLN G CG    
9107  C CD    . GLN G 194 ? 0.5116 0.4479 0.4368 -0.0150 0.0580  -0.0442 195 GLN G CD    
9108  O OE1   . GLN G 194 ? 0.4861 0.4207 0.4049 -0.0132 0.0565  -0.0450 195 GLN G OE1   
9109  N NE2   . GLN G 194 ? 0.5430 0.4828 0.4742 -0.0168 0.0561  -0.0452 195 GLN G NE2   
9110  N N     . TRP G 195 ? 0.4530 0.3914 0.3907 -0.0184 0.0687  -0.0333 196 TRP G N     
9111  C CA    . TRP G 195 ? 0.4639 0.4030 0.4026 -0.0193 0.0694  -0.0315 196 TRP G CA    
9112  C C     . TRP G 195 ? 0.4738 0.4160 0.4195 -0.0211 0.0720  -0.0297 196 TRP G C     
9113  O O     . TRP G 195 ? 0.4344 0.3764 0.3807 -0.0219 0.0739  -0.0283 196 TRP G O     
9114  C CB    . TRP G 195 ? 0.4606 0.4024 0.4007 -0.0201 0.0659  -0.0318 196 TRP G CB    
9115  C CG    . TRP G 195 ? 0.4317 0.3718 0.3662 -0.0184 0.0630  -0.0337 196 TRP G CG    
9116  C CD1   . TRP G 195 ? 0.4441 0.3806 0.3713 -0.0166 0.0626  -0.0338 196 TRP G CD1   
9117  C CD2   . TRP G 195 ? 0.3908 0.3330 0.3266 -0.0184 0.0599  -0.0358 196 TRP G CD2   
9118  N NE1   . TRP G 195 ? 0.4668 0.4036 0.3909 -0.0153 0.0594  -0.0359 196 TRP G NE1   
9119  C CE2   . TRP G 195 ? 0.4273 0.3677 0.3567 -0.0166 0.0577  -0.0373 196 TRP G CE2   
9120  C CE3   . TRP G 195 ? 0.3768 0.3222 0.3185 -0.0198 0.0590  -0.0366 196 TRP G CE3   
9121  C CZ2   . TRP G 195 ? 0.4158 0.3580 0.3452 -0.0163 0.0545  -0.0398 196 TRP G CZ2   
9122  C CZ3   . TRP G 195 ? 0.3987 0.3452 0.3401 -0.0196 0.0562  -0.0389 196 TRP G CZ3   
9123  C CH2   . TRP G 195 ? 0.3875 0.3327 0.3231 -0.0180 0.0539  -0.0406 196 TRP G CH2   
9124  N N     . TYR G 196 ? 0.4625 0.4075 0.4136 -0.0215 0.0720  -0.0300 197 TYR G N     
9125  C CA    . TYR G 196 ? 0.4427 0.3916 0.4010 -0.0228 0.0738  -0.0284 197 TYR G CA    
9126  C C     . TYR G 196 ? 0.4346 0.3825 0.3940 -0.0218 0.0766  -0.0284 197 TYR G C     
9127  O O     . TYR G 196 ? 0.4275 0.3740 0.3856 -0.0207 0.0759  -0.0298 197 TYR G O     
9128  C CB    . TYR G 196 ? 0.3962 0.3501 0.3607 -0.0242 0.0709  -0.0282 197 TYR G CB    
9129  C CG    . TYR G 196 ? 0.4120 0.3669 0.3755 -0.0252 0.0681  -0.0283 197 TYR G CG    
9130  C CD1   . TYR G 196 ? 0.4155 0.3721 0.3809 -0.0267 0.0686  -0.0271 197 TYR G CD1   
9131  C CD2   . TYR G 196 ? 0.4041 0.3582 0.3648 -0.0247 0.0652  -0.0299 197 TYR G CD2   
9132  C CE1   . TYR G 196 ? 0.3703 0.3274 0.3346 -0.0274 0.0663  -0.0273 197 TYR G CE1   
9133  C CE2   . TYR G 196 ? 0.3710 0.3260 0.3308 -0.0253 0.0628  -0.0300 197 TYR G CE2   
9134  C CZ    . TYR G 196 ? 0.3568 0.3132 0.3182 -0.0266 0.0634  -0.0287 197 TYR G CZ    
9135  O OH    . TYR G 196 ? 0.3380 0.2950 0.2985 -0.0271 0.0612  -0.0289 197 TYR G OH    
9136  N N     . PRO G 197 ? 0.4660 0.4147 0.4280 -0.0220 0.0800  -0.0270 198 PRO G N     
9137  C CA    . PRO G 197 ? 0.5022 0.4508 0.4665 -0.0210 0.0829  -0.0269 198 PRO G CA    
9138  C C     . PRO G 197 ? 0.5173 0.4696 0.4876 -0.0210 0.0813  -0.0268 198 PRO G C     
9139  O O     . PRO G 197 ? 0.5910 0.5465 0.5644 -0.0222 0.0783  -0.0267 198 PRO G O     
9140  C CB    . PRO G 197 ? 0.4940 0.4446 0.4619 -0.0218 0.0863  -0.0252 198 PRO G CB    
9141  C CG    . PRO G 197 ? 0.4992 0.4480 0.4632 -0.0229 0.0860  -0.0249 198 PRO G CG    
9142  C CD    . PRO G 197 ? 0.4871 0.4367 0.4501 -0.0234 0.0815  -0.0257 198 PRO G CD    
9143  N N     . LEU G 198 ? 0.5337 0.4852 0.5054 -0.0196 0.0836  -0.0270 199 LEU G N     
9144  C CA    . LEU G 198 ? 0.5268 0.4807 0.5036 -0.0193 0.0827  -0.0268 199 LEU G CA    
9145  C C     . LEU G 198 ? 0.4923 0.4526 0.4773 -0.0201 0.0829  -0.0247 199 LEU G C     
9146  O O     . LEU G 198 ? 0.4375 0.4010 0.4270 -0.0203 0.0811  -0.0241 199 LEU G O     
9147  C CB    . LEU G 198 ? 0.5569 0.5073 0.5320 -0.0174 0.0852  -0.0277 199 LEU G CB    
9148  C CG    . LEU G 198 ? 0.6101 0.5546 0.5774 -0.0165 0.0846  -0.0301 199 LEU G CG    
9149  C CD1   . LEU G 198 ? 0.6289 0.5699 0.5950 -0.0147 0.0871  -0.0311 199 LEU G CD1   
9150  C CD2   . LEU G 198 ? 0.6174 0.5621 0.5837 -0.0175 0.0805  -0.0314 199 LEU G CD2   
9151  N N     . ASP G 199 ? 0.4723 0.4343 0.4590 -0.0207 0.0853  -0.0237 200 ASP G N     
9152  C CA    . ASP G 199 ? 0.4964 0.4650 0.4910 -0.0215 0.0858  -0.0220 200 ASP G CA    
9153  C C     . ASP G 199 ? 0.4860 0.4577 0.4819 -0.0238 0.0833  -0.0216 200 ASP G C     
9154  O O     . ASP G 199 ? 0.4753 0.4523 0.4770 -0.0250 0.0837  -0.0206 200 ASP G O     
9155  C CB    . ASP G 199 ? 0.5361 0.5055 0.5329 -0.0210 0.0900  -0.0213 200 ASP G CB    
9156  C CG    . ASP G 199 ? 0.5921 0.5579 0.5837 -0.0219 0.0921  -0.0217 200 ASP G CG    
9157  O OD1   . ASP G 199 ? 0.6292 0.5916 0.6151 -0.0226 0.0901  -0.0225 200 ASP G OD1   
9158  O OD2   . ASP G 199 ? 0.6014 0.5678 0.5948 -0.0218 0.0958  -0.0212 200 ASP G OD2   
9159  N N     . HIS G 200 ? 0.4677 0.4363 0.4585 -0.0244 0.0808  -0.0227 201 HIS G N     
9160  C CA    . HIS G 200 ? 0.4715 0.4424 0.4628 -0.0264 0.0785  -0.0225 201 HIS G CA    
9161  C C     . HIS G 200 ? 0.4296 0.4059 0.4267 -0.0271 0.0757  -0.0217 201 HIS G C     
9162  O O     . HIS G 200 ? 0.3733 0.3491 0.3702 -0.0262 0.0740  -0.0220 201 HIS G O     
9163  C CB    . HIS G 200 ? 0.5116 0.4776 0.4956 -0.0264 0.0767  -0.0238 201 HIS G CB    
9164  C CG    . HIS G 200 ? 0.4988 0.4663 0.4827 -0.0282 0.0747  -0.0236 201 HIS G CG    
9165  N ND1   . HIS G 200 ? 0.5168 0.4841 0.5003 -0.0296 0.0764  -0.0232 201 HIS G ND1   
9166  C CD2   . HIS G 200 ? 0.4797 0.4488 0.4640 -0.0290 0.0713  -0.0240 201 HIS G CD2   
9167  C CE1   . HIS G 200 ? 0.4762 0.4447 0.4597 -0.0310 0.0740  -0.0233 201 HIS G CE1   
9168  N NE2   . HIS G 200 ? 0.4860 0.4558 0.4700 -0.0306 0.0709  -0.0237 201 HIS G NE2   
9169  N N     . GLU G 201 ? 0.3763 0.3578 0.3784 -0.0286 0.0755  -0.0208 202 GLU G N     
9170  C CA    . GLU G 201 ? 0.4051 0.3923 0.4126 -0.0292 0.0730  -0.0200 202 GLU G CA    
9171  C C     . GLU G 201 ? 0.3858 0.3718 0.3903 -0.0300 0.0697  -0.0206 202 GLU G C     
9172  O O     . GLU G 201 ? 0.3848 0.3696 0.3865 -0.0315 0.0690  -0.0212 202 GLU G O     
9173  C CB    . GLU G 201 ? 0.4418 0.4349 0.4549 -0.0308 0.0735  -0.0192 202 GLU G CB    
9174  C CG    . GLU G 201 ? 0.5020 0.5013 0.5202 -0.0314 0.0707  -0.0184 202 GLU G CG    
9175  C CD    . GLU G 201 ? 0.5696 0.5753 0.5935 -0.0332 0.0708  -0.0180 202 GLU G CD    
9176  O OE1   . GLU G 201 ? 0.7033 0.7121 0.7317 -0.0327 0.0731  -0.0175 202 GLU G OE1   
9177  O OE2   . GLU G 201 ? 0.7022 0.7100 0.7264 -0.0352 0.0687  -0.0184 202 GLU G OE2   
9178  N N     . VAL G 202 ? 0.3495 0.3356 0.3545 -0.0290 0.0680  -0.0205 203 VAL G N     
9179  C CA    . VAL G 202 ? 0.3155 0.3015 0.3189 -0.0298 0.0649  -0.0209 203 VAL G CA    
9180  C C     . VAL G 202 ? 0.3065 0.2981 0.3152 -0.0301 0.0633  -0.0196 203 VAL G C     
9181  O O     . VAL G 202 ? 0.2856 0.2807 0.2988 -0.0293 0.0643  -0.0183 203 VAL G O     
9182  C CB    . VAL G 202 ? 0.3078 0.2891 0.3071 -0.0287 0.0643  -0.0221 203 VAL G CB    
9183  C CG1   . VAL G 202 ? 0.3140 0.2900 0.3074 -0.0283 0.0655  -0.0235 203 VAL G CG1   
9184  C CG2   . VAL G 202 ? 0.3069 0.2882 0.3087 -0.0271 0.0653  -0.0214 203 VAL G CG2   
9185  N N     . VAL G 203 ? 0.3135 0.3058 0.3212 -0.0310 0.0607  -0.0198 204 VAL G N     
9186  C CA    . VAL G 203 ? 0.3260 0.3235 0.3379 -0.0314 0.0589  -0.0185 204 VAL G CA    
9187  C C     . VAL G 203 ? 0.3225 0.3185 0.3329 -0.0310 0.0572  -0.0185 204 VAL G C     
9188  O O     . VAL G 203 ? 0.3886 0.3818 0.3954 -0.0318 0.0560  -0.0198 204 VAL G O     
9189  C CB    . VAL G 203 ? 0.3321 0.3331 0.3449 -0.0334 0.0576  -0.0187 204 VAL G CB    
9190  C CG1   . VAL G 203 ? 0.3411 0.3474 0.3575 -0.0337 0.0556  -0.0175 204 VAL G CG1   
9191  C CG2   . VAL G 203 ? 0.3382 0.3404 0.3527 -0.0342 0.0596  -0.0189 204 VAL G CG2   
9192  N N     . ILE G 204 ? 0.3191 0.3167 0.3324 -0.0296 0.0572  -0.0170 205 ILE G N     
9193  C CA    . ILE G 204 ? 0.3069 0.3037 0.3195 -0.0294 0.0558  -0.0167 205 ILE G CA    
9194  C C     . ILE G 204 ? 0.3106 0.3122 0.3250 -0.0304 0.0537  -0.0157 205 ILE G C     
9195  O O     . ILE G 204 ? 0.3053 0.3113 0.3233 -0.0297 0.0535  -0.0142 205 ILE G O     
9196  C CB    . ILE G 204 ? 0.2944 0.2897 0.3086 -0.0274 0.0572  -0.0155 205 ILE G CB    
9197  C CG1   . ILE G 204 ? 0.3096 0.2998 0.3216 -0.0265 0.0593  -0.0168 205 ILE G CG1   
9198  C CG2   . ILE G 204 ? 0.2766 0.2712 0.2904 -0.0273 0.0560  -0.0148 205 ILE G CG2   
9199  C CD1   . ILE G 204 ? 0.3191 0.3071 0.3325 -0.0245 0.0610  -0.0158 205 ILE G CD1   
9200  N N     . TYR G 205 ? 0.3388 0.3395 0.3506 -0.0318 0.0521  -0.0167 206 TYR G N     
9201  C CA    . TYR G 205 ? 0.3565 0.3612 0.3691 -0.0329 0.0501  -0.0162 206 TYR G CA    
9202  C C     . TYR G 205 ? 0.3840 0.3881 0.3960 -0.0326 0.0491  -0.0155 206 TYR G C     
9203  O O     . TYR G 205 ? 0.3836 0.3838 0.3933 -0.0327 0.0494  -0.0164 206 TYR G O     
9204  C CB    . TYR G 205 ? 0.3497 0.3540 0.3600 -0.0348 0.0493  -0.0178 206 TYR G CB    
9205  C CG    . TYR G 205 ? 0.3647 0.3724 0.3751 -0.0361 0.0473  -0.0177 206 TYR G CG    
9206  C CD1   . TYR G 205 ? 0.3685 0.3814 0.3819 -0.0365 0.0465  -0.0168 206 TYR G CD1   
9207  C CD2   . TYR G 205 ? 0.3652 0.3712 0.3729 -0.0368 0.0461  -0.0185 206 TYR G CD2   
9208  C CE1   . TYR G 205 ? 0.3723 0.3882 0.3854 -0.0376 0.0446  -0.0168 206 TYR G CE1   
9209  C CE2   . TYR G 205 ? 0.3936 0.4024 0.4011 -0.0379 0.0445  -0.0184 206 TYR G CE2   
9210  C CZ    . TYR G 205 ? 0.3900 0.4036 0.4000 -0.0383 0.0437  -0.0176 206 TYR G CZ    
9211  O OH    . TYR G 205 ? 0.3565 0.3727 0.3658 -0.0394 0.0421  -0.0177 206 TYR G OH    
9212  N N     . GLU G 206 ? 0.3497 0.3579 0.3636 -0.0323 0.0480  -0.0138 207 GLU G N     
9213  C CA    . GLU G 206 ? 0.3650 0.3730 0.3780 -0.0321 0.0471  -0.0129 207 GLU G CA    
9214  C C     . GLU G 206 ? 0.3261 0.3390 0.3395 -0.0329 0.0452  -0.0123 207 GLU G C     
9215  O O     . GLU G 206 ? 0.3350 0.3521 0.3509 -0.0321 0.0447  -0.0109 207 GLU G O     
9216  C CB    . GLU G 206 ? 0.4041 0.4109 0.4184 -0.0300 0.0483  -0.0109 207 GLU G CB    
9217  C CG    . GLU G 206 ? 0.4379 0.4394 0.4514 -0.0294 0.0503  -0.0118 207 GLU G CG    
9218  C CD    . GLU G 206 ? 0.4689 0.4687 0.4837 -0.0272 0.0518  -0.0098 207 GLU G CD    
9219  O OE1   . GLU G 206 ? 0.4953 0.4979 0.5114 -0.0260 0.0513  -0.0076 207 GLU G OE1   
9220  O OE2   . GLU G 206 ? 0.5068 0.5020 0.5209 -0.0267 0.0536  -0.0106 207 GLU G OE2   
9221  N N     . ALA G 207 ? 0.2886 0.3008 0.2995 -0.0345 0.0441  -0.0135 208 ALA G N     
9222  C CA    . ALA G 207 ? 0.3014 0.3175 0.3120 -0.0354 0.0423  -0.0133 208 ALA G CA    
9223  C C     . ALA G 207 ? 0.2931 0.3109 0.3040 -0.0340 0.0418  -0.0110 208 ALA G C     
9224  O O     . ALA G 207 ? 0.3027 0.3171 0.3126 -0.0331 0.0429  -0.0102 208 ALA G O     
9225  C CB    . ALA G 207 ? 0.3094 0.3238 0.3171 -0.0372 0.0416  -0.0151 208 ALA G CB    
9226  N N     . ALA G 208 ? 0.2878 0.3106 0.2997 -0.0338 0.0403  -0.0101 209 ALA G N     
9227  C CA    . ALA G 208 ? 0.3293 0.3541 0.3410 -0.0321 0.0397  -0.0077 209 ALA G CA    
9228  C C     . ALA G 208 ? 0.3672 0.3901 0.3754 -0.0329 0.0393  -0.0078 209 ALA G C     
9229  O O     . ALA G 208 ? 0.4113 0.4337 0.4179 -0.0349 0.0387  -0.0098 209 ALA G O     
9230  C CB    . ALA G 208 ? 0.3654 0.3967 0.3791 -0.0316 0.0378  -0.0070 209 ALA G CB    
9231  N N     . ASN G 209 ? 0.3979 0.4196 0.4051 -0.0313 0.0399  -0.0056 210 ASN G N     
9232  C CA    . ASN G 209 ? 0.3858 0.4056 0.3899 -0.0319 0.0399  -0.0054 210 ASN G CA    
9233  C C     . ASN G 209 ? 0.4012 0.4250 0.4038 -0.0308 0.0384  -0.0036 210 ASN G C     
9234  O O     . ASN G 209 ? 0.4213 0.4445 0.4210 -0.0313 0.0382  -0.0034 210 ASN G O     
9235  C CB    . ASN G 209 ? 0.3920 0.4065 0.3955 -0.0312 0.0422  -0.0045 210 ASN G CB    
9236  C CG    . ASN G 209 ? 0.4194 0.4303 0.4240 -0.0322 0.0435  -0.0066 210 ASN G CG    
9237  O OD1   . ASN G 209 ? 0.4742 0.4845 0.4780 -0.0341 0.0430  -0.0089 210 ASN G OD1   
9238  N ND2   . ASN G 209 ? 0.4428 0.4510 0.4490 -0.0309 0.0451  -0.0058 210 ASN G ND2   
9239  N N     . LEU G 210 ? 0.3761 0.4042 0.3808 -0.0292 0.0372  -0.0022 211 LEU G N     
9240  C CA    . LEU G 210 ? 0.3956 0.4283 0.3990 -0.0279 0.0354  -0.0005 211 LEU G CA    
9241  C C     . LEU G 210 ? 0.3964 0.4354 0.4019 -0.0288 0.0330  -0.0020 211 LEU G C     
9242  O O     . LEU G 210 ? 0.3838 0.4238 0.3926 -0.0296 0.0333  -0.0033 211 LEU G O     
9243  C CB    . LEU G 210 ? 0.3933 0.4256 0.3971 -0.0245 0.0362  0.0029  211 LEU G CB    
9244  C CG    . LEU G 210 ? 0.4407 0.4666 0.4424 -0.0236 0.0388  0.0045  211 LEU G CG    
9245  C CD1   . LEU G 210 ? 0.4622 0.4876 0.4639 -0.0200 0.0396  0.0081  211 LEU G CD1   
9246  C CD2   . LEU G 210 ? 0.4836 0.5077 0.4811 -0.0249 0.0388  0.0042  211 LEU G CD2   
9247  N N     . PRO G 211 ? 0.3857 0.4291 0.3893 -0.0289 0.0308  -0.0019 212 PRO G N     
9248  C CA    . PRO G 211 ? 0.4218 0.4713 0.4273 -0.0303 0.0285  -0.0037 212 PRO G CA    
9249  C C     . PRO G 211 ? 0.4609 0.5162 0.4705 -0.0282 0.0273  -0.0023 212 PRO G C     
9250  O O     . PRO G 211 ? 0.5180 0.5790 0.5303 -0.0294 0.0255  -0.0039 212 PRO G O     
9251  C CB    . PRO G 211 ? 0.4247 0.4762 0.4261 -0.0310 0.0267  -0.0041 212 PRO G CB    
9252  C CG    . PRO G 211 ? 0.3779 0.4269 0.3761 -0.0282 0.0275  -0.0009 212 PRO G CG    
9253  C CD    . PRO G 211 ? 0.4099 0.4523 0.4090 -0.0279 0.0305  -0.0002 212 PRO G CD    
9254  N N     . ILE G 212 ? 0.4622 0.5160 0.4723 -0.0250 0.0285  0.0006  213 ILE G N     
9255  C CA    . ILE G 212 ? 0.4449 0.5038 0.4590 -0.0224 0.0277  0.0023  213 ILE G CA    
9256  C C     . ILE G 212 ? 0.4559 0.5117 0.4737 -0.0220 0.0301  0.0022  213 ILE G C     
9257  O O     . ILE G 212 ? 0.4648 0.5241 0.4866 -0.0199 0.0301  0.0034  213 ILE G O     
9258  C CB    . ILE G 212 ? 0.4831 0.5428 0.4949 -0.0186 0.0271  0.0059  213 ILE G CB    
9259  C CG1   . ILE G 212 ? 0.5391 0.5905 0.5476 -0.0174 0.0300  0.0079  213 ILE G CG1   
9260  C CG2   . ILE G 212 ? 0.5039 0.5684 0.5124 -0.0187 0.0242  0.0058  213 ILE G CG2   
9261  C CD1   . ILE G 212 ? 0.5496 0.5962 0.5610 -0.0170 0.0328  0.0079  213 ILE G CD1   
9262  N N     . GLN G 213 ? 0.4729 0.5221 0.4892 -0.0239 0.0322  0.0008  214 GLN G N     
9263  C CA    . GLN G 213 ? 0.4924 0.5376 0.5111 -0.0236 0.0347  0.0006  214 GLN G CA    
9264  C C     . GLN G 213 ? 0.4919 0.5386 0.5133 -0.0263 0.0347  -0.0023 214 GLN G C     
9265  O O     . GLN G 213 ? 0.4969 0.5433 0.5166 -0.0291 0.0340  -0.0046 214 GLN G O     
9266  C CB    . GLN G 213 ? 0.5186 0.5559 0.5340 -0.0240 0.0369  0.0007  214 GLN G CB    
9267  C CG    . GLN G 213 ? 0.5279 0.5605 0.5451 -0.0237 0.0394  0.0003  214 GLN G CG    
9268  C CD    . GLN G 213 ? 0.4902 0.5157 0.5045 -0.0248 0.0413  -0.0005 214 GLN G CD    
9269  O OE1   . GLN G 213 ? 0.5004 0.5245 0.5116 -0.0258 0.0409  -0.0006 214 GLN G OE1   
9270  N NE2   . GLN G 213 ? 0.4583 0.4796 0.4736 -0.0246 0.0433  -0.0011 214 GLN G NE2   
9271  N N     . ALA G 214 ? 0.4628 0.5108 0.4882 -0.0252 0.0358  -0.0021 215 ALA G N     
9272  C CA    . ALA G 214 ? 0.4998 0.5481 0.5276 -0.0275 0.0366  -0.0046 215 ALA G CA    
9273  C C     . ALA G 214 ? 0.4434 0.4842 0.4693 -0.0282 0.0391  -0.0055 215 ALA G C     
9274  O O     . ALA G 214 ? 0.4567 0.4932 0.4816 -0.0263 0.0406  -0.0040 215 ALA G O     
9275  C CB    . ALA G 214 ? 0.5773 0.6310 0.6105 -0.0261 0.0367  -0.0040 215 ALA G CB    
9276  N N     . PRO G 215 ? 0.4511 0.4898 0.4761 -0.0309 0.0396  -0.0080 216 PRO G N     
9277  C CA    . PRO G 215 ? 0.4494 0.4814 0.4723 -0.0314 0.0417  -0.0090 216 PRO G CA    
9278  C C     . PRO G 215 ? 0.4197 0.4502 0.4451 -0.0297 0.0438  -0.0084 216 PRO G C     
9279  O O     . PRO G 215 ? 0.3941 0.4293 0.4234 -0.0286 0.0438  -0.0076 216 PRO G O     
9280  C CB    . PRO G 215 ? 0.4540 0.4853 0.4756 -0.0343 0.0414  -0.0116 216 PRO G CB    
9281  C CG    . PRO G 215 ? 0.4640 0.5018 0.4888 -0.0352 0.0401  -0.0120 216 PRO G CG    
9282  C CD    . PRO G 215 ? 0.4835 0.5261 0.5095 -0.0334 0.0383  -0.0099 216 PRO G CD    
9283  N N     . ARG G 216 ? 0.4195 0.4438 0.4428 -0.0294 0.0456  -0.0088 217 ARG G N     
9284  C CA    . ARG G 216 ? 0.4033 0.4254 0.4282 -0.0280 0.0478  -0.0086 217 ARG G CA    
9285  C C     . ARG G 216 ? 0.3592 0.3795 0.3835 -0.0297 0.0488  -0.0108 217 ARG G C     
9286  O O     . ARG G 216 ? 0.3256 0.3420 0.3464 -0.0313 0.0488  -0.0124 217 ARG G O     
9287  C CB    . ARG G 216 ? 0.3986 0.4146 0.4212 -0.0266 0.0493  -0.0081 217 ARG G CB    
9288  C CG    . ARG G 216 ? 0.4405 0.4538 0.4645 -0.0251 0.0518  -0.0081 217 ARG G CG    
9289  C CD    . ARG G 216 ? 0.4423 0.4491 0.4638 -0.0243 0.0533  -0.0082 217 ARG G CD    
9290  N NE    . ARG G 216 ? 0.4318 0.4359 0.4544 -0.0225 0.0557  -0.0080 217 ARG G NE    
9291  C CZ    . ARG G 216 ? 0.3988 0.3971 0.4196 -0.0219 0.0574  -0.0085 217 ARG G CZ    
9292  N NH1   . ARG G 216 ? 0.3301 0.3249 0.3481 -0.0230 0.0570  -0.0093 217 ARG G NH1   
9293  N NH2   . ARG G 216 ? 0.3708 0.3669 0.3926 -0.0202 0.0597  -0.0084 217 ARG G NH2   
9294  N N     . ILE G 217 ? 0.3977 0.4212 0.4254 -0.0294 0.0498  -0.0108 218 ILE G N     
9295  C CA    . ILE G 217 ? 0.4379 0.4596 0.4650 -0.0309 0.0513  -0.0125 218 ILE G CA    
9296  C C     . ILE G 217 ? 0.4820 0.5034 0.5118 -0.0292 0.0537  -0.0119 218 ILE G C     
9297  O O     . ILE G 217 ? 0.5609 0.5870 0.5948 -0.0291 0.0543  -0.0117 218 ILE G O     
9298  C CB    . ILE G 217 ? 0.4077 0.4341 0.4366 -0.0333 0.0501  -0.0135 218 ILE G CB    
9299  C CG1   . ILE G 217 ? 0.3686 0.3956 0.3949 -0.0348 0.0477  -0.0140 218 ILE G CG1   
9300  C CG2   . ILE G 217 ? 0.3901 0.4138 0.4178 -0.0349 0.0520  -0.0152 218 ILE G CG2   
9301  C CD1   . ILE G 217 ? 0.3775 0.4086 0.4052 -0.0372 0.0466  -0.0152 218 ILE G CD1   
9302  N N     . GLU G 218 ? 0.4747 0.4904 0.5020 -0.0278 0.0553  -0.0119 219 GLU G N     
9303  C CA    . GLU G 218 ? 0.4744 0.4889 0.5036 -0.0258 0.0578  -0.0114 219 GLU G CA    
9304  C C     . GLU G 218 ? 0.4202 0.4307 0.4468 -0.0268 0.0598  -0.0132 219 GLU G C     
9305  O O     . GLU G 218 ? 0.3887 0.3938 0.4107 -0.0274 0.0599  -0.0145 219 GLU G O     
9306  C CB    . GLU G 218 ? 0.5269 0.5373 0.5547 -0.0236 0.0586  -0.0104 219 GLU G CB    
9307  C CG    . GLU G 218 ? 0.5928 0.6010 0.6219 -0.0215 0.0614  -0.0101 219 GLU G CG    
9308  C CD    . GLU G 218 ? 0.6338 0.6376 0.6618 -0.0194 0.0624  -0.0092 219 GLU G CD    
9309  O OE1   . GLU G 218 ? 0.7422 0.7449 0.7686 -0.0196 0.0609  -0.0086 219 GLU G OE1   
9310  O OE2   . GLU G 218 ? 0.8114 0.8126 0.8400 -0.0176 0.0648  -0.0091 219 GLU G OE2   
9311  N N     . ARG G 219 ? 0.4050 0.4185 0.4348 -0.0270 0.0614  -0.0132 220 ARG G N     
9312  C CA    . ARG G 219 ? 0.4189 0.4288 0.4464 -0.0277 0.0637  -0.0146 220 ARG G CA    
9313  C C     . ARG G 219 ? 0.4106 0.4174 0.4382 -0.0253 0.0665  -0.0142 220 ARG G C     
9314  O O     . ARG G 219 ? 0.4429 0.4532 0.4749 -0.0234 0.0672  -0.0128 220 ARG G O     
9315  C CB    . ARG G 219 ? 0.4113 0.4257 0.4420 -0.0294 0.0644  -0.0149 220 ARG G CB    
9316  C CG    . ARG G 219 ? 0.4543 0.4715 0.4849 -0.0320 0.0619  -0.0156 220 ARG G CG    
9317  C CD    . ARG G 219 ? 0.4746 0.4969 0.5094 -0.0338 0.0627  -0.0160 220 ARG G CD    
9318  N NE    . ARG G 219 ? 0.5295 0.5543 0.5640 -0.0363 0.0603  -0.0168 220 ARG G NE    
9319  C CZ    . ARG G 219 ? 0.5910 0.6113 0.6206 -0.0381 0.0599  -0.0180 220 ARG G CZ    
9320  N NH1   . ARG G 219 ? 0.6991 0.7127 0.7238 -0.0376 0.0616  -0.0186 220 ARG G NH1   
9321  N NH2   . ARG G 219 ? 0.5547 0.5774 0.5844 -0.0401 0.0579  -0.0187 220 ARG G NH2   
9322  N N     . LEU G 220 ? 0.3911 0.3915 0.4137 -0.0253 0.0679  -0.0156 221 LEU G N     
9323  C CA    . LEU G 220 ? 0.3904 0.3872 0.4122 -0.0231 0.0706  -0.0156 221 LEU G CA    
9324  C C     . LEU G 220 ? 0.3961 0.3868 0.4121 -0.0237 0.0721  -0.0174 221 LEU G C     
9325  O O     . LEU G 220 ? 0.4481 0.4367 0.4601 -0.0253 0.0706  -0.0185 221 LEU G O     
9326  C CB    . LEU G 220 ? 0.4293 0.4239 0.4508 -0.0214 0.0699  -0.0150 221 LEU G CB    
9327  C CG    . LEU G 220 ? 0.4211 0.4107 0.4374 -0.0224 0.0683  -0.0164 221 LEU G CG    
9328  C CD1   . LEU G 220 ? 0.4451 0.4323 0.4615 -0.0209 0.0682  -0.0157 221 LEU G CD1   
9329  C CD2   . LEU G 220 ? 0.4522 0.4443 0.4678 -0.0245 0.0655  -0.0166 221 LEU G CD2   
9330  N N     . PRO G 221 ? 0.3836 0.3713 0.3986 -0.0222 0.0752  -0.0177 222 PRO G N     
9331  C CA    . PRO G 221 ? 0.3945 0.3760 0.4032 -0.0223 0.0766  -0.0194 222 PRO G CA    
9332  C C     . PRO G 221 ? 0.4076 0.3843 0.4114 -0.0221 0.0748  -0.0208 222 PRO G C     
9333  O O     . PRO G 221 ? 0.4090 0.3853 0.4141 -0.0212 0.0741  -0.0204 222 PRO G O     
9334  C CB    . PRO G 221 ? 0.4078 0.3881 0.4175 -0.0204 0.0803  -0.0192 222 PRO G CB    
9335  C CG    . PRO G 221 ? 0.4117 0.3957 0.4272 -0.0187 0.0803  -0.0176 222 PRO G CG    
9336  C CD    . PRO G 221 ? 0.3878 0.3779 0.4076 -0.0200 0.0774  -0.0165 222 PRO G CD    
9337  N N     . LEU G 222 ? 0.3916 0.3644 0.3895 -0.0230 0.0742  -0.0223 223 LEU G N     
9338  C CA    . LEU G 222 ? 0.4257 0.3947 0.4192 -0.0231 0.0723  -0.0239 223 LEU G CA    
9339  C C     . LEU G 222 ? 0.4351 0.4006 0.4277 -0.0215 0.0736  -0.0247 223 LEU G C     
9340  O O     . LEU G 222 ? 0.4516 0.4151 0.4428 -0.0216 0.0720  -0.0258 223 LEU G O     
9341  C CB    . LEU G 222 ? 0.4753 0.4407 0.4625 -0.0236 0.0721  -0.0254 223 LEU G CB    
9342  C CG    . LEU G 222 ? 0.5288 0.4905 0.5110 -0.0235 0.0700  -0.0275 223 LEU G CG    
9343  C CD1   . LEU G 222 ? 0.5630 0.5274 0.5472 -0.0248 0.0668  -0.0274 223 LEU G CD1   
9344  C CD2   . LEU G 222 ? 0.5718 0.5298 0.5474 -0.0233 0.0702  -0.0288 223 LEU G CD2   
9345  N N     . ALA G 223 ? 0.4638 0.4284 0.4574 -0.0200 0.0767  -0.0242 224 ALA G N     
9346  C CA    . ALA G 223 ? 0.5017 0.4621 0.4937 -0.0183 0.0785  -0.0252 224 ALA G CA    
9347  C C     . ALA G 223 ? 0.4513 0.4132 0.4479 -0.0177 0.0780  -0.0241 224 ALA G C     
9348  O O     . ALA G 223 ? 0.5058 0.4636 0.5007 -0.0169 0.0785  -0.0252 224 ALA G O     
9349  C CB    . ALA G 223 ? 0.5623 0.5216 0.5542 -0.0168 0.0822  -0.0249 224 ALA G CB    
9350  N N     . ASN G 224 ? 0.4452 0.4127 0.4473 -0.0179 0.0770  -0.0219 225 ASN G N     
9351  C CA    . ASN G 224 ? 0.4373 0.4064 0.4436 -0.0168 0.0769  -0.0203 225 ASN G CA    
9352  C C     . ASN G 224 ? 0.4240 0.3930 0.4297 -0.0182 0.0739  -0.0205 225 ASN G C     
9353  O O     . ASN G 224 ? 0.4199 0.3894 0.4282 -0.0174 0.0736  -0.0193 225 ASN G O     
9354  C CB    . ASN G 224 ? 0.4704 0.4460 0.4830 -0.0160 0.0773  -0.0178 225 ASN G CB    
9355  C CG    . ASN G 224 ? 0.4685 0.4445 0.4827 -0.0144 0.0806  -0.0175 225 ASN G CG    
9356  O OD1   . ASN G 224 ? 0.5243 0.4953 0.5344 -0.0139 0.0827  -0.0191 225 ASN G OD1   
9357  N ND2   . ASN G 224 ? 0.5071 0.4893 0.5272 -0.0136 0.0811  -0.0156 225 ASN G ND2   
9358  N N     . LEU G 225 ? 0.4394 0.4077 0.4415 -0.0201 0.0719  -0.0221 226 LEU G N     
9359  C CA    . LEU G 225 ? 0.4108 0.3794 0.4124 -0.0216 0.0692  -0.0225 226 LEU G CA    
9360  C C     . LEU G 225 ? 0.4506 0.4156 0.4521 -0.0210 0.0697  -0.0229 226 LEU G C     
9361  O O     . LEU G 225 ? 0.4132 0.3797 0.4173 -0.0211 0.0688  -0.0216 226 LEU G O     
9362  C CB    . LEU G 225 ? 0.4363 0.4035 0.4333 -0.0231 0.0675  -0.0246 226 LEU G CB    
9363  C CG    . LEU G 225 ? 0.4502 0.4179 0.4467 -0.0247 0.0647  -0.0253 226 LEU G CG    
9364  C CD1   . LEU G 225 ? 0.4843 0.4571 0.4845 -0.0254 0.0632  -0.0232 226 LEU G CD1   
9365  C CD2   . LEU G 225 ? 0.4506 0.4165 0.4423 -0.0257 0.0632  -0.0275 226 LEU G CD2   
9366  N N     . PRO G 226 ? 0.4642 0.4239 0.4625 -0.0203 0.0714  -0.0249 227 PRO G N     
9367  C CA    . PRO G 226 ? 0.4780 0.4336 0.4759 -0.0202 0.0720  -0.0259 227 PRO G CA    
9368  C C     . PRO G 226 ? 0.4644 0.4205 0.4665 -0.0186 0.0734  -0.0233 227 PRO G C     
9369  O O     . PRO G 226 ? 0.5142 0.4675 0.5165 -0.0189 0.0736  -0.0235 227 PRO G O     
9370  C CB    . PRO G 226 ? 0.4648 0.4152 0.4586 -0.0195 0.0740  -0.0283 227 PRO G CB    
9371  C CG    . PRO G 226 ? 0.4668 0.4186 0.4576 -0.0199 0.0733  -0.0292 227 PRO G CG    
9372  C CD    . PRO G 226 ? 0.4602 0.4176 0.4549 -0.0198 0.0728  -0.0264 227 PRO G CD    
9373  N N     . GLN G 227 ? 0.5170 0.4767 0.5224 -0.0169 0.0745  -0.0210 228 GLN G N     
9374  C CA    . GLN G 227 ? 0.5422 0.5028 0.5516 -0.0148 0.0759  -0.0184 228 GLN G CA    
9375  C C     . GLN G 227 ? 0.5511 0.5174 0.5638 -0.0152 0.0736  -0.0159 228 GLN G C     
9376  O O     . GLN G 227 ? 0.5099 0.4773 0.5254 -0.0135 0.0741  -0.0136 228 GLN G O     
9377  C CB    . GLN G 227 ? 0.5895 0.5511 0.6010 -0.0124 0.0785  -0.0173 228 GLN G CB    
9378  C CG    . GLN G 227 ? 0.6338 0.5891 0.6422 -0.0114 0.0814  -0.0193 228 GLN G CG    
9379  C CD    . GLN G 227 ? 0.6419 0.5951 0.6455 -0.0130 0.0811  -0.0221 228 GLN G CD    
9380  O OE1   . GLN G 227 ? 0.6870 0.6434 0.6907 -0.0132 0.0810  -0.0220 228 GLN G OE1   
9381  N NE2   . GLN G 227 ? 0.7191 0.6669 0.7185 -0.0140 0.0810  -0.0248 228 GLN G NE2   
9382  N N     . ALA G 228 ? 0.5318 0.5015 0.5437 -0.0173 0.0711  -0.0166 229 ALA G N     
9383  C CA    . ALA G 228 ? 0.5060 0.4814 0.5206 -0.0178 0.0689  -0.0146 229 ALA G CA    
9384  C C     . ALA G 228 ? 0.4603 0.4341 0.4745 -0.0183 0.0679  -0.0139 229 ALA G C     
9385  O O     . ALA G 228 ? 0.4655 0.4343 0.4772 -0.0192 0.0684  -0.0156 229 ALA G O     
9386  C CB    . ALA G 228 ? 0.5540 0.5322 0.5671 -0.0200 0.0669  -0.0158 229 ALA G CB    
9387  N N     . HIS G 229 ? 0.4911 0.4695 0.5082 -0.0177 0.0666  -0.0114 230 HIS G N     
9388  C CA    . HIS G 229 ? 0.5464 0.5237 0.5630 -0.0180 0.0657  -0.0104 230 HIS G CA    
9389  C C     . HIS G 229 ? 0.5574 0.5368 0.5724 -0.0208 0.0632  -0.0116 230 HIS G C     
9390  O O     . HIS G 229 ? 0.6198 0.6044 0.6360 -0.0213 0.0613  -0.0109 230 HIS G O     
9391  C CB    . HIS G 229 ? 0.5786 0.5597 0.5984 -0.0157 0.0656  -0.0070 230 HIS G CB    
9392  C CG    . HIS G 229 ? 0.6894 0.6690 0.7085 -0.0157 0.0652  -0.0055 230 HIS G CG    
9393  N ND1   . HIS G 229 ? 0.7529 0.7277 0.7717 -0.0138 0.0674  -0.0041 230 HIS G ND1   
9394  C CD2   . HIS G 229 ? 0.7266 0.7084 0.7448 -0.0172 0.0631  -0.0051 230 HIS G CD2   
9395  C CE1   . HIS G 229 ? 0.7757 0.7498 0.7936 -0.0143 0.0667  -0.0028 230 HIS G CE1   
9396  N NE2   . HIS G 229 ? 0.7950 0.7735 0.8125 -0.0163 0.0641  -0.0034 230 HIS G NE2   
9397  N N     . LEU G 230 ? 0.4693 0.4445 0.4816 -0.0225 0.0630  -0.0137 231 LEU G N     
9398  C CA    . LEU G 230 ? 0.4435 0.4204 0.4544 -0.0249 0.0608  -0.0151 231 LEU G CA    
9399  C C     . LEU G 230 ? 0.4192 0.3955 0.4301 -0.0255 0.0604  -0.0140 231 LEU G C     
9400  O O     . LEU G 230 ? 0.4335 0.4059 0.4445 -0.0248 0.0621  -0.0134 231 LEU G O     
9401  C CB    . LEU G 230 ? 0.4113 0.3849 0.4192 -0.0263 0.0607  -0.0183 231 LEU G CB    
9402  C CG    . LEU G 230 ? 0.4200 0.3935 0.4269 -0.0258 0.0613  -0.0194 231 LEU G CG    
9403  C CD1   . LEU G 230 ? 0.4257 0.3961 0.4291 -0.0270 0.0610  -0.0226 231 LEU G CD1   
9404  C CD2   . LEU G 230 ? 0.3786 0.3573 0.3867 -0.0260 0.0601  -0.0183 231 LEU G CD2   
9405  N N     . MET G 231 ? 0.4184 0.3983 0.4291 -0.0268 0.0582  -0.0138 232 MET G N     
9406  C CA    . MET G 231 ? 0.3874 0.3670 0.3978 -0.0277 0.0578  -0.0130 232 MET G CA    
9407  C C     . MET G 231 ? 0.4053 0.3852 0.4140 -0.0301 0.0562  -0.0156 232 MET G C     
9408  O O     . MET G 231 ? 0.4353 0.4168 0.4431 -0.0308 0.0551  -0.0172 232 MET G O     
9409  C CB    . MET G 231 ? 0.4270 0.4111 0.4386 -0.0266 0.0567  -0.0101 232 MET G CB    
9410  C CG    . MET G 231 ? 0.4899 0.4741 0.5034 -0.0238 0.0581  -0.0074 232 MET G CG    
9411  S SD    . MET G 231 ? 0.6464 0.6237 0.6593 -0.0228 0.0610  -0.0065 232 MET G SD    
9412  C CE    . MET G 231 ? 0.7131 0.6897 0.7244 -0.0247 0.0604  -0.0063 232 MET G CE    
9413  N N     . PRO G 232 ? 0.4042 0.3826 0.4125 -0.0314 0.0564  -0.0159 233 PRO G N     
9414  C CA    . PRO G 232 ? 0.4227 0.4018 0.4298 -0.0335 0.0550  -0.0183 233 PRO G CA    
9415  C C     . PRO G 232 ? 0.4244 0.4079 0.4309 -0.0340 0.0527  -0.0185 233 PRO G C     
9416  O O     . PRO G 232 ? 0.4575 0.4415 0.4628 -0.0351 0.0516  -0.0208 233 PRO G O     
9417  C CB    . PRO G 232 ? 0.4117 0.3898 0.4193 -0.0344 0.0557  -0.0174 233 PRO G CB    
9418  C CG    . PRO G 232 ? 0.4105 0.3847 0.4188 -0.0330 0.0582  -0.0157 233 PRO G CG    
9419  C CD    . PRO G 232 ? 0.4027 0.3786 0.4117 -0.0307 0.0581  -0.0139 233 PRO G CD    
9420  N N     . ILE G 233 ? 0.4060 0.3928 0.4133 -0.0330 0.0521  -0.0161 234 ILE G N     
9421  C CA    . ILE G 233 ? 0.4141 0.4050 0.4209 -0.0337 0.0502  -0.0162 234 ILE G CA    
9422  C C     . ILE G 233 ? 0.4080 0.4001 0.4149 -0.0332 0.0499  -0.0167 234 ILE G C     
9423  O O     . ILE G 233 ? 0.4193 0.4146 0.4261 -0.0337 0.0486  -0.0167 234 ILE G O     
9424  C CB    . ILE G 233 ? 0.4376 0.4317 0.4450 -0.0331 0.0495  -0.0137 234 ILE G CB    
9425  C CG1   . ILE G 233 ? 0.4373 0.4326 0.4465 -0.0310 0.0502  -0.0112 234 ILE G CG1   
9426  C CG2   . ILE G 233 ? 0.4794 0.4719 0.4861 -0.0337 0.0501  -0.0132 234 ILE G CG2   
9427  C CD1   . ILE G 233 ? 0.4330 0.4321 0.4425 -0.0302 0.0492  -0.0088 234 ILE G CD1   
9428  N N     . SER G 234 ? 0.3760 0.3653 0.3831 -0.0323 0.0514  -0.0172 235 SER G N     
9429  C CA    . SER G 234 ? 0.3675 0.3575 0.3747 -0.0317 0.0517  -0.0176 235 SER G CA    
9430  C C     . SER G 234 ? 0.3307 0.3197 0.3354 -0.0329 0.0508  -0.0200 235 SER G C     
9431  O O     . SER G 234 ? 0.2641 0.2505 0.2671 -0.0335 0.0507  -0.0219 235 SER G O     
9432  C CB    . SER G 234 ? 0.3971 0.3844 0.4052 -0.0302 0.0537  -0.0173 235 SER G CB    
9433  O OG    . SER G 234 ? 0.3728 0.3615 0.3834 -0.0286 0.0545  -0.0147 235 SER G OG    
9434  N N     . THR G 235 ? 0.3308 0.3220 0.3353 -0.0332 0.0503  -0.0200 236 THR G N     
9435  C CA    . THR G 235 ? 0.3197 0.3095 0.3215 -0.0338 0.0499  -0.0220 236 THR G CA    
9436  C C     . THR G 235 ? 0.3011 0.2903 0.3030 -0.0330 0.0514  -0.0218 236 THR G C     
9437  O O     . THR G 235 ? 0.3332 0.3251 0.3378 -0.0326 0.0520  -0.0203 236 THR G O     
9438  C CB    . THR G 235 ? 0.3574 0.3497 0.3585 -0.0350 0.0483  -0.0222 236 THR G CB    
9439  O OG1   . THR G 235 ? 0.3684 0.3609 0.3693 -0.0356 0.0473  -0.0224 236 THR G OG1   
9440  C CG2   . THR G 235 ? 0.3642 0.3547 0.3622 -0.0354 0.0480  -0.0238 236 THR G CG2   
9441  N N     . LEU G 236 ? 0.2881 0.2739 0.2870 -0.0328 0.0520  -0.0235 237 LEU G N     
9442  C CA    . LEU G 236 ? 0.2768 0.2612 0.2750 -0.0320 0.0537  -0.0235 237 LEU G CA    
9443  C C     . LEU G 236 ? 0.2813 0.2659 0.2774 -0.0328 0.0534  -0.0240 237 LEU G C     
9444  O O     . LEU G 236 ? 0.3148 0.2974 0.3074 -0.0331 0.0525  -0.0255 237 LEU G O     
9445  C CB    . LEU G 236 ? 0.2718 0.2520 0.2676 -0.0310 0.0548  -0.0249 237 LEU G CB    
9446  C CG    . LEU G 236 ? 0.2820 0.2600 0.2762 -0.0300 0.0569  -0.0251 237 LEU G CG    
9447  C CD1   . LEU G 236 ? 0.2608 0.2410 0.2591 -0.0292 0.0587  -0.0232 237 LEU G CD1   
9448  C CD2   . LEU G 236 ? 0.3050 0.2785 0.2955 -0.0292 0.0576  -0.0270 237 LEU G CD2   
9449  N N     . LEU G 237 ? 0.2893 0.2762 0.2875 -0.0331 0.0544  -0.0230 238 LEU G N     
9450  C CA    A LEU G 237 ? 0.2721 0.2587 0.2685 -0.0340 0.0548  -0.0234 238 LEU G CA    
9451  C CA    B LEU G 237 ? 0.2747 0.2612 0.2710 -0.0340 0.0548  -0.0234 238 LEU G CA    
9452  C C     . LEU G 237 ? 0.2670 0.2509 0.2619 -0.0331 0.0573  -0.0236 238 LEU G C     
9453  O O     . LEU G 237 ? 0.2725 0.2579 0.2705 -0.0326 0.0589  -0.0226 238 LEU G O     
9454  C CB    A LEU G 237 ? 0.2749 0.2662 0.2749 -0.0353 0.0542  -0.0224 238 LEU G CB    
9455  C CB    B LEU G 237 ? 0.2751 0.2664 0.2750 -0.0353 0.0542  -0.0224 238 LEU G CB    
9456  C CG    A LEU G 237 ? 0.2756 0.2666 0.2746 -0.0366 0.0552  -0.0227 238 LEU G CG    
9457  C CG    B LEU G 237 ? 0.2754 0.2661 0.2736 -0.0367 0.0545  -0.0230 238 LEU G CG    
9458  C CD1   A LEU G 237 ? 0.2670 0.2552 0.2617 -0.0372 0.0541  -0.0239 238 LEU G CD1   
9459  C CD1   B LEU G 237 ? 0.2824 0.2782 0.2848 -0.0382 0.0541  -0.0223 238 LEU G CD1   
9460  C CD2   A LEU G 237 ? 0.2905 0.2868 0.2941 -0.0379 0.0550  -0.0219 238 LEU G CD2   
9461  C CD2   B LEU G 237 ? 0.2711 0.2582 0.2669 -0.0362 0.0570  -0.0234 238 LEU G CD2   
9462  N N     . ILE G 238 ? 0.2640 0.2439 0.2540 -0.0329 0.0576  -0.0247 239 ILE G N     
9463  C CA    . ILE G 238 ? 0.2754 0.2520 0.2628 -0.0320 0.0601  -0.0249 239 ILE G CA    
9464  C C     . ILE G 238 ? 0.2896 0.2653 0.2753 -0.0331 0.0611  -0.0248 239 ILE G C     
9465  O O     . ILE G 238 ? 0.3257 0.2983 0.3067 -0.0329 0.0604  -0.0256 239 ILE G O     
9466  C CB    . ILE G 238 ? 0.2727 0.2448 0.2551 -0.0305 0.0599  -0.0263 239 ILE G CB    
9467  C CG1   . ILE G 238 ? 0.2929 0.2655 0.2773 -0.0299 0.0592  -0.0266 239 ILE G CG1   
9468  C CG2   . ILE G 238 ? 0.2830 0.2512 0.2617 -0.0295 0.0626  -0.0265 239 ILE G CG2   
9469  C CD1   . ILE G 238 ? 0.3032 0.2717 0.2830 -0.0287 0.0589  -0.0284 239 ILE G CD1   
9470  N N     . PRO G 239 ? 0.3101 0.2887 0.2997 -0.0342 0.0627  -0.0238 240 PRO G N     
9471  C CA    . PRO G 239 ? 0.3041 0.2818 0.2926 -0.0356 0.0640  -0.0238 240 PRO G CA    
9472  C C     . PRO G 239 ? 0.3294 0.3010 0.3117 -0.0346 0.0661  -0.0243 240 PRO G C     
9473  O O     . PRO G 239 ? 0.3503 0.3190 0.3296 -0.0327 0.0666  -0.0246 240 PRO G O     
9474  C CB    . PRO G 239 ? 0.3278 0.3102 0.3224 -0.0368 0.0656  -0.0229 240 PRO G CB    
9475  C CG    . PRO G 239 ? 0.3213 0.3081 0.3205 -0.0360 0.0641  -0.0223 240 PRO G CG    
9476  C CD    . PRO G 239 ? 0.3030 0.2859 0.2984 -0.0341 0.0635  -0.0228 240 PRO G CD    
9477  N N     . PRO G 240 ? 0.3452 0.3145 0.3251 -0.0356 0.0673  -0.0243 241 PRO G N     
9478  C CA    . PRO G 240 ? 0.3725 0.3356 0.3459 -0.0344 0.0695  -0.0244 241 PRO G CA    
9479  C C     . PRO G 240 ? 0.3756 0.3373 0.3490 -0.0335 0.0726  -0.0239 241 PRO G C     
9480  O O     . PRO G 240 ? 0.3736 0.3390 0.3525 -0.0346 0.0744  -0.0233 241 PRO G O     
9481  C CB    . PRO G 240 ? 0.3582 0.3198 0.3307 -0.0363 0.0707  -0.0242 241 PRO G CB    
9482  C CG    . PRO G 240 ? 0.3506 0.3171 0.3276 -0.0381 0.0681  -0.0245 241 PRO G CG    
9483  C CD    . PRO G 240 ? 0.3714 0.3436 0.3544 -0.0380 0.0669  -0.0242 241 PRO G CD    
9484  N N     . ALA G 241 ? 0.4281 0.3847 0.3951 -0.0313 0.0733  -0.0244 242 ALA G N     
9485  C CA    . ALA G 241 ? 0.4373 0.3916 0.4030 -0.0302 0.0765  -0.0241 242 ALA G CA    
9486  C C     . ALA G 241 ? 0.4803 0.4299 0.4416 -0.0304 0.0800  -0.0235 242 ALA G C     
9487  O O     . ALA G 241 ? 0.5242 0.4721 0.4850 -0.0300 0.0834  -0.0230 242 ALA G O     
9488  C CB    . ALA G 241 ? 0.4728 0.4243 0.4339 -0.0278 0.0754  -0.0250 242 ALA G CB    
9489  N N     . LYS G 242 ? 0.4593 0.4065 0.4174 -0.0310 0.0792  -0.0234 243 LYS G N     
9490  C CA    . LYS G 242 ? 0.5578 0.4998 0.5112 -0.0313 0.0825  -0.0227 243 LYS G CA    
9491  C C     . LYS G 242 ? 0.6451 0.5881 0.6007 -0.0337 0.0821  -0.0226 243 LYS G C     
9492  O O     . LYS G 242 ? 0.6764 0.6225 0.6342 -0.0343 0.0787  -0.0232 243 LYS G O     
9493  C CB    . LYS G 242 ? 0.5888 0.5240 0.5326 -0.0284 0.0824  -0.0229 243 LYS G CB    
9494  C CG    . LYS G 242 ? 0.6422 0.5762 0.5830 -0.0260 0.0824  -0.0235 243 LYS G CG    
9495  C CD    . LYS G 242 ? 0.7022 0.6301 0.6333 -0.0230 0.0817  -0.0239 243 LYS G CD    
9496  C CE    . LYS G 242 ? 0.7995 0.7211 0.7242 -0.0224 0.0854  -0.0227 243 LYS G CE    
9497  N NZ    . LYS G 242 ? 0.7949 0.7108 0.7097 -0.0191 0.0845  -0.0230 243 LYS G NZ    
9498  N N     . LYS G 243 ? 0.6508 0.5907 0.6054 -0.0351 0.0858  -0.0219 244 LYS G N     
9499  C CA    . LYS G 243 ? 0.7141 0.6537 0.6700 -0.0376 0.0860  -0.0220 244 LYS G CA    
9500  C C     . LYS G 243 ? 0.6785 0.6110 0.6258 -0.0358 0.0857  -0.0218 244 LYS G C     
9501  O O     . LYS G 243 ? 0.6171 0.5448 0.5574 -0.0328 0.0861  -0.0214 244 LYS G O     
9502  C CB    . LYS G 243 ? 0.8100 0.7500 0.7698 -0.0404 0.0903  -0.0216 244 LYS G CB    
9503  C CG    . LYS G 243 ? 0.8959 0.8441 0.8653 -0.0423 0.0903  -0.0218 244 LYS G CG    
9504  C CD    . LYS G 243 ? 0.9912 0.9409 0.9655 -0.0456 0.0942  -0.0218 244 LYS G CD    
9505  C CE    . LYS G 243 ? 1.0286 0.9723 0.9985 -0.0449 0.0993  -0.0209 244 LYS G CE    
9506  N NZ    . LYS G 243 ? 1.0432 0.9880 1.0133 -0.0426 0.1001  -0.0205 244 LYS G NZ    
9507  N N     . LEU G 244 ? 0.7094 0.6414 0.6571 -0.0374 0.0850  -0.0221 245 LEU G N     
9508  C CA    . LEU G 244 ? 0.7350 0.6604 0.6749 -0.0357 0.0847  -0.0218 245 LEU G CA    
9509  C C     . LEU G 244 ? 0.7531 0.6707 0.6867 -0.0349 0.0894  -0.0206 245 LEU G C     
9510  O O     . LEU G 244 ? 0.8246 0.7417 0.7611 -0.0376 0.0932  -0.0202 245 LEU G O     
9511  C CB    . LEU G 244 ? 0.7241 0.6509 0.6667 -0.0379 0.0833  -0.0224 245 LEU G CB    
9512  C CG    . LEU G 244 ? 0.6865 0.6206 0.6348 -0.0386 0.0788  -0.0235 245 LEU G CG    
9513  C CD1   . LEU G 244 ? 0.6579 0.5924 0.6076 -0.0407 0.0779  -0.0242 245 LEU G CD1   
9514  C CD2   . LEU G 244 ? 0.6836 0.6182 0.6287 -0.0353 0.0754  -0.0238 245 LEU G CD2   
9515  N N     . GLU G 245 ? 0.7890 0.7008 0.7139 -0.0313 0.0891  -0.0200 246 GLU G N     
9516  C CA    . GLU G 245 ? 0.8132 0.7166 0.7304 -0.0299 0.0934  -0.0186 246 GLU G CA    
9517  C C     . GLU G 245 ? 0.8003 0.6976 0.7106 -0.0281 0.0929  -0.0181 246 GLU G C     
9518  O O     . GLU G 245 ? 0.7610 0.6598 0.6698 -0.0262 0.0888  -0.0188 246 GLU G O     
9519  C CB    . GLU G 245 ? 0.8180 0.7193 0.7299 -0.0266 0.0939  -0.0182 246 GLU G CB    
9520  C CG    . GLU G 245 ? 0.8847 0.7913 0.8030 -0.0281 0.0950  -0.0186 246 GLU G CG    
9521  C CD    . GLU G 245 ? 0.9268 0.8310 0.8397 -0.0250 0.0956  -0.0184 246 GLU G CD    
9522  O OE1   . GLU G 245 ? 0.9948 0.8918 0.9000 -0.0233 0.0991  -0.0173 246 GLU G OE1   
9523  O OE2   . GLU G 245 ? 1.0519 0.9609 0.9678 -0.0243 0.0928  -0.0195 246 GLU G OE2   
9524  N N     . TYR G 246 ? 0.7121 0.6023 0.6184 -0.0289 0.0974  -0.0169 247 TYR G N     
9525  C CA    . TYR G 246 ? 0.7226 0.6063 0.6225 -0.0274 0.0976  -0.0163 247 TYR G CA    
9526  C C     . TYR G 246 ? 0.6295 0.5092 0.5202 -0.0221 0.0953  -0.0156 247 TYR G C     
9527  O O     . TYR G 246 ? 0.6080 0.4867 0.4950 -0.0199 0.0958  -0.0152 247 TYR G O     
9528  C CB    . TYR G 246 ? 0.7191 0.5952 0.6161 -0.0293 0.1035  -0.0150 247 TYR G CB    
9529  C CG    . TYR G 246 ? 0.7571 0.6373 0.6634 -0.0348 0.1056  -0.0160 247 TYR G CG    
9530  C CD1   . TYR G 246 ? 0.7777 0.6607 0.6885 -0.0372 0.1036  -0.0172 247 TYR G CD1   
9531  C CD2   . TYR G 246 ? 0.7673 0.6488 0.6777 -0.0374 0.1096  -0.0158 247 TYR G CD2   
9532  C CE1   . TYR G 246 ? 0.7455 0.6326 0.6646 -0.0422 0.1052  -0.0184 247 TYR G CE1   
9533  C CE2   . TYR G 246 ? 0.7263 0.6123 0.6455 -0.0424 0.1113  -0.0169 247 TYR G CE2   
9534  C CZ    . TYR G 246 ? 0.7721 0.6609 0.6955 -0.0448 0.1090  -0.0183 247 TYR G CZ    
9535  O OH    . TYR G 246 ? 0.8121 0.7057 0.7441 -0.0498 0.1104  -0.0196 247 TYR G OH    
9536  N N     . ASN G 247 ? 0.5716 0.4494 0.4590 -0.0201 0.0928  -0.0157 248 ASN G N     
9537  C CA    . ASN G 247 ? 0.5160 0.3908 0.3951 -0.0150 0.0902  -0.0153 248 ASN G CA    
9538  C C     . ASN G 247 ? 0.5159 0.3803 0.3855 -0.0126 0.0937  -0.0133 248 ASN G C     
9539  O O     . ASN G 247 ? 0.5263 0.3880 0.3936 -0.0114 0.0927  -0.0131 248 ASN G O     
9540  C CB    . ASN G 247 ? 0.5128 0.3935 0.3951 -0.0140 0.0847  -0.0168 248 ASN G CB    
9541  C CG    . ASN G 247 ? 0.5098 0.3888 0.3846 -0.0088 0.0816  -0.0167 248 ASN G CG    
9542  O OD1   . ASN G 247 ? 0.5528 0.4254 0.4190 -0.0056 0.0836  -0.0152 248 ASN G OD1   
9543  N ND2   . ASN G 247 ? 0.4770 0.3617 0.3547 -0.0078 0.0767  -0.0181 248 ASN G ND2   
9544  N N     . TYR G 248 ? 0.5148 0.3732 0.3788 -0.0117 0.0980  -0.0117 249 TYR G N     
9545  C CA    . TYR G 248 ? 0.5317 0.3793 0.3868 -0.0099 0.1025  -0.0095 249 TYR G CA    
9546  C C     . TYR G 248 ? 0.5161 0.3599 0.3627 -0.0045 0.0995  -0.0088 249 TYR G C     
9547  O O     . TYR G 248 ? 0.5072 0.3436 0.3485 -0.0033 0.1017  -0.0074 249 TYR G O     
9548  C CB    . TYR G 248 ? 0.5412 0.3837 0.3912 -0.0094 0.1072  -0.0080 249 TYR G CB    
9549  C CG    . TYR G 248 ? 0.5510 0.3960 0.4090 -0.0147 0.1113  -0.0084 249 TYR G CG    
9550  C CD1   . TYR G 248 ? 0.5861 0.4266 0.4459 -0.0183 0.1160  -0.0078 249 TYR G CD1   
9551  C CD2   . TYR G 248 ? 0.5672 0.4190 0.4308 -0.0161 0.1105  -0.0094 249 TYR G CD2   
9552  C CE1   . TYR G 248 ? 0.5933 0.4369 0.4610 -0.0232 0.1196  -0.0083 249 TYR G CE1   
9553  C CE2   . TYR G 248 ? 0.5699 0.4245 0.4410 -0.0207 0.1141  -0.0098 249 TYR G CE2   
9554  C CZ    . TYR G 248 ? 0.5770 0.4279 0.4504 -0.0242 0.1186  -0.0093 249 TYR G CZ    
9555  O OH    . TYR G 248 ? 0.6374 0.4919 0.5189 -0.0288 0.1220  -0.0098 249 TYR G OH    
9556  N N     . ALA G 249 ? 0.5254 0.3743 0.3709 -0.0013 0.0946  -0.0098 250 ALA G N     
9557  C CA    . ALA G 249 ? 0.5540 0.4006 0.3920 0.0041  0.0912  -0.0094 250 ALA G CA    
9558  C C     . ALA G 249 ? 0.5663 0.4126 0.4064 0.0037  0.0900  -0.0096 250 ALA G C     
9559  O O     . ALA G 249 ? 0.5584 0.3974 0.3909 0.0071  0.0912  -0.0080 250 ALA G O     
9560  C CB    . ALA G 249 ? 0.5644 0.4189 0.4040 0.0062  0.0857  -0.0113 250 ALA G CB    
9561  N N     . ILE G 250 ? 0.6258 0.4799 0.4761 -0.0002 0.0877  -0.0116 251 ILE G N     
9562  C CA    . ILE G 250 ? 0.5593 0.4143 0.4124 -0.0007 0.0860  -0.0122 251 ILE G CA    
9563  C C     . ILE G 250 ? 0.5275 0.3753 0.3801 -0.0036 0.0912  -0.0111 251 ILE G C     
9564  O O     . ILE G 250 ? 0.5171 0.3594 0.3655 -0.0018 0.0920  -0.0103 251 ILE G O     
9565  C CB    . ILE G 250 ? 0.5748 0.4405 0.4384 -0.0038 0.0818  -0.0147 251 ILE G CB    
9566  C CG1   . ILE G 250 ? 0.6286 0.5011 0.4931 -0.0015 0.0772  -0.0160 251 ILE G CG1   
9567  C CG2   . ILE G 250 ? 0.5504 0.4172 0.4165 -0.0041 0.0800  -0.0155 251 ILE G CG2   
9568  C CD1   . ILE G 250 ? 0.6330 0.5038 0.4900 0.0043  0.0742  -0.0157 251 ILE G CD1   
9569  N N     . LEU G 251 ? 0.5125 0.3607 0.3697 -0.0082 0.0948  -0.0112 252 LEU G N     
9570  C CA    . LEU G 251 ? 0.5349 0.3768 0.3926 -0.0117 0.1000  -0.0105 252 LEU G CA    
9571  C C     . LEU G 251 ? 0.5943 0.4244 0.4407 -0.0077 0.1035  -0.0080 252 LEU G C     
9572  O O     . LEU G 251 ? 0.5967 0.4212 0.4415 -0.0083 0.1056  -0.0076 252 LEU G O     
9573  C CB    . LEU G 251 ? 0.5326 0.3761 0.3953 -0.0161 0.1037  -0.0106 252 LEU G CB    
9574  C CG    . LEU G 251 ? 0.4956 0.3502 0.3698 -0.0204 0.1009  -0.0129 252 LEU G CG    
9575  C CD1   . LEU G 251 ? 0.4825 0.3383 0.3614 -0.0243 0.1049  -0.0129 252 LEU G CD1   
9576  C CD2   . LEU G 251 ? 0.5224 0.3804 0.4027 -0.0233 0.0991  -0.0145 252 LEU G CD2   
9577  N N     . ALA G 252 ? 0.6747 0.5009 0.5131 -0.0036 0.1042  -0.0064 253 ALA G N     
9578  C CA    . ALA G 252 ? 0.7281 0.5428 0.5548 0.0007  0.1076  -0.0037 253 ALA G CA    
9579  C C     . ALA G 252 ? 0.7294 0.5421 0.5524 0.0045  0.1047  -0.0035 253 ALA G C     
9580  O O     . ALA G 252 ? 0.7098 0.5135 0.5280 0.0052  0.1082  -0.0021 253 ALA G O     
9581  C CB    . ALA G 252 ? 0.7519 0.5648 0.5709 0.0050  0.1074  -0.0024 253 ALA G CB    
9582  N N     . LYS G 253 ? 0.7038 0.5246 0.5293 0.0071  0.0985  -0.0050 254 LYS G N     
9583  C CA    . LYS G 253 ? 0.6596 0.4799 0.4823 0.0110  0.0953  -0.0051 254 LYS G CA    
9584  C C     . LYS G 253 ? 0.6374 0.4563 0.4652 0.0072  0.0970  -0.0059 254 LYS G C     
9585  O O     . LYS G 253 ? 0.5892 0.4020 0.4121 0.0100  0.0977  -0.0049 254 LYS G O     
9586  C CB    . LYS G 253 ? 0.6408 0.4717 0.4676 0.0130  0.0885  -0.0071 254 LYS G CB    
9587  C CG    . LYS G 253 ? 0.6859 0.5183 0.5072 0.0171  0.0863  -0.0066 254 LYS G CG    
9588  C CD    . LYS G 253 ? 0.7194 0.5620 0.5446 0.0190  0.0797  -0.0089 254 LYS G CD    
9589  C CE    . LYS G 253 ? 0.7690 0.6130 0.5889 0.0226  0.0777  -0.0088 254 LYS G CE    
9590  N NZ    . LYS G 253 ? 0.8228 0.6579 0.6304 0.0284  0.0792  -0.0063 254 LYS G NZ    
9591  N N     . LEU G 254 ? 0.6299 0.4545 0.4674 0.0010  0.0976  -0.0077 255 LEU G N     
9592  C CA    . LEU G 254 ? 0.6787 0.5026 0.5215 -0.0033 0.0992  -0.0089 255 LEU G CA    
9593  C C     . LEU G 254 ? 0.7099 0.5224 0.5478 -0.0050 0.1061  -0.0071 255 LEU G C     
9594  O O     . LEU G 254 ? 0.7573 0.5663 0.5972 -0.0079 0.1084  -0.0078 255 LEU G O     
9595  C CB    . LEU G 254 ? 0.6933 0.5275 0.5478 -0.0090 0.0973  -0.0114 255 LEU G CB    
9596  C CG    . LEU G 254 ? 0.7159 0.5611 0.5760 -0.0080 0.0910  -0.0132 255 LEU G CG    
9597  C CD1   . LEU G 254 ? 0.6967 0.5507 0.5676 -0.0137 0.0897  -0.0154 255 LEU G CD1   
9598  C CD2   . LEU G 254 ? 0.7387 0.5837 0.5967 -0.0047 0.0880  -0.0136 255 LEU G CD2   
9599  N N     . GLY G 255 ? 0.7358 0.5426 0.5673 -0.0033 0.1094  -0.0051 256 GLY G N     
9600  C CA    . GLY G 255 ? 0.6619 0.4574 0.4880 -0.0046 0.1163  -0.0031 256 GLY G CA    
9601  C C     . GLY G 255 ? 0.6571 0.4548 0.4921 -0.0122 0.1197  -0.0048 256 GLY G C     
9602  O O     . GLY G 255 ? 0.6402 0.4301 0.4739 -0.0149 0.1248  -0.0044 256 GLY G O     
9603  N N     . ILE G 256 ? 0.6422 0.4508 0.4862 -0.0154 0.1169  -0.0067 257 ILE G N     
9604  C CA    . ILE G 256 ? 0.6458 0.4583 0.4990 -0.0223 0.1194  -0.0084 257 ILE G CA    
9605  C C     . ILE G 256 ? 0.6359 0.4535 0.4922 -0.0234 0.1199  -0.0083 257 ILE G C     
9606  O O     . ILE G 256 ? 0.6112 0.4293 0.4625 -0.0191 0.1181  -0.0071 257 ILE G O     
9607  C CB    . ILE G 256 ? 0.5936 0.4154 0.4564 -0.0257 0.1152  -0.0112 257 ILE G CB    
9608  C CG1   . ILE G 256 ? 0.5603 0.3932 0.4278 -0.0240 0.1089  -0.0124 257 ILE G CG1   
9609  C CG2   . ILE G 256 ? 0.6226 0.4390 0.4820 -0.0243 0.1150  -0.0114 257 ILE G CG2   
9610  C CD1   . ILE G 256 ? 0.5566 0.3989 0.4335 -0.0274 0.1050  -0.0150 257 ILE G CD1   
9611  N N     . GLY G 257 ? 0.6642 0.4859 0.5289 -0.0293 0.1224  -0.0096 258 GLY G N     
9612  C CA    . GLY G 257 ? 0.6456 0.4727 0.5145 -0.0309 0.1232  -0.0097 258 GLY G CA    
9613  C C     . GLY G 257 ? 0.6592 0.4977 0.5407 -0.0361 0.1208  -0.0123 258 GLY G C     
9614  O O     . GLY G 257 ? 0.6018 0.4434 0.4884 -0.0387 0.1190  -0.0141 258 GLY G O     
9615  N N     . PRO G 258 ? 0.6837 0.5287 0.5704 -0.0374 0.1208  -0.0127 259 PRO G N     
9616  C CA    . PRO G 258 ? 0.7096 0.5657 0.6081 -0.0419 0.1185  -0.0149 259 PRO G CA    
9617  C C     . PRO G 258 ? 0.7979 0.6542 0.7026 -0.0475 0.1213  -0.0164 259 PRO G C     
9618  O O     . PRO G 258 ? 0.8254 0.6893 0.7378 -0.0504 0.1180  -0.0185 259 PRO G O     
9619  C CB    . PRO G 258 ? 0.7178 0.5773 0.6185 -0.0420 0.1202  -0.0144 259 PRO G CB    
9620  C CG    . PRO G 258 ? 0.7236 0.5764 0.6136 -0.0363 0.1204  -0.0122 259 PRO G CG    
9621  C CD    . PRO G 258 ? 0.7259 0.5678 0.6070 -0.0345 0.1229  -0.0109 259 PRO G CD    
9622  N N     . GLU G 259 ? 0.8518 0.6993 0.7528 -0.0492 0.1275  -0.0154 260 GLU G N     
9623  C CA    . GLU G 259 ? 0.8701 0.7174 0.7771 -0.0550 0.1310  -0.0170 260 GLU G CA    
9624  C C     . GLU G 259 ? 0.8210 0.6650 0.7263 -0.0555 0.1294  -0.0181 260 GLU G C     
9625  O O     . GLU G 259 ? 0.7725 0.6178 0.6835 -0.0605 0.1308  -0.0201 260 GLU G O     
9626  C CB    . GLU G 259 ? 0.8764 0.7146 0.7796 -0.0566 0.1385  -0.0156 260 GLU G CB    
9627  C CG    . GLU G 259 ? 0.9286 0.7533 0.8189 -0.0523 0.1415  -0.0130 260 GLU G CG    
9628  C CD    . GLU G 259 ? 0.9149 0.7378 0.7969 -0.0457 0.1391  -0.0107 260 GLU G CD    
9629  O OE1   . GLU G 259 ? 0.8453 0.6772 0.7317 -0.0447 0.1353  -0.0113 260 GLU G OE1   
9630  O OE2   . GLU G 259 ? 0.9199 0.7325 0.7911 -0.0416 0.1410  -0.0085 260 GLU G OE2   
9631  N N     . ASP G 260 ? 0.7784 0.6183 0.6760 -0.0503 0.1265  -0.0169 261 ASP G N     
9632  C CA    . ASP G 260 ? 0.6926 0.5287 0.5877 -0.0499 0.1251  -0.0177 261 ASP G CA    
9633  C C     . ASP G 260 ? 0.7322 0.5793 0.6347 -0.0509 0.1188  -0.0200 261 ASP G C     
9634  O O     . ASP G 260 ? 0.7208 0.5673 0.6242 -0.0521 0.1175  -0.0214 261 ASP G O     
9635  C CB    . ASP G 260 ? 0.7133 0.5398 0.5968 -0.0438 0.1253  -0.0153 261 ASP G CB    
9636  C CG    . ASP G 260 ? 0.7417 0.5562 0.6166 -0.0425 0.1317  -0.0127 261 ASP G CG    
9637  O OD1   . ASP G 260 ? 0.7692 0.5776 0.6447 -0.0464 0.1369  -0.0131 261 ASP G OD1   
9638  O OD2   . ASP G 260 ? 0.7830 0.5943 0.6507 -0.0375 0.1316  -0.0104 261 ASP G OD2   
9639  N N     . LEU G 261 ? 0.7005 0.5570 0.6079 -0.0502 0.1152  -0.0202 262 LEU G N     
9640  C CA    . LEU G 261 ? 0.7008 0.5678 0.6151 -0.0510 0.1094  -0.0221 262 LEU G CA    
9641  C C     . LEU G 261 ? 0.7879 0.6591 0.7102 -0.0569 0.1101  -0.0246 262 LEU G C     
9642  O O     . LEU G 261 ? 0.7943 0.6662 0.7210 -0.0609 0.1137  -0.0252 262 LEU G O     
9643  C CB    . LEU G 261 ? 0.6750 0.5504 0.5934 -0.0497 0.1065  -0.0219 262 LEU G CB    
9644  C CG    . LEU G 261 ? 0.6835 0.5556 0.5944 -0.0441 0.1055  -0.0198 262 LEU G CG    
9645  C CD1   . LEU G 261 ? 0.6377 0.5187 0.5534 -0.0434 0.1023  -0.0200 262 LEU G CD1   
9646  C CD2   . LEU G 261 ? 0.7120 0.5808 0.6166 -0.0400 0.1024  -0.0195 262 LEU G CD2   
9647  N N     . GLY G 262 ? 0.7943 0.6685 0.7184 -0.0573 0.1065  -0.0262 263 GLY G N     
9648  C CA    . GLY G 262 ? 0.8331 0.7116 0.7641 -0.0626 0.1065  -0.0289 263 GLY G CA    
9649  C C     . GLY G 262 ? 0.7830 0.6738 0.7236 -0.0652 0.1033  -0.0302 263 GLY G C     
9650  O O     . GLY G 262 ? 0.7768 0.6716 0.7240 -0.0702 0.1044  -0.0322 263 GLY G O     
9651  O OXT   . GLY G 262 ? 0.7401 0.6362 0.6813 -0.0620 0.0999  -0.0293 263 GLY G OXT   
9712  N N     . LEU H 9   ? 0.4038 0.4884 0.3726 -0.0216 0.0561  -0.0219 11  LEU H N     
9713  C CA    . LEU H 9   ? 0.4386 0.5060 0.4069 -0.0226 0.0568  -0.0273 11  LEU H CA    
9714  C C     . LEU H 9   ? 0.4143 0.4739 0.3794 -0.0226 0.0567  -0.0290 11  LEU H C     
9715  O O     . LEU H 9   ? 0.4135 0.4635 0.3769 -0.0216 0.0557  -0.0338 11  LEU H O     
9716  C CB    . LEU H 9   ? 0.4638 0.5225 0.4347 -0.0277 0.0574  -0.0251 11  LEU H CB    
9717  C CG    . LEU H 9   ? 0.4938 0.5404 0.4646 -0.0299 0.0587  -0.0299 11  LEU H CG    
9718  C CD1   . LEU H 9   ? 0.4706 0.5166 0.4418 -0.0278 0.0587  -0.0354 11  LEU H CD1   
9719  C CD2   . LEU H 9   ? 0.4818 0.5239 0.4552 -0.0327 0.0583  -0.0293 11  LEU H CD2   
9720  N N     . GLY H 10  ? 0.3934 0.4570 0.3577 -0.0244 0.0568  -0.0245 12  GLY H N     
9721  C CA    . GLY H 10  ? 0.3884 0.4448 0.3494 -0.0246 0.0566  -0.0255 12  GLY H CA    
9722  C C     . GLY H 10  ? 0.4108 0.4711 0.3687 -0.0174 0.0538  -0.0302 12  GLY H C     
9723  O O     . GLY H 10  ? 0.3774 0.4277 0.3319 -0.0166 0.0521  -0.0322 12  GLY H O     
9724  N N     . GLN H 11  ? 0.4159 0.4913 0.3747 -0.0117 0.0525  -0.0323 13  GLN H N     
9725  C CA    . GLN H 11  ? 0.4404 0.5234 0.3965 -0.0026 0.0485  -0.0384 13  GLN H CA    
9726  C C     . GLN H 11  ? 0.4150 0.4907 0.3711 0.0026  0.0448  -0.0460 13  GLN H C     
9727  O O     . GLN H 11  ? 0.3875 0.4562 0.3408 0.0091  0.0392  -0.0526 13  GLN H O     
9728  C CB    . GLN H 11  ? 0.4915 0.6023 0.4485 0.0014  0.0488  -0.0366 13  GLN H CB    
9729  C CG    . GLN H 11  ? 0.5388 0.6585 0.4960 -0.0038 0.0509  -0.0292 13  GLN H CG    
9730  C CD    . GLN H 11  ? 0.5323 0.6837 0.4908 -0.0017 0.0510  -0.0259 13  GLN H CD    
9731  O OE1   . GLN H 11  ? 0.6789 0.8458 0.6357 0.0028  0.0497  -0.0276 13  GLN H OE1   
9732  N NE2   . GLN H 11  ? 0.4980 0.6612 0.4592 -0.0051 0.0523  -0.0207 13  GLN H NE2   
9733  N N     . ASP H 12  ? 0.4304 0.5071 0.3896 -0.0001 0.0469  -0.0453 14  ASP H N     
9734  C CA    . ASP H 12  ? 0.4372 0.5108 0.3972 0.0047  0.0433  -0.0526 14  ASP H CA    
9735  C C     . ASP H 12  ? 0.4483 0.4994 0.4086 -0.0018 0.0427  -0.0532 14  ASP H C     
9736  O O     . ASP H 12  ? 0.4346 0.4825 0.3972 -0.0087 0.0469  -0.0493 14  ASP H O     
9737  C CB    . ASP H 12  ? 0.4530 0.5441 0.4161 0.0063  0.0453  -0.0518 14  ASP H CB    
9738  C CG    . ASP H 12  ? 0.4995 0.5906 0.4638 0.0123  0.0415  -0.0602 14  ASP H CG    
9739  O OD1   . ASP H 12  ? 0.5676 0.6426 0.5308 0.0144  0.0363  -0.0666 14  ASP H OD1   
9740  O OD2   . ASP H 12  ? 0.5335 0.6404 0.5000 0.0144  0.0429  -0.0600 14  ASP H OD2   
9741  N N     . ALA H 13  ? 0.4549 0.4916 0.4127 0.0007  0.0365  -0.0581 15  ALA H N     
9742  C CA    . ALA H 13  ? 0.4789 0.4961 0.4365 -0.0070 0.0349  -0.0572 15  ALA H CA    
9743  C C     . ALA H 13  ? 0.5317 0.5500 0.4933 -0.0086 0.0350  -0.0602 15  ALA H C     
9744  O O     . ALA H 13  ? 0.5326 0.5436 0.4958 -0.0172 0.0372  -0.0575 15  ALA H O     
9745  C CB    . ALA H 13  ? 0.5064 0.5071 0.4603 -0.0043 0.0262  -0.0606 15  ALA H CB    
9746  N N     . GLN H 14  ? 0.5302 0.5603 0.4934 0.0000  0.0325  -0.0663 16  GLN H N     
9747  C CA    . GLN H 14  ? 0.5982 0.6316 0.5652 -0.0002 0.0324  -0.0699 16  GLN H CA    
9748  C C     . GLN H 14  ? 0.5751 0.6166 0.5449 -0.0065 0.0404  -0.0639 16  GLN H C     
9749  O O     . GLN H 14  ? 0.6020 0.6386 0.5742 -0.0124 0.0418  -0.0638 16  GLN H O     
9750  C CB    . GLN H 14  ? 0.6300 0.6787 0.5977 0.0115  0.0284  -0.0777 16  GLN H CB    
9751  C CG    . GLN H 14  ? 0.7401 0.7939 0.7117 0.0122  0.0281  -0.0820 16  GLN H CG    
9752  C CD    . GLN H 14  ? 0.8470 0.8812 0.8204 0.0062  0.0231  -0.0850 16  GLN H CD    
9753  O OE1   . GLN H 14  ? 0.8967 0.9167 0.8687 0.0088  0.0140  -0.0903 16  GLN H OE1   
9754  N NE2   . GLN H 14  ? 0.8981 0.9317 0.8745 -0.0022 0.0279  -0.0814 16  GLN H NE2   
9755  N N     . LEU H 15  ? 0.5597 0.6139 0.5290 -0.0050 0.0446  -0.0591 17  LEU H N     
9756  C CA    . LEU H 15  ? 0.5320 0.5919 0.5037 -0.0097 0.0499  -0.0536 17  LEU H CA    
9757  C C     . LEU H 15  ? 0.5104 0.5580 0.4820 -0.0180 0.0525  -0.0501 17  LEU H C     
9758  O O     . LEU H 15  ? 0.5150 0.5627 0.4891 -0.0217 0.0550  -0.0493 17  LEU H O     
9759  C CB    . LEU H 15  ? 0.5557 0.6303 0.5267 -0.0075 0.0517  -0.0480 17  LEU H CB    
9760  C CG    . LEU H 15  ? 0.5799 0.6582 0.5531 -0.0120 0.0545  -0.0416 17  LEU H CG    
9761  C CD1   . LEU H 15  ? 0.5994 0.6846 0.5752 -0.0096 0.0542  -0.0439 17  LEU H CD1   
9762  C CD2   . LEU H 15  ? 0.5973 0.6872 0.5697 -0.0127 0.0549  -0.0340 17  LEU H CD2   
9763  N N     . MET H 16  ? 0.4794 0.5181 0.4478 -0.0199 0.0515  -0.0487 18  MET H N     
9764  C CA    . MET H 16  ? 0.4934 0.5234 0.4609 -0.0273 0.0538  -0.0455 18  MET H CA    
9765  C C     . MET H 16  ? 0.4915 0.5168 0.4610 -0.0326 0.0535  -0.0478 18  MET H C     
9766  O O     . MET H 16  ? 0.4545 0.4829 0.4260 -0.0369 0.0568  -0.0470 18  MET H O     
9767  C CB    . MET H 16  ? 0.4965 0.5180 0.4597 -0.0280 0.0518  -0.0437 18  MET H CB    
9768  C CG    . MET H 16  ? 0.5320 0.5470 0.4939 -0.0357 0.0539  -0.0403 18  MET H CG    
9769  S SD    . MET H 16  ? 0.5789 0.6012 0.5426 -0.0377 0.0589  -0.0372 18  MET H SD    
9770  C CE    . MET H 16  ? 0.5496 0.5731 0.5104 -0.0341 0.0581  -0.0340 18  MET H CE    
9771  N N     . GLU H 17  ? 0.5254 0.5440 0.4944 -0.0320 0.0487  -0.0513 19  GLU H N     
9772  C CA    . GLU H 17  ? 0.5336 0.5479 0.5045 -0.0387 0.0473  -0.0525 19  GLU H CA    
9773  C C     . GLU H 17  ? 0.5285 0.5542 0.5041 -0.0378 0.0504  -0.0554 19  GLU H C     
9774  O O     . GLU H 17  ? 0.4935 0.5225 0.4714 -0.0442 0.0522  -0.0555 19  GLU H O     
9775  C CB    . GLU H 17  ? 0.5815 0.5839 0.5514 -0.0379 0.0392  -0.0556 19  GLU H CB    
9776  C CG    . GLU H 17  ? 0.6507 0.6391 0.6156 -0.0399 0.0346  -0.0523 19  GLU H CG    
9777  C CD    . GLU H 17  ? 0.7155 0.7007 0.6787 -0.0511 0.0372  -0.0453 19  GLU H CD    
9778  O OE1   . GLU H 17  ? 0.7369 0.7201 0.7017 -0.0601 0.0355  -0.0435 19  GLU H OE1   
9779  O OE2   . GLU H 17  ? 0.7841 0.7712 0.7445 -0.0512 0.0409  -0.0415 19  GLU H OE2   
9780  N N     . ASP H 18  ? 0.5257 0.5594 0.5025 -0.0300 0.0507  -0.0576 20  ASP H N     
9781  C CA    . ASP H 18  ? 0.5323 0.5763 0.5129 -0.0280 0.0528  -0.0599 20  ASP H CA    
9782  C C     . ASP H 18  ? 0.4723 0.5204 0.4539 -0.0308 0.0571  -0.0569 20  ASP H C     
9783  O O     . ASP H 18  ? 0.4392 0.4930 0.4239 -0.0321 0.0584  -0.0593 20  ASP H O     
9784  C CB    . ASP H 18  ? 0.6238 0.6769 0.6045 -0.0195 0.0517  -0.0614 20  ASP H CB    
9785  C CG    . ASP H 18  ? 0.7301 0.7828 0.7106 -0.0142 0.0464  -0.0673 20  ASP H CG    
9786  O OD1   . ASP H 18  ? 0.8557 0.8972 0.8363 -0.0178 0.0425  -0.0701 20  ASP H OD1   
9787  O OD2   . ASP H 18  ? 0.7765 0.8406 0.7567 -0.0065 0.0454  -0.0690 20  ASP H OD2   
9788  N N     . TYR H 19  ? 0.4511 0.4965 0.4302 -0.0309 0.0583  -0.0525 21  TYR H N     
9789  C CA    . TYR H 19  ? 0.4438 0.4912 0.4238 -0.0323 0.0605  -0.0506 21  TYR H CA    
9790  C C     . TYR H 19  ? 0.4842 0.5325 0.4651 -0.0380 0.0621  -0.0526 21  TYR H C     
9791  O O     . TYR H 19  ? 0.4958 0.5508 0.4794 -0.0375 0.0629  -0.0557 21  TYR H O     
9792  C CB    . TYR H 19  ? 0.4359 0.4799 0.4132 -0.0318 0.0605  -0.0456 21  TYR H CB    
9793  C CG    . TYR H 19  ? 0.4514 0.4946 0.4296 -0.0333 0.0611  -0.0445 21  TYR H CG    
9794  C CD1   . TYR H 19  ? 0.4275 0.4726 0.4081 -0.0306 0.0591  -0.0437 21  TYR H CD1   
9795  C CD2   . TYR H 19  ? 0.4321 0.4724 0.4086 -0.0371 0.0624  -0.0444 21  TYR H CD2   
9796  C CE1   . TYR H 19  ? 0.4353 0.4775 0.4169 -0.0308 0.0574  -0.0442 21  TYR H CE1   
9797  C CE2   . TYR H 19  ? 0.4514 0.4920 0.4288 -0.0370 0.0619  -0.0452 21  TYR H CE2   
9798  C CZ    . TYR H 19  ? 0.4358 0.4764 0.4160 -0.0335 0.0589  -0.0458 21  TYR H CZ    
9799  O OH    . TYR H 19  ? 0.5550 0.5939 0.5364 -0.0323 0.0563  -0.0479 21  TYR H OH    
9800  N N     . LYS H 20  ? 0.5395 0.5824 0.5176 -0.0431 0.0621  -0.0508 22  LYS H N     
9801  C CA    . LYS H 20  ? 0.5864 0.6337 0.5646 -0.0500 0.0637  -0.0510 22  LYS H CA    
9802  C C     . LYS H 20  ? 0.6143 0.6703 0.5963 -0.0528 0.0638  -0.0549 22  LYS H C     
9803  O O     . LYS H 20  ? 0.6682 0.7357 0.6518 -0.0566 0.0658  -0.0567 22  LYS H O     
9804  C CB    . LYS H 20  ? 0.6550 0.6940 0.6290 -0.0560 0.0624  -0.0464 22  LYS H CB    
9805  C CG    . LYS H 20  ? 0.7178 0.7506 0.6880 -0.0537 0.0627  -0.0430 22  LYS H CG    
9806  C CD    . LYS H 20  ? 0.7765 0.8034 0.7423 -0.0602 0.0615  -0.0384 22  LYS H CD    
9807  C CE    . LYS H 20  ? 0.8436 0.8597 0.8078 -0.0634 0.0565  -0.0368 22  LYS H CE    
9808  N NZ    . LYS H 20  ? 0.8989 0.9085 0.8586 -0.0710 0.0542  -0.0310 22  LYS H NZ    
9809  N N     . GLN H 21  ? 0.6201 0.6728 0.6035 -0.0504 0.0613  -0.0568 23  GLN H N     
9810  C CA    . GLN H 21  ? 0.6007 0.6617 0.5882 -0.0527 0.0608  -0.0609 23  GLN H CA    
9811  C C     . GLN H 21  ? 0.5366 0.6099 0.5274 -0.0477 0.0632  -0.0652 23  GLN H C     
9812  O O     . GLN H 21  ? 0.4633 0.5493 0.4570 -0.0509 0.0645  -0.0685 23  GLN H O     
9813  C CB    . GLN H 21  ? 0.5966 0.6515 0.5850 -0.0493 0.0569  -0.0632 23  GLN H CB    
9814  C CG    . GLN H 21  ? 0.6738 0.7160 0.6601 -0.0546 0.0519  -0.0611 23  GLN H CG    
9815  C CD    . GLN H 21  ? 0.7327 0.7777 0.7208 -0.0662 0.0506  -0.0595 23  GLN H CD    
9816  O OE1   . GLN H 21  ? 0.7497 0.8036 0.7375 -0.0728 0.0542  -0.0563 23  GLN H OE1   
9817  N NE2   . GLN H 21  ? 0.7607 0.7999 0.7509 -0.0690 0.0448  -0.0616 23  GLN H NE2   
9818  N N     . ASN H 22  ? 0.4562 0.5264 0.4465 -0.0399 0.0628  -0.0649 24  ASN H N     
9819  C CA    . ASN H 22  ? 0.4599 0.5375 0.4529 -0.0342 0.0626  -0.0685 24  ASN H CA    
9820  C C     . ASN H 22  ? 0.4248 0.4953 0.4159 -0.0294 0.0611  -0.0648 24  ASN H C     
9821  O O     . ASN H 22  ? 0.4635 0.5315 0.4543 -0.0252 0.0593  -0.0623 24  ASN H O     
9822  C CB    . ASN H 22  ? 0.5130 0.5958 0.5089 -0.0307 0.0612  -0.0721 24  ASN H CB    
9823  C CG    . ASN H 22  ? 0.5359 0.6264 0.5346 -0.0248 0.0600  -0.0763 24  ASN H CG    
9824  O OD1   . ASN H 22  ? 0.5383 0.6281 0.5366 -0.0224 0.0591  -0.0768 24  ASN H OD1   
9825  N ND2   . ASN H 22  ? 0.5105 0.6076 0.5117 -0.0216 0.0589  -0.0800 24  ASN H ND2   
9826  N N     . PRO H 23  ? 0.3970 0.4654 0.3868 -0.0305 0.0614  -0.0639 25  PRO H N     
9827  C CA    . PRO H 23  ? 0.4149 0.4753 0.4033 -0.0275 0.0590  -0.0599 25  PRO H CA    
9828  C C     . PRO H 23  ? 0.4229 0.4822 0.4133 -0.0219 0.0548  -0.0596 25  PRO H C     
9829  O O     . PRO H 23  ? 0.3929 0.4478 0.3820 -0.0211 0.0530  -0.0534 25  PRO H O     
9830  C CB    . PRO H 23  ? 0.4135 0.4755 0.4017 -0.0287 0.0592  -0.0626 25  PRO H CB    
9831  C CG    . PRO H 23  ? 0.4040 0.4732 0.3913 -0.0349 0.0631  -0.0638 25  PRO H CG    
9832  C CD    . PRO H 23  ? 0.4101 0.4854 0.3998 -0.0354 0.0637  -0.0664 25  PRO H CD    
9833  N N     . GLU H 24  ? 0.4367 0.5013 0.4299 -0.0181 0.0526  -0.0660 26  GLU H N     
9834  C CA    . GLU H 24  ? 0.4950 0.5561 0.4897 -0.0124 0.0467  -0.0658 26  GLU H CA    
9835  C C     . GLU H 24  ? 0.4503 0.5135 0.4447 -0.0115 0.0468  -0.0616 26  GLU H C     
9836  O O     . GLU H 24  ? 0.4023 0.4606 0.3960 -0.0097 0.0424  -0.0556 26  GLU H O     
9837  C CB    . GLU H 24  ? 0.6108 0.6790 0.6085 -0.0070 0.0438  -0.0754 26  GLU H CB    
9838  C CG    . GLU H 24  ? 0.6911 0.7563 0.6893 -0.0042 0.0398  -0.0801 26  GLU H CG    
9839  C CD    . GLU H 24  ? 0.7719 0.8449 0.7732 0.0040  0.0347  -0.0910 26  GLU H CD    
9840  O OE1   . GLU H 24  ? 0.9306 1.0162 0.9329 0.0052  0.0364  -0.0993 26  GLU H OE1   
9841  O OE2   . GLU H 24  ? 0.8117 0.8798 0.8141 0.0095  0.0287  -0.0914 26  GLU H OE2   
9842  N N     . ALA H 25  ? 0.4295 0.5006 0.4244 -0.0131 0.0512  -0.0645 27  ALA H N     
9843  C CA    . ALA H 25  ? 0.4463 0.5219 0.4412 -0.0112 0.0511  -0.0627 27  ALA H CA    
9844  C C     . ALA H 25  ? 0.4608 0.5334 0.4526 -0.0124 0.0510  -0.0544 27  ALA H C     
9845  O O     . ALA H 25  ? 0.4501 0.5259 0.4413 -0.0099 0.0484  -0.0493 27  ALA H O     
9846  C CB    . ALA H 25  ? 0.4824 0.5652 0.4788 -0.0132 0.0544  -0.0683 27  ALA H CB    
9847  N N     . VAL H 26  ? 0.4276 0.4962 0.4175 -0.0162 0.0537  -0.0529 28  VAL H N     
9848  C CA    . VAL H 26  ? 0.4645 0.5335 0.4515 -0.0168 0.0539  -0.0466 28  VAL H CA    
9849  C C     . VAL H 26  ? 0.4806 0.5466 0.4669 -0.0175 0.0505  -0.0387 28  VAL H C     
9850  O O     . VAL H 26  ? 0.4793 0.5520 0.4643 -0.0171 0.0492  -0.0321 28  VAL H O     
9851  C CB    . VAL H 26  ? 0.4401 0.5043 0.4251 -0.0201 0.0564  -0.0474 28  VAL H CB    
9852  C CG1   . VAL H 26  ? 0.4845 0.5506 0.4667 -0.0198 0.0561  -0.0417 28  VAL H CG1   
9853  C CG2   . VAL H 26  ? 0.4352 0.5003 0.4208 -0.0207 0.0576  -0.0535 28  VAL H CG2   
9854  N N     . MET H 27  ? 0.4861 0.5433 0.4734 -0.0187 0.0483  -0.0393 29  MET H N     
9855  C CA    . MET H 27  ? 0.4726 0.5232 0.4597 -0.0204 0.0432  -0.0320 29  MET H CA    
9856  C C     . MET H 27  ? 0.4801 0.5321 0.4681 -0.0183 0.0377  -0.0274 29  MET H C     
9857  O O     . MET H 27  ? 0.4763 0.5289 0.4632 -0.0213 0.0340  -0.0174 29  MET H O     
9858  C CB    . MET H 27  ? 0.4392 0.4796 0.4275 -0.0207 0.0407  -0.0362 29  MET H CB    
9859  C CG    . MET H 27  ? 0.4716 0.5099 0.4582 -0.0242 0.0443  -0.0364 29  MET H CG    
9860  S SD    . MET H 27  ? 0.4560 0.4856 0.4440 -0.0234 0.0406  -0.0418 29  MET H SD    
9861  C CE    . MET H 27  ? 0.4898 0.5279 0.4798 -0.0192 0.0429  -0.0535 29  MET H CE    
9862  N N     . ARG H 28  ? 0.5185 0.5722 0.5083 -0.0138 0.0368  -0.0341 30  ARG H N     
9863  C CA    . ARG H 28  ? 0.5816 0.6366 0.5718 -0.0111 0.0313  -0.0301 30  ARG H CA    
9864  C C     . ARG H 28  ? 0.5382 0.6071 0.5265 -0.0119 0.0338  -0.0235 30  ARG H C     
9865  O O     . ARG H 28  ? 0.5720 0.6440 0.5592 -0.0130 0.0290  -0.0142 30  ARG H O     
9866  C CB    . ARG H 28  ? 0.6302 0.6868 0.6228 -0.0052 0.0303  -0.0400 30  ARG H CB    
9867  C CG    . ARG H 28  ? 0.7215 0.7674 0.7161 -0.0019 0.0243  -0.0461 30  ARG H CG    
9868  C CD    . ARG H 28  ? 0.8241 0.8752 0.8210 0.0051  0.0222  -0.0556 30  ARG H CD    
9869  N NE    . ARG H 28  ? 0.9359 0.9775 0.9345 0.0106  0.0138  -0.0618 30  ARG H NE    
9870  C CZ    . ARG H 28  ? 0.9861 1.0257 0.9858 0.0115  0.0139  -0.0691 30  ARG H CZ    
9871  N NH1   . ARG H 28  ? 1.0140 1.0459 1.0153 0.0184  0.0045  -0.0760 30  ARG H NH1   
9872  N NH2   . ARG H 28  ? 1.0018 1.0475 1.0009 0.0061  0.0224  -0.0698 30  ARG H NH2   
9873  N N     . ALA H 29  ? 0.5168 0.5947 0.5046 -0.0113 0.0404  -0.0286 31  ALA H N     
9874  C CA    . ALA H 29  ? 0.5192 0.6128 0.5054 -0.0097 0.0425  -0.0259 31  ALA H CA    
9875  C C     . ALA H 29  ? 0.5070 0.6071 0.4908 -0.0138 0.0415  -0.0149 31  ALA H C     
9876  O O     . ALA H 29  ? 0.5662 0.6832 0.5485 -0.0128 0.0413  -0.0096 31  ALA H O     
9877  C CB    . ALA H 29  ? 0.4714 0.5691 0.4578 -0.0076 0.0475  -0.0352 31  ALA H CB    
9878  N N     . HIS H 30  ? 0.5106 0.6000 0.4942 -0.0184 0.0408  -0.0117 32  HIS H N     
9879  C CA    . HIS H 30  ? 0.5079 0.6041 0.4898 -0.0233 0.0397  -0.0013 32  HIS H CA    
9880  C C     . HIS H 30  ? 0.4714 0.5582 0.4540 -0.0287 0.0321  0.0093  32  HIS H C     
9881  O O     . HIS H 30  ? 0.4597 0.5489 0.4416 -0.0350 0.0297  0.0192  32  HIS H O     
9882  C CB    . HIS H 30  ? 0.4893 0.5817 0.4704 -0.0247 0.0436  -0.0048 32  HIS H CB    
9883  C CG    . HIS H 30  ? 0.4827 0.5855 0.4625 -0.0199 0.0484  -0.0123 32  HIS H CG    
9884  N ND1   . HIS H 30  ? 0.4751 0.5712 0.4557 -0.0163 0.0508  -0.0229 32  HIS H ND1   
9885  C CD2   . HIS H 30  ? 0.4615 0.5815 0.4394 -0.0178 0.0499  -0.0112 32  HIS H CD2   
9886  C CE1   . HIS H 30  ? 0.4982 0.6032 0.4774 -0.0124 0.0526  -0.0277 32  HIS H CE1   
9887  N NE2   . HIS H 30  ? 0.4787 0.5988 0.4562 -0.0121 0.0521  -0.0217 32  HIS H NE2   
9888  N N     . GLY H 31  ? 0.4810 0.5567 0.4650 -0.0262 0.0273  0.0069  33  GLY H N     
9889  C CA    . GLY H 31  ? 0.5128 0.5786 0.4971 -0.0300 0.0175  0.0171  33  GLY H CA    
9890  C C     . GLY H 31  ? 0.5559 0.6014 0.5417 -0.0336 0.0117  0.0177  33  GLY H C     
9891  O O     . GLY H 31  ? 0.5553 0.5930 0.5413 -0.0399 0.0030  0.0292  33  GLY H O     
9892  N N     . LEU H 32  ? 0.5512 0.5889 0.5383 -0.0300 0.0158  0.0058  34  LEU H N     
9893  C CA    . LEU H 32  ? 0.5473 0.5671 0.5359 -0.0313 0.0100  0.0034  34  LEU H CA    
9894  C C     . LEU H 32  ? 0.5431 0.5483 0.5337 -0.0260 0.0003  -0.0013 34  LEU H C     
9895  O O     . LEU H 32  ? 0.5079 0.5174 0.4990 -0.0194 0.0023  -0.0094 34  LEU H O     
9896  C CB    . LEU H 32  ? 0.5450 0.5653 0.5338 -0.0292 0.0177  -0.0072 34  LEU H CB    
9897  C CG    . LEU H 32  ? 0.5332 0.5623 0.5201 -0.0340 0.0242  -0.0029 34  LEU H CG    
9898  C CD1   . LEU H 32  ? 0.5460 0.5930 0.5310 -0.0329 0.0312  -0.0018 34  LEU H CD1   
9899  C CD2   . LEU H 32  ? 0.5413 0.5657 0.5282 -0.0328 0.0285  -0.0118 34  LEU H CD2   
9900  N N     . THR H 33  ? 0.5702 0.5578 0.5620 -0.0287 -0.0112 0.0034  35  THR H N     
9901  C CA    . THR H 33  ? 0.5440 0.5149 0.5375 -0.0227 -0.0234 -0.0013 35  THR H CA    
9902  C C     . THR H 33  ? 0.5377 0.5068 0.5331 -0.0135 -0.0211 -0.0194 35  THR H C     
9903  O O     . THR H 33  ? 0.4806 0.4578 0.4759 -0.0141 -0.0118 -0.0254 35  THR H O     
9904  C CB    . THR H 33  ? 0.5495 0.5002 0.5438 -0.0288 -0.0381 0.0090  35  THR H CB    
9905  O OG1   . THR H 33  ? 0.5260 0.4719 0.5216 -0.0305 -0.0366 0.0041  35  THR H OG1   
9906  C CG2   . THR H 33  ? 0.5661 0.5231 0.5586 -0.0402 -0.0402 0.0288  35  THR H CG2   
9907  N N     . ASP H 34  ? 0.5650 0.5249 0.5620 -0.0048 -0.0305 -0.0278 36  ASP H N     
9908  C CA    . ASP H 34  ? 0.6108 0.5739 0.6097 0.0049  -0.0294 -0.0456 36  ASP H CA    
9909  C C     . ASP H 34  ? 0.5911 0.5463 0.5912 0.0045  -0.0322 -0.0505 36  ASP H C     
9910  O O     . ASP H 34  ? 0.5609 0.5282 0.5614 0.0071  -0.0239 -0.0609 36  ASP H O     
9911  C CB    . ASP H 34  ? 0.6839 0.6391 0.6844 0.0154  -0.0411 -0.0538 36  ASP H CB    
9912  C CG    . ASP H 34  ? 0.7563 0.7211 0.7559 0.0172  -0.0383 -0.0508 36  ASP H CG    
9913  O OD1   . ASP H 34  ? 0.8165 0.7954 0.8143 0.0108  -0.0267 -0.0435 36  ASP H OD1   
9914  O OD2   . ASP H 34  ? 0.8359 0.7939 0.8363 0.0259  -0.0485 -0.0566 36  ASP H OD2   
9915  N N     . GLU H 35  ? 0.6146 0.5501 0.6152 0.0004  -0.0447 -0.0424 37  GLU H N     
9916  C CA    . GLU H 35  ? 0.6252 0.5511 0.6273 0.0002  -0.0497 -0.0470 37  GLU H CA    
9917  C C     . GLU H 35  ? 0.5906 0.5301 0.5910 -0.0077 -0.0355 -0.0428 37  GLU H C     
9918  O O     . GLU H 35  ? 0.5369 0.4804 0.5377 -0.0052 -0.0321 -0.0519 37  GLU H O     
9919  C CB    . GLU H 35  ? 0.7019 0.6024 0.7052 -0.0044 -0.0673 -0.0372 37  GLU H CB    
9920  C CG    . GLU H 35  ? 0.7627 0.6634 0.7641 -0.0186 -0.0654 -0.0161 37  GLU H CG    
9921  C CD    . GLU H 35  ? 0.8642 0.7406 0.8670 -0.0258 -0.0837 -0.0037 37  GLU H CD    
9922  O OE1   . GLU H 35  ? 0.8731 0.7357 0.8782 -0.0266 -0.0921 -0.0072 37  GLU H OE1   
9923  O OE2   . GLU H 35  ? 0.8428 0.7143 0.8445 -0.0311 -0.0904 0.0098  37  GLU H OE2   
9924  N N     . GLN H 36  ? 0.6146 0.5621 0.6128 -0.0166 -0.0278 -0.0292 38  GLN H N     
9925  C CA    . GLN H 36  ? 0.5964 0.5565 0.5927 -0.0231 -0.0155 -0.0249 38  GLN H CA    
9926  C C     . GLN H 36  ? 0.5621 0.5380 0.5575 -0.0182 -0.0033 -0.0366 38  GLN H C     
9927  O O     . GLN H 36  ? 0.5735 0.5545 0.5681 -0.0195 0.0028  -0.0402 38  GLN H O     
9928  C CB    . GLN H 36  ? 0.6055 0.5743 0.5999 -0.0314 -0.0113 -0.0099 38  GLN H CB    
9929  C CG    . GLN H 36  ? 0.6000 0.5572 0.5951 -0.0397 -0.0227 0.0047  38  GLN H CG    
9930  C CD    . GLN H 36  ? 0.5843 0.5563 0.5773 -0.0473 -0.0185 0.0194  38  GLN H CD    
9931  O OE1   . GLN H 36  ? 0.5195 0.5093 0.5106 -0.0450 -0.0076 0.0175  38  GLN H OE1   
9932  N NE2   . GLN H 36  ? 0.5806 0.5466 0.5741 -0.0566 -0.0281 0.0343  38  GLN H NE2   
9933  N N     . ILE H 37  ? 0.5388 0.5226 0.5344 -0.0131 -0.0005 -0.0416 39  ILE H N     
9934  C CA    . ILE H 37  ? 0.5662 0.5653 0.5614 -0.0099 0.0098  -0.0514 39  ILE H CA    
9935  C C     . ILE H 37  ? 0.5528 0.5529 0.5495 -0.0041 0.0073  -0.0642 39  ILE H C     
9936  O O     . ILE H 37  ? 0.5301 0.5412 0.5258 -0.0055 0.0154  -0.0686 39  ILE H O     
9937  C CB    . ILE H 37  ? 0.5718 0.5792 0.5675 -0.0060 0.0117  -0.0541 39  ILE H CB    
9938  C CG1   . ILE H 37  ? 0.5798 0.5907 0.5738 -0.0110 0.0149  -0.0425 39  ILE H CG1   
9939  C CG2   . ILE H 37  ? 0.5643 0.5877 0.5606 -0.0035 0.0204  -0.0646 39  ILE H CG2   
9940  C CD1   . ILE H 37  ? 0.5811 0.6012 0.5756 -0.0071 0.0170  -0.0453 39  ILE H CD1   
9941  N N     . ASN H 38  ? 0.5588 0.5478 0.5578 0.0027  -0.0049 -0.0701 40  ASN H N     
9942  C CA    . ASN H 38  ? 0.5888 0.5810 0.5896 0.0106  -0.0093 -0.0843 40  ASN H CA    
9943  C C     . ASN H 38  ? 0.5689 0.5600 0.5686 0.0062  -0.0068 -0.0832 40  ASN H C     
9944  O O     . ASN H 38  ? 0.5435 0.5489 0.5428 0.0086  -0.0013 -0.0921 40  ASN H O     
9945  C CB    . ASN H 38  ? 0.6713 0.6478 0.6747 0.0196  -0.0258 -0.0907 40  ASN H CB    
9946  C CG    . ASN H 38  ? 0.7078 0.6893 0.7132 0.0296  -0.0318 -0.1073 40  ASN H CG    
9947  O OD1   . ASN H 38  ? 0.7066 0.7103 0.7123 0.0351  -0.0251 -0.1188 40  ASN H OD1   
9948  N ND2   . ASN H 38  ? 0.7629 0.7259 0.7696 0.0319  -0.0446 -0.1089 40  ASN H ND2   
9949  N N     . ALA H 39  ? 0.5423 0.5182 0.5415 -0.0007 -0.0111 -0.0716 41  ALA H N     
9950  C CA    . ALA H 39  ? 0.5198 0.4933 0.5183 -0.0050 -0.0099 -0.0698 41  ALA H CA    
9951  C C     . ALA H 39  ? 0.4796 0.4702 0.4749 -0.0098 0.0050  -0.0684 41  ALA H C     
9952  O O     . ALA H 39  ? 0.4366 0.4330 0.4309 -0.0098 0.0080  -0.0729 41  ALA H O     
9953  C CB    . ALA H 39  ? 0.5255 0.4828 0.5242 -0.0131 -0.0166 -0.0561 41  ALA H CB    
9954  N N     . VAL H 40  ? 0.4552 0.4531 0.4489 -0.0135 0.0132  -0.0620 42  VAL H N     
9955  C CA    . VAL H 40  ? 0.4570 0.4675 0.4477 -0.0181 0.0252  -0.0600 42  VAL H CA    
9956  C C     . VAL H 40  ? 0.4549 0.4803 0.4456 -0.0142 0.0297  -0.0710 42  VAL H C     
9957  O O     . VAL H 40  ? 0.4471 0.4804 0.4356 -0.0170 0.0353  -0.0721 42  VAL H O     
9958  C CB    . VAL H 40  ? 0.4731 0.4870 0.4625 -0.0216 0.0307  -0.0522 42  VAL H CB    
9959  C CG1   . VAL H 40  ? 0.4779 0.5029 0.4646 -0.0248 0.0408  -0.0525 42  VAL H CG1   
9960  C CG2   . VAL H 40  ? 0.4681 0.4744 0.4570 -0.0266 0.0278  -0.0404 42  VAL H CG2   
9961  N N     . MET H 41  ? 0.4783 0.5090 0.4713 -0.0082 0.0269  -0.0786 43  MET H N     
9962  C CA    . MET H 41  ? 0.5048 0.5549 0.4984 -0.0053 0.0315  -0.0884 43  MET H CA    
9963  C C     . MET H 41  ? 0.4906 0.5475 0.4847 -0.0002 0.0277  -0.0982 43  MET H C     
9964  O O     . MET H 41  ? 0.4986 0.5747 0.4916 -0.0013 0.0336  -0.1030 43  MET H O     
9965  C CB    . MET H 41  ? 0.5515 0.6074 0.5478 0.0008  0.0286  -0.0947 43  MET H CB    
9966  C CG    . MET H 41  ? 0.5704 0.6238 0.5662 -0.0035 0.0328  -0.0867 43  MET H CG    
9967  S SD    . MET H 41  ? 0.6297 0.6914 0.6223 -0.0136 0.0446  -0.0796 43  MET H SD    
9968  C CE    . MET H 41  ? 0.6463 0.7313 0.6395 -0.0137 0.0490  -0.0892 43  MET H CE    
9969  N N     . THR H 42  ? 0.4742 0.5158 0.4700 0.0048  0.0171  -0.1007 44  THR H N     
9970  C CA    . THR H 42  ? 0.4948 0.5414 0.4915 0.0114  0.0114  -0.1116 44  THR H CA    
9971  C C     . THR H 42  ? 0.4954 0.5399 0.4893 0.0046  0.0158  -0.1054 44  THR H C     
9972  O O     . THR H 42  ? 0.5104 0.5644 0.5041 0.0084  0.0143  -0.1135 44  THR H O     
9973  C CB    . THR H 42  ? 0.5463 0.5747 0.5464 0.0201  -0.0042 -0.1177 44  THR H CB    
9974  O OG1   . THR H 42  ? 0.5506 0.5559 0.5502 0.0127  -0.0078 -0.1041 44  THR H OG1   
9975  C CG2   . THR H 42  ? 0.5470 0.5777 0.5496 0.0283  -0.0097 -0.1251 44  THR H CG2   
9976  N N     . GLY H 43  ? 0.5128 0.5467 0.5045 -0.0044 0.0208  -0.0918 45  GLY H N     
9977  C CA    . GLY H 43  ? 0.4916 0.5231 0.4805 -0.0106 0.0247  -0.0853 45  GLY H CA    
9978  C C     . GLY H 43  ? 0.5345 0.5505 0.5253 -0.0088 0.0144  -0.0860 45  GLY H C     
9979  O O     . GLY H 43  ? 0.6249 0.6438 0.6145 -0.0093 0.0148  -0.0880 45  GLY H O     
9980  N N     . ASP H 44  ? 0.5417 0.5410 0.5356 -0.0071 0.0045  -0.0838 46  ASP H N     
9981  C CA    . ASP H 44  ? 0.5655 0.5469 0.5619 -0.0069 -0.0076 -0.0830 46  ASP H CA    
9982  C C     . ASP H 44  ? 0.5517 0.5232 0.5472 -0.0174 -0.0061 -0.0671 46  ASP H C     
9983  O O     . ASP H 44  ? 0.5519 0.5123 0.5489 -0.0207 -0.0116 -0.0587 46  ASP H O     
9984  C CB    . ASP H 44  ? 0.6111 0.5791 0.6114 0.0009  -0.0221 -0.0898 46  ASP H CB    
9985  C CG    . ASP H 44  ? 0.6653 0.6113 0.6687 0.0010  -0.0378 -0.0895 46  ASP H CG    
9986  O OD1   . ASP H 44  ? 0.6783 0.6212 0.6812 -0.0056 -0.0366 -0.0835 46  ASP H OD1   
9987  O OD2   . ASP H 44  ? 0.6957 0.6273 0.7022 0.0078  -0.0520 -0.0954 46  ASP H OD2   
9988  N N     . MET H 45  ? 0.5782 0.5559 0.5711 -0.0226 0.0011  -0.0630 47  MET H N     
9989  C CA    . MET H 45  ? 0.5959 0.5705 0.5876 -0.0318 0.0041  -0.0492 47  MET H CA    
9990  C C     . MET H 45  ? 0.6622 0.6200 0.6576 -0.0358 -0.0088 -0.0429 47  MET H C     
9991  O O     . MET H 45  ? 0.7089 0.6643 0.7046 -0.0431 -0.0094 -0.0304 47  MET H O     
9992  C CB    . MET H 45  ? 0.5993 0.5832 0.5877 -0.0347 0.0122  -0.0481 47  MET H CB    
9993  C CG    . MET H 45  ? 0.5774 0.5760 0.5617 -0.0334 0.0239  -0.0508 47  MET H CG    
9994  S SD    . MET H 45  ? 0.5484 0.5511 0.5312 -0.0358 0.0307  -0.0439 47  MET H SD    
9995  C CE    . MET H 45  ? 0.5641 0.5669 0.5499 -0.0290 0.0266  -0.0530 47  MET H CE    
9996  N N     . GLU H 46  ? 0.6805 0.6279 0.6789 -0.0313 -0.0198 -0.0516 48  GLU H N     
9997  C CA    . GLU H 46  ? 0.7540 0.6826 0.7563 -0.0359 -0.0344 -0.0459 48  GLU H CA    
9998  C C     . GLU H 46  ? 0.7770 0.6946 0.7810 -0.0388 -0.0418 -0.0373 48  GLU H C     
9999  O O     . GLU H 46  ? 0.8630 0.7762 0.8677 -0.0490 -0.0448 -0.0225 48  GLU H O     
10000 C CB    . GLU H 46  ? 0.8103 0.7283 0.8158 -0.0279 -0.0471 -0.0599 48  GLU H CB    
10001 C CG    . GLU H 46  ? 0.9179 0.8113 0.9281 -0.0320 -0.0660 -0.0550 48  GLU H CG    
10002 C CD    . GLU H 46  ? 0.9510 0.8411 0.9621 -0.0455 -0.0670 -0.0404 48  GLU H CD    
10003 O OE1   . GLU H 46  ? 0.9351 0.8428 0.9430 -0.0503 -0.0527 -0.0349 48  GLU H OE1   
10004 O OE2   . GLU H 46  ? 0.9598 0.8301 0.9750 -0.0514 -0.0830 -0.0344 48  GLU H OE2   
10005 N N     . LYS H 47  ? 0.7815 0.6970 0.7859 -0.0297 -0.0448 -0.0463 49  LYS H N     
10006 C CA    . LYS H 47  ? 0.7701 0.6754 0.7754 -0.0309 -0.0520 -0.0392 49  LYS H CA    
10007 C C     . LYS H 47  ? 0.7535 0.6705 0.7563 -0.0406 -0.0415 -0.0235 49  LYS H C     
10008 O O     . LYS H 47  ? 0.7946 0.7038 0.7983 -0.0484 -0.0486 -0.0100 49  LYS H O     
10009 C CB    . LYS H 47  ? 0.7796 0.6887 0.7849 -0.0190 -0.0521 -0.0522 49  LYS H CB    
10010 C CG    . LYS H 47  ? 0.7877 0.6880 0.7934 -0.0192 -0.0586 -0.0454 49  LYS H CG    
10011 C CD    . LYS H 47  ? 0.8106 0.6845 0.8194 -0.0228 -0.0787 -0.0384 49  LYS H CD    
10012 C CE    . LYS H 47  ? 0.8140 0.6741 0.8243 -0.0127 -0.0920 -0.0463 49  LYS H CE    
10013 N NZ    . LYS H 47  ? 0.8411 0.6724 0.8540 -0.0171 -0.1133 -0.0381 49  LYS H NZ    
10014 N N     . LEU H 48  ? 0.6772 0.6137 0.6767 -0.0398 -0.0255 -0.0255 50  LEU H N     
10015 C CA    . LEU H 48  ? 0.6454 0.5953 0.6424 -0.0464 -0.0156 -0.0137 50  LEU H CA    
10016 C C     . LEU H 48  ? 0.6533 0.6027 0.6509 -0.0573 -0.0187 0.0000  50  LEU H C     
10017 O O     . LEU H 48  ? 0.6214 0.5780 0.6184 -0.0641 -0.0177 0.0125  50  LEU H O     
10018 C CB    . LEU H 48  ? 0.5963 0.5633 0.5897 -0.0434 -0.0006 -0.0195 50  LEU H CB    
10019 C CG    . LEU H 48  ? 0.5730 0.5462 0.5657 -0.0356 0.0043  -0.0292 50  LEU H CG    
10020 C CD1   . LEU H 48  ? 0.5498 0.5379 0.5391 -0.0353 0.0175  -0.0321 50  LEU H CD1   
10021 C CD2   . LEU H 48  ? 0.5694 0.5415 0.5626 -0.0356 0.0017  -0.0237 50  LEU H CD2   
10022 N N     . LYS H 49  ? 0.6946 0.6380 0.6936 -0.0590 -0.0227 -0.0029 51  LYS H N     
10023 C CA    . LYS H 49  ? 0.7304 0.6741 0.7307 -0.0698 -0.0266 0.0092  51  LYS H CA    
10024 C C     . LYS H 49  ? 0.7359 0.6616 0.7400 -0.0764 -0.0431 0.0186  51  LYS H C     
10025 O O     . LYS H 49  ? 0.8379 0.7682 0.8429 -0.0878 -0.0462 0.0340  51  LYS H O     
10026 C CB    . LYS H 49  ? 0.7647 0.7079 0.7655 -0.0688 -0.0257 0.0022  51  LYS H CB    
10027 C CG    . LYS H 49  ? 0.7712 0.7316 0.7676 -0.0645 -0.0106 -0.0039 51  LYS H CG    
10028 C CD    . LYS H 49  ? 0.8441 0.8051 0.8404 -0.0636 -0.0100 -0.0101 51  LYS H CD    
10029 C CE    . LYS H 49  ? 0.8411 0.8181 0.8326 -0.0612 0.0037  -0.0124 51  LYS H CE    
10030 N NZ    . LYS H 49  ? 0.8304 0.8099 0.8215 -0.0625 0.0039  -0.0147 51  LYS H NZ    
10031 N N     . THR H 50  ? 0.7811 0.6875 0.7874 -0.0690 -0.0545 0.0091  52  THR H N     
10032 C CA    . THR H 50  ? 0.7970 0.6813 0.8066 -0.0738 -0.0730 0.0167  52  THR H CA    
10033 C C     . THR H 50  ? 0.7879 0.6780 0.7959 -0.0791 -0.0721 0.0303  52  THR H C     
10034 O O     . THR H 50  ? 0.7472 0.6304 0.7568 -0.0907 -0.0825 0.0463  52  THR H O     
10035 C CB    . THR H 50  ? 0.8150 0.6793 0.8268 -0.0612 -0.0851 0.0001  52  THR H CB    
10036 O OG1   . THR H 50  ? 0.8869 0.7485 0.9003 -0.0579 -0.0869 -0.0105 52  THR H OG1   
10037 C CG2   . THR H 50  ? 0.8577 0.6954 0.8725 -0.0641 -0.1063 0.0067  52  THR H CG2   
10038 N N     . LEU H 51  ? 0.7884 0.6925 0.7933 -0.0711 -0.0599 0.0241  53  LEU H N     
10039 C CA    . LEU H 51  ? 0.7660 0.6779 0.7691 -0.0740 -0.0581 0.0345  53  LEU H CA    
10040 C C     . LEU H 51  ? 0.7567 0.6934 0.7577 -0.0838 -0.0471 0.0480  53  LEU H C     
10041 O O     . LEU H 51  ? 0.6945 0.6416 0.6941 -0.0891 -0.0468 0.0601  53  LEU H O     
10042 C CB    . LEU H 51  ? 0.7132 0.6310 0.7144 -0.0615 -0.0503 0.0214  53  LEU H CB    
10043 C CG    . LEU H 51  ? 0.7161 0.6141 0.7193 -0.0505 -0.0620 0.0080  53  LEU H CG    
10044 C CD1   . LEU H 51  ? 0.6551 0.5651 0.6567 -0.0392 -0.0519 -0.0050 53  LEU H CD1   
10045 C CD2   . LEU H 51  ? 0.7548 0.6322 0.7596 -0.0545 -0.0800 0.0182  53  LEU H CD2   
10046 N N     . SER H 52  ? 0.7438 0.6915 0.7443 -0.0853 -0.0386 0.0452  54  SER H N     
10047 C CA    . SER H 52  ? 0.8078 0.7803 0.8065 -0.0929 -0.0291 0.0557  54  SER H CA    
10048 C C     . SER H 52  ? 0.8885 0.8592 0.8901 -0.1057 -0.0376 0.0679  54  SER H C     
10049 O O     . SER H 52  ? 0.9516 0.9395 0.9525 -0.1096 -0.0304 0.0703  54  SER H O     
10050 C CB    . SER H 52  ? 0.8064 0.7940 0.8023 -0.0855 -0.0142 0.0448  54  SER H CB    
10051 O OG    . SER H 52  ? 0.8109 0.8230 0.8051 -0.0909 -0.0064 0.0531  54  SER H OG    
10052 N N     . GLY H 53  ? 0.8845 0.8336 0.8892 -0.1122 -0.0542 0.0753  55  GLY H N     
10053 C CA    . GLY H 53  ? 0.8925 0.8360 0.9008 -0.1258 -0.0651 0.0875  55  GLY H CA    
10054 C C     . GLY H 53  ? 0.8869 0.8419 0.8955 -0.1259 -0.0569 0.0818  55  GLY H C     
10055 O O     . GLY H 53  ? 0.9572 0.9296 0.9667 -0.1372 -0.0557 0.0937  55  GLY H O     
10056 N N     . ASP H 54  ? 0.9341 0.8811 0.9418 -0.1134 -0.0516 0.0636  56  ASP H N     
10057 C CA    . ASP H 54  ? 1.0166 0.9740 1.0236 -0.1116 -0.0433 0.0567  56  ASP H CA    
10058 C C     . ASP H 54  ? 1.0447 0.9794 1.0554 -0.1106 -0.0551 0.0488  56  ASP H C     
10059 O O     . ASP H 54  ? 1.1210 1.0523 1.1306 -0.1002 -0.0506 0.0334  56  ASP H O     
10060 C CB    . ASP H 54  ? 1.1072 1.0771 1.1097 -0.0993 -0.0275 0.0437  56  ASP H CB    
10061 C CG    . ASP H 54  ? 1.1751 1.1588 1.1757 -0.0976 -0.0179 0.0387  56  ASP H CG    
10062 O OD1   . ASP H 54  ? 1.3269 1.3137 1.3299 -0.1060 -0.0222 0.0453  56  ASP H OD1   
10063 O OD2   . ASP H 54  ? 1.1668 1.1577 1.1636 -0.0884 -0.0069 0.0287  56  ASP H OD2   
10064 N N     . SER H 55  ? 1.0392 0.9592 1.0544 -0.1220 -0.0711 0.0597  57  SER H N     
10065 C CA    . SER H 55  ? 1.0532 0.9501 1.0727 -0.1217 -0.0852 0.0526  57  SER H CA    
10066 C C     . SER H 55  ? 1.0717 0.9819 1.0910 -0.1215 -0.0771 0.0469  57  SER H C     
10067 O O     . SER H 55  ? 1.1700 1.0660 1.1918 -0.1170 -0.0845 0.0358  57  SER H O     
10068 C CB    . SER H 55  ? 1.0486 0.9273 1.0729 -0.1361 -0.1048 0.0678  57  SER H CB    
10069 O OG    . SER H 55  ? 0.9679 0.8687 0.9924 -0.1521 -0.1009 0.0875  57  SER H OG    
10070 N N     . SER H 56  ? 1.0760 1.0142 1.0923 -0.1254 -0.0625 0.0538  58  SER H N     
10071 C CA    . SER H 56  ? 1.0630 1.0160 1.0783 -0.1249 -0.0541 0.0494  58  SER H CA    
10072 C C     . SER H 56  ? 1.0189 0.9539 1.0360 -0.1165 -0.0604 0.0335  58  SER H C     
10073 O O     . SER H 56  ? 1.0312 0.9715 1.0442 -0.1042 -0.0499 0.0200  58  SER H O     
10074 C CB    . SER H 56  ? 1.0895 1.0664 1.0990 -0.1173 -0.0357 0.0454  58  SER H CB    
10075 O OG    . SER H 56  ? 1.1449 1.1351 1.1531 -0.1162 -0.0287 0.0413  58  SER H OG    
10076 N N     . ALA H 60  ? 0.8704 0.8804 0.8707 -0.0941 -0.0125 -0.0007 62  ALA H N     
10077 C CA    . ALA H 60  ? 0.8830 0.8976 0.8789 -0.0857 -0.0070 -0.0112 62  ALA H CA    
10078 C C     . ALA H 60  ? 0.8565 0.8882 0.8456 -0.0817 0.0059  -0.0091 62  ALA H C     
10079 O O     . ALA H 60  ? 0.8666 0.9128 0.8556 -0.0865 0.0085  -0.0014 62  ALA H O     
10080 C CB    . ALA H 60  ? 0.8808 0.8955 0.8808 -0.0901 -0.0147 -0.0125 62  ALA H CB    
10081 N N     . LEU H 61  ? 0.7722 0.8026 0.7555 -0.0729 0.0130  -0.0161 63  LEU H N     
10082 C CA    . LEU H 61  ? 0.7206 0.7620 0.6972 -0.0687 0.0232  -0.0145 63  LEU H CA    
10083 C C     . LEU H 61  ? 0.6843 0.7320 0.6559 -0.0641 0.0266  -0.0193 63  LEU H C     
10084 O O     . LEU H 61  ? 0.6636 0.7171 0.6288 -0.0595 0.0334  -0.0192 63  LEU H O     
10085 C CB    . LEU H 61  ? 0.7430 0.7784 0.7165 -0.0637 0.0277  -0.0174 63  LEU H CB    
10086 C CG    . LEU H 61  ? 0.7840 0.8121 0.7620 -0.0670 0.0239  -0.0138 63  LEU H CG    
10087 C CD1   . LEU H 61  ? 0.8345 0.8592 0.8092 -0.0618 0.0291  -0.0173 63  LEU H CD1   
10088 C CD2   . LEU H 61  ? 0.7339 0.7716 0.7141 -0.0735 0.0236  -0.0033 63  LEU H CD2   
10089 N N     . VAL H 62  ? 0.6094 0.6551 0.5840 -0.0653 0.0208  -0.0234 64  VAL H N     
10090 C CA    . VAL H 62  ? 0.6108 0.6637 0.5810 -0.0613 0.0230  -0.0278 64  VAL H CA    
10091 C C     . VAL H 62  ? 0.6033 0.6691 0.5735 -0.0646 0.0240  -0.0218 64  VAL H C     
10092 O O     . VAL H 62  ? 0.5044 0.5731 0.4811 -0.0719 0.0180  -0.0177 64  VAL H O     
10093 C CB    . VAL H 62  ? 0.6702 0.7174 0.6439 -0.0602 0.0157  -0.0362 64  VAL H CB    
10094 C CG1   . VAL H 62  ? 0.6762 0.7328 0.6454 -0.0563 0.0177  -0.0404 64  VAL H CG1   
10095 C CG2   . VAL H 62  ? 0.6863 0.7250 0.6601 -0.0553 0.0142  -0.0439 64  VAL H CG2   
10096 N N     . IML H 63  ? 0.6210 0.6957 0.5842 -0.0595 0.0304  -0.0211 65  IML H N     
10097 C CA    . IML H 63  ? 0.5830 0.6729 0.5461 -0.0607 0.0307  -0.0174 65  IML H CA    
10098 C C     . IML H 63  ? 0.5685 0.6629 0.5250 -0.0544 0.0328  -0.0218 65  IML H C     
10099 O O     . IML H 63  ? 0.5303 0.6348 0.4824 -0.0504 0.0354  -0.0202 65  IML H O     
10100 C CB    . IML H 63  ? 0.5806 0.6800 0.5423 -0.0599 0.0344  -0.0119 65  IML H CB    
10101 C CN    . IML H 63  ? 0.6589 0.7292 0.6146 -0.0529 0.0361  -0.0238 65  IML H CN    
10102 C CG2   . IML H 63  ? 0.5689 0.6863 0.5361 -0.0663 0.0317  -0.0060 65  IML H CG2   
10103 C CG1   . IML H 63  ? 0.6110 0.7004 0.5734 -0.0605 0.0359  -0.0102 65  IML H CG1   
10104 C CD1   . IML H 63  ? 0.5663 0.6612 0.5240 -0.0551 0.0406  -0.0087 65  IML H CD1   
10105 N N     . SER H 64  ? 0.6043 0.6924 0.5601 -0.0527 0.0309  -0.0277 66  SER H N     
10106 C CA    . SER H 64  ? 0.5556 0.6487 0.5049 -0.0472 0.0325  -0.0313 66  SER H CA    
10107 C C     . SER H 64  ? 0.5081 0.5985 0.4595 -0.0469 0.0284  -0.0385 66  SER H C     
10108 O O     . SER H 64  ? 0.5824 0.6646 0.5389 -0.0490 0.0248  -0.0419 66  SER H O     
10109 C CB    . SER H 64  ? 0.5542 0.6437 0.4942 -0.0413 0.0378  -0.0303 66  SER H CB    
10110 O OG    . SER H 64  ? 0.5499 0.6300 0.4894 -0.0415 0.0394  -0.0319 66  SER H OG    
10111 N N     . HIS H 65  ? 0.4737 0.5718 0.4208 -0.0432 0.0284  -0.0416 67  HIS H N     
10112 C CA    . HIS H 65  ? 0.5163 0.6156 0.4641 -0.0409 0.0249  -0.0497 67  HIS H CA    
10113 C C     . HIS H 65  ? 0.4837 0.5903 0.4214 -0.0348 0.0290  -0.0506 67  HIS H C     
10114 O O     . HIS H 65  ? 0.4950 0.6030 0.4260 -0.0327 0.0330  -0.0449 67  HIS H O     
10115 C CB    . HIS H 65  ? 0.5476 0.6504 0.5034 -0.0450 0.0173  -0.0528 67  HIS H CB    
10116 C CG    . HIS H 65  ? 0.5692 0.6838 0.5237 -0.0457 0.0181  -0.0489 67  HIS H CG    
10117 N ND1   . HIS H 65  ? 0.5941 0.7181 0.5418 -0.0399 0.0201  -0.0513 67  HIS H ND1   
10118 C CD2   . HIS H 65  ? 0.6306 0.7518 0.5896 -0.0511 0.0172  -0.0428 67  HIS H CD2   
10119 C CE1   . HIS H 65  ? 0.6232 0.7579 0.5715 -0.0411 0.0199  -0.0478 67  HIS H CE1   
10120 N NE2   . HIS H 65  ? 0.6432 0.7779 0.5985 -0.0479 0.0184  -0.0427 67  HIS H NE2   
10121 N N     . GLY H 66  ? 0.5013 0.6130 0.4380 -0.0315 0.0268  -0.0581 68  GLY H N     
10122 C CA    . GLY H 66  ? 0.4915 0.6123 0.4184 -0.0266 0.0301  -0.0582 68  GLY H CA    
10123 C C     . GLY H 66  ? 0.5190 0.6506 0.4470 -0.0237 0.0257  -0.0656 68  GLY H C     
10124 O O     . GLY H 66  ? 0.5238 0.6655 0.4455 -0.0195 0.0270  -0.0688 68  GLY H O     
10125 N N     . ASN H 67  ? 0.5321 0.6632 0.4683 -0.0268 0.0203  -0.0679 69  ASN H N     
10126 C CA    . ASN H 67  ? 0.5599 0.7007 0.4982 -0.0246 0.0151  -0.0752 69  ASN H CA    
10127 C C     . ASN H 67  ? 0.5688 0.7187 0.5010 -0.0227 0.0176  -0.0704 69  ASN H C     
10128 O O     . ASN H 67  ? 0.5908 0.7500 0.5246 -0.0213 0.0137  -0.0752 69  ASN H O     
10129 C CB    . ASN H 67  ? 0.5582 0.6932 0.5089 -0.0299 0.0062  -0.0801 69  ASN H CB    
10130 C CG    . ASN H 67  ? 0.5739 0.6983 0.5302 -0.0300 0.0016  -0.0863 69  ASN H CG    
10131 O OD1   . ASN H 67  ? 0.5757 0.6990 0.5271 -0.0266 0.0064  -0.0864 69  ASN H OD1   
10132 N ND2   . ASN H 67  ? 0.5808 0.6973 0.5474 -0.0339 -0.0087 -0.0915 69  ASN H ND2   
10133 N N     . GLY H 68  ? 0.5784 0.7253 0.5039 -0.0221 0.0231  -0.0617 70  GLY H N     
10134 C CA    . GLY H 68  ? 0.5922 0.7462 0.5109 -0.0185 0.0245  -0.0575 70  GLY H CA    
10135 C C     . GLY H 68  ? 0.6058 0.7660 0.5320 -0.0218 0.0214  -0.0571 70  GLY H C     
10136 O O     . GLY H 68  ? 0.6204 0.7888 0.5418 -0.0178 0.0219  -0.0548 70  GLY H O     
10137 N N     . SAH I .   ? 0.4767 0.4615 0.4638 -0.0282 0.0444  -0.0306 301 SAH A N     
10138 C CA    . SAH I .   ? 0.4617 0.4476 0.4462 -0.0265 0.0445  -0.0301 301 SAH A CA    
10139 C CB    . SAH I .   ? 0.4841 0.4683 0.4665 -0.0257 0.0455  -0.0297 301 SAH A CB    
10140 C CG    . SAH I .   ? 0.5053 0.4856 0.4869 -0.0262 0.0462  -0.0296 301 SAH A CG    
10141 S SD    . SAH I .   ? 0.5127 0.4913 0.4919 -0.0257 0.0474  -0.0287 301 SAH A SD    
10142 C C     . SAH I .   ? 0.4362 0.4259 0.4219 -0.0266 0.0437  -0.0298 301 SAH A C     
10143 O O     . SAH I .   ? 0.4600 0.4509 0.4483 -0.0280 0.0430  -0.0301 301 SAH A O     
10144 O OXT   . SAH I .   ? 0.4323 0.4237 0.4165 -0.0255 0.0437  -0.0293 301 SAH A OXT   
10145 C "C5'" . SAH I .   ? 0.5118 0.4893 0.4874 -0.0231 0.0470  -0.0282 301 SAH A "C5'" 
10146 C "C4'" . SAH I .   ? 0.4592 0.4395 0.4336 -0.0219 0.0470  -0.0277 301 SAH A "C4'" 
10147 O "O4'" . SAH I .   ? 0.4794 0.4638 0.4557 -0.0220 0.0461  -0.0281 301 SAH A "O4'" 
10148 C "C3'" . SAH I .   ? 0.4547 0.4340 0.4261 -0.0196 0.0468  -0.0270 301 SAH A "C3'" 
10149 O "O3'" . SAH I .   ? 0.4245 0.4005 0.3937 -0.0195 0.0475  -0.0261 301 SAH A "O3'" 
10150 C "C2'" . SAH I .   ? 0.4471 0.4310 0.4189 -0.0188 0.0463  -0.0267 301 SAH A "C2'" 
10151 O "O2'" . SAH I .   ? 0.4375 0.4222 0.4088 -0.0194 0.0466  -0.0263 301 SAH A "O2'" 
10152 C "C1'" . SAH I .   ? 0.4660 0.4527 0.4408 -0.0202 0.0457  -0.0274 301 SAH A "C1'" 
10153 N N9    . SAH I .   ? 0.4801 0.4681 0.4550 -0.0191 0.0451  -0.0276 301 SAH A N9    
10154 C C8    . SAH I .   ? 0.5151 0.5009 0.4901 -0.0192 0.0450  -0.0283 301 SAH A C8    
10155 N N7    . SAH I .   ? 0.4968 0.4846 0.4715 -0.0178 0.0446  -0.0283 301 SAH A N7    
10156 C C5    . SAH I .   ? 0.5121 0.5042 0.4868 -0.0168 0.0444  -0.0275 301 SAH A C5    
10157 C C6    . SAH I .   ? 0.5194 0.5160 0.4942 -0.0151 0.0441  -0.0269 301 SAH A C6    
10158 N N6    . SAH I .   ? 0.5068 0.5043 0.4812 -0.0140 0.0440  -0.0273 301 SAH A N6    
10159 N N1    . SAH I .   ? 0.5204 0.5210 0.4958 -0.0148 0.0438  -0.0258 301 SAH A N1    
10160 C C2    . SAH I .   ? 0.5285 0.5280 0.5039 -0.0158 0.0438  -0.0256 301 SAH A C2    
10161 N N3    . SAH I .   ? 0.5167 0.5122 0.4917 -0.0172 0.0442  -0.0262 301 SAH A N3    
10162 C C4    . SAH I .   ? 0.5088 0.5008 0.4837 -0.0176 0.0446  -0.0270 301 SAH A C4    
10163 N N     . SAH J .   ? 0.2681 0.2530 0.2509 -0.0391 0.0340  -0.0430 301 SAH C N     
10164 C CA    . SAH J .   ? 0.2756 0.2611 0.2569 -0.0377 0.0340  -0.0426 301 SAH C CA    
10165 C CB    . SAH J .   ? 0.2743 0.2591 0.2545 -0.0358 0.0330  -0.0437 301 SAH C CB    
10166 C CG    . SAH J .   ? 0.2805 0.2624 0.2612 -0.0357 0.0320  -0.0447 301 SAH C CG    
10167 S SD    . SAH J .   ? 0.2918 0.2725 0.2708 -0.0335 0.0307  -0.0463 301 SAH C SD    
10168 C C     . SAH J .   ? 0.2850 0.2731 0.2655 -0.0379 0.0349  -0.0417 301 SAH C C     
10169 O O     . SAH J .   ? 0.2819 0.2705 0.2629 -0.0393 0.0355  -0.0412 301 SAH C O     
10170 O OXT   . SAH J .   ? 0.2832 0.2727 0.2628 -0.0365 0.0349  -0.0415 301 SAH C OXT   
10171 C "C5'" . SAH J .   ? 0.2817 0.2616 0.2589 -0.0316 0.0308  -0.0460 301 SAH C "C5'" 
10172 C "C4'" . SAH J .   ? 0.2727 0.2552 0.2484 -0.0298 0.0314  -0.0456 301 SAH C "C4'" 
10173 O "O4'" . SAH J .   ? 0.2647 0.2502 0.2413 -0.0309 0.0326  -0.0442 301 SAH C "O4'" 
10174 C "C3'" . SAH J .   ? 0.2745 0.2564 0.2487 -0.0276 0.0314  -0.0456 301 SAH C "C3'" 
10175 O "O3'" . SAH J .   ? 0.2814 0.2609 0.2539 -0.0259 0.0304  -0.0471 301 SAH C "O3'" 
10176 C "C2'" . SAH J .   ? 0.2656 0.2515 0.2396 -0.0269 0.0326  -0.0447 301 SAH C "C2'" 
10177 O "O2'" . SAH J .   ? 0.2573 0.2440 0.2299 -0.0258 0.0328  -0.0453 301 SAH C "O2'" 
10178 C "C1'" . SAH J .   ? 0.2609 0.2486 0.2368 -0.0294 0.0333  -0.0436 301 SAH C "C1'" 
10179 N N9    . SAH J .   ? 0.2635 0.2520 0.2403 -0.0300 0.0335  -0.0425 301 SAH C N9    
10180 C C8    . SAH J .   ? 0.2436 0.2298 0.2210 -0.0313 0.0332  -0.0422 301 SAH C C8    
10181 N N7    . SAH J .   ? 0.2560 0.2434 0.2337 -0.0314 0.0334  -0.0412 301 SAH C N7    
10182 C C5    . SAH J .   ? 0.2487 0.2396 0.2264 -0.0303 0.0339  -0.0408 301 SAH C C5    
10183 C C6    . SAH J .   ? 0.2366 0.2307 0.2149 -0.0299 0.0342  -0.0398 301 SAH C C6    
10184 N N6    . SAH J .   ? 0.2471 0.2408 0.2255 -0.0303 0.0339  -0.0390 301 SAH C N6    
10185 N N1    . SAH J .   ? 0.2207 0.2185 0.1995 -0.0289 0.0349  -0.0397 301 SAH C N1    
10186 C C2    . SAH J .   ? 0.2094 0.2072 0.1874 -0.0283 0.0353  -0.0404 301 SAH C C2    
10187 N N3    . SAH J .   ? 0.2174 0.2122 0.1945 -0.0284 0.0350  -0.0413 301 SAH C N3    
10188 C C4    . SAH J .   ? 0.2463 0.2379 0.2234 -0.0295 0.0342  -0.0415 301 SAH C C4    
10189 N N     . SAH K .   ? 0.4298 0.4044 0.4066 -0.0421 0.0435  -0.0326 301 SAH E N     
10190 C CA    . SAH K .   ? 0.4066 0.3804 0.3825 -0.0414 0.0433  -0.0322 301 SAH E CA    
10191 C CB    . SAH K .   ? 0.4042 0.3757 0.3786 -0.0416 0.0434  -0.0320 301 SAH E CB    
10192 C CG    . SAH K .   ? 0.4291 0.3991 0.4027 -0.0425 0.0439  -0.0323 301 SAH E CG    
10193 S SD    . SAH K .   ? 0.4362 0.4033 0.4075 -0.0431 0.0441  -0.0318 301 SAH E SD    
10194 C C     . SAH K .   ? 0.4227 0.3976 0.3992 -0.0411 0.0428  -0.0316 301 SAH E C     
10195 O O     . SAH K .   ? 0.4192 0.3954 0.3966 -0.0412 0.0426  -0.0315 301 SAH E O     
10196 O OXT   . SAH K .   ? 0.3865 0.3608 0.3625 -0.0407 0.0425  -0.0312 301 SAH E OXT   
10197 C "C5'" . SAH K .   ? 0.4295 0.3943 0.3995 -0.0420 0.0431  -0.0316 301 SAH E "C5'" 
10198 C "C4'" . SAH K .   ? 0.4266 0.3910 0.3960 -0.0411 0.0425  -0.0311 301 SAH E "C4'" 
10199 O "O4'" . SAH K .   ? 0.4225 0.3897 0.3938 -0.0404 0.0423  -0.0312 301 SAH E "O4'" 
10200 C "C3'" . SAH K .   ? 0.4446 0.4067 0.4128 -0.0401 0.0415  -0.0310 301 SAH E "C3'" 
10201 O "O3'" . SAH K .   ? 0.4019 0.3604 0.3674 -0.0408 0.0412  -0.0305 301 SAH E "O3'" 
10202 C "C2'" . SAH K .   ? 0.4364 0.4001 0.4055 -0.0391 0.0409  -0.0308 301 SAH E "C2'" 
10203 O "O2'" . SAH K .   ? 0.4214 0.3838 0.3891 -0.0394 0.0407  -0.0303 301 SAH E "O2'" 
10204 C "C1'" . SAH K .   ? 0.4464 0.4136 0.4178 -0.0393 0.0415  -0.0311 301 SAH E "C1'" 
10205 N N9    . SAH K .   ? 0.5107 0.4798 0.4835 -0.0385 0.0414  -0.0316 301 SAH E N9    
10206 C C8    . SAH K .   ? 0.4839 0.4535 0.4570 -0.0386 0.0418  -0.0321 301 SAH E C8    
10207 N N7    . SAH K .   ? 0.4247 0.3964 0.3988 -0.0377 0.0417  -0.0326 301 SAH E N7    
10208 C C5    . SAH K .   ? 0.4767 0.4495 0.4515 -0.0370 0.0413  -0.0323 301 SAH E C5    
10209 C C6    . SAH K .   ? 0.4700 0.4457 0.4462 -0.0360 0.0411  -0.0326 301 SAH E C6    
10210 N N6    . SAH K .   ? 0.4445 0.4224 0.4214 -0.0355 0.0415  -0.0333 301 SAH E N6    
10211 N N1    . SAH K .   ? 0.4790 0.4555 0.4560 -0.0357 0.0406  -0.0322 301 SAH E N1    
10212 C C2    . SAH K .   ? 0.4687 0.4430 0.4448 -0.0362 0.0401  -0.0316 301 SAH E C2    
10213 N N3    . SAH K .   ? 0.4727 0.4442 0.4471 -0.0370 0.0403  -0.0313 301 SAH E N3    
10214 C C4    . SAH K .   ? 0.5077 0.4788 0.4817 -0.0375 0.0409  -0.0317 301 SAH E C4    
10215 N N     . SAH L .   ? 0.2909 0.2904 0.2891 -0.0412 0.0419  -0.0270 301 SAH G N     
10216 C CA    . SAH L .   ? 0.3025 0.3013 0.3012 -0.0406 0.0425  -0.0253 301 SAH G CA    
10217 C CB    . SAH L .   ? 0.3141 0.3104 0.3132 -0.0400 0.0430  -0.0263 301 SAH G CB    
10218 C CG    . SAH L .   ? 0.3388 0.3337 0.3395 -0.0404 0.0441  -0.0267 301 SAH G CG    
10219 S SD    . SAH L .   ? 0.3461 0.3380 0.3468 -0.0399 0.0446  -0.0284 301 SAH G SD    
10220 C C     . SAH L .   ? 0.3084 0.3083 0.3058 -0.0404 0.0417  -0.0249 301 SAH G C     
10221 O O     . SAH L .   ? 0.3164 0.3170 0.3123 -0.0408 0.0409  -0.0259 301 SAH G O     
10222 O OXT   . SAH L .   ? 0.2892 0.2893 0.2874 -0.0399 0.0420  -0.0237 301 SAH G OXT   
10223 C "C5'" . SAH L .   ? 0.3033 0.2936 0.3052 -0.0390 0.0462  -0.0260 301 SAH G "C5'" 
10224 C "C4'" . SAH L .   ? 0.2813 0.2712 0.2822 -0.0380 0.0462  -0.0256 301 SAH G "C4'" 
10225 O "O4'" . SAH L .   ? 0.2623 0.2549 0.2627 -0.0380 0.0453  -0.0244 301 SAH G "O4'" 
10226 C "C3'" . SAH L .   ? 0.2838 0.2723 0.2860 -0.0370 0.0477  -0.0239 301 SAH G "C3'" 
10227 O "O3'" . SAH L .   ? 0.3140 0.2992 0.3160 -0.0367 0.0487  -0.0254 301 SAH G "O3'" 
10228 C "C2'" . SAH L .   ? 0.2655 0.2555 0.2671 -0.0363 0.0474  -0.0231 301 SAH G "C2'" 
10229 O "O2'" . SAH L .   ? 0.2618 0.2500 0.2616 -0.0360 0.0474  -0.0248 301 SAH G "O2'" 
10230 C "C1'" . SAH L .   ? 0.2524 0.2454 0.2535 -0.0371 0.0459  -0.0229 301 SAH G "C1'" 
10231 N N9    . SAH L .   ? 0.2358 0.2314 0.2384 -0.0370 0.0458  -0.0206 301 SAH G N9    
10232 C C8    . SAH L .   ? 0.2388 0.2350 0.2418 -0.0374 0.0458  -0.0197 301 SAH G C8    
10233 N N7    . SAH L .   ? 0.2521 0.2507 0.2559 -0.0368 0.0456  -0.0176 301 SAH G N7    
10234 C C5    . SAH L .   ? 0.2359 0.2360 0.2404 -0.0363 0.0454  -0.0172 301 SAH G C5    
10235 C C6    . SAH L .   ? 0.2307 0.2342 0.2366 -0.0356 0.0449  -0.0154 301 SAH G C6    
10236 N N6    . SAH L .   ? 0.2438 0.2497 0.2502 -0.0351 0.0444  -0.0136 301 SAH G N6    
10237 N N1    . SAH L .   ? 0.2229 0.2274 0.2298 -0.0354 0.0450  -0.0157 301 SAH G N1    
10238 C C2    . SAH L .   ? 0.2122 0.2140 0.2181 -0.0356 0.0457  -0.0175 301 SAH G C2    
10239 N N3    . SAH L .   ? 0.2183 0.2167 0.2223 -0.0360 0.0460  -0.0192 301 SAH G N3    
10240 C C4    . SAH L .   ? 0.2299 0.2279 0.2336 -0.0364 0.0457  -0.0190 301 SAH G C4    
# 
