data_9UJ2
# 
_entry.id   9UJ2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9UJ2         pdb_00009uj2 10.2210/pdb9uj2/pdb 
WWPDB D_1300058532 ?            ?                   
# 
_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       2025-05-21 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9UJ2 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 kmb@inbi.ras.ru           Konstantin Boyko     M. 'principal investigator/group leader' 0000-0001-8229-189X 
3 nikolai.sluchanko@mail.ru Nikolai    Sluchanko N. 'principal investigator/group leader' 0000-0002-8608-1416 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Boyko, K.M.'     1 ? 
'Matyuta, I.O.'   2 ? 
'Minyaev, M.E.'   3 ? 
'Perfilova, K.V.' 4 ? 
'Sluchanko, N.N.' 5 ? 
# 
_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            Biochem.Biophys.Res.Commun. 
_citation.journal_id_ASTM           BBRCA9 
_citation.journal_id_CSD            0146 
_citation.journal_id_ISSN           1090-2104 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            767 
_citation.language                  ? 
_citation.page_first                151915 
_citation.page_last                 151915 
_citation.title                     
;High-resolution structure reveals enhanced 14-3-3 binding by a mutant SARS-CoV-2 nucleoprotein variant with improved replicative fitness.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bbrc.2025.151915 
_citation.pdbx_database_id_PubMed   40318379 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Perfilova, K.V.' 1 ? 
primary 'Matyuta, I.O.'   2 ? 
primary 'Minyaev, M.E.'   3 ? 
primary 'Boyko, K.M.'     4 ? 
primary 'Cooley, R.B.'    5 ? 
primary 'Sluchanko, N.N.' 6 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '14-3-3 protein zeta/delta,Peptide from Nucleoprotein' 27855.271 1   ? 
S202R,S58A,E73A,K74A,K75A,K157A,K158A,E159A ? ? 
2 polymer     man '14-3-3 protein zeta/delta,Peptide from Nucleoprotein' 27887.336 1   ? 
S202R,S58A,E73A,K74A,K75A,K157A,K158A,E159A ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                         62.068    16  ? ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                106.120   7   ? ? ? ? 
5 water       nat water                                                  18.015    437 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Protein kinase C inhibitor protein 1,KCIP-1,N,Nucleocapsid protein,NC,Protein N' 
2 'Protein kinase C inhibitor protein 1,KCIP-1,N,Nucleocapsid protein,NC,Protein N' 
# 
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 yes 
;GPHMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSAWRVVSSIEQKTEGAAAAQQ
MAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISA
AAMQPTHPIRLGLALNFSVFYYEILNSPEKA(OCY)SLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTGGGG
SRRG(TPO)SPARMAGN
;
;GPHMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSAWRVVSSIEQKTEGAAAAQQ
MAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISA
AAMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTGGGGSRRG
TSPARMAGN
;
B ? 
2 'polypeptide(L)' no yes 
;GPHMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSAWRVVSSIEQKTEGAAAAQQ
MAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISA
AAMQPTHPIRLGLALNFSVFYYEILNSPEKA(CME)SLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTGGGG
SRRG(TPO)SPARMAGN
;
;GPHMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSAWRVVSSIEQKTEGAAAAQQ
MAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISA
AAMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTGGGGSRRG
TSPARMAGN
;
A ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 1,2-ETHANEDIOL          EDO 
4 'DI(HYDROXYETHYL)ETHER' PEG 
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   PRO n 
1 3   HIS n 
1 4   MET n 
1 5   ASP n 
1 6   LYS n 
1 7   ASN n 
1 8   GLU n 
1 9   LEU n 
1 10  VAL n 
1 11  GLN n 
1 12  LYS n 
1 13  ALA n 
1 14  LYS n 
1 15  LEU n 
1 16  ALA n 
1 17  GLU n 
1 18  GLN n 
1 19  ALA n 
1 20  GLU n 
1 21  ARG n 
1 22  TYR n 
1 23  ASP n 
1 24  ASP n 
1 25  MET n 
1 26  ALA n 
1 27  ALA n 
1 28  CYS n 
1 29  MET n 
1 30  LYS n 
1 31  SER n 
1 32  VAL n 
1 33  THR n 
1 34  GLU n 
1 35  GLN n 
1 36  GLY n 
1 37  ALA n 
1 38  GLU n 
1 39  LEU n 
1 40  SER n 
1 41  ASN n 
1 42  GLU n 
1 43  GLU n 
1 44  ARG n 
1 45  ASN n 
1 46  LEU n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  ALA n 
1 51  TYR n 
1 52  LYS n 
1 53  ASN n 
1 54  VAL n 
1 55  VAL n 
1 56  GLY n 
1 57  ALA n 
1 58  ARG n 
1 59  ARG n 
1 60  SER n 
1 61  ALA n 
1 62  TRP n 
1 63  ARG n 
1 64  VAL n 
1 65  VAL n 
1 66  SER n 
1 67  SER n 
1 68  ILE n 
1 69  GLU n 
1 70  GLN n 
1 71  LYS n 
1 72  THR n 
1 73  GLU n 
1 74  GLY n 
1 75  ALA n 
1 76  ALA n 
1 77  ALA n 
1 78  ALA n 
1 79  GLN n 
1 80  GLN n 
1 81  MET n 
1 82  ALA n 
1 83  ARG n 
1 84  GLU n 
1 85  TYR n 
1 86  ARG n 
1 87  GLU n 
1 88  LYS n 
1 89  ILE n 
1 90  GLU n 
1 91  THR n 
1 92  GLU n 
1 93  LEU n 
1 94  ARG n 
1 95  ASP n 
1 96  ILE n 
1 97  CYS n 
1 98  ASN n 
1 99  ASP n 
1 100 VAL n 
1 101 LEU n 
1 102 SER n 
1 103 LEU n 
1 104 LEU n 
1 105 GLU n 
1 106 LYS n 
1 107 PHE n 
1 108 LEU n 
1 109 ILE n 
1 110 PRO n 
1 111 ASN n 
1 112 ALA n 
1 113 SER n 
1 114 GLN n 
1 115 ALA n 
1 116 GLU n 
1 117 SER n 
1 118 LYS n 
1 119 VAL n 
1 120 PHE n 
1 121 TYR n 
1 122 LEU n 
1 123 LYS n 
1 124 MET n 
1 125 LYS n 
1 126 GLY n 
1 127 ASP n 
1 128 TYR n 
1 129 TYR n 
1 130 ARG n 
1 131 TYR n 
1 132 LEU n 
1 133 ALA n 
1 134 GLU n 
1 135 VAL n 
1 136 ALA n 
1 137 ALA n 
1 138 GLY n 
1 139 ASP n 
1 140 ASP n 
1 141 LYS n 
1 142 LYS n 
1 143 GLY n 
1 144 ILE n 
1 145 VAL n 
1 146 ASP n 
1 147 GLN n 
1 148 SER n 
1 149 GLN n 
1 150 GLN n 
1 151 ALA n 
1 152 TYR n 
1 153 GLN n 
1 154 GLU n 
1 155 ALA n 
1 156 PHE n 
1 157 GLU n 
1 158 ILE n 
1 159 SER n 
1 160 ALA n 
1 161 ALA n 
1 162 ALA n 
1 163 MET n 
1 164 GLN n 
1 165 PRO n 
1 166 THR n 
1 167 HIS n 
1 168 PRO n 
1 169 ILE n 
1 170 ARG n 
1 171 LEU n 
1 172 GLY n 
1 173 LEU n 
1 174 ALA n 
1 175 LEU n 
1 176 ASN n 
1 177 PHE n 
1 178 SER n 
1 179 VAL n 
1 180 PHE n 
1 181 TYR n 
1 182 TYR n 
1 183 GLU n 
1 184 ILE n 
1 185 LEU n 
1 186 ASN n 
1 187 SER n 
1 188 PRO n 
1 189 GLU n 
1 190 LYS n 
1 191 ALA n 
1 192 OCY n 
1 193 SER n 
1 194 LEU n 
1 195 ALA n 
1 196 LYS n 
1 197 THR n 
1 198 ALA n 
1 199 PHE n 
1 200 ASP n 
1 201 GLU n 
1 202 ALA n 
1 203 ILE n 
1 204 ALA n 
1 205 GLU n 
1 206 LEU n 
1 207 ASP n 
1 208 THR n 
1 209 LEU n 
1 210 SER n 
1 211 GLU n 
1 212 GLU n 
1 213 SER n 
1 214 TYR n 
1 215 LYS n 
1 216 ASP n 
1 217 SER n 
1 218 THR n 
1 219 LEU n 
1 220 ILE n 
1 221 MET n 
1 222 GLN n 
1 223 LEU n 
1 224 LEU n 
1 225 ARG n 
1 226 ASP n 
1 227 ASN n 
1 228 LEU n 
1 229 THR n 
1 230 LEU n 
1 231 TRP n 
1 232 THR n 
1 233 GLY n 
1 234 GLY n 
1 235 GLY n 
1 236 GLY n 
1 237 SER n 
1 238 ARG n 
1 239 ARG n 
1 240 GLY n 
1 241 TPO n 
1 242 SER n 
1 243 PRO n 
1 244 ALA n 
1 245 ARG n 
1 246 MET n 
1 247 ALA n 
1 248 GLY n 
1 249 ASN n 
2 1   GLY n 
2 2   PRO n 
2 3   HIS n 
2 4   MET n 
2 5   ASP n 
2 6   LYS n 
2 7   ASN n 
2 8   GLU n 
2 9   LEU n 
2 10  VAL n 
2 11  GLN n 
2 12  LYS n 
2 13  ALA n 
2 14  LYS n 
2 15  LEU n 
2 16  ALA n 
2 17  GLU n 
2 18  GLN n 
2 19  ALA n 
2 20  GLU n 
2 21  ARG n 
2 22  TYR n 
2 23  ASP n 
2 24  ASP n 
2 25  MET n 
2 26  ALA n 
2 27  ALA n 
2 28  CYS n 
2 29  MET n 
2 30  LYS n 
2 31  SER n 
2 32  VAL n 
2 33  THR n 
2 34  GLU n 
2 35  GLN n 
2 36  GLY n 
2 37  ALA n 
2 38  GLU n 
2 39  LEU n 
2 40  SER n 
2 41  ASN n 
2 42  GLU n 
2 43  GLU n 
2 44  ARG n 
2 45  ASN n 
2 46  LEU n 
2 47  LEU n 
2 48  SER n 
2 49  VAL n 
2 50  ALA n 
2 51  TYR n 
2 52  LYS n 
2 53  ASN n 
2 54  VAL n 
2 55  VAL n 
2 56  GLY n 
2 57  ALA n 
2 58  ARG n 
2 59  ARG n 
2 60  SER n 
2 61  ALA n 
2 62  TRP n 
2 63  ARG n 
2 64  VAL n 
2 65  VAL n 
2 66  SER n 
2 67  SER n 
2 68  ILE n 
2 69  GLU n 
2 70  GLN n 
2 71  LYS n 
2 72  THR n 
2 73  GLU n 
2 74  GLY n 
2 75  ALA n 
2 76  ALA n 
2 77  ALA n 
2 78  ALA n 
2 79  GLN n 
2 80  GLN n 
2 81  MET n 
2 82  ALA n 
2 83  ARG n 
2 84  GLU n 
2 85  TYR n 
2 86  ARG n 
2 87  GLU n 
2 88  LYS n 
2 89  ILE n 
2 90  GLU n 
2 91  THR n 
2 92  GLU n 
2 93  LEU n 
2 94  ARG n 
2 95  ASP n 
2 96  ILE n 
2 97  CYS n 
2 98  ASN n 
2 99  ASP n 
2 100 VAL n 
2 101 LEU n 
2 102 SER n 
2 103 LEU n 
2 104 LEU n 
2 105 GLU n 
2 106 LYS n 
2 107 PHE n 
2 108 LEU n 
2 109 ILE n 
2 110 PRO n 
2 111 ASN n 
2 112 ALA n 
2 113 SER n 
2 114 GLN n 
2 115 ALA n 
2 116 GLU n 
2 117 SER n 
2 118 LYS n 
2 119 VAL n 
2 120 PHE n 
2 121 TYR n 
2 122 LEU n 
2 123 LYS n 
2 124 MET n 
2 125 LYS n 
2 126 GLY n 
2 127 ASP n 
2 128 TYR n 
2 129 TYR n 
2 130 ARG n 
2 131 TYR n 
2 132 LEU n 
2 133 ALA n 
2 134 GLU n 
2 135 VAL n 
2 136 ALA n 
2 137 ALA n 
2 138 GLY n 
2 139 ASP n 
2 140 ASP n 
2 141 LYS n 
2 142 LYS n 
2 143 GLY n 
2 144 ILE n 
2 145 VAL n 
2 146 ASP n 
2 147 GLN n 
2 148 SER n 
2 149 GLN n 
2 150 GLN n 
2 151 ALA n 
2 152 TYR n 
2 153 GLN n 
2 154 GLU n 
2 155 ALA n 
2 156 PHE n 
2 157 GLU n 
2 158 ILE n 
2 159 SER n 
2 160 ALA n 
2 161 ALA n 
2 162 ALA n 
2 163 MET n 
2 164 GLN n 
2 165 PRO n 
2 166 THR n 
2 167 HIS n 
2 168 PRO n 
2 169 ILE n 
2 170 ARG n 
2 171 LEU n 
2 172 GLY n 
2 173 LEU n 
2 174 ALA n 
2 175 LEU n 
2 176 ASN n 
2 177 PHE n 
2 178 SER n 
2 179 VAL n 
2 180 PHE n 
2 181 TYR n 
2 182 TYR n 
2 183 GLU n 
2 184 ILE n 
2 185 LEU n 
2 186 ASN n 
2 187 SER n 
2 188 PRO n 
2 189 GLU n 
2 190 LYS n 
2 191 ALA n 
2 192 CME n 
2 193 SER n 
2 194 LEU n 
2 195 ALA n 
2 196 LYS n 
2 197 THR n 
2 198 ALA n 
2 199 PHE n 
2 200 ASP n 
2 201 GLU n 
2 202 ALA n 
2 203 ILE n 
2 204 ALA n 
2 205 GLU n 
2 206 LEU n 
2 207 ASP n 
2 208 THR n 
2 209 LEU n 
2 210 SER n 
2 211 GLU n 
2 212 GLU n 
2 213 SER n 
2 214 TYR n 
2 215 LYS n 
2 216 ASP n 
2 217 SER n 
2 218 THR n 
2 219 LEU n 
2 220 ILE n 
2 221 MET n 
2 222 GLN n 
2 223 LEU n 
2 224 LEU n 
2 225 ARG n 
2 226 ASP n 
2 227 ASN n 
2 228 LEU n 
2 229 THR n 
2 230 LEU n 
2 231 TRP n 
2 232 THR n 
2 233 GLY n 
2 234 GLY n 
2 235 GLY n 
2 236 GLY n 
2 237 SER n 
2 238 ARG n 
2 239 ARG n 
2 240 GLY n 
2 241 TPO n 
2 242 SER n 
2 243 PRO n 
2 244 ALA n 
2 245 ARG n 
2 246 MET n 
2 247 ALA n 
2 248 GLY n 
2 249 ASN 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   232 human                ? YWHAZ ? ? ? ? ? ? 'Homo sapiens' 9606    ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 233 249 2019-nCoV,SARS-CoV-2 ? ?     ? ? ? ? ? ? 
'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   232 human                ? YWHAZ ? ? ? ? ? ? 'Homo sapiens' 9606    ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 2 sample 'Biological sequence' 233 249 2019-nCoV,SARS-CoV-2 ? ?     ? ? ? ? ? ? 
'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? 
# 
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 
CME 'L-peptide linking' n 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' ?                  'C5 H11 N O3 S2' 197.276 
CYS 'L-peptide linking' y CYSTEINE                           ?                  'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                     'ETHYLENE GLYCOL'  'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE                          ?                  'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                    ?                  'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                            ?                  'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                          ?                  'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                              ?                  'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                         ?                  'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                            ?                  'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                             ?                  'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                         ?                  'C5 H11 N O2 S'  149.211 
OCY 'L-peptide linking' n HYDROXYETHYLCYSTEINE               ?                  'C5 H11 N O3 S'  165.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'            ?                  'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE                      ?                  'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                            ?                  'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                             ?                  'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                          ?                  'C4 H9 N O3'     119.119 
TPO 'L-peptide linking' n PHOSPHOTHREONINE                   PHOSPHONOTHREONINE 'C4 H10 N O6 P'  199.099 
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  ?   ?   ?   B . n 
A 1 2   PRO 2   -1  ?   ?   ?   B . n 
A 1 3   HIS 3   0   ?   ?   ?   B . n 
A 1 4   MET 4   1   ?   ?   ?   B . n 
A 1 5   ASP 5   2   2   ASP ASP B . n 
A 1 6   LYS 6   3   3   LYS LYS B . n 
A 1 7   ASN 7   4   4   ASN ASN B . n 
A 1 8   GLU 8   5   5   GLU GLU B . n 
A 1 9   LEU 9   6   6   LEU LEU B . n 
A 1 10  VAL 10  7   7   VAL VAL B . n 
A 1 11  GLN 11  8   8   GLN GLN B . n 
A 1 12  LYS 12  9   9   LYS LYS B . n 
A 1 13  ALA 13  10  10  ALA ALA B . n 
A 1 14  LYS 14  11  11  LYS LYS B . n 
A 1 15  LEU 15  12  12  LEU LEU B . n 
A 1 16  ALA 16  13  13  ALA ALA B . n 
A 1 17  GLU 17  14  14  GLU GLU B . n 
A 1 18  GLN 18  15  15  GLN GLN B . n 
A 1 19  ALA 19  16  16  ALA ALA B . n 
A 1 20  GLU 20  17  17  GLU GLU B . n 
A 1 21  ARG 21  18  18  ARG ARG B . n 
A 1 22  TYR 22  19  19  TYR TYR B . n 
A 1 23  ASP 23  20  20  ASP ASP B . n 
A 1 24  ASP 24  21  21  ASP ASP B . n 
A 1 25  MET 25  22  22  MET MET B . n 
A 1 26  ALA 26  23  23  ALA ALA B . n 
A 1 27  ALA 27  24  24  ALA ALA B . n 
A 1 28  CYS 28  25  25  CYS CYS B . n 
A 1 29  MET 29  26  26  MET MET B . n 
A 1 30  LYS 30  27  27  LYS LYS B . n 
A 1 31  SER 31  28  28  SER SER B . n 
A 1 32  VAL 32  29  29  VAL VAL B . n 
A 1 33  THR 33  30  30  THR THR B . n 
A 1 34  GLU 34  31  31  GLU GLU B . n 
A 1 35  GLN 35  32  32  GLN GLN B . n 
A 1 36  GLY 36  33  33  GLY GLY B . n 
A 1 37  ALA 37  34  34  ALA ALA B . n 
A 1 38  GLU 38  35  35  GLU GLU B . n 
A 1 39  LEU 39  36  36  LEU LEU B . n 
A 1 40  SER 40  37  37  SER SER B . n 
A 1 41  ASN 41  38  38  ASN ASN B . n 
A 1 42  GLU 42  39  39  GLU GLU B . n 
A 1 43  GLU 43  40  40  GLU GLU B . n 
A 1 44  ARG 44  41  41  ARG ARG B . n 
A 1 45  ASN 45  42  42  ASN ASN B . n 
A 1 46  LEU 46  43  43  LEU LEU B . n 
A 1 47  LEU 47  44  44  LEU LEU B . n 
A 1 48  SER 48  45  45  SER SER B . n 
A 1 49  VAL 49  46  46  VAL VAL B . n 
A 1 50  ALA 50  47  47  ALA ALA B . n 
A 1 51  TYR 51  48  48  TYR TYR B . n 
A 1 52  LYS 52  49  49  LYS LYS B . n 
A 1 53  ASN 53  50  50  ASN ASN B . n 
A 1 54  VAL 54  51  51  VAL VAL B . n 
A 1 55  VAL 55  52  52  VAL VAL B . n 
A 1 56  GLY 56  53  53  GLY GLY B . n 
A 1 57  ALA 57  54  54  ALA ALA B . n 
A 1 58  ARG 58  55  55  ARG ARG B . n 
A 1 59  ARG 59  56  56  ARG ARG B . n 
A 1 60  SER 60  57  57  SER SER B . n 
A 1 61  ALA 61  58  58  ALA ALA B . n 
A 1 62  TRP 62  59  59  TRP TRP B . n 
A 1 63  ARG 63  60  60  ARG ARG B . n 
A 1 64  VAL 64  61  61  VAL VAL B . n 
A 1 65  VAL 65  62  62  VAL VAL B . n 
A 1 66  SER 66  63  63  SER SER B . n 
A 1 67  SER 67  64  64  SER SER B . n 
A 1 68  ILE 68  65  65  ILE ILE B . n 
A 1 69  GLU 69  66  66  GLU GLU B . n 
A 1 70  GLN 70  67  67  GLN GLN B . n 
A 1 71  LYS 71  68  68  LYS LYS B . n 
A 1 72  THR 72  69  69  THR THR B . n 
A 1 73  GLU 73  70  ?   ?   ?   B . n 
A 1 74  GLY 74  71  ?   ?   ?   B . n 
A 1 75  ALA 75  72  ?   ?   ?   B . n 
A 1 76  ALA 76  73  73  ALA ALA B . n 
A 1 77  ALA 77  74  74  ALA ALA B . n 
A 1 78  ALA 78  75  75  ALA ALA B . n 
A 1 79  GLN 79  76  76  GLN GLN B . n 
A 1 80  GLN 80  77  77  GLN GLN B . n 
A 1 81  MET 81  78  78  MET MET B . n 
A 1 82  ALA 82  79  79  ALA ALA B . n 
A 1 83  ARG 83  80  80  ARG ARG B . n 
A 1 84  GLU 84  81  81  GLU GLU B . n 
A 1 85  TYR 85  82  82  TYR TYR B . n 
A 1 86  ARG 86  83  83  ARG ARG B . n 
A 1 87  GLU 87  84  84  GLU GLU B . n 
A 1 88  LYS 88  85  85  LYS LYS B . n 
A 1 89  ILE 89  86  86  ILE ILE B . n 
A 1 90  GLU 90  87  87  GLU GLU B . n 
A 1 91  THR 91  88  88  THR THR B . n 
A 1 92  GLU 92  89  89  GLU GLU B . n 
A 1 93  LEU 93  90  90  LEU LEU B . n 
A 1 94  ARG 94  91  91  ARG ARG B . n 
A 1 95  ASP 95  92  92  ASP ASP B . n 
A 1 96  ILE 96  93  93  ILE ILE B . n 
A 1 97  CYS 97  94  94  CYS CYS B . n 
A 1 98  ASN 98  95  95  ASN ASN B . n 
A 1 99  ASP 99  96  96  ASP ASP B . n 
A 1 100 VAL 100 97  97  VAL VAL B . n 
A 1 101 LEU 101 98  98  LEU LEU B . n 
A 1 102 SER 102 99  99  SER SER B . n 
A 1 103 LEU 103 100 100 LEU LEU B . n 
A 1 104 LEU 104 101 101 LEU LEU B . n 
A 1 105 GLU 105 102 102 GLU GLU B . n 
A 1 106 LYS 106 103 103 LYS LYS B . n 
A 1 107 PHE 107 104 104 PHE PHE B . n 
A 1 108 LEU 108 105 105 LEU LEU B . n 
A 1 109 ILE 109 106 106 ILE ILE B . n 
A 1 110 PRO 110 107 107 PRO PRO B . n 
A 1 111 ASN 111 108 108 ASN ASN B . n 
A 1 112 ALA 112 109 109 ALA ALA B . n 
A 1 113 SER 113 110 110 SER SER B . n 
A 1 114 GLN 114 111 111 GLN GLN B . n 
A 1 115 ALA 115 112 112 ALA ALA B . n 
A 1 116 GLU 116 113 113 GLU GLU B . n 
A 1 117 SER 117 114 114 SER SER B . n 
A 1 118 LYS 118 115 115 LYS LYS B . n 
A 1 119 VAL 119 116 116 VAL VAL B . n 
A 1 120 PHE 120 117 117 PHE PHE B . n 
A 1 121 TYR 121 118 118 TYR TYR B . n 
A 1 122 LEU 122 119 119 LEU LEU B . n 
A 1 123 LYS 123 120 120 LYS LYS B . n 
A 1 124 MET 124 121 121 MET MET B . n 
A 1 125 LYS 125 122 122 LYS LYS B . n 
A 1 126 GLY 126 123 123 GLY GLY B . n 
A 1 127 ASP 127 124 124 ASP ASP B . n 
A 1 128 TYR 128 125 125 TYR TYR B . n 
A 1 129 TYR 129 126 126 TYR TYR B . n 
A 1 130 ARG 130 127 127 ARG ARG B . n 
A 1 131 TYR 131 128 128 TYR TYR B . n 
A 1 132 LEU 132 129 129 LEU LEU B . n 
A 1 133 ALA 133 130 130 ALA ALA B . n 
A 1 134 GLU 134 131 131 GLU GLU B . n 
A 1 135 VAL 135 132 132 VAL VAL B . n 
A 1 136 ALA 136 133 133 ALA ALA B . n 
A 1 137 ALA 137 134 134 ALA ALA B . n 
A 1 138 GLY 138 135 135 GLY GLY B . n 
A 1 139 ASP 139 136 136 ASP ASP B . n 
A 1 140 ASP 140 137 137 ASP ASP B . n 
A 1 141 LYS 141 138 138 LYS LYS B . n 
A 1 142 LYS 142 139 139 LYS LYS B . n 
A 1 143 GLY 143 140 140 GLY GLY B . n 
A 1 144 ILE 144 141 141 ILE ILE B . n 
A 1 145 VAL 145 142 142 VAL VAL B . n 
A 1 146 ASP 146 143 143 ASP ASP B . n 
A 1 147 GLN 147 144 144 GLN GLN B . n 
A 1 148 SER 148 145 145 SER SER B . n 
A 1 149 GLN 149 146 146 GLN GLN B . n 
A 1 150 GLN 150 147 147 GLN GLN B . n 
A 1 151 ALA 151 148 148 ALA ALA B . n 
A 1 152 TYR 152 149 149 TYR TYR B . n 
A 1 153 GLN 153 150 150 GLN GLN B . n 
A 1 154 GLU 154 151 151 GLU GLU B . n 
A 1 155 ALA 155 152 152 ALA ALA B . n 
A 1 156 PHE 156 153 153 PHE PHE B . n 
A 1 157 GLU 157 154 154 GLU GLU B . n 
A 1 158 ILE 158 155 155 ILE ILE B . n 
A 1 159 SER 159 156 156 SER SER B . n 
A 1 160 ALA 160 157 157 ALA ALA B . n 
A 1 161 ALA 161 158 158 ALA ALA B . n 
A 1 162 ALA 162 159 159 ALA ALA B . n 
A 1 163 MET 163 160 160 MET MET B . n 
A 1 164 GLN 164 161 161 GLN GLN B . n 
A 1 165 PRO 165 162 162 PRO PRO B . n 
A 1 166 THR 166 163 163 THR THR B . n 
A 1 167 HIS 167 164 164 HIS HIS B . n 
A 1 168 PRO 168 165 165 PRO PRO B . n 
A 1 169 ILE 169 166 166 ILE ILE B . n 
A 1 170 ARG 170 167 167 ARG ARG B . n 
A 1 171 LEU 171 168 168 LEU LEU B . n 
A 1 172 GLY 172 169 169 GLY GLY B . n 
A 1 173 LEU 173 170 170 LEU LEU B . n 
A 1 174 ALA 174 171 171 ALA ALA B . n 
A 1 175 LEU 175 172 172 LEU LEU B . n 
A 1 176 ASN 176 173 173 ASN ASN B . n 
A 1 177 PHE 177 174 174 PHE PHE B . n 
A 1 178 SER 178 175 175 SER SER B . n 
A 1 179 VAL 179 176 176 VAL VAL B . n 
A 1 180 PHE 180 177 177 PHE PHE B . n 
A 1 181 TYR 181 178 178 TYR TYR B . n 
A 1 182 TYR 182 179 179 TYR TYR B . n 
A 1 183 GLU 183 180 180 GLU GLU B . n 
A 1 184 ILE 184 181 181 ILE ILE B . n 
A 1 185 LEU 185 182 182 LEU LEU B . n 
A 1 186 ASN 186 183 183 ASN ASN B . n 
A 1 187 SER 187 184 184 SER SER B . n 
A 1 188 PRO 188 185 185 PRO PRO B . n 
A 1 189 GLU 189 186 186 GLU GLU B . n 
A 1 190 LYS 190 187 187 LYS LYS B . n 
A 1 191 ALA 191 188 188 ALA ALA B . n 
A 1 192 OCY 192 189 189 OCY OCY B . n 
A 1 193 SER 193 190 190 SER SER B . n 
A 1 194 LEU 194 191 191 LEU LEU B . n 
A 1 195 ALA 195 192 192 ALA ALA B . n 
A 1 196 LYS 196 193 193 LYS LYS B . n 
A 1 197 THR 197 194 194 THR THR B . n 
A 1 198 ALA 198 195 195 ALA ALA B . n 
A 1 199 PHE 199 196 196 PHE PHE B . n 
A 1 200 ASP 200 197 197 ASP ASP B . n 
A 1 201 GLU 201 198 198 GLU GLU B . n 
A 1 202 ALA 202 199 199 ALA ALA B . n 
A 1 203 ILE 203 200 200 ILE ILE B . n 
A 1 204 ALA 204 201 201 ALA ALA B . n 
A 1 205 GLU 205 202 202 GLU GLU B . n 
A 1 206 LEU 206 203 203 LEU LEU B . n 
A 1 207 ASP 207 204 204 ASP ASP B . n 
A 1 208 THR 208 205 205 THR THR B . n 
A 1 209 LEU 209 206 206 LEU LEU B . n 
A 1 210 SER 210 207 207 SER SER B . n 
A 1 211 GLU 211 208 208 GLU GLU B . n 
A 1 212 GLU 212 209 209 GLU GLU B . n 
A 1 213 SER 213 210 210 SER SER B . n 
A 1 214 TYR 214 211 211 TYR TYR B . n 
A 1 215 LYS 215 212 212 LYS LYS B . n 
A 1 216 ASP 216 213 213 ASP ASP B . n 
A 1 217 SER 217 214 214 SER SER B . n 
A 1 218 THR 218 215 215 THR THR B . n 
A 1 219 LEU 219 216 216 LEU LEU B . n 
A 1 220 ILE 220 217 217 ILE ILE B . n 
A 1 221 MET 221 218 218 MET MET B . n 
A 1 222 GLN 222 219 219 GLN GLN B . n 
A 1 223 LEU 223 220 220 LEU LEU B . n 
A 1 224 LEU 224 221 221 LEU LEU B . n 
A 1 225 ARG 225 222 222 ARG ARG B . n 
A 1 226 ASP 226 223 223 ASP ASP B . n 
A 1 227 ASN 227 224 224 ASN ASN B . n 
A 1 228 LEU 228 225 225 LEU LEU B . n 
A 1 229 THR 229 226 226 THR THR B . n 
A 1 230 LEU 230 227 227 LEU LEU B . n 
A 1 231 TRP 231 228 228 TRP TRP B . n 
A 1 232 THR 232 229 229 THR THR B . n 
A 1 233 GLY 233 230 230 GLY GLY B . n 
A 1 234 GLY 234 231 231 GLY GLY B . n 
A 1 235 GLY 235 232 232 GLY GLY B . n 
A 1 236 GLY 236 233 233 GLY GLY B . n 
A 1 237 SER 237 234 234 SER SER B . n 
A 1 238 ARG 238 235 235 ARG ARG B . n 
A 1 239 ARG 239 236 236 ARG ARG B . n 
A 1 240 GLY 240 237 237 GLY GLY B . n 
A 1 241 TPO 241 238 238 TPO TPO B . n 
A 1 242 SER 242 239 239 SER SER B . n 
A 1 243 PRO 243 240 240 PRO PRO B . n 
A 1 244 ALA 244 241 241 ALA ALA B . n 
A 1 245 ARG 245 242 242 ARG ARG B . n 
A 1 246 MET 246 243 243 MET MET B . n 
A 1 247 ALA 247 244 244 ALA ALA B . n 
A 1 248 GLY 248 245 245 GLY GLY B . n 
A 1 249 ASN 249 246 246 ASN ASN B . n 
B 2 1   GLY 1   -2  ?   ?   ?   A . n 
B 2 2   PRO 2   -1  ?   ?   ?   A . n 
B 2 3   HIS 3   0   ?   ?   ?   A . n 
B 2 4   MET 4   1   ?   ?   ?   A . n 
B 2 5   ASP 5   2   2   ASP ASP A . n 
B 2 6   LYS 6   3   3   LYS LYS A . n 
B 2 7   ASN 7   4   4   ASN ASN A . n 
B 2 8   GLU 8   5   5   GLU GLU A . n 
B 2 9   LEU 9   6   6   LEU LEU A . n 
B 2 10  VAL 10  7   7   VAL VAL A . n 
B 2 11  GLN 11  8   8   GLN GLN A . n 
B 2 12  LYS 12  9   9   LYS LYS A . n 
B 2 13  ALA 13  10  10  ALA ALA A . n 
B 2 14  LYS 14  11  11  LYS LYS A . n 
B 2 15  LEU 15  12  12  LEU LEU A . n 
B 2 16  ALA 16  13  13  ALA ALA A . n 
B 2 17  GLU 17  14  14  GLU GLU A . n 
B 2 18  GLN 18  15  15  GLN GLN A . n 
B 2 19  ALA 19  16  16  ALA ALA A . n 
B 2 20  GLU 20  17  17  GLU GLU A . n 
B 2 21  ARG 21  18  18  ARG ARG A . n 
B 2 22  TYR 22  19  19  TYR TYR A . n 
B 2 23  ASP 23  20  20  ASP ASP A . n 
B 2 24  ASP 24  21  21  ASP ASP A . n 
B 2 25  MET 25  22  22  MET MET A . n 
B 2 26  ALA 26  23  23  ALA ALA A . n 
B 2 27  ALA 27  24  24  ALA ALA A . n 
B 2 28  CYS 28  25  25  CYS CYS A . n 
B 2 29  MET 29  26  26  MET MET A . n 
B 2 30  LYS 30  27  27  LYS LYS A . n 
B 2 31  SER 31  28  28  SER SER A . n 
B 2 32  VAL 32  29  29  VAL VAL A . n 
B 2 33  THR 33  30  30  THR THR A . n 
B 2 34  GLU 34  31  31  GLU GLU A . n 
B 2 35  GLN 35  32  32  GLN GLN A . n 
B 2 36  GLY 36  33  33  GLY GLY A . n 
B 2 37  ALA 37  34  34  ALA ALA A . n 
B 2 38  GLU 38  35  35  GLU GLU A . n 
B 2 39  LEU 39  36  36  LEU LEU A . n 
B 2 40  SER 40  37  37  SER SER A . n 
B 2 41  ASN 41  38  38  ASN ASN A . n 
B 2 42  GLU 42  39  39  GLU GLU A . n 
B 2 43  GLU 43  40  40  GLU GLU A . n 
B 2 44  ARG 44  41  41  ARG ARG A . n 
B 2 45  ASN 45  42  42  ASN ASN A . n 
B 2 46  LEU 46  43  43  LEU LEU A . n 
B 2 47  LEU 47  44  44  LEU LEU A . n 
B 2 48  SER 48  45  45  SER SER A . n 
B 2 49  VAL 49  46  46  VAL VAL A . n 
B 2 50  ALA 50  47  47  ALA ALA A . n 
B 2 51  TYR 51  48  48  TYR TYR A . n 
B 2 52  LYS 52  49  49  LYS LYS A . n 
B 2 53  ASN 53  50  50  ASN ASN A . n 
B 2 54  VAL 54  51  51  VAL VAL A . n 
B 2 55  VAL 55  52  52  VAL VAL A . n 
B 2 56  GLY 56  53  53  GLY GLY A . n 
B 2 57  ALA 57  54  54  ALA ALA A . n 
B 2 58  ARG 58  55  55  ARG ARG A . n 
B 2 59  ARG 59  56  56  ARG ARG A . n 
B 2 60  SER 60  57  57  SER SER A . n 
B 2 61  ALA 61  58  58  ALA ALA A . n 
B 2 62  TRP 62  59  59  TRP TRP A . n 
B 2 63  ARG 63  60  60  ARG ARG A . n 
B 2 64  VAL 64  61  61  VAL VAL A . n 
B 2 65  VAL 65  62  62  VAL VAL A . n 
B 2 66  SER 66  63  63  SER SER A . n 
B 2 67  SER 67  64  64  SER SER A . n 
B 2 68  ILE 68  65  65  ILE ILE A . n 
B 2 69  GLU 69  66  66  GLU GLU A . n 
B 2 70  GLN 70  67  67  GLN GLN A . n 
B 2 71  LYS 71  68  ?   ?   ?   A . n 
B 2 72  THR 72  69  ?   ?   ?   A . n 
B 2 73  GLU 73  70  ?   ?   ?   A . n 
B 2 74  GLY 74  71  ?   ?   ?   A . n 
B 2 75  ALA 75  72  72  ALA ALA A . n 
B 2 76  ALA 76  73  73  ALA ALA A . n 
B 2 77  ALA 77  74  74  ALA ALA A . n 
B 2 78  ALA 78  75  75  ALA ALA A . n 
B 2 79  GLN 79  76  76  GLN GLN A . n 
B 2 80  GLN 80  77  77  GLN GLN A . n 
B 2 81  MET 81  78  78  MET MET A . n 
B 2 82  ALA 82  79  79  ALA ALA A . n 
B 2 83  ARG 83  80  80  ARG ARG A . n 
B 2 84  GLU 84  81  81  GLU GLU A . n 
B 2 85  TYR 85  82  82  TYR TYR A . n 
B 2 86  ARG 86  83  83  ARG ARG A . n 
B 2 87  GLU 87  84  84  GLU GLU A . n 
B 2 88  LYS 88  85  85  LYS LYS A . n 
B 2 89  ILE 89  86  86  ILE ILE A . n 
B 2 90  GLU 90  87  87  GLU GLU A . n 
B 2 91  THR 91  88  88  THR THR A . n 
B 2 92  GLU 92  89  89  GLU GLU A . n 
B 2 93  LEU 93  90  90  LEU LEU A . n 
B 2 94  ARG 94  91  91  ARG ARG A . n 
B 2 95  ASP 95  92  92  ASP ASP A . n 
B 2 96  ILE 96  93  93  ILE ILE A . n 
B 2 97  CYS 97  94  94  CYS CYS A . n 
B 2 98  ASN 98  95  95  ASN ASN A . n 
B 2 99  ASP 99  96  96  ASP ASP A . n 
B 2 100 VAL 100 97  97  VAL VAL A . n 
B 2 101 LEU 101 98  98  LEU LEU A . n 
B 2 102 SER 102 99  99  SER SER A . n 
B 2 103 LEU 103 100 100 LEU LEU A . n 
B 2 104 LEU 104 101 101 LEU LEU A . n 
B 2 105 GLU 105 102 102 GLU GLU A . n 
B 2 106 LYS 106 103 103 LYS LYS A . n 
B 2 107 PHE 107 104 104 PHE PHE A . n 
B 2 108 LEU 108 105 105 LEU LEU A . n 
B 2 109 ILE 109 106 106 ILE ILE A . n 
B 2 110 PRO 110 107 107 PRO PRO A . n 
B 2 111 ASN 111 108 108 ASN ASN A . n 
B 2 112 ALA 112 109 109 ALA ALA A . n 
B 2 113 SER 113 110 110 SER SER A . n 
B 2 114 GLN 114 111 111 GLN GLN A . n 
B 2 115 ALA 115 112 112 ALA ALA A . n 
B 2 116 GLU 116 113 113 GLU GLU A . n 
B 2 117 SER 117 114 114 SER SER A . n 
B 2 118 LYS 118 115 115 LYS LYS A . n 
B 2 119 VAL 119 116 116 VAL VAL A . n 
B 2 120 PHE 120 117 117 PHE PHE A . n 
B 2 121 TYR 121 118 118 TYR TYR A . n 
B 2 122 LEU 122 119 119 LEU LEU A . n 
B 2 123 LYS 123 120 120 LYS LYS A . n 
B 2 124 MET 124 121 121 MET MET A . n 
B 2 125 LYS 125 122 122 LYS LYS A . n 
B 2 126 GLY 126 123 123 GLY GLY A . n 
B 2 127 ASP 127 124 124 ASP ASP A . n 
B 2 128 TYR 128 125 125 TYR TYR A . n 
B 2 129 TYR 129 126 126 TYR TYR A . n 
B 2 130 ARG 130 127 127 ARG ARG A . n 
B 2 131 TYR 131 128 128 TYR TYR A . n 
B 2 132 LEU 132 129 129 LEU LEU A . n 
B 2 133 ALA 133 130 130 ALA ALA A . n 
B 2 134 GLU 134 131 131 GLU GLU A . n 
B 2 135 VAL 135 132 132 VAL VAL A . n 
B 2 136 ALA 136 133 133 ALA ALA A . n 
B 2 137 ALA 137 134 134 ALA ALA A . n 
B 2 138 GLY 138 135 135 GLY GLY A . n 
B 2 139 ASP 139 136 136 ASP ASP A . n 
B 2 140 ASP 140 137 137 ASP ASP A . n 
B 2 141 LYS 141 138 138 LYS LYS A . n 
B 2 142 LYS 142 139 139 LYS LYS A . n 
B 2 143 GLY 143 140 140 GLY GLY A . n 
B 2 144 ILE 144 141 141 ILE ILE A . n 
B 2 145 VAL 145 142 142 VAL VAL A . n 
B 2 146 ASP 146 143 143 ASP ASP A . n 
B 2 147 GLN 147 144 144 GLN GLN A . n 
B 2 148 SER 148 145 145 SER SER A . n 
B 2 149 GLN 149 146 146 GLN GLN A . n 
B 2 150 GLN 150 147 147 GLN GLN A . n 
B 2 151 ALA 151 148 148 ALA ALA A . n 
B 2 152 TYR 152 149 149 TYR TYR A . n 
B 2 153 GLN 153 150 150 GLN GLN A . n 
B 2 154 GLU 154 151 151 GLU GLU A . n 
B 2 155 ALA 155 152 152 ALA ALA A . n 
B 2 156 PHE 156 153 153 PHE PHE A . n 
B 2 157 GLU 157 154 154 GLU GLU A . n 
B 2 158 ILE 158 155 155 ILE ILE A . n 
B 2 159 SER 159 156 156 SER SER A . n 
B 2 160 ALA 160 157 157 ALA ALA A . n 
B 2 161 ALA 161 158 158 ALA ALA A . n 
B 2 162 ALA 162 159 159 ALA ALA A . n 
B 2 163 MET 163 160 160 MET MET A . n 
B 2 164 GLN 164 161 161 GLN GLN A . n 
B 2 165 PRO 165 162 162 PRO PRO A . n 
B 2 166 THR 166 163 163 THR THR A . n 
B 2 167 HIS 167 164 164 HIS HIS A . n 
B 2 168 PRO 168 165 165 PRO PRO A . n 
B 2 169 ILE 169 166 166 ILE ILE A . n 
B 2 170 ARG 170 167 167 ARG ARG A . n 
B 2 171 LEU 171 168 168 LEU LEU A . n 
B 2 172 GLY 172 169 169 GLY GLY A . n 
B 2 173 LEU 173 170 170 LEU LEU A . n 
B 2 174 ALA 174 171 171 ALA ALA A . n 
B 2 175 LEU 175 172 172 LEU LEU A . n 
B 2 176 ASN 176 173 173 ASN ASN A . n 
B 2 177 PHE 177 174 174 PHE PHE A . n 
B 2 178 SER 178 175 175 SER SER A . n 
B 2 179 VAL 179 176 176 VAL VAL A . n 
B 2 180 PHE 180 177 177 PHE PHE A . n 
B 2 181 TYR 181 178 178 TYR TYR A . n 
B 2 182 TYR 182 179 179 TYR TYR A . n 
B 2 183 GLU 183 180 180 GLU GLU A . n 
B 2 184 ILE 184 181 181 ILE ILE A . n 
B 2 185 LEU 185 182 182 LEU LEU A . n 
B 2 186 ASN 186 183 183 ASN ASN A . n 
B 2 187 SER 187 184 184 SER SER A . n 
B 2 188 PRO 188 185 185 PRO PRO A . n 
B 2 189 GLU 189 186 186 GLU GLU A . n 
B 2 190 LYS 190 187 187 LYS LYS A . n 
B 2 191 ALA 191 188 188 ALA ALA A . n 
B 2 192 CME 192 189 189 CME CYS A . n 
B 2 193 SER 193 190 190 SER SER A . n 
B 2 194 LEU 194 191 191 LEU LEU A . n 
B 2 195 ALA 195 192 192 ALA ALA A . n 
B 2 196 LYS 196 193 193 LYS LYS A . n 
B 2 197 THR 197 194 194 THR THR A . n 
B 2 198 ALA 198 195 195 ALA ALA A . n 
B 2 199 PHE 199 196 196 PHE PHE A . n 
B 2 200 ASP 200 197 197 ASP ASP A . n 
B 2 201 GLU 201 198 198 GLU GLU A . n 
B 2 202 ALA 202 199 199 ALA ALA A . n 
B 2 203 ILE 203 200 200 ILE ILE A . n 
B 2 204 ALA 204 201 201 ALA ALA A . n 
B 2 205 GLU 205 202 202 GLU GLU A . n 
B 2 206 LEU 206 203 203 LEU LEU A . n 
B 2 207 ASP 207 204 204 ASP ASP A . n 
B 2 208 THR 208 205 205 THR THR A . n 
B 2 209 LEU 209 206 206 LEU LEU A . n 
B 2 210 SER 210 207 207 SER SER A . n 
B 2 211 GLU 211 208 208 GLU GLU A . n 
B 2 212 GLU 212 209 209 GLU GLU A . n 
B 2 213 SER 213 210 210 SER SER A . n 
B 2 214 TYR 214 211 211 TYR TYR A . n 
B 2 215 LYS 215 212 212 LYS LYS A . n 
B 2 216 ASP 216 213 213 ASP ASP A . n 
B 2 217 SER 217 214 214 SER SER A . n 
B 2 218 THR 218 215 215 THR THR A . n 
B 2 219 LEU 219 216 216 LEU LEU A . n 
B 2 220 ILE 220 217 217 ILE ILE A . n 
B 2 221 MET 221 218 218 MET MET A . n 
B 2 222 GLN 222 219 219 GLN GLN A . n 
B 2 223 LEU 223 220 220 LEU LEU A . n 
B 2 224 LEU 224 221 221 LEU LEU A . n 
B 2 225 ARG 225 222 222 ARG ARG A . n 
B 2 226 ASP 226 223 223 ASP ASP A . n 
B 2 227 ASN 227 224 224 ASN ASN A . n 
B 2 228 LEU 228 225 225 LEU LEU A . n 
B 2 229 THR 229 226 226 THR THR A . n 
B 2 230 LEU 230 227 227 LEU LEU A . n 
B 2 231 TRP 231 228 228 TRP TRP A . n 
B 2 232 THR 232 229 229 THR THR A . n 
B 2 233 GLY 233 230 230 GLY GLY A . n 
B 2 234 GLY 234 231 231 GLY GLY A . n 
B 2 235 GLY 235 232 232 GLY GLY A . n 
B 2 236 GLY 236 233 233 GLY GLY A . n 
B 2 237 SER 237 234 234 SER SER A . n 
B 2 238 ARG 238 235 235 ARG ARG A . n 
B 2 239 ARG 239 236 236 ARG ARG A . n 
B 2 240 GLY 240 237 237 GLY GLY A . n 
B 2 241 TPO 241 238 238 TPO TPO A . n 
B 2 242 SER 242 239 239 SER SER A . n 
B 2 243 PRO 243 240 240 PRO PRO A . n 
B 2 244 ALA 244 241 241 ALA ALA A . n 
B 2 245 ARG 245 242 242 ARG ARG A . n 
B 2 246 MET 246 243 243 MET MET A . n 
B 2 247 ALA 247 244 244 ALA ALA A . n 
B 2 248 GLY 248 245 245 GLY GLY A . n 
B 2 249 ASN 249 246 246 ASN ASN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        TPO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TPO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  3 EDO 1   301 299 EDO EDO B . 
D  3 EDO 1   302 300 EDO EDO B . 
E  3 EDO 1   303 304 EDO EDO B . 
F  3 EDO 1   304 307 EDO EDO B . 
G  3 EDO 1   305 308 EDO EDO B . 
H  3 EDO 1   306 309 EDO EDO B . 
I  4 PEG 1   307 315 PEG PEG B . 
J  3 EDO 1   308 316 EDO EDO B . 
K  3 EDO 1   301 299 EDO EDO A . 
L  3 EDO 1   302 303 EDO EDO A . 
M  3 EDO 1   303 305 EDO EDO A . 
N  3 EDO 1   304 306 EDO EDO A . 
O  3 EDO 1   305 308 EDO EDO A . 
P  4 PEG 1   306 309 PEG PEG A . 
Q  3 EDO 1   307 310 EDO EDO A . 
R  4 PEG 1   308 315 PEG PEG A . 
S  4 PEG 1   309 317 PEG PEG A . 
T  3 EDO 1   310 318 EDO EDO A . 
U  3 EDO 1   311 319 EDO EDO A . 
V  4 PEG 1   312 321 PEG PEG A . 
W  4 PEG 1   313 322 PEG PEG A . 
X  3 EDO 1   314 323 EDO EDO A . 
Y  4 PEG 1   315 324 PEG PEG A . 
Z  5 HOH 1   401 521 HOH HOH B . 
Z  5 HOH 2   402 299 HOH HOH B . 
Z  5 HOH 3   403 408 HOH HOH B . 
Z  5 HOH 4   404 334 HOH HOH B . 
Z  5 HOH 5   405 269 HOH HOH B . 
Z  5 HOH 6   406 192 HOH HOH B . 
Z  5 HOH 7   407 362 HOH HOH B . 
Z  5 HOH 8   408 286 HOH HOH B . 
Z  5 HOH 9   409 451 HOH HOH B . 
Z  5 HOH 10  410 16  HOH HOH B . 
Z  5 HOH 11  411 336 HOH HOH B . 
Z  5 HOH 12  412 112 HOH HOH B . 
Z  5 HOH 13  413 431 HOH HOH B . 
Z  5 HOH 14  414 418 HOH HOH B . 
Z  5 HOH 15  415 95  HOH HOH B . 
Z  5 HOH 16  416 143 HOH HOH B . 
Z  5 HOH 17  417 524 HOH HOH B . 
Z  5 HOH 18  418 309 HOH HOH B . 
Z  5 HOH 19  419 46  HOH HOH B . 
Z  5 HOH 20  420 227 HOH HOH B . 
Z  5 HOH 21  421 156 HOH HOH B . 
Z  5 HOH 22  422 444 HOH HOH B . 
Z  5 HOH 23  423 148 HOH HOH B . 
Z  5 HOH 24  424 512 HOH HOH B . 
Z  5 HOH 25  425 233 HOH HOH B . 
Z  5 HOH 26  426 504 HOH HOH B . 
Z  5 HOH 27  427 470 HOH HOH B . 
Z  5 HOH 28  428 304 HOH HOH B . 
Z  5 HOH 29  429 410 HOH HOH B . 
Z  5 HOH 30  430 289 HOH HOH B . 
Z  5 HOH 31  431 357 HOH HOH B . 
Z  5 HOH 32  432 457 HOH HOH B . 
Z  5 HOH 33  433 359 HOH HOH B . 
Z  5 HOH 34  434 298 HOH HOH B . 
Z  5 HOH 35  435 181 HOH HOH B . 
Z  5 HOH 36  436 152 HOH HOH B . 
Z  5 HOH 37  437 363 HOH HOH B . 
Z  5 HOH 38  438 400 HOH HOH B . 
Z  5 HOH 39  439 171 HOH HOH B . 
Z  5 HOH 40  440 422 HOH HOH B . 
Z  5 HOH 41  441 324 HOH HOH B . 
Z  5 HOH 42  442 213 HOH HOH B . 
Z  5 HOH 43  443 169 HOH HOH B . 
Z  5 HOH 44  444 323 HOH HOH B . 
Z  5 HOH 45  445 209 HOH HOH B . 
Z  5 HOH 46  446 128 HOH HOH B . 
Z  5 HOH 47  447 83  HOH HOH B . 
Z  5 HOH 48  448 374 HOH HOH B . 
Z  5 HOH 49  449 305 HOH HOH B . 
Z  5 HOH 50  450 133 HOH HOH B . 
Z  5 HOH 51  451 42  HOH HOH B . 
Z  5 HOH 52  452 123 HOH HOH B . 
Z  5 HOH 53  453 94  HOH HOH B . 
Z  5 HOH 54  454 335 HOH HOH B . 
Z  5 HOH 55  455 449 HOH HOH B . 
Z  5 HOH 56  456 24  HOH HOH B . 
Z  5 HOH 57  457 292 HOH HOH B . 
Z  5 HOH 58  458 183 HOH HOH B . 
Z  5 HOH 59  459 174 HOH HOH B . 
Z  5 HOH 60  460 188 HOH HOH B . 
Z  5 HOH 61  461 40  HOH HOH B . 
Z  5 HOH 62  462 483 HOH HOH B . 
Z  5 HOH 63  463 464 HOH HOH B . 
Z  5 HOH 64  464 137 HOH HOH B . 
Z  5 HOH 65  465 312 HOH HOH B . 
Z  5 HOH 66  466 217 HOH HOH B . 
Z  5 HOH 67  467 173 HOH HOH B . 
Z  5 HOH 68  468 237 HOH HOH B . 
Z  5 HOH 69  469 248 HOH HOH B . 
Z  5 HOH 70  470 232 HOH HOH B . 
Z  5 HOH 71  471 56  HOH HOH B . 
Z  5 HOH 72  472 474 HOH HOH B . 
Z  5 HOH 73  473 337 HOH HOH B . 
Z  5 HOH 74  474 440 HOH HOH B . 
Z  5 HOH 75  475 517 HOH HOH B . 
Z  5 HOH 76  476 407 HOH HOH B . 
Z  5 HOH 77  477 36  HOH HOH B . 
Z  5 HOH 78  478 462 HOH HOH B . 
Z  5 HOH 79  479 124 HOH HOH B . 
Z  5 HOH 80  480 520 HOH HOH B . 
Z  5 HOH 81  481 11  HOH HOH B . 
Z  5 HOH 82  482 241 HOH HOH B . 
Z  5 HOH 83  483 39  HOH HOH B . 
Z  5 HOH 84  484 297 HOH HOH B . 
Z  5 HOH 85  485 438 HOH HOH B . 
Z  5 HOH 86  486 179 HOH HOH B . 
Z  5 HOH 87  487 268 HOH HOH B . 
Z  5 HOH 88  488 53  HOH HOH B . 
Z  5 HOH 89  489 74  HOH HOH B . 
Z  5 HOH 90  490 409 HOH HOH B . 
Z  5 HOH 91  491 358 HOH HOH B . 
Z  5 HOH 92  492 114 HOH HOH B . 
Z  5 HOH 93  493 20  HOH HOH B . 
Z  5 HOH 94  494 446 HOH HOH B . 
Z  5 HOH 95  495 207 HOH HOH B . 
Z  5 HOH 96  496 505 HOH HOH B . 
Z  5 HOH 97  497 421 HOH HOH B . 
Z  5 HOH 98  498 13  HOH HOH B . 
Z  5 HOH 99  499 81  HOH HOH B . 
Z  5 HOH 100 500 151 HOH HOH B . 
Z  5 HOH 101 501 308 HOH HOH B . 
Z  5 HOH 102 502 6   HOH HOH B . 
Z  5 HOH 103 503 85  HOH HOH B . 
Z  5 HOH 104 504 146 HOH HOH B . 
Z  5 HOH 105 505 78  HOH HOH B . 
Z  5 HOH 106 506 89  HOH HOH B . 
Z  5 HOH 107 507 238 HOH HOH B . 
Z  5 HOH 108 508 477 HOH HOH B . 
Z  5 HOH 109 509 63  HOH HOH B . 
Z  5 HOH 110 510 452 HOH HOH B . 
Z  5 HOH 111 511 43  HOH HOH B . 
Z  5 HOH 112 512 315 HOH HOH B . 
Z  5 HOH 113 513 99  HOH HOH B . 
Z  5 HOH 114 514 487 HOH HOH B . 
Z  5 HOH 115 515 433 HOH HOH B . 
Z  5 HOH 116 516 356 HOH HOH B . 
Z  5 HOH 117 517 259 HOH HOH B . 
Z  5 HOH 118 518 54  HOH HOH B . 
Z  5 HOH 119 519 9   HOH HOH B . 
Z  5 HOH 120 520 224 HOH HOH B . 
Z  5 HOH 121 521 177 HOH HOH B . 
Z  5 HOH 122 522 27  HOH HOH B . 
Z  5 HOH 123 523 184 HOH HOH B . 
Z  5 HOH 124 524 65  HOH HOH B . 
Z  5 HOH 125 525 468 HOH HOH B . 
Z  5 HOH 126 526 120 HOH HOH B . 
Z  5 HOH 127 527 117 HOH HOH B . 
Z  5 HOH 128 528 50  HOH HOH B . 
Z  5 HOH 129 529 481 HOH HOH B . 
Z  5 HOH 130 530 69  HOH HOH B . 
Z  5 HOH 131 531 423 HOH HOH B . 
Z  5 HOH 132 532 523 HOH HOH B . 
Z  5 HOH 133 533 253 HOH HOH B . 
Z  5 HOH 134 534 160 HOH HOH B . 
Z  5 HOH 135 535 306 HOH HOH B . 
Z  5 HOH 136 536 113 HOH HOH B . 
Z  5 HOH 137 537 10  HOH HOH B . 
Z  5 HOH 138 538 379 HOH HOH B . 
Z  5 HOH 139 539 239 HOH HOH B . 
Z  5 HOH 140 540 317 HOH HOH B . 
Z  5 HOH 141 541 204 HOH HOH B . 
Z  5 HOH 142 542 340 HOH HOH B . 
Z  5 HOH 143 543 267 HOH HOH B . 
Z  5 HOH 144 544 12  HOH HOH B . 
Z  5 HOH 145 545 316 HOH HOH B . 
Z  5 HOH 146 546 391 HOH HOH B . 
Z  5 HOH 147 547 424 HOH HOH B . 
Z  5 HOH 148 548 73  HOH HOH B . 
Z  5 HOH 149 549 377 HOH HOH B . 
Z  5 HOH 150 550 77  HOH HOH B . 
Z  5 HOH 151 551 373 HOH HOH B . 
Z  5 HOH 152 552 60  HOH HOH B . 
Z  5 HOH 153 553 510 HOH HOH B . 
Z  5 HOH 154 554 450 HOH HOH B . 
Z  5 HOH 155 555 488 HOH HOH B . 
Z  5 HOH 156 556 55  HOH HOH B . 
Z  5 HOH 157 557 25  HOH HOH B . 
Z  5 HOH 158 558 270 HOH HOH B . 
Z  5 HOH 159 559 176 HOH HOH B . 
Z  5 HOH 160 560 121 HOH HOH B . 
Z  5 HOH 161 561 522 HOH HOH B . 
Z  5 HOH 162 562 106 HOH HOH B . 
Z  5 HOH 163 563 70  HOH HOH B . 
Z  5 HOH 164 564 508 HOH HOH B . 
Z  5 HOH 165 565 220 HOH HOH B . 
Z  5 HOH 166 566 282 HOH HOH B . 
Z  5 HOH 167 567 295 HOH HOH B . 
Z  5 HOH 168 568 347 HOH HOH B . 
Z  5 HOH 169 569 436 HOH HOH B . 
Z  5 HOH 170 570 245 HOH HOH B . 
Z  5 HOH 171 571 441 HOH HOH B . 
Z  5 HOH 172 572 355 HOH HOH B . 
Z  5 HOH 173 573 372 HOH HOH B . 
Z  5 HOH 174 574 390 HOH HOH B . 
Z  5 HOH 175 575 102 HOH HOH B . 
Z  5 HOH 176 576 478 HOH HOH B . 
Z  5 HOH 177 577 353 HOH HOH B . 
Z  5 HOH 178 578 469 HOH HOH B . 
Z  5 HOH 179 579 294 HOH HOH B . 
Z  5 HOH 180 580 458 HOH HOH B . 
Z  5 HOH 181 581 420 HOH HOH B . 
Z  5 HOH 182 582 189 HOH HOH B . 
Z  5 HOH 183 583 285 HOH HOH B . 
Z  5 HOH 184 584 384 HOH HOH B . 
Z  5 HOH 185 585 439 HOH HOH B . 
Z  5 HOH 186 586 479 HOH HOH B . 
Z  5 HOH 187 587 389 HOH HOH B . 
Z  5 HOH 188 588 482 HOH HOH B . 
Z  5 HOH 189 589 437 HOH HOH B . 
Z  5 HOH 190 590 163 HOH HOH B . 
Z  5 HOH 191 591 518 HOH HOH B . 
Z  5 HOH 192 592 142 HOH HOH B . 
Z  5 HOH 193 593 157 HOH HOH B . 
Z  5 HOH 194 594 319 HOH HOH B . 
Z  5 HOH 195 595 489 HOH HOH B . 
Z  5 HOH 196 596 443 HOH HOH B . 
Z  5 HOH 197 597 166 HOH HOH B . 
Z  5 HOH 198 598 493 HOH HOH B . 
Z  5 HOH 199 599 109 HOH HOH B . 
Z  5 HOH 200 600 51  HOH HOH B . 
Z  5 HOH 201 601 283 HOH HOH B . 
Z  5 HOH 202 602 311 HOH HOH B . 
Z  5 HOH 203 603 339 HOH HOH B . 
Z  5 HOH 204 604 338 HOH HOH B . 
Z  5 HOH 205 605 129 HOH HOH B . 
Z  5 HOH 206 606 385 HOH HOH B . 
Z  5 HOH 207 607 442 HOH HOH B . 
Z  5 HOH 208 608 264 HOH HOH B . 
Z  5 HOH 209 609 221 HOH HOH B . 
Z  5 HOH 210 610 492 HOH HOH B . 
Z  5 HOH 211 611 490 HOH HOH B . 
Z  5 HOH 212 612 348 HOH HOH B . 
Z  5 HOH 213 613 108 HOH HOH B . 
Z  5 HOH 214 614 383 HOH HOH B . 
Z  5 HOH 215 615 322 HOH HOH B . 
Z  5 HOH 216 616 480 HOH HOH B . 
Z  5 HOH 217 617 273 HOH HOH B . 
Z  5 HOH 218 618 476 HOH HOH B . 
Z  5 HOH 219 619 392 HOH HOH B . 
Z  5 HOH 220 620 405 HOH HOH B . 
Z  5 HOH 221 621 502 HOH HOH B . 
Z  5 HOH 222 622 97  HOH HOH B . 
Z  5 HOH 223 623 202 HOH HOH B . 
Z  5 HOH 224 624 516 HOH HOH B . 
Z  5 HOH 225 625 272 HOH HOH B . 
AA 5 HOH 1   401 525 HOH HOH A . 
AA 5 HOH 2   402 193 HOH HOH A . 
AA 5 HOH 3   403 456 HOH HOH A . 
AA 5 HOH 4   404 280 HOH HOH A . 
AA 5 HOH 5   405 201 HOH HOH A . 
AA 5 HOH 6   406 495 HOH HOH A . 
AA 5 HOH 7   407 381 HOH HOH A . 
AA 5 HOH 8   408 255 HOH HOH A . 
AA 5 HOH 9   409 155 HOH HOH A . 
AA 5 HOH 10  410 500 HOH HOH A . 
AA 5 HOH 11  411 342 HOH HOH A . 
AA 5 HOH 12  412 126 HOH HOH A . 
AA 5 HOH 13  413 28  HOH HOH A . 
AA 5 HOH 14  414 131 HOH HOH A . 
AA 5 HOH 15  415 361 HOH HOH A . 
AA 5 HOH 16  416 84  HOH HOH A . 
AA 5 HOH 17  417 513 HOH HOH A . 
AA 5 HOH 18  418 380 HOH HOH A . 
AA 5 HOH 19  419 64  HOH HOH A . 
AA 5 HOH 20  420 329 HOH HOH A . 
AA 5 HOH 21  421 194 HOH HOH A . 
AA 5 HOH 22  422 225 HOH HOH A . 
AA 5 HOH 23  423 509 HOH HOH A . 
AA 5 HOH 24  424 82  HOH HOH A . 
AA 5 HOH 25  425 350 HOH HOH A . 
AA 5 HOH 26  426 291 HOH HOH A . 
AA 5 HOH 27  427 266 HOH HOH A . 
AA 5 HOH 28  428 242 HOH HOH A . 
AA 5 HOH 29  429 175 HOH HOH A . 
AA 5 HOH 30  430 172 HOH HOH A . 
AA 5 HOH 31  431 118 HOH HOH A . 
AA 5 HOH 32  432 230 HOH HOH A . 
AA 5 HOH 33  433 328 HOH HOH A . 
AA 5 HOH 34  434 191 HOH HOH A . 
AA 5 HOH 35  435 158 HOH HOH A . 
AA 5 HOH 36  436 290 HOH HOH A . 
AA 5 HOH 37  437 367 HOH HOH A . 
AA 5 HOH 38  438 86  HOH HOH A . 
AA 5 HOH 39  439 246 HOH HOH A . 
AA 5 HOH 40  440 251 HOH HOH A . 
AA 5 HOH 41  441 62  HOH HOH A . 
AA 5 HOH 42  442 190 HOH HOH A . 
AA 5 HOH 43  443 370 HOH HOH A . 
AA 5 HOH 44  444 139 HOH HOH A . 
AA 5 HOH 45  445 149 HOH HOH A . 
AA 5 HOH 46  446 29  HOH HOH A . 
AA 5 HOH 47  447 178 HOH HOH A . 
AA 5 HOH 48  448 313 HOH HOH A . 
AA 5 HOH 49  449 314 HOH HOH A . 
AA 5 HOH 50  450 96  HOH HOH A . 
AA 5 HOH 51  451 250 HOH HOH A . 
AA 5 HOH 52  452 411 HOH HOH A . 
AA 5 HOH 53  453 75  HOH HOH A . 
AA 5 HOH 54  454 34  HOH HOH A . 
AA 5 HOH 55  455 130 HOH HOH A . 
AA 5 HOH 56  456 71  HOH HOH A . 
AA 5 HOH 57  457 135 HOH HOH A . 
AA 5 HOH 58  458 256 HOH HOH A . 
AA 5 HOH 59  459 122 HOH HOH A . 
AA 5 HOH 60  460 67  HOH HOH A . 
AA 5 HOH 61  461 7   HOH HOH A . 
AA 5 HOH 62  462 254 HOH HOH A . 
AA 5 HOH 63  463 226 HOH HOH A . 
AA 5 HOH 64  464 45  HOH HOH A . 
AA 5 HOH 65  465 349 HOH HOH A . 
AA 5 HOH 66  466 21  HOH HOH A . 
AA 5 HOH 67  467 68  HOH HOH A . 
AA 5 HOH 68  468 212 HOH HOH A . 
AA 5 HOH 69  469 5   HOH HOH A . 
AA 5 HOH 70  470 132 HOH HOH A . 
AA 5 HOH 71  471 471 HOH HOH A . 
AA 5 HOH 72  472 310 HOH HOH A . 
AA 5 HOH 73  473 138 HOH HOH A . 
AA 5 HOH 74  474 199 HOH HOH A . 
AA 5 HOH 75  475 203 HOH HOH A . 
AA 5 HOH 76  476 14  HOH HOH A . 
AA 5 HOH 77  477 145 HOH HOH A . 
AA 5 HOH 78  478 382 HOH HOH A . 
AA 5 HOH 79  479 413 HOH HOH A . 
AA 5 HOH 80  480 414 HOH HOH A . 
AA 5 HOH 81  481 330 HOH HOH A . 
AA 5 HOH 82  482 369 HOH HOH A . 
AA 5 HOH 83  483 210 HOH HOH A . 
AA 5 HOH 84  484 284 HOH HOH A . 
AA 5 HOH 85  485 187 HOH HOH A . 
AA 5 HOH 86  486 136 HOH HOH A . 
AA 5 HOH 87  487 22  HOH HOH A . 
AA 5 HOH 88  488 244 HOH HOH A . 
AA 5 HOH 89  489 499 HOH HOH A . 
AA 5 HOH 90  490 515 HOH HOH A . 
AA 5 HOH 91  491 485 HOH HOH A . 
AA 5 HOH 92  492 38  HOH HOH A . 
AA 5 HOH 93  493 105 HOH HOH A . 
AA 5 HOH 94  494 296 HOH HOH A . 
AA 5 HOH 95  495 57  HOH HOH A . 
AA 5 HOH 96  496 211 HOH HOH A . 
AA 5 HOH 97  497 514 HOH HOH A . 
AA 5 HOH 98  498 327 HOH HOH A . 
AA 5 HOH 99  499 387 HOH HOH A . 
AA 5 HOH 100 500 368 HOH HOH A . 
AA 5 HOH 101 501 115 HOH HOH A . 
AA 5 HOH 102 502 406 HOH HOH A . 
AA 5 HOH 103 503 154 HOH HOH A . 
AA 5 HOH 104 504 196 HOH HOH A . 
AA 5 HOH 105 505 47  HOH HOH A . 
AA 5 HOH 106 506 395 HOH HOH A . 
AA 5 HOH 107 507 398 HOH HOH A . 
AA 5 HOH 108 508 111 HOH HOH A . 
AA 5 HOH 109 509 125 HOH HOH A . 
AA 5 HOH 110 510 79  HOH HOH A . 
AA 5 HOH 111 511 222 HOH HOH A . 
AA 5 HOH 112 512 396 HOH HOH A . 
AA 5 HOH 113 513 31  HOH HOH A . 
AA 5 HOH 114 514 165 HOH HOH A . 
AA 5 HOH 115 515 497 HOH HOH A . 
AA 5 HOH 116 516 261 HOH HOH A . 
AA 5 HOH 117 517 58  HOH HOH A . 
AA 5 HOH 118 518 507 HOH HOH A . 
AA 5 HOH 119 519 49  HOH HOH A . 
AA 5 HOH 120 520 352 HOH HOH A . 
AA 5 HOH 121 521 455 HOH HOH A . 
AA 5 HOH 122 522 473 HOH HOH A . 
AA 5 HOH 123 523 247 HOH HOH A . 
AA 5 HOH 124 524 271 HOH HOH A . 
AA 5 HOH 125 525 307 HOH HOH A . 
AA 5 HOH 126 526 498 HOH HOH A . 
AA 5 HOH 127 527 80  HOH HOH A . 
AA 5 HOH 128 528 402 HOH HOH A . 
AA 5 HOH 129 529 491 HOH HOH A . 
AA 5 HOH 130 530 61  HOH HOH A . 
AA 5 HOH 131 531 277 HOH HOH A . 
AA 5 HOH 132 532 107 HOH HOH A . 
AA 5 HOH 133 533 331 HOH HOH A . 
AA 5 HOH 134 534 41  HOH HOH A . 
AA 5 HOH 135 535 92  HOH HOH A . 
AA 5 HOH 136 536 98  HOH HOH A . 
AA 5 HOH 137 537 432 HOH HOH A . 
AA 5 HOH 138 538 231 HOH HOH A . 
AA 5 HOH 139 539 141 HOH HOH A . 
AA 5 HOH 140 540 293 HOH HOH A . 
AA 5 HOH 141 541 228 HOH HOH A . 
AA 5 HOH 142 542 426 HOH HOH A . 
AA 5 HOH 143 543 197 HOH HOH A . 
AA 5 HOH 144 544 200 HOH HOH A . 
AA 5 HOH 145 545 104 HOH HOH A . 
AA 5 HOH 146 546 412 HOH HOH A . 
AA 5 HOH 147 547 278 HOH HOH A . 
AA 5 HOH 148 548 17  HOH HOH A . 
AA 5 HOH 149 549 219 HOH HOH A . 
AA 5 HOH 150 550 404 HOH HOH A . 
AA 5 HOH 151 551 365 HOH HOH A . 
AA 5 HOH 152 552 87  HOH HOH A . 
AA 5 HOH 153 553 415 HOH HOH A . 
AA 5 HOH 154 554 275 HOH HOH A . 
AA 5 HOH 155 555 475 HOH HOH A . 
AA 5 HOH 156 556 318 HOH HOH A . 
AA 5 HOH 157 557 260 HOH HOH A . 
AA 5 HOH 158 558 506 HOH HOH A . 
AA 5 HOH 159 559 198 HOH HOH A . 
AA 5 HOH 160 560 366 HOH HOH A . 
AA 5 HOH 161 561 116 HOH HOH A . 
AA 5 HOH 162 562 288 HOH HOH A . 
AA 5 HOH 163 563 430 HOH HOH A . 
AA 5 HOH 164 564 234 HOH HOH A . 
AA 5 HOH 165 565 527 HOH HOH A . 
AA 5 HOH 166 566 281 HOH HOH A . 
AA 5 HOH 167 567 263 HOH HOH A . 
AA 5 HOH 168 568 302 HOH HOH A . 
AA 5 HOH 169 569 300 HOH HOH A . 
AA 5 HOH 170 570 526 HOH HOH A . 
AA 5 HOH 171 571 378 HOH HOH A . 
AA 5 HOH 172 572 344 HOH HOH A . 
AA 5 HOH 173 573 101 HOH HOH A . 
AA 5 HOH 174 574 343 HOH HOH A . 
AA 5 HOH 175 575 386 HOH HOH A . 
AA 5 HOH 176 576 167 HOH HOH A . 
AA 5 HOH 177 577 360 HOH HOH A . 
AA 5 HOH 178 578 371 HOH HOH A . 
AA 5 HOH 179 579 159 HOH HOH A . 
AA 5 HOH 180 580 484 HOH HOH A . 
AA 5 HOH 181 581 472 HOH HOH A . 
AA 5 HOH 182 582 301 HOH HOH A . 
AA 5 HOH 183 583 276 HOH HOH A . 
AA 5 HOH 184 584 351 HOH HOH A . 
AA 5 HOH 185 585 76  HOH HOH A . 
AA 5 HOH 186 586 448 HOH HOH A . 
AA 5 HOH 187 587 496 HOH HOH A . 
AA 5 HOH 188 588 466 HOH HOH A . 
AA 5 HOH 189 589 134 HOH HOH A . 
AA 5 HOH 190 590 459 HOH HOH A . 
AA 5 HOH 191 591 240 HOH HOH A . 
AA 5 HOH 192 592 144 HOH HOH A . 
AA 5 HOH 193 593 321 HOH HOH A . 
AA 5 HOH 194 594 162 HOH HOH A . 
AA 5 HOH 195 595 345 HOH HOH A . 
AA 5 HOH 196 596 44  HOH HOH A . 
AA 5 HOH 197 597 519 HOH HOH A . 
AA 5 HOH 198 598 235 HOH HOH A . 
AA 5 HOH 199 599 59  HOH HOH A . 
AA 5 HOH 200 600 320 HOH HOH A . 
AA 5 HOH 201 601 435 HOH HOH A . 
AA 5 HOH 202 602 486 HOH HOH A . 
AA 5 HOH 203 603 467 HOH HOH A . 
AA 5 HOH 204 604 341 HOH HOH A . 
AA 5 HOH 205 605 223 HOH HOH A . 
AA 5 HOH 206 606 346 HOH HOH A . 
AA 5 HOH 207 607 434 HOH HOH A . 
AA 5 HOH 208 608 88  HOH HOH A . 
AA 5 HOH 209 609 501 HOH HOH A . 
AA 5 HOH 210 610 428 HOH HOH A . 
AA 5 HOH 211 611 429 HOH HOH A . 
AA 5 HOH 212 612 447 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B ASP 136 ? CG  ? A ASP 139 CG  
2 1 Y 1 B ASP 136 ? OD1 ? A ASP 139 OD1 
3 1 Y 1 B ASP 136 ? OD2 ? A ASP 139 OD2 
4 1 Y 1 A ASP 136 ? CG  ? B ASP 139 CG  
5 1 Y 1 A ASP 136 ? OD1 ? B ASP 139 OD1 
6 1 Y 1 A ASP 136 ? OD2 ? B ASP 139 OD2 
7 1 Y 1 A ASN 246 ? CG  ? B ASN 249 CG  
8 1 Y 1 A ASN 246 ? OD1 ? B ASN 249 OD1 
9 1 Y 1 A ASN 246 ? ND2 ? B ASN 249 ND2 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0430 ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        ? 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        ? 3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .        ? 4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .        ? 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9UJ2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.555 
_cell.length_a_esd                 ? 
_cell.length_b                     84.452 
_cell.length_b_esd                 ? 
_cell.length_c                     139.873 
_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                         9UJ2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9UJ2 
_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             3.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.71 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.8M Ammonium sulfate, 0.1M BIS-TRIS pH 6.5, 2% v/v Polyethylene glycol monomethyl ether 550' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            288 
# 
_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                         'RIGAKU HyPix-6000HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-15 
_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   1.54184 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        RIGAKU 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54184 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9UJ2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               21.76 
_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                                     67049 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.96 
_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                                0.111 
_reflns.pdbx_Rpim_I_all                                0.035 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       676288 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.106 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           23631 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3849 
_reflns_shell.percent_possible_obs                          97.2 
_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                               6.1 
_reflns_shell.pdbx_chi_squared                              0.91 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.1 
_reflns_shell.pdbx_Rrim_I_all                               0.935 
_reflns_shell.pdbx_Rpim_I_all                               0.367 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.725 
_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                                  0.857 
_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]                            -0.76 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            2.17 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.41 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.992 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.953 
_refine.correlation_coeff_Fo_to_Fc_free          0.933 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9UJ2 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             21.76 
_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                     63642 
_refine.ls_number_reflns_R_free                  3233 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.42 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19667 
_refine.ls_R_factor_R_free                       0.23302 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19484 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                       0.111 
_refine.pdbx_overall_ESU_R_Free                  0.113 
_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                             6.073 
_refine.overall_SU_ML                            0.094 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        21.76 
_refine_hist.number_atoms_solvent             437 
_refine_hist.number_atoms_total               4335 
_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        3781 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         117 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  0.012  4054 ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.016  3911 ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 2.079  1.846  5428 ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.952  1.767  9028 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 5.968  5.000  513  ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 11.672 5.000  29   ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 14.775 10.000 735  ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.116  0.200  589  ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  4794 ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  914  ? 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' ? 1.437  1.276  1989 ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 1.436  1.277  1990 ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 2.162  2.290  2499 ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 2.162  2.291  2500 ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 2.437  1.577  2065 ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 2.437  1.577  2066 ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 3.696  2.724  2922 ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 5.882  15.28  4707 ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 5.766  14.07  4566 ? r_long_range_B_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          1.800 
_refine_ls_shell.d_res_low                           1.846 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                226 
_refine_ls_shell.number_reflns_R_work                4530 
_refine_ls_shell.percent_reflns_obs                  97.26 
_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                     0.295 
_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.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      20 
_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                     0.337 
# 
_struct.entry_id                     9UJ2 
_struct.title                        '14-3-3 zeta chimera with the S202R peptide of SARS-CoV-2 N (residues 200-213)' 
_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        9UJ2 
_struct_keywords.text            'phosphopeptide, coronavirus, chimera, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 3 ? 
D  N N 3 ? 
E  N N 3 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 4 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 4 ? 
Q  N N 3 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 5 ? 
AA 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 1433Z_HUMAN P63104 ? 1 
;MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAR
EYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEM
QPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWT
;
1   
2 UNP NCAP_SARS2  P0DTC9 ? 1 GSSRGTSPARMAGN 200 
3 UNP 1433Z_HUMAN P63104 ? 2 
;MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAR
EYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEM
QPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWT
;
1   
4 UNP NCAP_SARS2  P0DTC9 ? 2 GSSRGTSPARMAGN 200 
# 
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 9UJ2 B 4   ? 232 ? P63104 1   ? 229 ? 1   229 
2 2 9UJ2 B 236 ? 249 ? P0DTC9 200 ? 213 ? 233 246 
3 3 9UJ2 A 4   ? 232 ? P63104 1   ? 229 ? 1   229 
4 4 9UJ2 A 236 ? 249 ? P0DTC9 200 ? 213 ? 233 246 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9UJ2 GLY B 1   ? UNP P63104 ?   ?   'expression tag'      -2  1  
1 9UJ2 PRO B 2   ? UNP P63104 ?   ?   'expression tag'      -1  2  
1 9UJ2 HIS B 3   ? UNP P63104 ?   ?   'expression tag'      0   3  
1 9UJ2 ALA B 61  ? UNP P63104 SER 58  'engineered mutation' 58  4  
1 9UJ2 ALA B 76  ? UNP P63104 GLU 73  'engineered mutation' 73  5  
1 9UJ2 ALA B 77  ? UNP P63104 LYS 74  'engineered mutation' 74  6  
1 9UJ2 ALA B 78  ? UNP P63104 LYS 75  'engineered mutation' 75  7  
1 9UJ2 ALA B 160 ? UNP P63104 LYS 157 'engineered mutation' 157 8  
1 9UJ2 ALA B 161 ? UNP P63104 LYS 158 'engineered mutation' 158 9  
1 9UJ2 ALA B 162 ? UNP P63104 GLU 159 'engineered mutation' 159 10 
1 9UJ2 GLY B 233 ? UNP P63104 ?   ?   linker                230 11 
1 9UJ2 GLY B 234 ? UNP P63104 ?   ?   linker                231 12 
1 9UJ2 GLY B 235 ? UNP P63104 ?   ?   linker                232 13 
2 9UJ2 ARG B 238 ? UNP P0DTC9 SER 202 'engineered mutation' 235 14 
3 9UJ2 GLY A 1   ? UNP P63104 ?   ?   'expression tag'      -2  15 
3 9UJ2 PRO A 2   ? UNP P63104 ?   ?   'expression tag'      -1  16 
3 9UJ2 HIS A 3   ? UNP P63104 ?   ?   'expression tag'      0   17 
3 9UJ2 ALA A 61  ? UNP P63104 SER 58  'engineered mutation' 58  18 
3 9UJ2 ALA A 76  ? UNP P63104 GLU 73  'engineered mutation' 73  19 
3 9UJ2 ALA A 77  ? UNP P63104 LYS 74  'engineered mutation' 74  20 
3 9UJ2 ALA A 78  ? UNP P63104 LYS 75  'engineered mutation' 75  21 
3 9UJ2 ALA A 160 ? UNP P63104 LYS 157 'engineered mutation' 157 22 
3 9UJ2 ALA A 161 ? UNP P63104 LYS 158 'engineered mutation' 158 23 
3 9UJ2 ALA A 162 ? UNP P63104 GLU 159 'engineered mutation' 159 24 
3 9UJ2 GLY A 233 ? UNP P63104 ?   ?   linker                230 25 
3 9UJ2 GLY A 234 ? UNP P63104 ?   ?   linker                231 26 
3 9UJ2 GLY A 235 ? UNP P63104 ?   ?   linker                232 27 
4 9UJ2 ARG A 238 ? UNP P0DTC9 SER 202 'engineered mutation' 235 28 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5850  ? 
1 MORE         36    ? 
1 'SSA (A^2)'  22800 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 5   ? GLU A 20  ? ASP B 2   GLU B 17  1 ? 16 
HELX_P HELX_P2  AA2 ARG A 21  ? GLN A 35  ? ARG B 18  GLN B 32  1 ? 15 
HELX_P HELX_P3  AA3 SER A 40  ? THR A 72  ? SER B 37  THR B 69  1 ? 33 
HELX_P HELX_P4  AA4 ALA A 77  ? PHE A 107 ? ALA B 74  PHE B 104 1 ? 31 
HELX_P HELX_P5  AA5 PHE A 107 ? ALA A 112 ? PHE B 104 ALA B 109 1 ? 6  
HELX_P HELX_P6  AA6 GLN A 114 ? GLU A 134 ? GLN B 111 GLU B 131 1 ? 21 
HELX_P HELX_P7  AA7 ALA A 137 ? MET A 163 ? ALA B 134 MET B 160 1 ? 27 
HELX_P HELX_P8  AA8 HIS A 167 ? ILE A 184 ? HIS B 164 ILE B 181 1 ? 18 
HELX_P HELX_P9  AA9 SER A 187 ? GLU A 205 ? SER B 184 GLU B 202 1 ? 19 
HELX_P HELX_P10 AB1 LEU A 206 ? LEU A 209 ? LEU B 203 LEU B 206 5 ? 4  
HELX_P HELX_P11 AB2 SER A 213 ? THR A 232 ? SER B 210 THR B 229 1 ? 20 
HELX_P HELX_P12 AB3 LYS B 6   ? ALA B 19  ? LYS A 3   ALA A 16  1 ? 14 
HELX_P HELX_P13 AB4 ARG B 21  ? GLN B 35  ? ARG A 18  GLN A 32  1 ? 15 
HELX_P HELX_P14 AB5 SER B 40  ? GLN B 70  ? SER A 37  GLN A 67  1 ? 31 
HELX_P HELX_P15 AB6 ALA B 76  ? PHE B 107 ? ALA A 73  PHE A 104 1 ? 32 
HELX_P HELX_P16 AB7 PHE B 107 ? ALA B 112 ? PHE A 104 ALA A 109 1 ? 6  
HELX_P HELX_P17 AB8 GLN B 114 ? GLU B 134 ? GLN A 111 GLU A 131 1 ? 21 
HELX_P HELX_P18 AB9 GLY B 138 ? MET B 163 ? GLY A 135 MET A 160 1 ? 26 
HELX_P HELX_P19 AC1 HIS B 167 ? ILE B 184 ? HIS A 164 ILE A 181 1 ? 18 
HELX_P HELX_P20 AC2 SER B 187 ? ALA B 204 ? SER A 184 ALA A 201 1 ? 18 
HELX_P HELX_P21 AC3 GLU B 205 ? LEU B 209 ? GLU A 202 LEU A 206 5 ? 5  
HELX_P HELX_P22 AC4 SER B 210 ? GLY B 234 ? SER A 207 GLY A 231 1 ? 25 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A ALA 191 C ? ? ? 1_555 A OCY 192 N ? ? B ALA 188 B OCY 189 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale2 covale both ? A OCY 192 C ? ? ? 1_555 A SER 193 N ? ? B OCY 189 B SER 190 1_555 ? ? ? ? ? ? ? 1.349 ? ? 
covale3 covale both ? A GLY 240 C ? ? ? 1_555 A TPO 241 N ? ? B GLY 237 B TPO 238 1_555 ? ? ? ? ? ? ? 1.354 ? ? 
covale4 covale both ? A TPO 241 C ? ? ? 1_555 A SER 242 N ? ? B TPO 238 B SER 239 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale5 covale both ? B ALA 191 C ? ? ? 1_555 B CME 192 N ? ? A ALA 188 A CME 189 1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale6 covale both ? B CME 192 C ? ? ? 1_555 B SER 193 N A ? A CME 189 A SER 190 1_555 ? ? ? ? ? ? ? 1.344 ? ? 
covale7 covale both ? B CME 192 C ? ? ? 1_555 B SER 193 N B ? A CME 189 A SER 190 1_555 ? ? ? ? ? ? ? 1.351 ? ? 
covale8 covale both ? B GLY 240 C ? ? ? 1_555 B TPO 241 N ? ? A GLY 237 A TPO 238 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale9 covale both ? B TPO 241 C ? ? ? 1_555 B SER 242 N ? ? A TPO 238 A SER 239 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
# 
_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 OCY A 192 ? . . . . OCY B 189 ? 1_555 . . . . . . . CYS 1 OCY Hydroxyethylation    'Named protein modification' 
2 TPO A 241 ? . . . . TPO B 238 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation      'Named protein modification' 
3 CME B 192 ? . . . . CME A 189 ? 1_555 . . . . . . . CYS 1 CME Beta-mercaptoethanol 'Named protein modification' 
4 TPO B 241 ? . . . . TPO A 238 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation      'Named protein modification' 
# 
_pdbx_entry_details.entry_id                   9UJ2 
_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 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             102 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             102 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.320 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            0.068 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 NE B ARG 18  ? ? CZ B ARG 18  ? ? NH2 B ARG 18  ? ? 117.15 120.30 -3.15  0.50 N 
2  1 NE B ARG 55  ? ? CZ B ARG 55  ? ? NH1 B ARG 55  ? ? 123.75 120.30 3.45   0.50 N 
3  1 NE B ARG 60  ? ? CZ B ARG 60  ? ? NH1 B ARG 60  ? ? 123.86 120.30 3.56   0.50 N 
4  1 NE B ARG 83  ? ? CZ B ARG 83  ? ? NH1 B ARG 83  ? ? 124.18 120.30 3.88   0.50 N 
5  1 CG B MET 121 ? B SD B MET 121 ? B CE  B MET 121 ? B 89.24  100.20 -10.96 1.60 N 
6  1 NE B ARG 222 ? ? CZ B ARG 222 ? ? NH2 B ARG 222 ? ? 117.17 120.30 -3.13  0.50 N 
7  1 NE A ARG 56  ? ? CZ A ARG 56  ? ? NH2 A ARG 56  ? ? 116.83 120.30 -3.47  0.50 N 
8  1 CD A ARG 80  ? ? NE A ARG 80  ? ? CZ  A ARG 80  ? ? 132.87 123.60 9.27   1.40 N 
9  1 CD A ARG 83  ? ? NE A ARG 83  ? ? CZ  A ARG 83  ? ? 133.29 123.60 9.69   1.40 N 
10 1 NE A ARG 83  ? ? CZ A ARG 83  ? ? NH2 A ARG 83  ? ? 116.78 120.30 -3.52  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG B 18  ? ? -100.39 79.03  
2 1 PHE B 104 ? ? -121.39 -57.15 
3 1 ARG A 18  ? ? -102.40 76.24  
4 1 PHE A 104 ? ? -120.13 -55.90 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG B 55  ? ? 0.116 'SIDE CHAIN' 
2 1 ARG B 91  ? A 0.171 'SIDE CHAIN' 
3 1 ARG A 55  ? ? 0.094 'SIDE CHAIN' 
4 1 ARG A 242 ? ? 0.083 'SIDE CHAIN' 
# 
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 A OCY 192 B OCY 189 ? CYS 'modified residue' 
2 A TPO 241 B TPO 238 ? THR 'modified residue' 
3 B CME 192 A CME 189 ? CYS 'modified residue' 
4 B TPO 241 A TPO 238 ? THR '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 -25.136 5.500  -8.693 0.0116 0.0641 0.0857 0.0193 0.0113  0.0613  1.8049 1.3387 2.1028 0.3740  
0.6351 0.3031  -0.0608 0.0212 0.0397 0.1020 0.2416 -0.0799 -0.0286 -0.0870 -0.0532 
'X-RAY DIFFRACTION' 2 ? refined -3.999  -4.379 20.565 0.0204 0.0653 0.0447 0.0119 -0.0098 -0.0367 0.8335 1.8207 1.8751 -0.3770 
0.2931 -0.3676 -0.0155 0.0117 0.0038 0.0070 0.1049 0.0156  0.1456  -0.0048 0.0175  
# 
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 B 2   B 246 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 1 B 301 B 308 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 3 2 A 2   A 246 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 4 2 A 301 A 315 ? ? ? ? ? ? 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 625 ? 6.44 . 
2 1 O ? A HOH 611 ? 6.12 . 
3 1 O ? A HOH 612 ? 6.62 . 
# 
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 GLY -2 ? A GLY 1  
2  1 Y 1 B PRO -1 ? A PRO 2  
3  1 Y 1 B HIS 0  ? A HIS 3  
4  1 Y 1 B MET 1  ? A MET 4  
5  1 Y 1 B GLU 70 ? A GLU 73 
6  1 Y 1 B GLY 71 ? A GLY 74 
7  1 Y 1 B ALA 72 ? A ALA 75 
8  1 Y 1 A GLY -2 ? B GLY 1  
9  1 Y 1 A PRO -1 ? B PRO 2  
10 1 Y 1 A HIS 0  ? B HIS 3  
11 1 Y 1 A MET 1  ? B MET 4  
12 1 Y 1 A LYS 68 ? B LYS 71 
13 1 Y 1 A THR 69 ? B THR 72 
14 1 Y 1 A GLU 70 ? B GLU 73 
15 1 Y 1 A GLY 71 ? B GLY 74 
# 
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  
CME N    N N N 74  
CME CA   C N R 75  
CME CB   C N N 76  
CME SG   S N N 77  
CME SD   S N N 78  
CME CE   C N N 79  
CME CZ   C N N 80  
CME OH   O N N 81  
CME C    C N N 82  
CME O    O N N 83  
CME OXT  O N N 84  
CME H    H N N 85  
CME H2   H N N 86  
CME HA   H N N 87  
CME HB2  H N N 88  
CME HB3  H N N 89  
CME HE2  H N N 90  
CME HE3  H N N 91  
CME HZ2  H N N 92  
CME HZ3  H N N 93  
CME HH   H N N 94  
CME HXT  H N N 95  
CYS N    N N N 96  
CYS CA   C N R 97  
CYS C    C N N 98  
CYS O    O N N 99  
CYS CB   C N N 100 
CYS SG   S N N 101 
CYS OXT  O N N 102 
CYS H    H N N 103 
CYS H2   H N N 104 
CYS HA   H N N 105 
CYS HB2  H N N 106 
CYS HB3  H N N 107 
CYS HG   H N N 108 
CYS HXT  H N N 109 
EDO C1   C N N 110 
EDO O1   O N N 111 
EDO C2   C N N 112 
EDO O2   O N N 113 
EDO H11  H N N 114 
EDO H12  H N N 115 
EDO HO1  H N N 116 
EDO H21  H N N 117 
EDO H22  H N N 118 
EDO HO2  H N N 119 
GLN N    N N N 120 
GLN CA   C N S 121 
GLN C    C N N 122 
GLN O    O N N 123 
GLN CB   C N N 124 
GLN CG   C N N 125 
GLN CD   C N N 126 
GLN OE1  O N N 127 
GLN NE2  N N N 128 
GLN OXT  O N N 129 
GLN H    H N N 130 
GLN H2   H N N 131 
GLN HA   H N N 132 
GLN HB2  H N N 133 
GLN HB3  H N N 134 
GLN HG2  H N N 135 
GLN HG3  H N N 136 
GLN HE21 H N N 137 
GLN HE22 H N N 138 
GLN HXT  H N N 139 
GLU N    N N N 140 
GLU CA   C N S 141 
GLU C    C N N 142 
GLU O    O N N 143 
GLU CB   C N N 144 
GLU CG   C N N 145 
GLU CD   C N N 146 
GLU OE1  O N N 147 
GLU OE2  O N N 148 
GLU OXT  O N N 149 
GLU H    H N N 150 
GLU H2   H N N 151 
GLU HA   H N N 152 
GLU HB2  H N N 153 
GLU HB3  H N N 154 
GLU HG2  H N N 155 
GLU HG3  H N N 156 
GLU HE2  H N N 157 
GLU HXT  H N N 158 
GLY N    N N N 159 
GLY CA   C N N 160 
GLY C    C N N 161 
GLY O    O N N 162 
GLY OXT  O N N 163 
GLY H    H N N 164 
GLY H2   H N N 165 
GLY HA2  H N N 166 
GLY HA3  H N N 167 
GLY HXT  H N N 168 
HIS N    N N N 169 
HIS CA   C N S 170 
HIS C    C N N 171 
HIS O    O N N 172 
HIS CB   C N N 173 
HIS CG   C Y N 174 
HIS ND1  N Y N 175 
HIS CD2  C Y N 176 
HIS CE1  C Y N 177 
HIS NE2  N Y N 178 
HIS OXT  O N N 179 
HIS H    H N N 180 
HIS H2   H N N 181 
HIS HA   H N N 182 
HIS HB2  H N N 183 
HIS HB3  H N N 184 
HIS HD1  H N N 185 
HIS HD2  H N N 186 
HIS HE1  H N N 187 
HIS HE2  H N N 188 
HIS HXT  H N N 189 
HOH O    O N N 190 
HOH H1   H N N 191 
HOH H2   H N N 192 
ILE N    N N N 193 
ILE CA   C N S 194 
ILE C    C N N 195 
ILE O    O N N 196 
ILE CB   C N S 197 
ILE CG1  C N N 198 
ILE CG2  C N N 199 
ILE CD1  C N N 200 
ILE OXT  O N N 201 
ILE H    H N N 202 
ILE H2   H N N 203 
ILE HA   H N N 204 
ILE HB   H N N 205 
ILE HG12 H N N 206 
ILE HG13 H N N 207 
ILE HG21 H N N 208 
ILE HG22 H N N 209 
ILE HG23 H N N 210 
ILE HD11 H N N 211 
ILE HD12 H N N 212 
ILE HD13 H N N 213 
ILE HXT  H N N 214 
LEU N    N N N 215 
LEU CA   C N S 216 
LEU C    C N N 217 
LEU O    O N N 218 
LEU CB   C N N 219 
LEU CG   C N N 220 
LEU CD1  C N N 221 
LEU CD2  C N N 222 
LEU OXT  O N N 223 
LEU H    H N N 224 
LEU H2   H N N 225 
LEU HA   H N N 226 
LEU HB2  H N N 227 
LEU HB3  H N N 228 
LEU HG   H N N 229 
LEU HD11 H N N 230 
LEU HD12 H N N 231 
LEU HD13 H N N 232 
LEU HD21 H N N 233 
LEU HD22 H N N 234 
LEU HD23 H N N 235 
LEU HXT  H N N 236 
LYS N    N N N 237 
LYS CA   C N S 238 
LYS C    C N N 239 
LYS O    O N N 240 
LYS CB   C N N 241 
LYS CG   C N N 242 
LYS CD   C N N 243 
LYS CE   C N N 244 
LYS NZ   N N N 245 
LYS OXT  O N N 246 
LYS H    H N N 247 
LYS H2   H N N 248 
LYS HA   H N N 249 
LYS HB2  H N N 250 
LYS HB3  H N N 251 
LYS HG2  H N N 252 
LYS HG3  H N N 253 
LYS HD2  H N N 254 
LYS HD3  H N N 255 
LYS HE2  H N N 256 
LYS HE3  H N N 257 
LYS HZ1  H N N 258 
LYS HZ2  H N N 259 
LYS HZ3  H N N 260 
LYS HXT  H N N 261 
MET N    N N N 262 
MET CA   C N S 263 
MET C    C N N 264 
MET O    O N N 265 
MET CB   C N N 266 
MET CG   C N N 267 
MET SD   S N N 268 
MET CE   C N N 269 
MET OXT  O N N 270 
MET H    H N N 271 
MET H2   H N N 272 
MET HA   H N N 273 
MET HB2  H N N 274 
MET HB3  H N N 275 
MET HG2  H N N 276 
MET HG3  H N N 277 
MET HE1  H N N 278 
MET HE2  H N N 279 
MET HE3  H N N 280 
MET HXT  H N N 281 
OCY N    N N N 282 
OCY CA   C N R 283 
OCY CB   C N N 284 
OCY SG   S N N 285 
OCY CD   C N N 286 
OCY CE   C N N 287 
OCY OZ   O N N 288 
OCY C    C N N 289 
OCY O    O N N 290 
OCY OXT  O N N 291 
OCY H    H N N 292 
OCY H2   H N N 293 
OCY HA   H N N 294 
OCY HB2  H N N 295 
OCY HB3  H N N 296 
OCY HD2  H N N 297 
OCY HD3  H N N 298 
OCY HE2  H N N 299 
OCY HE3  H N N 300 
OCY HZ   H N N 301 
OCY HXT  H N N 302 
PEG C1   C N N 303 
PEG O1   O N N 304 
PEG C2   C N N 305 
PEG O2   O N N 306 
PEG C3   C N N 307 
PEG C4   C N N 308 
PEG O4   O N N 309 
PEG H11  H N N 310 
PEG H12  H N N 311 
PEG HO1  H N N 312 
PEG H21  H N N 313 
PEG H22  H N N 314 
PEG H31  H N N 315 
PEG H32  H N N 316 
PEG H41  H N N 317 
PEG H42  H N N 318 
PEG HO4  H N N 319 
PHE N    N N N 320 
PHE CA   C N S 321 
PHE C    C N N 322 
PHE O    O N N 323 
PHE CB   C N N 324 
PHE CG   C Y N 325 
PHE CD1  C Y N 326 
PHE CD2  C Y N 327 
PHE CE1  C Y N 328 
PHE CE2  C Y N 329 
PHE CZ   C Y N 330 
PHE OXT  O N N 331 
PHE H    H N N 332 
PHE H2   H N N 333 
PHE HA   H N N 334 
PHE HB2  H N N 335 
PHE HB3  H N N 336 
PHE HD1  H N N 337 
PHE HD2  H N N 338 
PHE HE1  H N N 339 
PHE HE2  H N N 340 
PHE HZ   H N N 341 
PHE HXT  H N N 342 
PRO N    N N N 343 
PRO CA   C N S 344 
PRO C    C N N 345 
PRO O    O N N 346 
PRO CB   C N N 347 
PRO CG   C N N 348 
PRO CD   C N N 349 
PRO OXT  O N N 350 
PRO H    H N N 351 
PRO HA   H N N 352 
PRO HB2  H N N 353 
PRO HB3  H N N 354 
PRO HG2  H N N 355 
PRO HG3  H N N 356 
PRO HD2  H N N 357 
PRO HD3  H N N 358 
PRO HXT  H N N 359 
SER N    N N N 360 
SER CA   C N S 361 
SER C    C N N 362 
SER O    O N N 363 
SER CB   C N N 364 
SER OG   O N N 365 
SER OXT  O N N 366 
SER H    H N N 367 
SER H2   H N N 368 
SER HA   H N N 369 
SER HB2  H N N 370 
SER HB3  H N N 371 
SER HG   H N N 372 
SER HXT  H N N 373 
THR N    N N N 374 
THR CA   C N S 375 
THR C    C N N 376 
THR O    O N N 377 
THR CB   C N R 378 
THR OG1  O N N 379 
THR CG2  C N N 380 
THR OXT  O N N 381 
THR H    H N N 382 
THR H2   H N N 383 
THR HA   H N N 384 
THR HB   H N N 385 
THR HG1  H N N 386 
THR HG21 H N N 387 
THR HG22 H N N 388 
THR HG23 H N N 389 
THR HXT  H N N 390 
TPO N    N N N 391 
TPO CA   C N S 392 
TPO CB   C N R 393 
TPO CG2  C N N 394 
TPO OG1  O N N 395 
TPO P    P N N 396 
TPO O1P  O N N 397 
TPO O2P  O N N 398 
TPO O3P  O N N 399 
TPO C    C N N 400 
TPO O    O N N 401 
TPO OXT  O N N 402 
TPO H    H N N 403 
TPO H2   H N N 404 
TPO HA   H N N 405 
TPO HB   H N N 406 
TPO HG21 H N N 407 
TPO HG22 H N N 408 
TPO HG23 H N N 409 
TPO HOP2 H N N 410 
TPO HOP3 H N N 411 
TPO HXT  H N N 412 
TRP N    N N N 413 
TRP CA   C N S 414 
TRP C    C N N 415 
TRP O    O N N 416 
TRP CB   C N N 417 
TRP CG   C Y N 418 
TRP CD1  C Y N 419 
TRP CD2  C Y N 420 
TRP NE1  N Y N 421 
TRP CE2  C Y N 422 
TRP CE3  C Y N 423 
TRP CZ2  C Y N 424 
TRP CZ3  C Y N 425 
TRP CH2  C Y N 426 
TRP OXT  O N N 427 
TRP H    H N N 428 
TRP H2   H N N 429 
TRP HA   H N N 430 
TRP HB2  H N N 431 
TRP HB3  H N N 432 
TRP HD1  H N N 433 
TRP HE1  H N N 434 
TRP HE3  H N N 435 
TRP HZ2  H N N 436 
TRP HZ3  H N N 437 
TRP HH2  H N N 438 
TRP HXT  H N N 439 
TYR N    N N N 440 
TYR CA   C N S 441 
TYR C    C N N 442 
TYR O    O N N 443 
TYR CB   C N N 444 
TYR CG   C Y N 445 
TYR CD1  C Y N 446 
TYR CD2  C Y N 447 
TYR CE1  C Y N 448 
TYR CE2  C Y N 449 
TYR CZ   C Y N 450 
TYR OH   O N N 451 
TYR OXT  O N N 452 
TYR H    H N N 453 
TYR H2   H N N 454 
TYR HA   H N N 455 
TYR HB2  H N N 456 
TYR HB3  H N N 457 
TYR HD1  H N N 458 
TYR HD2  H N N 459 
TYR HE1  H N N 460 
TYR HE2  H N N 461 
TYR HH   H N N 462 
TYR HXT  H N N 463 
VAL N    N N N 464 
VAL CA   C N S 465 
VAL C    C N N 466 
VAL O    O N N 467 
VAL CB   C N N 468 
VAL CG1  C N N 469 
VAL CG2  C N N 470 
VAL OXT  O N N 471 
VAL H    H N N 472 
VAL H2   H N N 473 
VAL HA   H N N 474 
VAL HB   H N N 475 
VAL HG11 H N N 476 
VAL HG12 H N N 477 
VAL HG13 H N N 478 
VAL HG21 H N N 479 
VAL HG22 H N N 480 
VAL HG23 H N N 481 
VAL HXT  H N N 482 
# 
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  
CME N   CA   sing N N 70  
CME N   H    sing N N 71  
CME N   H2   sing N N 72  
CME CA  CB   sing N N 73  
CME CA  C    sing N N 74  
CME CA  HA   sing N N 75  
CME CB  SG   sing N N 76  
CME CB  HB2  sing N N 77  
CME CB  HB3  sing N N 78  
CME SG  SD   sing N N 79  
CME SD  CE   sing N N 80  
CME CE  CZ   sing N N 81  
CME CE  HE2  sing N N 82  
CME CE  HE3  sing N N 83  
CME CZ  OH   sing N N 84  
CME CZ  HZ2  sing N N 85  
CME CZ  HZ3  sing N N 86  
CME OH  HH   sing N N 87  
CME C   O    doub N N 88  
CME C   OXT  sing N N 89  
CME OXT HXT  sing N N 90  
CYS N   CA   sing N N 91  
CYS N   H    sing N N 92  
CYS N   H2   sing N N 93  
CYS CA  C    sing N N 94  
CYS CA  CB   sing N N 95  
CYS CA  HA   sing N N 96  
CYS C   O    doub N N 97  
CYS C   OXT  sing N N 98  
CYS CB  SG   sing N N 99  
CYS CB  HB2  sing N N 100 
CYS CB  HB3  sing N N 101 
CYS SG  HG   sing N N 102 
CYS OXT HXT  sing N N 103 
EDO C1  O1   sing N N 104 
EDO C1  C2   sing N N 105 
EDO C1  H11  sing N N 106 
EDO C1  H12  sing N N 107 
EDO O1  HO1  sing N N 108 
EDO C2  O2   sing N N 109 
EDO C2  H21  sing N N 110 
EDO C2  H22  sing N N 111 
EDO O2  HO2  sing N N 112 
GLN N   CA   sing N N 113 
GLN N   H    sing N N 114 
GLN N   H2   sing N N 115 
GLN CA  C    sing N N 116 
GLN CA  CB   sing N N 117 
GLN CA  HA   sing N N 118 
GLN C   O    doub N N 119 
GLN C   OXT  sing N N 120 
GLN CB  CG   sing N N 121 
GLN CB  HB2  sing N N 122 
GLN CB  HB3  sing N N 123 
GLN CG  CD   sing N N 124 
GLN CG  HG2  sing N N 125 
GLN CG  HG3  sing N N 126 
GLN CD  OE1  doub N N 127 
GLN CD  NE2  sing N N 128 
GLN NE2 HE21 sing N N 129 
GLN NE2 HE22 sing N N 130 
GLN OXT HXT  sing N N 131 
GLU N   CA   sing N N 132 
GLU N   H    sing N N 133 
GLU N   H2   sing N N 134 
GLU CA  C    sing N N 135 
GLU CA  CB   sing N N 136 
GLU CA  HA   sing N N 137 
GLU C   O    doub N N 138 
GLU C   OXT  sing N N 139 
GLU CB  CG   sing N N 140 
GLU CB  HB2  sing N N 141 
GLU CB  HB3  sing N N 142 
GLU CG  CD   sing N N 143 
GLU CG  HG2  sing N N 144 
GLU CG  HG3  sing N N 145 
GLU CD  OE1  doub N N 146 
GLU CD  OE2  sing N N 147 
GLU OE2 HE2  sing N N 148 
GLU OXT HXT  sing N N 149 
GLY N   CA   sing N N 150 
GLY N   H    sing N N 151 
GLY N   H2   sing N N 152 
GLY CA  C    sing N N 153 
GLY CA  HA2  sing N N 154 
GLY CA  HA3  sing N N 155 
GLY C   O    doub N N 156 
GLY C   OXT  sing N N 157 
GLY OXT HXT  sing N N 158 
HIS N   CA   sing N N 159 
HIS N   H    sing N N 160 
HIS N   H2   sing N N 161 
HIS CA  C    sing N N 162 
HIS CA  CB   sing N N 163 
HIS CA  HA   sing N N 164 
HIS C   O    doub N N 165 
HIS C   OXT  sing N N 166 
HIS CB  CG   sing N N 167 
HIS CB  HB2  sing N N 168 
HIS CB  HB3  sing N N 169 
HIS CG  ND1  sing Y N 170 
HIS CG  CD2  doub Y N 171 
HIS ND1 CE1  doub Y N 172 
HIS ND1 HD1  sing N N 173 
HIS CD2 NE2  sing Y N 174 
HIS CD2 HD2  sing N N 175 
HIS CE1 NE2  sing Y N 176 
HIS CE1 HE1  sing N N 177 
HIS NE2 HE2  sing N N 178 
HIS OXT HXT  sing N N 179 
HOH O   H1   sing N N 180 
HOH O   H2   sing N N 181 
ILE N   CA   sing N N 182 
ILE N   H    sing N N 183 
ILE N   H2   sing N N 184 
ILE CA  C    sing N N 185 
ILE CA  CB   sing N N 186 
ILE CA  HA   sing N N 187 
ILE C   O    doub N N 188 
ILE C   OXT  sing N N 189 
ILE CB  CG1  sing N N 190 
ILE CB  CG2  sing N N 191 
ILE CB  HB   sing N N 192 
ILE CG1 CD1  sing N N 193 
ILE CG1 HG12 sing N N 194 
ILE CG1 HG13 sing N N 195 
ILE CG2 HG21 sing N N 196 
ILE CG2 HG22 sing N N 197 
ILE CG2 HG23 sing N N 198 
ILE CD1 HD11 sing N N 199 
ILE CD1 HD12 sing N N 200 
ILE CD1 HD13 sing N N 201 
ILE OXT HXT  sing N N 202 
LEU N   CA   sing N N 203 
LEU N   H    sing N N 204 
LEU N   H2   sing N N 205 
LEU CA  C    sing N N 206 
LEU CA  CB   sing N N 207 
LEU CA  HA   sing N N 208 
LEU C   O    doub N N 209 
LEU C   OXT  sing N N 210 
LEU CB  CG   sing N N 211 
LEU CB  HB2  sing N N 212 
LEU CB  HB3  sing N N 213 
LEU CG  CD1  sing N N 214 
LEU CG  CD2  sing N N 215 
LEU CG  HG   sing N N 216 
LEU CD1 HD11 sing N N 217 
LEU CD1 HD12 sing N N 218 
LEU CD1 HD13 sing N N 219 
LEU CD2 HD21 sing N N 220 
LEU CD2 HD22 sing N N 221 
LEU CD2 HD23 sing N N 222 
LEU OXT HXT  sing N N 223 
LYS N   CA   sing N N 224 
LYS N   H    sing N N 225 
LYS N   H2   sing N N 226 
LYS CA  C    sing N N 227 
LYS CA  CB   sing N N 228 
LYS CA  HA   sing N N 229 
LYS C   O    doub N N 230 
LYS C   OXT  sing N N 231 
LYS CB  CG   sing N N 232 
LYS CB  HB2  sing N N 233 
LYS CB  HB3  sing N N 234 
LYS CG  CD   sing N N 235 
LYS CG  HG2  sing N N 236 
LYS CG  HG3  sing N N 237 
LYS CD  CE   sing N N 238 
LYS CD  HD2  sing N N 239 
LYS CD  HD3  sing N N 240 
LYS CE  NZ   sing N N 241 
LYS CE  HE2  sing N N 242 
LYS CE  HE3  sing N N 243 
LYS NZ  HZ1  sing N N 244 
LYS NZ  HZ2  sing N N 245 
LYS NZ  HZ3  sing N N 246 
LYS OXT HXT  sing N N 247 
MET N   CA   sing N N 248 
MET N   H    sing N N 249 
MET N   H2   sing N N 250 
MET CA  C    sing N N 251 
MET CA  CB   sing N N 252 
MET CA  HA   sing N N 253 
MET C   O    doub N N 254 
MET C   OXT  sing N N 255 
MET CB  CG   sing N N 256 
MET CB  HB2  sing N N 257 
MET CB  HB3  sing N N 258 
MET CG  SD   sing N N 259 
MET CG  HG2  sing N N 260 
MET CG  HG3  sing N N 261 
MET SD  CE   sing N N 262 
MET CE  HE1  sing N N 263 
MET CE  HE2  sing N N 264 
MET CE  HE3  sing N N 265 
MET OXT HXT  sing N N 266 
OCY N   CA   sing N N 267 
OCY N   H    sing N N 268 
OCY N   H2   sing N N 269 
OCY CA  CB   sing N N 270 
OCY CA  C    sing N N 271 
OCY CA  HA   sing N N 272 
OCY CB  SG   sing N N 273 
OCY CB  HB2  sing N N 274 
OCY CB  HB3  sing N N 275 
OCY SG  CD   sing N N 276 
OCY CD  CE   sing N N 277 
OCY CD  HD2  sing N N 278 
OCY CD  HD3  sing N N 279 
OCY CE  OZ   sing N N 280 
OCY CE  HE2  sing N N 281 
OCY CE  HE3  sing N N 282 
OCY OZ  HZ   sing N N 283 
OCY C   O    doub N N 284 
OCY C   OXT  sing N N 285 
OCY OXT HXT  sing N N 286 
PEG C1  O1   sing N N 287 
PEG C1  C2   sing N N 288 
PEG C1  H11  sing N N 289 
PEG C1  H12  sing N N 290 
PEG O1  HO1  sing N N 291 
PEG C2  O2   sing N N 292 
PEG C2  H21  sing N N 293 
PEG C2  H22  sing N N 294 
PEG O2  C3   sing N N 295 
PEG C3  C4   sing N N 296 
PEG C3  H31  sing N N 297 
PEG C3  H32  sing N N 298 
PEG C4  O4   sing N N 299 
PEG C4  H41  sing N N 300 
PEG C4  H42  sing N N 301 
PEG O4  HO4  sing N N 302 
PHE N   CA   sing N N 303 
PHE N   H    sing N N 304 
PHE N   H2   sing N N 305 
PHE CA  C    sing N N 306 
PHE CA  CB   sing N N 307 
PHE CA  HA   sing N N 308 
PHE C   O    doub N N 309 
PHE C   OXT  sing N N 310 
PHE CB  CG   sing N N 311 
PHE CB  HB2  sing N N 312 
PHE CB  HB3  sing N N 313 
PHE CG  CD1  doub Y N 314 
PHE CG  CD2  sing Y N 315 
PHE CD1 CE1  sing Y N 316 
PHE CD1 HD1  sing N N 317 
PHE CD2 CE2  doub Y N 318 
PHE CD2 HD2  sing N N 319 
PHE CE1 CZ   doub Y N 320 
PHE CE1 HE1  sing N N 321 
PHE CE2 CZ   sing Y N 322 
PHE CE2 HE2  sing N N 323 
PHE CZ  HZ   sing N N 324 
PHE OXT HXT  sing N N 325 
PRO N   CA   sing N N 326 
PRO N   CD   sing N N 327 
PRO N   H    sing N N 328 
PRO CA  C    sing N N 329 
PRO CA  CB   sing N N 330 
PRO CA  HA   sing N N 331 
PRO C   O    doub N N 332 
PRO C   OXT  sing N N 333 
PRO CB  CG   sing N N 334 
PRO CB  HB2  sing N N 335 
PRO CB  HB3  sing N N 336 
PRO CG  CD   sing N N 337 
PRO CG  HG2  sing N N 338 
PRO CG  HG3  sing N N 339 
PRO CD  HD2  sing N N 340 
PRO CD  HD3  sing N N 341 
PRO OXT HXT  sing N N 342 
SER N   CA   sing N N 343 
SER N   H    sing N N 344 
SER N   H2   sing N N 345 
SER CA  C    sing N N 346 
SER CA  CB   sing N N 347 
SER CA  HA   sing N N 348 
SER C   O    doub N N 349 
SER C   OXT  sing N N 350 
SER CB  OG   sing N N 351 
SER CB  HB2  sing N N 352 
SER CB  HB3  sing N N 353 
SER OG  HG   sing N N 354 
SER OXT HXT  sing N N 355 
THR N   CA   sing N N 356 
THR N   H    sing N N 357 
THR N   H2   sing N N 358 
THR CA  C    sing N N 359 
THR CA  CB   sing N N 360 
THR CA  HA   sing N N 361 
THR C   O    doub N N 362 
THR C   OXT  sing N N 363 
THR CB  OG1  sing N N 364 
THR CB  CG2  sing N N 365 
THR CB  HB   sing N N 366 
THR OG1 HG1  sing N N 367 
THR CG2 HG21 sing N N 368 
THR CG2 HG22 sing N N 369 
THR CG2 HG23 sing N N 370 
THR OXT HXT  sing N N 371 
TPO N   CA   sing N N 372 
TPO N   H    sing N N 373 
TPO N   H2   sing N N 374 
TPO CA  CB   sing N N 375 
TPO CA  C    sing N N 376 
TPO CA  HA   sing N N 377 
TPO CB  CG2  sing N N 378 
TPO CB  OG1  sing N N 379 
TPO CB  HB   sing N N 380 
TPO CG2 HG21 sing N N 381 
TPO CG2 HG22 sing N N 382 
TPO CG2 HG23 sing N N 383 
TPO OG1 P    sing N N 384 
TPO P   O1P  doub N N 385 
TPO P   O2P  sing N N 386 
TPO P   O3P  sing N N 387 
TPO O2P HOP2 sing N N 388 
TPO O3P HOP3 sing N N 389 
TPO C   O    doub N N 390 
TPO C   OXT  sing N N 391 
TPO OXT HXT  sing N N 392 
TRP N   CA   sing N N 393 
TRP N   H    sing N N 394 
TRP N   H2   sing N N 395 
TRP CA  C    sing N N 396 
TRP CA  CB   sing N N 397 
TRP CA  HA   sing N N 398 
TRP C   O    doub N N 399 
TRP C   OXT  sing N N 400 
TRP CB  CG   sing N N 401 
TRP CB  HB2  sing N N 402 
TRP CB  HB3  sing N N 403 
TRP CG  CD1  doub Y N 404 
TRP CG  CD2  sing Y N 405 
TRP CD1 NE1  sing Y N 406 
TRP CD1 HD1  sing N N 407 
TRP CD2 CE2  doub Y N 408 
TRP CD2 CE3  sing Y N 409 
TRP NE1 CE2  sing Y N 410 
TRP NE1 HE1  sing N N 411 
TRP CE2 CZ2  sing Y N 412 
TRP CE3 CZ3  doub Y N 413 
TRP CE3 HE3  sing N N 414 
TRP CZ2 CH2  doub Y N 415 
TRP CZ2 HZ2  sing N N 416 
TRP CZ3 CH2  sing Y N 417 
TRP CZ3 HZ3  sing N N 418 
TRP CH2 HH2  sing N N 419 
TRP OXT HXT  sing N N 420 
TYR N   CA   sing N N 421 
TYR N   H    sing N N 422 
TYR N   H2   sing N N 423 
TYR CA  C    sing N N 424 
TYR CA  CB   sing N N 425 
TYR CA  HA   sing N N 426 
TYR C   O    doub N N 427 
TYR C   OXT  sing N N 428 
TYR CB  CG   sing N N 429 
TYR CB  HB2  sing N N 430 
TYR CB  HB3  sing N N 431 
TYR CG  CD1  doub Y N 432 
TYR CG  CD2  sing Y N 433 
TYR CD1 CE1  sing Y N 434 
TYR CD1 HD1  sing N N 435 
TYR CD2 CE2  doub Y N 436 
TYR CD2 HD2  sing N N 437 
TYR CE1 CZ   doub Y N 438 
TYR CE1 HE1  sing N N 439 
TYR CE2 CZ   sing Y N 440 
TYR CE2 HE2  sing N N 441 
TYR CZ  OH   sing N N 442 
TYR OH  HH   sing N N 443 
TYR OXT HXT  sing N N 444 
VAL N   CA   sing N N 445 
VAL N   H    sing N N 446 
VAL N   H2   sing N N 447 
VAL CA  C    sing N N 448 
VAL CA  CB   sing N N 449 
VAL CA  HA   sing N N 450 
VAL C   O    doub N N 451 
VAL C   OXT  sing N N 452 
VAL CB  CG1  sing N N 453 
VAL CB  CG2  sing N N 454 
VAL CB  HB   sing N N 455 
VAL CG1 HG11 sing N N 456 
VAL CG1 HG12 sing N N 457 
VAL CG1 HG13 sing N N 458 
VAL CG2 HG21 sing N N 459 
VAL CG2 HG22 sing N N 460 
VAL CG2 HG23 sing N N 461 
VAL OXT HXT  sing N N 462 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9UJ2 
_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]   0.016514 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011841 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.007149 
_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 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP A  1 5   ? 0.862   12.723  -14.945 1.00 52.73 ? 2   ASP B N   1 
ATOM   2    C CA  . ASP A  1 5   ? 0.708   11.788  -16.097 1.00 54.59 ? 2   ASP B CA  1 
ATOM   3    C C   . ASP A  1 5   ? -0.534  10.912  -15.868 1.00 50.01 ? 2   ASP B C   1 
ATOM   4    O O   . ASP A  1 5   ? -0.737  10.404  -14.764 1.00 47.68 ? 2   ASP B O   1 
ATOM   5    C CB  . ASP A  1 5   ? 1.976   10.968  -16.312 1.00 60.35 ? 2   ASP B CB  1 
ATOM   6    C CG  . ASP A  1 5   ? 1.872   9.802   -17.292 1.00 63.85 ? 2   ASP B CG  1 
ATOM   7    O OD1 . ASP A  1 5   ? 1.665   8.654   -16.822 1.00 58.39 ? 2   ASP B OD1 1 
ATOM   8    O OD2 . ASP A  1 5   ? 2.021   10.046  -18.520 1.00 71.70 ? 2   ASP B OD2 1 
ATOM   9    N N   . LYS A  1 6   ? -1.295  10.649  -16.947 1.00 50.38 ? 3   LYS B N   1 
ATOM   10   C CA  . LYS A  1 6   ? -2.623  10.031  -16.886 1.00 48.36 ? 3   LYS B CA  1 
ATOM   11   C C   . LYS A  1 6   ? -2.504  8.553   -16.528 1.00 46.81 ? 3   LYS B C   1 
ATOM   12   O O   . LYS A  1 6   ? -3.126  8.085   -15.573 1.00 42.28 ? 3   LYS B O   1 
ATOM   13   C CB  . LYS A  1 6   ? -3.408  10.152  -18.204 1.00 51.33 ? 3   LYS B CB  1 
ATOM   14   C CG  . LYS A  1 6   ? -4.918  10.210  -18.029 1.00 53.14 ? 3   LYS B CG  1 
ATOM   15   C CD  . LYS A  1 6   ? -5.756  9.802   -19.241 1.00 55.74 ? 3   LYS B CD  1 
ATOM   16   C CE  . LYS A  1 6   ? -5.911  8.317   -19.284 1.00 56.36 ? 3   LYS B CE  1 
ATOM   17   N NZ  . LYS A  1 6   ? -5.983  7.772   -20.639 1.00 58.00 ? 3   LYS B NZ  1 
ATOM   18   N N   . ASN A  1 7   ? -1.657  7.843   -17.290 1.00 46.88 ? 4   ASN B N   1 
ATOM   19   C CA  . ASN A  1 7   ? -1.410  6.423   -17.109 1.00 46.98 ? 4   ASN B CA  1 
ATOM   20   C C   . ASN A  1 7   ? -0.954  6.126   -15.667 1.00 43.77 ? 4   ASN B C   1 
ATOM   21   O O   . ASN A  1 7   ? -1.446  5.187   -15.063 1.00 41.67 ? 4   ASN B O   1 
ATOM   22   C CB  . ASN A  1 7   ? -0.486  5.913   -18.211 1.00 50.33 ? 4   ASN B CB  1 
ATOM   23   C CG  . ASN A  1 7   ? -0.198  4.446   -18.030 1.00 52.75 ? 4   ASN B CG  1 
ATOM   24   O OD1 . ASN A  1 7   ? 0.884   4.089   -17.562 1.00 56.66 ? 4   ASN B OD1 1 
ATOM   25   N ND2 . ASN A  1 7   ? -1.172  3.599   -18.314 1.00 52.35 ? 4   ASN B ND2 1 
ATOM   26   N N   . GLU A  1 8   ? -0.076  6.963   -15.105 1.00 43.06 ? 5   GLU B N   1 
ATOM   27   C CA  . GLU A  1 8   ? 0.360   6.830   -13.718 1.00 42.36 ? 5   GLU B CA  1 
ATOM   28   C C   . GLU A  1 8   ? -0.777  6.985   -12.686 1.00 36.79 ? 5   GLU B C   1 
ATOM   29   O O   . GLU A  1 8   ? -0.843  6.220   -11.725 1.00 34.60 ? 5   GLU B O   1 
ATOM   30   C CB  . GLU A  1 8   ? 1.481   7.846   -13.578 1.00 45.43 ? 5   GLU B CB  1 
ATOM   31   C CG  . GLU A  1 8   ? 1.966   8.088   -12.162 1.00 48.29 ? 5   GLU B CG  1 
ATOM   32   C CD  . GLU A  1 8   ? 3.284   8.829   -12.164 1.00 53.39 ? 5   GLU B CD  1 
ATOM   33   O OE1 . GLU A  1 8   ? 3.839   9.375   -13.178 1.00 54.98 ? 5   GLU B OE1 1 
ATOM   34   O OE2 . GLU A  1 8   ? 3.752   8.801   -11.013 1.00 56.27 ? 5   GLU B OE2 1 
ATOM   35   N N   . LEU A  1 9   ? -1.568  8.064   -12.785 1.00 34.43 ? 6   LEU B N   1 
ATOM   36   C CA  . LEU A  1 9   ? -2.731  8.272   -11.931 1.00 31.38 ? 6   LEU B CA  1 
ATOM   37   C C   . LEU A  1 9   ? -3.705  7.086   -11.984 1.00 29.08 ? 6   LEU B C   1 
ATOM   38   O O   . LEU A  1 9   ? -4.265  6.709   -10.942 1.00 26.59 ? 6   LEU B O   1 
ATOM   39   C CB  . LEU A  1 9   ? -3.430  9.571   -12.318 1.00 32.48 ? 6   LEU B CB  1 
ATOM   40   C CG  . LEU A  1 9   ? -2.721  10.871  -11.953 1.00 34.89 ? 6   LEU B CG  1 
ATOM   41   C CD1 . LEU A  1 9   ? -3.350  12.039  -12.679 1.00 35.59 ? 6   LEU B CD1 1 
ATOM   42   C CD2 . LEU A  1 9   ? -2.800  11.079  -10.450 1.00 35.91 ? 6   LEU B CD2 1 
ATOM   43   N N   . VAL A  1 10  ? -3.908  6.508   -13.178 1.00 28.39 ? 7   VAL B N   1 
ATOM   44   C CA  . VAL A  1 10  ? -4.791  5.357   -13.329 1.00 27.63 ? 7   VAL B CA  1 
ATOM   45   C C   . VAL A  1 10  ? -4.197  4.153   -12.589 1.00 27.82 ? 7   VAL B C   1 
ATOM   46   O O   . VAL A  1 10  ? -4.945  3.489   -11.889 1.00 26.33 ? 7   VAL B O   1 
ATOM   47   C CB  . VAL A  1 10  ? -5.111  5.080   -14.816 1.00 28.09 ? 7   VAL B CB  1 
ATOM   48   C CG1 . VAL A  1 10  ? -5.750  3.719   -15.062 1.00 26.89 ? 7   VAL B CG1 1 
ATOM   49   C CG2 . VAL A  1 10  ? -6.007  6.204   -15.359 1.00 28.05 ? 7   VAL B CG2 1 
ATOM   50   N N   . GLN A  1 11  ? -2.891  3.893   -12.761 1.00 30.70 ? 8   GLN B N   1 
ATOM   51   C CA  . GLN A  1 11  ? -2.206  2.846   -12.002 1.00 31.67 ? 8   GLN B CA  1 
ATOM   52   C C   . GLN A  1 11  ? -2.310  3.068   -10.485 1.00 30.38 ? 8   GLN B C   1 
ATOM   53   O O   . GLN A  1 11  ? -2.612  2.110   -9.770  1.00 28.84 ? 8   GLN B O   1 
ATOM   54   C CB  . GLN A  1 11  ? -0.771  2.577   -12.478 1.00 37.43 ? 8   GLN B CB  1 
ATOM   55   C CG  . GLN A  1 11  ? -0.600  2.104   -13.923 1.00 40.89 ? 8   GLN B CG  1 
ATOM   56   C CD  . GLN A  1 11  ? -1.483  0.932   -14.298 1.00 43.00 ? 8   GLN B CD  1 
ATOM   57   O OE1 . GLN A  1 11  ? -1.295  -0.197  -13.828 1.00 49.49 ? 8   GLN B OE1 1 
ATOM   58   N NE2 . GLN A  1 11  ? -2.493  1.196   -15.109 1.00 41.38 ? 8   GLN B NE2 1 
ATOM   59   N N   . LYS A  1 12  ? -2.168  4.311   -9.998  1.00 31.54 ? 9   LYS B N   1 
ATOM   60   C CA  . LYS A  1 12  ? -2.258  4.589   -8.565  1.00 32.36 ? 9   LYS B CA  1 
ATOM   61   C C   . LYS A  1 12  ? -3.696  4.354   -8.077  1.00 29.23 ? 9   LYS B C   1 
ATOM   62   O O   . LYS A  1 12  ? -3.858  3.855   -6.968  1.00 25.56 ? 9   LYS B O   1 
ATOM   63   C CB  . LYS A  1 12  ? -1.707  5.977   -8.238  1.00 37.29 ? 9   LYS B CB  1 
ATOM   64   C CG  . LYS A  1 12  ? -1.764  6.532   -6.801  1.00 44.68 ? 9   LYS B CG  1 
ATOM   65   C CD  . LYS A  1 12  ? -0.646  6.423   -5.774  1.00 55.10 ? 9   LYS B CD  1 
ATOM   66   C CE  . LYS A  1 12  ? -0.733  7.487   -4.667  1.00 62.28 ? 9   LYS B CE  1 
ATOM   67   N NZ  . LYS A  1 12  ? -2.000  7.829   -3.997  1.00 67.25 ? 9   LYS B NZ  1 
ATOM   68   N N   . ALA A  1 13  ? -4.703  4.746   -8.889  1.00 26.08 ? 10  ALA B N   1 
ATOM   69   C CA  . ALA A  1 13  ? -6.098  4.495   -8.584  1.00 24.70 ? 10  ALA B CA  1 
ATOM   70   C C   . ALA A  1 13  ? -6.385  3.009   -8.416  1.00 23.42 ? 10  ALA B C   1 
ATOM   71   O O   . ALA A  1 13  ? -7.100  2.667   -7.479  1.00 22.08 ? 10  ALA B O   1 
ATOM   72   C CB  . ALA A  1 13  ? -7.023  5.107   -9.609  1.00 24.78 ? 10  ALA B CB  1 
ATOM   73   N N   . LYS A  1 14  ? -5.828  2.153   -9.281  1.00 24.26 ? 11  LYS B N   1 
ATOM   74   C CA  . LYS A  1 14  ? -6.004  0.712   -9.189  1.00 24.10 ? 11  LYS B CA  1 
ATOM   75   C C   . LYS A  1 14  ? -5.397  0.146   -7.889  1.00 24.24 ? 11  LYS B C   1 
ATOM   76   O O   . LYS A  1 14  ? -5.968  -0.734  -7.240  1.00 23.43 ? 11  LYS B O   1 
ATOM   77   C CB  . LYS A  1 14  ? -5.340  0.054   -10.404 1.00 26.18 ? 11  LYS B CB  1 
ATOM   78   C CG  . LYS A  1 14  ? -6.051  0.240   -11.735 1.00 26.47 ? 11  LYS B CG  1 
ATOM   79   C CD  . LYS A  1 14  ? -5.213  -0.477  -12.772 1.00 29.66 ? 11  LYS B CD  1 
ATOM   80   C CE  . LYS A  1 14  ? -5.945  -0.788  -13.994 1.00 32.17 ? 11  LYS B CE  1 
ATOM   81   N NZ  . LYS A  1 14  ? -4.997  -1.431  -14.918 1.00 36.22 ? 11  LYS B NZ  1 
ATOM   82   N N   . LEU A  1 15  ? -4.211  0.645   -7.542  1.00 24.97 ? 12  LEU B N   1 
ATOM   83   C CA  . LEU A  1 15  ? -3.529  0.265   -6.317  1.00 25.44 ? 12  LEU B CA  1 
ATOM   84   C C   . LEU A  1 15  ? -4.343  0.668   -5.085  1.00 23.31 ? 12  LEU B C   1 
ATOM   85   O O   . LEU A  1 15  ? -4.544  -0.180  -4.201  1.00 22.65 ? 12  LEU B O   1 
ATOM   86   C CB  . LEU A  1 15  ? -2.155  0.908   -6.295  1.00 28.04 ? 12  LEU B CB  1 
ATOM   87   C CG  . LEU A  1 15  ? -1.144  0.294   -5.340  1.00 31.41 ? 12  LEU B CG  1 
ATOM   88   C CD1 . LEU A  1 15  ? -0.843  -1.145  -5.612  1.00 33.50 ? 12  LEU B CD1 1 
ATOM   89   C CD2 . LEU A  1 15  ? 0.145   1.081   -5.532  1.00 32.53 ? 12  LEU B CD2 1 
ATOM   90   N N   . ALA A  1 16  ? -4.853  1.926   -5.093  1.00 21.80 ? 13  ALA B N   1 
ATOM   91   C CA  . ALA A  1 16  ? -5.707  2.430   -4.038  1.00 20.87 ? 13  ALA B CA  1 
ATOM   92   C C   . ALA A  1 16  ? -6.951  1.542   -3.880  1.00 20.43 ? 13  ALA B C   1 
ATOM   93   O O   . ALA A  1 16  ? -7.354  1.246   -2.751  1.00 20.68 ? 13  ALA B O   1 
ATOM   94   C CB  . ALA A  1 16  ? -6.126  3.864   -4.343  1.00 20.37 ? 13  ALA B CB  1 
ATOM   95   N N   . GLU A  1 17  ? -7.583  1.159   -5.010  1.00 20.08 ? 14  GLU B N   1 
ATOM   96   C CA  . GLU A  1 17  ? -8.764  0.301   -4.954  1.00 19.50 ? 14  GLU B CA  1 
ATOM   97   C C   . GLU A  1 17  ? -8.409  -1.004  -4.213  1.00 20.66 ? 14  GLU B C   1 
ATOM   98   O O   . GLU A  1 17  ? -9.170  -1.428  -3.355  1.00 19.98 ? 14  GLU B O   1 
ATOM   99   C CB  . GLU A  1 17  ? -9.281  -0.078  -6.332  1.00 20.07 ? 14  GLU B CB  1 
ATOM   100  C CG  . GLU A  1 17  ? -10.573 -0.884  -6.268  1.00 19.72 ? 14  GLU B CG  1 
ATOM   101  C CD  . GLU A  1 17  ? -11.265 -1.182  -7.581  1.00 21.32 ? 14  GLU B CD  1 
ATOM   102  O OE1 . GLU A  1 17  ? -10.679 -0.940  -8.646  1.00 22.55 ? 14  GLU B OE1 1 
ATOM   103  O OE2 . GLU A  1 17  ? -12.419 -1.603  -7.484  1.00 20.65 ? 14  GLU B OE2 1 
ATOM   104  N N   . GLN A  1 18  ? -7.323  -1.663  -4.582  1.00 23.08 ? 15  GLN B N   1 
ATOM   105  C CA  . GLN A  1 18  ? -6.880  -2.868  -3.887  1.00 25.05 ? 15  GLN B CA  1 
ATOM   106  C C   . GLN A  1 18  ? -6.655  -2.661  -2.382  1.00 23.94 ? 15  GLN B C   1 
ATOM   107  O O   . GLN A  1 18  ? -7.019  -3.541  -1.601  1.00 24.47 ? 15  GLN B O   1 
ATOM   108  C CB  . GLN A  1 18  ? -5.626  -3.480  -4.492  1.00 29.96 ? 15  GLN B CB  1 
ATOM   109  C CG  . GLN A  1 18  ? -5.893  -4.621  -5.467  1.00 37.12 ? 15  GLN B CG  1 
ATOM   110  C CD  . GLN A  1 18  ? -5.756  -4.189  -6.892  1.00 44.17 ? 15  GLN B CD  1 
ATOM   111  O OE1 . GLN A  1 18  ? -6.755  -4.159  -7.626  1.00 58.52 ? 15  GLN B OE1 1 
ATOM   112  N NE2 . GLN A  1 18  ? -4.505  -3.940  -7.292  1.00 43.86 ? 15  GLN B NE2 1 
ATOM   113  N N   . ALA A  1 19  ? -6.089  -1.514  -1.995  1.00 22.40 ? 16  ALA B N   1 
ATOM   114  C CA  . ALA A  1 19  ? -5.898  -1.133  -0.596  1.00 22.69 ? 16  ALA B CA  1 
ATOM   115  C C   . ALA A  1 19  ? -7.182  -0.702  0.131   1.00 21.46 ? 16  ALA B C   1 
ATOM   116  O O   . ALA A  1 19  ? -7.091  -0.482  1.333   1.00 20.91 ? 16  ALA B O   1 
ATOM   117  C CB  . ALA A  1 19  ? -4.860  -0.031  -0.503  1.00 22.83 ? 16  ALA B CB  1 
ATOM   118  N N   . GLU A  1 20  ? -8.305  -0.556  -0.596  1.00 20.93 ? 17  GLU B N   1 
ATOM   119  C CA  . GLU A  1 20  ? -9.585  -0.012  -0.144  1.00 21.20 ? 17  GLU B CA  1 
ATOM   120  C C   . GLU A  1 20  ? -9.365  1.399   0.404   1.00 21.15 ? 17  GLU B C   1 
ATOM   121  O O   . GLU A  1 20  ? -9.915  1.739   1.428   1.00 21.06 ? 17  GLU B O   1 
ATOM   122  C CB  . GLU A  1 20  ? -10.229 -1.039  0.809   1.00 24.91 ? 17  GLU B CB  1 
ATOM   123  C CG  . GLU A  1 20  ? -10.438 -2.429  0.208   1.00 26.95 ? 17  GLU B CG  1 
ATOM   124  C CD  . GLU A  1 20  ? -11.154 -3.353  1.172   1.00 29.49 ? 17  GLU B CD  1 
ATOM   125  O OE1 . GLU A  1 20  ? -12.313 -3.145  1.407   1.00 35.57 ? 17  GLU B OE1 1 
ATOM   126  O OE2 . GLU A  1 20  ? -10.488 -4.130  1.813   1.00 39.69 ? 17  GLU B OE2 1 
ATOM   127  N N   . ARG A  1 21  ? -8.462  2.192   -0.221  1.00 20.37 ? 18  ARG B N   1 
ATOM   128  C CA  . ARG A  1 21  ? -8.202  3.576   0.130   1.00 20.70 ? 18  ARG B CA  1 
ATOM   129  C C   . ARG A  1 21  ? -8.951  4.454   -0.873  1.00 20.02 ? 18  ARG B C   1 
ATOM   130  O O   . ARG A  1 21  ? -8.381  4.997   -1.828  1.00 18.98 ? 18  ARG B O   1 
ATOM   131  C CB  . ARG A  1 21  ? -6.681  3.750   0.179   1.00 23.04 ? 18  ARG B CB  1 
ATOM   132  C CG  . ARG A  1 21  ? -6.162  3.196   1.505   1.00 23.13 ? 18  ARG B CG  1 
ATOM   133  C CD  . ARG A  1 21  ? -4.776  3.430   1.690   1.00 24.97 ? 18  ARG B CD  1 
ATOM   134  N NE  . ARG A  1 21  ? -4.350  4.831   1.697   1.00 24.49 ? 18  ARG B NE  1 
ATOM   135  C CZ  . ARG A  1 21  ? -3.859  5.499   2.702   1.00 24.27 ? 18  ARG B CZ  1 
ATOM   136  N NH1 . ARG A  1 21  ? -3.850  5.001   3.924   1.00 24.18 ? 18  ARG B NH1 1 
ATOM   137  N NH2 . ARG A  1 21  ? -3.419  6.700   2.459   1.00 24.41 ? 18  ARG B NH2 1 
ATOM   138  N N   . TYR A  1 22  ? -10.267 4.588   -0.636  1.00 18.73 ? 19  TYR B N   1 
ATOM   139  C CA  . TYR A  1 22  ? -11.143 5.139   -1.669  1.00 19.42 ? 19  TYR B CA  1 
ATOM   140  C C   . TYR A  1 22  ? -11.001 6.652   -1.807  1.00 18.51 ? 19  TYR B C   1 
ATOM   141  O O   . TYR A  1 22  ? -11.282 7.157   -2.899  1.00 18.64 ? 19  TYR B O   1 
ATOM   142  C CB  . TYR A  1 22  ? -12.615 4.757   -1.447  1.00 18.41 ? 19  TYR B CB  1 
ATOM   143  C CG  . TYR A  1 22  ? -12.774 3.250   -1.560  1.00 20.28 ? 19  TYR B CG  1 
ATOM   144  C CD1 . TYR A  1 22  ? -12.638 2.595   -2.799  1.00 20.92 ? 19  TYR B CD1 1 
ATOM   145  C CD2 . TYR A  1 22  ? -13.053 2.458   -0.420  1.00 19.21 ? 19  TYR B CD2 1 
ATOM   146  C CE1 . TYR A  1 22  ? -12.812 1.206   -2.899  1.00 21.99 ? 19  TYR B CE1 1 
ATOM   147  C CE2 . TYR A  1 22  ? -13.213 1.089   -0.519  1.00 19.85 ? 19  TYR B CE2 1 
ATOM   148  C CZ  . TYR A  1 22  ? -13.074 0.472   -1.745  1.00 22.34 ? 19  TYR B CZ  1 
ATOM   149  O OH  . TYR A  1 22  ? -13.281 -0.838  -1.772  1.00 24.68 ? 19  TYR B OH  1 
ATOM   150  N N   . ASP A  1 23  ? -10.597 7.390   -0.772  1.00 18.96 ? 20  ASP B N   1 
ATOM   151  C CA  . ASP A  1 23  ? -10.298 8.806   -0.925  1.00 20.46 ? 20  ASP B CA  1 
ATOM   152  C C   . ASP A  1 23  ? -9.139  9.006   -1.900  1.00 21.54 ? 20  ASP B C   1 
ATOM   153  O O   . ASP A  1 23  ? -9.228  9.859   -2.779  1.00 21.87 ? 20  ASP B O   1 
ATOM   154  C CB  . ASP A  1 23  ? -10.010 9.464   0.407   1.00 22.19 ? 20  ASP B CB  1 
ATOM   155  C CG  . ASP A  1 23  ? -11.170 9.538   1.375   1.00 23.47 ? 20  ASP B CG  1 
ATOM   156  O OD1 . ASP A  1 23  ? -12.310 9.681   0.914   1.00 23.06 ? 20  ASP B OD1 1 
ATOM   157  O OD2 . ASP A  1 23  ? -10.865 9.679   2.589   1.00 25.22 ? 20  ASP B OD2 1 
ATOM   158  N N   . ASP A  1 24  ? -8.062  8.211   -1.729  1.00 21.99 ? 21  ASP B N   1 
ATOM   159  C CA  . ASP A  1 24  ? -6.926  8.226   -2.651  1.00 22.04 ? 21  ASP B CA  1 
ATOM   160  C C   . ASP A  1 24  ? -7.379  7.866   -4.076  1.00 21.81 ? 21  ASP B C   1 
ATOM   161  O O   . ASP A  1 24  ? -7.012  8.553   -5.017  1.00 23.74 ? 21  ASP B O   1 
ATOM   162  C CB  . ASP A  1 24  ? -5.828  7.268   -2.218  1.00 22.44 ? 21  ASP B CB  1 
ATOM   163  C CG  . ASP A  1 24  ? -5.065  7.610   -0.934  1.00 23.45 ? 21  ASP B CG  1 
ATOM   164  O OD1 . ASP A  1 24  ? -5.250  8.751   -0.406  1.00 24.43 ? 21  ASP B OD1 1 
ATOM   165  O OD2 . ASP A  1 24  ? -4.321  6.752   -0.488  1.00 22.96 ? 21  ASP B OD2 1 
ATOM   166  N N   . MET A  1 25  ? -8.216  6.841   -4.213  1.00 20.05 ? 22  MET B N   1 
ATOM   167  C CA  . MET A  1 25  ? -8.700  6.408   -5.509  1.00 20.58 ? 22  MET B CA  1 
ATOM   168  C C   . MET A  1 25  ? -9.491  7.537   -6.189  1.00 19.29 ? 22  MET B C   1 
ATOM   169  O O   . MET A  1 25  ? -9.277  7.779   -7.368  1.00 20.05 ? 22  MET B O   1 
ATOM   170  C CB  . MET A  1 25  ? -9.598  5.185   -5.353  1.00 19.92 ? 22  MET B CB  1 
ATOM   171  C CG  . MET A  1 25  ? -9.896  4.438   -6.612  1.00 19.94 ? 22  MET B CG  1 
ATOM   172  S SD  . MET A  1 25  ? -11.036 3.124   -6.174  1.00 18.93 ? 22  MET B SD  1 
ATOM   173  C CE  . MET A  1 25  ? -11.250 2.542   -7.856  1.00 20.87 ? 22  MET B CE  1 
ATOM   174  N N   . ALA A  1 26  ? -10.359 8.223   -5.441  1.00 18.90 ? 23  ALA B N   1 
ATOM   175  C CA  . ALA A  1 26  ? -11.172 9.308   -5.954  1.00 18.98 ? 23  ALA B CA  1 
ATOM   176  C C   . ALA A  1 26  ? -10.312 10.506  -6.379  1.00 20.48 ? 23  ALA B C   1 
ATOM   177  O O   . ALA A  1 26  ? -10.572 11.085  -7.445  1.00 21.65 ? 23  ALA B O   1 
ATOM   178  C CB  . ALA A  1 26  ? -12.250 9.700   -4.947  1.00 18.51 ? 23  ALA B CB  1 
ATOM   179  N N   . ALA A  1 27  ? -9.333  10.900  -5.543  1.00 21.02 ? 24  ALA B N   1 
ATOM   180  C CA  . ALA A  1 27  ? -8.401  11.971  -5.870  1.00 22.99 ? 24  ALA B CA  1 
ATOM   181  C C   . ALA A  1 27  ? -7.671  11.680  -7.186  1.00 24.00 ? 24  ALA B C   1 
ATOM   182  O O   . ALA A  1 27  ? -7.562  12.582  -8.030  1.00 25.17 ? 24  ALA B O   1 
ATOM   183  C CB  . ALA A  1 27  ? -7.441  12.280  -4.731  1.00 24.65 ? 24  ALA B CB  1 
ATOM   184  N N   . CYS A  1 28  ? -7.240  10.424  -7.393  1.00 24.41 ? 25  CYS B N   1 
ATOM   185  C CA  . CYS A  1 28  ? -6.569  10.038  -8.630  1.00 25.02 ? 25  CYS B CA  1 
ATOM   186  C C   . CYS A  1 28  ? -7.490  10.231  -9.847  1.00 25.07 ? 25  CYS B C   1 
ATOM   187  O O   . CYS A  1 28  ? -7.099  10.866  -10.841 1.00 25.52 ? 25  CYS B O   1 
ATOM   188  C CB  . CYS A  1 28  ? -6.063  8.605   -8.590  1.00 25.15 ? 25  CYS B CB  1 
ATOM   189  S SG  . CYS A  1 28  ? -4.661  8.340   -7.481  1.00 27.76 ? 25  CYS B SG  1 
ATOM   190  N N   . MET A  1 29  ? -8.720  9.726   -9.746  1.00 23.47 ? 26  MET B N   1 
ATOM   191  C CA  . MET A  1 29  ? -9.650  9.756   -10.869 1.00 23.58 ? 26  MET B CA  1 
ATOM   192  C C   . MET A  1 29  ? -10.233 11.137  -11.140 1.00 23.97 ? 26  MET B C   1 
ATOM   193  O O   . MET A  1 29  ? -10.496 11.429  -12.298 1.00 23.62 ? 26  MET B O   1 
ATOM   194  C CB  . MET A  1 29  ? -10.733 8.699   -10.732 1.00 22.36 ? 26  MET B CB  1 
ATOM   195  C CG  . MET A  1 29  ? -10.198 7.277   -10.759 1.00 23.10 ? 26  MET B CG  1 
ATOM   196  S SD  . MET A  1 29  ? -8.998  6.939   -12.059 1.00 24.88 ? 26  MET B SD  1 
ATOM   197  C CE  . MET A  1 29  ? -9.890  7.294   -13.580 1.00 24.74 ? 26  MET B CE  1 
ATOM   198  N N   . LYS A  1 30  ? -10.380 11.970  -10.110 1.00 24.97 ? 27  LYS B N   1 
ATOM   199  C CA  . LYS A  1 30  ? -10.711 13.378  -10.297 1.00 26.26 ? 27  LYS B CA  1 
ATOM   200  C C   . LYS A  1 30  ? -9.601  14.090  -11.083 1.00 28.54 ? 27  LYS B C   1 
ATOM   201  O O   . LYS A  1 30  ? -9.906  14.790  -12.048 1.00 28.18 ? 27  LYS B O   1 
ATOM   202  C CB  . LYS A  1 30  ? -10.929 14.028  -8.930  1.00 28.00 ? 27  LYS B CB  1 
ATOM   203  C CG  . LYS A  1 30  ? -11.226 15.529  -8.846  1.00 30.53 ? 27  LYS B CG  1 
ATOM   204  C CD  . LYS A  1 30  ? -11.602 15.945  -7.424  1.00 32.31 ? 27  LYS B CD  1 
ATOM   205  C CE  . LYS A  1 30  ? -12.317 17.251  -7.293  1.00 35.68 ? 27  LYS B CE  1 
ATOM   206  N NZ  . LYS A  1 30  ? -11.400 18.345  -7.442  1.00 37.78 ? 27  LYS B NZ  1 
ATOM   207  N N   . SER A  1 31  ? -8.331  13.827  -10.731 1.00 28.77 ? 28  SER B N   1 
ATOM   208  C CA  . SER A  1 31  ? -7.206  14.418  -11.447 1.00 31.74 ? 28  SER B CA  1 
ATOM   209  C C   . SER A  1 31  ? -7.180  13.992  -12.917 1.00 31.37 ? 28  SER B C   1 
ATOM   210  O O   . SER A  1 31  ? -7.038  14.865  -13.768 1.00 32.06 ? 28  SER B O   1 
ATOM   211  C CB  . SER A  1 31  ? -5.913  14.117  -10.754 1.00 34.01 ? 28  SER B CB  1 
ATOM   212  O OG  . SER A  1 31  ? -5.896  14.858  -9.538  1.00 36.87 ? 28  SER B OG  1 
ATOM   213  N N   . VAL A  1 32  ? -7.427  12.697  -13.181 1.00 29.71 ? 29  VAL B N   1 
ATOM   214  C CA  . VAL A  1 32  ? -7.505  12.156  -14.531 1.00 29.87 ? 29  VAL B CA  1 
ATOM   215  C C   . VAL A  1 32  ? -8.618  12.870  -15.307 1.00 29.86 ? 29  VAL B C   1 
ATOM   216  O O   . VAL A  1 32  ? -8.352  13.389  -16.385 1.00 31.96 ? 29  VAL B O   1 
ATOM   217  C CB  . VAL A  1 32  ? -7.697  10.627  -14.553 1.00 29.33 ? 29  VAL B CB  1 
ATOM   218  C CG1 . VAL A  1 32  ? -7.989  10.075  -15.958 1.00 29.98 ? 29  VAL B CG1 1 
ATOM   219  C CG2 . VAL A  1 32  ? -6.508  9.886   -13.933 1.00 29.77 ? 29  VAL B CG2 1 
ATOM   220  N N   . THR A  1 33  ? -9.823  12.924  -14.740 1.00 28.71 ? 30  THR B N   1 
ATOM   221  C CA  . THR A  1 33  ? -10.979 13.584  -15.375 1.00 28.50 ? 30  THR B CA  1 
ATOM   222  C C   . THR A  1 33  ? -10.652 15.031  -15.756 1.00 30.06 ? 30  THR B C   1 
ATOM   223  O O   . THR A  1 33  ? -10.874 15.419  -16.918 1.00 30.88 ? 30  THR B O   1 
ATOM   224  C CB  . THR A  1 33  ? -12.201 13.509  -14.457 1.00 27.19 ? 30  THR B CB  1 
ATOM   225  O OG1 . THR A  1 33  ? -12.463 12.105  -14.292 1.00 25.27 ? 30  THR B OG1 1 
ATOM   226  C CG2 . THR A  1 33  ? -13.405 14.244  -15.043 1.00 26.69 ? 30  THR B CG2 1 
ATOM   227  N N   . GLU A  1 34  ? -10.061 15.779  -14.805 1.00 30.19 ? 31  GLU B N   1 
ATOM   228  C CA  . GLU A  1 34  ? -9.695  17.172  -14.988 1.00 33.21 ? 31  GLU B CA  1 
ATOM   229  C C   . GLU A  1 34  ? -8.657  17.409  -16.095 1.00 36.07 ? 31  GLU B C   1 
ATOM   230  O O   . GLU A  1 34  ? -8.532  18.549  -16.559 1.00 36.56 ? 31  GLU B O   1 
ATOM   231  C CB  . GLU A  1 34  ? -9.239  17.780  -13.660 1.00 34.74 ? 31  GLU B CB  1 
ATOM   232  C CG  . GLU A  1 34  ? -10.386 18.047  -12.697 1.00 34.31 ? 31  GLU B CG  1 
ATOM   233  C CD  . GLU A  1 34  ? -10.026 18.297  -11.242 1.00 34.55 ? 31  GLU B CD  1 
ATOM   234  O OE1 . GLU A  1 34  ? -8.887  18.072  -10.812 1.00 34.23 ? 31  GLU B OE1 1 
ATOM   235  O OE2 . GLU A  1 34  ? -10.937 18.725  -10.514 1.00 34.24 ? 31  GLU B OE2 1 
ATOM   236  N N   . GLN A  1 35  ? -7.881  16.390  -16.520 1.00 37.09 ? 32  GLN B N   1 
ATOM   237  C CA  . GLN A  1 35  ? -6.982  16.547  -17.661 1.00 38.85 ? 32  GLN B CA  1 
ATOM   238  C C   . GLN A  1 35  ? -7.746  16.724  -18.976 1.00 39.10 ? 32  GLN B C   1 
ATOM   239  O O   . GLN A  1 35  ? -7.148  17.163  -19.958 1.00 41.00 ? 32  GLN B O   1 
ATOM   240  C CB  . GLN A  1 35  ? -6.039  15.380  -17.886 1.00 39.74 ? 32  GLN B CB  1 
ATOM   241  C CG  . GLN A  1 35  ? -5.154  15.066  -16.696 1.00 42.19 ? 32  GLN B CG  1 
ATOM   242  C CD  . GLN A  1 35  ? -4.029  14.114  -17.041 1.00 48.14 ? 32  GLN B CD  1 
ATOM   243  O OE1 . GLN A  1 35  ? -4.026  13.494  -18.115 1.00 52.50 ? 32  GLN B OE1 1 
ATOM   244  N NE2 . GLN A  1 35  ? -3.041  14.020  -16.153 1.00 48.58 ? 32  GLN B NE2 1 
ATOM   245  N N   . GLY A  1 36  ? -9.023  16.331  -19.011 1.00 37.68 ? 33  GLY B N   1 
ATOM   246  C CA  . GLY A  1 36  ? -9.957  16.747  -20.041 1.00 39.47 ? 33  GLY B CA  1 
ATOM   247  C C   . GLY A  1 36  ? -10.097 15.732  -21.172 1.00 40.03 ? 33  GLY B C   1 
ATOM   248  O O   . GLY A  1 36  ? -10.956 15.947  -22.019 1.00 45.23 ? 33  GLY B O   1 
ATOM   249  N N   . ALA A  1 37  ? -9.291  14.649  -21.199 1.00 37.47 ? 34  ALA B N   1 
ATOM   250  C CA  . ALA A  1 37  ? -9.440  13.562  -22.149 1.00 36.05 ? 34  ALA B CA  1 
ATOM   251  C C   . ALA A  1 37  ? -10.612 12.678  -21.724 1.00 33.71 ? 34  ALA B C   1 
ATOM   252  O O   . ALA A  1 37  ? -10.962 12.571  -20.523 1.00 29.39 ? 34  ALA B O   1 
ATOM   253  C CB  . ALA A  1 37  ? -8.138  12.791  -22.314 1.00 36.88 ? 34  ALA B CB  1 
ATOM   254  N N   . GLU A  1 38  ? -11.262 12.080  -22.743 1.00 33.53 ? 35  GLU B N   1 
ATOM   255  C CA  . GLU A  1 38  ? -12.323 11.117  -22.492 1.00 33.21 ? 35  GLU B CA  1 
ATOM   256  C C   . GLU A  1 38  ? -11.736 9.900   -21.769 1.00 32.00 ? 35  GLU B C   1 
ATOM   257  O O   . GLU A  1 38  ? -10.598 9.499   -22.081 1.00 33.15 ? 35  GLU B O   1 
ATOM   258  C CB  . GLU A  1 38  ? -12.964 10.613  -23.780 1.00 34.04 ? 35  GLU B CB  1 
ATOM   259  C CG  . GLU A  1 38  ? -13.990 11.569  -24.366 1.00 35.90 ? 35  GLU B CG  1 
ATOM   260  C CD  . GLU A  1 38  ? -14.504 10.994  -25.686 1.00 37.05 ? 35  GLU B CD  1 
ATOM   261  O OE1 . GLU A  1 38  ? -15.391 10.133  -25.601 1.00 37.37 ? 35  GLU B OE1 1 
ATOM   262  O OE2 . GLU A  1 38  ? -13.937 11.303  -26.753 1.00 40.00 ? 35  GLU B OE2 1 
ATOM   263  N N   . LEU A  1 39  ? -12.521 9.355   -20.829 1.00 29.97 ? 36  LEU B N   1 
ATOM   264  C CA  . LEU A  1 39  ? -12.159 8.165   -20.079 1.00 28.98 ? 36  LEU B CA  1 
ATOM   265  C C   . LEU A  1 39  ? -12.454 6.906   -20.892 1.00 29.71 ? 36  LEU B C   1 
ATOM   266  O O   . LEU A  1 39  ? -13.443 6.843   -21.613 1.00 28.96 ? 36  LEU B O   1 
ATOM   267  C CB  . LEU A  1 39  ? -12.902 8.121   -18.750 1.00 26.64 ? 36  LEU B CB  1 
ATOM   268  C CG  . LEU A  1 39  ? -12.774 9.351   -17.849 1.00 26.48 ? 36  LEU B CG  1 
ATOM   269  C CD1 . LEU A  1 39  ? -13.538 9.085   -16.546 1.00 24.46 ? 36  LEU B CD1 1 
ATOM   270  C CD2 . LEU A  1 39  ? -11.351 9.763   -17.558 1.00 27.00 ? 36  LEU B CD2 1 
ATOM   271  N N   . SER A  1 40  ? -11.585 5.896   -20.761 1.00 29.69 ? 37  SER B N   1 
ATOM   272  C CA  . SER A  1 40  ? -11.874 4.515   -21.143 1.00 28.44 ? 37  SER B CA  1 
ATOM   273  C C   . SER A  1 40  ? -12.919 3.884   -20.222 1.00 25.91 ? 37  SER B C   1 
ATOM   274  O O   . SER A  1 40  ? -13.248 4.423   -19.147 1.00 23.91 ? 37  SER B O   1 
ATOM   275  C CB  . SER A  1 40  ? -10.614 3.666   -21.143 1.00 29.52 ? 37  SER B CB  1 
ATOM   276  O OG  . SER A  1 40  ? -10.239 3.350   -19.802 1.00 28.05 ? 37  SER B OG  1 
ATOM   277  N N   . ASN A  1 41  ? -13.428 2.714   -20.636 1.00 26.85 ? 38  ASN B N   1 
ATOM   278  C CA  . ASN A  1 41  ? -14.375 1.949   -19.812 1.00 28.81 ? 38  ASN B CA  1 
ATOM   279  C C   . ASN A  1 41  ? -13.779 1.611   -18.437 1.00 25.20 ? 38  ASN B C   1 
ATOM   280  O O   . ASN A  1 41  ? -14.451 1.762   -17.422 1.00 24.73 ? 38  ASN B O   1 
ATOM   281  C CB  . ASN A  1 41  ? -14.851 0.683   -20.520 1.00 32.88 ? 38  ASN B CB  1 
ATOM   282  C CG  . ASN A  1 41  ? -15.821 0.964   -21.654 1.00 41.99 ? 38  ASN B CG  1 
ATOM   283  O OD1 . ASN A  1 41  ? -16.095 2.113   -22.017 1.00 46.20 ? 38  ASN B OD1 1 
ATOM   284  N ND2 . ASN A  1 41  ? -16.343 -0.087  -22.265 1.00 47.19 ? 38  ASN B ND2 1 
ATOM   285  N N   . GLU A  1 42  ? -12.511 1.165   -18.422 1.00 27.44 ? 39  GLU B N   1 
ATOM   286  C CA  . GLU A  1 42  ? -11.801 0.870   -17.175 1.00 27.98 ? 39  GLU B CA  1 
ATOM   287  C C   . GLU A  1 42  ? -11.720 2.092   -16.241 1.00 24.40 ? 39  GLU B C   1 
ATOM   288  O O   . GLU A  1 42  ? -11.998 1.969   -15.056 1.00 22.73 ? 39  GLU B O   1 
ATOM   289  C CB  . GLU A  1 42  ? -10.417 0.310   -17.517 1.00 31.54 ? 39  GLU B CB  1 
ATOM   290  C CG  . GLU A  1 42  ? -9.704  -0.278  -16.308 1.00 36.54 ? 39  GLU B CG  1 
ATOM   291  C CD  . GLU A  1 42  ? -8.310  -0.782  -16.648 1.00 40.41 ? 39  GLU B CD  1 
ATOM   292  O OE1 . GLU A  1 42  ? -7.502  -0.029  -17.266 1.00 39.38 ? 39  GLU B OE1 1 
ATOM   293  O OE2 . GLU A  1 42  ? -8.076  -1.930  -16.233 1.00 47.53 ? 39  GLU B OE2 1 
ATOM   294  N N   . GLU A  1 43  ? -11.413 3.264   -16.796 1.00 22.50 ? 40  GLU B N   1 
ATOM   295  C CA  . GLU A  1 43  ? -11.290 4.508   -16.064 1.00 22.19 ? 40  GLU B CA  1 
ATOM   296  C C   . GLU A  1 43  ? -12.632 4.986   -15.545 1.00 21.24 ? 40  GLU B C   1 
ATOM   297  O O   . GLU A  1 43  ? -12.693 5.431   -14.407 1.00 20.26 ? 40  GLU B O   1 
ATOM   298  C CB  . GLU A  1 43  ? -10.602 5.549   -16.947 1.00 23.80 ? 40  GLU B CB  1 
ATOM   299  C CG  . GLU A  1 43  ? -9.162  5.228   -17.289 1.00 25.78 ? 40  GLU B CG  1 
ATOM   300  C CD  . GLU A  1 43  ? -8.631  5.907   -18.552 1.00 29.39 ? 40  GLU B CD  1 
ATOM   301  O OE1 . GLU A  1 43  ? -9.312  6.776   -19.177 1.00 29.43 ? 40  GLU B OE1 1 
ATOM   302  O OE2 . GLU A  1 43  ? -7.494  5.551   -18.914 1.00 30.22 ? 40  GLU B OE2 1 
ATOM   303  N N   . ARG A  1 44  ? -13.712 4.830   -16.330 1.00 20.72 ? 41  ARG B N   1 
ATOM   304  C CA  . ARG A  1 44  ? -15.046 5.106   -15.851 1.00 21.25 ? 41  ARG B CA  1 
ATOM   305  C C   . ARG A  1 44  ? -15.350 4.251   -14.636 1.00 19.41 ? 41  ARG B C   1 
ATOM   306  O O   . ARG A  1 44  ? -15.871 4.769   -13.647 1.00 19.38 ? 41  ARG B O   1 
ATOM   307  C CB  . ARG A  1 44  ? -16.202 4.798   -16.831 1.00 22.99 ? 41  ARG B CB  1 
ATOM   308  C CG  . ARG A  1 44  ? -16.427 6.012   -17.698 1.00 25.71 ? 41  ARG B CG  1 
ATOM   309  C CD  . ARG A  1 44  ? -17.591 5.771   -18.681 1.00 25.54 ? 41  ARG B CD  1 
ATOM   310  N NE  . ARG A  1 44  ? -17.133 5.038   -19.858 1.00 26.22 ? 41  ARG B NE  1 
ATOM   311  C CZ  . ARG A  1 44  ? -16.360 5.504   -20.824 1.00 30.18 ? 41  ARG B CZ  1 
ATOM   312  N NH1 . ARG A  1 44  ? -16.057 6.783   -20.858 1.00 30.85 ? 41  ARG B NH1 1 
ATOM   313  N NH2 . ARG A  1 44  ? -15.933 4.727   -21.807 1.00 30.53 ? 41  ARG B NH2 1 
ATOM   314  N N   . ASN A  1 45  ? -15.062 2.948   -14.736 1.00 20.11 ? 42  ASN B N   1 
ATOM   315  C CA  . ASN A  1 45  ? -15.331 2.035   -13.627 1.00 17.90 ? 42  ASN B CA  1 
ATOM   316  C C   . ASN A  1 45  ? -14.528 2.454   -12.395 1.00 17.28 ? 42  ASN B C   1 
ATOM   317  O O   . ASN A  1 45  ? -15.088 2.372   -11.308 1.00 17.31 ? 42  ASN B O   1 
ATOM   318  C CB  . ASN A  1 45  ? -15.097 0.585   -13.993 1.00 20.59 ? 42  ASN B CB  1 
ATOM   319  C CG  . ASN A  1 45  ? -16.199 0.010   -14.856 1.00 21.36 ? 42  ASN B CG  1 
ATOM   320  O OD1 . ASN A  1 45  ? -17.340 0.464   -14.839 1.00 21.59 ? 42  ASN B OD1 1 
ATOM   321  N ND2 . ASN A  1 45  ? -15.830 -0.928  -15.704 1.00 23.03 ? 42  ASN B ND2 1 
ATOM   322  N N   . LEU A  1 46  ? -13.266 2.862   -12.551 1.00 17.54 ? 43  LEU B N   1 
ATOM   323  C CA  . LEU A  1 46  ? -12.459 3.359   -11.427 1.00 18.26 ? 43  LEU B CA  1 
ATOM   324  C C   . LEU A  1 46  ? -13.092 4.588   -10.782 1.00 18.53 ? 43  LEU B C   1 
ATOM   325  O O   . LEU A  1 46  ? -13.178 4.665   -9.561  1.00 18.50 ? 43  LEU B O   1 
ATOM   326  C CB  . LEU A  1 46  ? -11.017 3.597   -11.847 1.00 19.52 ? 43  LEU B CB  1 
ATOM   327  C CG  . LEU A  1 46  ? -10.237 2.333   -12.234 1.00 19.72 ? 43  LEU B CG  1 
ATOM   328  C CD1 . LEU A  1 46  ? -8.992  2.724   -12.992 1.00 22.09 ? 43  LEU B CD1 1 
ATOM   329  C CD2 . LEU A  1 46  ? -9.899  1.448   -11.046 1.00 19.50 ? 43  LEU B CD2 1 
ATOM   330  N N   . LEU A  1 47  ? -13.501 5.575   -11.601 1.00 18.83 ? 44  LEU B N   1 
ATOM   331  C CA  . LEU A  1 47  ? -14.177 6.753   -11.097 1.00 19.37 ? 44  LEU B CA  1 
ATOM   332  C C   . LEU A  1 47  ? -15.457 6.392   -10.341 1.00 17.35 ? 44  LEU B C   1 
ATOM   333  O O   . LEU A  1 47  ? -15.673 6.913   -9.254  1.00 15.58 ? 44  LEU B O   1 
ATOM   334  C CB  . LEU A  1 47  ? -14.510 7.686   -12.275 1.00 20.74 ? 44  LEU B CB  1 
ATOM   335  C CG  . LEU A  1 47  ? -15.221 8.982   -11.916 1.00 21.17 ? 44  LEU B CG  1 
ATOM   336  C CD1 . LEU A  1 47  ? -14.249 9.932   -11.218 1.00 25.48 ? 44  LEU B CD1 1 
ATOM   337  C CD2 . LEU A  1 47  ? -15.865 9.605   -13.148 1.00 22.84 ? 44  LEU B CD2 1 
ATOM   338  N N   . SER A  1 48  ? -16.256 5.508   -10.922 1.00 16.53 ? 45  SER B N   1 
ATOM   339  C CA  . SER A  1 48  ? -17.524 5.097   -10.368 1.00 17.21 ? 45  SER B CA  1 
ATOM   340  C C   . SER A  1 48  ? -17.348 4.396   -9.012  1.00 17.22 ? 45  SER B C   1 
ATOM   341  O O   . SER A  1 48  ? -18.034 4.730   -8.047  1.00 16.99 ? 45  SER B O   1 
ATOM   342  C CB  . SER A  1 48  ? -18.268 4.214   -11.344 1.00 17.76 ? 45  SER B CB  1 
ATOM   343  O OG  . SER A  1 48  ? -19.546 3.850   -10.832 1.00 16.87 ? 45  SER B OG  1 
ATOM   344  N N   . VAL A  1 49  ? -16.390 3.456   -8.966  1.00 15.31 ? 46  VAL B N   1 
ATOM   345  C CA  . VAL A  1 49  ? -16.122 2.722   -7.731  1.00 15.65 ? 46  VAL B CA  1 
ATOM   346  C C   . VAL A  1 49  ? -15.646 3.680   -6.638  1.00 15.44 ? 46  VAL B C   1 
ATOM   347  O O   . VAL A  1 49  ? -16.073 3.524   -5.481  1.00 14.87 ? 46  VAL B O   1 
ATOM   348  C CB  . VAL A  1 49  ? -15.175 1.532   -8.017  1.00 16.15 ? 46  VAL B CB  1 
ATOM   349  C CG1 . VAL A  1 49  ? -14.608 0.969   -6.700  1.00 16.36 ? 46  VAL B CG1 1 
ATOM   350  C CG2 . VAL A  1 49  ? -15.843 0.414   -8.805  1.00 16.38 ? 46  VAL B CG2 1 
ATOM   351  N N   . ALA A  1 50  ? -14.708 4.595   -6.987  1.00 16.81 ? 47  ALA B N   1 
ATOM   352  C CA  . ALA A  1 50  ? -14.095 5.461   -6.014  1.00 17.89 ? 47  ALA B CA  1 
ATOM   353  C C   . ALA A  1 50  ? -15.160 6.291   -5.311  1.00 16.85 ? 47  ALA B C   1 
ATOM   354  O O   . ALA A  1 50  ? -15.303 6.243   -4.084  1.00 16.55 ? 47  ALA B O   1 
ATOM   355  C CB  . ALA A  1 50  ? -13.048 6.350   -6.672  1.00 19.81 ? 47  ALA B CB  1 
ATOM   356  N N   . TYR A  1 51  ? -15.976 7.006   -6.101  1.00 16.45 ? 48  TYR B N   1 
ATOM   357  C CA  . TYR A  1 51  ? -17.007 7.872   -5.531  1.00 16.95 ? 48  TYR B CA  1 
ATOM   358  C C   . TYR A  1 51  ? -18.139 7.100   -4.852  1.00 17.25 ? 48  TYR B C   1 
ATOM   359  O O   . TYR A  1 51  ? -18.677 7.630   -3.875  1.00 17.82 ? 48  TYR B O   1 
ATOM   360  C CB  . TYR A  1 51  ? -17.439 8.902   -6.590  1.00 17.46 ? 48  TYR B CB  1 
ATOM   361  C CG  . TYR A  1 51  ? -16.479 10.080  -6.675  1.00 19.56 ? 48  TYR B CG  1 
ATOM   362  C CD1 . TYR A  1 51  ? -16.450 11.045  -5.656  1.00 20.55 ? 48  TYR B CD1 1 
ATOM   363  C CD2 . TYR A  1 51  ? -15.544 10.198  -7.697  1.00 19.81 ? 48  TYR B CD2 1 
ATOM   364  C CE1 . TYR A  1 51  ? -15.614 12.159  -5.722  1.00 22.25 ? 48  TYR B CE1 1 
ATOM   365  C CE2 . TYR A  1 51  ? -14.692 11.298  -7.761  1.00 22.28 ? 48  TYR B CE2 1 
ATOM   366  C CZ  . TYR A  1 51  ? -14.716 12.270  -6.773  1.00 21.92 ? 48  TYR B CZ  1 
ATOM   367  O OH  . TYR A  1 51  ? -13.874 13.309  -6.826  1.00 22.27 ? 48  TYR B OH  1 
ATOM   368  N N   A LYS A  1 52  ? -18.497 5.897   -5.336  0.50 16.68 ? 49  LYS B N   1 
ATOM   369  N N   B LYS A  1 52  ? -18.497 5.899   -5.336  0.50 17.53 ? 49  LYS B N   1 
ATOM   370  C CA  A LYS A  1 52  ? -19.541 5.105   -4.694  0.50 17.00 ? 49  LYS B CA  1 
ATOM   371  C CA  B LYS A  1 52  ? -19.536 5.102   -4.697  0.50 18.65 ? 49  LYS B CA  1 
ATOM   372  C C   A LYS A  1 52  ? -19.165 4.807   -3.244  0.50 16.87 ? 49  LYS B C   1 
ATOM   373  C C   B LYS A  1 52  ? -19.165 4.804   -3.245  0.50 17.73 ? 49  LYS B C   1 
ATOM   374  O O   A LYS A  1 52  ? -20.000 4.912   -2.342  0.50 16.05 ? 49  LYS B O   1 
ATOM   375  O O   B LYS A  1 52  ? -20.001 4.913   -2.344  0.50 16.76 ? 49  LYS B O   1 
ATOM   376  C CB  A LYS A  1 52  ? -19.850 3.787   -5.411  0.50 18.56 ? 49  LYS B CB  1 
ATOM   377  C CB  B LYS A  1 52  ? -19.789 3.810   -5.478  0.50 22.13 ? 49  LYS B CB  1 
ATOM   378  C CG  A LYS A  1 52  ? -21.150 3.150   -4.839  0.50 19.25 ? 49  LYS B CG  1 
ATOM   379  C CG  B LYS A  1 52  ? -20.943 2.995   -4.898  0.50 25.25 ? 49  LYS B CG  1 
ATOM   380  C CD  A LYS A  1 52  ? -21.991 2.221   -5.732  0.50 20.84 ? 49  LYS B CD  1 
ATOM   381  C CD  B LYS A  1 52  ? -22.006 2.528   -5.894  0.50 29.01 ? 49  LYS B CD  1 
ATOM   382  C CE  A LYS A  1 52  ? -23.109 1.466   -4.993  0.50 18.17 ? 49  LYS B CE  1 
ATOM   383  C CE  B LYS A  1 52  ? -23.358 2.348   -5.209  0.50 26.79 ? 49  LYS B CE  1 
ATOM   384  N NZ  A LYS A  1 52  ? -23.499 0.163   -5.553  0.50 16.98 ? 49  LYS B NZ  1 
ATOM   385  N NZ  B LYS A  1 52  ? -23.839 3.682   -4.865  0.50 25.28 ? 49  LYS B NZ  1 
ATOM   386  N N   . ASN A  1 53  ? -17.888 4.458   -3.045  1.00 16.12 ? 50  ASN B N   1 
ATOM   387  C CA  . ASN A  1 53  ? -17.369 4.147   -1.724  1.00 16.76 ? 50  ASN B CA  1 
ATOM   388  C C   . ASN A  1 53  ? -17.243 5.413   -0.867  1.00 16.12 ? 50  ASN B C   1 
ATOM   389  O O   . ASN A  1 53  ? -17.530 5.346   0.335   1.00 16.50 ? 50  ASN B O   1 
ATOM   390  C CB  . ASN A  1 53  ? -16.086 3.318   -1.847  1.00 16.79 ? 50  ASN B CB  1 
ATOM   391  C CG  . ASN A  1 53  ? -16.402 1.909   -2.271  1.00 18.77 ? 50  ASN B CG  1 
ATOM   392  O OD1 . ASN A  1 53  ? -16.252 1.533   -3.446  1.00 21.31 ? 50  ASN B OD1 1 
ATOM   393  N ND2 . ASN A  1 53  ? -16.829 1.094   -1.324  1.00 18.15 ? 50  ASN B ND2 1 
ATOM   394  N N   . VAL A  1 54  ? -16.786 6.548   -1.465  1.00 14.94 ? 51  VAL B N   1 
ATOM   395  C CA  . VAL A  1 54  ? -16.542 7.752   -0.695  1.00 15.84 ? 51  VAL B CA  1 
ATOM   396  C C   . VAL A  1 54  ? -17.915 8.281   -0.238  1.00 15.68 ? 51  VAL B C   1 
ATOM   397  O O   . VAL A  1 54  ? -18.098 8.599   0.944   1.00 16.07 ? 51  VAL B O   1 
ATOM   398  C CB  . VAL A  1 54  ? -15.723 8.806   -1.492  1.00 15.69 ? 51  VAL B CB  1 
ATOM   399  C CG1 . VAL A  1 54  ? -15.722 10.200  -0.850  1.00 16.49 ? 51  VAL B CG1 1 
ATOM   400  C CG2 . VAL A  1 54  ? -14.302 8.338   -1.724  1.00 16.38 ? 51  VAL B CG2 1 
ATOM   401  N N   . VAL A  1 55  ? -18.904 8.331   -1.153  1.00 16.28 ? 52  VAL B N   1 
ATOM   402  C CA  . VAL A  1 55  ? -20.220 8.829   -0.759  1.00 16.14 ? 52  VAL B CA  1 
ATOM   403  C C   . VAL A  1 55  ? -20.924 7.802   0.142   1.00 15.66 ? 52  VAL B C   1 
ATOM   404  O O   . VAL A  1 55  ? -21.645 8.231   1.049   1.00 18.13 ? 52  VAL B O   1 
ATOM   405  C CB  . VAL A  1 55  ? -21.074 9.286   -1.949  1.00 15.42 ? 52  VAL B CB  1 
ATOM   406  C CG1 . VAL A  1 55  ? -21.738 8.139   -2.714  1.00 14.71 ? 52  VAL B CG1 1 
ATOM   407  C CG2 . VAL A  1 55  ? -22.152 10.275  -1.492  1.00 16.61 ? 52  VAL B CG2 1 
ATOM   408  N N   . GLY A  1 56  ? -20.759 6.496   -0.149  1.00 15.04 ? 53  GLY B N   1 
ATOM   409  C CA  . GLY A  1 56  ? -21.422 5.430   0.589   1.00 15.87 ? 53  GLY B CA  1 
ATOM   410  C C   . GLY A  1 56  ? -21.138 5.455   2.084   1.00 16.18 ? 53  GLY B C   1 
ATOM   411  O O   . GLY A  1 56  ? -22.032 5.107   2.842   1.00 16.28 ? 53  GLY B O   1 
ATOM   412  N N   . ALA A  1 57  ? -19.889 5.762   2.485   1.00 18.00 ? 54  ALA B N   1 
ATOM   413  C CA  . ALA A  1 57  ? -19.495 5.899   3.897   1.00 17.87 ? 54  ALA B CA  1 
ATOM   414  C C   . ALA A  1 57  ? -20.382 6.931   4.606   1.00 17.09 ? 54  ALA B C   1 
ATOM   415  O O   . ALA A  1 57  ? -20.844 6.685   5.727   1.00 17.85 ? 54  ALA B O   1 
ATOM   416  C CB  . ALA A  1 57  ? -18.020 6.271   4.008   1.00 18.43 ? 54  ALA B CB  1 
ATOM   417  N N   . ARG A  1 58  ? -20.652 8.047   3.933   1.00 17.21 ? 55  ARG B N   1 
ATOM   418  C CA  . ARG A  1 58  ? -21.515 9.113   4.448   1.00 17.89 ? 55  ARG B CA  1 
ATOM   419  C C   . ARG A  1 58  ? -22.995 8.727   4.407   1.00 17.44 ? 55  ARG B C   1 
ATOM   420  O O   . ARG A  1 58  ? -23.718 9.009   5.354   1.00 17.91 ? 55  ARG B O   1 
ATOM   421  C CB  . ARG A  1 58  ? -21.276 10.466  3.749   1.00 19.52 ? 55  ARG B CB  1 
ATOM   422  C CG  . ARG A  1 58  ? -20.065 11.247  4.255   1.00 20.21 ? 55  ARG B CG  1 
ATOM   423  C CD  . ARG A  1 58  ? -18.808 10.532  3.872   1.00 19.25 ? 55  ARG B CD  1 
ATOM   424  N NE  . ARG A  1 58  ? -17.605 11.334  4.040   1.00 19.51 ? 55  ARG B NE  1 
ATOM   425  C CZ  . ARG A  1 58  ? -16.423 10.825  3.764   1.00 19.99 ? 55  ARG B CZ  1 
ATOM   426  N NH1 . ARG A  1 58  ? -16.229 9.839   2.897   1.00 19.29 ? 55  ARG B NH1 1 
ATOM   427  N NH2 . ARG A  1 58  ? -15.382 11.367  4.311   1.00 22.01 ? 55  ARG B NH2 1 
ATOM   428  N N   . ARG A  1 59  ? -23.448 8.052   3.362   1.00 17.07 ? 56  ARG B N   1 
ATOM   429  C CA  . ARG A  1 59  ? -24.836 7.584   3.284   1.00 16.90 ? 56  ARG B CA  1 
ATOM   430  C C   . ARG A  1 59  ? -25.191 6.624   4.422   1.00 17.60 ? 56  ARG B C   1 
ATOM   431  O O   . ARG A  1 59  ? -26.210 6.852   5.086   1.00 18.72 ? 56  ARG B O   1 
ATOM   432  C CB  . ARG A  1 59  ? -25.125 6.946   1.936   1.00 16.76 ? 56  ARG B CB  1 
ATOM   433  C CG  . ARG A  1 59  ? -25.012 7.939   0.780   1.00 17.43 ? 56  ARG B CG  1 
ATOM   434  C CD  . ARG A  1 59  ? -25.056 7.171   -0.532  1.00 17.23 ? 56  ARG B CD  1 
ATOM   435  N NE  . ARG A  1 59  ? -26.414 6.654   -0.770  1.00 17.88 ? 56  ARG B NE  1 
ATOM   436  C CZ  . ARG A  1 59  ? -26.727 5.586   -1.511  1.00 17.90 ? 56  ARG B CZ  1 
ATOM   437  N NH1 . ARG A  1 59  ? -25.788 4.838   -2.093  1.00 16.26 ? 56  ARG B NH1 1 
ATOM   438  N NH2 . ARG A  1 59  ? -28.009 5.223   -1.609  1.00 15.65 ? 56  ARG B NH2 1 
ATOM   439  N N   A SER A  1 60  ? -24.312 5.628   4.673   0.50 17.22 ? 57  SER B N   1 
ATOM   440  N N   B SER A  1 60  ? -24.311 5.631   4.683   0.50 17.22 ? 57  SER B N   1 
ATOM   441  C CA  A SER A  1 60  ? -24.399 4.694   5.797   0.50 17.98 ? 57  SER B CA  1 
ATOM   442  C CA  B SER A  1 60  ? -24.439 4.701   5.805   0.50 17.97 ? 57  SER B CA  1 
ATOM   443  C C   A SER A  1 60  ? -24.462 5.417   7.143   0.50 18.57 ? 57  SER B C   1 
ATOM   444  C C   B SER A  1 60  ? -24.474 5.425   7.148   0.50 18.57 ? 57  SER B C   1 
ATOM   445  O O   A SER A  1 60  ? -25.347 5.134   7.971   0.50 19.79 ? 57  SER B O   1 
ATOM   446  O O   B SER A  1 60  ? -25.347 5.138   7.983   0.50 19.78 ? 57  SER B O   1 
ATOM   447  C CB  A SER A  1 60  ? -23.225 3.699   5.755   0.50 18.15 ? 57  SER B CB  1 
ATOM   448  C CB  B SER A  1 60  ? -23.330 3.657   5.823   0.50 18.20 ? 57  SER B CB  1 
ATOM   449  O OG  A SER A  1 60  ? -23.498 2.664   4.820   0.50 18.81 ? 57  SER B OG  1 
ATOM   450  O OG  B SER A  1 60  ? -23.655 2.685   6.808   0.50 19.88 ? 57  SER B OG  1 
ATOM   451  N N   . ALA A  1 61  ? -23.498 6.331   7.354   1.00 18.41 ? 58  ALA B N   1 
ATOM   452  C CA  . ALA A  1 61  ? -23.372 7.057   8.622   1.00 19.47 ? 58  ALA B CA  1 
ATOM   453  C C   . ALA A  1 61  ? -24.602 7.947   8.838   1.00 19.62 ? 58  ALA B C   1 
ATOM   454  O O   . ALA A  1 61  ? -25.156 7.969   9.937   1.00 19.80 ? 58  ALA B O   1 
ATOM   455  C CB  . ALA A  1 61  ? -22.133 7.894   8.633   1.00 19.83 ? 58  ALA B CB  1 
ATOM   456  N N   . TRP A  1 62  ? -25.056 8.571   7.739   1.00 18.98 ? 59  TRP B N   1 
ATOM   457  C CA  . TRP A  1 62  ? -26.248 9.414   7.779   1.00 20.39 ? 59  TRP B CA  1 
ATOM   458  C C   . TRP A  1 62  ? -27.501 8.664   8.238   1.00 20.61 ? 59  TRP B C   1 
ATOM   459  O O   . TRP A  1 62  ? -28.244 9.182   9.091   1.00 21.90 ? 59  TRP B O   1 
ATOM   460  C CB  . TRP A  1 62  ? -26.476 10.090  6.416   1.00 20.14 ? 59  TRP B CB  1 
ATOM   461  C CG  . TRP A  1 62  ? -27.562 11.127  6.480   1.00 21.08 ? 59  TRP B CG  1 
ATOM   462  C CD1 . TRP A  1 62  ? -27.431 12.448  6.806   1.00 22.89 ? 59  TRP B CD1 1 
ATOM   463  C CD2 . TRP A  1 62  ? -28.971 10.896  6.261   1.00 21.22 ? 59  TRP B CD2 1 
ATOM   464  N NE1 . TRP A  1 62  ? -28.658 13.055  6.792   1.00 23.32 ? 59  TRP B NE1 1 
ATOM   465  C CE2 . TRP A  1 62  ? -29.616 12.135  6.471   1.00 22.91 ? 59  TRP B CE2 1 
ATOM   466  C CE3 . TRP A  1 62  ? -29.745 9.778   5.907   1.00 21.31 ? 59  TRP B CE3 1 
ATOM   467  C CZ2 . TRP A  1 62  ? -31.001 12.294  6.312   1.00 23.07 ? 59  TRP B CZ2 1 
ATOM   468  C CZ3 . TRP A  1 62  ? -31.123 9.929   5.766   1.00 22.29 ? 59  TRP B CZ3 1 
ATOM   469  C CH2 . TRP A  1 62  ? -31.733 11.177  5.995   1.00 22.73 ? 59  TRP B CH2 1 
ATOM   470  N N   . ARG A  1 63  ? -27.737 7.465   7.699   1.00 20.46 ? 60  ARG B N   1 
ATOM   471  C CA  . ARG A  1 63  ? -28.916 6.672   8.063   1.00 20.95 ? 60  ARG B CA  1 
ATOM   472  C C   . ARG A  1 63  ? -28.870 6.255   9.525   1.00 21.70 ? 60  ARG B C   1 
ATOM   473  O O   . ARG A  1 63  ? -29.884 6.349   10.221  1.00 22.16 ? 60  ARG B O   1 
ATOM   474  C CB  . ARG A  1 63  ? -29.118 5.467   7.136   1.00 21.85 ? 60  ARG B CB  1 
ATOM   475  C CG  . ARG A  1 63  ? -29.516 5.835   5.712   1.00 21.95 ? 60  ARG B CG  1 
ATOM   476  C CD  . ARG A  1 63  ? -29.965 4.614   4.942   1.00 22.62 ? 60  ARG B CD  1 
ATOM   477  N NE  . ARG A  1 63  ? -28.912 3.600   4.792   1.00 22.06 ? 60  ARG B NE  1 
ATOM   478  C CZ  . ARG A  1 63  ? -27.988 3.553   3.831   1.00 21.30 ? 60  ARG B CZ  1 
ATOM   479  N NH1 . ARG A  1 63  ? -27.788 4.528   2.945   1.00 20.30 ? 60  ARG B NH1 1 
ATOM   480  N NH2 . ARG A  1 63  ? -27.180 2.511   3.767   1.00 22.01 ? 60  ARG B NH2 1 
ATOM   481  N N   . VAL A  1 64  ? -27.677 5.861   10.018  1.00 20.60 ? 61  VAL B N   1 
ATOM   482  C CA  . VAL A  1 64  ? -27.523 5.501   11.413  1.00 21.51 ? 61  VAL B CA  1 
ATOM   483  C C   . VAL A  1 64  ? -27.802 6.705   12.311  1.00 21.88 ? 61  VAL B C   1 
ATOM   484  O O   . VAL A  1 64  ? -28.530 6.567   13.316  1.00 22.79 ? 61  VAL B O   1 
ATOM   485  C CB  . VAL A  1 64  ? -26.120 4.916   11.680  1.00 21.19 ? 61  VAL B CB  1 
ATOM   486  C CG1 . VAL A  1 64  ? -25.798 4.830   13.159  1.00 23.46 ? 61  VAL B CG1 1 
ATOM   487  C CG2 . VAL A  1 64  ? -25.982 3.569   10.993  1.00 21.18 ? 61  VAL B CG2 1 
ATOM   488  N N   . VAL A  1 65  ? -27.167 7.847   12.028  1.00 22.05 ? 62  VAL B N   1 
ATOM   489  C CA  . VAL A  1 65  ? -27.286 9.008   12.916  1.00 24.56 ? 62  VAL B CA  1 
ATOM   490  C C   . VAL A  1 65  ? -28.724 9.572   12.883  1.00 27.09 ? 62  VAL B C   1 
ATOM   491  O O   . VAL A  1 65  ? -29.297 9.871   13.942  1.00 30.66 ? 62  VAL B O   1 
ATOM   492  C CB  . VAL A  1 65  ? -26.183 10.039  12.631  1.00 25.11 ? 62  VAL B CB  1 
ATOM   493  C CG1 . VAL A  1 65  ? -26.307 11.291  13.468  1.00 27.29 ? 62  VAL B CG1 1 
ATOM   494  C CG2 . VAL A  1 65  ? -24.793 9.437   12.892  1.00 25.03 ? 62  VAL B CG2 1 
ATOM   495  N N   . SER A  1 66  ? -29.332 9.628   11.697  1.00 27.49 ? 63  SER B N   1 
ATOM   496  C CA  . SER A  1 66  ? -30.724 10.046  11.512  1.00 29.87 ? 63  SER B CA  1 
ATOM   497  C C   . SER A  1 66  ? -31.688 9.160   12.303  1.00 30.92 ? 63  SER B C   1 
ATOM   498  O O   . SER A  1 66  ? -32.551 9.666   13.011  1.00 33.93 ? 63  SER B O   1 
ATOM   499  C CB  . SER A  1 66  ? -31.015 10.088  10.027  1.00 28.85 ? 63  SER B CB  1 
ATOM   500  O OG  . SER A  1 66  ? -32.336 10.486  9.718   1.00 36.48 ? 63  SER B OG  1 
ATOM   501  N N   . SER A  1 67  ? -31.516 7.848   12.223  1.00 30.68 ? 64  SER B N   1 
ATOM   502  C CA  . SER A  1 67  ? -32.256 6.901   13.039  1.00 33.19 ? 64  SER B CA  1 
ATOM   503  C C   . SER A  1 67  ? -32.106 7.149   14.552  1.00 35.77 ? 64  SER B C   1 
ATOM   504  O O   . SER A  1 67  ? -33.118 7.156   15.273  1.00 39.43 ? 64  SER B O   1 
ATOM   505  C CB  . SER A  1 67  ? -31.883 5.501   12.638  1.00 34.78 ? 64  SER B CB  1 
ATOM   506  O OG  . SER A  1 67  ? -32.503 4.547   13.485  1.00 40.40 ? 64  SER B OG  1 
ATOM   507  N N   . ILE A  1 68  ? -30.865 7.346   15.042  1.00 34.23 ? 65  ILE B N   1 
ATOM   508  C CA  . ILE A  1 68  ? -30.607 7.672   16.446  1.00 36.71 ? 65  ILE B CA  1 
ATOM   509  C C   . ILE A  1 68  ? -31.310 8.980   16.831  1.00 39.61 ? 65  ILE B C   1 
ATOM   510  O O   . ILE A  1 68  ? -31.907 9.023   17.917  1.00 43.98 ? 65  ILE B O   1 
ATOM   511  C CB  . ILE A  1 68  ? -29.098 7.671   16.801  1.00 35.42 ? 65  ILE B CB  1 
ATOM   512  C CG1 . ILE A  1 68  ? -28.508 6.240   16.763  1.00 35.11 ? 65  ILE B CG1 1 
ATOM   513  C CG2 . ILE A  1 68  ? -28.789 8.336   18.160  1.00 36.91 ? 65  ILE B CG2 1 
ATOM   514  C CD1 . ILE A  1 68  ? -26.990 6.173   16.619  1.00 35.17 ? 65  ILE B CD1 1 
ATOM   515  N N   . GLU A  1 69  ? -31.239 10.007  15.967  1.00 38.70 ? 66  GLU B N   1 
ATOM   516  C CA  . GLU A  1 69  ? -31.913 11.287  16.189  1.00 42.59 ? 66  GLU B CA  1 
ATOM   517  C C   . GLU A  1 69  ? -33.418 11.140  16.451  1.00 45.38 ? 66  GLU B C   1 
ATOM   518  O O   . GLU A  1 69  ? -33.937 11.784  17.368  1.00 46.22 ? 66  GLU B O   1 
ATOM   519  C CB  . GLU A  1 69  ? -31.764 12.147  14.944  1.00 41.62 ? 66  GLU B CB  1 
ATOM   520  C CG  . GLU A  1 69  ? -32.123 13.610  15.120  1.00 42.79 ? 66  GLU B CG  1 
ATOM   521  C CD  . GLU A  1 69  ? -31.817 14.401  13.862  1.00 43.44 ? 66  GLU B CD  1 
ATOM   522  O OE1 . GLU A  1 69  ? -31.380 13.893  12.798  1.00 45.81 ? 66  GLU B OE1 1 
ATOM   523  O OE2 . GLU A  1 69  ? -32.019 15.615  13.981  1.00 46.88 ? 66  GLU B OE2 1 
ATOM   524  N N   . GLN A  1 70  ? -34.080 10.328  15.605  1.00 49.17 ? 67  GLN B N   1 
ATOM   525  C CA  . GLN A  1 70  ? -35.503 10.023  15.692  1.00 53.21 ? 67  GLN B CA  1 
ATOM   526  C C   . GLN A  1 70  ? -35.842 9.173   16.924  1.00 57.42 ? 67  GLN B C   1 
ATOM   527  O O   . GLN A  1 70  ? -36.910 9.385   17.478  1.00 59.88 ? 67  GLN B O   1 
ATOM   528  C CB  . GLN A  1 70  ? -36.014 9.282   14.460  1.00 52.77 ? 67  GLN B CB  1 
ATOM   529  C CG  . GLN A  1 70  ? -35.930 10.045  13.140  1.00 54.55 ? 67  GLN B CG  1 
ATOM   530  C CD  . GLN A  1 70  ? -35.927 9.133   11.920  1.00 61.24 ? 67  GLN B CD  1 
ATOM   531  O OE1 . GLN A  1 70  ? -36.220 7.930   11.966  1.00 68.53 ? 67  GLN B OE1 1 
ATOM   532  N NE2 . GLN A  1 70  ? -35.571 9.686   10.773  1.00 61.21 ? 67  GLN B NE2 1 
ATOM   533  N N   . LYS A  1 71  ? -34.956 8.242   17.341  1.00 61.97 ? 68  LYS B N   1 
ATOM   534  C CA  . LYS A  1 71  ? -35.119 7.337   18.487  1.00 69.21 ? 68  LYS B CA  1 
ATOM   535  C C   . LYS A  1 71  ? -35.392 8.110   19.785  1.00 74.08 ? 68  LYS B C   1 
ATOM   536  O O   . LYS A  1 71  ? -36.253 7.700   20.567  1.00 83.54 ? 68  LYS B O   1 
ATOM   537  C CB  . LYS A  1 71  ? -33.889 6.429   18.687  1.00 72.55 ? 68  LYS B CB  1 
ATOM   538  C CG  . LYS A  1 71  ? -34.131 5.068   19.342  1.00 78.67 ? 68  LYS B CG  1 
ATOM   539  C CD  . LYS A  1 71  ? -34.223 3.858   18.410  1.00 77.42 ? 68  LYS B CD  1 
ATOM   540  C CE  . LYS A  1 71  ? -35.489 3.745   17.615  1.00 78.78 ? 68  LYS B CE  1 
ATOM   541  N NZ  . LYS A  1 71  ? -35.413 4.433   16.325  1.00 75.10 ? 68  LYS B NZ  1 
ATOM   542  N N   . THR A  1 72  ? -34.630 9.197   20.007  1.00 72.43 ? 69  THR B N   1 
ATOM   543  C CA  . THR A  1 72  ? -35.053 10.309  20.852  1.00 71.52 ? 69  THR B CA  1 
ATOM   544  C C   . THR A  1 72  ? -35.809 11.314  19.998  1.00 74.09 ? 69  THR B C   1 
ATOM   545  O O   . THR A  1 72  ? -36.913 11.689  20.420  1.00 75.64 ? 69  THR B O   1 
ATOM   546  C CB  . THR A  1 72  ? -33.872 10.950  21.572  1.00 69.82 ? 69  THR B CB  1 
ATOM   547  O OG1 . THR A  1 72  ? -34.564 11.967  22.298  1.00 72.93 ? 69  THR B OG1 1 
ATOM   548  C CG2 . THR A  1 72  ? -32.729 11.434  20.689  1.00 63.33 ? 69  THR B CG2 1 
ATOM   549  N N   . ALA A  1 76  ? -32.936 15.047  24.668  1.00 71.55 ? 73  ALA B N   1 
ATOM   550  C CA  . ALA A  1 76  ? -33.087 16.410  24.094  1.00 71.76 ? 73  ALA B CA  1 
ATOM   551  C C   . ALA A  1 76  ? -31.734 17.046  23.762  1.00 68.41 ? 73  ALA B C   1 
ATOM   552  O O   . ALA A  1 76  ? -31.557 17.541  22.653  1.00 68.10 ? 73  ALA B O   1 
ATOM   553  C CB  . ALA A  1 76  ? -33.866 17.276  25.045  1.00 74.36 ? 73  ALA B CB  1 
ATOM   554  N N   . ALA A  1 77  ? -30.818 17.080  24.743  1.00 65.75 ? 74  ALA B N   1 
ATOM   555  C CA  . ALA A  1 77  ? -29.414 17.423  24.522  1.00 63.13 ? 74  ALA B CA  1 
ATOM   556  C C   . ALA A  1 77  ? -28.719 16.345  23.676  1.00 59.96 ? 74  ALA B C   1 
ATOM   557  O O   . ALA A  1 77  ? -27.904 16.670  22.811  1.00 55.87 ? 74  ALA B O   1 
ATOM   558  C CB  . ALA A  1 77  ? -28.728 17.652  25.861  1.00 66.15 ? 74  ALA B CB  1 
ATOM   559  N N   . ALA A  1 78  ? -29.068 15.065  23.916  1.00 57.43 ? 75  ALA B N   1 
ATOM   560  C CA  . ALA A  1 78  ? -28.750 13.928  23.058  1.00 55.12 ? 75  ALA B CA  1 
ATOM   561  C C   . ALA A  1 78  ? -29.284 14.094  21.634  1.00 53.44 ? 75  ALA B C   1 
ATOM   562  O O   . ALA A  1 78  ? -28.586 13.760  20.662  1.00 47.91 ? 75  ALA B O   1 
ATOM   563  C CB  . ALA A  1 78  ? -29.302 12.647  23.664  1.00 54.98 ? 75  ALA B CB  1 
ATOM   564  N N   . GLN A  1 79  ? -30.546 14.549  21.526  1.00 53.68 ? 76  GLN B N   1 
ATOM   565  C CA  . GLN A  1 79  ? -31.176 14.799  20.238  1.00 52.15 ? 76  GLN B CA  1 
ATOM   566  C C   . GLN A  1 79  ? -30.445 15.923  19.493  1.00 49.07 ? 76  GLN B C   1 
ATOM   567  O O   . GLN A  1 79  ? -30.251 15.789  18.286  1.00 46.84 ? 76  GLN B O   1 
ATOM   568  C CB  . GLN A  1 79  ? -32.685 15.085  20.327  1.00 56.84 ? 76  GLN B CB  1 
ATOM   569  C CG  . GLN A  1 79  ? -33.450 14.600  19.091  1.00 56.87 ? 76  GLN B CG  1 
ATOM   570  C CD  . GLN A  1 79  ? -34.682 15.399  18.709  1.00 65.15 ? 76  GLN B CD  1 
ATOM   571  O OE1 . GLN A  1 79  ? -35.102 16.375  19.354  1.00 69.31 ? 76  GLN B OE1 1 
ATOM   572  N NE2 . GLN A  1 79  ? -35.299 14.953  17.624  1.00 68.93 ? 76  GLN B NE2 1 
ATOM   573  N N   . GLN A  1 80  ? -30.049 17.005  20.199  1.00 48.23 ? 77  GLN B N   1 
ATOM   574  C CA  . GLN A  1 80  ? -29.280 18.088  19.600  1.00 47.71 ? 77  GLN B CA  1 
ATOM   575  C C   . GLN A  1 80  ? -27.942 17.578  19.044  1.00 44.70 ? 77  GLN B C   1 
ATOM   576  O O   . GLN A  1 80  ? -27.559 17.963  17.932  1.00 41.09 ? 77  GLN B O   1 
ATOM   577  C CB  . GLN A  1 80  ? -29.068 19.254  20.559  1.00 50.76 ? 77  GLN B CB  1 
ATOM   578  C CG  . GLN A  1 80  ? -28.224 20.388  19.971  1.00 52.09 ? 77  GLN B CG  1 
ATOM   579  C CD  . GLN A  1 80  ? -28.195 21.673  20.778  1.00 56.67 ? 77  GLN B CD  1 
ATOM   580  O OE1 . GLN A  1 80  ? -29.214 22.140  21.311  1.00 60.64 ? 77  GLN B OE1 1 
ATOM   581  N NE2 . GLN A  1 80  ? -27.013 22.279  20.858  1.00 56.75 ? 77  GLN B NE2 1 
ATOM   582  N N   . MET A  1 81  ? -27.204 16.786  19.844  1.00 44.47 ? 78  MET B N   1 
ATOM   583  C CA  . MET A  1 81  ? -25.929 16.241  19.367  1.00 41.92 ? 78  MET B CA  1 
ATOM   584  C C   . MET A  1 81  ? -26.105 15.390  18.120  1.00 37.71 ? 78  MET B C   1 
ATOM   585  O O   . MET A  1 81  ? -25.341 15.529  17.183  1.00 35.37 ? 78  MET B O   1 
ATOM   586  C CB  . MET A  1 81  ? -25.230 15.399  20.426  1.00 44.42 ? 78  MET B CB  1 
ATOM   587  C CG  . MET A  1 81  ? -23.826 14.930  20.019  1.00 43.77 ? 78  MET B CG  1 
ATOM   588  S SD  . MET A  1 81  ? -23.107 14.079  21.430  1.00 50.30 ? 78  MET B SD  1 
ATOM   589  C CE  . MET A  1 81  ? -23.083 15.283  22.765  1.00 47.27 ? 78  MET B CE  1 
ATOM   590  N N   . ALA A  1 82  ? -27.105 14.509  18.119  1.00 36.81 ? 79  ALA B N   1 
ATOM   591  C CA  . ALA A  1 82  ? -27.429 13.704  16.954  1.00 34.70 ? 79  ALA B CA  1 
ATOM   592  C C   . ALA A  1 82  ? -27.752 14.568  15.730  1.00 34.16 ? 79  ALA B C   1 
ATOM   593  O O   . ALA A  1 82  ? -27.245 14.296  14.640  1.00 30.97 ? 79  ALA B O   1 
ATOM   594  C CB  . ALA A  1 82  ? -28.535 12.762  17.298  1.00 35.50 ? 79  ALA B CB  1 
ATOM   595  N N   . ARG A  1 83  ? -28.551 15.642  15.916  1.00 36.04 ? 80  ARG B N   1 
ATOM   596  C CA  . ARG A  1 83  ? -28.859 16.586  14.843  1.00 36.28 ? 80  ARG B CA  1 
ATOM   597  C C   . ARG A  1 83  ? -27.585 17.203  14.266  1.00 34.02 ? 80  ARG B C   1 
ATOM   598  O O   . ARG A  1 83  ? -27.421 17.220  13.044  1.00 33.30 ? 80  ARG B O   1 
ATOM   599  C CB  . ARG A  1 83  ? -29.780 17.739  15.299  1.00 40.35 ? 80  ARG B CB  1 
ATOM   600  C CG  . ARG A  1 83  ? -30.031 18.846  14.283  1.00 43.30 ? 80  ARG B CG  1 
ATOM   601  C CD  . ARG A  1 83  ? -31.091 19.866  14.698  1.00 47.71 ? 80  ARG B CD  1 
ATOM   602  N NE  . ARG A  1 83  ? -30.582 20.849  15.659  1.00 53.22 ? 80  ARG B NE  1 
ATOM   603  C CZ  . ARG A  1 83  ? -30.909 20.999  16.965  1.00 59.58 ? 80  ARG B CZ  1 
ATOM   604  N NH1 . ARG A  1 83  ? -31.695 20.142  17.590  1.00 61.93 ? 80  ARG B NH1 1 
ATOM   605  N NH2 . ARG A  1 83  ? -30.424 22.000  17.684  1.00 63.65 ? 80  ARG B NH2 1 
ATOM   606  N N   . GLU A  1 84  ? -26.744 17.747  15.140  1.00 34.87 ? 81  GLU B N   1 
ATOM   607  C CA  . GLU A  1 84  ? -25.557 18.478  14.707  1.00 36.70 ? 81  GLU B CA  1 
ATOM   608  C C   . GLU A  1 84  ? -24.559 17.542  14.017  1.00 34.34 ? 81  GLU B C   1 
ATOM   609  O O   . GLU A  1 84  ? -23.949 17.910  13.019  1.00 32.99 ? 81  GLU B O   1 
ATOM   610  C CB  . GLU A  1 84  ? -24.926 19.222  15.871  1.00 40.28 ? 81  GLU B CB  1 
ATOM   611  C CG  . GLU A  1 84  ? -25.801 20.361  16.389  1.00 43.62 ? 81  GLU B CG  1 
ATOM   612  C CD  . GLU A  1 84  ? -25.308 21.049  17.645  1.00 48.73 ? 81  GLU B CD  1 
ATOM   613  O OE1 . GLU A  1 84  ? -24.185 20.690  18.046  1.00 50.62 ? 81  GLU B OE1 1 
ATOM   614  O OE2 . GLU A  1 84  ? -25.973 21.961  18.212  1.00 49.75 ? 81  GLU B OE2 1 
ATOM   615  N N   . TYR A  1 85  ? -24.478 16.291  14.481  1.00 33.91 ? 82  TYR B N   1 
ATOM   616  C CA  . TYR A  1 85  ? -23.641 15.290  13.828  1.00 31.17 ? 82  TYR B CA  1 
ATOM   617  C C   . TYR A  1 85  ? -24.168 14.900  12.453  1.00 29.21 ? 82  TYR B C   1 
ATOM   618  O O   . TYR A  1 85  ? -23.376 14.839  11.500  1.00 26.75 ? 82  TYR B O   1 
ATOM   619  C CB  . TYR A  1 85  ? -23.478 14.090  14.758  1.00 32.26 ? 82  TYR B CB  1 
ATOM   620  C CG  . TYR A  1 85  ? -22.233 13.262  14.476  1.00 31.14 ? 82  TYR B CG  1 
ATOM   621  C CD1 . TYR A  1 85  ? -20.972 13.846  14.254  1.00 32.79 ? 82  TYR B CD1 1 
ATOM   622  C CD2 . TYR A  1 85  ? -22.307 11.887  14.482  1.00 30.99 ? 82  TYR B CD2 1 
ATOM   623  C CE1 . TYR A  1 85  ? -19.840 13.070  14.017  1.00 33.48 ? 82  TYR B CE1 1 
ATOM   624  C CE2 . TYR A  1 85  ? -21.167 11.102  14.260  1.00 31.06 ? 82  TYR B CE2 1 
ATOM   625  C CZ  . TYR A  1 85  ? -19.948 11.688  13.967  1.00 30.11 ? 82  TYR B CZ  1 
ATOM   626  O OH  . TYR A  1 85  ? -18.821 10.920  13.808  1.00 27.28 ? 82  TYR B OH  1 
ATOM   627  N N   . ARG A  1 86  ? -25.497 14.687  12.337  1.00 29.34 ? 83  ARG B N   1 
ATOM   628  C CA  . ARG A  1 86  ? -26.168 14.499  11.058  1.00 29.28 ? 83  ARG B CA  1 
ATOM   629  C C   . ARG A  1 86  ? -25.821 15.631  10.062  1.00 28.39 ? 83  ARG B C   1 
ATOM   630  O O   . ARG A  1 86  ? -25.582 15.350  8.896   1.00 26.36 ? 83  ARG B O   1 
ATOM   631  C CB  . ARG A  1 86  ? -27.681 14.249  11.231  1.00 31.74 ? 83  ARG B CB  1 
ATOM   632  C CG  . ARG A  1 86  ? -28.457 14.218  9.925   1.00 32.65 ? 83  ARG B CG  1 
ATOM   633  C CD  . ARG A  1 86  ? -29.922 14.003  9.919   1.00 35.94 ? 83  ARG B CD  1 
ATOM   634  N NE  . ARG A  1 86  ? -30.705 15.043  10.583  1.00 38.89 ? 83  ARG B NE  1 
ATOM   635  C CZ  . ARG A  1 86  ? -30.763 16.380  10.407  1.00 41.94 ? 83  ARG B CZ  1 
ATOM   636  N NH1 . ARG A  1 86  ? -30.284 17.012  9.347   1.00 40.94 ? 83  ARG B NH1 1 
ATOM   637  N NH2 . ARG A  1 86  ? -31.388 17.106  11.323  1.00 45.83 ? 83  ARG B NH2 1 
ATOM   638  N N   . GLU A  1 87  ? -25.859 16.881  10.508  1.00 31.21 ? 84  GLU B N   1 
ATOM   639  C CA  . GLU A  1 87  ? -25.587 18.044  9.671   1.00 32.66 ? 84  GLU B CA  1 
ATOM   640  C C   . GLU A  1 87  ? -24.139 18.058  9.174   1.00 31.02 ? 84  GLU B C   1 
ATOM   641  O O   . GLU A  1 87  ? -23.897 18.342  8.005   1.00 30.45 ? 84  GLU B O   1 
ATOM   642  C CB  . GLU A  1 87  ? -25.950 19.333  10.413  1.00 35.59 ? 84  GLU B CB  1 
ATOM   643  C CG  . GLU A  1 87  ? -27.463 19.518  10.546  1.00 37.43 ? 84  GLU B CG  1 
ATOM   644  C CD  . GLU A  1 87  ? -27.929 20.556  11.525  1.00 42.38 ? 84  GLU B CD  1 
ATOM   645  O OE1 . GLU A  1 87  ? -27.094 21.162  12.247  1.00 41.57 ? 84  GLU B OE1 1 
ATOM   646  O OE2 . GLU A  1 87  ? -29.175 20.687  11.576  1.00 44.36 ? 84  GLU B OE2 1 
ATOM   647  N N   . LYS A  1 88  ? -23.190 17.679  10.035  1.00 32.48 ? 85  LYS B N   1 
ATOM   648  C CA  . LYS A  1 88  ? -21.783 17.526  9.654   1.00 32.60 ? 85  LYS B CA  1 
ATOM   649  C C   . LYS A  1 88  ? -21.624 16.496  8.537   1.00 29.09 ? 85  LYS B C   1 
ATOM   650  O O   . LYS A  1 88  ? -20.940 16.764  7.538   1.00 29.45 ? 85  LYS B O   1 
ATOM   651  C CB  . LYS A  1 88  ? -20.908 17.169  10.860  1.00 35.84 ? 85  LYS B CB  1 
ATOM   652  C CG  . LYS A  1 88  ? -19.410 16.963  10.583  1.00 40.97 ? 85  LYS B CG  1 
ATOM   653  C CD  . LYS A  1 88  ? -18.653 16.303  11.736  1.00 48.06 ? 85  LYS B CD  1 
ATOM   654  C CE  . LYS A  1 88  ? -18.331 17.224  12.894  1.00 55.05 ? 85  LYS B CE  1 
ATOM   655  N NZ  . LYS A  1 88  ? -17.229 16.624  13.652  1.00 60.19 ? 85  LYS B NZ  1 
ATOM   656  N N   . ILE A  1 89  ? -22.302 15.353  8.696   1.00 27.12 ? 86  ILE B N   1 
ATOM   657  C CA  . ILE A  1 89  ? -22.279 14.275  7.723   1.00 25.04 ? 86  ILE B CA  1 
ATOM   658  C C   . ILE A  1 89  ? -22.917 14.740  6.410   1.00 25.25 ? 86  ILE B C   1 
ATOM   659  O O   . ILE A  1 89  ? -22.417 14.386  5.348   1.00 26.53 ? 86  ILE B O   1 
ATOM   660  C CB  . ILE A  1 89  ? -22.899 12.984  8.307   1.00 24.50 ? 86  ILE B CB  1 
ATOM   661  C CG1 . ILE A  1 89  ? -22.106 12.456  9.535   1.00 25.58 ? 86  ILE B CG1 1 
ATOM   662  C CG2 . ILE A  1 89  ? -23.041 11.894  7.253   1.00 23.11 ? 86  ILE B CG2 1 
ATOM   663  C CD1 . ILE A  1 89  ? -22.877 11.455  10.369  1.00 25.84 ? 86  ILE B CD1 1 
ATOM   664  N N   . GLU A  1 90  ? -24.052 15.430  6.496   1.00 26.10 ? 87  GLU B N   1 
ATOM   665  C CA  . GLU A  1 90  ? -24.739 16.029  5.365   1.00 27.39 ? 87  GLU B CA  1 
ATOM   666  C C   . GLU A  1 90  ? -23.844 16.993  4.591   1.00 26.96 ? 87  GLU B C   1 
ATOM   667  O O   . GLU A  1 90  ? -23.898 16.960  3.360   1.00 26.64 ? 87  GLU B O   1 
ATOM   668  C CB  . GLU A  1 90  ? -25.984 16.802  5.809   1.00 29.35 ? 87  GLU B CB  1 
ATOM   669  C CG  . GLU A  1 90  ? -27.274 16.005  5.701   1.00 32.01 ? 87  GLU B CG  1 
ATOM   670  C CD  . GLU A  1 90  ? -28.447 16.589  6.469   1.00 33.89 ? 87  GLU B CD  1 
ATOM   671  O OE1 . GLU A  1 90  ? -28.460 17.797  6.805   1.00 40.86 ? 87  GLU B OE1 1 
ATOM   672  O OE2 . GLU A  1 90  ? -29.267 15.777  6.911   1.00 33.58 ? 87  GLU B OE2 1 
ATOM   673  N N   . THR A  1 91  ? -23.079 17.858  5.284   1.00 27.74 ? 88  THR B N   1 
ATOM   674  C CA  . THR A  1 91  ? -22.188 18.795  4.599   1.00 28.49 ? 88  THR B CA  1 
ATOM   675  C C   . THR A  1 91  ? -21.154 18.008  3.778   1.00 25.87 ? 88  THR B C   1 
ATOM   676  O O   . THR A  1 91  ? -20.979 18.272  2.585   1.00 25.36 ? 88  THR B O   1 
ATOM   677  C CB  . THR A  1 91  ? -21.540 19.763  5.587   1.00 30.85 ? 88  THR B CB  1 
ATOM   678  O OG1 . THR A  1 91  ? -22.579 20.474  6.218   1.00 31.72 ? 88  THR B OG1 1 
ATOM   679  C CG2 . THR A  1 91  ? -20.533 20.701  4.948   1.00 32.70 ? 88  THR B CG2 1 
ATOM   680  N N   . GLU A  1 92  ? -20.525 16.985  4.372   1.00 24.95 ? 89  GLU B N   1 
ATOM   681  C CA  . GLU A  1 92  ? -19.583 16.139  3.636   1.00 23.59 ? 89  GLU B CA  1 
ATOM   682  C C   . GLU A  1 92  ? -20.247 15.478  2.430   1.00 23.54 ? 89  GLU B C   1 
ATOM   683  O O   . GLU A  1 92  ? -19.695 15.478  1.329   1.00 22.37 ? 89  GLU B O   1 
ATOM   684  C CB  . GLU A  1 92  ? -19.005 15.016  4.494   1.00 24.03 ? 89  GLU B CB  1 
ATOM   685  C CG  . GLU A  1 92  ? -18.136 15.508  5.643   1.00 26.70 ? 89  GLU B CG  1 
ATOM   686  C CD  . GLU A  1 92  ? -17.662 14.383  6.526   1.00 26.54 ? 89  GLU B CD  1 
ATOM   687  O OE1 . GLU A  1 92  ? -17.724 13.219  6.109   1.00 25.97 ? 89  GLU B OE1 1 
ATOM   688  O OE2 . GLU A  1 92  ? -17.163 14.710  7.634   1.00 30.70 ? 89  GLU B OE2 1 
ATOM   689  N N   . LEU A  1 93  ? -21.458 14.957  2.637   1.00 23.31 ? 90  LEU B N   1 
ATOM   690  C CA  . LEU A  1 93  ? -22.205 14.264  1.597   1.00 26.61 ? 90  LEU B CA  1 
ATOM   691  C C   . LEU A  1 93  ? -22.473 15.210  0.413   1.00 26.22 ? 90  LEU B C   1 
ATOM   692  O O   . LEU A  1 93  ? -22.172 14.816  -0.711  1.00 26.66 ? 90  LEU B O   1 
ATOM   693  C CB  . LEU A  1 93  ? -23.459 13.647  2.214   1.00 28.93 ? 90  LEU B CB  1 
ATOM   694  C CG  . LEU A  1 93  ? -24.093 12.464  1.471   1.00 33.64 ? 90  LEU B CG  1 
ATOM   695  C CD1 . LEU A  1 93  ? -24.863 11.545  2.399   1.00 37.08 ? 90  LEU B CD1 1 
ATOM   696  C CD2 . LEU A  1 93  ? -25.032 12.989  0.418   1.00 38.51 ? 90  LEU B CD2 1 
ATOM   697  N N   A ARG A  1 94  ? -22.909 16.443  0.688   0.60 27.30 ? 91  ARG B N   1 
ATOM   698  N N   B ARG A  1 94  ? -22.918 16.448  0.689   0.40 27.45 ? 91  ARG B N   1 
ATOM   699  C CA  A ARG A  1 94  ? -23.169 17.448  -0.337  0.60 30.02 ? 91  ARG B CA  1 
ATOM   700  C CA  B ARG A  1 94  ? -23.171 17.471  -0.322  0.40 29.53 ? 91  ARG B CA  1 
ATOM   701  C C   A ARG A  1 94  ? -21.904 17.824  -1.098  0.60 31.12 ? 91  ARG B C   1 
ATOM   702  C C   B ARG A  1 94  ? -21.906 17.826  -1.097  0.40 30.48 ? 91  ARG B C   1 
ATOM   703  O O   A ARG A  1 94  ? -21.970 17.945  -2.320  0.60 31.45 ? 91  ARG B O   1 
ATOM   704  O O   B ARG A  1 94  ? -21.973 17.945  -2.320  0.40 30.68 ? 91  ARG B O   1 
ATOM   705  C CB  A ARG A  1 94  ? -23.824 18.712  0.237   0.60 32.58 ? 91  ARG B CB  1 
ATOM   706  C CB  B ARG A  1 94  ? -23.694 18.796  0.254   0.40 31.70 ? 91  ARG B CB  1 
ATOM   707  C CG  A ARG A  1 94  ? -25.248 18.398  0.669   0.60 33.73 ? 91  ARG B CG  1 
ATOM   708  C CG  B ARG A  1 94  ? -25.123 18.820  0.777   0.40 32.66 ? 91  ARG B CG  1 
ATOM   709  C CD  A ARG A  1 94  ? -26.118 19.531  1.194   0.60 36.04 ? 91  ARG B CD  1 
ATOM   710  C CD  B ARG A  1 94  ? -25.508 20.121  1.498   0.40 34.30 ? 91  ARG B CD  1 
ATOM   711  N NE  A ARG A  1 94  ? -27.458 18.927  1.237   0.60 35.78 ? 91  ARG B NE  1 
ATOM   712  N NE  B ARG A  1 94  ? -26.641 19.760  2.357   0.40 34.06 ? 91  ARG B NE  1 
ATOM   713  C CZ  A ARG A  1 94  ? -28.395 19.039  0.277   0.60 35.09 ? 91  ARG B CZ  1 
ATOM   714  C CZ  B ARG A  1 94  ? -26.714 19.931  3.664   0.40 33.75 ? 91  ARG B CZ  1 
ATOM   715  N NH1 A ARG A  1 94  ? -28.526 20.176  -0.400  0.60 32.51 ? 91  ARG B NH1 1 
ATOM   716  N NH1 B ARG A  1 94  ? -25.795 20.640  4.294   0.40 34.43 ? 91  ARG B NH1 1 
ATOM   717  N NH2 A ARG A  1 94  ? -29.181 17.979  0.017   0.60 31.57 ? 91  ARG B NH2 1 
ATOM   718  N NH2 B ARG A  1 94  ? -27.739 19.414  4.314   0.40 33.12 ? 91  ARG B NH2 1 
ATOM   719  N N   . ASP A  1 95  ? -20.787 17.993  -0.373  1.00 30.25 ? 92  ASP B N   1 
ATOM   720  C CA  . ASP A  1 95  ? -19.490 18.306  -0.959  1.00 30.70 ? 92  ASP B CA  1 
ATOM   721  C C   . ASP A  1 95  ? -19.015 17.198  -1.893  1.00 27.90 ? 92  ASP B C   1 
ATOM   722  O O   . ASP A  1 95  ? -18.594 17.519  -3.009  1.00 25.55 ? 92  ASP B O   1 
ATOM   723  C CB  . ASP A  1 95  ? -18.436 18.662  0.079   1.00 34.50 ? 92  ASP B CB  1 
ATOM   724  C CG  . ASP A  1 95  ? -18.726 19.902  0.913   1.00 36.94 ? 92  ASP B CG  1 
ATOM   725  O OD1 . ASP A  1 95  ? -19.725 20.597  0.652   1.00 46.68 ? 92  ASP B OD1 1 
ATOM   726  O OD2 . ASP A  1 95  ? -18.014 20.123  1.895   1.00 43.31 ? 92  ASP B OD2 1 
ATOM   727  N N   . ILE A  1 96  ? -19.216 15.919  -1.496  1.00 25.64 ? 93  ILE B N   1 
ATOM   728  C CA  . ILE A  1 96  ? -18.861 14.775  -2.331  1.00 24.24 ? 93  ILE B CA  1 
ATOM   729  C C   . ILE A  1 96  ? -19.716 14.778  -3.604  1.00 22.73 ? 93  ILE B C   1 
ATOM   730  O O   . ILE A  1 96  ? -19.176 14.675  -4.709  1.00 21.21 ? 93  ILE B O   1 
ATOM   731  C CB  . ILE A  1 96  ? -18.958 13.444  -1.574  1.00 22.80 ? 93  ILE B CB  1 
ATOM   732  C CG1 . ILE A  1 96  ? -17.933 13.363  -0.388  1.00 26.81 ? 93  ILE B CG1 1 
ATOM   733  C CG2 . ILE A  1 96  ? -18.777 12.239  -2.506  1.00 22.67 ? 93  ILE B CG2 1 
ATOM   734  C CD1 . ILE A  1 96  ? -18.416 12.405  0.702   1.00 26.00 ? 93  ILE B CD1 1 
ATOM   735  N N   . CYS A  1 97  ? -21.048 14.896  -3.429  1.00 22.59 ? 94  CYS B N   1 
ATOM   736  C CA  . CYS A  1 97  ? -21.961 14.966  -4.546  1.00 23.84 ? 94  CYS B CA  1 
ATOM   737  C C   . CYS A  1 97  ? -21.665 16.127  -5.507  1.00 24.16 ? 94  CYS B C   1 
ATOM   738  O O   . CYS A  1 97  ? -21.611 15.873  -6.715  1.00 26.22 ? 94  CYS B O   1 
ATOM   739  C CB  . CYS A  1 97  ? -23.413 14.961  -4.076  1.00 22.86 ? 94  CYS B CB  1 
ATOM   740  S SG  . CYS A  1 97  ? -23.891 13.366  -3.355  1.00 21.53 ? 94  CYS B SG  1 
ATOM   741  N N   . ASN A  1 98  ? -21.317 17.289  -4.961  1.00 25.12 ? 95  ASN B N   1 
ATOM   742  C CA  . ASN A  1 98  ? -20.994 18.458  -5.762  1.00 29.96 ? 95  ASN B CA  1 
ATOM   743  C C   . ASN A  1 98  ? -19.729 18.244  -6.584  1.00 27.79 ? 95  ASN B C   1 
ATOM   744  O O   . ASN A  1 98  ? -19.741 18.656  -7.738  1.00 26.56 ? 95  ASN B O   1 
ATOM   745  C CB  . ASN A  1 98  ? -20.937 19.732  -4.937  1.00 31.91 ? 95  ASN B CB  1 
ATOM   746  C CG  . ASN A  1 98  ? -22.300 20.188  -4.447  1.00 38.42 ? 95  ASN B CG  1 
ATOM   747  O OD1 . ASN A  1 98  ? -23.385 19.800  -4.935  1.00 40.06 ? 95  ASN B OD1 1 
ATOM   748  N ND2 . ASN A  1 98  ? -22.260 21.008  -3.414  1.00 38.56 ? 95  ASN B ND2 1 
ATOM   749  N N   . ASP A  1 99  ? -18.697 17.591  -6.013  1.00 27.63 ? 96  ASP B N   1 
ATOM   750  C CA  . ASP A  1 99  ? -17.490 17.272  -6.774  1.00 29.27 ? 96  ASP B CA  1 
ATOM   751  C C   . ASP A  1 99  ? -17.807 16.413  -7.993  1.00 26.64 ? 96  ASP B C   1 
ATOM   752  O O   . ASP A  1 99  ? -17.416 16.770  -9.102  1.00 25.65 ? 96  ASP B O   1 
ATOM   753  C CB  . ASP A  1 99  ? -16.406 16.579  -5.961  1.00 30.31 ? 96  ASP B CB  1 
ATOM   754  C CG  . ASP A  1 99  ? -15.478 17.480  -5.161  1.00 36.91 ? 96  ASP B CG  1 
ATOM   755  O OD1 . ASP A  1 99  ? -15.619 18.723  -5.177  1.00 41.63 ? 96  ASP B OD1 1 
ATOM   756  O OD2 . ASP A  1 99  ? -14.612 16.950  -4.497  1.00 36.67 ? 96  ASP B OD2 1 
ATOM   757  N N   . VAL A  1 100 ? -18.567 15.335  -7.776  1.00 23.54 ? 97  VAL B N   1 
ATOM   758  C CA  . VAL A  1 100 ? -18.909 14.405  -8.845  1.00 23.24 ? 97  VAL B CA  1 
ATOM   759  C C   . VAL A  1 100 ? -19.739 15.110  -9.913  1.00 21.94 ? 97  VAL B C   1 
ATOM   760  O O   . VAL A  1 100 ? -19.465 14.961  -11.098 1.00 20.73 ? 97  VAL B O   1 
ATOM   761  C CB  . VAL A  1 100 ? -19.693 13.173  -8.337  1.00 22.62 ? 97  VAL B CB  1 
ATOM   762  C CG1 . VAL A  1 100 ? -20.209 12.254  -9.444  1.00 23.01 ? 97  VAL B CG1 1 
ATOM   763  C CG2 . VAL A  1 100 ? -18.822 12.384  -7.429  1.00 21.51 ? 97  VAL B CG2 1 
ATOM   764  N N   . LEU A  1 101 ? -20.777 15.791  -9.463  1.00 21.81 ? 98  LEU B N   1 
ATOM   765  C CA  . LEU A  1 101 ? -21.676 16.487  -10.378 1.00 23.49 ? 98  LEU B CA  1 
ATOM   766  C C   . LEU A  1 101 ? -20.940 17.537  -11.216 1.00 23.97 ? 98  LEU B C   1 
ATOM   767  O O   . LEU A  1 101 ? -21.276 17.673  -12.395 1.00 25.58 ? 98  LEU B O   1 
ATOM   768  C CB  . LEU A  1 101 ? -22.828 17.056  -9.560  1.00 23.41 ? 98  LEU B CB  1 
ATOM   769  C CG  . LEU A  1 101 ? -23.801 16.012  -9.002  1.00 23.47 ? 98  LEU B CG  1 
ATOM   770  C CD1 . LEU A  1 101 ? -24.799 16.693  -8.064  1.00 23.81 ? 98  LEU B CD1 1 
ATOM   771  C CD2 . LEU A  1 101 ? -24.518 15.248  -10.101 1.00 21.80 ? 98  LEU B CD2 1 
ATOM   772  N N   . SER A  1 102 ? -19.976 18.258  -10.624 1.00 26.19 ? 99  SER B N   1 
ATOM   773  C CA  . SER A  1 102 ? -19.142 19.201  -11.363 1.00 29.44 ? 99  SER B CA  1 
ATOM   774  C C   . SER A  1 102 ? -18.297 18.528  -12.433 1.00 28.21 ? 99  SER B C   1 
ATOM   775  O O   . SER A  1 102 ? -18.203 19.076  -13.520 1.00 29.99 ? 99  SER B O   1 
ATOM   776  C CB  . SER A  1 102 ? -18.243 20.020  -10.474 1.00 34.44 ? 99  SER B CB  1 
ATOM   777  O OG  . SER A  1 102 ? -19.020 21.030  -9.882  1.00 41.32 ? 99  SER B OG  1 
ATOM   778  N N   . LEU A  1 103 ? -17.646 17.403  -12.105 1.00 26.52 ? 100 LEU B N   1 
ATOM   779  C CA  . LEU A  1 103 ? -16.861 16.621  -13.065 1.00 27.06 ? 100 LEU B CA  1 
ATOM   780  C C   . LEU A  1 103 ? -17.723 16.196  -14.255 1.00 26.82 ? 100 LEU B C   1 
ATOM   781  O O   . LEU A  1 103 ? -17.296 16.295  -15.394 1.00 27.53 ? 100 LEU B O   1 
ATOM   782  C CB  . LEU A  1 103 ? -16.233 15.385  -12.399 1.00 24.67 ? 100 LEU B CB  1 
ATOM   783  C CG  . LEU A  1 103 ? -15.161 15.648  -11.326 1.00 24.79 ? 100 LEU B CG  1 
ATOM   784  C CD1 . LEU A  1 103 ? -14.721 14.335  -10.786 1.00 24.87 ? 100 LEU B CD1 1 
ATOM   785  C CD2 . LEU A  1 103 ? -13.933 16.479  -11.768 1.00 26.82 ? 100 LEU B CD2 1 
ATOM   786  N N   . LEU A  1 104 ? -18.944 15.739  -13.958 1.00 25.93 ? 101 LEU B N   1 
ATOM   787  C CA  . LEU A  1 104 ? -19.888 15.309  -14.968 1.00 26.56 ? 101 LEU B CA  1 
ATOM   788  C C   . LEU A  1 104 ? -20.308 16.462  -15.877 1.00 27.53 ? 101 LEU B C   1 
ATOM   789  O O   . LEU A  1 104 ? -20.253 16.296  -17.084 1.00 28.29 ? 101 LEU B O   1 
ATOM   790  C CB  . LEU A  1 104 ? -21.066 14.652  -14.262 1.00 26.02 ? 101 LEU B CB  1 
ATOM   791  C CG  . LEU A  1 104 ? -20.792 13.302  -13.607 1.00 25.45 ? 101 LEU B CG  1 
ATOM   792  C CD1 . LEU A  1 104 ? -21.944 12.977  -12.670 1.00 26.15 ? 101 LEU B CD1 1 
ATOM   793  C CD2 . LEU A  1 104 ? -20.661 12.177  -14.626 1.00 25.83 ? 101 LEU B CD2 1 
ATOM   794  N N   . GLU A  1 105 ? -20.665 17.603  -15.290 1.00 28.35 ? 102 GLU B N   1 
ATOM   795  C CA  . GLU A  1 105 ? -21.117 18.761  -16.034 1.00 32.90 ? 102 GLU B CA  1 
ATOM   796  C C   . GLU A  1 105 ? -19.970 19.415  -16.814 1.00 32.80 ? 102 GLU B C   1 
ATOM   797  O O   . GLU A  1 105 ? -20.164 19.735  -17.985 1.00 31.94 ? 102 GLU B O   1 
ATOM   798  C CB  . GLU A  1 105 ? -21.823 19.745  -15.099 1.00 36.18 ? 102 GLU B CB  1 
ATOM   799  C CG  . GLU A  1 105 ? -22.933 20.515  -15.809 1.00 42.42 ? 102 GLU B CG  1 
ATOM   800  C CD  . GLU A  1 105 ? -24.080 19.631  -16.324 1.00 41.90 ? 102 GLU B CD  1 
ATOM   801  O OE1 . GLU A  1 105 ? -24.680 20.185  -17.270 1.00 42.05 ? 102 GLU B OE1 1 
ATOM   802  O OE2 . GLU A  1 105 ? -24.374 18.469  -15.851 1.00 39.87 ? 102 GLU B OE2 1 
ATOM   803  N N   . LYS A  1 106 ? -18.804 19.611  -16.173 1.00 32.69 ? 103 LYS B N   1 
ATOM   804  C CA  . LYS A  1 106 ? -17.689 20.317  -16.772 1.00 35.47 ? 103 LYS B CA  1 
ATOM   805  C C   . LYS A  1 106 ? -16.951 19.479  -17.822 1.00 34.21 ? 103 LYS B C   1 
ATOM   806  O O   . LYS A  1 106 ? -16.456 20.072  -18.785 1.00 34.47 ? 103 LYS B O   1 
ATOM   807  C CB  . LYS A  1 106 ? -16.626 20.778  -15.766 1.00 41.47 ? 103 LYS B CB  1 
ATOM   808  C CG  . LYS A  1 106 ? -16.773 22.083  -14.950 1.00 46.57 ? 103 LYS B CG  1 
ATOM   809  C CD  . LYS A  1 106 ? -15.427 22.563  -14.385 1.00 49.24 ? 103 LYS B CD  1 
ATOM   810  C CE  . LYS A  1 106 ? -14.441 22.981  -15.461 1.00 53.42 ? 103 LYS B CE  1 
ATOM   811  N NZ  . LYS A  1 106 ? -13.477 24.005  -15.047 1.00 53.53 ? 103 LYS B NZ  1 
ATOM   812  N N   . PHE A  1 107 ? -16.764 18.161  -17.617 1.00 31.13 ? 104 PHE B N   1 
ATOM   813  C CA  . PHE A  1 107 ? -15.898 17.339  -18.461 1.00 31.35 ? 104 PHE B CA  1 
ATOM   814  C C   . PHE A  1 107 ? -16.630 16.172  -19.118 1.00 30.70 ? 104 PHE B C   1 
ATOM   815  O O   . PHE A  1 107 ? -16.541 15.999  -20.323 1.00 31.91 ? 104 PHE B O   1 
ATOM   816  C CB  . PHE A  1 107 ? -14.739 16.795  -17.628 1.00 30.40 ? 104 PHE B CB  1 
ATOM   817  C CG  . PHE A  1 107 ? -13.851 17.886  -17.061 1.00 32.52 ? 104 PHE B CG  1 
ATOM   818  C CD1 . PHE A  1 107 ? -12.911 18.525  -17.874 1.00 34.47 ? 104 PHE B CD1 1 
ATOM   819  C CD2 . PHE A  1 107 ? -13.961 18.276  -15.726 1.00 31.90 ? 104 PHE B CD2 1 
ATOM   820  C CE1 . PHE A  1 107 ? -12.105 19.540  -17.361 1.00 37.14 ? 104 PHE B CE1 1 
ATOM   821  C CE2 . PHE A  1 107 ? -13.157 19.286  -15.223 1.00 34.64 ? 104 PHE B CE2 1 
ATOM   822  C CZ  . PHE A  1 107 ? -12.221 19.915  -16.036 1.00 35.91 ? 104 PHE B CZ  1 
ATOM   823  N N   . LEU A  1 108 ? -17.259 15.302  -18.325 1.00 28.26 ? 105 LEU B N   1 
ATOM   824  C CA  . LEU A  1 108 ? -17.555 13.939  -18.751 1.00 27.65 ? 105 LEU B CA  1 
ATOM   825  C C   . LEU A  1 108 ? -18.729 13.905  -19.721 1.00 28.31 ? 105 LEU B C   1 
ATOM   826  O O   . LEU A  1 108 ? -18.590 13.323  -20.800 1.00 29.83 ? 105 LEU B O   1 
ATOM   827  C CB  . LEU A  1 108 ? -17.759 13.021  -17.552 1.00 26.26 ? 105 LEU B CB  1 
ATOM   828  C CG  . LEU A  1 108 ? -16.536 12.874  -16.627 1.00 26.25 ? 105 LEU B CG  1 
ATOM   829  C CD1 . LEU A  1 108 ? -16.883 12.172  -15.340 1.00 25.40 ? 105 LEU B CD1 1 
ATOM   830  C CD2 . LEU A  1 108 ? -15.391 12.161  -17.349 1.00 27.65 ? 105 LEU B CD2 1 
ATOM   831  N N   . ILE A  1 109 ? -19.859 14.529  -19.352 1.00 29.02 ? 106 ILE B N   1 
ATOM   832  C CA  . ILE A  1 109 ? -21.051 14.544  -20.205 1.00 29.37 ? 106 ILE B CA  1 
ATOM   833  C C   . ILE A  1 109 ? -20.736 15.286  -21.514 1.00 31.85 ? 106 ILE B C   1 
ATOM   834  O O   . ILE A  1 109 ? -20.924 14.656  -22.551 1.00 32.30 ? 106 ILE B O   1 
ATOM   835  C CB  . ILE A  1 109 ? -22.314 15.086  -19.487 1.00 29.36 ? 106 ILE B CB  1 
ATOM   836  C CG1 . ILE A  1 109 ? -22.755 14.168  -18.352 1.00 27.08 ? 106 ILE B CG1 1 
ATOM   837  C CG2 . ILE A  1 109 ? -23.461 15.343  -20.472 1.00 29.55 ? 106 ILE B CG2 1 
ATOM   838  C CD1 . ILE A  1 109 ? -23.672 14.805  -17.305 1.00 27.42 ? 106 ILE B CD1 1 
ATOM   839  N N   . PRO A  1 110 ? -20.268 16.569  -21.539 1.00 32.36 ? 107 PRO B N   1 
ATOM   840  C CA  . PRO A  1 110 ? -20.093 17.267  -22.815 1.00 36.64 ? 107 PRO B CA  1 
ATOM   841  C C   . PRO A  1 110 ? -19.066 16.675  -23.777 1.00 38.12 ? 107 PRO B C   1 
ATOM   842  O O   . PRO A  1 110 ? -19.164 16.970  -24.961 1.00 40.40 ? 107 PRO B O   1 
ATOM   843  C CB  . PRO A  1 110 ? -19.727 18.720  -22.447 1.00 37.01 ? 107 PRO B CB  1 
ATOM   844  C CG  . PRO A  1 110 ? -19.276 18.647  -21.015 1.00 35.84 ? 107 PRO B CG  1 
ATOM   845  C CD  . PRO A  1 110 ? -19.935 17.442  -20.397 1.00 32.13 ? 107 PRO B CD  1 
ATOM   846  N N   . ASN A  1 111 ? -18.073 15.917  -23.277 1.00 37.71 ? 108 ASN B N   1 
ATOM   847  C CA  . ASN A  1 111 ? -17.028 15.345  -24.123 1.00 39.05 ? 108 ASN B CA  1 
ATOM   848  C C   . ASN A  1 111 ? -17.283 13.886  -24.474 1.00 35.69 ? 108 ASN B C   1 
ATOM   849  O O   . ASN A  1 111 ? -16.516 13.379  -25.291 1.00 34.45 ? 108 ASN B O   1 
ATOM   850  C CB  . ASN A  1 111 ? -15.649 15.603  -23.523 1.00 41.40 ? 108 ASN B CB  1 
ATOM   851  C CG  . ASN A  1 111 ? -15.344 17.085  -23.445 1.00 45.71 ? 108 ASN B CG  1 
ATOM   852  O OD1 . ASN A  1 111 ? -15.457 17.821  -24.435 1.00 52.41 ? 108 ASN B OD1 1 
ATOM   853  N ND2 . ASN A  1 111 ? -14.964 17.566  -22.273 1.00 50.27 ? 108 ASN B ND2 1 
ATOM   854  N N   . ALA A  1 112 ? -18.366 13.270  -23.978 1.00 32.47 ? 109 ALA B N   1 
ATOM   855  C CA  . ALA A  1 112 ? -18.659 11.861  -24.220 1.00 31.96 ? 109 ALA B CA  1 
ATOM   856  C C   . ALA A  1 112 ? -19.017 11.682  -25.695 1.00 35.05 ? 109 ALA B C   1 
ATOM   857  O O   . ALA A  1 112 ? -19.971 12.335  -26.163 1.00 36.22 ? 109 ALA B O   1 
ATOM   858  C CB  . ALA A  1 112 ? -19.753 11.358  -23.270 1.00 29.55 ? 109 ALA B CB  1 
ATOM   859  N N   . SER A  1 113 ? -18.127 10.988  -26.440 1.00 35.09 ? 110 SER B N   1 
ATOM   860  C CA  . SER A  1 113 ? -18.223 10.769  -27.877 1.00 36.05 ? 110 SER B CA  1 
ATOM   861  C C   . SER A  1 113 ? -18.946 9.476   -28.280 1.00 34.28 ? 110 SER B C   1 
ATOM   862  O O   . SER A  1 113 ? -19.063 9.237   -29.474 1.00 34.31 ? 110 SER B O   1 
ATOM   863  C CB  . SER A  1 113 ? -16.830 10.839  -28.515 1.00 40.13 ? 110 SER B CB  1 
ATOM   864  O OG  . SER A  1 113 ? -16.085 9.668   -28.242 1.00 39.22 ? 110 SER B OG  1 
ATOM   865  N N   . GLN A  1 114 ? -19.419 8.677   -27.317 1.00 32.58 ? 111 GLN B N   1 
ATOM   866  C CA  . GLN A  1 114 ? -20.154 7.434   -27.540 1.00 32.36 ? 111 GLN B CA  1 
ATOM   867  C C   . GLN A  1 114 ? -21.432 7.482   -26.710 1.00 30.60 ? 111 GLN B C   1 
ATOM   868  O O   . GLN A  1 114 ? -21.414 8.010   -25.586 1.00 28.40 ? 111 GLN B O   1 
ATOM   869  C CB  . GLN A  1 114 ? -19.311 6.263   -27.020 1.00 34.87 ? 111 GLN B CB  1 
ATOM   870  C CG  . GLN A  1 114 ? -18.044 5.937   -27.825 1.00 38.26 ? 111 GLN B CG  1 
ATOM   871  C CD  . GLN A  1 114 ? -18.332 5.357   -29.198 1.00 43.65 ? 111 GLN B CD  1 
ATOM   872  O OE1 . GLN A  1 114 ? -17.633 5.613   -30.181 1.00 47.82 ? 111 GLN B OE1 1 
ATOM   873  N NE2 . GLN A  1 114 ? -19.392 4.566   -29.292 1.00 45.11 ? 111 GLN B NE2 1 
ATOM   874  N N   . ALA A  1 115 ? -22.519 6.883   -27.229 1.00 30.42 ? 112 ALA B N   1 
ATOM   875  C CA  . ALA A  1 115 ? -23.775 6.815   -26.481 1.00 30.96 ? 112 ALA B CA  1 
ATOM   876  C C   . ALA A  1 115 ? -23.619 6.045   -25.181 1.00 29.82 ? 112 ALA B C   1 
ATOM   877  O O   . ALA A  1 115 ? -24.178 6.479   -24.170 1.00 28.84 ? 112 ALA B O   1 
ATOM   878  C CB  . ALA A  1 115 ? -24.890 6.205   -27.285 1.00 33.79 ? 112 ALA B CB  1 
ATOM   879  N N   . GLU A  1 116 ? -22.833 4.947   -25.197 1.00 29.23 ? 113 GLU B N   1 
ATOM   880  C CA  . GLU A  1 116 ? -22.623 4.163   -23.992 1.00 29.15 ? 113 GLU B CA  1 
ATOM   881  C C   . GLU A  1 116 ? -22.093 5.005   -22.832 1.00 26.58 ? 113 GLU B C   1 
ATOM   882  O O   . GLU A  1 116 ? -22.639 4.912   -21.745 1.00 25.16 ? 113 GLU B O   1 
ATOM   883  C CB  . GLU A  1 116 ? -21.636 3.005   -24.136 1.00 31.51 ? 113 GLU B CB  1 
ATOM   884  C CG  . GLU A  1 116 ? -22.222 1.812   -24.875 1.00 36.90 ? 113 GLU B CG  1 
ATOM   885  C CD  . GLU A  1 116 ? -21.483 0.485   -24.780 1.00 40.51 ? 113 GLU B CD  1 
ATOM   886  O OE1 . GLU A  1 116 ? -20.529 0.281   -23.985 1.00 47.18 ? 113 GLU B OE1 1 
ATOM   887  O OE2 . GLU A  1 116 ? -21.932 -0.377  -25.537 1.00 37.31 ? 113 GLU B OE2 1 
ATOM   888  N N   A SER A  1 117 ? -21.032 5.797   -23.091 0.50 25.46 ? 114 SER B N   1 
ATOM   889  N N   B SER A  1 117 ? -21.034 5.796   -23.088 0.50 27.16 ? 114 SER B N   1 
ATOM   890  C CA  A SER A  1 117 ? -20.422 6.637   -22.069 0.50 23.93 ? 114 SER B CA  1 
ATOM   891  C CA  B SER A  1 117 ? -20.425 6.636   -22.066 0.50 26.71 ? 114 SER B CA  1 
ATOM   892  C C   A SER A  1 117 ? -21.377 7.758   -21.651 0.50 23.85 ? 114 SER B C   1 
ATOM   893  C C   B SER A  1 117 ? -21.381 7.756   -21.649 0.50 25.30 ? 114 SER B C   1 
ATOM   894  O O   A SER A  1 117 ? -21.457 8.060   -20.467 0.50 23.04 ? 114 SER B O   1 
ATOM   895  O O   B SER A  1 117 ? -21.459 8.061   -20.466 0.50 24.39 ? 114 SER B O   1 
ATOM   896  C CB  A SER A  1 117 ? -19.044 7.158   -22.494 0.50 24.19 ? 114 SER B CB  1 
ATOM   897  C CB  B SER A  1 117 ? -19.082 7.178   -22.529 0.50 28.78 ? 114 SER B CB  1 
ATOM   898  O OG  A SER A  1 117 ? -19.072 8.136   -23.527 0.50 23.63 ? 114 SER B OG  1 
ATOM   899  O OG  B SER A  1 117 ? -18.285 6.131   -23.053 0.50 30.30 ? 114 SER B OG  1 
ATOM   900  N N   . LYS A  1 118 ? -22.100 8.343   -22.618 1.00 25.02 ? 115 LYS B N   1 
ATOM   901  C CA  . LYS A  1 118 ? -23.052 9.409   -22.329 1.00 26.17 ? 115 LYS B CA  1 
ATOM   902  C C   . LYS A  1 118 ? -24.164 8.913   -21.382 1.00 24.91 ? 115 LYS B C   1 
ATOM   903  O O   . LYS A  1 118 ? -24.411 9.579   -20.377 1.00 26.66 ? 115 LYS B O   1 
ATOM   904  C CB  . LYS A  1 118 ? -23.686 10.029  -23.570 1.00 29.08 ? 115 LYS B CB  1 
ATOM   905  C CG  . LYS A  1 118 ? -24.388 11.339  -23.223 1.00 32.97 ? 115 LYS B CG  1 
ATOM   906  C CD  . LYS A  1 118 ? -24.926 12.040  -24.439 1.00 37.04 ? 115 LYS B CD  1 
ATOM   907  C CE  . LYS A  1 118 ? -25.786 13.208  -24.065 1.00 37.15 ? 115 LYS B CE  1 
ATOM   908  N NZ  . LYS A  1 118 ? -26.144 13.937  -25.275 1.00 39.00 ? 115 LYS B NZ  1 
ATOM   909  N N   . VAL A  1 119 ? -24.728 7.731   -21.664 1.00 23.05 ? 116 VAL B N   1 
ATOM   910  C CA  . VAL A  1 119 ? -25.706 7.085   -20.775 1.00 22.01 ? 116 VAL B CA  1 
ATOM   911  C C   . VAL A  1 119 ? -25.088 6.844   -19.404 1.00 20.37 ? 116 VAL B C   1 
ATOM   912  O O   . VAL A  1 119 ? -25.759 7.114   -18.402 1.00 21.23 ? 116 VAL B O   1 
ATOM   913  C CB  . VAL A  1 119 ? -26.290 5.776   -21.355 1.00 21.95 ? 116 VAL B CB  1 
ATOM   914  C CG1 . VAL A  1 119 ? -27.183 4.995   -20.413 1.00 23.59 ? 116 VAL B CG1 1 
ATOM   915  C CG2 . VAL A  1 119 ? -27.072 5.986   -22.613 1.00 24.98 ? 116 VAL B CG2 1 
ATOM   916  N N   . PHE A  1 120 ? -23.864 6.277   -19.359 1.00 20.20 ? 117 PHE B N   1 
ATOM   917  C CA  . PHE A  1 120 ? -23.201 5.991   -18.094 1.00 19.55 ? 117 PHE B CA  1 
ATOM   918  C C   . PHE A  1 120 ? -23.138 7.249   -17.221 1.00 18.56 ? 117 PHE B C   1 
ATOM   919  O O   . PHE A  1 120 ? -23.428 7.192   -16.021 1.00 17.42 ? 117 PHE B O   1 
ATOM   920  C CB  . PHE A  1 120 ? -21.811 5.404   -18.379 1.00 20.39 ? 117 PHE B CB  1 
ATOM   921  C CG  . PHE A  1 120 ? -21.028 5.047   -17.128 1.00 23.45 ? 117 PHE B CG  1 
ATOM   922  C CD1 . PHE A  1 120 ? -20.331 6.009   -16.392 1.00 24.33 ? 117 PHE B CD1 1 
ATOM   923  C CD2 . PHE A  1 120 ? -20.966 3.722   -16.703 1.00 24.11 ? 117 PHE B CD2 1 
ATOM   924  C CE1 . PHE A  1 120 ? -19.636 5.642   -15.238 1.00 25.10 ? 117 PHE B CE1 1 
ATOM   925  C CE2 . PHE A  1 120 ? -20.257 3.362   -15.550 1.00 26.86 ? 117 PHE B CE2 1 
ATOM   926  C CZ  . PHE A  1 120 ? -19.607 4.320   -14.817 1.00 25.27 ? 117 PHE B CZ  1 
ATOM   927  N N   . TYR A  1 121 ? -22.746 8.378   -17.821 1.00 19.28 ? 118 TYR B N   1 
ATOM   928  C CA  . TYR A  1 121 ? -22.594 9.639   -17.111 1.00 19.27 ? 118 TYR B CA  1 
ATOM   929  C C   . TYR A  1 121 ? -23.926 10.277  -16.749 1.00 18.64 ? 118 TYR B C   1 
ATOM   930  O O   . TYR A  1 121 ? -23.963 10.913  -15.701 1.00 20.74 ? 118 TYR B O   1 
ATOM   931  C CB  . TYR A  1 121 ? -21.737 10.630  -17.914 1.00 20.98 ? 118 TYR B CB  1 
ATOM   932  C CG  . TYR A  1 121 ? -20.301 10.174  -18.147 1.00 21.82 ? 118 TYR B CG  1 
ATOM   933  C CD1 . TYR A  1 121 ? -19.502 9.680   -17.112 1.00 21.30 ? 118 TYR B CD1 1 
ATOM   934  C CD2 . TYR A  1 121 ? -19.734 10.256  -19.417 1.00 24.08 ? 118 TYR B CD2 1 
ATOM   935  C CE1 . TYR A  1 121 ? -18.181 9.285   -17.337 1.00 21.78 ? 118 TYR B CE1 1 
ATOM   936  C CE2 . TYR A  1 121 ? -18.441 9.805   -19.656 1.00 24.29 ? 118 TYR B CE2 1 
ATOM   937  C CZ  . TYR A  1 121 ? -17.661 9.335   -18.613 1.00 23.94 ? 118 TYR B CZ  1 
ATOM   938  O OH  . TYR A  1 121 ? -16.368 8.956   -18.843 1.00 24.72 ? 118 TYR B OH  1 
ATOM   939  N N   . LEU A  1 122 ? -24.925 10.234  -17.641 1.00 20.04 ? 119 LEU B N   1 
ATOM   940  C CA  . LEU A  1 122 ? -26.258 10.747  -17.327 1.00 19.60 ? 119 LEU B CA  1 
ATOM   941  C C   . LEU A  1 122 ? -26.869 9.946   -16.179 1.00 18.39 ? 119 LEU B C   1 
ATOM   942  O O   . LEU A  1 122 ? -27.464 10.537  -15.281 1.00 19.54 ? 119 LEU B O   1 
ATOM   943  C CB  . LEU A  1 122 ? -27.148 10.819  -18.563 1.00 21.20 ? 119 LEU B CB  1 
ATOM   944  C CG  . LEU A  1 122 ? -26.811 11.931  -19.567 1.00 23.55 ? 119 LEU B CG  1 
ATOM   945  C CD1 . LEU A  1 122 ? -27.643 11.737  -20.808 1.00 25.11 ? 119 LEU B CD1 1 
ATOM   946  C CD2 . LEU A  1 122 ? -27.045 13.327  -18.971 1.00 24.49 ? 119 LEU B CD2 1 
ATOM   947  N N   . LYS A  1 123 ? -26.679 8.616   -16.170 1.00 18.36 ? 120 LYS B N   1 
ATOM   948  C CA  . LYS A  1 123 ? -27.048 7.764   -15.042 1.00 17.41 ? 120 LYS B CA  1 
ATOM   949  C C   . LYS A  1 123 ? -26.341 8.171   -13.750 1.00 17.60 ? 120 LYS B C   1 
ATOM   950  O O   . LYS A  1 123 ? -26.972 8.293   -12.680 1.00 16.72 ? 120 LYS B O   1 
ATOM   951  C CB  . LYS A  1 123 ? -26.724 6.294   -15.303 1.00 18.36 ? 120 LYS B CB  1 
ATOM   952  C CG  . LYS A  1 123 ? -27.163 5.298   -14.244 1.00 18.69 ? 120 LYS B CG  1 
ATOM   953  C CD  . LYS A  1 123 ? -26.578 3.904   -14.465 1.00 18.77 ? 120 LYS B CD  1 
ATOM   954  C CE  . LYS A  1 123 ? -26.430 3.179   -13.160 1.00 17.04 ? 120 LYS B CE  1 
ATOM   955  N NZ  . LYS A  1 123 ? -25.396 3.748   -12.270 1.00 17.18 ? 120 LYS B NZ  1 
ATOM   956  N N   . MET A  1 124 ? -25.015 8.403   -13.826 1.00 19.27 ? 121 MET B N   1 
ATOM   957  C CA  A MET A  1 124 ? -24.259 8.867   -12.674 0.50 18.18 ? 121 MET B CA  1 
ATOM   958  C CA  B MET A  1 124 ? -24.254 8.868   -12.673 0.50 18.51 ? 121 MET B CA  1 
ATOM   959  C C   . MET A  1 124 ? -24.782 10.209  -12.143 1.00 18.14 ? 121 MET B C   1 
ATOM   960  O O   . MET A  1 124 ? -24.912 10.400  -10.915 1.00 17.47 ? 121 MET B O   1 
ATOM   961  C CB  A MET A  1 124 ? -22.780 8.973   -13.044 0.50 18.82 ? 121 MET B CB  1 
ATOM   962  C CB  B MET A  1 124 ? -22.758 8.993   -12.990 0.50 19.63 ? 121 MET B CB  1 
ATOM   963  C CG  A MET A  1 124 ? -21.855 9.028   -11.868 0.50 18.62 ? 121 MET B CG  1 
ATOM   964  C CG  B MET A  1 124 ? -21.899 9.061   -11.729 0.50 19.94 ? 121 MET B CG  1 
ATOM   965  S SD  A MET A  1 124 ? -20.228 8.613   -12.525 0.50 19.65 ? 121 MET B SD  1 
ATOM   966  S SD  B MET A  1 124 ? -20.152 9.383   -11.998 0.50 22.31 ? 121 MET B SD  1 
ATOM   967  C CE  A MET A  1 124 ? -19.474 8.539   -10.894 0.50 18.48 ? 121 MET B CE  1 
ATOM   968  C CE  B MET A  1 124 ? -20.248 8.481   -13.543 0.50 21.25 ? 121 MET B CE  1 
ATOM   969  N N   . LYS A  1 125 ? -25.132 11.146  -13.043 1.00 19.33 ? 122 LYS B N   1 
ATOM   970  C CA  . LYS A  1 125 ? -25.709 12.418  -12.635 1.00 19.21 ? 122 LYS B CA  1 
ATOM   971  C C   . LYS A  1 125 ? -27.036 12.200  -11.868 1.00 19.49 ? 122 LYS B C   1 
ATOM   972  O O   . LYS A  1 125 ? -27.276 12.842  -10.823 1.00 20.20 ? 122 LYS B O   1 
ATOM   973  C CB  . LYS A  1 125 ? -25.864 13.335  -13.861 1.00 19.52 ? 122 LYS B CB  1 
ATOM   974  C CG  . LYS A  1 125 ? -26.454 14.716  -13.623 1.00 19.59 ? 122 LYS B CG  1 
ATOM   975  C CD  . LYS A  1 125 ? -26.487 15.521  -14.905 1.00 21.90 ? 122 LYS B CD  1 
ATOM   976  C CE  . LYS A  1 125 ? -27.020 16.917  -14.711 1.00 22.85 ? 122 LYS B CE  1 
ATOM   977  N NZ  . LYS A  1 125 ? -26.983 17.662  -15.987 1.00 25.52 ? 122 LYS B NZ  1 
ATOM   978  N N   . GLY A  1 126 ? -27.904 11.342  -12.411 1.00 19.05 ? 123 GLY B N   1 
ATOM   979  C CA  . GLY A  1 126 ? -29.125 10.951  -11.741 1.00 19.81 ? 123 GLY B CA  1 
ATOM   980  C C   . GLY A  1 126 ? -28.843 10.383  -10.331 1.00 19.06 ? 123 GLY B C   1 
ATOM   981  O O   . GLY A  1 126 ? -29.512 10.810  -9.389  1.00 17.77 ? 123 GLY B O   1 
ATOM   982  N N   . ASP A  1 127 ? -27.838 9.505   -10.227 1.00 17.81 ? 124 ASP B N   1 
ATOM   983  C CA  . ASP A  1 127 ? -27.438 8.865   -8.974  1.00 17.84 ? 124 ASP B CA  1 
ATOM   984  C C   . ASP A  1 127 ? -27.022 9.904   -7.930  1.00 17.87 ? 124 ASP B C   1 
ATOM   985  O O   . ASP A  1 127 ? -27.460 9.805   -6.771  1.00 18.23 ? 124 ASP B O   1 
ATOM   986  C CB  . ASP A  1 127 ? -26.334 7.825   -9.221  1.00 16.88 ? 124 ASP B CB  1 
ATOM   987  C CG  . ASP A  1 127 ? -26.700 6.565   -10.008 1.00 17.78 ? 124 ASP B CG  1 
ATOM   988  O OD1 . ASP A  1 127 ? -27.885 6.152   -10.010 1.00 17.66 ? 124 ASP B OD1 1 
ATOM   989  O OD2 . ASP A  1 127 ? -25.778 5.966   -10.620 1.00 16.09 ? 124 ASP B OD2 1 
ATOM   990  N N   . TYR A  1 128 ? -26.106 10.841  -8.298  1.00 17.72 ? 125 TYR B N   1 
ATOM   991  C CA  . TYR A  1 128 ? -25.540 11.777  -7.327  1.00 18.26 ? 125 TYR B CA  1 
ATOM   992  C C   . TYR A  1 128 ? -26.574 12.821  -6.888  1.00 19.04 ? 125 TYR B C   1 
ATOM   993  O O   . TYR A  1 128 ? -26.561 13.245  -5.714  1.00 19.96 ? 125 TYR B O   1 
ATOM   994  C CB  . TYR A  1 128 ? -24.139 12.253  -7.754  1.00 17.70 ? 125 TYR B CB  1 
ATOM   995  C CG  . TYR A  1 128 ? -23.143 11.153  -7.440  1.00 17.35 ? 125 TYR B CG  1 
ATOM   996  C CD1 . TYR A  1 128 ? -22.950 10.096  -8.313  1.00 17.78 ? 125 TYR B CD1 1 
ATOM   997  C CD2 . TYR A  1 128 ? -22.452 11.110  -6.241  1.00 18.53 ? 125 TYR B CD2 1 
ATOM   998  C CE1 . TYR A  1 128 ? -22.091 9.039   -8.045  1.00 17.53 ? 125 TYR B CE1 1 
ATOM   999  C CE2 . TYR A  1 128 ? -21.575 10.057  -5.955  1.00 17.09 ? 125 TYR B CE2 1 
ATOM   1000 C CZ  . TYR A  1 128 ? -21.445 8.986   -6.829  1.00 17.63 ? 125 TYR B CZ  1 
ATOM   1001 O OH  . TYR A  1 128 ? -20.623 7.922   -6.583  1.00 18.29 ? 125 TYR B OH  1 
ATOM   1002 N N   . TYR A  1 129 ? -27.441 13.264  -7.812  1.00 22.07 ? 126 TYR B N   1 
ATOM   1003 C CA  . TYR A  1 129 ? -28.592 14.076  -7.434  1.00 20.78 ? 126 TYR B CA  1 
ATOM   1004 C C   . TYR A  1 129 ? -29.543 13.265  -6.541  1.00 19.41 ? 126 TYR B C   1 
ATOM   1005 O O   . TYR A  1 129 ? -30.095 13.838  -5.629  1.00 19.97 ? 126 TYR B O   1 
ATOM   1006 C CB  . TYR A  1 129 ? -29.344 14.686  -8.619  1.00 22.31 ? 126 TYR B CB  1 
ATOM   1007 C CG  . TYR A  1 129 ? -28.700 15.967  -9.124  1.00 23.97 ? 126 TYR B CG  1 
ATOM   1008 C CD1 . TYR A  1 129 ? -28.793 17.142  -8.358  1.00 24.59 ? 126 TYR B CD1 1 
ATOM   1009 C CD2 . TYR A  1 129 ? -28.082 16.030  -10.382 1.00 23.57 ? 126 TYR B CD2 1 
ATOM   1010 C CE1 . TYR A  1 129 ? -28.257 18.334  -8.811  1.00 26.94 ? 126 TYR B CE1 1 
ATOM   1011 C CE2 . TYR A  1 129 ? -27.529 17.216  -10.838 1.00 25.42 ? 126 TYR B CE2 1 
ATOM   1012 C CZ  . TYR A  1 129 ? -27.631 18.361  -10.057 1.00 27.58 ? 126 TYR B CZ  1 
ATOM   1013 O OH  . TYR A  1 129 ? -27.073 19.508  -10.467 1.00 28.03 ? 126 TYR B OH  1 
ATOM   1014 N N   . ARG A  1 130 ? -29.718 11.964  -6.800  1.00 17.41 ? 127 ARG B N   1 
ATOM   1015 C CA  . ARG A  1 130 ? -30.549 11.110  -5.960  1.00 17.57 ? 127 ARG B CA  1 
ATOM   1016 C C   . ARG A  1 130 ? -30.003 10.983  -4.521  1.00 18.04 ? 127 ARG B C   1 
ATOM   1017 O O   . ARG A  1 130 ? -30.786 11.039  -3.563  1.00 16.91 ? 127 ARG B O   1 
ATOM   1018 C CB  . ARG A  1 130 ? -30.732 9.728   -6.587  1.00 17.71 ? 127 ARG B CB  1 
ATOM   1019 C CG  . ARG A  1 130 ? -31.419 8.713   -5.664  1.00 17.52 ? 127 ARG B CG  1 
ATOM   1020 C CD  . ARG A  1 130 ? -31.947 7.485   -6.437  1.00 15.52 ? 127 ARG B CD  1 
ATOM   1021 N NE  . ARG A  1 130 ? -30.842 6.738   -7.054  1.00 15.40 ? 127 ARG B NE  1 
ATOM   1022 C CZ  . ARG A  1 130 ? -30.044 5.854   -6.440  1.00 15.46 ? 127 ARG B CZ  1 
ATOM   1023 N NH1 . ARG A  1 130 ? -30.247 5.485   -5.183  1.00 15.25 ? 127 ARG B NH1 1 
ATOM   1024 N NH2 . ARG A  1 130 ? -29.026 5.328   -7.078  1.00 14.46 ? 127 ARG B NH2 1 
ATOM   1025 N N   . TYR A  1 131 ? -28.687 10.859  -4.378  1.00 17.11 ? 128 TYR B N   1 
ATOM   1026 C CA  . TYR A  1 131 ? -28.073 10.870  -3.062  1.00 17.54 ? 128 TYR B CA  1 
ATOM   1027 C C   . TYR A  1 131 ? -28.255 12.208  -2.360  1.00 18.69 ? 128 TYR B C   1 
ATOM   1028 O O   . TYR A  1 131 ? -28.515 12.199  -1.153  1.00 20.24 ? 128 TYR B O   1 
ATOM   1029 C CB  . TYR A  1 131 ? -26.597 10.459  -3.129  1.00 17.59 ? 128 TYR B CB  1 
ATOM   1030 C CG  . TYR A  1 131 ? -26.297 9.163   -3.848  1.00 17.80 ? 128 TYR B CG  1 
ATOM   1031 C CD1 . TYR A  1 131 ? -27.174 8.068   -3.846  1.00 16.67 ? 128 TYR B CD1 1 
ATOM   1032 C CD2 . TYR A  1 131 ? -25.115 9.032   -4.592  1.00 17.60 ? 128 TYR B CD2 1 
ATOM   1033 C CE1 . TYR A  1 131 ? -26.906 6.911   -4.566  1.00 16.18 ? 128 TYR B CE1 1 
ATOM   1034 C CE2 . TYR A  1 131 ? -24.825 7.870   -5.285  1.00 16.41 ? 128 TYR B CE2 1 
ATOM   1035 C CZ  . TYR A  1 131 ? -25.708 6.785   -5.246  1.00 16.31 ? 128 TYR B CZ  1 
ATOM   1036 O OH  . TYR A  1 131 ? -25.431 5.627   -5.914  1.00 15.25 ? 128 TYR B OH  1 
ATOM   1037 N N   . LEU A  1 132 ? -28.163 13.338  -3.084  1.00 19.59 ? 129 LEU B N   1 
ATOM   1038 C CA  . LEU A  1 132 ? -28.552 14.640  -2.535  1.00 21.89 ? 129 LEU B CA  1 
ATOM   1039 C C   . LEU A  1 132 ? -30.021 14.634  -2.078  1.00 21.47 ? 129 LEU B C   1 
ATOM   1040 O O   . LEU A  1 132 ? -30.322 15.163  -0.998  1.00 21.91 ? 129 LEU B O   1 
ATOM   1041 C CB  . LEU A  1 132 ? -28.284 15.794  -3.504  1.00 24.57 ? 129 LEU B CB  1 
ATOM   1042 C CG  . LEU A  1 132 ? -26.815 16.131  -3.796  1.00 25.35 ? 129 LEU B CG  1 
ATOM   1043 C CD1 . LEU A  1 132 ? -26.768 17.231  -4.881  1.00 25.78 ? 129 LEU B CD1 1 
ATOM   1044 C CD2 . LEU A  1 132 ? -26.111 16.613  -2.553  1.00 26.31 ? 129 LEU B CD2 1 
ATOM   1045 N N   . ALA A  1 133 ? -30.915 14.031  -2.876  1.00 21.67 ? 130 ALA B N   1 
ATOM   1046 C CA  . ALA A  1 133 ? -32.341 14.007  -2.569  1.00 22.22 ? 130 ALA B CA  1 
ATOM   1047 C C   . ALA A  1 133 ? -32.636 13.174  -1.300  1.00 22.47 ? 130 ALA B C   1 
ATOM   1048 O O   . ALA A  1 133 ? -33.601 13.435  -0.594  1.00 21.93 ? 130 ALA B O   1 
ATOM   1049 C CB  . ALA A  1 133 ? -33.128 13.507  -3.756  1.00 22.73 ? 130 ALA B CB  1 
ATOM   1050 N N   . GLU A  1 134 ? -31.769 12.209  -0.966  1.00 21.24 ? 131 GLU B N   1 
ATOM   1051 C CA  . GLU A  1 134 ? -31.909 11.428  0.260   1.00 21.34 ? 131 GLU B CA  1 
ATOM   1052 C C   . GLU A  1 134 ? -31.864 12.277  1.528   1.00 22.76 ? 131 GLU B C   1 
ATOM   1053 O O   . GLU A  1 134 ? -32.477 11.880  2.499   1.00 24.47 ? 131 GLU B O   1 
ATOM   1054 C CB  . GLU A  1 134 ? -30.937 10.261  0.372   1.00 19.89 ? 131 GLU B CB  1 
ATOM   1055 C CG  . GLU A  1 134 ? -31.056 9.159   -0.666  1.00 18.78 ? 131 GLU B CG  1 
ATOM   1056 C CD  . GLU A  1 134 ? -29.959 8.098   -0.640  1.00 17.63 ? 131 GLU B CD  1 
ATOM   1057 O OE1 . GLU A  1 134 ? -28.930 8.258   0.035   1.00 18.40 ? 131 GLU B OE1 1 
ATOM   1058 O OE2 . GLU A  1 134 ? -30.180 7.108   -1.332  1.00 20.23 ? 131 GLU B OE2 1 
ATOM   1059 N N   . VAL A  1 135 ? -31.163 13.413  1.533   1.00 23.47 ? 132 VAL B N   1 
ATOM   1060 C CA  . VAL A  1 135 ? -31.013 14.225  2.728   1.00 26.47 ? 132 VAL B CA  1 
ATOM   1061 C C   . VAL A  1 135 ? -31.624 15.626  2.578   1.00 30.10 ? 132 VAL B C   1 
ATOM   1062 O O   . VAL A  1 135 ? -31.681 16.336  3.582   1.00 32.57 ? 132 VAL B O   1 
ATOM   1063 C CB  . VAL A  1 135 ? -29.512 14.233  3.111   1.00 25.97 ? 132 VAL B CB  1 
ATOM   1064 C CG1 . VAL A  1 135 ? -28.972 12.787  3.156   1.00 24.34 ? 132 VAL B CG1 1 
ATOM   1065 C CG2 . VAL A  1 135 ? -28.621 15.093  2.206   1.00 25.58 ? 132 VAL B CG2 1 
ATOM   1066 N N   . ALA A  1 136 ? -32.108 16.038  1.384   1.00 30.04 ? 133 ALA B N   1 
ATOM   1067 C CA  . ALA A  1 136 ? -32.514 17.423  1.185   1.00 31.47 ? 133 ALA B CA  1 
ATOM   1068 C C   . ALA A  1 136 ? -33.891 17.681  1.828   1.00 32.79 ? 133 ALA B C   1 
ATOM   1069 O O   . ALA A  1 136 ? -34.675 16.751  1.952   1.00 29.58 ? 133 ALA B O   1 
ATOM   1070 C CB  . ALA A  1 136 ? -32.502 17.741  -0.299  1.00 32.56 ? 133 ALA B CB  1 
ATOM   1071 N N   . ALA A  1 137 ? -34.190 18.951  2.169   1.00 36.78 ? 134 ALA B N   1 
ATOM   1072 C CA  . ALA A  1 137 ? -35.520 19.424  2.575   1.00 39.64 ? 134 ALA B CA  1 
ATOM   1073 C C   . ALA A  1 137 ? -35.943 20.746  1.891   1.00 45.76 ? 134 ALA B C   1 
ATOM   1074 O O   . ALA A  1 137 ? -35.132 21.441  1.281   1.00 44.07 ? 134 ALA B O   1 
ATOM   1075 C CB  . ALA A  1 137 ? -35.512 19.580  4.079   1.00 41.22 ? 134 ALA B CB  1 
ATOM   1076 N N   . GLY A  1 138 ? -37.246 21.097  1.977   1.00 49.65 ? 135 GLY B N   1 
ATOM   1077 C CA  . GLY A  1 138 ? -37.746 22.429  1.616   1.00 54.11 ? 135 GLY B CA  1 
ATOM   1078 C C   . GLY A  1 138 ? -37.722 22.718  0.104   1.00 54.93 ? 135 GLY B C   1 
ATOM   1079 O O   . GLY A  1 138 ? -37.851 21.790  -0.700  1.00 58.00 ? 135 GLY B O   1 
ATOM   1080 N N   . ASP A  1 139 ? -37.556 24.007  -0.274  1.00 58.18 ? 136 ASP B N   1 
ATOM   1081 C CA  . ASP A  1 139 ? -37.555 24.429  -1.683  1.00 56.28 ? 136 ASP B CA  1 
ATOM   1082 C C   . ASP A  1 139 ? -36.404 23.739  -2.451  1.00 51.57 ? 136 ASP B C   1 
ATOM   1083 O O   . ASP A  1 139 ? -36.607 23.250  -3.557  1.00 51.94 ? 136 ASP B O   1 
ATOM   1084 C CB  . ASP A  1 139 ? -37.763 25.943  -1.837  1.00 54.99 ? 136 ASP B CB  1 
ATOM   1085 N N   . ASP A  1 140 ? -35.230 23.577  -1.820  1.00 49.99 ? 137 ASP B N   1 
ATOM   1086 C CA  . ASP A  1 140 ? -34.023 22.955  -2.372  1.00 45.74 ? 137 ASP B CA  1 
ATOM   1087 C C   . ASP A  1 140 ? -34.215 21.508  -2.885  1.00 42.04 ? 137 ASP B C   1 
ATOM   1088 O O   . ASP A  1 140 ? -33.640 21.102  -3.910  1.00 36.65 ? 137 ASP B O   1 
ATOM   1089 C CB  . ASP A  1 140 ? -32.963 22.999  -1.276  1.00 49.35 ? 137 ASP B CB  1 
ATOM   1090 C CG  . ASP A  1 140 ? -31.610 22.385  -1.599  1.00 53.37 ? 137 ASP B CG  1 
ATOM   1091 O OD1 . ASP A  1 140 ? -31.042 22.819  -2.625  1.00 56.34 ? 137 ASP B OD1 1 
ATOM   1092 O OD2 . ASP A  1 140 ? -31.157 21.463  -0.851  1.00 55.99 ? 137 ASP B OD2 1 
ATOM   1093 N N   . LYS A  1 141 ? -35.004 20.717  -2.139  1.00 39.77 ? 138 LYS B N   1 
ATOM   1094 C CA  . LYS A  1 141 ? -35.269 19.330  -2.471  1.00 37.60 ? 138 LYS B CA  1 
ATOM   1095 C C   . LYS A  1 141 ? -35.975 19.201  -3.813  1.00 36.42 ? 138 LYS B C   1 
ATOM   1096 O O   . LYS A  1 141 ? -35.633 18.310  -4.588  1.00 31.01 ? 138 LYS B O   1 
ATOM   1097 C CB  . LYS A  1 141 ? -36.155 18.635  -1.435  1.00 39.50 ? 138 LYS B CB  1 
ATOM   1098 C CG  . LYS A  1 141 ? -36.291 17.124  -1.623  1.00 39.85 ? 138 LYS B CG  1 
ATOM   1099 C CD  . LYS A  1 141 ? -37.016 16.448  -0.467  1.00 45.46 ? 138 LYS B CD  1 
ATOM   1100 C CE  . LYS A  1 141 ? -36.802 14.976  -0.331  1.00 43.20 ? 138 LYS B CE  1 
ATOM   1101 N NZ  . LYS A  1 141 ? -37.959 14.226  -0.800  1.00 43.28 ? 138 LYS B NZ  1 
ATOM   1102 N N   . LYS A  1 142 ? -37.002 20.038  -4.044  1.00 40.62 ? 139 LYS B N   1 
ATOM   1103 C CA  . LYS A  1 142 ? -37.723 20.054  -5.313  1.00 41.69 ? 139 LYS B CA  1 
ATOM   1104 C C   . LYS A  1 142 ? -36.766 20.198  -6.504  1.00 35.50 ? 139 LYS B C   1 
ATOM   1105 O O   . LYS A  1 142 ? -36.855 19.412  -7.430  1.00 32.94 ? 139 LYS B O   1 
ATOM   1106 C CB  . LYS A  1 142 ? -38.839 21.105  -5.325  1.00 47.08 ? 139 LYS B CB  1 
ATOM   1107 C CG  . LYS A  1 142 ? -39.691 21.131  -6.594  1.00 56.32 ? 139 LYS B CG  1 
ATOM   1108 C CD  . LYS A  1 142 ? -39.233 22.104  -7.685  1.00 65.44 ? 139 LYS B CD  1 
ATOM   1109 C CE  . LYS A  1 142 ? -40.332 22.536  -8.617  1.00 69.34 ? 139 LYS B CE  1 
ATOM   1110 N NZ  . LYS A  1 142 ? -40.989 21.393  -9.255  1.00 69.46 ? 139 LYS B NZ  1 
ATOM   1111 N N   . GLY A  1 143 ? -35.844 21.156  -6.442  1.00 35.76 ? 140 GLY B N   1 
ATOM   1112 C CA  . GLY A  1 143 ? -34.841 21.350  -7.476  1.00 34.68 ? 140 GLY B CA  1 
ATOM   1113 C C   . GLY A  1 143 ? -33.944 20.142  -7.705  1.00 32.54 ? 140 GLY B C   1 
ATOM   1114 O O   . GLY A  1 143 ? -33.692 19.767  -8.848  1.00 31.64 ? 140 GLY B O   1 
ATOM   1115 N N   . ILE A  1 144 ? -33.498 19.517  -6.608  1.00 30.20 ? 141 ILE B N   1 
ATOM   1116 C CA  . ILE A  1 144 ? -32.627 18.360  -6.660  1.00 27.73 ? 141 ILE B CA  1 
ATOM   1117 C C   . ILE A  1 144 ? -33.343 17.162  -7.293  1.00 25.06 ? 141 ILE B C   1 
ATOM   1118 O O   . ILE A  1 144 ? -32.761 16.453  -8.116  1.00 22.06 ? 141 ILE B O   1 
ATOM   1119 C CB  . ILE A  1 144 ? -32.054 18.100  -5.244  1.00 28.10 ? 141 ILE B CB  1 
ATOM   1120 C CG1 . ILE A  1 144 ? -31.033 19.202  -4.855  1.00 31.11 ? 141 ILE B CG1 1 
ATOM   1121 C CG2 . ILE A  1 144 ? -31.467 16.703  -5.096  1.00 27.00 ? 141 ILE B CG2 1 
ATOM   1122 C CD1 . ILE A  1 144 ? -30.647 19.245  -3.386  1.00 31.80 ? 141 ILE B CD1 1 
ATOM   1123 N N   . VAL A  1 145 ? -34.574 16.886  -6.852  1.00 24.55 ? 142 VAL B N   1 
ATOM   1124 C CA  . VAL A  1 145 ? -35.373 15.778  -7.355  1.00 24.54 ? 142 VAL B CA  1 
ATOM   1125 C C   . VAL A  1 145 ? -35.602 15.938  -8.858  1.00 24.99 ? 142 VAL B C   1 
ATOM   1126 O O   . VAL A  1 145 ? -35.432 14.971  -9.574  1.00 24.06 ? 142 VAL B O   1 
ATOM   1127 C CB  . VAL A  1 145 ? -36.685 15.597  -6.546  1.00 26.42 ? 142 VAL B CB  1 
ATOM   1128 C CG1 . VAL A  1 145 ? -37.660 14.598  -7.178  1.00 26.74 ? 142 VAL B CG1 1 
ATOM   1129 C CG2 . VAL A  1 145 ? -36.402 15.187  -5.093  1.00 25.48 ? 142 VAL B CG2 1 
ATOM   1130 N N   . ASP A  1 146 ? -35.977 17.143  -9.318  1.00 29.13 ? 143 ASP B N   1 
ATOM   1131 C CA  . ASP A  1 146 ? -36.146 17.434  -10.738 1.00 31.30 ? 143 ASP B CA  1 
ATOM   1132 C C   . ASP A  1 146 ? -34.859 17.207  -11.547 1.00 28.82 ? 143 ASP B C   1 
ATOM   1133 O O   . ASP A  1 146 ? -34.922 16.618  -12.615 1.00 27.19 ? 143 ASP B O   1 
ATOM   1134 C CB  . ASP A  1 146 ? -36.764 18.810  -10.937 1.00 37.13 ? 143 ASP B CB  1 
ATOM   1135 C CG  . ASP A  1 146 ? -38.237 18.947  -10.536 1.00 44.64 ? 143 ASP B CG  1 
ATOM   1136 O OD1 . ASP A  1 146 ? -38.928 17.895  -10.349 1.00 44.33 ? 143 ASP B OD1 1 
ATOM   1137 O OD2 . ASP A  1 146 ? -38.691 20.117  -10.403 1.00 54.12 ? 143 ASP B OD2 1 
ATOM   1138 N N   . GLN A  1 147 ? -33.696 17.587  -11.002 1.00 28.66 ? 144 GLN B N   1 
ATOM   1139 C CA  . GLN A  1 147 ? -32.405 17.354  -11.658 1.00 26.79 ? 144 GLN B CA  1 
ATOM   1140 C C   . GLN A  1 147 ? -32.134 15.861  -11.800 1.00 24.61 ? 144 GLN B C   1 
ATOM   1141 O O   . GLN A  1 147 ? -31.721 15.414  -12.866 1.00 24.44 ? 144 GLN B O   1 
ATOM   1142 C CB  . GLN A  1 147 ? -31.240 18.044  -10.958 1.00 27.75 ? 144 GLN B CB  1 
ATOM   1143 C CG  . GLN A  1 147 ? -31.176 19.563  -11.066 1.00 31.33 ? 144 GLN B CG  1 
ATOM   1144 C CD  . GLN A  1 147 ? -30.924 20.051  -12.478 1.00 33.42 ? 144 GLN B CD  1 
ATOM   1145 O OE1 . GLN A  1 147 ? -30.076 19.534  -13.218 1.00 32.82 ? 144 GLN B OE1 1 
ATOM   1146 N NE2 . GLN A  1 147 ? -31.764 20.968  -12.923 1.00 38.66 ? 144 GLN B NE2 1 
ATOM   1147 N N   . SER A  1 148 ? -32.397 15.088  -10.740 1.00 23.04 ? 145 SER B N   1 
ATOM   1148 C CA  . SER A  1 148 ? -32.185 13.644  -10.779 1.00 22.24 ? 145 SER B CA  1 
ATOM   1149 C C   . SER A  1 148 ? -33.073 13.034  -11.851 1.00 21.60 ? 145 SER B C   1 
ATOM   1150 O O   . SER A  1 148 ? -32.592 12.254  -12.668 1.00 21.49 ? 145 SER B O   1 
ATOM   1151 C CB  . SER A  1 148 ? -32.407 13.010  -9.429  1.00 21.26 ? 145 SER B CB  1 
ATOM   1152 O OG  . SER A  1 148 ? -32.186 11.615  -9.472  1.00 19.52 ? 145 SER B OG  1 
ATOM   1153 N N   . GLN A  1 149 ? -34.375 13.394  -11.821 1.00 23.07 ? 146 GLN B N   1 
ATOM   1154 C CA  . GLN A  1 149 ? -35.325 12.795  -12.741 1.00 24.05 ? 146 GLN B CA  1 
ATOM   1155 C C   . GLN A  1 149 ? -34.984 13.111  -14.214 1.00 24.35 ? 146 GLN B C   1 
ATOM   1156 O O   . GLN A  1 149 ? -35.021 12.191  -15.039 1.00 23.31 ? 146 GLN B O   1 
ATOM   1157 C CB  . GLN A  1 149 ? -36.748 13.245  -12.416 1.00 27.01 ? 146 GLN B CB  1 
ATOM   1158 C CG  . GLN A  1 149 ? -37.780 12.441  -13.193 1.00 28.18 ? 146 GLN B CG  1 
ATOM   1159 C CD  . GLN A  1 149 ? -39.173 12.555  -12.619 1.00 32.21 ? 146 GLN B CD  1 
ATOM   1160 O OE1 . GLN A  1 149 ? -39.433 13.408  -11.778 1.00 31.59 ? 146 GLN B OE1 1 
ATOM   1161 N NE2 . GLN A  1 149 ? -40.080 11.700  -13.069 1.00 33.52 ? 146 GLN B NE2 1 
ATOM   1162 N N   . GLN A  1 150 ? -34.620 14.371  -14.491 1.00 26.15 ? 147 GLN B N   1 
ATOM   1163 C CA  . GLN A  1 150 ? -34.273 14.826  -15.846 1.00 29.63 ? 147 GLN B CA  1 
ATOM   1164 C C   . GLN A  1 150 ? -33.051 14.066  -16.369 1.00 26.76 ? 147 GLN B C   1 
ATOM   1165 O O   . GLN A  1 150 ? -33.034 13.704  -17.538 1.00 25.49 ? 147 GLN B O   1 
ATOM   1166 C CB  . GLN A  1 150 ? -34.080 16.340  -15.928 1.00 34.64 ? 147 GLN B CB  1 
ATOM   1167 C CG  . GLN A  1 150 ? -35.387 17.125  -16.045 1.00 42.87 ? 147 GLN B CG  1 
ATOM   1168 C CD  . GLN A  1 150 ? -35.287 18.602  -15.664 1.00 53.25 ? 147 GLN B CD  1 
ATOM   1169 O OE1 . GLN A  1 150 ? -34.352 19.306  -16.063 1.00 59.15 ? 147 GLN B OE1 1 
ATOM   1170 N NE2 . GLN A  1 150 ? -36.233 19.103  -14.868 1.00 60.45 ? 147 GLN B NE2 1 
ATOM   1171 N N   . ALA A  1 151 ? -32.072 13.808  -15.493 1.00 25.06 ? 148 ALA B N   1 
ATOM   1172 C CA  . ALA A  1 151 ? -30.848 13.126  -15.879 1.00 22.62 ? 148 ALA B CA  1 
ATOM   1173 C C   . ALA A  1 151 ? -31.134 11.660  -16.183 1.00 21.76 ? 148 ALA B C   1 
ATOM   1174 O O   . ALA A  1 151 ? -30.742 11.142  -17.220 1.00 21.88 ? 148 ALA B O   1 
ATOM   1175 C CB  . ALA A  1 151 ? -29.798 13.256  -14.782 1.00 21.91 ? 148 ALA B CB  1 
ATOM   1176 N N   . TYR A  1 152 ? -31.886 11.015  -15.284 1.00 20.17 ? 149 TYR B N   1 
ATOM   1177 C CA  . TYR A  1 152 ? -32.325 9.654   -15.516 1.00 19.10 ? 149 TYR B CA  1 
ATOM   1178 C C   . TYR A  1 152 ? -33.177 9.515   -16.769 1.00 21.12 ? 149 TYR B C   1 
ATOM   1179 O O   . TYR A  1 152 ? -32.971 8.536   -17.483 1.00 21.03 ? 149 TYR B O   1 
ATOM   1180 C CB  . TYR A  1 152 ? -33.076 9.144   -14.293 1.00 18.18 ? 149 TYR B CB  1 
ATOM   1181 C CG  . TYR A  1 152 ? -32.228 8.709   -13.093 1.00 16.42 ? 149 TYR B CG  1 
ATOM   1182 C CD1 . TYR A  1 152 ? -31.102 7.891   -13.220 1.00 15.98 ? 149 TYR B CD1 1 
ATOM   1183 C CD2 . TYR A  1 152 ? -32.648 9.023   -11.804 1.00 17.52 ? 149 TYR B CD2 1 
ATOM   1184 C CE1 . TYR A  1 152 ? -30.425 7.384   -12.108 1.00 14.85 ? 149 TYR B CE1 1 
ATOM   1185 C CE2 . TYR A  1 152 ? -31.971 8.568   -10.681 1.00 15.65 ? 149 TYR B CE2 1 
ATOM   1186 C CZ  . TYR A  1 152 ? -30.842 7.751   -10.840 1.00 15.40 ? 149 TYR B CZ  1 
ATOM   1187 O OH  . TYR A  1 152 ? -30.229 7.319   -9.689  1.00 16.69 ? 149 TYR B OH  1 
ATOM   1188 N N   . GLN A  1 153 ? -34.119 10.439  -17.010 1.00 21.78 ? 150 GLN B N   1 
ATOM   1189 C CA  . GLN A  1 153 ? -34.989 10.343  -18.164 1.00 21.77 ? 150 GLN B CA  1 
ATOM   1190 C C   . GLN A  1 153 ? -34.203 10.432  -19.490 1.00 23.18 ? 150 GLN B C   1 
ATOM   1191 O O   . GLN A  1 153 ? -34.482 9.660   -20.408 1.00 21.31 ? 150 GLN B O   1 
ATOM   1192 C CB  . GLN A  1 153 ? -36.037 11.464  -18.142 1.00 23.66 ? 150 GLN B CB  1 
ATOM   1193 C CG  . GLN A  1 153 ? -37.176 11.311  -19.131 1.00 24.67 ? 150 GLN B CG  1 
ATOM   1194 C CD  . GLN A  1 153 ? -37.879 9.985   -19.044 1.00 24.98 ? 150 GLN B CD  1 
ATOM   1195 O OE1 . GLN A  1 153 ? -38.178 9.433   -17.972 1.00 25.36 ? 150 GLN B OE1 1 
ATOM   1196 N NE2 . GLN A  1 153 ? -38.081 9.394   -20.200 1.00 27.38 ? 150 GLN B NE2 1 
ATOM   1197 N N   . GLU A  1 154 ? -33.253 11.358  -19.551 1.00 23.08 ? 151 GLU B N   1 
ATOM   1198 C CA  . GLU A  1 154 ? -32.400 11.499  -20.727 1.00 25.44 ? 151 GLU B CA  1 
ATOM   1199 C C   . GLU A  1 154 ? -31.549 10.244  -20.944 1.00 23.30 ? 151 GLU B C   1 
ATOM   1200 O O   . GLU A  1 154 ? -31.533 9.694   -22.056 1.00 22.17 ? 151 GLU B O   1 
ATOM   1201 C CB  . GLU A  1 154 ? -31.510 12.735  -20.703 1.00 27.17 ? 151 GLU B CB  1 
ATOM   1202 C CG  . GLU A  1 154 ? -30.887 12.966  -22.089 1.00 30.83 ? 151 GLU B CG  1 
ATOM   1203 C CD  . GLU A  1 154 ? -29.988 14.165  -22.221 1.00 36.62 ? 151 GLU B CD  1 
ATOM   1204 O OE1 . GLU A  1 154 ? -29.854 14.928  -21.245 1.00 37.37 ? 151 GLU B OE1 1 
ATOM   1205 O OE2 . GLU A  1 154 ? -29.441 14.329  -23.359 1.00 42.60 ? 151 GLU B OE2 1 
ATOM   1206 N N   . ALA A  1 155 ? -30.953 9.734   -19.852 1.00 22.61 ? 152 ALA B N   1 
ATOM   1207 C CA  . ALA A  1 155 ? -30.233 8.469   -19.926 1.00 21.73 ? 152 ALA B CA  1 
ATOM   1208 C C   . ALA A  1 155 ? -31.137 7.351   -20.446 1.00 21.54 ? 152 ALA B C   1 
ATOM   1209 O O   . ALA A  1 155 ? -30.711 6.570   -21.265 1.00 19.97 ? 152 ALA B O   1 
ATOM   1210 C CB  . ALA A  1 155 ? -29.622 8.117   -18.600 1.00 19.74 ? 152 ALA B CB  1 
ATOM   1211 N N   . PHE A  1 156 ? -32.393 7.276   -19.950 1.00 21.88 ? 153 PHE B N   1 
ATOM   1212 C CA  . PHE A  1 156 ? -33.310 6.196   -20.291 1.00 22.95 ? 153 PHE B CA  1 
ATOM   1213 C C   . PHE A  1 156 ? -33.685 6.235   -21.781 1.00 24.02 ? 153 PHE B C   1 
ATOM   1214 O O   . PHE A  1 156 ? -33.844 5.194   -22.406 1.00 23.20 ? 153 PHE B O   1 
ATOM   1215 C CB  . PHE A  1 156 ? -34.519 6.327   -19.361 1.00 24.43 ? 153 PHE B CB  1 
ATOM   1216 C CG  . PHE A  1 156 ? -35.548 5.225   -19.461 1.00 25.54 ? 153 PHE B CG  1 
ATOM   1217 C CD1 . PHE A  1 156 ? -35.360 4.028   -18.795 1.00 26.91 ? 153 PHE B CD1 1 
ATOM   1218 C CD2 . PHE A  1 156 ? -36.683 5.368   -20.269 1.00 31.86 ? 153 PHE B CD2 1 
ATOM   1219 C CE1 . PHE A  1 156 ? -36.301 3.014   -18.860 1.00 28.75 ? 153 PHE B CE1 1 
ATOM   1220 C CE2 . PHE A  1 156 ? -37.619 4.328   -20.354 1.00 32.63 ? 153 PHE B CE2 1 
ATOM   1221 C CZ  . PHE A  1 156 ? -37.453 3.182   -19.597 1.00 32.34 ? 153 PHE B CZ  1 
ATOM   1222 N N   . GLU A  1 157 ? -33.938 7.429   -22.310 1.00 25.77 ? 154 GLU B N   1 
ATOM   1223 C CA  . GLU A  1 157 ? -34.291 7.602   -23.711 1.00 28.86 ? 154 GLU B CA  1 
ATOM   1224 C C   . GLU A  1 157 ? -33.120 7.237   -24.629 1.00 27.23 ? 154 GLU B C   1 
ATOM   1225 O O   . GLU A  1 157 ? -33.358 6.536   -25.605 1.00 29.30 ? 154 GLU B O   1 
ATOM   1226 C CB  . GLU A  1 157 ? -34.756 9.046   -23.939 1.00 31.56 ? 154 GLU B CB  1 
ATOM   1227 C CG  . GLU A  1 157 ? -36.115 9.324   -23.281 1.00 34.82 ? 154 GLU B CG  1 
ATOM   1228 C CD  . GLU A  1 157 ? -36.463 10.814  -23.190 1.00 41.02 ? 154 GLU B CD  1 
ATOM   1229 O OE1 . GLU A  1 157 ? -35.695 11.721  -23.688 1.00 41.75 ? 154 GLU B OE1 1 
ATOM   1230 O OE2 . GLU A  1 157 ? -37.557 11.037  -22.602 1.00 36.32 ? 154 GLU B OE2 1 
ATOM   1231 N N   . ILE A  1 158 ? -31.902 7.679   -24.289 1.00 27.65 ? 155 ILE B N   1 
ATOM   1232 C CA  . ILE A  1 158 ? -30.717 7.390   -25.109 1.00 28.74 ? 155 ILE B CA  1 
ATOM   1233 C C   . ILE A  1 158 ? -30.485 5.882   -25.104 1.00 28.50 ? 155 ILE B C   1 
ATOM   1234 O O   . ILE A  1 158 ? -30.348 5.271   -26.167 1.00 30.91 ? 155 ILE B O   1 
ATOM   1235 C CB  . ILE A  1 158 ? -29.480 8.167   -24.660 1.00 28.34 ? 155 ILE B CB  1 
ATOM   1236 C CG1 . ILE A  1 158 ? -29.693 9.671   -24.838 1.00 29.08 ? 155 ILE B CG1 1 
ATOM   1237 C CG2 . ILE A  1 158 ? -28.199 7.688   -25.381 1.00 32.31 ? 155 ILE B CG2 1 
ATOM   1238 C CD1 . ILE A  1 158 ? -28.646 10.529  -24.172 1.00 29.59 ? 155 ILE B CD1 1 
ATOM   1239 N N   . SER A  1 159 ? -30.540 5.284   -23.903 1.00 25.62 ? 156 SER B N   1 
ATOM   1240 C CA  . SER A  1 159 ? -30.335 3.864   -23.733 1.00 24.73 ? 156 SER B CA  1 
ATOM   1241 C C   . SER A  1 159 ? -31.407 3.059   -24.442 1.00 24.33 ? 156 SER B C   1 
ATOM   1242 O O   . SER A  1 159 ? -31.097 2.020   -25.003 1.00 26.79 ? 156 SER B O   1 
ATOM   1243 C CB  . SER A  1 159 ? -30.318 3.545   -22.228 1.00 24.49 ? 156 SER B CB  1 
ATOM   1244 O OG  . SER A  1 159 ? -30.647 2.206   -22.039 1.00 29.44 ? 156 SER B OG  1 
ATOM   1245 N N   . ALA A  1 160 ? -32.682 3.479   -24.371 1.00 23.84 ? 157 ALA B N   1 
ATOM   1246 C CA  . ALA A  1 160 ? -33.758 2.796   -25.074 1.00 25.73 ? 157 ALA B CA  1 
ATOM   1247 C C   . ALA A  1 160 ? -33.516 2.697   -26.592 1.00 27.43 ? 157 ALA B C   1 
ATOM   1248 O O   . ALA A  1 160 ? -34.031 1.760   -27.193 1.00 30.92 ? 157 ALA B O   1 
ATOM   1249 C CB  . ALA A  1 160 ? -35.142 3.431   -24.842 1.00 27.10 ? 157 ALA B CB  1 
ATOM   1250 N N   . ALA A  1 161 ? -32.806 3.619   -27.189 1.00 29.76 ? 158 ALA B N   1 
ATOM   1251 C CA  . ALA A  1 161 ? -32.562 3.554   -28.633 1.00 33.89 ? 158 ALA B CA  1 
ATOM   1252 C C   . ALA A  1 161 ? -31.137 3.101   -29.000 1.00 34.56 ? 158 ALA B C   1 
ATOM   1253 O O   . ALA A  1 161 ? -30.956 2.639   -30.125 1.00 33.28 ? 158 ALA B O   1 
ATOM   1254 C CB  . ALA A  1 161 ? -32.983 4.849   -29.250 1.00 34.10 ? 158 ALA B CB  1 
ATOM   1255 N N   . ALA A  1 162 ? -30.139 3.249   -28.118 1.00 32.07 ? 159 ALA B N   1 
ATOM   1256 C CA  . ALA A  1 162 ? -28.750 2.893   -28.438 1.00 32.41 ? 159 ALA B CA  1 
ATOM   1257 C C   . ALA A  1 162 ? -28.389 1.453   -28.038 1.00 29.53 ? 159 ALA B C   1 
ATOM   1258 O O   . ALA A  1 162 ? -27.523 0.809   -28.671 1.00 27.89 ? 159 ALA B O   1 
ATOM   1259 C CB  . ALA A  1 162 ? -27.805 3.872   -27.778 1.00 33.82 ? 159 ALA B CB  1 
ATOM   1260 N N   . MET A  1 163 ? -28.996 0.958   -26.950 1.00 25.88 ? 160 MET B N   1 
ATOM   1261 C CA  . MET A  1 163 ? -28.493 -0.188  -26.213 1.00 25.85 ? 160 MET B CA  1 
ATOM   1262 C C   . MET A  1 163 ? -29.509 -1.333  -26.273 1.00 24.14 ? 160 MET B C   1 
ATOM   1263 O O   . MET A  1 163 ? -30.749 -1.134  -26.290 1.00 22.39 ? 160 MET B O   1 
ATOM   1264 C CB  . MET A  1 163 ? -28.207 0.192   -24.770 1.00 25.72 ? 160 MET B CB  1 
ATOM   1265 C CG  . MET A  1 163 ? -27.100 1.240   -24.555 1.00 27.01 ? 160 MET B CG  1 
ATOM   1266 S SD  . MET A  1 163 ? -26.962 1.463   -22.770 1.00 32.73 ? 160 MET B SD  1 
ATOM   1267 C CE  . MET A  1 163 ? -25.563 2.565   -22.675 1.00 31.36 ? 160 MET B CE  1 
ATOM   1268 N N   . GLN A  1 164 ? -28.961 -2.562  -26.265 1.00 23.24 ? 161 GLN B N   1 
ATOM   1269 C CA  A GLN A  1 164 ? -29.773 -3.767  -26.221 0.50 22.65 ? 161 GLN B CA  1 
ATOM   1270 C CA  B GLN A  1 164 ? -29.783 -3.759  -26.221 0.50 23.36 ? 161 GLN B CA  1 
ATOM   1271 C C   . GLN A  1 164 ? -30.302 -3.923  -24.791 1.00 21.21 ? 161 GLN B C   1 
ATOM   1272 O O   . GLN A  1 164 ? -29.667 -3.460  -23.847 1.00 18.98 ? 161 GLN B O   1 
ATOM   1273 C CB  A GLN A  1 164 ? -29.008 -5.009  -26.673 0.50 23.34 ? 161 GLN B CB  1 
ATOM   1274 C CB  B GLN A  1 164 ? -29.026 -4.980  -26.726 0.50 25.18 ? 161 GLN B CB  1 
ATOM   1275 C CG  A GLN A  1 164 ? -28.596 -5.002  -28.150 0.50 24.80 ? 161 GLN B CG  1 
ATOM   1276 C CG  B GLN A  1 164 ? -28.788 -4.948  -28.237 0.50 27.78 ? 161 GLN B CG  1 
ATOM   1277 C CD  A GLN A  1 164 ? -29.675 -5.505  -29.091 0.50 25.58 ? 161 GLN B CD  1 
ATOM   1278 C CD  B GLN A  1 164 ? -27.618 -5.799  -28.674 0.50 29.59 ? 161 GLN B CD  1 
ATOM   1279 O OE1 A GLN A  1 164 ? -30.811 -5.744  -28.679 0.50 26.90 ? 161 GLN B OE1 1 
ATOM   1280 O OE1 B GLN A  1 164 ? -26.706 -6.074  -27.887 0.50 30.23 ? 161 GLN B OE1 1 
ATOM   1281 N NE2 A GLN A  1 164 ? -29.348 -5.719  -30.351 0.50 25.74 ? 161 GLN B NE2 1 
ATOM   1282 N NE2 B GLN A  1 164 ? -27.637 -6.243  -29.919 0.50 31.92 ? 161 GLN B NE2 1 
ATOM   1283 N N   . PRO A  1 165 ? -31.471 -4.576  -24.585 1.00 21.37 ? 162 PRO B N   1 
ATOM   1284 C CA  . PRO A  1 165 ? -32.020 -4.702  -23.218 1.00 21.12 ? 162 PRO B CA  1 
ATOM   1285 C C   . PRO A  1 165 ? -31.137 -5.417  -22.186 1.00 20.91 ? 162 PRO B C   1 
ATOM   1286 O O   . PRO A  1 165 ? -31.324 -5.209  -20.987 1.00 19.91 ? 162 PRO B O   1 
ATOM   1287 C CB  . PRO A  1 165 ? -33.373 -5.324  -23.425 1.00 21.44 ? 162 PRO B CB  1 
ATOM   1288 C CG  . PRO A  1 165 ? -33.685 -5.221  -24.857 1.00 23.29 ? 162 PRO B CG  1 
ATOM   1289 C CD  . PRO A  1 165 ? -32.394 -5.119  -25.589 1.00 22.13 ? 162 PRO B CD  1 
ATOM   1290 N N   . THR A  1 166 ? -30.222 -6.277  -22.656 1.00 20.72 ? 163 THR B N   1 
ATOM   1291 C CA  . THR A  1 166 ? -29.274 -6.986  -21.787 1.00 22.51 ? 163 THR B CA  1 
ATOM   1292 C C   . THR A  1 166 ? -28.018 -6.192  -21.419 1.00 21.99 ? 163 THR B C   1 
ATOM   1293 O O   . THR A  1 166 ? -27.170 -6.728  -20.681 1.00 20.52 ? 163 THR B O   1 
ATOM   1294 C CB  . THR A  1 166 ? -28.893 -8.289  -22.478 1.00 24.75 ? 163 THR B CB  1 
ATOM   1295 O OG1 . THR A  1 166 ? -28.452 -7.990  -23.805 1.00 27.77 ? 163 THR B OG1 1 
ATOM   1296 C CG2 . THR A  1 166 ? -30.102 -9.218  -22.539 1.00 25.52 ? 163 THR B CG2 1 
ATOM   1297 N N   . HIS A  1 167 ? -27.840 -4.969  -21.971 1.00 19.29 ? 164 HIS B N   1 
ATOM   1298 C CA  . HIS A  1 167 ? -26.642 -4.192  -21.753 1.00 18.40 ? 164 HIS B CA  1 
ATOM   1299 C C   . HIS A  1 167 ? -26.565 -3.851  -20.259 1.00 16.82 ? 164 HIS B C   1 
ATOM   1300 O O   . HIS A  1 167 ? -27.530 -3.329  -19.695 1.00 15.37 ? 164 HIS B O   1 
ATOM   1301 C CB  . HIS A  1 167 ? -26.586 -2.969  -22.674 1.00 18.59 ? 164 HIS B CB  1 
ATOM   1302 C CG  . HIS A  1 167 ? -25.245 -2.341  -22.680 1.00 19.81 ? 164 HIS B CG  1 
ATOM   1303 N ND1 . HIS A  1 167 ? -24.581 -1.930  -21.551 1.00 20.09 ? 164 HIS B ND1 1 
ATOM   1304 C CD2 . HIS A  1 167 ? -24.466 -2.061  -23.674 1.00 20.80 ? 164 HIS B CD2 1 
ATOM   1305 C CE1 . HIS A  1 167 ? -23.431 -1.421  -21.857 1.00 21.95 ? 164 HIS B CE1 1 
ATOM   1306 N NE2 . HIS A  1 167 ? -23.328 -1.495  -23.161 1.00 22.55 ? 164 HIS B NE2 1 
ATOM   1307 N N   . PRO A  1 168 ? -25.467 -4.179  -19.558 1.00 17.67 ? 165 PRO B N   1 
ATOM   1308 C CA  . PRO A  1 168 ? -25.378 -3.883  -18.126 1.00 16.04 ? 165 PRO B CA  1 
ATOM   1309 C C   . PRO A  1 168 ? -25.711 -2.432  -17.724 1.00 16.35 ? 165 PRO B C   1 
ATOM   1310 O O   . PRO A  1 168 ? -26.316 -2.205  -16.692 1.00 15.35 ? 165 PRO B O   1 
ATOM   1311 C CB  . PRO A  1 168 ? -23.967 -4.250  -17.716 1.00 17.48 ? 165 PRO B CB  1 
ATOM   1312 C CG  . PRO A  1 168 ? -23.471 -5.058  -18.830 1.00 19.01 ? 165 PRO B CG  1 
ATOM   1313 C CD  . PRO A  1 168 ? -24.259 -4.872  -20.068 1.00 18.20 ? 165 PRO B CD  1 
ATOM   1314 N N   . ILE A  1 169 ? -25.361 -1.449  -18.568 1.00 16.45 ? 166 ILE B N   1 
ATOM   1315 C CA  . ILE A  1 169 ? -25.642 -0.040  -18.287 1.00 16.75 ? 166 ILE B CA  1 
ATOM   1316 C C   . ILE A  1 169 ? -27.147 0.215   -18.356 1.00 16.70 ? 166 ILE B C   1 
ATOM   1317 O O   . ILE A  1 169 ? -27.666 0.936   -17.509 1.00 17.56 ? 166 ILE B O   1 
ATOM   1318 C CB  . ILE A  1 169 ? -24.811 0.907   -19.177 1.00 18.82 ? 166 ILE B CB  1 
ATOM   1319 C CG1 . ILE A  1 169 ? -23.279 0.692   -18.934 1.00 19.53 ? 166 ILE B CG1 1 
ATOM   1320 C CG2 . ILE A  1 169 ? -25.219 2.371   -18.932 1.00 18.67 ? 166 ILE B CG2 1 
ATOM   1321 C CD1 . ILE A  1 169 ? -22.389 1.440   -19.913 1.00 21.80 ? 166 ILE B CD1 1 
ATOM   1322 N N   . ARG A  1 170 ? -27.820 -0.277  -19.401 1.00 17.31 ? 167 ARG B N   1 
ATOM   1323 C CA  . ARG A  1 170 ? -29.264 -0.210  -19.524 1.00 17.84 ? 167 ARG B CA  1 
ATOM   1324 C C   . ARG A  1 170 ? -29.951 -0.870  -18.315 1.00 17.30 ? 167 ARG B C   1 
ATOM   1325 O O   . ARG A  1 170 ? -30.846 -0.251  -17.728 1.00 19.03 ? 167 ARG B O   1 
ATOM   1326 C CB  . ARG A  1 170 ? -29.691 -0.851  -20.851 1.00 18.67 ? 167 ARG B CB  1 
ATOM   1327 C CG  . ARG A  1 170 ? -31.196 -0.766  -21.068 1.00 20.40 ? 167 ARG B CG  1 
ATOM   1328 C CD  . ARG A  1 170 ? -31.637 -0.866  -22.485 1.00 21.95 ? 167 ARG B CD  1 
ATOM   1329 N NE  . ARG A  1 170 ? -33.112 -0.957  -22.551 1.00 22.58 ? 167 ARG B NE  1 
ATOM   1330 C CZ  . ARG A  1 170 ? -33.763 -1.336  -23.640 1.00 22.77 ? 167 ARG B CZ  1 
ATOM   1331 N NH1 . ARG A  1 170 ? -33.110 -1.435  -24.797 1.00 23.71 ? 167 ARG B NH1 1 
ATOM   1332 N NH2 . ARG A  1 170 ? -35.052 -1.557  -23.592 1.00 23.10 ? 167 ARG B NH2 1 
ATOM   1333 N N   . LEU A  1 171 ? -29.483 -2.056  -17.921 1.00 15.69 ? 168 LEU B N   1 
ATOM   1334 C CA  . LEU A  1 171 ? -30.046 -2.743  -16.744 1.00 16.34 ? 168 LEU B CA  1 
ATOM   1335 C C   . LEU A  1 171 ? -29.816 -1.918  -15.463 1.00 16.01 ? 168 LEU B C   1 
ATOM   1336 O O   . LEU A  1 171 ? -30.749 -1.725  -14.679 1.00 15.40 ? 168 LEU B O   1 
ATOM   1337 C CB  . LEU A  1 171 ? -29.426 -4.137  -16.679 1.00 17.26 ? 168 LEU B CB  1 
ATOM   1338 C CG  . LEU A  1 171 ? -29.970 -5.097  -17.746 1.00 18.92 ? 168 LEU B CG  1 
ATOM   1339 C CD1 . LEU A  1 171 ? -29.032 -6.269  -17.814 1.00 21.16 ? 168 LEU B CD1 1 
ATOM   1340 C CD2 . LEU A  1 171 ? -31.437 -5.492  -17.500 1.00 19.22 ? 168 LEU B CD2 1 
ATOM   1341 N N   . GLY A  1 172 ? -28.567 -1.485  -15.261 1.00 14.24 ? 169 GLY B N   1 
ATOM   1342 C CA  . GLY A  1 172 ? -28.200 -0.682  -14.084 1.00 14.11 ? 169 GLY B CA  1 
ATOM   1343 C C   . GLY A  1 172 ? -28.964 0.623   -13.948 1.00 12.95 ? 169 GLY B C   1 
ATOM   1344 O O   . GLY A  1 172 ? -29.440 0.991   -12.873 1.00 13.51 ? 169 GLY B O   1 
ATOM   1345 N N   . LEU A  1 173 ? -29.158 1.303   -15.086 1.00 14.86 ? 170 LEU B N   1 
ATOM   1346 C CA  . LEU A  1 173 ? -30.002 2.489   -15.132 1.00 14.08 ? 170 LEU B CA  1 
ATOM   1347 C C   . LEU A  1 173 ? -31.447 2.141   -14.753 1.00 14.31 ? 170 LEU B C   1 
ATOM   1348 O O   . LEU A  1 173 ? -32.073 2.886   -14.011 1.00 13.94 ? 170 LEU B O   1 
ATOM   1349 C CB  . LEU A  1 173 ? -29.898 3.102   -16.538 1.00 15.42 ? 170 LEU B CB  1 
ATOM   1350 C CG  . LEU A  1 173 ? -30.920 4.171   -16.910 1.00 16.33 ? 170 LEU B CG  1 
ATOM   1351 C CD1 . LEU A  1 173 ? -30.789 5.393   -15.986 1.00 16.59 ? 170 LEU B CD1 1 
ATOM   1352 C CD2 . LEU A  1 173 ? -30.601 4.598   -18.317 1.00 17.51 ? 170 LEU B CD2 1 
ATOM   1353 N N   . ALA A  1 174 ? -32.003 1.070   -15.340 1.00 14.82 ? 171 ALA B N   1 
ATOM   1354 C CA  . ALA A  1 174 ? -33.374 0.671   -15.013 1.00 14.63 ? 171 ALA B CA  1 
ATOM   1355 C C   . ALA A  1 174 ? -33.521 0.417   -13.502 1.00 15.66 ? 171 ALA B C   1 
ATOM   1356 O O   . ALA A  1 174 ? -34.475 0.926   -12.868 1.00 15.54 ? 171 ALA B O   1 
ATOM   1357 C CB  . ALA A  1 174 ? -33.793 -0.554  -15.779 1.00 14.32 ? 171 ALA B CB  1 
ATOM   1358 N N   . LEU A  1 175 ? -32.567 -0.357  -12.968 1.00 15.75 ? 172 LEU B N   1 
ATOM   1359 C CA  . LEU A  1 175 ? -32.533 -0.607  -11.527 1.00 14.87 ? 172 LEU B CA  1 
ATOM   1360 C C   . LEU A  1 175 ? -32.589 0.689   -10.706 1.00 14.80 ? 172 LEU B C   1 
ATOM   1361 O O   . LEU A  1 175 ? -33.423 0.810   -9.842  1.00 14.90 ? 172 LEU B O   1 
ATOM   1362 C CB  . LEU A  1 175 ? -31.276 -1.421  -11.209 1.00 13.73 ? 172 LEU B CB  1 
ATOM   1363 C CG  . LEU A  1 175 ? -31.175 -1.935  -9.773  1.00 14.18 ? 172 LEU B CG  1 
ATOM   1364 C CD1 . LEU A  1 175 ? -32.256 -2.913  -9.330  1.00 14.94 ? 172 LEU B CD1 1 
ATOM   1365 C CD2 . LEU A  1 175 ? -29.838 -2.526  -9.513  1.00 15.34 ? 172 LEU B CD2 1 
ATOM   1366 N N   . ASN A  1 176 ? -31.682 1.637   -10.987 1.00 14.95 ? 173 ASN B N   1 
ATOM   1367 C CA  . ASN A  1 176 ? -31.547 2.861   -10.189 1.00 13.88 ? 173 ASN B CA  1 
ATOM   1368 C C   . ASN A  1 176 ? -32.717 3.829   -10.405 1.00 15.28 ? 173 ASN B C   1 
ATOM   1369 O O   . ASN A  1 176 ? -33.174 4.456   -9.430  1.00 14.83 ? 173 ASN B O   1 
ATOM   1370 C CB  . ASN A  1 176 ? -30.215 3.544   -10.452 1.00 13.96 ? 173 ASN B CB  1 
ATOM   1371 C CG  . ASN A  1 176 ? -29.059 2.752   -9.868  1.00 15.14 ? 173 ASN B CG  1 
ATOM   1372 O OD1 . ASN A  1 176 ? -29.214 1.589   -9.475  1.00 14.89 ? 173 ASN B OD1 1 
ATOM   1373 N ND2 . ASN A  1 176 ? -27.896 3.376   -9.801  1.00 15.37 ? 173 ASN B ND2 1 
ATOM   1374 N N   . PHE A  1 177 ? -33.169 3.957   -11.660 1.00 14.82 ? 174 PHE B N   1 
ATOM   1375 C CA  . PHE A  1 177 ? -34.326 4.782   -11.933 1.00 16.07 ? 174 PHE B CA  1 
ATOM   1376 C C   . PHE A  1 177 ? -35.583 4.219   -11.239 1.00 15.84 ? 174 PHE B C   1 
ATOM   1377 O O   . PHE A  1 177 ? -36.402 5.027   -10.734 1.00 16.77 ? 174 PHE B O   1 
ATOM   1378 C CB  . PHE A  1 177 ? -34.539 4.971   -13.438 1.00 16.68 ? 174 PHE B CB  1 
ATOM   1379 C CG  . PHE A  1 177 ? -35.306 6.194   -13.901 1.00 17.35 ? 174 PHE B CG  1 
ATOM   1380 C CD1 . PHE A  1 177 ? -35.749 7.226   -13.053 1.00 17.29 ? 174 PHE B CD1 1 
ATOM   1381 C CD2 . PHE A  1 177 ? -35.532 6.309   -15.266 1.00 17.15 ? 174 PHE B CD2 1 
ATOM   1382 C CE1 . PHE A  1 177 ? -36.406 8.328   -13.578 1.00 18.30 ? 174 PHE B CE1 1 
ATOM   1383 C CE2 . PHE A  1 177 ? -36.252 7.379   -15.774 1.00 19.07 ? 174 PHE B CE2 1 
ATOM   1384 C CZ  . PHE A  1 177 ? -36.635 8.404   -14.933 1.00 19.26 ? 174 PHE B CZ  1 
ATOM   1385 N N   A SER A  1 178 ? -35.752 2.885   -11.257 0.50 15.86 ? 175 SER B N   1 
ATOM   1386 N N   B SER A  1 178 ? -35.752 2.870   -11.248 0.50 16.29 ? 175 SER B N   1 
ATOM   1387 C CA  A SER A  1 178 ? -36.817 2.220   -10.510 0.50 16.06 ? 175 SER B CA  1 
ATOM   1388 C CA  B SER A  1 178 ? -36.802 2.174   -10.488 0.50 16.79 ? 175 SER B CA  1 
ATOM   1389 C C   A SER A  1 178 ? -36.767 2.562   -9.018  0.50 16.10 ? 175 SER B C   1 
ATOM   1390 C C   B SER A  1 178 ? -36.766 2.560   -9.011  0.50 16.49 ? 175 SER B C   1 
ATOM   1391 O O   A SER A  1 178 ? -37.797 2.971   -8.470  0.50 16.35 ? 175 SER B O   1 
ATOM   1392 O O   B SER A  1 178 ? -37.798 2.974   -8.472  0.50 16.69 ? 175 SER B O   1 
ATOM   1393 C CB  A SER A  1 178 ? -36.815 0.726   -10.740 0.50 16.26 ? 175 SER B CB  1 
ATOM   1394 C CB  B SER A  1 178 ? -36.811 0.618   -10.642 0.50 17.55 ? 175 SER B CB  1 
ATOM   1395 O OG  A SER A  1 178 ? -37.604 0.108   -9.753  0.50 15.95 ? 175 SER B OG  1 
ATOM   1396 O OG  B SER A  1 178 ? -35.827 -0.100  -9.893  0.50 17.34 ? 175 SER B OG  1 
ATOM   1397 N N   . VAL A  1 179 ? -35.557 2.566   -8.425  1.00 15.84 ? 176 VAL B N   1 
ATOM   1398 C CA  . VAL A  1 179 ? -35.383 2.899   -7.007  1.00 15.54 ? 176 VAL B CA  1 
ATOM   1399 C C   . VAL A  1 179 ? -35.736 4.354   -6.737  1.00 16.54 ? 176 VAL B C   1 
ATOM   1400 O O   . VAL A  1 179 ? -36.396 4.643   -5.726  1.00 15.01 ? 176 VAL B O   1 
ATOM   1401 C CB  . VAL A  1 179 ? -34.010 2.476   -6.484  1.00 15.62 ? 176 VAL B CB  1 
ATOM   1402 C CG1 . VAL A  1 179 ? -33.709 3.115   -5.118  1.00 16.97 ? 176 VAL B CG1 1 
ATOM   1403 C CG2 . VAL A  1 179 ? -33.915 0.942   -6.430  1.00 15.24 ? 176 VAL B CG2 1 
ATOM   1404 N N   . PHE A  1 180 ? -35.307 5.254   -7.641  1.00 16.25 ? 177 PHE B N   1 
ATOM   1405 C CA  . PHE A  1 180 ? -35.716 6.643   -7.573  1.00 16.98 ? 177 PHE B CA  1 
ATOM   1406 C C   . PHE A  1 180 ? -37.227 6.824   -7.531  1.00 17.48 ? 177 PHE B C   1 
ATOM   1407 O O   . PHE A  1 180 ? -37.728 7.599   -6.698  1.00 18.22 ? 177 PHE B O   1 
ATOM   1408 C CB  . PHE A  1 180 ? -35.119 7.351   -8.800  1.00 16.94 ? 177 PHE B CB  1 
ATOM   1409 C CG  . PHE A  1 180 ? -35.514 8.803   -8.896  1.00 18.11 ? 177 PHE B CG  1 
ATOM   1410 C CD1 . PHE A  1 180 ? -34.854 9.777   -8.145  1.00 18.29 ? 177 PHE B CD1 1 
ATOM   1411 C CD2 . PHE A  1 180 ? -36.534 9.196   -9.767  1.00 19.36 ? 177 PHE B CD2 1 
ATOM   1412 C CE1 . PHE A  1 180 ? -35.210 11.111  -8.265  1.00 19.66 ? 177 PHE B CE1 1 
ATOM   1413 C CE2 . PHE A  1 180 ? -36.949 10.544  -9.820  1.00 21.29 ? 177 PHE B CE2 1 
ATOM   1414 C CZ  . PHE A  1 180 ? -36.273 11.488  -9.080  1.00 21.04 ? 177 PHE B CZ  1 
ATOM   1415 N N   . TYR A  1 181 ? -37.961 6.137   -8.414  1.00 18.03 ? 178 TYR B N   1 
ATOM   1416 C CA  . TYR A  1 181 ? -39.412 6.205   -8.363  1.00 18.39 ? 178 TYR B CA  1 
ATOM   1417 C C   . TYR A  1 181 ? -39.895 5.708   -7.007  1.00 18.02 ? 178 TYR B C   1 
ATOM   1418 O O   . TYR A  1 181 ? -40.760 6.338   -6.415  1.00 19.53 ? 178 TYR B O   1 
ATOM   1419 C CB  . TYR A  1 181 ? -40.117 5.419   -9.459  1.00 19.97 ? 178 TYR B CB  1 
ATOM   1420 C CG  . TYR A  1 181 ? -40.252 6.243   -10.738 1.00 21.37 ? 178 TYR B CG  1 
ATOM   1421 C CD1 . TYR A  1 181 ? -41.301 7.137   -10.870 1.00 24.90 ? 178 TYR B CD1 1 
ATOM   1422 C CD2 . TYR A  1 181 ? -39.375 6.110   -11.816 1.00 22.85 ? 178 TYR B CD2 1 
ATOM   1423 C CE1 . TYR A  1 181 ? -41.444 7.917   -12.015 1.00 28.95 ? 178 TYR B CE1 1 
ATOM   1424 C CE2 . TYR A  1 181 ? -39.477 6.901   -12.947 1.00 24.75 ? 178 TYR B CE2 1 
ATOM   1425 C CZ  . TYR A  1 181 ? -40.496 7.827   -13.031 1.00 27.81 ? 178 TYR B CZ  1 
ATOM   1426 O OH  . TYR A  1 181 ? -40.679 8.556   -14.178 1.00 31.61 ? 178 TYR B OH  1 
ATOM   1427 N N   . TYR A  1 182 ? -39.328 4.575   -6.551  1.00 17.51 ? 179 TYR B N   1 
ATOM   1428 C CA  . TYR A  1 182 ? -39.855 3.910   -5.368  1.00 17.77 ? 179 TYR B CA  1 
ATOM   1429 C C   . TYR A  1 182 ? -39.722 4.803   -4.145  1.00 18.33 ? 179 TYR B C   1 
ATOM   1430 O O   . TYR A  1 182 ? -40.706 4.992   -3.424  1.00 19.61 ? 179 TYR B O   1 
ATOM   1431 C CB  . TYR A  1 182 ? -39.162 2.572   -5.121  1.00 17.54 ? 179 TYR B CB  1 
ATOM   1432 C CG  . TYR A  1 182 ? -39.870 1.726   -4.092  1.00 17.98 ? 179 TYR B CG  1 
ATOM   1433 C CD1 . TYR A  1 182 ? -39.605 1.872   -2.728  1.00 18.71 ? 179 TYR B CD1 1 
ATOM   1434 C CD2 . TYR A  1 182 ? -40.814 0.804   -4.487  1.00 19.73 ? 179 TYR B CD2 1 
ATOM   1435 C CE1 . TYR A  1 182 ? -40.299 1.105   -1.788  1.00 20.70 ? 179 TYR B CE1 1 
ATOM   1436 C CE2 . TYR A  1 182 ? -41.560 0.073   -3.568  1.00 21.43 ? 179 TYR B CE2 1 
ATOM   1437 C CZ  . TYR A  1 182 ? -41.281 0.216   -2.216  1.00 21.54 ? 179 TYR B CZ  1 
ATOM   1438 O OH  . TYR A  1 182 ? -41.947 -0.578  -1.338  1.00 23.81 ? 179 TYR B OH  1 
ATOM   1439 N N   . GLU A  1 183 ? -38.497 5.276   -3.893  1.00 18.76 ? 180 GLU B N   1 
ATOM   1440 C CA  . GLU A  1 183 ? -38.183 5.885   -2.617  1.00 20.40 ? 180 GLU B CA  1 
ATOM   1441 C C   . GLU A  1 183 ? -37.993 7.399   -2.663  1.00 20.19 ? 180 GLU B C   1 
ATOM   1442 O O   . GLU A  1 183 ? -38.035 8.002   -1.589  1.00 19.95 ? 180 GLU B O   1 
ATOM   1443 C CB  . GLU A  1 183 ? -37.079 5.082   -1.940  1.00 20.53 ? 180 GLU B CB  1 
ATOM   1444 C CG  . GLU A  1 183 ? -35.689 5.291   -2.451  1.00 20.06 ? 180 GLU B CG  1 
ATOM   1445 C CD  . GLU A  1 183 ? -34.670 4.456   -1.695  1.00 20.55 ? 180 GLU B CD  1 
ATOM   1446 O OE1 . GLU A  1 183 ? -34.943 3.382   -1.060  1.00 19.65 ? 180 GLU B OE1 1 
ATOM   1447 O OE2 . GLU A  1 183 ? -33.520 4.928   -1.753  1.00 19.58 ? 180 GLU B OE2 1 
ATOM   1448 N N   . ILE A  1 184 ? -37.722 8.009   -3.809  1.00 19.64 ? 181 ILE B N   1 
ATOM   1449 C CA  . ILE A  1 184 ? -37.610 9.466   -3.853  1.00 20.31 ? 181 ILE B CA  1 
ATOM   1450 C C   . ILE A  1 184 ? -38.965 10.065  -4.214  1.00 22.31 ? 181 ILE B C   1 
ATOM   1451 O O   . ILE A  1 184 ? -39.396 11.001  -3.543  1.00 21.79 ? 181 ILE B O   1 
ATOM   1452 C CB  . ILE A  1 184 ? -36.468 9.919   -4.775  1.00 19.48 ? 181 ILE B CB  1 
ATOM   1453 C CG1 . ILE A  1 184 ? -35.145 9.261   -4.389  1.00 19.01 ? 181 ILE B CG1 1 
ATOM   1454 C CG2 . ILE A  1 184 ? -36.401 11.467  -4.798  1.00 20.50 ? 181 ILE B CG2 1 
ATOM   1455 C CD1 . ILE A  1 184 ? -34.657 9.419   -2.958  1.00 18.81 ? 181 ILE B CD1 1 
ATOM   1456 N N   . LEU A  1 185 ? -39.615 9.539   -5.258  1.00 21.89 ? 182 LEU B N   1 
ATOM   1457 C CA  . LEU A  1 185 ? -40.946 10.001  -5.670  1.00 25.10 ? 182 LEU B CA  1 
ATOM   1458 C C   . LEU A  1 185 ? -42.089 9.322   -4.928  1.00 24.39 ? 182 LEU B C   1 
ATOM   1459 O O   . LEU A  1 185 ? -43.197 9.798   -5.098  1.00 26.24 ? 182 LEU B O   1 
ATOM   1460 C CB  . LEU A  1 185 ? -41.094 9.783   -7.172  1.00 25.62 ? 182 LEU B CB  1 
ATOM   1461 C CG  . LEU A  1 185 ? -40.132 10.578  -8.053  1.00 26.61 ? 182 LEU B CG  1 
ATOM   1462 C CD1 . LEU A  1 185 ? -40.458 10.239  -9.517  1.00 27.70 ? 182 LEU B CD1 1 
ATOM   1463 C CD2 . LEU A  1 185 ? -40.235 12.067  -7.771  1.00 28.51 ? 182 LEU B CD2 1 
ATOM   1464 N N   . ASN A  1 186 ? -41.838 8.241   -4.168  1.00 23.76 ? 183 ASN B N   1 
ATOM   1465 C CA  . ASN A  1 186 ? -42.876 7.481   -3.444  1.00 25.79 ? 183 ASN B CA  1 
ATOM   1466 C C   . ASN A  1 186 ? -43.950 7.018   -4.414  1.00 24.81 ? 183 ASN B C   1 
ATOM   1467 O O   . ASN A  1 186 ? -45.120 7.273   -4.176  1.00 25.66 ? 183 ASN B O   1 
ATOM   1468 C CB  . ASN A  1 186 ? -43.443 8.231   -2.237  1.00 30.76 ? 183 ASN B CB  1 
ATOM   1469 C CG  . ASN A  1 186 ? -42.333 8.692   -1.334  1.00 36.50 ? 183 ASN B CG  1 
ATOM   1470 O OD1 . ASN A  1 186 ? -42.173 9.902   -1.127  1.00 45.50 ? 183 ASN B OD1 1 
ATOM   1471 N ND2 . ASN A  1 186 ? -41.526 7.770   -0.839  1.00 34.93 ? 183 ASN B ND2 1 
ATOM   1472 N N   . SER A  1 187 ? -43.517 6.364   -5.504  1.00 23.94 ? 184 SER B N   1 
ATOM   1473 C CA  . SER A  1 187 ? -44.320 5.879   -6.623  1.00 24.64 ? 184 SER B CA  1 
ATOM   1474 C C   . SER A  1 187 ? -44.094 4.387   -6.817  1.00 22.87 ? 184 SER B C   1 
ATOM   1475 O O   . SER A  1 187 ? -43.363 3.968   -7.712  1.00 22.30 ? 184 SER B O   1 
ATOM   1476 C CB  . SER A  1 187 ? -43.995 6.620   -7.869  1.00 25.86 ? 184 SER B CB  1 
ATOM   1477 O OG  . SER A  1 187 ? -44.537 7.899   -7.791  1.00 29.45 ? 184 SER B OG  1 
ATOM   1478 N N   . PRO A  1 188 ? -44.585 3.508   -5.913  1.00 23.35 ? 185 PRO B N   1 
ATOM   1479 C CA  . PRO A  1 188 ? -44.122 2.098   -5.924  1.00 22.04 ? 185 PRO B CA  1 
ATOM   1480 C C   . PRO A  1 188 ? -44.599 1.297   -7.128  1.00 21.13 ? 185 PRO B C   1 
ATOM   1481 O O   . PRO A  1 188 ? -43.855 0.499   -7.682  1.00 20.79 ? 185 PRO B O   1 
ATOM   1482 C CB  . PRO A  1 188 ? -44.567 1.566   -4.568  1.00 22.38 ? 185 PRO B CB  1 
ATOM   1483 C CG  . PRO A  1 188 ? -45.718 2.459   -4.262  1.00 24.79 ? 185 PRO B CG  1 
ATOM   1484 C CD  . PRO A  1 188 ? -45.360 3.824   -4.734  1.00 24.24 ? 185 PRO B CD  1 
ATOM   1485 N N   . GLU A  1 189 ? -45.803 1.573   -7.596  1.00 21.39 ? 186 GLU B N   1 
ATOM   1486 C CA  . GLU A  1 189 ? -46.364 0.865   -8.751  1.00 22.95 ? 186 GLU B CA  1 
ATOM   1487 C C   . GLU A  1 189 ? -45.525 1.194   -9.995  1.00 22.49 ? 186 GLU B C   1 
ATOM   1488 O O   . GLU A  1 189 ? -45.116 0.283   -10.736 1.00 21.28 ? 186 GLU B O   1 
ATOM   1489 C CB  . GLU A  1 189 ? -47.853 1.143   -8.996  1.00 24.16 ? 186 GLU B CB  1 
ATOM   1490 C CG  . GLU A  1 189 ? -48.722 0.740   -7.818  1.00 24.90 ? 186 GLU B CG  1 
ATOM   1491 C CD  . GLU A  1 189 ? -48.719 1.694   -6.643  1.00 24.72 ? 186 GLU B CD  1 
ATOM   1492 O OE1 . GLU A  1 189 ? -48.212 2.828   -6.696  1.00 23.61 ? 186 GLU B OE1 1 
ATOM   1493 O OE2 . GLU A  1 189 ? -49.132 1.244   -5.549  1.00 25.49 ? 186 GLU B OE2 1 
ATOM   1494 N N   . LYS A  1 190 ? -45.216 2.488   -10.191 1.00 24.06 ? 187 LYS B N   1 
ATOM   1495 C CA  . LYS A  1 190 ? -44.361 2.952   -11.283 1.00 24.93 ? 187 LYS B CA  1 
ATOM   1496 C C   . LYS A  1 190 ? -42.971 2.345   -11.168 1.00 22.27 ? 187 LYS B C   1 
ATOM   1497 O O   . LYS A  1 190 ? -42.401 1.928   -12.176 1.00 21.99 ? 187 LYS B O   1 
ATOM   1498 C CB  . LYS A  1 190 ? -44.241 4.481   -11.401 1.00 29.41 ? 187 LYS B CB  1 
ATOM   1499 C CG  . LYS A  1 190 ? -45.466 5.184   -11.925 1.00 38.53 ? 187 LYS B CG  1 
ATOM   1500 C CD  . LYS A  1 190 ? -45.621 6.631   -11.450 1.00 46.15 ? 187 LYS B CD  1 
ATOM   1501 C CE  . LYS A  1 190 ? -46.950 7.224   -11.804 1.00 51.49 ? 187 LYS B CE  1 
ATOM   1502 N NZ  . LYS A  1 190 ? -46.952 7.641   -13.209 1.00 55.34 ? 187 LYS B NZ  1 
ATOM   1503 N N   . ALA A  1 191 ? -42.410 2.316   -9.948  1.00 21.53 ? 188 ALA B N   1 
ATOM   1504 C CA  . ALA A  1 191 ? -41.102 1.701   -9.706  1.00 18.99 ? 188 ALA B CA  1 
ATOM   1505 C C   . ALA A  1 191 ? -41.109 0.216   -10.117 1.00 18.39 ? 188 ALA B C   1 
ATOM   1506 O O   . ALA A  1 191 ? -40.185 -0.234  -10.767 1.00 18.97 ? 188 ALA B O   1 
ATOM   1507 C CB  . ALA A  1 191 ? -40.753 1.827   -8.253  1.00 19.37 ? 188 ALA B CB  1 
HETATM 1508 N N   . OCY A  1 192 ? -42.135 -0.533  -9.703  1.00 18.62 ? 189 OCY B N   1 
HETATM 1509 C CA  . OCY A  1 192 ? -42.282 -1.944  -10.063 1.00 19.57 ? 189 OCY B CA  1 
HETATM 1510 C CB  . OCY A  1 192 ? -43.425 -2.594  -9.289  1.00 21.51 ? 189 OCY B CB  1 
HETATM 1511 S SG  . OCY A  1 192 ? -42.926 -2.831  -7.567  1.00 24.50 ? 189 OCY B SG  1 
HETATM 1512 C CD  . OCY A  1 192 ? -44.382 -3.514  -6.744  1.00 28.08 ? 189 OCY B CD  1 
HETATM 1513 C CE  . OCY A  1 192 ? -45.135 -2.306  -6.371  1.00 29.56 ? 189 OCY B CE  1 
HETATM 1514 O OZ  . OCY A  1 192 ? -46.399 -2.655  -5.974  1.00 36.64 ? 189 OCY B OZ  1 
HETATM 1515 C C   . OCY A  1 192 ? -42.433 -2.147  -11.570 1.00 19.64 ? 189 OCY B C   1 
HETATM 1516 O O   . OCY A  1 192 ? -41.781 -3.037  -12.102 1.00 20.04 ? 189 OCY B O   1 
ATOM   1517 N N   . SER A  1 193 ? -43.272 -1.321  -12.228 1.00 20.30 ? 190 SER B N   1 
ATOM   1518 C CA  . SER A  1 193 ? -43.499 -1.393  -13.665 1.00 21.57 ? 190 SER B CA  1 
ATOM   1519 C C   . SER A  1 193 ? -42.158 -1.222  -14.394 1.00 20.33 ? 190 SER B C   1 
ATOM   1520 O O   . SER A  1 193 ? -41.839 -2.041  -15.243 1.00 20.14 ? 190 SER B O   1 
ATOM   1521 C CB  . SER A  1 193 ? -44.441 -0.346  -14.089 1.00 23.20 ? 190 SER B CB  1 
ATOM   1522 O OG  . SER A  1 193 ? -44.734 -0.562  -15.442 1.00 24.88 ? 190 SER B OG  1 
ATOM   1523 N N   . LEU A  1 194 ? -41.396 -0.185  -14.047 1.00 20.09 ? 191 LEU B N   1 
ATOM   1524 C CA  . LEU A  1 194 ? -40.087 0.088   -14.675 1.00 19.29 ? 191 LEU B CA  1 
ATOM   1525 C C   . LEU A  1 194 ? -39.130 -1.109  -14.523 1.00 18.96 ? 191 LEU B C   1 
ATOM   1526 O O   . LEU A  1 194 ? -38.536 -1.546  -15.505 1.00 20.45 ? 191 LEU B O   1 
ATOM   1527 C CB  . LEU A  1 194 ? -39.529 1.389   -14.101 1.00 20.08 ? 191 LEU B CB  1 
ATOM   1528 C CG  . LEU A  1 194 ? -38.508 2.138   -14.950 1.00 21.44 ? 191 LEU B CG  1 
ATOM   1529 C CD1 . LEU A  1 194 ? -38.239 3.548   -14.368 1.00 22.46 ? 191 LEU B CD1 1 
ATOM   1530 C CD2 . LEU A  1 194 ? -37.201 1.391   -15.029 1.00 22.35 ? 191 LEU B CD2 1 
ATOM   1531 N N   . ALA A  1 195 ? -38.996 -1.654  -13.303 1.00 18.33 ? 192 ALA B N   1 
ATOM   1532 C CA  . ALA A  1 195 ? -38.075 -2.748  -13.005 1.00 16.78 ? 192 ALA B CA  1 
ATOM   1533 C C   . ALA A  1 195 ? -38.494 -4.022  -13.762 1.00 17.85 ? 192 ALA B C   1 
ATOM   1534 O O   . ALA A  1 195 ? -37.680 -4.695  -14.378 1.00 17.22 ? 192 ALA B O   1 
ATOM   1535 C CB  . ALA A  1 195 ? -38.014 -3.002  -11.504 1.00 17.76 ? 192 ALA B CB  1 
ATOM   1536 N N   . LYS A  1 196 ? -39.775 -4.354  -13.704 1.00 18.97 ? 193 LYS B N   1 
ATOM   1537 C CA  . LYS A  1 196 ? -40.326 -5.538  -14.341 1.00 20.14 ? 193 LYS B CA  1 
ATOM   1538 C C   . LYS A  1 196 ? -40.201 -5.470  -15.867 1.00 19.94 ? 193 LYS B C   1 
ATOM   1539 O O   . LYS A  1 196 ? -39.832 -6.479  -16.465 1.00 21.02 ? 193 LYS B O   1 
ATOM   1540 C CB  . LYS A  1 196 ? -41.809 -5.782  -13.992 1.00 23.17 ? 193 LYS B CB  1 
ATOM   1541 C CG  . LYS A  1 196 ? -42.211 -7.234  -14.387 1.00 25.21 ? 193 LYS B CG  1 
ATOM   1542 C CD  . LYS A  1 196 ? -43.522 -7.841  -13.939 1.00 33.14 ? 193 LYS B CD  1 
ATOM   1543 C CE  . LYS A  1 196 ? -43.628 -9.296  -14.372 1.00 34.20 ? 193 LYS B CE  1 
ATOM   1544 N NZ  . LYS A  1 196 ? -44.018 -9.390  -15.767 1.00 37.49 ? 193 LYS B NZ  1 
ATOM   1545 N N   . THR A  1 197 ? -40.544 -4.340  -16.472 1.00 19.61 ? 194 THR B N   1 
ATOM   1546 C CA  . THR A  1 197 ? -40.348 -4.111  -17.910 1.00 20.16 ? 194 THR B CA  1 
ATOM   1547 C C   . THR A  1 197 ? -38.888 -4.395  -18.306 1.00 19.12 ? 194 THR B C   1 
ATOM   1548 O O   . THR A  1 197 ? -38.662 -5.134  -19.273 1.00 19.03 ? 194 THR B O   1 
ATOM   1549 C CB  . THR A  1 197 ? -40.780 -2.689  -18.293 1.00 19.90 ? 194 THR B CB  1 
ATOM   1550 O OG1 . THR A  1 197 ? -42.204 -2.724  -18.150 1.00 20.32 ? 194 THR B OG1 1 
ATOM   1551 C CG2 . THR A  1 197 ? -40.472 -2.295  -19.734 1.00 21.10 ? 194 THR B CG2 1 
ATOM   1552 N N   . ALA A  1 198 ? -37.934 -3.803  -17.568 1.00 17.63 ? 195 ALA B N   1 
ATOM   1553 C CA  . ALA A  1 198 ? -36.517 -3.962  -17.857 1.00 17.29 ? 195 ALA B CA  1 
ATOM   1554 C C   . ALA A  1 198 ? -36.105 -5.443  -17.759 1.00 18.38 ? 195 ALA B C   1 
ATOM   1555 O O   . ALA A  1 198 ? -35.437 -5.958  -18.634 1.00 19.03 ? 195 ALA B O   1 
ATOM   1556 C CB  . ALA A  1 198 ? -35.702 -3.116  -16.921 1.00 17.11 ? 195 ALA B CB  1 
ATOM   1557 N N   . PHE A  1 199 ? -36.536 -6.135  -16.699 1.00 17.62 ? 196 PHE B N   1 
ATOM   1558 C CA  . PHE A  1 199 ? -36.305 -7.560  -16.527 1.00 18.39 ? 196 PHE B CA  1 
ATOM   1559 C C   . PHE A  1 199 ? -36.886 -8.369  -17.696 1.00 18.77 ? 196 PHE B C   1 
ATOM   1560 O O   . PHE A  1 199 ? -36.166 -9.167  -18.261 1.00 21.37 ? 196 PHE B O   1 
ATOM   1561 C CB  . PHE A  1 199 ? -36.893 -8.031  -15.185 1.00 18.93 ? 196 PHE B CB  1 
ATOM   1562 C CG  . PHE A  1 199 ? -36.586 -9.478  -14.862 1.00 21.63 ? 196 PHE B CG  1 
ATOM   1563 C CD1 . PHE A  1 199 ? -37.422 -10.511 -15.309 1.00 23.56 ? 196 PHE B CD1 1 
ATOM   1564 C CD2 . PHE A  1 199 ? -35.441 -9.805  -14.131 1.00 20.94 ? 196 PHE B CD2 1 
ATOM   1565 C CE1 . PHE A  1 199 ? -37.119 -11.849 -15.027 1.00 24.54 ? 196 PHE B CE1 1 
ATOM   1566 C CE2 . PHE A  1 199 ? -35.128 -11.123 -13.852 1.00 22.70 ? 196 PHE B CE2 1 
ATOM   1567 C CZ  . PHE A  1 199 ? -35.976 -12.167 -14.295 1.00 24.33 ? 196 PHE B CZ  1 
ATOM   1568 N N   . ASP A  1 200 ? -38.117 -8.112  -18.097 1.00 20.42 ? 197 ASP B N   1 
ATOM   1569 C CA  . ASP A  1 200 ? -38.811 -8.880  -19.139 1.00 22.04 ? 197 ASP B CA  1 
ATOM   1570 C C   . ASP A  1 200 ? -38.201 -8.637  -20.522 1.00 22.53 ? 197 ASP B C   1 
ATOM   1571 O O   . ASP A  1 200 ? -38.124 -9.579  -21.336 1.00 22.54 ? 197 ASP B O   1 
ATOM   1572 C CB  . ASP A  1 200 ? -40.307 -8.634  -19.081 1.00 23.75 ? 197 ASP B CB  1 
ATOM   1573 C CG  . ASP A  1 200 ? -41.034 -9.243  -17.876 1.00 25.16 ? 197 ASP B CG  1 
ATOM   1574 O OD1 . ASP A  1 200 ? -40.458 -10.133 -17.199 1.00 23.61 ? 197 ASP B OD1 1 
ATOM   1575 O OD2 . ASP A  1 200 ? -42.205 -8.850  -17.649 1.00 26.13 ? 197 ASP B OD2 1 
ATOM   1576 N N   . GLU A  1 201 ? -37.801 -7.383  -20.791 1.00 20.82 ? 198 GLU B N   1 
ATOM   1577 C CA  . GLU A  1 201 ? -37.149 -7.049  -22.052 1.00 21.94 ? 198 GLU B CA  1 
ATOM   1578 C C   . GLU A  1 201 ? -35.796 -7.757  -22.184 1.00 20.83 ? 198 GLU B C   1 
ATOM   1579 O O   . GLU A  1 201 ? -35.444 -8.175  -23.298 1.00 20.22 ? 198 GLU B O   1 
ATOM   1580 C CB  . GLU A  1 201 ? -37.000 -5.540  -22.242 1.00 21.79 ? 198 GLU B CB  1 
ATOM   1581 C CG  . GLU A  1 201 ? -38.316 -4.814  -22.512 1.00 23.53 ? 198 GLU B CG  1 
ATOM   1582 C CD  . GLU A  1 201 ? -38.237 -3.290  -22.451 1.00 25.77 ? 198 GLU B CD  1 
ATOM   1583 O OE1 . GLU A  1 201 ? -37.296 -2.724  -21.886 1.00 25.95 ? 198 GLU B OE1 1 
ATOM   1584 O OE2 . GLU A  1 201 ? -39.179 -2.649  -22.975 1.00 29.03 ? 198 GLU B OE2 1 
ATOM   1585 N N   . ALA A  1 202 ? -35.052 -7.850  -21.070 1.00 20.01 ? 199 ALA B N   1 
ATOM   1586 C CA  . ALA A  1 202 ? -33.795 -8.602  -21.047 1.00 20.30 ? 199 ALA B CA  1 
ATOM   1587 C C   . ALA A  1 202 ? -34.009 -10.104 -21.322 1.00 21.76 ? 199 ALA B C   1 
ATOM   1588 O O   . ALA A  1 202 ? -33.286 -10.645 -22.151 1.00 23.10 ? 199 ALA B O   1 
ATOM   1589 C CB  . ALA A  1 202 ? -33.069 -8.389  -19.766 1.00 18.77 ? 199 ALA B CB  1 
ATOM   1590 N N   . ILE A  1 203 ? -34.981 -10.745 -20.639 1.00 20.76 ? 200 ILE B N   1 
ATOM   1591 C CA  . ILE A  1 203 ? -35.375 -12.123 -20.906 1.00 21.91 ? 200 ILE B CA  1 
ATOM   1592 C C   . ILE A  1 203 ? -35.717 -12.319 -22.392 1.00 23.65 ? 200 ILE B C   1 
ATOM   1593 O O   . ILE A  1 203 ? -35.187 -13.232 -23.056 1.00 23.15 ? 200 ILE B O   1 
ATOM   1594 C CB  . ILE A  1 203 ? -36.551 -12.541 -19.992 1.00 22.14 ? 200 ILE B CB  1 
ATOM   1595 C CG1 . ILE A  1 203 ? -36.198 -12.560 -18.470 1.00 21.64 ? 200 ILE B CG1 1 
ATOM   1596 C CG2 . ILE A  1 203 ? -37.160 -13.882 -20.428 1.00 23.38 ? 200 ILE B CG2 1 
ATOM   1597 C CD1 . ILE A  1 203 ? -35.200 -13.611 -18.022 1.00 22.03 ? 200 ILE B CD1 1 
ATOM   1598 N N   . ALA A  1 204 ? -36.580 -11.421 -22.929 1.00 23.89 ? 201 ALA B N   1 
ATOM   1599 C CA  . ALA A  1 204 ? -37.069 -11.569 -24.295 1.00 25.31 ? 201 ALA B CA  1 
ATOM   1600 C C   . ALA A  1 204 ? -35.950 -11.399 -25.317 1.00 24.87 ? 201 ALA B C   1 
ATOM   1601 O O   . ALA A  1 204 ? -36.059 -11.990 -26.381 1.00 25.28 ? 201 ALA B O   1 
ATOM   1602 C CB  . ALA A  1 204 ? -38.229 -10.613 -24.618 1.00 25.70 ? 201 ALA B CB  1 
ATOM   1603 N N   . GLU A  1 205 ? -34.900 -10.613 -24.988 1.00 24.52 ? 202 GLU B N   1 
ATOM   1604 C CA  . GLU A  1 205 ? -33.751 -10.403 -25.877 1.00 26.39 ? 202 GLU B CA  1 
ATOM   1605 C C   . GLU A  1 205 ? -32.454 -10.955 -25.316 1.00 23.49 ? 202 GLU B C   1 
ATOM   1606 O O   . GLU A  1 205 ? -31.406 -10.424 -25.624 1.00 23.47 ? 202 GLU B O   1 
ATOM   1607 C CB  . GLU A  1 205 ? -33.854 -8.962  -26.384 1.00 29.98 ? 202 GLU B CB  1 
ATOM   1608 C CG  . GLU A  1 205 ? -34.750 -8.913  -27.626 1.00 36.86 ? 202 GLU B CG  1 
ATOM   1609 C CD  . GLU A  1 205 ? -35.714 -7.768  -27.790 1.00 44.35 ? 202 GLU B CD  1 
ATOM   1610 O OE1 . GLU A  1 205 ? -36.845 -8.084  -28.220 1.00 53.51 ? 202 GLU B OE1 1 
ATOM   1611 O OE2 . GLU A  1 205 ? -35.378 -6.603  -27.477 1.00 45.73 ? 202 GLU B OE2 1 
ATOM   1612 N N   . LEU A  1 206 ? -32.525 -12.147 -24.681 1.00 22.61 ? 203 LEU B N   1 
ATOM   1613 C CA  . LEU A  1 206 ? -31.331 -12.852 -24.228 1.00 22.22 ? 203 LEU B CA  1 
ATOM   1614 C C   . LEU A  1 206 ? -30.411 -13.274 -25.368 1.00 23.67 ? 203 LEU B C   1 
ATOM   1615 O O   . LEU A  1 206 ? -29.227 -13.484 -25.118 1.00 23.79 ? 203 LEU B O   1 
ATOM   1616 C CB  . LEU A  1 206 ? -31.673 -14.049 -23.334 1.00 22.18 ? 203 LEU B CB  1 
ATOM   1617 C CG  . LEU A  1 206 ? -31.916 -13.742 -21.872 1.00 21.80 ? 203 LEU B CG  1 
ATOM   1618 C CD1 . LEU A  1 206 ? -32.568 -15.008 -21.228 1.00 22.50 ? 203 LEU B CD1 1 
ATOM   1619 C CD2 . LEU A  1 206 ? -30.668 -13.336 -21.113 1.00 20.47 ? 203 LEU B CD2 1 
ATOM   1620 N N   . ASP A  1 207 ? -30.953 -13.374 -26.587 1.00 25.12 ? 204 ASP B N   1 
ATOM   1621 C CA  . ASP A  1 207 ? -30.180 -13.628 -27.803 1.00 27.35 ? 204 ASP B CA  1 
ATOM   1622 C C   . ASP A  1 207 ? -29.060 -12.594 -28.056 1.00 28.47 ? 204 ASP B C   1 
ATOM   1623 O O   . ASP A  1 207 ? -28.144 -12.925 -28.779 1.00 31.01 ? 204 ASP B O   1 
ATOM   1624 C CB  . ASP A  1 207 ? -31.111 -13.776 -28.988 1.00 28.53 ? 204 ASP B CB  1 
ATOM   1625 C CG  . ASP A  1 207 ? -31.925 -12.541 -29.323 1.00 27.79 ? 204 ASP B CG  1 
ATOM   1626 O OD1 . ASP A  1 207 ? -32.644 -12.070 -28.430 1.00 25.90 ? 204 ASP B OD1 1 
ATOM   1627 O OD2 . ASP A  1 207 ? -31.811 -12.070 -30.477 1.00 28.58 ? 204 ASP B OD2 1 
ATOM   1628 N N   . THR A  1 208 ? -29.221 -11.351 -27.586 1.00 28.05 ? 205 THR B N   1 
ATOM   1629 C CA  . THR A  1 208 ? -28.289 -10.241 -27.761 1.00 29.93 ? 205 THR B CA  1 
ATOM   1630 C C   . THR A  1 208 ? -27.274 -10.216 -26.605 1.00 26.27 ? 205 THR B C   1 
ATOM   1631 O O   . THR A  1 208 ? -26.428 -9.334  -26.608 1.00 26.63 ? 205 THR B O   1 
ATOM   1632 C CB  . THR A  1 208 ? -29.098 -8.917  -27.771 1.00 30.99 ? 205 THR B CB  1 
ATOM   1633 O OG1 . THR A  1 208 ? -29.615 -8.610  -26.454 1.00 37.38 ? 205 THR B OG1 1 
ATOM   1634 C CG2 . THR A  1 208 ? -30.210 -8.861  -28.801 1.00 34.83 ? 205 THR B CG2 1 
ATOM   1635 N N   . LEU A  1 209 ? -27.436 -11.021 -25.527 1.00 23.71 ? 206 LEU B N   1 
ATOM   1636 C CA  . LEU A  1 209 ? -26.500 -11.036 -24.410 1.00 22.49 ? 206 LEU B CA  1 
ATOM   1637 C C   . LEU A  1 209 ? -25.276 -11.856 -24.789 1.00 24.08 ? 206 LEU B C   1 
ATOM   1638 O O   . LEU A  1 209 ? -25.390 -13.053 -24.938 1.00 23.99 ? 206 LEU B O   1 
ATOM   1639 C CB  . LEU A  1 209 ? -27.169 -11.586 -23.140 1.00 21.51 ? 206 LEU B CB  1 
ATOM   1640 C CG  . LEU A  1 209 ? -26.283 -11.664 -21.915 1.00 20.54 ? 206 LEU B CG  1 
ATOM   1641 C CD1 . LEU A  1 209 ? -25.516 -10.370 -21.559 1.00 19.98 ? 206 LEU B CD1 1 
ATOM   1642 C CD2 . LEU A  1 209 ? -27.111 -12.144 -20.755 1.00 20.29 ? 206 LEU B CD2 1 
ATOM   1643 N N   . SER A  1 210 ? -24.122 -11.190 -24.978 1.00 24.45 ? 207 SER B N   1 
ATOM   1644 C CA  . SER A  1 210 ? -22.890 -11.872 -25.317 1.00 26.87 ? 207 SER B CA  1 
ATOM   1645 C C   . SER A  1 210 ? -22.471 -12.741 -24.132 1.00 27.91 ? 207 SER B C   1 
ATOM   1646 O O   . SER A  1 210 ? -22.727 -12.396 -22.986 1.00 27.34 ? 207 SER B O   1 
ATOM   1647 C CB  . SER A  1 210 ? -21.771 -10.887 -25.694 1.00 27.15 ? 207 SER B CB  1 
ATOM   1648 O OG  . SER A  1 210 ? -21.351 -10.200 -24.529 1.00 25.98 ? 207 SER B OG  1 
ATOM   1649 N N   . GLU A  1 211 ? -21.785 -13.822 -24.438 1.00 30.60 ? 208 GLU B N   1 
ATOM   1650 C CA  . GLU A  1 211 ? -21.160 -14.687 -23.450 1.00 33.85 ? 208 GLU B CA  1 
ATOM   1651 C C   . GLU A  1 211 ? -20.267 -13.903 -22.483 1.00 32.88 ? 208 GLU B C   1 
ATOM   1652 O O   . GLU A  1 211 ? -20.333 -14.109 -21.283 1.00 33.50 ? 208 GLU B O   1 
ATOM   1653 C CB  . GLU A  1 211 ? -20.416 -15.728 -24.282 1.00 38.44 ? 208 GLU B CB  1 
ATOM   1654 C CG  . GLU A  1 211 ? -19.625 -16.749 -23.488 1.00 42.96 ? 208 GLU B CG  1 
ATOM   1655 C CD  . GLU A  1 211 ? -19.508 -18.041 -24.288 1.00 48.75 ? 208 GLU B CD  1 
ATOM   1656 O OE1 . GLU A  1 211 ? -18.288 -18.290 -24.416 1.00 55.94 ? 208 GLU B OE1 1 
ATOM   1657 O OE2 . GLU A  1 211 ? -20.516 -18.682 -24.817 1.00 44.53 ? 208 GLU B OE2 1 
ATOM   1658 N N   . GLU A  1 212 ? -19.501 -12.931 -22.986 1.00 32.58 ? 209 GLU B N   1 
ATOM   1659 C CA  . GLU A  1 212 ? -18.589 -12.101 -22.206 1.00 31.45 ? 209 GLU B CA  1 
ATOM   1660 C C   . GLU A  1 212 ? -19.353 -11.228 -21.220 1.00 27.11 ? 209 GLU B C   1 
ATOM   1661 O O   . GLU A  1 212 ? -18.871 -11.053 -20.095 1.00 27.13 ? 209 GLU B O   1 
ATOM   1662 C CB  . GLU A  1 212 ? -17.767 -11.180 -23.115 1.00 35.33 ? 209 GLU B CB  1 
ATOM   1663 C CG  . GLU A  1 212 ? -16.873 -11.931 -24.105 1.00 42.14 ? 209 GLU B CG  1 
ATOM   1664 C CD  . GLU A  1 212 ? -17.416 -12.632 -25.379 1.00 48.93 ? 209 GLU B CD  1 
ATOM   1665 O OE1 . GLU A  1 212 ? -18.531 -12.366 -25.953 1.00 43.89 ? 209 GLU B OE1 1 
ATOM   1666 O OE2 . GLU A  1 212 ? -16.653 -13.558 -25.785 1.00 53.22 ? 209 GLU B OE2 1 
ATOM   1667 N N   . SER A  1 213 ? -20.537 -10.734 -21.614 1.00 24.17 ? 210 SER B N   1 
ATOM   1668 C CA  . SER A  1 213 ? -21.383 -9.930  -20.762 1.00 22.02 ? 210 SER B CA  1 
ATOM   1669 C C   . SER A  1 213 ? -22.288 -10.722 -19.794 1.00 19.87 ? 210 SER B C   1 
ATOM   1670 O O   . SER A  1 213 ? -22.928 -10.088 -18.966 1.00 17.38 ? 210 SER B O   1 
ATOM   1671 C CB  . SER A  1 213 ? -22.167 -8.986  -21.637 1.00 22.22 ? 210 SER B CB  1 
ATOM   1672 O OG  . SER A  1 213 ? -22.739 -7.952  -20.848 1.00 23.85 ? 210 SER B OG  1 
ATOM   1673 N N   . TYR A  1 214 ? -22.397 -12.061 -19.908 1.00 20.88 ? 211 TYR B N   1 
ATOM   1674 C CA  . TYR A  1 214 ? -23.424 -12.808 -19.187 1.00 21.05 ? 211 TYR B CA  1 
ATOM   1675 C C   . TYR A  1 214 ? -23.396 -12.526 -17.661 1.00 19.89 ? 211 TYR B C   1 
ATOM   1676 O O   . TYR A  1 214 ? -24.422 -12.198 -17.050 1.00 18.34 ? 211 TYR B O   1 
ATOM   1677 C CB  . TYR A  1 214 ? -23.312 -14.293 -19.546 1.00 21.80 ? 211 TYR B CB  1 
ATOM   1678 C CG  . TYR A  1 214 ? -24.340 -15.185 -18.861 1.00 21.74 ? 211 TYR B CG  1 
ATOM   1679 C CD1 . TYR A  1 214 ? -24.080 -15.719 -17.597 1.00 21.53 ? 211 TYR B CD1 1 
ATOM   1680 C CD2 . TYR A  1 214 ? -25.565 -15.510 -19.464 1.00 21.70 ? 211 TYR B CD2 1 
ATOM   1681 C CE1 . TYR A  1 214 ? -24.975 -16.585 -16.978 1.00 21.53 ? 211 TYR B CE1 1 
ATOM   1682 C CE2 . TYR A  1 214 ? -26.471 -16.356 -18.832 1.00 21.71 ? 211 TYR B CE2 1 
ATOM   1683 C CZ  . TYR A  1 214 ? -26.173 -16.897 -17.594 1.00 21.65 ? 211 TYR B CZ  1 
ATOM   1684 O OH  . TYR A  1 214 ? -27.063 -17.701 -16.959 1.00 21.22 ? 211 TYR B OH  1 
ATOM   1685 N N   . LYS A  1 215 ? -22.215 -12.649 -17.062 1.00 22.27 ? 212 LYS B N   1 
ATOM   1686 C CA  . LYS A  1 215 ? -22.056 -12.497 -15.613 1.00 23.30 ? 212 LYS B CA  1 
ATOM   1687 C C   . LYS A  1 215 ? -22.481 -11.101 -15.148 1.00 20.04 ? 212 LYS B C   1 
ATOM   1688 O O   . LYS A  1 215 ? -23.224 -10.954 -14.161 1.00 18.10 ? 212 LYS B O   1 
ATOM   1689 C CB  . LYS A  1 215 ? -20.619 -12.846 -15.151 1.00 27.44 ? 212 LYS B CB  1 
ATOM   1690 C CG  . LYS A  1 215 ? -20.285 -14.273 -14.680 1.00 34.57 ? 212 LYS B CG  1 
ATOM   1691 C CD  . LYS A  1 215 ? -20.987 -15.416 -15.412 1.00 41.79 ? 212 LYS B CD  1 
ATOM   1692 C CE  . LYS A  1 215 ? -20.661 -16.841 -14.955 1.00 53.00 ? 212 LYS B CE  1 
ATOM   1693 N NZ  . LYS A  1 215 ? -21.623 -17.269 -13.933 1.00 53.18 ? 212 LYS B NZ  1 
ATOM   1694 N N   . ASP A  1 216 ? -21.972 -10.093 -15.843 1.00 19.28 ? 213 ASP B N   1 
ATOM   1695 C CA  . ASP A  1 216 ? -22.310 -8.702  -15.556 1.00 19.12 ? 213 ASP B CA  1 
ATOM   1696 C C   . ASP A  1 216 ? -23.810 -8.417  -15.637 1.00 17.54 ? 213 ASP B C   1 
ATOM   1697 O O   . ASP A  1 216 ? -24.368 -7.736  -14.753 1.00 17.24 ? 213 ASP B O   1 
ATOM   1698 C CB  . ASP A  1 216 ? -21.577 -7.760  -16.514 1.00 20.27 ? 213 ASP B CB  1 
ATOM   1699 C CG  . ASP A  1 216 ? -20.069 -7.669  -16.332 1.00 22.28 ? 213 ASP B CG  1 
ATOM   1700 O OD1 . ASP A  1 216 ? -19.586 -8.052  -15.286 1.00 22.63 ? 213 ASP B OD1 1 
ATOM   1701 O OD2 . ASP A  1 216 ? -19.405 -7.252  -17.282 1.00 24.47 ? 213 ASP B OD2 1 
ATOM   1702 N N   . SER A  1 217 ? -24.423 -8.863  -16.731 1.00 17.25 ? 214 SER B N   1 
ATOM   1703 C CA  . SER A  1 217 ? -25.808 -8.541  -17.025 1.00 17.35 ? 214 SER B CA  1 
ATOM   1704 C C   . SER A  1 217 ? -26.725 -9.290  -16.068 1.00 16.45 ? 214 SER B C   1 
ATOM   1705 O O   . SER A  1 217 ? -27.662 -8.673  -15.541 1.00 16.08 ? 214 SER B O   1 
ATOM   1706 C CB  . SER A  1 217 ? -26.155 -8.836  -18.439 1.00 18.51 ? 214 SER B CB  1 
ATOM   1707 O OG  . SER A  1 217 ? -25.425 -7.931  -19.261 1.00 18.88 ? 214 SER B OG  1 
ATOM   1708 N N   . THR A  1 218 ? -26.472 -10.590 -15.896 1.00 17.01 ? 215 THR B N   1 
ATOM   1709 C CA  . THR A  1 218 ? -27.302 -11.437 -15.044 1.00 17.16 ? 215 THR B CA  1 
ATOM   1710 C C   . THR A  1 218 ? -27.255 -11.006 -13.584 1.00 17.35 ? 215 THR B C   1 
ATOM   1711 O O   . THR A  1 218 ? -28.300 -11.069 -12.916 1.00 16.39 ? 215 THR B O   1 
ATOM   1712 C CB  . THR A  1 218 ? -26.999 -12.930 -15.190 1.00 18.42 ? 215 THR B CB  1 
ATOM   1713 O OG1 . THR A  1 218 ? -25.664 -13.221 -14.825 1.00 19.08 ? 215 THR B OG1 1 
ATOM   1714 C CG2 . THR A  1 218 ? -27.346 -13.431 -16.591 1.00 19.63 ? 215 THR B CG2 1 
ATOM   1715 N N   . LEU A  1 219 ? -26.099 -10.501 -13.107 1.00 16.53 ? 216 LEU B N   1 
ATOM   1716 C CA  . LEU A  1 219 ? -26.035 -9.922  -11.766 1.00 18.46 ? 216 LEU B CA  1 
ATOM   1717 C C   . LEU A  1 219 ? -27.100 -8.839  -11.571 1.00 17.03 ? 216 LEU B C   1 
ATOM   1718 O O   . LEU A  1 219 ? -27.760 -8.816  -10.536 1.00 17.02 ? 216 LEU B O   1 
ATOM   1719 C CB  . LEU A  1 219 ? -24.637 -9.377  -11.515 1.00 20.52 ? 216 LEU B CB  1 
ATOM   1720 C CG  . LEU A  1 219 ? -24.367 -8.668  -10.199 1.00 24.60 ? 216 LEU B CG  1 
ATOM   1721 C CD1 . LEU A  1 219 ? -24.221 -9.729  -9.134  1.00 28.87 ? 216 LEU B CD1 1 
ATOM   1722 C CD2 . LEU A  1 219 ? -23.099 -7.795  -10.266 1.00 28.03 ? 216 LEU B CD2 1 
ATOM   1723 N N   . ILE A  1 220 ? -27.261 -7.952  -12.542 1.00 16.28 ? 217 ILE B N   1 
ATOM   1724 C CA  . ILE A  1 220 ? -28.165 -6.813  -12.430 1.00 15.28 ? 217 ILE B CA  1 
ATOM   1725 C C   . ILE A  1 220 ? -29.605 -7.306  -12.622 1.00 14.65 ? 217 ILE B C   1 
ATOM   1726 O O   . ILE A  1 220 ? -30.497 -6.769  -11.989 1.00 14.90 ? 217 ILE B O   1 
ATOM   1727 C CB  . ILE A  1 220 ? -27.785 -5.648  -13.352 1.00 15.22 ? 217 ILE B CB  1 
ATOM   1728 C CG1 . ILE A  1 220 ? -26.311 -5.208  -13.049 1.00 17.33 ? 217 ILE B CG1 1 
ATOM   1729 C CG2 . ILE A  1 220 ? -28.739 -4.455  -13.167 1.00 15.02 ? 217 ILE B CG2 1 
ATOM   1730 C CD1 . ILE A  1 220 ? -25.738 -4.134  -13.970 1.00 18.24 ? 217 ILE B CD1 1 
ATOM   1731 N N   . MET A  1 221 ? -29.851 -8.270  -13.511 1.00 14.67 ? 218 MET B N   1 
ATOM   1732 C CA  . MET A  1 221 ? -31.154 -8.920  -13.651 1.00 16.26 ? 218 MET B CA  1 
ATOM   1733 C C   . MET A  1 221 ? -31.616 -9.504  -12.311 1.00 16.52 ? 218 MET B C   1 
ATOM   1734 O O   . MET A  1 221 ? -32.784 -9.372  -11.928 1.00 16.99 ? 218 MET B O   1 
ATOM   1735 C CB  . MET A  1 221 ? -31.094 -9.967  -14.777 1.00 17.02 ? 218 MET B CB  1 
ATOM   1736 C CG  . MET A  1 221 ? -30.939 -9.366  -16.163 1.00 17.50 ? 218 MET B CG  1 
ATOM   1737 S SD  . MET A  1 221 ? -30.845 -10.648 -17.440 1.00 20.43 ? 218 MET B SD  1 
ATOM   1738 C CE  . MET A  1 221 ? -32.464 -11.415 -17.493 1.00 21.03 ? 218 MET B CE  1 
ATOM   1739 N N   . GLN A  1 222 ? -30.665 -10.144 -11.596 1.00 16.67 ? 219 GLN B N   1 
ATOM   1740 C CA  . GLN A  1 222 ? -30.903 -10.625 -10.247 1.00 17.22 ? 219 GLN B CA  1 
ATOM   1741 C C   . GLN A  1 222 ? -31.273 -9.519  -9.259  1.00 16.10 ? 219 GLN B C   1 
ATOM   1742 O O   . GLN A  1 222 ? -32.199 -9.749  -8.473  1.00 15.46 ? 219 GLN B O   1 
ATOM   1743 C CB  . GLN A  1 222 ? -29.757 -11.489 -9.759  1.00 17.55 ? 219 GLN B CB  1 
ATOM   1744 C CG  . GLN A  1 222 ? -29.686 -12.770 -10.582 1.00 20.23 ? 219 GLN B CG  1 
ATOM   1745 C CD  . GLN A  1 222 ? -28.307 -13.381 -10.679 1.00 21.60 ? 219 GLN B CD  1 
ATOM   1746 O OE1 . GLN A  1 222 ? -27.427 -13.192 -9.827  1.00 23.71 ? 219 GLN B OE1 1 
ATOM   1747 N NE2 . GLN A  1 222 ? -28.121 -14.159 -11.735 1.00 21.99 ? 219 GLN B NE2 1 
ATOM   1748 N N   . LEU A  1 223 ? -30.639 -8.349  -9.347  1.00 15.61 ? 220 LEU B N   1 
ATOM   1749 C CA  . LEU A  1 223 ? -30.984 -7.226  -8.460  1.00 14.35 ? 220 LEU B CA  1 
ATOM   1750 C C   . LEU A  1 223 ? -32.393 -6.724  -8.747  1.00 15.06 ? 220 LEU B C   1 
ATOM   1751 O O   . LEU A  1 223 ? -33.111 -6.407  -7.794  1.00 14.13 ? 220 LEU B O   1 
ATOM   1752 C CB  . LEU A  1 223 ? -29.961 -6.099  -8.647  1.00 14.49 ? 220 LEU B CB  1 
ATOM   1753 C CG  . LEU A  1 223 ? -28.561 -6.461  -8.135  1.00 16.08 ? 220 LEU B CG  1 
ATOM   1754 C CD1 . LEU A  1 223 ? -27.572 -5.412  -8.579  1.00 15.84 ? 220 LEU B CD1 1 
ATOM   1755 C CD2 . LEU A  1 223 ? -28.550 -6.648  -6.634  1.00 18.22 ? 220 LEU B CD2 1 
ATOM   1756 N N   . LEU A  1 224 ? -32.764 -6.617  -10.050 1.00 15.47 ? 221 LEU B N   1 
ATOM   1757 C CA  . LEU A  1 224 ? -34.129 -6.278  -10.436 1.00 16.60 ? 221 LEU B CA  1 
ATOM   1758 C C   . LEU A  1 224 ? -35.141 -7.228  -9.806  1.00 17.40 ? 221 LEU B C   1 
ATOM   1759 O O   . LEU A  1 224 ? -36.111 -6.752  -9.168  1.00 15.42 ? 221 LEU B O   1 
ATOM   1760 C CB  . LEU A  1 224 ? -34.250 -6.228  -11.948 1.00 16.62 ? 221 LEU B CB  1 
ATOM   1761 C CG  . LEU A  1 224 ? -33.579 -5.007  -12.595 1.00 17.61 ? 221 LEU B CG  1 
ATOM   1762 C CD1 . LEU A  1 224 ? -33.265 -5.262  -14.068 1.00 19.76 ? 221 LEU B CD1 1 
ATOM   1763 C CD2 . LEU A  1 224 ? -34.417 -3.738  -12.455 1.00 18.34 ? 221 LEU B CD2 1 
ATOM   1764 N N   . ARG A  1 225 ? -34.910 -8.561  -10.007 1.00 17.89 ? 222 ARG B N   1 
ATOM   1765 C CA  . ARG A  1 225 ? -35.796 -9.567  -9.423  1.00 19.19 ? 222 ARG B CA  1 
ATOM   1766 C C   . ARG A  1 225 ? -35.906 -9.379  -7.906  1.00 19.01 ? 222 ARG B C   1 
ATOM   1767 O O   . ARG A  1 225 ? -37.022 -9.454  -7.352  1.00 17.94 ? 222 ARG B O   1 
ATOM   1768 C CB  . ARG A  1 225 ? -35.408 -11.014 -9.769  1.00 20.82 ? 222 ARG B CB  1 
ATOM   1769 C CG  . ARG A  1 225 ? -36.273 -12.079 -9.091  1.00 23.35 ? 222 ARG B CG  1 
ATOM   1770 C CD  . ARG A  1 225 ? -36.105 -13.452 -9.708  1.00 24.99 ? 222 ARG B CD  1 
ATOM   1771 N NE  . ARG A  1 225 ? -36.838 -14.476 -8.955  1.00 25.94 ? 222 ARG B NE  1 
ATOM   1772 C CZ  . ARG A  1 225 ? -36.492 -14.989 -7.809  1.00 28.23 ? 222 ARG B CZ  1 
ATOM   1773 N NH1 . ARG A  1 225 ? -35.288 -14.801 -7.269  1.00 30.22 ? 222 ARG B NH1 1 
ATOM   1774 N NH2 . ARG A  1 225 ? -37.381 -15.737 -7.193  1.00 32.22 ? 222 ARG B NH2 1 
ATOM   1775 N N   . ASP A  1 226 ? -34.757 -9.215  -7.226  1.00 17.82 ? 223 ASP B N   1 
ATOM   1776 C CA  . ASP A  1 226 ? -34.768 -9.156  -5.758  1.00 18.51 ? 223 ASP B CA  1 
ATOM   1777 C C   . ASP A  1 226 ? -35.539 -7.940  -5.236  1.00 17.55 ? 223 ASP B C   1 
ATOM   1778 O O   . ASP A  1 226 ? -36.240 -8.069  -4.218  1.00 17.12 ? 223 ASP B O   1 
ATOM   1779 C CB  . ASP A  1 226 ? -33.374 -9.318  -5.189  1.00 18.81 ? 223 ASP B CB  1 
ATOM   1780 C CG  . ASP A  1 226 ? -32.674 -10.645 -5.459  1.00 20.25 ? 223 ASP B CG  1 
ATOM   1781 O OD1 . ASP A  1 226 ? -33.333 -11.592 -5.904  1.00 22.21 ? 223 ASP B OD1 1 
ATOM   1782 O OD2 . ASP A  1 226 ? -31.477 -10.717 -5.181  1.00 21.60 ? 223 ASP B OD2 1 
ATOM   1783 N N   . ASN A  1 227 ? -35.414 -6.792  -5.922  1.00 17.47 ? 224 ASN B N   1 
ATOM   1784 C CA  . ASN A  1 227 ? -36.205 -5.603  -5.591  1.00 17.35 ? 224 ASN B CA  1 
ATOM   1785 C C   . ASN A  1 227 ? -37.680 -5.872  -5.816  1.00 17.62 ? 224 ASN B C   1 
ATOM   1786 O O   . ASN A  1 227 ? -38.469 -5.540  -4.936  1.00 18.26 ? 224 ASN B O   1 
ATOM   1787 C CB  . ASN A  1 227 ? -35.761 -4.347  -6.336  1.00 16.10 ? 224 ASN B CB  1 
ATOM   1788 C CG  . ASN A  1 227 ? -34.459 -3.770  -5.832  1.00 15.85 ? 224 ASN B CG  1 
ATOM   1789 O OD1 . ASN A  1 227 ? -33.856 -4.278  -4.874  1.00 15.77 ? 224 ASN B OD1 1 
ATOM   1790 N ND2 . ASN A  1 227 ? -34.036 -2.684  -6.433  1.00 14.86 ? 224 ASN B ND2 1 
ATOM   1791 N N   . LEU A  1 228 ? -38.046 -6.526  -6.945  1.00 18.06 ? 225 LEU B N   1 
ATOM   1792 C CA  . LEU A  1 228 ? -39.438 -6.916  -7.166  1.00 19.17 ? 225 LEU B CA  1 
ATOM   1793 C C   . LEU A  1 228 ? -39.980 -7.865  -6.082  1.00 20.26 ? 225 LEU B C   1 
ATOM   1794 O O   . LEU A  1 228 ? -41.112 -7.639  -5.676  1.00 21.79 ? 225 LEU B O   1 
ATOM   1795 C CB  . LEU A  1 228 ? -39.621 -7.463  -8.580  1.00 19.85 ? 225 LEU B CB  1 
ATOM   1796 C CG  . LEU A  1 228 ? -39.453 -6.456  -9.720  1.00 20.16 ? 225 LEU B CG  1 
ATOM   1797 C CD1 . LEU A  1 228 ? -39.304 -7.109  -11.021 1.00 19.99 ? 225 LEU B CD1 1 
ATOM   1798 C CD2 . LEU A  1 228 ? -40.617 -5.467  -9.802  1.00 21.94 ? 225 LEU B CD2 1 
ATOM   1799 N N   . THR A  1 229 ? -39.178 -8.809  -5.545  1.00 19.23 ? 226 THR B N   1 
ATOM   1800 C CA  . THR A  1 229 ? -39.565 -9.724  -4.470  1.00 21.59 ? 226 THR B CA  1 
ATOM   1801 C C   . THR A  1 229 ? -39.825 -8.939  -3.187  1.00 21.29 ? 226 THR B C   1 
ATOM   1802 O O   . THR A  1 229 ? -40.848 -9.130  -2.549  1.00 23.19 ? 226 THR B O   1 
ATOM   1803 C CB  . THR A  1 229 ? -38.497 -10.817 -4.300  1.00 21.66 ? 226 THR B CB  1 
ATOM   1804 O OG1 . THR A  1 229 ? -38.418 -11.506 -5.542  1.00 21.09 ? 226 THR B OG1 1 
ATOM   1805 C CG2 . THR A  1 229 ? -38.787 -11.822 -3.198  1.00 23.10 ? 226 THR B CG2 1 
ATOM   1806 N N   . LEU A  1 230 ? -38.902 -8.074  -2.840  1.00 21.39 ? 227 LEU B N   1 
ATOM   1807 C CA  . LEU A  1 230 ? -39.015 -7.152  -1.708  1.00 20.78 ? 227 LEU B CA  1 
ATOM   1808 C C   . LEU A  1 230 ? -40.275 -6.293  -1.818  1.00 22.06 ? 227 LEU B C   1 
ATOM   1809 O O   . LEU A  1 230 ? -41.091 -6.268  -0.887  1.00 23.03 ? 227 LEU B O   1 
ATOM   1810 C CB  . LEU A  1 230 ? -37.757 -6.291  -1.602  1.00 20.12 ? 227 LEU B CB  1 
ATOM   1811 C CG  . LEU A  1 230 ? -37.743 -5.293  -0.440  1.00 20.90 ? 227 LEU B CG  1 
ATOM   1812 C CD1 . LEU A  1 230 ? -37.908 -6.025  0.916   1.00 22.17 ? 227 LEU B CD1 1 
ATOM   1813 C CD2 . LEU A  1 230 ? -36.512 -4.409  -0.513  1.00 19.32 ? 227 LEU B CD2 1 
ATOM   1814 N N   . TRP A  1 231 ? -40.474 -5.660  -2.970  1.00 22.19 ? 228 TRP B N   1 
ATOM   1815 C CA  . TRP A  1 231 ? -41.549 -4.678  -3.135  1.00 21.49 ? 228 TRP B CA  1 
ATOM   1816 C C   . TRP A  1 231 ? -42.959 -5.285  -3.238  1.00 23.84 ? 228 TRP B C   1 
ATOM   1817 O O   . TRP A  1 231 ? -43.952 -4.558  -3.019  1.00 24.28 ? 228 TRP B O   1 
ATOM   1818 C CB  . TRP A  1 231 ? -41.183 -3.761  -4.309  1.00 19.59 ? 228 TRP B CB  1 
ATOM   1819 C CG  . TRP A  1 231 ? -39.989 -2.881  -4.064  1.00 18.34 ? 228 TRP B CG  1 
ATOM   1820 C CD1 . TRP A  1 231 ? -39.369 -2.524  -2.910  1.00 18.13 ? 228 TRP B CD1 1 
ATOM   1821 C CD2 . TRP A  1 231 ? -39.255 -2.218  -5.106  1.00 17.59 ? 228 TRP B CD2 1 
ATOM   1822 N NE1 . TRP A  1 231 ? -38.339 -1.668  -3.160  1.00 17.93 ? 228 TRP B NE1 1 
ATOM   1823 C CE2 . TRP A  1 231 ? -38.241 -1.447  -4.494  1.00 16.98 ? 228 TRP B CE2 1 
ATOM   1824 C CE3 . TRP A  1 231 ? -39.423 -2.173  -6.490  1.00 17.34 ? 228 TRP B CE3 1 
ATOM   1825 C CZ2 . TRP A  1 231 ? -37.355 -0.651  -5.217  1.00 16.25 ? 228 TRP B CZ2 1 
ATOM   1826 C CZ3 . TRP A  1 231 ? -38.505 -1.446  -7.218  1.00 16.93 ? 228 TRP B CZ3 1 
ATOM   1827 C CH2 . TRP A  1 231 ? -37.476 -0.691  -6.595  1.00 16.09 ? 228 TRP B CH2 1 
ATOM   1828 N N   . THR A  1 232 ? -43.065 -6.583  -3.585  1.00 24.56 ? 229 THR B N   1 
ATOM   1829 C CA  . THR A  1 232 ? -44.314 -7.349  -3.593  1.00 27.43 ? 229 THR B CA  1 
ATOM   1830 C C   . THR A  1 232 ? -44.529 -8.187  -2.335  1.00 31.02 ? 229 THR B C   1 
ATOM   1831 O O   . THR A  1 232 ? -45.513 -8.917  -2.292  1.00 33.55 ? 229 THR B O   1 
ATOM   1832 C CB  . THR A  1 232 ? -44.366 -8.229  -4.849  1.00 26.88 ? 229 THR B CB  1 
ATOM   1833 O OG1 . THR A  1 232 ? -43.234 -9.089  -4.831  1.00 25.57 ? 229 THR B OG1 1 
ATOM   1834 C CG2 . THR A  1 232 ? -44.339 -7.409  -6.126  1.00 26.13 ? 229 THR B CG2 1 
ATOM   1835 N N   . GLY A  1 233 ? -43.721 -8.061  -1.289  1.00 30.61 ? 230 GLY B N   1 
ATOM   1836 C CA  . GLY A  1 233 ? -44.010 -8.685  -0.001  1.00 34.09 ? 230 GLY B CA  1 
ATOM   1837 C C   . GLY A  1 233 ? -43.359 -10.058 0.186   1.00 33.19 ? 230 GLY B C   1 
ATOM   1838 O O   . GLY A  1 233 ? -43.646 -10.684 1.187   1.00 32.96 ? 230 GLY B O   1 
ATOM   1839 N N   . GLY A  1 234 ? -42.457 -10.492 -0.720  1.00 31.48 ? 231 GLY B N   1 
ATOM   1840 C CA  . GLY A  1 234 ? -41.716 -11.742 -0.621  1.00 30.71 ? 231 GLY B CA  1 
ATOM   1841 C C   . GLY A  1 234 ? -40.441 -11.686 0.218   1.00 29.93 ? 231 GLY B C   1 
ATOM   1842 O O   . GLY A  1 234 ? -39.723 -12.679 0.253   1.00 29.63 ? 231 GLY B O   1 
ATOM   1843 N N   . GLY A  1 235 ? -40.136 -10.569 0.892   1.00 31.19 ? 232 GLY B N   1 
ATOM   1844 C CA  . GLY A  1 235 ? -39.033 -10.498 1.835   1.00 32.76 ? 232 GLY B CA  1 
ATOM   1845 C C   . GLY A  1 235 ? -37.758 -10.022 1.150   1.00 31.63 ? 232 GLY B C   1 
ATOM   1846 O O   . GLY A  1 235 ? -37.712 -9.824  -0.084  1.00 27.66 ? 232 GLY B O   1 
ATOM   1847 N N   . GLY A  1 236 ? -36.771 -9.736  2.011   1.00 30.47 ? 233 GLY B N   1 
ATOM   1848 C CA  . GLY A  1 236 ? -35.392 -9.437  1.660   1.00 28.80 ? 233 GLY B CA  1 
ATOM   1849 C C   . GLY A  1 236 ? -34.822 -8.331  2.556   1.00 30.84 ? 233 GLY B C   1 
ATOM   1850 O O   . GLY A  1 236 ? -35.549 -7.754  3.359   1.00 31.51 ? 233 GLY B O   1 
ATOM   1851 N N   . SER A  1 237 ? -33.517 -8.057  2.392   1.00 29.21 ? 234 SER B N   1 
ATOM   1852 C CA  . SER A  1 237 ? -32.823 -6.946  3.017   1.00 33.11 ? 234 SER B CA  1 
ATOM   1853 C C   . SER A  1 237 ? -33.068 -5.659  2.208   1.00 27.56 ? 234 SER B C   1 
ATOM   1854 O O   . SER A  1 237 ? -33.915 -5.599  1.315   1.00 31.68 ? 234 SER B O   1 
ATOM   1855 C CB  . SER A  1 237 ? -31.314 -7.324  3.162   1.00 34.85 ? 234 SER B CB  1 
ATOM   1856 O OG  . SER A  1 237 ? -30.838 -7.921  1.963   1.00 41.42 ? 234 SER B OG  1 
ATOM   1857 N N   . ARG A  1 238 ? -32.366 -4.587  2.578   1.00 24.29 ? 235 ARG B N   1 
ATOM   1858 C CA  . ARG A  1 238 ? -32.388 -3.308  1.905   1.00 22.47 ? 235 ARG B CA  1 
ATOM   1859 C C   . ARG A  1 238 ? -32.325 -3.494  0.390   1.00 20.77 ? 235 ARG B C   1 
ATOM   1860 O O   . ARG A  1 238 ? -31.486 -4.285  -0.101  1.00 18.67 ? 235 ARG B O   1 
ATOM   1861 C CB  . ARG A  1 238 ? -31.267 -2.405  2.440   1.00 24.68 ? 235 ARG B CB  1 
ATOM   1862 C CG  . ARG A  1 238 ? -31.010 -1.071  1.748   1.00 22.67 ? 235 ARG B CG  1 
ATOM   1863 C CD  . ARG A  1 238 ? -29.795 -0.354  2.291   1.00 24.79 ? 235 ARG B CD  1 
ATOM   1864 N NE  . ARG A  1 238 ? -29.411 0.808   1.477   1.00 22.54 ? 235 ARG B NE  1 
ATOM   1865 C CZ  . ARG A  1 238 ? -30.100 1.947   1.363   1.00 20.23 ? 235 ARG B CZ  1 
ATOM   1866 N NH1 . ARG A  1 238 ? -31.177 2.160   2.079   1.00 19.80 ? 235 ARG B NH1 1 
ATOM   1867 N NH2 . ARG A  1 238 ? -29.739 2.858   0.481   1.00 20.14 ? 235 ARG B NH2 1 
ATOM   1868 N N   . ARG A  1 239 ? -33.191 -2.730  -0.330  1.00 17.89 ? 236 ARG B N   1 
ATOM   1869 C CA  . ARG A  1 239 ? -33.238 -2.775  -1.780  1.00 17.62 ? 236 ARG B CA  1 
ATOM   1870 C C   . ARG A  1 239 ? -31.859 -2.582  -2.383  1.00 15.50 ? 236 ARG B C   1 
ATOM   1871 O O   . ARG A  1 239 ? -31.051 -1.828  -1.812  1.00 15.79 ? 236 ARG B O   1 
ATOM   1872 C CB  . ARG A  1 239 ? -34.165 -1.704  -2.387  1.00 17.27 ? 236 ARG B CB  1 
ATOM   1873 C CG  . ARG A  1 239 ? -33.688 -0.256  -2.511  1.00 16.73 ? 236 ARG B CG  1 
ATOM   1874 C CD  . ARG A  1 239 ? -33.242 0.416   -1.180  1.00 16.73 ? 236 ARG B CD  1 
ATOM   1875 N NE  . ARG A  1 239 ? -32.712 1.735   -1.547  1.00 16.27 ? 236 ARG B NE  1 
ATOM   1876 C CZ  . ARG A  1 239 ? -31.521 2.012   -2.114  1.00 15.83 ? 236 ARG B CZ  1 
ATOM   1877 N NH1 . ARG A  1 239 ? -30.616 1.054   -2.190  1.00 16.42 ? 236 ARG B NH1 1 
ATOM   1878 N NH2 . ARG A  1 239 ? -31.223 3.270   -2.460  1.00 14.91 ? 236 ARG B NH2 1 
ATOM   1879 N N   . GLY A  1 240 ? -31.650 -3.159  -3.583  1.00 15.32 ? 237 GLY B N   1 
ATOM   1880 C CA  . GLY A  1 240 ? -30.366 -2.999  -4.270  1.00 15.72 ? 237 GLY B CA  1 
ATOM   1881 C C   . GLY A  1 240 ? -30.403 -1.828  -5.258  1.00 15.44 ? 237 GLY B C   1 
ATOM   1882 O O   . GLY A  1 240 ? -31.422 -1.575  -5.929  1.00 15.04 ? 237 GLY B O   1 
HETATM 1883 N N   . TPO A  1 241 ? -29.258 -1.111  -5.341  1.00 14.28 ? 238 TPO B N   1 
HETATM 1884 C CA  . TPO A  1 241 ? -28.949 -0.325  -6.541  1.00 13.58 ? 238 TPO B CA  1 
HETATM 1885 C CB  . TPO A  1 241 ? -28.905 1.176   -6.214  1.00 13.13 ? 238 TPO B CB  1 
HETATM 1886 C CG2 . TPO A  1 241 ? -30.280 1.757   -5.925  1.00 15.09 ? 238 TPO B CG2 1 
HETATM 1887 O OG1 . TPO A  1 241 ? -28.077 1.370   -5.041  1.00 13.77 ? 238 TPO B OG1 1 
HETATM 1888 P P   . TPO A  1 241 ? -27.598 2.839   -4.594  1.00 15.53 ? 238 TPO B P   1 
HETATM 1889 O O1P . TPO A  1 241 ? -27.192 3.628   -5.817  1.00 14.06 ? 238 TPO B O1P 1 
HETATM 1890 O O2P . TPO A  1 241 ? -28.753 3.546   -3.873  1.00 14.04 ? 238 TPO B O2P 1 
HETATM 1891 O O3P . TPO A  1 241 ? -26.496 2.543   -3.584  1.00 13.77 ? 238 TPO B O3P 1 
HETATM 1892 C C   . TPO A  1 241 ? -27.728 -0.920  -7.246  1.00 13.57 ? 238 TPO B C   1 
HETATM 1893 O O   . TPO A  1 241 ? -27.107 -1.870  -6.820  1.00 12.18 ? 238 TPO B O   1 
ATOM   1894 N N   . SER A  1 242 ? -27.433 -0.334  -8.399  1.00 14.58 ? 239 SER B N   1 
ATOM   1895 C CA  . SER A  1 242 ? -26.514 -0.884  -9.362  1.00 15.54 ? 239 SER B CA  1 
ATOM   1896 C C   . SER A  1 242 ? -25.121 -0.981  -8.755  1.00 14.37 ? 239 SER B C   1 
ATOM   1897 O O   . SER A  1 242 ? -24.699 -0.075  -7.992  1.00 14.26 ? 239 SER B O   1 
ATOM   1898 C CB  . SER A  1 242 ? -26.510 0.013   -10.607 1.00 18.24 ? 239 SER B CB  1 
ATOM   1899 O OG  . SER A  1 242 ? -25.649 -0.506  -11.605 1.00 20.53 ? 239 SER B OG  1 
ATOM   1900 N N   . PRO A  1 243 ? -24.343 -2.026  -9.109  1.00 15.42 ? 240 PRO B N   1 
ATOM   1901 C CA  . PRO A  1 243 ? -22.921 -1.990  -8.829  1.00 17.63 ? 240 PRO B CA  1 
ATOM   1902 C C   . PRO A  1 243 ? -22.265 -0.805  -9.502  1.00 17.34 ? 240 PRO B C   1 
ATOM   1903 O O   . PRO A  1 243 ? -22.786 -0.298  -10.490 1.00 17.82 ? 240 PRO B O   1 
ATOM   1904 C CB  . PRO A  1 243 ? -22.363 -3.321  -9.330  1.00 19.25 ? 240 PRO B CB  1 
ATOM   1905 C CG  . PRO A  1 243 ? -23.380 -3.752  -10.349 1.00 21.05 ? 240 PRO B CG  1 
ATOM   1906 C CD  . PRO A  1 243 ? -24.711 -3.216  -9.914  1.00 18.07 ? 240 PRO B CD  1 
ATOM   1907 N N   . ALA A  1 244 ? -21.245 -0.245  -8.847  1.00 19.44 ? 241 ALA B N   1 
ATOM   1908 C CA  . ALA A  1 244 ? -20.407 0.805   -9.420  1.00 19.47 ? 241 ALA B CA  1 
ATOM   1909 C C   . ALA A  1 244 ? -19.730 0.365   -10.714 1.00 18.54 ? 241 ALA B C   1 
ATOM   1910 O O   . ALA A  1 244 ? -19.642 1.158   -11.639 1.00 20.17 ? 241 ALA B O   1 
ATOM   1911 C CB  . ALA A  1 244 ? -19.362 1.270   -8.408  1.00 21.07 ? 241 ALA B CB  1 
ATOM   1912 N N   . ARG A  1 245 ? -19.225 -0.875  -10.741 1.00 17.70 ? 242 ARG B N   1 
ATOM   1913 C CA  . ARG A  1 245 ? -18.627 -1.470  -11.935 1.00 18.29 ? 242 ARG B CA  1 
ATOM   1914 C C   . ARG A  1 245 ? -19.705 -2.347  -12.569 1.00 20.73 ? 242 ARG B C   1 
ATOM   1915 O O   . ARG A  1 245 ? -19.889 -3.474  -12.125 1.00 21.46 ? 242 ARG B O   1 
ATOM   1916 C CB  . ARG A  1 245 ? -17.329 -2.126  -11.461 1.00 18.25 ? 242 ARG B CB  1 
ATOM   1917 C CG  . ARG A  1 245 ? -16.608 -2.982  -12.494 1.00 21.41 ? 242 ARG B CG  1 
ATOM   1918 C CD  . ARG A  1 245 ? -15.203 -3.460  -12.119 1.00 21.00 ? 242 ARG B CD  1 
ATOM   1919 N NE  . ARG A  1 245 ? -14.165 -2.420  -11.979 1.00 21.60 ? 242 ARG B NE  1 
ATOM   1920 C CZ  . ARG A  1 245 ? -13.476 -2.095  -10.863 1.00 21.20 ? 242 ARG B CZ  1 
ATOM   1921 N NH1 . ARG A  1 245 ? -13.854 -2.549  -9.671  1.00 19.77 ? 242 ARG B NH1 1 
ATOM   1922 N NH2 . ARG A  1 245 ? -12.452 -1.236  -10.875 1.00 20.82 ? 242 ARG B NH2 1 
ATOM   1923 N N   . MET A  1 246 ? -20.428 -1.805  -13.580 1.00 20.30 ? 243 MET B N   1 
ATOM   1924 C CA  . MET A  1 246 ? -21.524 -2.492  -14.252 1.00 21.73 ? 243 MET B CA  1 
ATOM   1925 C C   . MET A  1 246 ? -21.034 -3.465  -15.327 1.00 21.57 ? 243 MET B C   1 
ATOM   1926 O O   . MET A  1 246 ? -21.576 -4.551  -15.374 1.00 20.76 ? 243 MET B O   1 
ATOM   1927 C CB  . MET A  1 246 ? -22.505 -1.501  -14.872 1.00 21.17 ? 243 MET B CB  1 
ATOM   1928 C CG  . MET A  1 246 ? -23.333 -0.784  -13.828 1.00 22.78 ? 243 MET B CG  1 
ATOM   1929 S SD  . MET A  1 246 ? -24.174 0.616   -14.597 1.00 25.40 ? 243 MET B SD  1 
ATOM   1930 C CE  . MET A  1 246 ? -22.901 1.838   -14.293 1.00 29.14 ? 243 MET B CE  1 
ATOM   1931 N N   . ALA A  1 247 ? -20.073 -3.069  -16.185 1.00 24.80 ? 244 ALA B N   1 
ATOM   1932 C CA  . ALA A  1 247 ? -19.631 -3.851  -17.341 1.00 24.55 ? 244 ALA B CA  1 
ATOM   1933 C C   . ALA A  1 247 ? -18.104 -3.893  -17.376 1.00 27.38 ? 244 ALA B C   1 
ATOM   1934 O O   . ALA A  1 247 ? -17.483 -2.824  -17.358 1.00 24.80 ? 244 ALA B O   1 
ATOM   1935 C CB  . ALA A  1 247 ? -20.200 -3.282  -18.634 1.00 27.27 ? 244 ALA B CB  1 
ATOM   1936 N N   . GLY A  1 248 ? -17.530 -5.116  -17.484 1.00 31.88 ? 245 GLY B N   1 
ATOM   1937 C CA  . GLY A  1 248 ? -16.119 -5.317  -17.763 1.00 31.84 ? 245 GLY B CA  1 
ATOM   1938 C C   . GLY A  1 248 ? -15.234 -5.014  -16.545 1.00 36.83 ? 245 GLY B C   1 
ATOM   1939 O O   . GLY A  1 248 ? -15.741 -4.889  -15.428 1.00 35.61 ? 245 GLY B O   1 
ATOM   1940 N N   . ASN A  1 249 ? -13.910 -4.885  -16.812 1.00 38.54 ? 246 ASN B N   1 
ATOM   1941 C CA  . ASN A  1 249 ? -12.867 -4.511  -15.857 1.00 43.09 ? 246 ASN B CA  1 
ATOM   1942 C C   . ASN A  1 249 ? -13.005 -3.052  -15.389 1.00 38.78 ? 246 ASN B C   1 
ATOM   1943 O O   . ASN A  1 249 ? -13.393 -2.162  -16.192 1.00 39.84 ? 246 ASN B O   1 
ATOM   1944 C CB  . ASN A  1 249 ? -11.452 -4.617  -16.450 1.00 48.46 ? 246 ASN B CB  1 
ATOM   1945 C CG  . ASN A  1 249 ? -10.976 -6.028  -16.710 1.00 59.08 ? 246 ASN B CG  1 
ATOM   1946 O OD1 . ASN A  1 249 ? -11.566 -7.010  -16.225 1.00 60.30 ? 246 ASN B OD1 1 
ATOM   1947 N ND2 . ASN A  1 249 ? -9.866  -6.136  -17.433 1.00 62.03 ? 246 ASN B ND2 1 
ATOM   1948 O OXT . ASN A  1 249 ? -12.650 -2.833  -14.243 1.00 41.04 ? 246 ASN B OXT 1 
ATOM   1949 N N   . ASP B  2 5   ? -16.204 19.653  27.475  1.00 52.47 ? 2   ASP A N   1 
ATOM   1950 C CA  . ASP B  2 5   ? -16.767 18.802  28.562  1.00 52.97 ? 2   ASP A CA  1 
ATOM   1951 C C   . ASP B  2 5   ? -16.569 17.303  28.229  1.00 48.98 ? 2   ASP A C   1 
ATOM   1952 O O   . ASP B  2 5   ? -16.818 16.879  27.093  1.00 47.20 ? 2   ASP A O   1 
ATOM   1953 C CB  . ASP B  2 5   ? -18.213 19.196  28.805  1.00 55.26 ? 2   ASP A CB  1 
ATOM   1954 C CG  . ASP B  2 5   ? -19.017 18.267  29.704  1.00 59.96 ? 2   ASP A CG  1 
ATOM   1955 O OD1 . ASP B  2 5   ? -19.745 17.425  29.147  1.00 57.24 ? 2   ASP A OD1 1 
ATOM   1956 O OD2 . ASP B  2 5   ? -18.924 18.396  30.946  1.00 70.04 ? 2   ASP A OD2 1 
ATOM   1957 N N   . LYS B  2 6   ? -16.224 16.496  29.263  1.00 47.20 ? 3   LYS A N   1 
ATOM   1958 C CA  . LYS B  2 6   ? -15.858 15.080  29.143  1.00 43.90 ? 3   LYS A CA  1 
ATOM   1959 C C   . LYS B  2 6   ? -17.085 14.248  28.766  1.00 41.56 ? 3   LYS A C   1 
ATOM   1960 O O   . LYS B  2 6   ? -17.043 13.531  27.783  1.00 38.17 ? 3   LYS A O   1 
ATOM   1961 C CB  . LYS B  2 6   ? -15.238 14.522  30.436  1.00 44.37 ? 3   LYS A CB  1 
ATOM   1962 C CG  . LYS B  2 6   ? -15.089 13.012  30.600  1.00 45.69 ? 3   LYS A CG  1 
ATOM   1963 C CD  . LYS B  2 6   ? -14.086 12.601  31.677  1.00 47.38 ? 3   LYS A CD  1 
ATOM   1964 C CE  . LYS B  2 6   ? -14.123 11.131  31.890  1.00 47.83 ? 3   LYS A CE  1 
ATOM   1965 N NZ  . LYS B  2 6   ? -12.853 10.609  32.424  1.00 48.65 ? 3   LYS A NZ  1 
ATOM   1966 N N   . ASN B  2 7   ? -18.189 14.396  29.527  1.00 45.62 ? 4   ASN A N   1 
ATOM   1967 C CA  . ASN B  2 7   ? -19.434 13.679  29.267  1.00 45.70 ? 4   ASN A CA  1 
ATOM   1968 C C   . ASN B  2 7   ? -19.920 13.878  27.815  1.00 43.42 ? 4   ASN A C   1 
ATOM   1969 O O   . ASN B  2 7   ? -20.239 12.886  27.153  1.00 42.12 ? 4   ASN A O   1 
ATOM   1970 C CB  . ASN B  2 7   ? -20.479 13.949  30.340  1.00 54.03 ? 4   ASN A CB  1 
ATOM   1971 C CG  . ASN B  2 7   ? -21.706 13.106  30.093  1.00 61.97 ? 4   ASN A CG  1 
ATOM   1972 O OD1 . ASN B  2 7   ? -22.716 13.614  29.596  1.00 67.30 ? 4   ASN A OD1 1 
ATOM   1973 N ND2 . ASN B  2 7   ? -21.614 11.805  30.326  1.00 69.06 ? 4   ASN A ND2 1 
ATOM   1974 N N   . GLU B  2 8   ? -19.871 15.112  27.303  1.00 40.62 ? 5   GLU A N   1 
ATOM   1975 C CA  . GLU B  2 8   ? -20.224 15.426  25.922  1.00 41.32 ? 5   GLU A CA  1 
ATOM   1976 C C   . GLU B  2 8   ? -19.349 14.711  24.876  1.00 37.43 ? 5   GLU A C   1 
ATOM   1977 O O   . GLU B  2 8   ? -19.881 14.173  23.903  1.00 34.47 ? 5   GLU A O   1 
ATOM   1978 C CB  . GLU B  2 8   ? -20.182 16.946  25.787  1.00 46.22 ? 5   GLU A CB  1 
ATOM   1979 C CG  . GLU B  2 8   ? -20.407 17.457  24.365  1.00 50.14 ? 5   GLU A CG  1 
ATOM   1980 C CD  . GLU B  2 8   ? -21.126 18.777  24.281  1.00 55.45 ? 5   GLU A CD  1 
ATOM   1981 O OE1 . GLU B  2 8   ? -20.813 19.659  25.099  1.00 58.91 ? 5   GLU A OE1 1 
ATOM   1982 O OE2 . GLU B  2 8   ? -22.013 18.894  23.414  1.00 62.03 ? 5   GLU A OE2 1 
ATOM   1983 N N   . LEU B  2 9   ? -18.026 14.841  25.006  1.00 35.47 ? 6   LEU A N   1 
ATOM   1984 C CA  . LEU B  2 9   ? -17.070 14.122  24.171  1.00 33.14 ? 6   LEU A CA  1 
ATOM   1985 C C   . LEU B  2 9   ? -17.322 12.617  24.145  1.00 30.60 ? 6   LEU A C   1 
ATOM   1986 O O   . LEU B  2 9   ? -17.217 12.002  23.087  1.00 27.14 ? 6   LEU A O   1 
ATOM   1987 C CB  . LEU B  2 9   ? -15.644 14.445  24.613  1.00 33.69 ? 6   LEU A CB  1 
ATOM   1988 C CG  . LEU B  2 9   ? -15.156 15.844  24.205  1.00 36.16 ? 6   LEU A CG  1 
ATOM   1989 C CD1 . LEU B  2 9   ? -13.868 16.184  24.972  1.00 36.18 ? 6   LEU A CD1 1 
ATOM   1990 C CD2 . LEU B  2 9   ? -14.949 15.927  22.682  1.00 34.83 ? 6   LEU A CD2 1 
ATOM   1991 N N   . VAL B  2 10  ? -17.607 12.027  25.313  1.00 31.53 ? 7   VAL A N   1 
ATOM   1992 C CA  . VAL B  2 10  ? -17.891 10.600  25.431  1.00 30.83 ? 7   VAL A CA  1 
ATOM   1993 C C   . VAL B  2 10  ? -19.171 10.250  24.657  1.00 31.88 ? 7   VAL A C   1 
ATOM   1994 O O   . VAL B  2 10  ? -19.159 9.249   23.942  1.00 30.60 ? 7   VAL A O   1 
ATOM   1995 C CB  . VAL B  2 10  ? -17.895 10.128  26.909  1.00 29.84 ? 7   VAL A CB  1 
ATOM   1996 C CG1 . VAL B  2 10  ? -18.518 8.750   27.112  1.00 28.84 ? 7   VAL A CG1 1 
ATOM   1997 C CG2 . VAL B  2 10  ? -16.460 10.160  27.453  1.00 30.52 ? 7   VAL A CG2 1 
ATOM   1998 N N   . GLN B  2 11  ? -20.240 11.047  24.811  1.00 33.40 ? 8   GLN A N   1 
ATOM   1999 C CA  . GLN B  2 11  ? -21.475 10.846  24.059  1.00 35.25 ? 8   GLN A CA  1 
ATOM   2000 C C   . GLN B  2 11  ? -21.214 10.971  22.550  1.00 33.21 ? 8   GLN A C   1 
ATOM   2001 O O   . GLN B  2 11  ? -21.729 10.131  21.803  1.00 31.04 ? 8   GLN A O   1 
ATOM   2002 C CB  . GLN B  2 11  ? -22.617 11.733  24.573  1.00 39.18 ? 8   GLN A CB  1 
ATOM   2003 C CG  . GLN B  2 11  ? -23.041 11.445  26.017  1.00 43.55 ? 8   GLN A CG  1 
ATOM   2004 C CD  . GLN B  2 11  ? -23.467 10.013  26.260  1.00 47.91 ? 8   GLN A CD  1 
ATOM   2005 O OE1 . GLN B  2 11  ? -24.512 9.577   25.762  1.00 54.33 ? 8   GLN A OE1 1 
ATOM   2006 N NE2 . GLN B  2 11  ? -22.642 9.249   26.966  1.00 47.60 ? 8   GLN A NE2 1 
ATOM   2007 N N   . LYS B  2 12  ? -20.370 11.937  22.113  1.00 31.91 ? 9   LYS A N   1 
ATOM   2008 C CA  . LYS B  2 12  ? -20.006 12.066  20.704  1.00 31.63 ? 9   LYS A CA  1 
ATOM   2009 C C   . LYS B  2 12  ? -19.220 10.840  20.222  1.00 28.09 ? 9   LYS A C   1 
ATOM   2010 O O   . LYS B  2 12  ? -19.431 10.367  19.122  1.00 25.22 ? 9   LYS A O   1 
ATOM   2011 C CB  . LYS B  2 12  ? -19.252 13.373  20.452  1.00 34.67 ? 9   LYS A CB  1 
ATOM   2012 C CG  . LYS B  2 12  ? -19.030 13.687  18.984  1.00 40.65 ? 9   LYS A CG  1 
ATOM   2013 C CD  . LYS B  2 12  ? -18.664 15.104  18.538  1.00 47.78 ? 9   LYS A CD  1 
ATOM   2014 C CE  . LYS B  2 12  ? -18.431 15.103  17.030  1.00 48.65 ? 9   LYS A CE  1 
ATOM   2015 N NZ  . LYS B  2 12  ? -18.524 16.432  16.436  1.00 49.37 ? 9   LYS A NZ  1 
ATOM   2016 N N   . ALA B  2 13  ? -18.315 10.320  21.059  1.00 26.06 ? 10  ALA A N   1 
ATOM   2017 C CA  . ALA B  2 13  ? -17.560 9.127   20.722  1.00 24.97 ? 10  ALA A CA  1 
ATOM   2018 C C   . ALA B  2 13  ? -18.482 7.925   20.475  1.00 24.25 ? 10  ALA A C   1 
ATOM   2019 O O   . ALA B  2 13  ? -18.231 7.179   19.545  1.00 24.28 ? 10  ALA A O   1 
ATOM   2020 C CB  . ALA B  2 13  ? -16.494 8.851   21.769  1.00 25.05 ? 10  ALA A CB  1 
ATOM   2021 N N   . LYS B  2 14  ? -19.491 7.719   21.324  1.00 25.87 ? 11  LYS A N   1 
ATOM   2022 C CA  . LYS B  2 14  ? -20.461 6.634   21.195  1.00 27.16 ? 11  LYS A CA  1 
ATOM   2023 C C   . LYS B  2 14  ? -21.285 6.760   19.900  1.00 26.49 ? 11  LYS A C   1 
ATOM   2024 O O   . LYS B  2 14  ? -21.534 5.764   19.210  1.00 25.72 ? 11  LYS A O   1 
ATOM   2025 C CB  . LYS B  2 14  ? -21.388 6.598   22.413  1.00 29.95 ? 11  LYS A CB  1 
ATOM   2026 C CG  . LYS B  2 14  ? -20.739 6.241   23.758  1.00 30.10 ? 11  LYS A CG  1 
ATOM   2027 C CD  . LYS B  2 14  ? -21.577 6.567   24.985  1.00 33.93 ? 11  LYS A CD  1 
ATOM   2028 C CE  . LYS B  2 14  ? -21.903 5.362   25.769  1.00 37.34 ? 11  LYS A CE  1 
ATOM   2029 N NZ  . LYS B  2 14  ? -22.663 5.662   26.980  1.00 40.05 ? 11  LYS A NZ  1 
ATOM   2030 N N   . LEU B  2 15  ? -21.670 7.990   19.575  1.00 26.93 ? 12  LEU A N   1 
ATOM   2031 C CA  . LEU B  2 15  ? -22.358 8.299   18.330  1.00 28.11 ? 12  LEU A CA  1 
ATOM   2032 C C   . LEU B  2 15  ? -21.501 7.973   17.106  1.00 26.76 ? 12  LEU A C   1 
ATOM   2033 O O   . LEU B  2 15  ? -21.969 7.295   16.193  1.00 27.14 ? 12  LEU A O   1 
ATOM   2034 C CB  . LEU B  2 15  ? -22.779 9.768   18.341  1.00 29.87 ? 12  LEU A CB  1 
ATOM   2035 C CG  . LEU B  2 15  ? -23.932 10.147  17.423  1.00 34.14 ? 12  LEU A CG  1 
ATOM   2036 C CD1 . LEU B  2 15  ? -25.192 9.311   17.620  1.00 34.41 ? 12  LEU A CD1 1 
ATOM   2037 C CD2 . LEU B  2 15  ? -24.241 11.613  17.703  1.00 35.77 ? 12  LEU A CD2 1 
ATOM   2038 N N   . ALA B  2 16  ? -20.243 8.423   17.131  1.00 25.09 ? 13  ALA A N   1 
ATOM   2039 C CA  . ALA B  2 16  ? -19.260 8.113   16.107  1.00 24.16 ? 13  ALA A CA  1 
ATOM   2040 C C   . ALA B  2 16  ? -19.081 6.612   15.913  1.00 23.48 ? 13  ALA A C   1 
ATOM   2041 O O   . ALA B  2 16  ? -18.986 6.136   14.769  1.00 22.25 ? 13  ALA A O   1 
ATOM   2042 C CB  . ALA B  2 16  ? -17.949 8.776   16.444  1.00 23.44 ? 13  ALA A CB  1 
ATOM   2043 N N   . GLU B  2 17  ? -19.023 5.860   17.034  1.00 22.94 ? 14  GLU A N   1 
ATOM   2044 C CA  . GLU B  2 17  ? -18.886 4.416   16.955  1.00 23.24 ? 14  GLU A CA  1 
ATOM   2045 C C   . GLU B  2 17  ? -20.053 3.791   16.181  1.00 23.48 ? 14  GLU A C   1 
ATOM   2046 O O   . GLU B  2 17  ? -19.808 2.996   15.275  1.00 21.11 ? 14  GLU A O   1 
ATOM   2047 C CB  . GLU B  2 17  ? -18.853 3.749   18.325  1.00 23.78 ? 14  GLU A CB  1 
ATOM   2048 C CG  . GLU B  2 17  ? -18.472 2.280   18.203  1.00 22.91 ? 14  GLU A CG  1 
ATOM   2049 C CD  . GLU B  2 17  ? -18.298 1.559   19.508  1.00 23.42 ? 14  GLU A CD  1 
ATOM   2050 O OE1 . GLU B  2 17  ? -18.526 2.117   20.577  1.00 22.45 ? 14  GLU A OE1 1 
ATOM   2051 O OE2 . GLU B  2 17  ? -17.825 0.411   19.366  1.00 24.91 ? 14  GLU A OE2 1 
ATOM   2052 N N   . GLN B  2 18  ? -21.269 4.198   16.510  1.00 25.84 ? 15  GLN A N   1 
ATOM   2053 C CA  . GLN B  2 18  ? -22.462 3.731   15.809  1.00 29.96 ? 15  GLN A CA  1 
ATOM   2054 C C   . GLN B  2 18  ? -22.398 4.026   14.307  1.00 28.06 ? 15  GLN A C   1 
ATOM   2055 O O   . GLN B  2 18  ? -22.753 3.156   13.507  1.00 29.30 ? 15  GLN A O   1 
ATOM   2056 C CB  . GLN B  2 18  ? -23.756 4.350   16.344  1.00 33.69 ? 15  GLN A CB  1 
ATOM   2057 C CG  . GLN B  2 18  ? -24.099 3.982   17.773  1.00 38.86 ? 15  GLN A CG  1 
ATOM   2058 C CD  . GLN B  2 18  ? -24.166 2.492   18.006  1.00 44.32 ? 15  GLN A CD  1 
ATOM   2059 O OE1 . GLN B  2 18  ? -24.637 1.704   17.170  1.00 52.54 ? 15  GLN A OE1 1 
ATOM   2060 N NE2 . GLN B  2 18  ? -23.661 2.093   19.153  1.00 47.97 ? 15  GLN A NE2 1 
ATOM   2061 N N   . ALA B  2 19  ? -21.944 5.233   13.962  1.00 27.52 ? 16  ALA A N   1 
ATOM   2062 C CA  . ALA B  2 19  ? -21.741 5.670   12.579  1.00 25.48 ? 16  ALA A CA  1 
ATOM   2063 C C   . ALA B  2 19  ? -20.535 5.064   11.858  1.00 23.19 ? 16  ALA A C   1 
ATOM   2064 O O   . ALA B  2 19  ? -20.395 5.403   10.681  1.00 24.18 ? 16  ALA A O   1 
ATOM   2065 C CB  . ALA B  2 19  ? -21.608 7.168   12.543  1.00 26.14 ? 16  ALA A CB  1 
ATOM   2066 N N   . GLU B  2 20  ? -19.625 4.368   12.561  1.00 21.71 ? 17  GLU A N   1 
ATOM   2067 C CA  A GLU B  2 20  ? -18.383 3.798   12.052  0.50 20.50 ? 17  GLU A CA  1 
ATOM   2068 C CA  B GLU B  2 20  ? -18.396 3.799   12.020  0.50 20.80 ? 17  GLU A CA  1 
ATOM   2069 C C   . GLU B  2 20  ? -17.476 4.923   11.550  1.00 20.07 ? 17  GLU A C   1 
ATOM   2070 O O   . GLU B  2 20  ? -16.834 4.790   10.522  1.00 19.31 ? 17  GLU A O   1 
ATOM   2071 C CB  A GLU B  2 20  ? -18.704 2.664   11.071  0.50 21.21 ? 17  GLU A CB  1 
ATOM   2072 C CB  B GLU B  2 20  ? -18.683 2.704   10.979  0.50 21.97 ? 17  GLU A CB  1 
ATOM   2073 C CG  A GLU B  2 20  ? -19.550 1.534   11.663  0.50 21.66 ? 17  GLU A CG  1 
ATOM   2074 C CG  B GLU B  2 20  ? -19.217 1.397   11.555  0.50 22.47 ? 17  GLU A CG  1 
ATOM   2075 C CD  A GLU B  2 20  ? -19.786 0.336   10.738  0.50 22.21 ? 17  GLU A CD  1 
ATOM   2076 C CD  B GLU B  2 20  ? -19.714 0.420   10.492  0.50 23.68 ? 17  GLU A CD  1 
ATOM   2077 O OE1 A GLU B  2 20  ? -18.810 -0.111  10.094  0.50 20.10 ? 17  GLU A OE1 1 
ATOM   2078 O OE1 B GLU B  2 20  ? -19.897 0.827   9.322   0.50 24.01 ? 17  GLU A OE1 1 
ATOM   2079 O OE2 A GLU B  2 20  ? -20.962 -0.090  10.624  0.50 22.40 ? 17  GLU A OE2 1 
ATOM   2080 O OE2 B GLU B  2 20  ? -19.943 -0.731  10.870  0.50 21.61 ? 17  GLU A OE2 1 
ATOM   2081 N N   . ARG B  2 21  ? -17.493 6.077   12.266  1.00 21.15 ? 18  ARG A N   1 
ATOM   2082 C CA  . ARG B  2 21  ? -16.670 7.246   12.003  1.00 21.55 ? 18  ARG A CA  1 
ATOM   2083 C C   . ARG B  2 21  ? -15.540 7.222   13.033  1.00 21.07 ? 18  ARG A C   1 
ATOM   2084 O O   . ARG B  2 21  ? -15.536 7.979   14.005  1.00 20.78 ? 18  ARG A O   1 
ATOM   2085 C CB  . ARG B  2 21  ? -17.566 8.493   12.007  1.00 24.06 ? 18  ARG A CB  1 
ATOM   2086 C CG  . ARG B  2 21  ? -18.324 8.561   10.670  1.00 24.54 ? 18  ARG A CG  1 
ATOM   2087 C CD  . ARG B  2 21  ? -19.128 9.766   10.549  1.00 24.89 ? 18  ARG A CD  1 
ATOM   2088 N NE  . ARG B  2 21  ? -18.308 10.970  10.522  1.00 25.50 ? 18  ARG A NE  1 
ATOM   2089 C CZ  . ARG B  2 21  ? -18.117 11.797  9.514   1.00 26.01 ? 18  ARG A CZ  1 
ATOM   2090 N NH1 . ARG B  2 21  ? -18.503 11.479  8.283   1.00 25.61 ? 18  ARG A NH1 1 
ATOM   2091 N NH2 . ARG B  2 21  ? -17.495 12.951  9.752   1.00 26.03 ? 18  ARG A NH2 1 
ATOM   2092 N N   . TYR B  2 22  ? -14.560 6.348   12.806  1.00 19.54 ? 19  TYR A N   1 
ATOM   2093 C CA  . TYR B  2 22  ? -13.528 6.019   13.769  1.00 19.55 ? 19  TYR A CA  1 
ATOM   2094 C C   . TYR B  2 22  ? -12.536 7.163   13.938  1.00 19.78 ? 19  TYR A C   1 
ATOM   2095 O O   . TYR B  2 22  ? -12.012 7.279   15.031  1.00 19.51 ? 19  TYR A O   1 
ATOM   2096 C CB  . TYR B  2 22  ? -12.815 4.686   13.458  1.00 18.35 ? 19  TYR A CB  1 
ATOM   2097 C CG  . TYR B  2 22  ? -13.835 3.537   13.498  1.00 18.68 ? 19  TYR A CG  1 
ATOM   2098 C CD1 . TYR B  2 22  ? -14.447 3.165   14.698  1.00 20.67 ? 19  TYR A CD1 1 
ATOM   2099 C CD2 . TYR B  2 22  ? -14.206 2.830   12.353  1.00 19.56 ? 19  TYR A CD2 1 
ATOM   2100 C CE1 . TYR B  2 22  ? -15.400 2.157   14.766  1.00 21.25 ? 19  TYR A CE1 1 
ATOM   2101 C CE2 . TYR B  2 22  ? -15.127 1.779   12.405  1.00 21.70 ? 19  TYR A CE2 1 
ATOM   2102 C CZ  . TYR B  2 22  ? -15.704 1.434   13.618  1.00 23.52 ? 19  TYR A CZ  1 
ATOM   2103 O OH  . TYR B  2 22  ? -16.597 0.445   13.737  1.00 26.76 ? 19  TYR A OH  1 
ATOM   2104 N N   . ASP B  2 23  ? -12.262 7.994   12.897  1.00 20.12 ? 20  ASP A N   1 
ATOM   2105 C CA  . ASP B  2 23  ? -11.416 9.165   13.100  1.00 21.71 ? 20  ASP A CA  1 
ATOM   2106 C C   . ASP B  2 23  ? -12.059 10.137  14.087  1.00 21.33 ? 20  ASP A C   1 
ATOM   2107 O O   . ASP B  2 23  ? -11.398 10.597  15.014  1.00 21.01 ? 20  ASP A O   1 
ATOM   2108 C CB  . ASP B  2 23  ? -11.101 9.877   11.794  1.00 23.48 ? 20  ASP A CB  1 
ATOM   2109 C CG  . ASP B  2 23  ? -10.238 9.089   10.832  1.00 24.18 ? 20  ASP A CG  1 
ATOM   2110 O OD1 . ASP B  2 23  ? -9.495  8.220   11.238  1.00 23.35 ? 20  ASP A OD1 1 
ATOM   2111 O OD2 . ASP B  2 23  ? -10.255 9.385   9.663   1.00 28.08 ? 20  ASP A OD2 1 
ATOM   2112 N N   . ASP B  2 24  ? -13.358 10.379  13.922  1.00 21.26 ? 21  ASP A N   1 
ATOM   2113 C CA  . ASP B  2 24  ? -14.126 11.195  14.849  1.00 21.41 ? 21  ASP A CA  1 
ATOM   2114 C C   . ASP B  2 24  ? -14.084 10.607  16.260  1.00 21.22 ? 21  ASP A C   1 
ATOM   2115 O O   . ASP B  2 24  ? -13.873 11.345  17.219  1.00 22.30 ? 21  ASP A O   1 
ATOM   2116 C CB  . ASP B  2 24  ? -15.557 11.407  14.397  1.00 22.80 ? 21  ASP A CB  1 
ATOM   2117 C CG  . ASP B  2 24  ? -15.772 12.266  13.162  1.00 24.17 ? 21  ASP A CG  1 
ATOM   2118 O OD1 . ASP B  2 24  ? -14.802 12.869  12.677  1.00 24.25 ? 21  ASP A OD1 1 
ATOM   2119 O OD2 . ASP B  2 24  ? -16.902 12.305  12.701  1.00 25.87 ? 21  ASP A OD2 1 
ATOM   2120 N N   . MET B  2 25  ? -14.292 9.296   16.368  1.00 20.78 ? 22  MET A N   1 
ATOM   2121 C CA  . MET B  2 25  ? -14.297 8.610   17.654  1.00 22.20 ? 22  MET A CA  1 
ATOM   2122 C C   . MET B  2 25  ? -12.953 8.761   18.356  1.00 20.33 ? 22  MET A C   1 
ATOM   2123 O O   . MET B  2 25  ? -12.946 9.030   19.544  1.00 22.40 ? 22  MET A O   1 
ATOM   2124 C CB  . MET B  2 25  ? -14.612 7.128   17.454  1.00 21.25 ? 22  MET A CB  1 
ATOM   2125 C CG  . MET B  2 25  ? -14.976 6.357   18.675  1.00 20.96 ? 22  MET A CG  1 
ATOM   2126 S SD  . MET B  2 25  ? -15.171 4.617   18.196  1.00 20.37 ? 22  MET A SD  1 
ATOM   2127 C CE  . MET B  2 25  ? -15.568 4.114   19.891  1.00 22.08 ? 22  MET A CE  1 
ATOM   2128 N N   . ALA B  2 26  ? -11.848 8.595   17.630  1.00 20.36 ? 23  ALA A N   1 
ATOM   2129 C CA  . ALA B  2 26  ? -10.499 8.660   18.155  1.00 19.48 ? 23  ALA A CA  1 
ATOM   2130 C C   . ALA B  2 26  ? -10.155 10.081  18.576  1.00 21.01 ? 23  ALA A C   1 
ATOM   2131 O O   . ALA B  2 26  ? -9.578  10.241  19.643  1.00 21.64 ? 23  ALA A O   1 
ATOM   2132 C CB  . ALA B  2 26  ? -9.500  8.158   17.131  1.00 18.04 ? 23  ALA A CB  1 
ATOM   2133 N N   . ALA B  2 27  ? -10.571 11.104  17.797  1.00 22.90 ? 24  ALA A N   1 
ATOM   2134 C CA  . ALA B  2 27  ? -10.394 12.514  18.150  1.00 24.05 ? 24  ALA A CA  1 
ATOM   2135 C C   . ALA B  2 27  ? -11.084 12.814  19.473  1.00 24.10 ? 24  ALA A C   1 
ATOM   2136 O O   . ALA B  2 27  ? -10.457 13.433  20.348  1.00 24.65 ? 24  ALA A O   1 
ATOM   2137 C CB  . ALA B  2 27  ? -10.822 13.465  17.039  1.00 24.38 ? 24  ALA A CB  1 
ATOM   2138 N N   . CYS B  2 28  ? -12.329 12.315  19.648  1.00 24.18 ? 25  CYS A N   1 
ATOM   2139 C CA  . CYS B  2 28  ? -13.064 12.519  20.890  1.00 25.23 ? 25  CYS A CA  1 
ATOM   2140 C C   . CYS B  2 28  ? -12.310 11.934  22.107  1.00 23.59 ? 25  CYS A C   1 
ATOM   2141 O O   . CYS B  2 28  ? -12.124 12.638  23.125  1.00 24.98 ? 25  CYS A O   1 
ATOM   2142 C CB  . CYS B  2 28  ? -14.476 11.910  20.827  1.00 26.94 ? 25  CYS A CB  1 
ATOM   2143 S SG  . CYS B  2 28  ? -15.603 12.815  19.742  1.00 28.07 ? 25  CYS A SG  1 
ATOM   2144 N N   . MET B  2 29  ? -11.861 10.681  21.970  1.00 21.23 ? 26  MET A N   1 
ATOM   2145 C CA  . MET B  2 29  ? -11.256 9.946   23.073  1.00 20.99 ? 26  MET A CA  1 
ATOM   2146 C C   . MET B  2 29  ? -9.848  10.440  23.365  1.00 21.76 ? 26  MET A C   1 
ATOM   2147 O O   . MET B  2 29  ? -9.496  10.456  24.529  1.00 20.60 ? 26  MET A O   1 
ATOM   2148 C CB  . MET B  2 29  ? -11.350 8.438   22.850  1.00 19.34 ? 26  MET A CB  1 
ATOM   2149 C CG  . MET B  2 29  ? -12.784 7.906   22.905  1.00 20.06 ? 26  MET A CG  1 
ATOM   2150 S SD  . MET B  2 29  ? -13.828 8.534   24.228  1.00 22.69 ? 26  MET A SD  1 
ATOM   2151 C CE  . MET B  2 29  ? -12.929 8.008   25.700  1.00 23.64 ? 26  MET A CE  1 
ATOM   2152 N N   . LYS B  2 30  ? -9.096  10.877  22.342  1.00 22.80 ? 27  LYS A N   1 
ATOM   2153 C CA  . LYS B  2 30  ? -7.852  11.622  22.560  1.00 24.54 ? 27  LYS A CA  1 
ATOM   2154 C C   . LYS B  2 30  ? -8.064  12.876  23.412  1.00 24.44 ? 27  LYS A C   1 
ATOM   2155 O O   . LYS B  2 30  ? -7.373  13.084  24.411  1.00 23.43 ? 27  LYS A O   1 
ATOM   2156 C CB  . LYS B  2 30  ? -7.202  11.919  21.196  1.00 25.37 ? 27  LYS A CB  1 
ATOM   2157 C CG  . LYS B  2 30  ? -5.848  12.716  21.232  1.00 25.67 ? 27  LYS A CG  1 
ATOM   2158 C CD  . LYS B  2 30  ? -5.263  12.848  19.823  1.00 26.00 ? 27  LYS A CD  1 
ATOM   2159 C CE  . LYS B  2 30  ? -3.827  13.209  19.662  1.00 28.06 ? 27  LYS A CE  1 
ATOM   2160 N NZ  . LYS B  2 30  ? -3.647  14.621  19.901  1.00 31.92 ? 27  LYS A NZ  1 
ATOM   2161 N N   . SER B  2 31  ? -9.084  13.684  23.072  1.00 25.18 ? 28  SER A N   1 
ATOM   2162 C CA  . SER B  2 31  ? -9.415  14.871  23.823  1.00 26.43 ? 28  SER A CA  1 
ATOM   2163 C C   . SER B  2 31  ? -9.783  14.564  25.275  1.00 27.21 ? 28  SER A C   1 
ATOM   2164 O O   . SER B  2 31  ? -9.249  15.214  26.175  1.00 26.21 ? 28  SER A O   1 
ATOM   2165 C CB  . SER B  2 31  ? -10.491 15.689  23.138  1.00 28.44 ? 28  SER A CB  1 
ATOM   2166 O OG  . SER B  2 31  ? -9.908  16.221  21.959  1.00 31.74 ? 28  SER A OG  1 
ATOM   2167 N N   . VAL B  2 32  ? -10.616 13.533  25.495  1.00 26.26 ? 29  VAL A N   1 
ATOM   2168 C CA  . VAL B  2 32  ? -10.971 13.063  26.834  1.00 27.17 ? 29  VAL A CA  1 
ATOM   2169 C C   . VAL B  2 32  ? -9.702  12.715  27.624  1.00 26.95 ? 29  VAL A C   1 
ATOM   2170 O O   . VAL B  2 32  ? -9.483  13.267  28.725  1.00 30.53 ? 29  VAL A O   1 
ATOM   2171 C CB  . VAL B  2 32  ? -11.961 11.872  26.808  1.00 26.83 ? 29  VAL A CB  1 
ATOM   2172 C CG1 . VAL B  2 32  ? -12.173 11.230  28.190  1.00 28.46 ? 29  VAL A CG1 1 
ATOM   2173 C CG2 . VAL B  2 32  ? -13.335 12.267  26.187  1.00 27.77 ? 29  VAL A CG2 1 
ATOM   2174 N N   . THR B  2 33  ? -8.848  11.872  27.039  1.00 24.59 ? 30  THR A N   1 
ATOM   2175 C CA  . THR B  2 33  ? -7.613  11.424  27.710  1.00 24.21 ? 30  THR A CA  1 
ATOM   2176 C C   . THR B  2 33  ? -6.752  12.632  28.134  1.00 27.36 ? 30  THR A C   1 
ATOM   2177 O O   . THR B  2 33  ? -6.329  12.700  29.298  1.00 27.61 ? 30  THR A O   1 
ATOM   2178 C CB  . THR B  2 33  ? -6.846  10.491  26.779  1.00 21.30 ? 30  THR A CB  1 
ATOM   2179 O OG1 . THR B  2 33  ? -7.692  9.371   26.434  1.00 20.37 ? 30  THR A OG1 1 
ATOM   2180 C CG2 . THR B  2 33  ? -5.531  10.048  27.406  1.00 20.65 ? 30  THR A CG2 1 
ATOM   2181 N N   . GLU B  2 34  ? -6.571  13.592  27.200  1.00 28.31 ? 31  GLU A N   1 
ATOM   2182 C CA  . GLU B  2 34  ? -5.780  14.807  27.424  1.00 30.59 ? 31  GLU A CA  1 
ATOM   2183 C C   . GLU B  2 34  ? -6.310  15.725  28.533  1.00 32.46 ? 31  GLU A C   1 
ATOM   2184 O O   . GLU B  2 34  ? -5.541  16.536  29.027  1.00 35.36 ? 31  GLU A O   1 
ATOM   2185 C CB  . GLU B  2 34  ? -5.626  15.579  26.113  1.00 30.12 ? 31  GLU A CB  1 
ATOM   2186 C CG  . GLU B  2 34  ? -4.700  14.891  25.133  1.00 29.71 ? 31  GLU A CG  1 
ATOM   2187 C CD  . GLU B  2 34  ? -4.706  15.411  23.715  1.00 29.12 ? 31  GLU A CD  1 
ATOM   2188 O OE1 . GLU B  2 34  ? -5.618  16.112  23.301  1.00 31.70 ? 31  GLU A OE1 1 
ATOM   2189 O OE2 . GLU B  2 34  ? -3.796  15.002  23.002  1.00 31.88 ? 31  GLU A OE2 1 
ATOM   2190 N N   . GLN B  2 35  ? -7.569  15.605  28.972  1.00 33.24 ? 32  GLN A N   1 
ATOM   2191 C CA  . GLN B  2 35  ? -8.034  16.325  30.152  1.00 33.56 ? 32  GLN A CA  1 
ATOM   2192 C C   . GLN B  2 35  ? -7.415  15.827  31.456  1.00 32.43 ? 32  GLN A C   1 
ATOM   2193 O O   . GLN B  2 35  ? -7.525  16.502  32.478  1.00 31.24 ? 32  GLN A O   1 
ATOM   2194 C CB  . GLN B  2 35  ? -9.533  16.239  30.350  1.00 36.89 ? 32  GLN A CB  1 
ATOM   2195 C CG  . GLN B  2 35  ? -10.303 16.853  29.198  1.00 40.37 ? 32  GLN A CG  1 
ATOM   2196 C CD  . GLN B  2 35  ? -11.791 16.879  29.465  1.00 46.12 ? 32  GLN A CD  1 
ATOM   2197 O OE1 . GLN B  2 35  ? -12.292 16.366  30.484  1.00 50.60 ? 32  GLN A OE1 1 
ATOM   2198 N NE2 . GLN B  2 35  ? -12.506 17.466  28.515  1.00 45.73 ? 32  GLN A NE2 1 
ATOM   2199 N N   . GLY B  2 36  ? -6.828  14.620  31.443  1.00 31.95 ? 33  GLY A N   1 
ATOM   2200 C CA  . GLY B  2 36  ? -5.952  14.171  32.506  1.00 33.57 ? 33  GLY A CA  1 
ATOM   2201 C C   . GLY B  2 36  ? -6.653  13.350  33.587  1.00 35.09 ? 33  GLY A C   1 
ATOM   2202 O O   . GLY B  2 36  ? -5.931  12.872  34.453  1.00 38.34 ? 33  GLY A O   1 
ATOM   2203 N N   . ALA B  2 37  ? -7.993  13.178  33.547  1.00 32.55 ? 34  ALA A N   1 
ATOM   2204 C CA  . ALA B  2 37  ? -8.701  12.323  34.497  1.00 32.03 ? 34  ALA A CA  1 
ATOM   2205 C C   . ALA B  2 37  ? -8.582  10.863  34.049  1.00 28.94 ? 34  ALA A C   1 
ATOM   2206 O O   . ALA B  2 37  ? -8.460  10.569  32.862  1.00 27.83 ? 34  ALA A O   1 
ATOM   2207 C CB  . ALA B  2 37  ? -10.164 12.786  34.662  1.00 32.60 ? 34  ALA A CB  1 
ATOM   2208 N N   . GLU B  2 38  ? -8.574  9.927   35.018  1.00 29.01 ? 35  GLU A N   1 
ATOM   2209 C CA  . GLU B  2 38  ? -8.624  8.497   34.714  1.00 29.17 ? 35  GLU A CA  1 
ATOM   2210 C C   . GLU B  2 38  ? -9.903  8.153   33.955  1.00 27.31 ? 35  GLU A C   1 
ATOM   2211 O O   . GLU B  2 38  ? -10.970 8.740   34.256  1.00 27.01 ? 35  GLU A O   1 
ATOM   2212 C CB  . GLU B  2 38  ? -8.670  7.622   35.967  1.00 32.06 ? 35  GLU A CB  1 
ATOM   2213 C CG  . GLU B  2 38  ? -7.286  7.311   36.499  1.00 32.19 ? 35  GLU A CG  1 
ATOM   2214 C CD  . GLU B  2 38  ? -7.413  6.451   37.743  1.00 33.58 ? 35  GLU A CD  1 
ATOM   2215 O OE1 . GLU B  2 38  ? -7.408  7.100   38.843  1.00 35.47 ? 35  GLU A OE1 1 
ATOM   2216 O OE2 . GLU B  2 38  ? -7.426  5.220   37.562  1.00 32.98 ? 35  GLU A OE2 1 
ATOM   2217 N N   . LEU B  2 39  ? -9.754  7.233   32.993  1.00 25.39 ? 36  LEU A N   1 
ATOM   2218 C CA  . LEU B  2 39  ? -10.871 6.736   32.222  1.00 25.52 ? 36  LEU A CA  1 
ATOM   2219 C C   . LEU B  2 39  ? -11.629 5.696   33.045  1.00 27.14 ? 36  LEU A C   1 
ATOM   2220 O O   . LEU B  2 39  ? -11.036 4.897   33.786  1.00 26.17 ? 36  LEU A O   1 
ATOM   2221 C CB  . LEU B  2 39  ? -10.384 6.184   30.885  1.00 23.52 ? 36  LEU A CB  1 
ATOM   2222 C CG  . LEU B  2 39  ? -9.545  7.133   30.018  1.00 23.18 ? 36  LEU A CG  1 
ATOM   2223 C CD1 . LEU B  2 39  ? -9.234  6.475   28.664  1.00 21.68 ? 36  LEU A CD1 1 
ATOM   2224 C CD2 . LEU B  2 39  ? -10.169 8.481   29.739  1.00 24.12 ? 36  LEU A CD2 1 
ATOM   2225 N N   . SER B  2 40  ? -12.955 5.649   32.827  1.00 27.63 ? 37  SER A N   1 
ATOM   2226 C CA  . SER B  2 40  ? -13.781 4.492   33.179  1.00 26.59 ? 37  SER A CA  1 
ATOM   2227 C C   . SER B  2 40  ? -13.521 3.312   32.248  1.00 25.80 ? 37  SER A C   1 
ATOM   2228 O O   . SER B  2 40  ? -12.895 3.460   31.174  1.00 23.36 ? 37  SER A O   1 
ATOM   2229 C CB  . SER B  2 40  ? -15.249 4.862   33.170  1.00 28.64 ? 37  SER A CB  1 
ATOM   2230 O OG  . SER B  2 40  ? -15.709 4.974   31.827  1.00 25.30 ? 37  SER A OG  1 
ATOM   2231 N N   . ASN B  2 41  ? -14.084 2.135   32.626  1.00 25.48 ? 38  ASN A N   1 
ATOM   2232 C CA  . ASN B  2 41  ? -14.041 0.956   31.755  1.00 25.89 ? 38  ASN A CA  1 
ATOM   2233 C C   . ASN B  2 41  ? -14.656 1.216   30.378  1.00 23.99 ? 38  ASN A C   1 
ATOM   2234 O O   . ASN B  2 41  ? -14.053 0.835   29.360  1.00 22.93 ? 38  ASN A O   1 
ATOM   2235 C CB  . ASN B  2 41  ? -14.702 -0.251  32.422  1.00 28.58 ? 38  ASN A CB  1 
ATOM   2236 C CG  . ASN B  2 41  ? -13.877 -0.830  33.555  1.00 33.80 ? 38  ASN A CG  1 
ATOM   2237 O OD1 . ASN B  2 41  ? -12.794 -0.332  33.895  1.00 34.69 ? 38  ASN A OD1 1 
ATOM   2238 N ND2 . ASN B  2 41  ? -14.368 -1.903  34.148  1.00 36.58 ? 38  ASN A ND2 1 
ATOM   2239 N N   . GLU B  2 42  ? -15.833 1.861   30.363  1.00 25.00 ? 39  GLU A N   1 
ATOM   2240 C CA  A GLU B  2 42  ? -16.487 2.193   29.109  0.50 24.75 ? 39  GLU A CA  1 
ATOM   2241 C CA  B GLU B  2 42  ? -16.510 2.245   29.132  0.50 24.29 ? 39  GLU A CA  1 
ATOM   2242 C C   . GLU B  2 42  ? -15.606 3.093   28.234  1.00 23.50 ? 39  GLU A C   1 
ATOM   2243 O O   . GLU B  2 42  ? -15.503 2.827   27.025  1.00 21.41 ? 39  GLU A O   1 
ATOM   2244 C CB  A GLU B  2 42  ? -17.864 2.797   29.335  0.50 27.45 ? 39  GLU A CB  1 
ATOM   2245 C CB  B GLU B  2 42  ? -17.750 2.993   29.601  0.50 26.35 ? 39  GLU A CB  1 
ATOM   2246 C CG  A GLU B  2 42  ? -18.692 2.694   28.063  0.50 29.59 ? 39  GLU A CG  1 
ATOM   2247 C CG  B GLU B  2 42  ? -18.593 3.646   28.511  0.50 27.68 ? 39  GLU A CG  1 
ATOM   2248 C CD  A GLU B  2 42  ? -20.055 3.334   28.060  0.50 32.37 ? 39  GLU A CD  1 
ATOM   2249 C CD  B GLU B  2 42  ? -19.918 4.050   29.118  0.50 29.35 ? 39  GLU A CD  1 
ATOM   2250 O OE1 A GLU B  2 42  ? -20.106 4.513   28.458  0.50 35.10 ? 39  GLU A OE1 1 
ATOM   2251 O OE1 B GLU B  2 42  ? -20.655 3.103   29.515  0.50 29.72 ? 39  GLU A OE1 1 
ATOM   2252 O OE2 A GLU B  2 42  ? -20.988 2.701   27.512  0.50 34.37 ? 39  GLU A OE2 1 
ATOM   2253 O OE2 B GLU B  2 42  ? -20.165 5.282   29.258  0.50 30.77 ? 39  GLU A OE2 1 
ATOM   2254 N N   . GLU B  2 43  ? -14.997 4.122   28.837  1.00 23.29 ? 40  GLU A N   1 
ATOM   2255 C CA  . GLU B  2 43  ? -14.137 5.050   28.121  1.00 24.08 ? 40  GLU A CA  1 
ATOM   2256 C C   . GLU B  2 43  ? -12.884 4.370   27.574  1.00 21.38 ? 40  GLU A C   1 
ATOM   2257 O O   . GLU B  2 43  ? -12.508 4.668   26.442  1.00 19.51 ? 40  GLU A O   1 
ATOM   2258 C CB  . GLU B  2 43  ? -13.799 6.226   29.024  1.00 24.78 ? 40  GLU A CB  1 
ATOM   2259 C CG  . GLU B  2 43  ? -14.983 7.144   29.338  1.00 26.88 ? 40  GLU A CG  1 
ATOM   2260 C CD  . GLU B  2 43  ? -14.901 7.930   30.631  1.00 31.51 ? 40  GLU A CD  1 
ATOM   2261 O OE1 . GLU B  2 43  ? -13.800 7.931   31.275  1.00 30.74 ? 40  GLU A OE1 1 
ATOM   2262 O OE2 . GLU B  2 43  ? -15.920 8.618   30.971  1.00 33.86 ? 40  GLU A OE2 1 
ATOM   2263 N N   . ARG B  2 44  ? -12.244 3.487   28.358  1.00 20.78 ? 41  ARG A N   1 
ATOM   2264 C CA  . ARG B  2 44  ? -11.168 2.654   27.853  1.00 21.10 ? 41  ARG A CA  1 
ATOM   2265 C C   . ARG B  2 44  ? -11.588 1.888   26.607  1.00 20.83 ? 41  ARG A C   1 
ATOM   2266 O O   . ARG B  2 44  ? -10.837 1.908   25.627  1.00 18.63 ? 41  ARG A O   1 
ATOM   2267 C CB  . ARG B  2 44  ? -10.591 1.555   28.773  1.00 24.15 ? 41  ARG A CB  1 
ATOM   2268 C CG  . ARG B  2 44  ? -9.526  2.158   29.656  1.00 23.97 ? 41  ARG A CG  1 
ATOM   2269 C CD  . ARG B  2 44  ? -8.976  1.166   30.689  1.00 24.48 ? 41  ARG A CD  1 
ATOM   2270 N NE  . ARG B  2 44  ? -9.882  0.999   31.837  1.00 25.56 ? 41  ARG A NE  1 
ATOM   2271 C CZ  . ARG B  2 44  ? -10.050 1.839   32.829  1.00 27.61 ? 41  ARG A CZ  1 
ATOM   2272 N NH1 . ARG B  2 44  ? -9.307  2.962   32.927  1.00 27.07 ? 41  ARG A NH1 1 
ATOM   2273 N NH2 . ARG B  2 44  ? -10.936 1.543   33.777  1.00 30.70 ? 41  ARG A NH2 1 
ATOM   2274 N N   . ASN B  2 45  ? -12.773 1.239   26.676  1.00 20.40 ? 42  ASN A N   1 
ATOM   2275 C CA  . ASN B  2 45  ? -13.272 0.495   25.535  1.00 19.38 ? 42  ASN A CA  1 
ATOM   2276 C C   . ASN B  2 45  ? -13.423 1.405   24.306  1.00 18.51 ? 42  ASN A C   1 
ATOM   2277 O O   . ASN B  2 45  ? -13.099 0.958   23.228  1.00 19.29 ? 42  ASN A O   1 
ATOM   2278 C CB  . ASN B  2 45  ? -14.524 -0.304  25.847  1.00 20.99 ? 42  ASN A CB  1 
ATOM   2279 C CG  . ASN B  2 45  ? -14.246 -1.543  26.676  1.00 24.16 ? 42  ASN A CG  1 
ATOM   2280 O OD1 . ASN B  2 45  ? -13.122 -2.084  26.703  1.00 27.17 ? 42  ASN A OD1 1 
ATOM   2281 N ND2 . ASN B  2 45  ? -15.287 -2.020  27.335  1.00 25.54 ? 42  ASN A ND2 1 
ATOM   2282 N N   . LEU B  2 46  ? -13.938 2.635   24.487  1.00 18.66 ? 43  LEU A N   1 
ATOM   2283 C CA  . LEU B  2 46  ? -14.127 3.590   23.396  1.00 18.24 ? 43  LEU A CA  1 
ATOM   2284 C C   . LEU B  2 46  ? -12.775 3.983   22.785  1.00 17.90 ? 43  LEU A C   1 
ATOM   2285 O O   . LEU B  2 46  ? -12.626 3.965   21.559  1.00 17.41 ? 43  LEU A O   1 
ATOM   2286 C CB  . LEU B  2 46  ? -14.890 4.798   23.918  1.00 19.13 ? 43  LEU A CB  1 
ATOM   2287 C CG  . LEU B  2 46  ? -16.353 4.568   24.318  1.00 20.20 ? 43  LEU A CG  1 
ATOM   2288 C CD1 . LEU B  2 46  ? -16.887 5.794   25.009  1.00 22.25 ? 43  LEU A CD1 1 
ATOM   2289 C CD2 . LEU B  2 46  ? -17.268 4.155   23.155  1.00 20.64 ? 43  LEU A CD2 1 
ATOM   2290 N N   . LEU B  2 47  ? -11.796 4.333   23.644  1.00 17.77 ? 44  LEU A N   1 
ATOM   2291 C CA  . LEU B  2 47  ? -10.439 4.602   23.188  1.00 17.90 ? 44  LEU A CA  1 
ATOM   2292 C C   . LEU B  2 47  ? -9.862  3.446   22.375  1.00 16.62 ? 44  LEU A C   1 
ATOM   2293 O O   . LEU B  2 47  ? -9.311  3.648   21.297  1.00 15.47 ? 44  LEU A O   1 
ATOM   2294 C CB  . LEU B  2 47  ? -9.543  4.925   24.381  1.00 18.87 ? 44  LEU A CB  1 
ATOM   2295 C CG  . LEU B  2 47  ? -8.104  5.303   24.034  1.00 19.18 ? 44  LEU A CG  1 
ATOM   2296 C CD1 . LEU B  2 47  ? -8.059  6.662   23.379  1.00 21.40 ? 44  LEU A CD1 1 
ATOM   2297 C CD2 . LEU B  2 47  ? -7.196  5.237   25.235  1.00 23.21 ? 44  LEU A CD2 1 
ATOM   2298 N N   . SER B  2 48  ? -9.976  2.238   22.916  1.00 18.04 ? 45  SER A N   1 
ATOM   2299 C CA  . SER B  2 48  ? -9.381  1.057   22.346  1.00 18.14 ? 45  SER A CA  1 
ATOM   2300 C C   . SER B  2 48  ? -10.031 0.738   20.992  1.00 18.28 ? 45  SER A C   1 
ATOM   2301 O O   . SER B  2 48  ? -9.321  0.485   20.036  1.00 19.03 ? 45  SER A O   1 
ATOM   2302 C CB  . SER B  2 48  ? -9.511  -0.092  23.336  1.00 20.03 ? 45  SER A CB  1 
ATOM   2303 O OG  . SER B  2 48  ? -9.001  -1.317  22.850  1.00 20.56 ? 45  SER A OG  1 
ATOM   2304 N N   . VAL B  2 49  ? -11.372 0.781   20.930  1.00 17.85 ? 46  VAL A N   1 
ATOM   2305 C CA  . VAL B  2 49  ? -12.096 0.540   19.678  1.00 16.68 ? 46  VAL A CA  1 
ATOM   2306 C C   . VAL B  2 49  ? -11.676 1.562   18.614  1.00 15.89 ? 46  VAL A C   1 
ATOM   2307 O O   . VAL B  2 49  ? -11.509 1.200   17.443  1.00 14.92 ? 46  VAL A O   1 
ATOM   2308 C CB  . VAL B  2 49  ? -13.614 0.503   19.930  1.00 17.48 ? 46  VAL A CB  1 
ATOM   2309 C CG1 . VAL B  2 49  ? -14.419 0.650   18.657  1.00 18.64 ? 46  VAL A CG1 1 
ATOM   2310 C CG2 . VAL B  2 49  ? -13.989 -0.801  20.685  1.00 18.85 ? 46  VAL A CG2 1 
ATOM   2311 N N   . ALA B  2 50  ? -11.649 2.842   18.994  1.00 17.22 ? 47  ALA A N   1 
ATOM   2312 C CA  . ALA B  2 50  ? -11.397 3.932   18.056  1.00 16.45 ? 47  ALA A CA  1 
ATOM   2313 C C   . ALA B  2 50  ? -10.043 3.690   17.383  1.00 15.99 ? 47  ALA A C   1 
ATOM   2314 O O   . ALA B  2 50  ? -9.958  3.561   16.155  1.00 16.71 ? 47  ALA A O   1 
ATOM   2315 C CB  . ALA B  2 50  ? -11.482 5.246   18.745  1.00 16.83 ? 47  ALA A CB  1 
ATOM   2316 N N   . TYR B  2 51  ? -8.973  3.569   18.157  1.00 16.54 ? 48  TYR A N   1 
ATOM   2317 C CA  . TYR B  2 51  ? -7.624  3.388   17.597  1.00 15.66 ? 48  TYR A CA  1 
ATOM   2318 C C   . TYR B  2 51  ? -7.430  2.025   16.906  1.00 16.21 ? 48  TYR A C   1 
ATOM   2319 O O   . TYR B  2 51  ? -6.674  1.993   15.918  1.00 16.91 ? 48  TYR A O   1 
ATOM   2320 C CB  . TYR B  2 51  ? -6.601  3.764   18.665  1.00 16.39 ? 48  TYR A CB  1 
ATOM   2321 C CG  . TYR B  2 51  ? -6.420  5.270   18.778  1.00 17.41 ? 48  TYR A CG  1 
ATOM   2322 C CD1 . TYR B  2 51  ? -5.737  5.964   17.776  1.00 17.69 ? 48  TYR A CD1 1 
ATOM   2323 C CD2 . TYR B  2 51  ? -6.883  6.008   19.864  1.00 18.24 ? 48  TYR A CD2 1 
ATOM   2324 C CE1 . TYR B  2 51  ? -5.475  7.330   17.870  1.00 19.02 ? 48  TYR A CE1 1 
ATOM   2325 C CE2 . TYR B  2 51  ? -6.646  7.387   19.961  1.00 19.40 ? 48  TYR A CE2 1 
ATOM   2326 C CZ  . TYR B  2 51  ? -5.981  8.062   18.942  1.00 19.31 ? 48  TYR A CZ  1 
ATOM   2327 O OH  . TYR B  2 51  ? -5.704  9.391   19.043  1.00 20.23 ? 48  TYR A OH  1 
ATOM   2328 N N   . LYS B  2 52  ? -8.097  0.934   17.358  1.00 15.43 ? 49  LYS A N   1 
ATOM   2329 C CA  A LYS B  2 52  ? -8.016  -0.356  16.685  0.33 16.38 ? 49  LYS A CA  1 
ATOM   2330 C CA  B LYS B  2 52  ? -7.968  -0.341  16.672  0.33 16.27 ? 49  LYS A CA  1 
ATOM   2331 C CA  C LYS B  2 52  ? -8.103  -0.387  16.700  0.33 16.11 ? 49  LYS A CA  1 
ATOM   2332 C C   . LYS B  2 52  ? -8.466  -0.201  15.231  1.00 15.67 ? 49  LYS A C   1 
ATOM   2333 O O   . LYS B  2 52  ? -7.810  -0.734  14.320  1.00 15.70 ? 49  LYS A O   1 
ATOM   2334 C CB  A LYS B  2 52  ? -8.855  -1.407  17.430  0.33 16.63 ? 49  LYS A CB  1 
ATOM   2335 C CB  B LYS B  2 52  ? -8.596  -1.528  17.408  0.33 16.26 ? 49  LYS A CB  1 
ATOM   2336 C CB  C LYS B  2 52  ? -9.118  -1.443  17.210  0.33 16.02 ? 49  LYS A CB  1 
ATOM   2337 C CG  A LYS B  2 52  ? -9.062  -2.838  16.886  0.33 17.75 ? 49  LYS A CG  1 
ATOM   2338 C CG  B LYS B  2 52  ? -7.960  -2.836  16.991  0.33 16.78 ? 49  LYS A CG  1 
ATOM   2339 C CG  C LYS B  2 52  ? -9.258  -2.891  16.537  0.33 17.01 ? 49  LYS A CG  1 
ATOM   2340 C CD  A LYS B  2 52  ? -7.996  -3.870  17.231  0.33 17.53 ? 49  LYS A CD  1 
ATOM   2341 C CD  B LYS B  2 52  ? -8.355  -4.109  17.746  0.33 18.21 ? 49  LYS A CD  1 
ATOM   2342 C CD  C LYS B  2 52  ? -10.641 -3.565  16.581  0.33 17.46 ? 49  LYS A CD  1 
ATOM   2343 C CE  A LYS B  2 52  ? -8.280  -5.223  16.617  0.33 16.45 ? 49  LYS A CE  1 
ATOM   2344 C CE  B LYS B  2 52  ? -7.487  -5.232  17.228  0.33 18.12 ? 49  LYS A CE  1 
ATOM   2345 C CE  C LYS B  2 52  ? -10.801 -5.114  16.486  0.33 18.06 ? 49  LYS A CE  1 
ATOM   2346 N NZ  A LYS B  2 52  ? -8.913  -6.251  17.442  0.33 15.68 ? 49  LYS A NZ  1 
ATOM   2347 N NZ  B LYS B  2 52  ? -6.181  -4.654  16.862  0.33 17.59 ? 49  LYS A NZ  1 
ATOM   2348 N NZ  C LYS B  2 52  ? -12.178 -5.691  16.607  0.33 19.08 ? 49  LYS A NZ  1 
ATOM   2349 N N   . ASN B  2 53  ? -9.576  0.504   15.036  1.00 15.84 ? 50  ASN A N   1 
ATOM   2350 C CA  . ASN B  2 53  ? -10.136 0.689   13.708  1.00 16.52 ? 50  ASN A CA  1 
ATOM   2351 C C   . ASN B  2 53  ? -9.268  1.657   12.897  1.00 16.08 ? 50  ASN A C   1 
ATOM   2352 O O   . ASN B  2 53  ? -9.119  1.464   11.690  1.00 16.01 ? 50  ASN A O   1 
ATOM   2353 C CB  . ASN B  2 53  ? -11.599 1.092   13.819  1.00 16.82 ? 50  ASN A CB  1 
ATOM   2354 C CG  . ASN B  2 53  ? -12.473 -0.110  14.130  1.00 19.41 ? 50  ASN A CG  1 
ATOM   2355 O OD1 . ASN B  2 53  ? -12.750 -0.890  13.214  1.00 21.32 ? 50  ASN A OD1 1 
ATOM   2356 N ND2 . ASN B  2 53  ? -12.848 -0.346  15.370  1.00 19.74 ? 50  ASN A ND2 1 
ATOM   2357 N N   . VAL B  2 54  ? -8.797  2.764   13.513  1.00 15.65 ? 51  VAL A N   1 
ATOM   2358 C CA  . VAL B  2 54  ? -7.984  3.749   12.789  1.00 16.37 ? 51  VAL A CA  1 
ATOM   2359 C C   . VAL B  2 54  ? -6.681  3.073   12.312  1.00 16.00 ? 51  VAL A C   1 
ATOM   2360 O O   . VAL B  2 54  ? -6.329  3.144   11.128  1.00 17.45 ? 51  VAL A O   1 
ATOM   2361 C CB  . VAL B  2 54  ? -7.764  5.043   13.626  1.00 15.58 ? 51  VAL A CB  1 
ATOM   2362 C CG1 . VAL B  2 54  ? -6.719  5.997   13.043  1.00 17.22 ? 51  VAL A CG1 1 
ATOM   2363 C CG2 . VAL B  2 54  ? -9.063  5.803   13.826  1.00 16.72 ? 51  VAL A CG2 1 
ATOM   2364 N N   . VAL B  2 55  ? -5.954  2.393   13.203  1.00 15.14 ? 52  VAL A N   1 
ATOM   2365 C CA  . VAL B  2 55  ? -4.722  1.724   12.822  1.00 14.53 ? 52  VAL A CA  1 
ATOM   2366 C C   . VAL B  2 55  ? -5.016  0.527   11.899  1.00 14.82 ? 52  VAL A C   1 
ATOM   2367 O O   . VAL B  2 55  ? -4.187  0.225   11.008  1.00 14.64 ? 52  VAL A O   1 
ATOM   2368 C CB  . VAL B  2 55  ? -3.827  1.314   14.021  1.00 15.18 ? 52  VAL A CB  1 
ATOM   2369 C CG1 . VAL B  2 55  ? -4.268  0.041   14.722  1.00 14.65 ? 52  VAL A CG1 1 
ATOM   2370 C CG2 . VAL B  2 55  ? -2.343  1.195   13.584  1.00 15.79 ? 52  VAL A CG2 1 
ATOM   2371 N N   . GLY B  2 56  ? -6.142  -0.173  12.143  1.00 13.69 ? 53  GLY A N   1 
ATOM   2372 C CA  . GLY B  2 56  ? -6.469  -1.376  11.405  1.00 15.15 ? 53  GLY A CA  1 
ATOM   2373 C C   . GLY B  2 56  ? -6.605  -1.143  9.894   1.00 15.95 ? 53  GLY A C   1 
ATOM   2374 O O   . GLY B  2 56  ? -6.203  -2.004  9.079   1.00 17.42 ? 53  GLY A O   1 
ATOM   2375 N N   . ALA B  2 57  ? -7.212  0.010   9.535   1.00 16.63 ? 54  ALA A N   1 
ATOM   2376 C CA  . ALA B  2 57  ? -7.337  0.366   8.116   1.00 17.97 ? 54  ALA A CA  1 
ATOM   2377 C C   . ALA B  2 57  ? -5.961  0.423   7.417   1.00 18.63 ? 54  ALA A C   1 
ATOM   2378 O O   . ALA B  2 57  ? -5.797  -0.061  6.297   1.00 18.44 ? 54  ALA A O   1 
ATOM   2379 C CB  . ALA B  2 57  ? -8.106  1.651   7.983   1.00 18.82 ? 54  ALA A CB  1 
ATOM   2380 N N   . ARG B  2 58  ? -4.960  0.943   8.136   1.00 16.36 ? 55  ARG A N   1 
ATOM   2381 C CA  . ARG B  2 58  ? -3.593  1.035   7.653   1.00 15.35 ? 55  ARG A CA  1 
ATOM   2382 C C   . ARG B  2 58  ? -2.884  -0.308  7.643   1.00 14.73 ? 55  ARG A C   1 
ATOM   2383 O O   . ARG B  2 58  ? -2.168  -0.615  6.690   1.00 15.47 ? 55  ARG A O   1 
ATOM   2384 C CB  . ARG B  2 58  ? -2.767  2.103   8.367   1.00 15.61 ? 55  ARG A CB  1 
ATOM   2385 C CG  . ARG B  2 58  ? -3.005  3.542   7.948   1.00 16.40 ? 55  ARG A CG  1 
ATOM   2386 C CD  . ARG B  2 58  ? -4.352  3.994   8.375   1.00 16.64 ? 55  ARG A CD  1 
ATOM   2387 N NE  . ARG B  2 58  ? -4.599  5.413   8.113   1.00 17.80 ? 55  ARG A NE  1 
ATOM   2388 C CZ  . ARG B  2 58  ? -5.767  5.954   8.348   1.00 18.49 ? 55  ARG A CZ  1 
ATOM   2389 N NH1 . ARG B  2 58  ? -6.609  5.397   9.214   1.00 19.14 ? 55  ARG A NH1 1 
ATOM   2390 N NH2 . ARG B  2 58  ? -6.022  7.118   7.779   1.00 18.85 ? 55  ARG A NH2 1 
ATOM   2391 N N   . ARG B  2 59  ? -3.094  -1.148  8.667   1.00 15.02 ? 56  ARG A N   1 
ATOM   2392 C CA  . ARG B  2 59  ? -2.461  -2.459  8.713   1.00 14.40 ? 56  ARG A CA  1 
ATOM   2393 C C   . ARG B  2 59  ? -2.914  -3.338  7.549   1.00 14.99 ? 56  ARG A C   1 
ATOM   2394 O O   . ARG B  2 59  ? -2.040  -3.902  6.888   1.00 14.43 ? 56  ARG A O   1 
ATOM   2395 C CB  . ARG B  2 59  ? -2.725  -3.160  10.039  1.00 14.57 ? 56  ARG A CB  1 
ATOM   2396 C CG  . ARG B  2 59  ? -2.079  -2.427  11.197  1.00 15.01 ? 56  ARG A CG  1 
ATOM   2397 C CD  . ARG B  2 59  ? -2.610  -2.989  12.516  1.00 15.04 ? 56  ARG A CD  1 
ATOM   2398 N NE  . ARG B  2 59  ? -2.158  -4.381  12.697  1.00 14.11 ? 56  ARG A NE  1 
ATOM   2399 C CZ  . ARG B  2 59  ? -2.795  -5.324  13.416  1.00 14.31 ? 56  ARG A CZ  1 
ATOM   2400 N NH1 . ARG B  2 59  ? -3.971  -5.035  14.001  1.00 12.71 ? 56  ARG A NH1 1 
ATOM   2401 N NH2 . ARG B  2 59  ? -2.168  -6.503  13.560  1.00 13.62 ? 56  ARG A NH2 1 
ATOM   2402 N N   . SER B  2 60  ? -4.226  -3.350  7.256   1.00 15.47 ? 57  SER A N   1 
ATOM   2403 C CA  . SER B  2 60  ? -4.783  -4.067  6.123   1.00 17.18 ? 57  SER A CA  1 
ATOM   2404 C C   . SER B  2 60  ? -4.246  -3.527  4.808   1.00 15.80 ? 57  SER A C   1 
ATOM   2405 O O   . SER B  2 60  ? -3.889  -4.310  3.956   1.00 16.84 ? 57  SER A O   1 
ATOM   2406 C CB  . SER B  2 60  ? -6.322  -4.013  6.034   1.00 19.50 ? 57  SER A CB  1 
ATOM   2407 O OG  . SER B  2 60  ? -6.819  -4.748  7.105   1.00 30.09 ? 57  SER A OG  1 
ATOM   2408 N N   . ALA B  2 61  ? -4.285  -2.210  4.614   1.00 16.20 ? 58  ALA A N   1 
ATOM   2409 C CA  . ALA B  2 61  ? -3.796  -1.596  3.365   1.00 16.69 ? 58  ALA A CA  1 
ATOM   2410 C C   . ALA B  2 61  ? -2.293  -1.880  3.177   1.00 16.59 ? 58  ALA A C   1 
ATOM   2411 O O   . ALA B  2 61  ? -1.863  -2.230  2.083   1.00 16.92 ? 58  ALA A O   1 
ATOM   2412 C CB  . ALA B  2 61  ? -4.109  -0.135  3.327   1.00 16.59 ? 58  ALA A CB  1 
ATOM   2413 N N   . TRP B  2 62  ? -1.526  -1.803  4.266   1.00 16.14 ? 59  TRP A N   1 
ATOM   2414 C CA  . TRP B  2 62  ? -0.106  -2.110  4.231   1.00 16.85 ? 59  TRP A CA  1 
ATOM   2415 C C   . TRP B  2 62  ? 0.168   -3.543  3.755   1.00 17.16 ? 59  TRP A C   1 
ATOM   2416 O O   . TRP B  2 62  ? 1.054   -3.742  2.918   1.00 18.01 ? 59  TRP A O   1 
ATOM   2417 C CB  . TRP B  2 62  ? 0.507   -1.872  5.620   1.00 16.05 ? 59  TRP A CB  1 
ATOM   2418 C CG  . TRP B  2 62  ? 2.006   -1.962  5.593   1.00 17.49 ? 59  TRP A CG  1 
ATOM   2419 C CD1 . TRP B  2 62  ? 2.882   -0.961  5.308   1.00 18.61 ? 59  TRP A CD1 1 
ATOM   2420 C CD2 . TRP B  2 62  ? 2.761   -3.160  5.827   1.00 18.23 ? 59  TRP A CD2 1 
ATOM   2421 N NE1 . TRP B  2 62  ? 4.153   -1.461  5.411   1.00 19.41 ? 59  TRP A NE1 1 
ATOM   2422 C CE2 . TRP B  2 62  ? 4.116   -2.809  5.671   1.00 20.15 ? 59  TRP A CE2 1 
ATOM   2423 C CE3 . TRP B  2 62  ? 2.425   -4.489  6.113   1.00 18.55 ? 59  TRP A CE3 1 
ATOM   2424 C CZ2 . TRP B  2 62  ? 5.131   -3.760  5.835   1.00 21.34 ? 59  TRP A CZ2 1 
ATOM   2425 C CZ3 . TRP B  2 62  ? 3.417   -5.439  6.237   1.00 19.95 ? 59  TRP A CZ3 1 
ATOM   2426 C CH2 . TRP B  2 62  ? 4.760   -5.053  6.144   1.00 22.12 ? 59  TRP A CH2 1 
ATOM   2427 N N   . ARG B  2 63  ? -0.572  -4.538  4.290   1.00 16.40 ? 60  ARG A N   1 
ATOM   2428 C CA  . ARG B  2 63  ? -0.396  -5.922  3.873   1.00 17.58 ? 60  ARG A CA  1 
ATOM   2429 C C   . ARG B  2 63  ? -0.715  -6.140  2.383   1.00 19.67 ? 60  ARG A C   1 
ATOM   2430 O O   . ARG B  2 63  ? 0.019   -6.828  1.672   1.00 19.60 ? 60  ARG A O   1 
ATOM   2431 C CB  . ARG B  2 63  ? -1.190  -6.891  4.731   1.00 17.63 ? 60  ARG A CB  1 
ATOM   2432 C CG  . ARG B  2 63  ? -0.658  -6.971  6.169   1.00 17.48 ? 60  ARG A CG  1 
ATOM   2433 C CD  . ARG B  2 63  ? -1.245  -8.134  6.966   1.00 19.54 ? 60  ARG A CD  1 
ATOM   2434 N NE  . ARG B  2 63  ? -2.711  -8.066  7.013   1.00 19.38 ? 60  ARG A NE  1 
ATOM   2435 C CZ  . ARG B  2 63  ? -3.420  -7.464  7.967   1.00 19.39 ? 60  ARG A CZ  1 
ATOM   2436 N NH1 . ARG B  2 63  ? -2.822  -6.740  8.890   1.00 19.59 ? 60  ARG A NH1 1 
ATOM   2437 N NH2 . ARG B  2 63  ? -4.728  -7.625  8.012   1.00 21.32 ? 60  ARG A NH2 1 
ATOM   2438 N N   . VAL B  2 64  ? -1.796  -5.526  1.923   1.00 18.91 ? 61  VAL A N   1 
ATOM   2439 C CA  . VAL B  2 64  ? -2.156  -5.551  0.503   1.00 20.39 ? 61  VAL A CA  1 
ATOM   2440 C C   . VAL B  2 64  ? -1.054  -4.938  -0.361  1.00 20.66 ? 61  VAL A C   1 
ATOM   2441 O O   . VAL B  2 64  ? -0.633  -5.571  -1.343  1.00 22.47 ? 61  VAL A O   1 
ATOM   2442 C CB  . VAL B  2 64  ? -3.514  -4.877  0.273   1.00 20.20 ? 61  VAL A CB  1 
ATOM   2443 C CG1 . VAL B  2 64  ? -3.808  -4.655  -1.210  1.00 22.68 ? 61  VAL A CG1 1 
ATOM   2444 C CG2 . VAL B  2 64  ? -4.641  -5.674  0.917   1.00 19.26 ? 61  VAL A CG2 1 
ATOM   2445 N N   . VAL B  2 65  ? -0.569  -3.754  0.002   1.00 19.69 ? 62  VAL A N   1 
ATOM   2446 C CA  . VAL B  2 65  ? 0.403   -3.057  -0.852  1.00 21.59 ? 62  VAL A CA  1 
ATOM   2447 C C   . VAL B  2 65  ? 1.768   -3.788  -0.830  1.00 23.88 ? 62  VAL A C   1 
ATOM   2448 O O   . VAL B  2 65  ? 2.344   -4.045  -1.899  1.00 26.33 ? 62  VAL A O   1 
ATOM   2449 C CB  . VAL B  2 65  ? 0.469   -1.552  -0.577  1.00 20.44 ? 62  VAL A CB  1 
ATOM   2450 C CG1 . VAL B  2 65  ? 1.482   -0.851  -1.493  1.00 22.51 ? 62  VAL A CG1 1 
ATOM   2451 C CG2 . VAL B  2 65  ? -0.876  -0.887  -0.780  1.00 19.55 ? 62  VAL A CG2 1 
ATOM   2452 N N   . SER B  2 66  ? 2.174   -4.299  0.336   1.00 25.19 ? 63  SER A N   1 
ATOM   2453 C CA  . SER B  2 66  ? 3.365   -5.141  0.492   1.00 28.40 ? 63  SER A CA  1 
ATOM   2454 C C   . SER B  2 66  ? 3.340   -6.403  -0.357  1.00 31.86 ? 63  SER A C   1 
ATOM   2455 O O   . SER B  2 66  ? 4.296   -6.703  -1.067  1.00 36.86 ? 63  SER A O   1 
ATOM   2456 C CB  . SER B  2 66  ? 3.484   -5.553  1.922   1.00 28.75 ? 63  SER A CB  1 
ATOM   2457 O OG  . SER B  2 66  ? 3.811   -4.405  2.661   1.00 31.76 ? 63  SER A OG  1 
ATOM   2458 N N   . SER B  2 67  ? 2.222   -7.119  -0.296  1.00 30.94 ? 64  SER A N   1 
ATOM   2459 C CA  . SER B  2 67  ? 1.994   -8.293  -1.115  1.00 33.73 ? 64  SER A CA  1 
ATOM   2460 C C   . SER B  2 67  ? 2.075   -7.976  -2.617  1.00 39.41 ? 64  SER A C   1 
ATOM   2461 O O   . SER B  2 67  ? 2.747   -8.723  -3.348  1.00 42.23 ? 64  SER A O   1 
ATOM   2462 C CB  . SER B  2 67  ? 0.688   -8.914  -0.743  1.00 37.10 ? 64  SER A CB  1 
ATOM   2463 O OG  . SER B  2 67  ? 0.413   -10.033 -1.578  1.00 42.23 ? 64  SER A OG  1 
ATOM   2464 N N   . ILE B  2 68  ? 1.394   -6.900  -3.076  1.00 35.42 ? 65  ILE A N   1 
ATOM   2465 C CA  . ILE B  2 68  ? 1.461   -6.443  -4.474  1.00 38.13 ? 65  ILE A CA  1 
ATOM   2466 C C   . ILE B  2 68  ? 2.911   -6.117  -4.847  1.00 42.04 ? 65  ILE A C   1 
ATOM   2467 O O   . ILE B  2 68  ? 3.348   -6.527  -5.924  1.00 49.31 ? 65  ILE A O   1 
ATOM   2468 C CB  . ILE B  2 68  ? 0.510   -5.253  -4.780  1.00 33.66 ? 65  ILE A CB  1 
ATOM   2469 C CG1 . ILE B  2 68  ? -0.956  -5.710  -4.744  1.00 34.54 ? 65  ILE A CG1 1 
ATOM   2470 C CG2 . ILE B  2 68  ? 0.839   -4.535  -6.115  1.00 36.92 ? 65  ILE A CG2 1 
ATOM   2471 C CD1 . ILE B  2 68  ? -1.973  -4.594  -4.617  1.00 32.27 ? 65  ILE A CD1 1 
ATOM   2472 N N   . GLU B  2 69  ? 3.637   -5.412  -3.961  1.00 42.85 ? 66  GLU A N   1 
ATOM   2473 C CA  . GLU B  2 69  ? 5.027   -5.002  -4.161  1.00 45.65 ? 66  GLU A CA  1 
ATOM   2474 C C   . GLU B  2 69  ? 5.961   -6.180  -4.514  1.00 54.19 ? 66  GLU A C   1 
ATOM   2475 O O   . GLU B  2 69  ? 6.929   -5.939  -5.225  1.00 55.88 ? 66  GLU A O   1 
ATOM   2476 C CB  . GLU B  2 69  ? 5.367   -4.097  -2.976  1.00 43.01 ? 66  GLU A CB  1 
ATOM   2477 C CG  . GLU B  2 69  ? 6.648   -3.300  -3.083  1.00 43.45 ? 66  GLU A CG  1 
ATOM   2478 C CD  . GLU B  2 69  ? 7.046   -2.561  -1.835  1.00 41.91 ? 66  GLU A CD  1 
ATOM   2479 O OE1 . GLU B  2 69  ? 6.424   -2.648  -0.757  1.00 45.29 ? 66  GLU A OE1 1 
ATOM   2480 O OE2 . GLU B  2 69  ? 8.104   -1.945  -1.907  1.00 43.80 ? 66  GLU A OE2 1 
ATOM   2481 N N   . GLN B  2 70  ? 5.651   -7.435  -4.104  1.00 59.32 ? 67  GLN A N   1 
ATOM   2482 C CA  . GLN B  2 70  ? 6.099   -8.667  -4.771  1.00 59.69 ? 67  GLN A CA  1 
ATOM   2483 C C   . GLN B  2 70  ? 5.048   -9.168  -5.787  1.00 54.95 ? 67  GLN A C   1 
ATOM   2484 O O   . GLN B  2 70  ? 5.414   -9.308  -6.965  1.00 62.07 ? 67  GLN A O   1 
ATOM   2485 C CB  . GLN B  2 70  ? 6.279   -9.818  -3.781  1.00 59.54 ? 67  GLN A CB  1 
ATOM   2486 C CG  . GLN B  2 70  ? 7.470   -9.629  -2.846  1.00 65.38 ? 67  GLN A CG  1 
ATOM   2487 C CD  . GLN B  2 70  ? 7.209   -8.693  -1.681  1.00 64.87 ? 67  GLN A CD  1 
ATOM   2488 O OE1 . GLN B  2 70  ? 6.373   -8.957  -0.810  1.00 64.50 ? 67  GLN A OE1 1 
ATOM   2489 N NE2 . GLN B  2 70  ? 7.936   -7.589  -1.639  1.00 69.57 ? 67  GLN A NE2 1 
ATOM   2490 N N   . ALA B  2 75  ? 7.802   -4.026  -13.499 1.00 51.22 ? 72  ALA A N   1 
ATOM   2491 C CA  . ALA B  2 75  ? 8.483   -2.877  -14.177 1.00 53.63 ? 72  ALA A CA  1 
ATOM   2492 C C   . ALA B  2 75  ? 8.874   -1.805  -13.153 1.00 50.50 ? 72  ALA A C   1 
ATOM   2493 O O   . ALA B  2 75  ? 8.280   -1.720  -12.077 1.00 46.26 ? 72  ALA A O   1 
ATOM   2494 C CB  . ALA B  2 75  ? 7.654   -2.262  -15.297 1.00 54.56 ? 72  ALA A CB  1 
ATOM   2495 N N   . ALA B  2 76  ? 9.896   -1.011  -13.509 1.00 49.01 ? 73  ALA A N   1 
ATOM   2496 C CA  . ALA B  2 76  ? 10.541  -0.075  -12.591 1.00 46.43 ? 73  ALA A CA  1 
ATOM   2497 C C   . ALA B  2 76  ? 9.532   0.936   -12.029 1.00 42.47 ? 73  ALA A C   1 
ATOM   2498 O O   . ALA B  2 76  ? 9.508   1.158   -10.821 1.00 38.59 ? 73  ALA A O   1 
ATOM   2499 C CB  . ALA B  2 76  ? 11.689  0.648   -13.298 1.00 47.13 ? 73  ALA A CB  1 
ATOM   2500 N N   . ALA B  2 77  ? 8.763   1.580   -12.926 1.00 42.87 ? 74  ALA A N   1 
ATOM   2501 C CA  . ALA B  2 77  ? 7.809   2.632   -12.557 1.00 42.27 ? 74  ALA A CA  1 
ATOM   2502 C C   . ALA B  2 77  ? 6.719   2.103   -11.617 1.00 39.58 ? 74  ALA A C   1 
ATOM   2503 O O   . ALA B  2 77  ? 6.422   2.744   -10.608 1.00 38.36 ? 74  ALA A O   1 
ATOM   2504 C CB  . ALA B  2 77  ? 7.232   3.250   -13.828 1.00 44.95 ? 74  ALA A CB  1 
ATOM   2505 N N   . ALA B  2 78  ? 6.195   0.909   -11.929 1.00 38.92 ? 75  ALA A N   1 
ATOM   2506 C CA  . ALA B  2 78  ? 5.230   0.179   -11.128 1.00 38.90 ? 75  ALA A CA  1 
ATOM   2507 C C   . ALA B  2 78  ? 5.746   -0.187  -9.736  1.00 34.88 ? 75  ALA A C   1 
ATOM   2508 O O   . ALA B  2 78  ? 5.005   -0.080  -8.734  1.00 32.69 ? 75  ALA A O   1 
ATOM   2509 C CB  . ALA B  2 78  ? 4.857   -1.084  -11.878 1.00 41.45 ? 75  ALA A CB  1 
ATOM   2510 N N   . GLN B  2 79  ? 6.998   -0.702  -9.682  1.00 34.18 ? 76  GLN A N   1 
ATOM   2511 C CA  A GLN B  2 79  ? 7.654   -1.121  -8.445  0.50 32.50 ? 76  GLN A CA  1 
ATOM   2512 C CA  B GLN B  2 79  ? 7.575   -1.132  -8.411  0.50 32.57 ? 76  GLN A CA  1 
ATOM   2513 C C   . GLN B  2 79  ? 7.790   0.092   -7.516  1.00 30.91 ? 76  GLN A C   1 
ATOM   2514 O O   . GLN B  2 79  ? 7.516   0.020   -6.328  1.00 29.90 ? 76  GLN A O   1 
ATOM   2515 C CB  A GLN B  2 79  ? 9.049   -1.700  -8.756  0.50 34.24 ? 76  GLN A CB  1 
ATOM   2516 C CB  B GLN B  2 79  ? 8.825   -2.001  -8.604  0.50 34.39 ? 76  GLN A CB  1 
ATOM   2517 C CG  A GLN B  2 79  ? 9.086   -3.126  -9.311  0.50 35.19 ? 76  GLN A CG  1 
ATOM   2518 C CG  B GLN B  2 79  ? 8.732   -3.278  -7.781  0.50 33.93 ? 76  GLN A CG  1 
ATOM   2519 C CD  A GLN B  2 79  ? 10.382  -3.455  -10.024 0.50 38.09 ? 76  GLN A CD  1 
ATOM   2520 C CD  B GLN B  2 79  ? 9.337   -3.186  -6.401  0.50 33.60 ? 76  GLN A CD  1 
ATOM   2521 O OE1 A GLN B  2 79  ? 11.471  -3.120  -9.549  0.50 39.47 ? 76  GLN A OE1 1 
ATOM   2522 O OE1 B GLN B  2 79  ? 8.620   -2.969  -5.418  0.50 33.00 ? 76  GLN A OE1 1 
ATOM   2523 N NE2 A GLN B  2 79  ? 10.305  -4.040  -11.218 0.50 39.38 ? 76  GLN A NE2 1 
ATOM   2524 N NE2 B GLN B  2 79  ? 10.648  -3.394  -6.318  0.50 35.23 ? 76  GLN A NE2 1 
ATOM   2525 N N   . GLN B  2 80  ? 8.255   1.210   -8.097  1.00 31.43 ? 77  GLN A N   1 
ATOM   2526 C CA  . GLN B  2 80  ? 8.451   2.445   -7.361  1.00 30.81 ? 77  GLN A CA  1 
ATOM   2527 C C   . GLN B  2 80  ? 7.123   2.973   -6.820  1.00 28.72 ? 77  GLN A C   1 
ATOM   2528 O O   . GLN B  2 80  ? 7.094   3.416   -5.690  1.00 26.98 ? 77  GLN A O   1 
ATOM   2529 C CB  . GLN B  2 80  ? 9.120   3.467   -8.270  1.00 32.63 ? 77  GLN A CB  1 
ATOM   2530 C CG  . GLN B  2 80  ? 9.293   4.840   -7.643  1.00 33.21 ? 77  GLN A CG  1 
ATOM   2531 C CD  . GLN B  2 80  ? 10.277  5.751   -8.335  1.00 36.38 ? 77  GLN A CD  1 
ATOM   2532 O OE1 . GLN B  2 80  ? 11.018  5.407   -9.262  1.00 37.63 ? 77  GLN A OE1 1 
ATOM   2533 N NE2 . GLN B  2 80  ? 10.233  6.989   -7.879  1.00 37.58 ? 77  GLN A NE2 1 
ATOM   2534 N N   . MET B  2 81  ? 6.069   2.999   -7.652  1.00 29.02 ? 78  MET A N   1 
ATOM   2535 C CA  . MET B  2 81  ? 4.753   3.451   -7.190  1.00 28.21 ? 78  MET A CA  1 
ATOM   2536 C C   . MET B  2 81  ? 4.274   2.637   -6.006  1.00 24.97 ? 78  MET A C   1 
ATOM   2537 O O   . MET B  2 81  ? 3.849   3.239   -5.016  1.00 23.71 ? 78  MET A O   1 
ATOM   2538 C CB  . MET B  2 81  ? 3.727   3.401   -8.324  1.00 30.81 ? 78  MET A CB  1 
ATOM   2539 C CG  . MET B  2 81  ? 2.228   3.658   -7.909  1.00 32.39 ? 78  MET A CG  1 
ATOM   2540 S SD  . MET B  2 81  ? 1.180   3.505   -9.381  1.00 38.97 ? 78  MET A SD  1 
ATOM   2541 C CE  . MET B  2 81  ? 2.006   4.428   -10.691 1.00 38.82 ? 78  MET A CE  1 
ATOM   2542 N N   . ALA B  2 82  ? 4.373   1.308   -6.096  1.00 24.10 ? 79  ALA A N   1 
ATOM   2543 C CA  . ALA B  2 82  ? 4.001   0.424   -5.012  1.00 22.81 ? 79  ALA A CA  1 
ATOM   2544 C C   . ALA B  2 82  ? 4.790   0.710   -3.733  1.00 21.87 ? 79  ALA A C   1 
ATOM   2545 O O   . ALA B  2 82  ? 4.219   0.800   -2.647  1.00 20.83 ? 79  ALA A O   1 
ATOM   2546 C CB  . ALA B  2 82  ? 4.179   -1.016  -5.449  1.00 23.49 ? 79  ALA A CB  1 
ATOM   2547 N N   . ARG B  2 83  ? 6.125   0.893   -3.884  1.00 22.85 ? 80  ARG A N   1 
ATOM   2548 C CA  . ARG B  2 83  ? 6.984   1.190   -2.741  1.00 22.41 ? 80  ARG A CA  1 
ATOM   2549 C C   . ARG B  2 83  ? 6.570   2.515   -2.098  1.00 21.66 ? 80  ARG A C   1 
ATOM   2550 O O   . ARG B  2 83  ? 6.369   2.530   -0.896  1.00 20.23 ? 80  ARG A O   1 
ATOM   2551 C CB  . ARG B  2 83  ? 8.489   1.303   -3.117  1.00 23.93 ? 80  ARG A CB  1 
ATOM   2552 C CG  . ARG B  2 83  ? 9.361   1.640   -1.893  1.00 23.59 ? 80  ARG A CG  1 
ATOM   2553 C CD  . ARG B  2 83  ? 10.829  1.659   -2.312  1.00 25.17 ? 80  ARG A CD  1 
ATOM   2554 N NE  . ARG B  2 83  ? 11.125  2.601   -3.382  1.00 26.77 ? 80  ARG A NE  1 
ATOM   2555 C CZ  . ARG B  2 83  ? 11.268  3.925   -3.410  1.00 27.30 ? 80  ARG A CZ  1 
ATOM   2556 N NH1 . ARG B  2 83  ? 11.028  4.603   -2.335  1.00 26.73 ? 80  ARG A NH1 1 
ATOM   2557 N NH2 . ARG B  2 83  ? 11.590  4.563   -4.502  1.00 28.95 ? 80  ARG A NH2 1 
ATOM   2558 N N   . GLU B  2 84  ? 6.407   3.574   -2.901  1.00 23.00 ? 81  GLU A N   1 
ATOM   2559 C CA  . GLU B  2 84  ? 6.110   4.899   -2.381  1.00 23.67 ? 81  GLU A CA  1 
ATOM   2560 C C   . GLU B  2 84  ? 4.732   4.943   -1.719  1.00 22.70 ? 81  GLU A C   1 
ATOM   2561 O O   . GLU B  2 84  ? 4.572   5.557   -0.696  1.00 22.41 ? 81  GLU A O   1 
ATOM   2562 C CB  . GLU B  2 84  ? 6.241   5.982   -3.435  1.00 25.85 ? 81  GLU A CB  1 
ATOM   2563 C CG  . GLU B  2 84  ? 7.682   6.153   -3.933  1.00 28.31 ? 81  GLU A CG  1 
ATOM   2564 C CD  . GLU B  2 84  ? 7.895   7.121   -5.064  1.00 30.82 ? 81  GLU A CD  1 
ATOM   2565 O OE1 . GLU B  2 84  ? 6.876   7.477   -5.702  1.00 31.08 ? 81  GLU A OE1 1 
ATOM   2566 O OE2 . GLU B  2 84  ? 9.051   7.551   -5.342  1.00 32.76 ? 81  GLU A OE2 1 
ATOM   2567 N N   . TYR B  2 85  ? 3.782   4.178   -2.238  1.00 23.08 ? 82  TYR A N   1 
ATOM   2568 C CA  . TYR B  2 85  ? 2.470   4.011   -1.613  1.00 21.59 ? 82  TYR A CA  1 
ATOM   2569 C C   . TYR B  2 85  ? 2.546   3.314   -0.273  1.00 20.26 ? 82  TYR A C   1 
ATOM   2570 O O   . TYR B  2 85  ? 1.943   3.789   0.694   1.00 18.56 ? 82  TYR A O   1 
ATOM   2571 C CB  . TYR B  2 85  ? 1.527   3.365   -2.639  1.00 22.16 ? 82  TYR A CB  1 
ATOM   2572 C CG  . TYR B  2 85  ? 0.054   3.632   -2.329  1.00 22.35 ? 82  TYR A CG  1 
ATOM   2573 C CD1 . TYR B  2 85  ? -0.429  4.917   -2.025  1.00 23.29 ? 82  TYR A CD1 1 
ATOM   2574 C CD2 . TYR B  2 85  ? -0.879  2.607   -2.411  1.00 23.86 ? 82  TYR A CD2 1 
ATOM   2575 C CE1 . TYR B  2 85  ? -1.755  5.153   -1.716  1.00 23.27 ? 82  TYR A CE1 1 
ATOM   2576 C CE2 . TYR B  2 85  ? -2.223  2.836   -2.097  1.00 23.53 ? 82  TYR A CE2 1 
ATOM   2577 C CZ  . TYR B  2 85  ? -2.673  4.128   -1.842  1.00 23.00 ? 82  TYR A CZ  1 
ATOM   2578 O OH  . TYR B  2 85  ? -3.982  4.421   -1.599  1.00 22.07 ? 82  TYR A OH  1 
ATOM   2579 N N   . ARG B  2 86  ? 3.293   2.202   -0.216  1.00 20.98 ? 83  ARG A N   1 
ATOM   2580 C CA  . ARG B  2 86  ? 3.570   1.518   1.028   1.00 20.64 ? 83  ARG A CA  1 
ATOM   2581 C C   . ARG B  2 86  ? 4.148   2.455   2.089   1.00 21.25 ? 83  ARG A C   1 
ATOM   2582 O O   . ARG B  2 86  ? 3.789   2.319   3.273   1.00 20.27 ? 83  ARG A O   1 
ATOM   2583 C CB  . ARG B  2 86  ? 4.393   0.231   0.891   1.00 21.67 ? 83  ARG A CB  1 
ATOM   2584 C CG  . ARG B  2 86  ? 4.811   -0.392  2.224   1.00 23.18 ? 83  ARG A CG  1 
ATOM   2585 C CD  . ARG B  2 86  ? 5.574   -1.605  2.207   1.00 26.53 ? 83  ARG A CD  1 
ATOM   2586 N NE  . ARG B  2 86  ? 6.864   -1.455  1.515   1.00 31.54 ? 83  ARG A NE  1 
ATOM   2587 C CZ  . ARG B  2 86  ? 7.954   -0.703  1.749   1.00 31.55 ? 83  ARG A CZ  1 
ATOM   2588 N NH1 . ARG B  2 86  ? 8.048   0.114   2.797   1.00 31.35 ? 83  ARG A NH1 1 
ATOM   2589 N NH2 . ARG B  2 86  ? 8.945   -0.784  0.855   1.00 32.42 ? 83  ARG A NH2 1 
ATOM   2590 N N   . GLU B  2 87  ? 5.120   3.287   1.698   1.00 22.59 ? 84  GLU A N   1 
ATOM   2591 C CA  . GLU B  2 87  ? 5.811   4.189   2.607   1.00 22.74 ? 84  GLU A CA  1 
ATOM   2592 C C   . GLU B  2 87  ? 4.830   5.229   3.164   1.00 22.53 ? 84  GLU A C   1 
ATOM   2593 O O   . GLU B  2 87  ? 4.881   5.527   4.355   1.00 21.86 ? 84  GLU A O   1 
ATOM   2594 C CB  . GLU B  2 87  ? 6.965   4.861   1.849   1.00 23.75 ? 84  GLU A CB  1 
ATOM   2595 C CG  . GLU B  2 87  ? 8.160   3.943   1.591   1.00 24.78 ? 84  GLU A CG  1 
ATOM   2596 C CD  . GLU B  2 87  ? 9.261   4.523   0.748   1.00 26.68 ? 84  GLU A CD  1 
ATOM   2597 O OE1 . GLU B  2 87  ? 9.110   5.644   0.238   1.00 27.60 ? 84  GLU A OE1 1 
ATOM   2598 O OE2 . GLU B  2 87  ? 10.307  3.840   0.576   1.00 29.11 ? 84  GLU A OE2 1 
ATOM   2599 N N   . LYS B  2 88  ? 3.930   5.745   2.313   1.00 23.58 ? 85  LYS A N   1 
ATOM   2600 C CA  . LYS B  2 88  ? 2.889   6.679   2.715   1.00 23.43 ? 85  LYS A CA  1 
ATOM   2601 C C   . LYS B  2 88  ? 1.985   6.058   3.769   1.00 21.67 ? 85  LYS A C   1 
ATOM   2602 O O   . LYS B  2 88  ? 1.690   6.728   4.770   1.00 20.50 ? 85  LYS A O   1 
ATOM   2603 C CB  . LYS B  2 88  ? 2.031   7.055   1.498   1.00 26.53 ? 85  LYS A CB  1 
ATOM   2604 C CG  . LYS B  2 88  ? 0.884   8.049   1.667   1.00 29.59 ? 85  LYS A CG  1 
ATOM   2605 C CD  . LYS B  2 88  ? 0.105   8.159   0.325   1.00 35.56 ? 85  LYS A CD  1 
ATOM   2606 C CE  . LYS B  2 88  ? -0.601  9.440   -0.062  1.00 40.38 ? 85  LYS A CE  1 
ATOM   2607 N NZ  . LYS B  2 88  ? -1.136  10.118  1.129   1.00 39.97 ? 85  LYS A NZ  1 
ATOM   2608 N N   . ILE B  2 89  ? 1.582   4.800   3.531   1.00 19.41 ? 86  ILE A N   1 
ATOM   2609 C CA  . ILE B  2 89  ? 0.758   4.059   4.466   1.00 19.84 ? 86  ILE A CA  1 
ATOM   2610 C C   . ILE B  2 89  ? 1.512   3.847   5.782   1.00 19.39 ? 86  ILE A C   1 
ATOM   2611 O O   . ILE B  2 89  ? 0.895   3.927   6.833   1.00 17.92 ? 86  ILE A O   1 
ATOM   2612 C CB  . ILE B  2 89  ? 0.223   2.763   3.816   1.00 20.03 ? 86  ILE A CB  1 
ATOM   2613 C CG1 . ILE B  2 89  ? -0.695  3.065   2.642   1.00 20.76 ? 86  ILE A CG1 1 
ATOM   2614 C CG2 . ILE B  2 89  ? -0.468  1.847   4.854   1.00 20.35 ? 86  ILE A CG2 1 
ATOM   2615 C CD1 . ILE B  2 89  ? -0.947  1.870   1.751   1.00 20.73 ? 86  ILE A CD1 1 
ATOM   2616 N N   . GLU B  2 90  ? 2.796   3.455   5.689   1.00 20.31 ? 87  GLU A N   1 
ATOM   2617 C CA  . GLU B  2 90  ? 3.672   3.254   6.840   1.00 22.19 ? 87  GLU A CA  1 
ATOM   2618 C C   . GLU B  2 90  ? 3.790   4.525   7.686   1.00 22.11 ? 87  GLU A C   1 
ATOM   2619 O O   . GLU B  2 90  ? 3.774   4.413   8.912   1.00 21.09 ? 87  GLU A O   1 
ATOM   2620 C CB  . GLU B  2 90  ? 5.086   2.847   6.424   1.00 25.03 ? 87  GLU A CB  1 
ATOM   2621 C CG  . GLU B  2 90  ? 5.466   1.414   6.705   1.00 28.57 ? 87  GLU A CG  1 
ATOM   2622 C CD  . GLU B  2 90  ? 6.653   0.954   5.870   1.00 30.11 ? 87  GLU A CD  1 
ATOM   2623 O OE1 . GLU B  2 90  ? 7.624   1.746   5.732   1.00 42.59 ? 87  GLU A OE1 1 
ATOM   2624 O OE2 . GLU B  2 90  ? 6.589   -0.145  5.308   1.00 29.08 ? 87  GLU A OE2 1 
ATOM   2625 N N   . THR B  2 91  ? 3.916   5.696   7.035   1.00 21.94 ? 88  THR A N   1 
ATOM   2626 C CA  . THR B  2 91  ? 4.016   6.964   7.743   1.00 22.66 ? 88  THR A CA  1 
ATOM   2627 C C   . THR B  2 91  ? 2.726   7.189   8.553   1.00 22.15 ? 88  THR A C   1 
ATOM   2628 O O   . THR B  2 91  ? 2.809   7.457   9.751   1.00 20.66 ? 88  THR A O   1 
ATOM   2629 C CB  . THR B  2 91  ? 4.362   8.108   6.783   1.00 23.67 ? 88  THR A CB  1 
ATOM   2630 O OG1 . THR B  2 91  ? 5.683   7.809   6.312   1.00 22.71 ? 88  THR A OG1 1 
ATOM   2631 C CG2 . THR B  2 91  ? 4.332   9.472   7.436   1.00 24.44 ? 88  THR A CG2 1 
ATOM   2632 N N   . GLU B  2 92  ? 1.547   6.978   7.938   1.00 22.30 ? 89  GLU A N   1 
ATOM   2633 C CA  . GLU B  2 92  ? 0.275   7.074   8.654   1.00 21.14 ? 89  GLU A CA  1 
ATOM   2634 C C   . GLU B  2 92  ? 0.241   6.114   9.847   1.00 20.95 ? 89  GLU A C   1 
ATOM   2635 O O   . GLU B  2 92  ? -0.117  6.528   10.948  1.00 19.38 ? 89  GLU A O   1 
ATOM   2636 C CB  . GLU B  2 92  ? -0.929  6.789   7.756   1.00 20.59 ? 89  GLU A CB  1 
ATOM   2637 C CG  . GLU B  2 92  ? -1.112  7.802   6.623   1.00 21.90 ? 89  GLU A CG  1 
ATOM   2638 C CD  . GLU B  2 92  ? -2.289  7.501   5.722   1.00 22.26 ? 89  GLU A CD  1 
ATOM   2639 O OE1 . GLU B  2 92  ? -3.100  6.610   6.072   1.00 19.79 ? 89  GLU A OE1 1 
ATOM   2640 O OE2 . GLU B  2 92  ? -2.396  8.188   4.682   1.00 23.12 ? 89  GLU A OE2 1 
ATOM   2641 N N   . LEU B  2 93  ? 0.681   4.860   9.623   1.00 21.15 ? 90  LEU A N   1 
ATOM   2642 C CA  . LEU B  2 93  ? 0.650   3.834   10.646  1.00 20.63 ? 90  LEU A CA  1 
ATOM   2643 C C   . LEU B  2 93  ? 1.521   4.230   11.830  1.00 21.63 ? 90  LEU A C   1 
ATOM   2644 O O   . LEU B  2 93  ? 1.015   4.197   12.968  1.00 24.49 ? 90  LEU A O   1 
ATOM   2645 C CB  . LEU B  2 93  ? 1.010   2.521   9.974   1.00 23.09 ? 90  LEU A CB  1 
ATOM   2646 C CG  . LEU B  2 93  ? 0.556   1.232   10.659  1.00 24.00 ? 90  LEU A CG  1 
ATOM   2647 C CD1 . LEU B  2 93  ? 0.481   0.117   9.619   1.00 25.89 ? 90  LEU A CD1 1 
ATOM   2648 C CD2 . LEU B  2 93  ? 1.599   0.866   11.714  1.00 28.47 ? 90  LEU A CD2 1 
ATOM   2649 N N   . ARG B  2 94  ? 2.748   4.720   11.567  1.00 21.23 ? 91  ARG A N   1 
ATOM   2650 C CA  . ARG B  2 94  ? 3.643   5.195   12.620  1.00 24.48 ? 91  ARG A CA  1 
ATOM   2651 C C   . ARG B  2 94  ? 3.089   6.388   13.392  1.00 23.42 ? 91  ARG A C   1 
ATOM   2652 O O   . ARG B  2 94  ? 3.229   6.418   14.621  1.00 23.85 ? 91  ARG A O   1 
ATOM   2653 C CB  . ARG B  2 94  ? 5.004   5.632   12.064  1.00 29.14 ? 91  ARG A CB  1 
ATOM   2654 C CG  . ARG B  2 94  ? 5.793   4.411   11.627  1.00 32.75 ? 91  ARG A CG  1 
ATOM   2655 C CD  . ARG B  2 94  ? 7.169   4.824   11.136  1.00 39.31 ? 91  ARG A CD  1 
ATOM   2656 N NE  . ARG B  2 94  ? 7.540   3.850   10.107  1.00 41.31 ? 91  ARG A NE  1 
ATOM   2657 C CZ  . ARG B  2 94  ? 8.410   2.859   10.225  1.00 48.70 ? 91  ARG A CZ  1 
ATOM   2658 N NH1 . ARG B  2 94  ? 9.284   2.804   11.235  1.00 50.01 ? 91  ARG A NH1 1 
ATOM   2659 N NH2 . ARG B  2 94  ? 8.434   1.918   9.293   1.00 55.17 ? 91  ARG A NH2 1 
ATOM   2660 N N   . ASP B  2 95  ? 2.469   7.338   12.673  1.00 21.95 ? 92  ASP A N   1 
ATOM   2661 C CA  . ASP B  2 95  ? 1.854   8.517   13.270  1.00 21.66 ? 92  ASP A CA  1 
ATOM   2662 C C   . ASP B  2 95  ? 0.718   8.129   14.197  1.00 19.59 ? 92  ASP A C   1 
ATOM   2663 O O   . ASP B  2 95  ? 0.668   8.674   15.320  1.00 20.64 ? 92  ASP A O   1 
ATOM   2664 C CB  . ASP B  2 95  ? 1.447   9.542   12.213  1.00 23.20 ? 92  ASP A CB  1 
ATOM   2665 C CG  . ASP B  2 95  ? 2.621   10.257  11.543  1.00 26.19 ? 92  ASP A CG  1 
ATOM   2666 O OD1 . ASP B  2 95  ? 3.759   10.048  11.981  1.00 29.46 ? 92  ASP A OD1 1 
ATOM   2667 O OD2 . ASP B  2 95  ? 2.399   10.919  10.522  1.00 30.45 ? 92  ASP A OD2 1 
ATOM   2668 N N   . ILE B  2 96  ? -0.107  7.146   13.768  1.00 17.62 ? 93  ILE A N   1 
ATOM   2669 C CA  . ILE B  2 96  ? -1.200  6.655   14.593  1.00 17.29 ? 93  ILE A CA  1 
ATOM   2670 C C   . ILE B  2 96  ? -0.628  5.997   15.851  1.00 17.09 ? 93  ILE A C   1 
ATOM   2671 O O   . ILE B  2 96  ? -1.071  6.327   16.969  1.00 17.41 ? 93  ILE A O   1 
ATOM   2672 C CB  . ILE B  2 96  ? -2.158  5.741   13.808  1.00 16.79 ? 93  ILE A CB  1 
ATOM   2673 C CG1 . ILE B  2 96  ? -2.881  6.503   12.672  1.00 17.23 ? 93  ILE A CG1 1 
ATOM   2674 C CG2 . ILE B  2 96  ? -3.158  5.006   14.724  1.00 17.46 ? 93  ILE A CG2 1 
ATOM   2675 C CD1 . ILE B  2 96  ? -3.334  5.613   11.518  1.00 17.74 ? 93  ILE A CD1 1 
ATOM   2676 N N   . CYS B  2 97  ? 0.320   5.079   15.672  1.00 16.17 ? 94  CYS A N   1 
ATOM   2677 C CA  . CYS B  2 97  ? 0.936   4.401   16.803  1.00 17.24 ? 94  CYS A CA  1 
ATOM   2678 C C   . CYS B  2 97  ? 1.617   5.366   17.770  1.00 17.76 ? 94  CYS A C   1 
ATOM   2679 O O   . CYS B  2 97  ? 1.439   5.207   18.984  1.00 17.27 ? 94  CYS A O   1 
ATOM   2680 C CB  . CYS B  2 97  ? 1.914   3.322   16.355  1.00 17.16 ? 94  CYS A CB  1 
ATOM   2681 S SG  . CYS B  2 97  ? 1.117   1.939   15.490  1.00 18.51 ? 94  CYS A SG  1 
ATOM   2682 N N   . ASN B  2 98  ? 2.281   6.389   17.258  1.00 19.86 ? 95  ASN A N   1 
ATOM   2683 C CA  . ASN B  2 98  ? 2.929   7.404   18.091  1.00 22.02 ? 95  ASN A CA  1 
ATOM   2684 C C   . ASN B  2 98  ? 1.926   8.210   18.900  1.00 21.36 ? 95  ASN A C   1 
ATOM   2685 O O   . ASN B  2 98  ? 2.227   8.482   20.066  1.00 20.62 ? 95  ASN A O   1 
ATOM   2686 C CB  . ASN B  2 98  ? 3.839   8.311   17.288  1.00 26.25 ? 95  ASN A CB  1 
ATOM   2687 C CG  . ASN B  2 98  ? 5.085   7.609   16.783  1.00 31.35 ? 95  ASN A CG  1 
ATOM   2688 O OD1 . ASN B  2 98  ? 5.500   6.538   17.265  1.00 34.63 ? 95  ASN A OD1 1 
ATOM   2689 N ND2 . ASN B  2 98  ? 5.687   8.226   15.774  1.00 33.75 ? 95  ASN A ND2 1 
ATOM   2690 N N   . ASP B  2 99  ? 0.758   8.556   18.331  1.00 22.07 ? 96  ASP A N   1 
ATOM   2691 C CA  . ASP B  2 99  ? -0.272  9.233   19.097  1.00 23.60 ? 96  ASP A CA  1 
ATOM   2692 C C   . ASP B  2 99  ? -0.704  8.382   20.286  1.00 22.75 ? 96  ASP A C   1 
ATOM   2693 O O   . ASP B  2 99  ? -0.766  8.891   21.400  1.00 21.95 ? 96  ASP A O   1 
ATOM   2694 C CB  . ASP B  2 99  ? -1.491  9.625   18.272  1.00 25.47 ? 96  ASP A CB  1 
ATOM   2695 C CG  . ASP B  2 99  ? -1.429  10.970  17.550  1.00 33.75 ? 96  ASP A CG  1 
ATOM   2696 O OD1 . ASP B  2 99  ? -0.352  11.679  17.574  1.00 35.49 ? 96  ASP A OD1 1 
ATOM   2697 O OD2 . ASP B  2 99  ? -2.463  11.300  16.933  1.00 35.79 ? 96  ASP A OD2 1 
ATOM   2698 N N   . VAL B  2 100 ? -1.050  7.123   20.008  1.00 21.92 ? 97  VAL A N   1 
ATOM   2699 C CA  . VAL B  2 100 ? -1.504  6.194   21.037  1.00 20.71 ? 97  VAL A CA  1 
ATOM   2700 C C   . VAL B  2 100 ? -0.448  6.021   22.112  1.00 19.60 ? 97  VAL A C   1 
ATOM   2701 O O   . VAL B  2 100 ? -0.754  6.105   23.289  1.00 18.61 ? 97  VAL A O   1 
ATOM   2702 C CB  . VAL B  2 100 ? -1.893  4.816   20.476  1.00 20.14 ? 97  VAL A CB  1 
ATOM   2703 C CG1 . VAL B  2 100 ? -2.216  3.788   21.583  1.00 21.38 ? 97  VAL A CG1 1 
ATOM   2704 C CG2 . VAL B  2 100 ? -3.073  4.963   19.550  1.00 21.65 ? 97  VAL A CG2 1 
ATOM   2705 N N   . LEU B  2 101 ? 0.771   5.720   21.680  1.00 18.77 ? 98  LEU A N   1 
ATOM   2706 C CA  . LEU B  2 101 ? 1.867   5.504   22.607  1.00 19.86 ? 98  LEU A CA  1 
ATOM   2707 C C   . LEU B  2 101 ? 2.164   6.728   23.484  1.00 21.74 ? 98  LEU A C   1 
ATOM   2708 O O   . LEU B  2 101 ? 2.447   6.543   24.680  1.00 21.49 ? 98  LEU A O   1 
ATOM   2709 C CB  . LEU B  2 101 ? 3.074   4.992   21.824  1.00 21.15 ? 98  LEU A CB  1 
ATOM   2710 C CG  . LEU B  2 101 ? 2.915   3.578   21.276  1.00 20.83 ? 98  LEU A CG  1 
ATOM   2711 C CD1 . LEU B  2 101 ? 4.016   3.184   20.246  1.00 19.32 ? 98  LEU A CD1 1 
ATOM   2712 C CD2 . LEU B  2 101 ? 2.807   2.563   22.356  1.00 19.59 ? 98  LEU A CD2 1 
ATOM   2713 N N   . SER B  2 102 ? 2.056   7.929   22.919  1.00 20.98 ? 99  SER A N   1 
ATOM   2714 C CA  . SER B  2 102 ? 2.188   9.158   23.669  1.00 24.55 ? 99  SER A CA  1 
ATOM   2715 C C   . SER B  2 102 ? 1.103   9.322   24.750  1.00 23.01 ? 99  SER A C   1 
ATOM   2716 O O   . SER B  2 102 ? 1.432   9.730   25.857  1.00 25.22 ? 99  SER A O   1 
ATOM   2717 C CB  . SER B  2 102 ? 2.231   10.313  22.699  1.00 25.76 ? 99  SER A CB  1 
ATOM   2718 O OG  . SER B  2 102 ? 2.427   11.507  23.435  1.00 30.12 ? 99  SER A OG  1 
ATOM   2719 N N   . LEU B  2 103 ? -0.170  9.046   24.410  1.00 22.06 ? 100 LEU A N   1 
ATOM   2720 C CA  . LEU B  2 103 ? -1.281  9.083   25.339  1.00 22.43 ? 100 LEU A CA  1 
ATOM   2721 C C   . LEU B  2 103 ? -1.044  8.128   26.499  1.00 21.49 ? 100 LEU A C   1 
ATOM   2722 O O   . LEU B  2 103 ? -1.290  8.503   27.644  1.00 20.37 ? 100 LEU A O   1 
ATOM   2723 C CB  . LEU B  2 103 ? -2.606  8.783   24.646  1.00 22.12 ? 100 LEU A CB  1 
ATOM   2724 C CG  . LEU B  2 103 ? -3.077  9.856   23.645  1.00 22.97 ? 100 LEU A CG  1 
ATOM   2725 C CD1 . LEU B  2 103 ? -4.317  9.342   22.971  1.00 23.71 ? 100 LEU A CD1 1 
ATOM   2726 C CD2 . LEU B  2 103 ? -3.335  11.262  24.230  1.00 23.89 ? 100 LEU A CD2 1 
ATOM   2727 N N   . LEU B  2 104 ? -0.575  6.924   26.182  1.00 19.95 ? 101 LEU A N   1 
ATOM   2728 C CA  . LEU B  2 104 ? -0.256  5.882   27.145  1.00 21.57 ? 101 LEU A CA  1 
ATOM   2729 C C   . LEU B  2 104 ? 0.857   6.324   28.096  1.00 24.73 ? 101 LEU A C   1 
ATOM   2730 O O   . LEU B  2 104 ? 0.642   6.244   29.307  1.00 22.80 ? 101 LEU A O   1 
ATOM   2731 C CB  . LEU B  2 104 ? 0.075   4.598   26.410  1.00 22.10 ? 101 LEU A CB  1 
ATOM   2732 C CG  . LEU B  2 104 ? -1.099  3.893   25.735  1.00 21.51 ? 101 LEU A CG  1 
ATOM   2733 C CD1 . LEU B  2 104 ? -0.557  2.839   24.762  1.00 21.54 ? 101 LEU A CD1 1 
ATOM   2734 C CD2 . LEU B  2 104 ? -2.000  3.219   26.751  1.00 21.01 ? 101 LEU A CD2 1 
ATOM   2735 N N   . GLU B  2 105 ? 1.954   6.874   27.540  1.00 23.59 ? 102 GLU A N   1 
ATOM   2736 C CA  . GLU B  2 105 ? 3.096   7.301   28.349  1.00 26.27 ? 102 GLU A CA  1 
ATOM   2737 C C   . GLU B  2 105 ? 2.763   8.547   29.165  1.00 24.54 ? 102 GLU A C   1 
ATOM   2738 O O   . GLU B  2 105 ? 3.081   8.595   30.358  1.00 25.82 ? 102 GLU A O   1 
ATOM   2739 C CB  . GLU B  2 105 ? 4.338   7.475   27.478  1.00 27.09 ? 102 GLU A CB  1 
ATOM   2740 C CG  . GLU B  2 105 ? 5.619   7.099   28.203  1.00 30.35 ? 102 GLU A CG  1 
ATOM   2741 C CD  . GLU B  2 105 ? 5.694   5.611   28.546  1.00 29.64 ? 102 GLU A CD  1 
ATOM   2742 O OE1 . GLU B  2 105 ? 6.517   5.497   29.472  1.00 33.64 ? 102 GLU A OE1 1 
ATOM   2743 O OE2 . GLU B  2 105 ? 5.014   4.614   28.012  1.00 25.52 ? 102 GLU A OE2 1 
ATOM   2744 N N   . LYS B  2 106 ? 2.133   9.563   28.557  1.00 24.54 ? 103 LYS A N   1 
ATOM   2745 C CA  . LYS B  2 106 ? 1.889   10.849  29.217  1.00 28.38 ? 103 LYS A CA  1 
ATOM   2746 C C   . LYS B  2 106 ? 0.718   10.780  30.219  1.00 26.92 ? 103 LYS A C   1 
ATOM   2747 O O   . LYS B  2 106 ? 0.795   11.408  31.261  1.00 26.15 ? 103 LYS A O   1 
ATOM   2748 C CB  . LYS B  2 106 ? 1.749   11.936  28.138  1.00 31.38 ? 103 LYS A CB  1 
ATOM   2749 C CG  . LYS B  2 106 ? 1.636   13.335  28.650  1.00 40.07 ? 103 LYS A CG  1 
ATOM   2750 C CD  . LYS B  2 106 ? 1.646   14.444  27.593  1.00 42.38 ? 103 LYS A CD  1 
ATOM   2751 C CE  . LYS B  2 106 ? 1.565   15.758  28.312  1.00 49.20 ? 103 LYS A CE  1 
ATOM   2752 N NZ  . LYS B  2 106 ? 1.363   16.848  27.354  1.00 52.15 ? 103 LYS A NZ  1 
ATOM   2753 N N   . PHE B  2 107 ? -0.381  10.055  29.932  1.00 24.09 ? 104 PHE A N   1 
ATOM   2754 C CA  . PHE B  2 107 ? -1.596  10.123  30.742  1.00 23.93 ? 104 PHE A CA  1 
ATOM   2755 C C   . PHE B  2 107 ? -1.984  8.780   31.342  1.00 23.41 ? 104 PHE A C   1 
ATOM   2756 O O   . PHE B  2 107 ? -2.157  8.698   32.537  1.00 26.05 ? 104 PHE A O   1 
ATOM   2757 C CB  . PHE B  2 107 ? -2.756  10.641  29.908  1.00 23.54 ? 104 PHE A CB  1 
ATOM   2758 C CG  . PHE B  2 107 ? -2.514  12.055  29.376  1.00 24.43 ? 104 PHE A CG  1 
ATOM   2759 C CD1 . PHE B  2 107 ? -2.679  13.155  30.216  1.00 26.44 ? 104 PHE A CD1 1 
ATOM   2760 C CD2 . PHE B  2 107 ? -2.128  12.272  28.054  1.00 24.17 ? 104 PHE A CD2 1 
ATOM   2761 C CE1 . PHE B  2 107 ? -2.433  14.452  29.764  1.00 27.40 ? 104 PHE A CE1 1 
ATOM   2762 C CE2 . PHE B  2 107 ? -1.896  13.566  27.588  1.00 26.21 ? 104 PHE A CE2 1 
ATOM   2763 C CZ  . PHE B  2 107 ? -2.080  14.663  28.429  1.00 27.19 ? 104 PHE A CZ  1 
ATOM   2764 N N   . LEU B  2 108 ? -2.157  7.751   30.521  1.00 21.31 ? 105 LEU A N   1 
ATOM   2765 C CA  . LEU B  2 108 ? -2.954  6.597   30.907  1.00 20.86 ? 105 LEU A CA  1 
ATOM   2766 C C   . LEU B  2 108 ? -2.162  5.699   31.858  1.00 21.49 ? 105 LEU A C   1 
ATOM   2767 O O   . LEU B  2 108 ? -2.671  5.386   32.938  1.00 22.03 ? 105 LEU A O   1 
ATOM   2768 C CB  . LEU B  2 108 ? -3.465  5.846   29.674  1.00 20.63 ? 105 LEU A CB  1 
ATOM   2769 C CG  . LEU B  2 108 ? -4.345  6.686   28.737  1.00 20.13 ? 105 LEU A CG  1 
ATOM   2770 C CD1 . LEU B  2 108 ? -4.541  5.989   27.446  1.00 20.33 ? 105 LEU A CD1 1 
ATOM   2771 C CD2 . LEU B  2 108 ? -5.682  7.059   29.386  1.00 22.34 ? 105 LEU A CD2 1 
ATOM   2772 N N   . ILE B  2 109 ? -0.923  5.314   31.507  1.00 20.04 ? 106 ILE A N   1 
ATOM   2773 C CA  . ILE B  2 109 ? -0.152  4.386   32.357  1.00 20.04 ? 106 ILE A CA  1 
ATOM   2774 C C   . ILE B  2 109 ? 0.151   5.033   33.717  1.00 22.33 ? 106 ILE A C   1 
ATOM   2775 O O   . ILE B  2 109 ? -0.172  4.394   34.734  1.00 21.29 ? 106 ILE A O   1 
ATOM   2776 C CB  . ILE B  2 109 ? 1.109   3.819   31.666  1.00 19.04 ? 106 ILE A CB  1 
ATOM   2777 C CG1 . ILE B  2 109 ? 0.738   2.901   30.491  1.00 18.11 ? 106 ILE A CG1 1 
ATOM   2778 C CG2 . ILE B  2 109 ? 2.017   3.074   32.644  1.00 19.72 ? 106 ILE A CG2 1 
ATOM   2779 C CD1 . ILE B  2 109 ? 1.854   2.644   29.485  1.00 17.30 ? 106 ILE A CD1 1 
ATOM   2780 N N   . PRO B  2 110 ? 0.717   6.263   33.801  1.00 25.70 ? 107 PRO A N   1 
ATOM   2781 C CA  . PRO B  2 110 ? 1.050   6.827   35.107  1.00 27.18 ? 107 PRO A CA  1 
ATOM   2782 C C   . PRO B  2 110 ? -0.130  7.126   36.031  1.00 28.33 ? 107 PRO A C   1 
ATOM   2783 O O   . PRO B  2 110 ? 0.070   7.181   37.243  1.00 29.69 ? 107 PRO A O   1 
ATOM   2784 C CB  . PRO B  2 110 ? 1.870   8.093   34.811  1.00 29.30 ? 107 PRO A CB  1 
ATOM   2785 C CG  . PRO B  2 110 ? 1.603   8.383   33.356  1.00 28.28 ? 107 PRO A CG  1 
ATOM   2786 C CD  . PRO B  2 110 ? 1.158   7.127   32.678  1.00 26.37 ? 107 PRO A CD  1 
ATOM   2787 N N   . ASN B  2 111 ? -1.324  7.325   35.482  1.00 28.08 ? 108 ASN A N   1 
ATOM   2788 C CA  . ASN B  2 111 ? -2.540  7.564   36.246  1.00 30.61 ? 108 ASN A CA  1 
ATOM   2789 C C   . ASN B  2 111 ? -3.372  6.327   36.577  1.00 27.05 ? 108 ASN A C   1 
ATOM   2790 O O   . ASN B  2 111 ? -4.369  6.492   37.279  1.00 26.79 ? 108 ASN A O   1 
ATOM   2791 C CB  . ASN B  2 111 ? -3.465  8.525   35.517  1.00 33.82 ? 108 ASN A CB  1 
ATOM   2792 C CG  . ASN B  2 111 ? -3.240  9.930   35.958  1.00 41.74 ? 108 ASN A CG  1 
ATOM   2793 O OD1 . ASN B  2 111 ? -4.219  10.601  36.316  1.00 55.17 ? 108 ASN A OD1 1 
ATOM   2794 N ND2 . ASN B  2 111 ? -1.988  10.358  35.946  1.00 45.57 ? 108 ASN A ND2 1 
ATOM   2795 N N   . ALA B  2 112 ? -3.004  5.143   36.094  1.00 25.52 ? 109 ALA A N   1 
ATOM   2796 C CA  . ALA B  2 112 ? -3.850  3.959   36.209  1.00 23.91 ? 109 ALA A CA  1 
ATOM   2797 C C   . ALA B  2 112 ? -3.822  3.492   37.663  1.00 25.51 ? 109 ALA A C   1 
ATOM   2798 O O   . ALA B  2 112 ? -2.798  2.966   38.111  1.00 27.64 ? 109 ALA A O   1 
ATOM   2799 C CB  . ALA B  2 112 ? -3.375  2.902   35.263  1.00 22.18 ? 109 ALA A CB  1 
ATOM   2800 N N   . SER B  2 113 ? -4.943  3.666   38.387  1.00 25.85 ? 110 SER A N   1 
ATOM   2801 C CA  . SER B  2 113 ? -5.022  3.473   39.831  1.00 26.50 ? 110 SER A CA  1 
ATOM   2802 C C   . SER B  2 113 ? -5.358  2.039   40.248  1.00 26.21 ? 110 SER A C   1 
ATOM   2803 O O   . SER B  2 113 ? -5.345  1.780   41.454  1.00 27.27 ? 110 SER A O   1 
ATOM   2804 C CB  . SER B  2 113 ? -5.963  4.488   40.424  1.00 27.27 ? 110 SER A CB  1 
ATOM   2805 O OG  . SER B  2 113 ? -7.278  4.171   40.030  1.00 26.54 ? 110 SER A OG  1 
ATOM   2806 N N   . GLN B  2 114 ? -5.672  1.140   39.312  1.00 25.58 ? 111 GLN A N   1 
ATOM   2807 C CA  . GLN B  2 114 ? -5.977  -0.262  39.571  1.00 26.03 ? 111 GLN A CA  1 
ATOM   2808 C C   . GLN B  2 114 ? -5.186  -1.158  38.634  1.00 23.46 ? 111 GLN A C   1 
ATOM   2809 O O   . GLN B  2 114 ? -4.796  -0.741  37.548  1.00 22.17 ? 111 GLN A O   1 
ATOM   2810 C CB  . GLN B  2 114 ? -7.463  -0.526  39.373  1.00 29.07 ? 111 GLN A CB  1 
ATOM   2811 C CG  . GLN B  2 114 ? -8.321  0.155   40.436  1.00 35.66 ? 111 GLN A CG  1 
ATOM   2812 C CD  . GLN B  2 114 ? -9.796  0.051   40.157  1.00 41.14 ? 111 GLN A CD  1 
ATOM   2813 O OE1 . GLN B  2 114 ? -10.238 0.112   38.994  1.00 41.55 ? 111 GLN A OE1 1 
ATOM   2814 N NE2 . GLN B  2 114 ? -10.552 -0.077  41.239  1.00 42.62 ? 111 GLN A NE2 1 
ATOM   2815 N N   . ALA B  2 115 ? -5.023  -2.424  39.054  1.00 22.78 ? 112 ALA A N   1 
ATOM   2816 C CA  . ALA B  2 115 ? -4.268  -3.399  38.281  1.00 23.41 ? 112 ALA A CA  1 
ATOM   2817 C C   . ALA B  2 115 ? -4.935  -3.621  36.936  1.00 22.87 ? 112 ALA A C   1 
ATOM   2818 O O   . ALA B  2 115 ? -4.218  -3.679  35.954  1.00 20.59 ? 112 ALA A O   1 
ATOM   2819 C CB  . ALA B  2 115 ? -4.130  -4.728  38.997  1.00 23.28 ? 112 ALA A CB  1 
ATOM   2820 N N   . GLU B  2 116 ? -6.286  -3.731  36.904  1.00 23.70 ? 113 GLU A N   1 
ATOM   2821 C CA  . GLU B  2 116 ? -6.978  -4.007  35.646  1.00 23.60 ? 113 GLU A CA  1 
ATOM   2822 C C   . GLU B  2 116 ? -6.654  -2.938  34.592  1.00 21.59 ? 113 GLU A C   1 
ATOM   2823 O O   . GLU B  2 116 ? -6.330  -3.305  33.477  1.00 22.54 ? 113 GLU A O   1 
ATOM   2824 C CB  . GLU B  2 116 ? -8.507  -3.985  35.774  1.00 27.80 ? 113 GLU A CB  1 
ATOM   2825 C CG  . GLU B  2 116 ? -9.128  -5.244  36.367  1.00 31.00 ? 113 GLU A CG  1 
ATOM   2826 C CD  . GLU B  2 116 ? -10.684 -5.155  36.471  1.00 35.35 ? 113 GLU A CD  1 
ATOM   2827 O OE1 . GLU B  2 116 ? -11.398 -4.435  35.695  1.00 31.10 ? 113 GLU A OE1 1 
ATOM   2828 O OE2 . GLU B  2 116 ? -11.221 -5.932  37.320  1.00 41.05 ? 113 GLU A OE2 1 
ATOM   2829 N N   . SER B  2 117 ? -6.746  -1.651  34.959  1.00 23.28 ? 114 SER A N   1 
ATOM   2830 C CA  . SER B  2 117 ? -6.503  -0.567  34.018  1.00 21.78 ? 114 SER A CA  1 
ATOM   2831 C C   . SER B  2 117 ? -5.027  -0.481  33.647  1.00 20.30 ? 114 SER A C   1 
ATOM   2832 O O   . SER B  2 117 ? -4.697  -0.232  32.493  1.00 18.85 ? 114 SER A O   1 
ATOM   2833 C CB  . SER B  2 117 ? -7.057  0.742   34.456  1.00 23.03 ? 114 SER A CB  1 
ATOM   2834 O OG  . SER B  2 117 ? -6.494  1.182   35.675  1.00 25.31 ? 114 SER A OG  1 
ATOM   2835 N N   . LYS B  2 118 ? -4.144  -0.712  34.617  1.00 21.61 ? 115 LYS A N   1 
ATOM   2836 C CA  . LYS B  2 118 ? -2.710  -0.695  34.374  1.00 20.96 ? 115 LYS A CA  1 
ATOM   2837 C C   . LYS B  2 118 ? -2.337  -1.759  33.361  1.00 19.02 ? 115 LYS A C   1 
ATOM   2838 O O   . LYS B  2 118 ? -1.634  -1.446  32.393  1.00 17.83 ? 115 LYS A O   1 
ATOM   2839 C CB  . LYS B  2 118 ? -1.913  -0.918  35.662  1.00 23.96 ? 115 LYS A CB  1 
ATOM   2840 C CG  . LYS B  2 118 ? -0.442  -0.576  35.507  1.00 27.16 ? 115 LYS A CG  1 
ATOM   2841 C CD  . LYS B  2 118 ? 0.246   -0.242  36.827  1.00 32.27 ? 115 LYS A CD  1 
ATOM   2842 C CE  . LYS B  2 118 ? 1.630   0.299   36.558  1.00 31.70 ? 115 LYS A CE  1 
ATOM   2843 N NZ  . LYS B  2 118 ? 2.335   0.303   37.821  1.00 32.50 ? 115 LYS A NZ  1 
ATOM   2844 N N   . VAL B  2 119 ? -2.851  -2.997  33.569  1.00 18.04 ? 116 VAL A N   1 
ATOM   2845 C CA  . VAL B  2 119 ? -2.620  -4.089  32.636  1.00 17.72 ? 116 VAL A CA  1 
ATOM   2846 C C   . VAL B  2 119 ? -3.205  -3.753  31.271  1.00 17.43 ? 116 VAL A C   1 
ATOM   2847 O O   . VAL B  2 119 ? -2.541  -4.012  30.284  1.00 15.97 ? 116 VAL A O   1 
ATOM   2848 C CB  . VAL B  2 119 ? -3.139  -5.441  33.192  1.00 18.28 ? 116 VAL A CB  1 
ATOM   2849 C CG1 . VAL B  2 119 ? -3.197  -6.585  32.186  1.00 17.26 ? 116 VAL A CG1 1 
ATOM   2850 C CG2 . VAL B  2 119 ? -2.329  -5.851  34.439  1.00 19.30 ? 116 VAL A CG2 1 
ATOM   2851 N N   . PHE B  2 120 ? -4.430  -3.226  31.220  1.00 17.96 ? 117 PHE A N   1 
ATOM   2852 C CA  . PHE B  2 120 ? -5.061  -2.856  29.959  1.00 17.06 ? 117 PHE A CA  1 
ATOM   2853 C C   . PHE B  2 120 ? -4.148  -1.935  29.167  1.00 16.93 ? 117 PHE A C   1 
ATOM   2854 O O   . PHE B  2 120 ? -3.957  -2.165  27.988  1.00 16.83 ? 117 PHE A O   1 
ATOM   2855 C CB  . PHE B  2 120 ? -6.378  -2.119  30.229  1.00 19.39 ? 117 PHE A CB  1 
ATOM   2856 C CG  . PHE B  2 120 ? -7.199  -1.771  29.007  1.00 20.35 ? 117 PHE A CG  1 
ATOM   2857 C CD1 . PHE B  2 120 ? -6.894  -0.666  28.214  1.00 20.00 ? 117 PHE A CD1 1 
ATOM   2858 C CD2 . PHE B  2 120 ? -8.235  -2.598  28.615  1.00 23.47 ? 117 PHE A CD2 1 
ATOM   2859 C CE1 . PHE B  2 120 ? -7.634  -0.372  27.091  1.00 21.36 ? 117 PHE A CE1 1 
ATOM   2860 C CE2 . PHE B  2 120 ? -9.004  -2.252  27.517  1.00 25.20 ? 117 PHE A CE2 1 
ATOM   2861 C CZ  . PHE B  2 120 ? -8.679  -1.163  26.756  1.00 23.01 ? 117 PHE A CZ  1 
ATOM   2862 N N   . TYR B  2 121 ? -3.566  -0.911  29.835  1.00 16.41 ? 118 TYR A N   1 
ATOM   2863 C CA  . TYR B  2 121 ? -2.747  0.073   29.135  1.00 15.88 ? 118 TYR A CA  1 
ATOM   2864 C C   . TYR B  2 121 ? -1.375  -0.485  28.785  1.00 15.19 ? 118 TYR A C   1 
ATOM   2865 O O   . TYR B  2 121 ? -0.855  -0.088  27.759  1.00 14.21 ? 118 TYR A O   1 
ATOM   2866 C CB  . TYR B  2 121 ? -2.625  1.347   29.959  1.00 16.71 ? 118 TYR A CB  1 
ATOM   2867 C CG  . TYR B  2 121 ? -3.932  2.083   30.216  1.00 17.17 ? 118 TYR A CG  1 
ATOM   2868 C CD1 . TYR B  2 121 ? -4.837  2.371   29.168  1.00 17.04 ? 118 TYR A CD1 1 
ATOM   2869 C CD2 . TYR B  2 121 ? -4.253  2.511   31.510  1.00 18.06 ? 118 TYR A CD2 1 
ATOM   2870 C CE1 . TYR B  2 121 ? -5.993  3.104   29.415  1.00 17.09 ? 118 TYR A CE1 1 
ATOM   2871 C CE2 . TYR B  2 121 ? -5.437  3.206   31.783  1.00 18.86 ? 118 TYR A CE2 1 
ATOM   2872 C CZ  . TYR B  2 121 ? -6.302  3.501   30.716  1.00 19.03 ? 118 TYR A CZ  1 
ATOM   2873 O OH  . TYR B  2 121 ? -7.457  4.193   30.963  1.00 19.55 ? 118 TYR A OH  1 
ATOM   2874 N N   . LEU B  2 122 ? -0.778  -1.319  29.652  1.00 16.37 ? 119 LEU A N   1 
ATOM   2875 C CA  . LEU B  2 122 ? 0.509   -1.937  29.335  1.00 16.73 ? 119 LEU A CA  1 
ATOM   2876 C C   . LEU B  2 122 ? 0.363   -2.908  28.167  1.00 15.68 ? 119 LEU A C   1 
ATOM   2877 O O   . LEU B  2 122 ? 1.216   -2.949  27.284  1.00 14.63 ? 119 LEU A O   1 
ATOM   2878 C CB  . LEU B  2 122 ? 1.132   -2.592  30.567  1.00 17.99 ? 119 LEU A CB  1 
ATOM   2879 C CG  . LEU B  2 122 ? 1.724   -1.627  31.589  1.00 19.75 ? 119 LEU A CG  1 
ATOM   2880 C CD1 . LEU B  2 122 ? 2.096   -2.407  32.830  1.00 20.58 ? 119 LEU A CD1 1 
ATOM   2881 C CD2 . LEU B  2 122 ? 2.960   -0.955  31.051  1.00 19.86 ? 119 LEU A CD2 1 
ATOM   2882 N N   . LYS B  2 123 ? -0.751  -3.646  28.138  1.00 14.20 ? 120 LYS A N   1 
ATOM   2883 C CA  . LYS B  2 123 ? -1.084  -4.478  26.973  1.00 14.12 ? 120 LYS A CA  1 
ATOM   2884 C C   . LYS B  2 123 ? -1.230  -3.636  25.719  1.00 13.89 ? 120 LYS A C   1 
ATOM   2885 O O   . LYS B  2 123 ? -0.666  -3.967  24.662  1.00 15.07 ? 120 LYS A O   1 
ATOM   2886 C CB  . LYS B  2 123 ? -2.419  -5.190  27.198  1.00 14.25 ? 120 LYS A CB  1 
ATOM   2887 C CG  . LYS B  2 123 ? -2.894  -6.056  26.065  1.00 14.64 ? 120 LYS A CG  1 
ATOM   2888 C CD  . LYS B  2 123 ? -4.272  -6.636  26.316  1.00 15.15 ? 120 LYS A CD  1 
ATOM   2889 C CE  . LYS B  2 123 ? -5.028  -6.881  25.001  1.00 15.18 ? 120 LYS A CE  1 
ATOM   2890 N NZ  . LYS B  2 123 ? -5.268  -5.668  24.191  1.00 14.45 ? 120 LYS A NZ  1 
ATOM   2891 N N   . MET B  2 124 ? -1.938  -2.518  25.826  1.00 15.83 ? 121 MET A N   1 
ATOM   2892 C CA  . MET B  2 124 ? -2.134  -1.621  24.683  1.00 15.98 ? 121 MET A CA  1 
ATOM   2893 C C   . MET B  2 124 ? -0.794  -1.069  24.178  1.00 15.04 ? 121 MET A C   1 
ATOM   2894 O O   . MET B  2 124 ? -0.566  -1.044  22.948  1.00 14.17 ? 121 MET A O   1 
ATOM   2895 C CB  . MET B  2 124 ? -3.107  -0.506  25.036  1.00 16.53 ? 121 MET A CB  1 
ATOM   2896 C CG  . MET B  2 124 ? -3.582  0.345   23.856  1.00 19.50 ? 121 MET A CG  1 
ATOM   2897 S SD  . MET B  2 124 ? -4.803  1.558   24.430  1.00 21.99 ? 121 MET A SD  1 
ATOM   2898 C CE  . MET B  2 124 ? -5.456  1.958   22.810  1.00 19.76 ? 121 MET A CE  1 
ATOM   2899 N N   . LYS B  2 125 ? 0.118   -0.693  25.107  1.00 15.58 ? 122 LYS A N   1 
ATOM   2900 C CA  . LYS B  2 125 ? 1.468   -0.279  24.735  1.00 16.35 ? 122 LYS A CA  1 
ATOM   2901 C C   . LYS B  2 125 ? 2.225   -1.360  23.950  1.00 16.37 ? 122 LYS A C   1 
ATOM   2902 O O   . LYS B  2 125 ? 2.842   -1.089  22.912  1.00 16.55 ? 122 LYS A O   1 
ATOM   2903 C CB  . LYS B  2 125 ? 2.231   0.111   26.012  1.00 16.64 ? 122 LYS A CB  1 
ATOM   2904 C CG  . LYS B  2 125 ? 3.643   0.669   25.796  1.00 16.50 ? 122 LYS A CG  1 
ATOM   2905 C CD  . LYS B  2 125 ? 4.232   1.194   27.091  1.00 17.97 ? 122 LYS A CD  1 
ATOM   2906 C CE  . LYS B  2 125 ? 5.616   1.648   26.843  1.00 19.41 ? 122 LYS A CE  1 
ATOM   2907 N NZ  . LYS B  2 125 ? 6.273   2.180   28.047  1.00 20.98 ? 122 LYS A NZ  1 
ATOM   2908 N N   . GLY B  2 126 ? 2.128   -2.593  24.450  1.00 16.02 ? 123 GLY A N   1 
ATOM   2909 C CA  . GLY B  2 126 ? 2.678   -3.779  23.796  1.00 16.55 ? 123 GLY A CA  1 
ATOM   2910 C C   . GLY B  2 126 ? 2.064   -3.945  22.402  1.00 14.73 ? 123 GLY A C   1 
ATOM   2911 O O   . GLY B  2 126 ? 2.836   -4.130  21.455  1.00 16.91 ? 123 GLY A O   1 
ATOM   2912 N N   . ASP B  2 127 ? 0.739   -3.753  22.276  1.00 13.89 ? 124 ASP A N   1 
ATOM   2913 C CA  . ASP B  2 127 ? 0.040   -3.866  21.018  1.00 15.50 ? 124 ASP A CA  1 
ATOM   2914 C C   . ASP B  2 127 ? 0.535   -2.844  19.974  1.00 17.31 ? 124 ASP A C   1 
ATOM   2915 O O   . ASP B  2 127 ? 0.760   -3.234  18.822  1.00 15.29 ? 124 ASP A O   1 
ATOM   2916 C CB  . ASP B  2 127 ? -1.467  -3.754  21.143  1.00 16.01 ? 124 ASP A CB  1 
ATOM   2917 C CG  . ASP B  2 127 ? -2.154  -4.858  21.908  1.00 15.96 ? 124 ASP A CG  1 
ATOM   2918 O OD1 . ASP B  2 127 ? -1.643  -5.992  21.914  1.00 17.86 ? 124 ASP A OD1 1 
ATOM   2919 O OD2 . ASP B  2 127 ? -3.186  -4.542  22.483  1.00 15.47 ? 124 ASP A OD2 1 
ATOM   2920 N N   . TYR B  2 128 ? 0.649   -1.562  20.352  1.00 17.72 ? 125 TYR A N   1 
ATOM   2921 C CA  . TYR B  2 128 ? 0.960   -0.506  19.399  1.00 16.56 ? 125 TYR A CA  1 
ATOM   2922 C C   . TYR B  2 128 ? 2.435   -0.555  19.002  1.00 18.14 ? 125 TYR A C   1 
ATOM   2923 O O   . TYR B  2 128 ? 2.746   -0.225  17.849  1.00 17.52 ? 125 TYR A O   1 
ATOM   2924 C CB  . TYR B  2 128 ? 0.410   0.856   19.864  1.00 17.16 ? 125 TYR A CB  1 
ATOM   2925 C CG  . TYR B  2 128 ? -1.066  0.899   19.521  1.00 15.82 ? 125 TYR A CG  1 
ATOM   2926 C CD1 . TYR B  2 128 ? -2.005  0.317   20.365  1.00 15.50 ? 125 TYR A CD1 1 
ATOM   2927 C CD2 . TYR B  2 128 ? -1.550  1.454   18.342  1.00 16.92 ? 125 TYR A CD2 1 
ATOM   2928 C CE1 . TYR B  2 128 ? -3.363  0.267   20.064  1.00 16.91 ? 125 TYR A CE1 1 
ATOM   2929 C CE2 . TYR B  2 128 ? -2.902  1.404   18.005  1.00 15.98 ? 125 TYR A CE2 1 
ATOM   2930 C CZ  . TYR B  2 128 ? -3.815  0.764   18.858  1.00 16.06 ? 125 TYR A CZ  1 
ATOM   2931 O OH  . TYR B  2 128 ? -5.138  0.703   18.615  1.00 18.08 ? 125 TYR A OH  1 
ATOM   2932 N N   . TYR B  2 129 ? 3.338   -0.945  19.918  1.00 16.15 ? 126 TYR A N   1 
ATOM   2933 C CA  . TYR B  2 129 ? 4.708   -1.264  19.529  1.00 17.43 ? 126 TYR A CA  1 
ATOM   2934 C C   . TYR B  2 129 ? 4.746   -2.500  18.641  1.00 15.76 ? 126 TYR A C   1 
ATOM   2935 O O   . TYR B  2 129 ? 5.572   -2.561  17.740  1.00 15.93 ? 126 TYR A O   1 
ATOM   2936 C CB  . TYR B  2 129 ? 5.639   -1.435  20.723  1.00 18.79 ? 126 TYR A CB  1 
ATOM   2937 C CG  . TYR B  2 129 ? 6.165   -0.118  21.245  1.00 20.00 ? 126 TYR A CG  1 
ATOM   2938 C CD1 . TYR B  2 129 ? 7.107   0.596   20.509  1.00 21.15 ? 126 TYR A CD1 1 
ATOM   2939 C CD2 . TYR B  2 129 ? 5.771   0.407   22.483  1.00 20.72 ? 126 TYR A CD2 1 
ATOM   2940 C CE1 . TYR B  2 129 ? 7.655   1.769   21.004  1.00 22.85 ? 126 TYR A CE1 1 
ATOM   2941 C CE2 . TYR B  2 129 ? 6.286   1.606   22.968  1.00 23.17 ? 126 TYR A CE2 1 
ATOM   2942 C CZ  . TYR B  2 129 ? 7.213   2.296   22.210  1.00 24.13 ? 126 TYR A CZ  1 
ATOM   2943 O OH  . TYR B  2 129 ? 7.805   3.414   22.638  1.00 23.31 ? 126 TYR A OH  1 
ATOM   2944 N N   . ARG B  2 130 ? 3.883   -3.496  18.888  1.00 14.35 ? 127 ARG A N   1 
ATOM   2945 C CA  . ARG B  2 130 ? 3.788   -4.652  18.022  1.00 13.82 ? 127 ARG A CA  1 
ATOM   2946 C C   . ARG B  2 130 ? 3.373   -4.256  16.607  1.00 15.03 ? 127 ARG A C   1 
ATOM   2947 O O   . ARG B  2 130 ? 3.940   -4.811  15.649  1.00 15.69 ? 127 ARG A O   1 
ATOM   2948 C CB  . ARG B  2 130 ? 2.858   -5.730  18.575  1.00 14.19 ? 127 ARG A CB  1 
ATOM   2949 C CG  . ARG B  2 130 ? 2.683   -6.929  17.675  1.00 13.34 ? 127 ARG A CG  1 
ATOM   2950 C CD  . ARG B  2 130 ? 2.068   -8.125  18.387  1.00 13.53 ? 127 ARG A CD  1 
ATOM   2951 N NE  . ARG B  2 130 ? 0.754   -7.819  18.974  1.00 13.59 ? 127 ARG A NE  1 
ATOM   2952 C CZ  . ARG B  2 130 ? -0.399  -7.761  18.336  1.00 13.57 ? 127 ARG A CZ  1 
ATOM   2953 N NH1 . ARG B  2 130 ? -0.490  -8.127  17.049  1.00 12.56 ? 127 ARG A NH1 1 
ATOM   2954 N NH2 . ARG B  2 130 ? -1.446  -7.381  19.017  1.00 13.63 ? 127 ARG A NH2 1 
ATOM   2955 N N   . TYR B  2 131 ? 2.399   -3.355  16.487  1.00 15.74 ? 128 TYR A N   1 
ATOM   2956 C CA  . TYR B  2 131 ? 2.000   -2.865  15.163  1.00 15.48 ? 128 TYR A CA  1 
ATOM   2957 C C   . TYR B  2 131 ? 3.139   -2.141  14.476  1.00 15.90 ? 128 TYR A C   1 
ATOM   2958 O O   . TYR B  2 131 ? 3.334   -2.365  13.281  1.00 20.00 ? 128 TYR A O   1 
ATOM   2959 C CB  . TYR B  2 131 ? 0.716   -2.035  15.259  1.00 15.99 ? 128 TYR A CB  1 
ATOM   2960 C CG  . TYR B  2 131 ? -0.464  -2.721  15.947  1.00 14.97 ? 128 TYR A CG  1 
ATOM   2961 C CD1 . TYR B  2 131 ? -0.701  -4.091  15.883  1.00 14.54 ? 128 TYR A CD1 1 
ATOM   2962 C CD2 . TYR B  2 131 ? -1.413  -1.956  16.616  1.00 13.86 ? 128 TYR A CD2 1 
ATOM   2963 C CE1 . TYR B  2 131 ? -1.746  -4.707  16.560  1.00 13.70 ? 128 TYR A CE1 1 
ATOM   2964 C CE2 . TYR B  2 131 ? -2.491  -2.532  17.239  1.00 12.90 ? 128 TYR A CE2 1 
ATOM   2965 C CZ  . TYR B  2 131 ? -2.681  -3.910  17.216  1.00 13.55 ? 128 TYR A CZ  1 
ATOM   2966 O OH  . TYR B  2 131 ? -3.721  -4.484  17.888  1.00 15.59 ? 128 TYR A OH  1 
ATOM   2967 N N   . LEU B  2 132 ? 3.913   -1.334  15.201  1.00 15.59 ? 129 LEU A N   1 
ATOM   2968 C CA  . LEU B  2 132 ? 5.171   -0.786  14.694  1.00 17.28 ? 129 LEU A CA  1 
ATOM   2969 C C   . LEU B  2 132 ? 6.146   -1.885  14.236  1.00 16.78 ? 129 LEU A C   1 
ATOM   2970 O O   . LEU B  2 132 ? 6.719   -1.762  13.169  1.00 17.88 ? 129 LEU A O   1 
ATOM   2971 C CB  . LEU B  2 132 ? 5.838   0.175   15.684  1.00 18.10 ? 129 LEU A CB  1 
ATOM   2972 C CG  . LEU B  2 132 ? 5.094   1.487   15.985  1.00 20.00 ? 129 LEU A CG  1 
ATOM   2973 C CD1 . LEU B  2 132 ? 5.797   2.303   17.067  1.00 21.26 ? 129 LEU A CD1 1 
ATOM   2974 C CD2 . LEU B  2 132 ? 4.931   2.370   14.755  1.00 22.34 ? 129 LEU A CD2 1 
ATOM   2975 N N   . ALA B  2 133 ? 6.290   -2.962  15.003  1.00 16.93 ? 130 ALA A N   1 
ATOM   2976 C CA  . ALA B  2 133 ? 7.213   -4.055  14.675  1.00 18.02 ? 130 ALA A CA  1 
ATOM   2977 C C   . ALA B  2 133 ? 6.812   -4.807  13.405  1.00 17.88 ? 130 ALA A C   1 
ATOM   2978 O O   . ALA B  2 133 ? 7.692   -5.306  12.679  1.00 17.77 ? 130 ALA A O   1 
ATOM   2979 C CB  . ALA B  2 133 ? 7.296   -5.041  15.843  1.00 17.92 ? 130 ALA A CB  1 
ATOM   2980 N N   . GLU B  2 134 ? 5.501   -4.837  13.103  1.00 16.47 ? 131 GLU A N   1 
ATOM   2981 C CA  . GLU B  2 134 ? 5.024   -5.421  11.848  1.00 18.34 ? 131 GLU A CA  1 
ATOM   2982 C C   . GLU B  2 134 ? 5.591   -4.753  10.591  1.00 20.39 ? 131 GLU A C   1 
ATOM   2983 O O   . GLU B  2 134 ? 5.658   -5.428  9.580   1.00 20.44 ? 131 GLU A O   1 
ATOM   2984 C CB  . GLU B  2 134 ? 3.487   -5.415  11.721  1.00 18.05 ? 131 GLU A CB  1 
ATOM   2985 C CG  . GLU B  2 134 ? 2.736   -6.257  12.754  1.00 17.26 ? 131 GLU A CG  1 
ATOM   2986 C CD  . GLU B  2 134 ? 1.228   -6.085  12.793  1.00 17.43 ? 131 GLU A CD  1 
ATOM   2987 O OE1 . GLU B  2 134 ? 0.689   -5.235  12.066  1.00 15.89 ? 131 GLU A OE1 1 
ATOM   2988 O OE2 . GLU B  2 134 ? 0.614   -6.959  13.389  1.00 18.78 ? 131 GLU A OE2 1 
ATOM   2989 N N   . VAL B  2 135 ? 5.977   -3.467  10.637  1.00 20.11 ? 132 VAL A N   1 
ATOM   2990 C CA  . VAL B  2 135 ? 6.473   -2.760  9.462   1.00 23.30 ? 132 VAL A CA  1 
ATOM   2991 C C   . VAL B  2 135 ? 7.948   -2.362  9.590   1.00 24.88 ? 132 VAL A C   1 
ATOM   2992 O O   . VAL B  2 135 ? 8.522   -2.018  8.584   1.00 26.12 ? 132 VAL A O   1 
ATOM   2993 C CB  . VAL B  2 135 ? 5.547   -1.579  9.136   1.00 25.42 ? 132 VAL A CB  1 
ATOM   2994 C CG1 . VAL B  2 135 ? 4.106   -2.077  9.020   1.00 23.92 ? 132 VAL A CG1 1 
ATOM   2995 C CG2 . VAL B  2 135 ? 5.671   -0.416  10.121  1.00 29.92 ? 132 VAL A CG2 1 
ATOM   2996 N N   . ALA B  2 136 ? 8.536   -2.368  10.786  1.00 24.39 ? 133 ALA A N   1 
ATOM   2997 C CA  . ALA B  2 136 ? 9.872   -1.805  10.992  1.00 27.49 ? 133 ALA A CA  1 
ATOM   2998 C C   . ALA B  2 136 ? 10.935  -2.720  10.358  1.00 30.93 ? 133 ALA A C   1 
ATOM   2999 O O   . ALA B  2 136 ? 10.788  -3.936  10.401  1.00 32.54 ? 133 ALA A O   1 
ATOM   3000 C CB  . ALA B  2 136 ? 10.114  -1.606  12.489  1.00 28.69 ? 133 ALA A CB  1 
ATOM   3001 N N   . ALA B  2 137 ? 11.995  -2.125  9.801   1.00 35.69 ? 134 ALA A N   1 
ATOM   3002 C CA  . ALA B  2 137 ? 13.122  -2.842  9.212   1.00 43.39 ? 134 ALA A CA  1 
ATOM   3003 C C   . ALA B  2 137 ? 14.364  -1.969  9.335   1.00 52.17 ? 134 ALA A C   1 
ATOM   3004 O O   . ALA B  2 137 ? 14.486  -1.015  8.581   1.00 62.64 ? 134 ALA A O   1 
ATOM   3005 C CB  . ALA B  2 137 ? 12.820  -3.180  7.763   1.00 43.71 ? 134 ALA A CB  1 
ATOM   3006 N N   . GLY B  2 138 ? 15.197  -2.203  10.356  1.00 63.25 ? 135 GLY A N   1 
ATOM   3007 C CA  . GLY B  2 138 ? 16.546  -1.640  10.389  1.00 65.57 ? 135 GLY A CA  1 
ATOM   3008 C C   . GLY B  2 138 ? 17.087  -1.567  11.806  1.00 71.79 ? 135 GLY A C   1 
ATOM   3009 O O   . GLY B  2 138 ? 16.788  -2.454  12.609  1.00 75.50 ? 135 GLY A O   1 
ATOM   3010 N N   . ASP B  2 139 ? 17.844  -0.493  12.107  1.00 75.70 ? 136 ASP A N   1 
ATOM   3011 C CA  . ASP B  2 139 ? 18.366  -0.253  13.457  1.00 72.90 ? 136 ASP A CA  1 
ATOM   3012 C C   . ASP B  2 139 ? 17.202  -0.109  14.459  1.00 59.44 ? 136 ASP A C   1 
ATOM   3013 O O   . ASP B  2 139 ? 17.246  -0.737  15.520  1.00 60.49 ? 136 ASP A O   1 
ATOM   3014 C CB  . ASP B  2 139 ? 19.464  0.814   13.468  1.00 70.53 ? 136 ASP A CB  1 
ATOM   3015 N N   . ASP B  2 140 ? 16.106  0.586   14.073  1.00 54.72 ? 137 ASP A N   1 
ATOM   3016 C CA  . ASP B  2 140 ? 15.003  0.847   14.999  1.00 46.35 ? 137 ASP A CA  1 
ATOM   3017 C C   . ASP B  2 140 ? 14.149  -0.393  15.289  1.00 40.19 ? 137 ASP A C   1 
ATOM   3018 O O   . ASP B  2 140 ? 13.408  -0.307  16.244  1.00 32.07 ? 137 ASP A O   1 
ATOM   3019 C CB  . ASP B  2 140 ? 14.181  2.071   14.624  1.00 48.67 ? 137 ASP A CB  1 
ATOM   3020 C CG  . ASP B  2 140 ? 13.116  1.862   13.560  1.00 53.66 ? 137 ASP A CG  1 
ATOM   3021 O OD1 . ASP B  2 140 ? 13.352  1.008   12.661  1.00 61.02 ? 137 ASP A OD1 1 
ATOM   3022 O OD2 . ASP B  2 140 ? 12.077  2.564   13.613  1.00 50.53 ? 137 ASP A OD2 1 
ATOM   3023 N N   . LYS B  2 141 ? 14.186  -1.479  14.486  1.00 37.35 ? 138 LYS A N   1 
ATOM   3024 C CA  . LYS B  2 141 ? 13.337  -2.650  14.703  1.00 35.96 ? 138 LYS A CA  1 
ATOM   3025 C C   . LYS B  2 141 ? 13.607  -3.293  16.064  1.00 31.73 ? 138 LYS A C   1 
ATOM   3026 O O   . LYS B  2 141 ? 12.674  -3.649  16.796  1.00 27.81 ? 138 LYS A O   1 
ATOM   3027 C CB  . LYS B  2 141 ? 13.544  -3.747  13.646  1.00 41.25 ? 138 LYS A CB  1 
ATOM   3028 C CG  . LYS B  2 141 ? 12.553  -4.927  13.795  1.00 45.29 ? 138 LYS A CG  1 
ATOM   3029 C CD  . LYS B  2 141 ? 12.424  -5.826  12.569  1.00 51.45 ? 138 LYS A CD  1 
ATOM   3030 C CE  . LYS B  2 141 ? 11.085  -6.525  12.433  1.00 49.03 ? 138 LYS A CE  1 
ATOM   3031 N NZ  . LYS B  2 141 ? 11.210  -7.949  12.718  1.00 45.91 ? 138 LYS A NZ  1 
ATOM   3032 N N   . LYS B  2 142 ? 14.901  -3.482  16.357  1.00 33.48 ? 139 LYS A N   1 
ATOM   3033 C CA  . LYS B  2 142 ? 15.334  -4.040  17.636  1.00 36.62 ? 139 LYS A CA  1 
ATOM   3034 C C   . LYS B  2 142 ? 14.739  -3.276  18.815  1.00 30.26 ? 139 LYS A C   1 
ATOM   3035 O O   . LYS B  2 142 ? 14.167  -3.896  19.696  1.00 28.44 ? 139 LYS A O   1 
ATOM   3036 C CB  . LYS B  2 142 ? 16.864  -4.060  17.756  1.00 42.44 ? 139 LYS A CB  1 
ATOM   3037 C CG  . LYS B  2 142 ? 17.367  -4.891  18.924  1.00 52.67 ? 139 LYS A CG  1 
ATOM   3038 C CD  . LYS B  2 142 ? 18.850  -4.762  19.272  1.00 59.24 ? 139 LYS A CD  1 
ATOM   3039 C CE  . LYS B  2 142 ? 19.221  -5.749  20.351  1.00 65.39 ? 139 LYS A CE  1 
ATOM   3040 N NZ  . LYS B  2 142 ? 18.386  -5.672  21.563  1.00 68.33 ? 139 LYS A NZ  1 
ATOM   3041 N N   . GLY B  2 143 ? 14.839  -1.943  18.791  1.00 30.44 ? 140 GLY A N   1 
ATOM   3042 C CA  . GLY B  2 143 ? 14.267  -1.050  19.791  1.00 29.38 ? 140 GLY A CA  1 
ATOM   3043 C C   . GLY B  2 143 ? 12.761  -1.237  19.954  1.00 26.60 ? 140 GLY A C   1 
ATOM   3044 O O   . GLY B  2 143 ? 12.262  -1.337  21.076  1.00 25.45 ? 140 GLY A O   1 
ATOM   3045 N N   . ILE B  2 144 ? 12.055  -1.278  18.822  1.00 23.80 ? 141 ILE A N   1 
ATOM   3046 C CA  . ILE B  2 144 ? 10.615  -1.386  18.807  1.00 22.57 ? 141 ILE A CA  1 
ATOM   3047 C C   . ILE B  2 144 ? 10.152  -2.715  19.438  1.00 21.65 ? 141 ILE A C   1 
ATOM   3048 O O   . ILE B  2 144 ? 9.225   -2.730  20.259  1.00 21.37 ? 141 ILE A O   1 
ATOM   3049 C CB  . ILE B  2 144 ? 10.099  -1.120  17.370  1.00 21.46 ? 141 ILE A CB  1 
ATOM   3050 C CG1 . ILE B  2 144 ? 10.226  0.382   17.053  1.00 23.20 ? 141 ILE A CG1 1 
ATOM   3051 C CG2 . ILE B  2 144 ? 8.697   -1.634  17.149  1.00 18.88 ? 141 ILE A CG2 1 
ATOM   3052 C CD1 . ILE B  2 144 ? 10.085  0.759   15.591  1.00 23.85 ? 141 ILE A CD1 1 
ATOM   3053 N N   . VAL B  2 145 ? 10.776  -3.818  19.003  1.00 22.25 ? 142 VAL A N   1 
ATOM   3054 C CA  . VAL B  2 145 ? 10.435  -5.143  19.484  1.00 21.84 ? 142 VAL A CA  1 
ATOM   3055 C C   . VAL B  2 145 ? 10.676  -5.223  20.995  1.00 21.12 ? 142 VAL A C   1 
ATOM   3056 O O   . VAL B  2 145 ? 9.824   -5.760  21.685  1.00 20.22 ? 142 VAL A O   1 
ATOM   3057 C CB  . VAL B  2 145 ? 11.208  -6.231  18.681  1.00 23.90 ? 142 VAL A CB  1 
ATOM   3058 C CG1 . VAL B  2 145 ? 11.103  -7.639  19.306  1.00 24.82 ? 142 VAL A CG1 1 
ATOM   3059 C CG2 . VAL B  2 145 ? 10.877  -6.242  17.173  1.00 22.14 ? 142 VAL A CG2 1 
ATOM   3060 N N   A ASP B  2 146 ? 11.835  -4.746  21.492  0.50 21.37 ? 143 ASP A N   1 
ATOM   3061 N N   B ASP B  2 146 ? 11.832  -4.729  21.473  0.50 22.93 ? 143 ASP A N   1 
ATOM   3062 C CA  A ASP B  2 146 ? 12.164  -4.733  22.916  0.50 21.41 ? 143 ASP A CA  1 
ATOM   3063 C CA  B ASP B  2 146 ? 12.177  -4.693  22.887  0.50 24.19 ? 143 ASP A CA  1 
ATOM   3064 C C   A ASP B  2 146 ? 11.118  -3.960  23.734  0.50 21.26 ? 143 ASP A C   1 
ATOM   3065 C C   B ASP B  2 146 ? 11.141  -3.949  23.732  0.50 22.84 ? 143 ASP A C   1 
ATOM   3066 O O   A ASP B  2 146 ? 10.691  -4.458  24.777  0.50 21.18 ? 143 ASP A O   1 
ATOM   3067 O O   B ASP B  2 146 ? 10.767  -4.450  24.794  0.50 22.79 ? 143 ASP A O   1 
ATOM   3068 C CB  A ASP B  2 146 ? 13.591  -4.242  23.180  0.50 22.31 ? 143 ASP A CB  1 
ATOM   3069 C CB  B ASP B  2 146 ? 13.539  -4.058  23.114  0.50 27.23 ? 143 ASP A CB  1 
ATOM   3070 C CG  A ASP B  2 146 ? 14.736  -5.140  22.709  0.50 22.60 ? 143 ASP A CG  1 
ATOM   3071 C CG  B ASP B  2 146 ? 14.020  -4.124  24.553  0.50 29.86 ? 143 ASP A CG  1 
ATOM   3072 O OD1 A ASP B  2 146 ? 14.471  -6.283  22.302  0.50 22.07 ? 143 ASP A OD1 1 
ATOM   3073 O OD1 B ASP B  2 146 ? 13.979  -5.225  25.139  0.50 31.28 ? 143 ASP A OD1 1 
ATOM   3074 O OD2 A ASP B  2 146 ? 15.893  -4.669  22.673  0.50 23.11 ? 143 ASP A OD2 1 
ATOM   3075 O OD2 B ASP B  2 146 ? 14.422  -3.067  25.077  0.50 33.36 ? 143 ASP A OD2 1 
ATOM   3076 N N   . GLN B  2 147 ? 10.647  -2.806  23.216  1.00 21.03 ? 144 GLN A N   1 
ATOM   3077 C CA  . GLN B  2 147 ? 9.600   -2.027  23.868  1.00 21.68 ? 144 GLN A CA  1 
ATOM   3078 C C   . GLN B  2 147 ? 8.290   -2.814  23.958  1.00 20.04 ? 144 GLN A C   1 
ATOM   3079 O O   . GLN B  2 147 ? 7.667   -2.820  25.009  1.00 20.35 ? 144 GLN A O   1 
ATOM   3080 C CB  . GLN B  2 147 ? 9.331   -0.686  23.174  1.00 22.45 ? 144 GLN A CB  1 
ATOM   3081 C CG  . GLN B  2 147 ? 10.432  0.368   23.290  1.00 24.97 ? 144 GLN A CG  1 
ATOM   3082 C CD  . GLN B  2 147 ? 10.604  0.873   24.704  1.00 29.57 ? 144 GLN A CD  1 
ATOM   3083 O OE1 . GLN B  2 147 ? 9.644   1.258   25.383  1.00 29.03 ? 144 GLN A OE1 1 
ATOM   3084 N NE2 . GLN B  2 147 ? 11.819  0.744   25.218  1.00 35.40 ? 144 GLN A NE2 1 
ATOM   3085 N N   . SER B  2 148 ? 7.889   -3.493  22.873  1.00 18.74 ? 145 SER A N   1 
ATOM   3086 C CA  . SER B  2 148 ? 6.682   -4.293  22.873  1.00 17.78 ? 145 SER A CA  1 
ATOM   3087 C C   . SER B  2 148 ? 6.756   -5.390  23.933  1.00 18.59 ? 145 SER A C   1 
ATOM   3088 O O   . SER B  2 148 ? 5.844   -5.535  24.758  1.00 16.21 ? 145 SER A O   1 
ATOM   3089 C CB  . SER B  2 148 ? 6.402   -4.897  21.486  1.00 16.69 ? 145 SER A CB  1 
ATOM   3090 O OG  . SER B  2 148 ? 5.177   -5.616  21.474  1.00 15.70 ? 145 SER A OG  1 
ATOM   3091 N N   . GLN B  2 149 ? 7.873   -6.105  23.934  1.00 18.57 ? 146 GLN A N   1 
ATOM   3092 C CA  . GLN B  2 149 ? 8.048   -7.249  24.813  1.00 20.16 ? 146 GLN A CA  1 
ATOM   3093 C C   . GLN B  2 149 ? 8.055   -6.804  26.286  1.00 19.93 ? 146 GLN A C   1 
ATOM   3094 O O   . GLN B  2 149 ? 7.428   -7.492  27.091  1.00 19.13 ? 146 GLN A O   1 
ATOM   3095 C CB  . GLN B  2 149 ? 9.316   -8.008  24.430  1.00 21.84 ? 146 GLN A CB  1 
ATOM   3096 C CG  . GLN B  2 149 ? 9.558   -9.238  25.300  1.00 25.08 ? 146 GLN A CG  1 
ATOM   3097 C CD  . GLN B  2 149 ? 10.532  -10.251 24.757  1.00 29.35 ? 146 GLN A CD  1 
ATOM   3098 O OE1 . GLN B  2 149 ? 10.616  -11.356 25.324  1.00 30.71 ? 146 GLN A OE1 1 
ATOM   3099 N NE2 . GLN B  2 149 ? 11.283  -9.906  23.711  1.00 28.90 ? 146 GLN A NE2 1 
ATOM   3100 N N   . GLN B  2 150 ? 8.750   -5.705  26.614  1.00 20.47 ? 147 GLN A N   1 
ATOM   3101 C CA  A GLN B  2 150 ? 8.884   -5.211  27.978  0.50 21.96 ? 147 GLN A CA  1 
ATOM   3102 C CA  B GLN B  2 150 ? 8.875   -5.270  27.995  0.50 20.90 ? 147 GLN A CA  1 
ATOM   3103 C C   . GLN B  2 150 ? 7.508   -4.793  28.487  1.00 20.35 ? 147 GLN A C   1 
ATOM   3104 O O   . GLN B  2 150 ? 7.215   -4.993  29.651  1.00 20.45 ? 147 GLN A O   1 
ATOM   3105 C CB  A GLN B  2 150 ? 9.922   -4.087  28.078  0.50 24.66 ? 147 GLN A CB  1 
ATOM   3106 C CB  B GLN B  2 150 ? 9.972   -4.225  28.204  0.50 22.06 ? 147 GLN A CB  1 
ATOM   3107 C CG  A GLN B  2 150 ? 9.757   -3.124  29.260  0.50 27.45 ? 147 GLN A CG  1 
ATOM   3108 C CG  B GLN B  2 150 ? 11.402  -4.723  27.993  0.50 23.13 ? 147 GLN A CG  1 
ATOM   3109 C CD  A GLN B  2 150 ? 10.948  -2.242  29.565  0.50 30.47 ? 147 GLN A CD  1 
ATOM   3110 C CD  B GLN B  2 150 ? 12.446  -3.621  28.062  0.50 25.83 ? 147 GLN A CD  1 
ATOM   3111 O OE1 A GLN B  2 150 ? 11.569  -2.364  30.626  0.50 29.63 ? 147 GLN A OE1 1 
ATOM   3112 O OE1 B GLN B  2 150 ? 12.226  -2.542  28.618  0.50 27.78 ? 147 GLN A OE1 1 
ATOM   3113 N NE2 A GLN B  2 150 ? 11.234  -1.312  28.658  0.50 31.34 ? 147 GLN A NE2 1 
ATOM   3114 N NE2 B GLN B  2 150 ? 13.642  -3.881  27.554  0.50 27.26 ? 147 GLN A NE2 1 
ATOM   3115 N N   . ALA B  2 151 ? 6.692   -4.167  27.617  1.00 18.18 ? 148 ALA A N   1 
ATOM   3116 C CA  . ALA B  2 151 ? 5.373   -3.697  28.007  1.00 18.00 ? 148 ALA A CA  1 
ATOM   3117 C C   . ALA B  2 151 ? 4.473   -4.905  28.273  1.00 16.54 ? 148 ALA A C   1 
ATOM   3118 O O   . ALA B  2 151 ? 3.823   -4.987  29.312  1.00 16.84 ? 148 ALA A O   1 
ATOM   3119 C CB  . ALA B  2 151 ? 4.838   -2.767  26.966  1.00 17.49 ? 148 ALA A CB  1 
ATOM   3120 N N   . TYR B  2 152 ? 4.490   -5.876  27.352  1.00 15.03 ? 149 TYR A N   1 
ATOM   3121 C CA  . TYR B  2 152 ? 3.760   -7.110  27.555  1.00 15.25 ? 149 TYR A CA  1 
ATOM   3122 C C   . TYR B  2 152 ? 4.209   -7.879  28.795  1.00 15.70 ? 149 TYR A C   1 
ATOM   3123 O O   . TYR B  2 152 ? 3.357   -8.393  29.509  1.00 15.91 ? 149 TYR A O   1 
ATOM   3124 C CB  . TYR B  2 152 ? 3.878   -8.000  26.317  1.00 15.46 ? 149 TYR A CB  1 
ATOM   3125 C CG  . TYR B  2 152 ? 3.031   -7.652  25.101  1.00 15.85 ? 149 TYR A CG  1 
ATOM   3126 C CD1 . TYR B  2 152 ? 1.652   -7.383  25.184  1.00 16.89 ? 149 TYR A CD1 1 
ATOM   3127 C CD2 . TYR B  2 152 ? 3.574   -7.745  23.812  1.00 16.17 ? 149 TYR A CD2 1 
ATOM   3128 C CE1 . TYR B  2 152 ? 0.893   -7.133  24.047  1.00 15.96 ? 149 TYR A CE1 1 
ATOM   3129 C CE2 . TYR B  2 152 ? 2.827   -7.491  22.674  1.00 16.09 ? 149 TYR A CE2 1 
ATOM   3130 C CZ  . TYR B  2 152 ? 1.467   -7.232  22.777  1.00 15.78 ? 149 TYR A CZ  1 
ATOM   3131 O OH  . TYR B  2 152 ? 0.793   -7.020  21.614  1.00 16.56 ? 149 TYR A OH  1 
ATOM   3132 N N   . GLN B  2 153 ? 5.526   -7.975  29.034  1.00 16.32 ? 150 GLN A N   1 
ATOM   3133 C CA  . GLN B  2 153 ? 6.046   -8.703  30.178  1.00 18.67 ? 150 GLN A CA  1 
ATOM   3134 C C   . GLN B  2 153 ? 5.562   -8.075  31.495  1.00 19.19 ? 150 GLN A C   1 
ATOM   3135 O O   . GLN B  2 153 ? 5.177   -8.795  32.414  1.00 20.96 ? 150 GLN A O   1 
ATOM   3136 C CB  . GLN B  2 153 ? 7.585   -8.706  30.130  1.00 19.81 ? 150 GLN A CB  1 
ATOM   3137 C CG  . GLN B  2 153 ? 8.247   -9.634  31.117  1.00 21.01 ? 150 GLN A CG  1 
ATOM   3138 C CD  . GLN B  2 153 ? 7.714   -11.047 31.109  1.00 23.30 ? 150 GLN A CD  1 
ATOM   3139 O OE1 . GLN B  2 153 ? 7.481   -11.647 32.160  1.00 27.54 ? 150 GLN A OE1 1 
ATOM   3140 N NE2 . GLN B  2 153 ? 7.528   -11.616 29.939  1.00 22.65 ? 150 GLN A NE2 1 
ATOM   3141 N N   . GLU B  2 154 ? 5.618   -6.755  31.594  1.00 20.38 ? 151 GLU A N   1 
ATOM   3142 C CA  . GLU B  2 154 ? 5.132   -6.061  32.785  1.00 21.64 ? 151 GLU A CA  1 
ATOM   3143 C C   . GLU B  2 154 ? 3.626   -6.277  33.005  1.00 20.51 ? 151 GLU A C   1 
ATOM   3144 O O   . GLU B  2 154 ? 3.227   -6.629  34.117  1.00 20.14 ? 151 GLU A O   1 
ATOM   3145 C CB  . GLU B  2 154 ? 5.496   -4.604  32.806  1.00 22.94 ? 151 GLU A CB  1 
ATOM   3146 C CG  . GLU B  2 154 ? 5.119   -3.942  34.132  1.00 26.19 ? 151 GLU A CG  1 
ATOM   3147 C CD  . GLU B  2 154 ? 5.434   -2.487  34.240  1.00 28.73 ? 151 GLU A CD  1 
ATOM   3148 O OE1 . GLU B  2 154 ? 5.938   -1.889  33.276  1.00 27.14 ? 151 GLU A OE1 1 
ATOM   3149 O OE2 . GLU B  2 154 ? 5.166   -2.003  35.361  1.00 31.92 ? 151 GLU A OE2 1 
ATOM   3150 N N   . ALA B  2 155 ? 2.835   -6.127  31.928  1.00 18.65 ? 152 ALA A N   1 
ATOM   3151 C CA  . ALA B  2 155 ? 1.408   -6.434  31.957  1.00 19.10 ? 152 ALA A CA  1 
ATOM   3152 C C   . ALA B  2 155 ? 1.184   -7.855  32.444  1.00 19.37 ? 152 ALA A C   1 
ATOM   3153 O O   . ALA B  2 155 ? 0.302   -8.052  33.265  1.00 20.36 ? 152 ALA A O   1 
ATOM   3154 C CB  . ALA B  2 155 ? 0.766   -6.273  30.574  1.00 17.21 ? 152 ALA A CB  1 
ATOM   3155 N N   . PHE B  2 156 ? 1.983   -8.824  31.948  1.00 18.28 ? 153 PHE A N   1 
ATOM   3156 C CA  . PHE B  2 156 ? 1.815   -10.235 32.228  1.00 18.29 ? 153 PHE A CA  1 
ATOM   3157 C C   . PHE B  2 156 ? 2.082   -10.534 33.706  1.00 19.46 ? 153 PHE A C   1 
ATOM   3158 O O   . PHE B  2 156 ? 1.358   -11.344 34.293  1.00 18.57 ? 153 PHE A O   1 
ATOM   3159 C CB  . PHE B  2 156 ? 2.748   -11.029 31.300  1.00 19.90 ? 153 PHE A CB  1 
ATOM   3160 C CG  . PHE B  2 156 ? 2.631   -12.537 31.363  1.00 20.87 ? 153 PHE A CG  1 
ATOM   3161 C CD1 . PHE B  2 156 ? 1.611   -13.193 30.673  1.00 22.45 ? 153 PHE A CD1 1 
ATOM   3162 C CD2 . PHE B  2 156 ? 3.506   -13.299 32.145  1.00 26.94 ? 153 PHE A CD2 1 
ATOM   3163 C CE1 . PHE B  2 156 ? 1.468   -14.583 30.739  1.00 23.57 ? 153 PHE A CE1 1 
ATOM   3164 C CE2 . PHE B  2 156 ? 3.381   -14.697 32.193  1.00 28.61 ? 153 PHE A CE2 1 
ATOM   3165 C CZ  . PHE B  2 156 ? 2.391   -15.341 31.451  1.00 25.84 ? 153 PHE A CZ  1 
ATOM   3166 N N   . GLU B  2 157 ? 3.155   -9.933  34.253  1.00 19.03 ? 154 GLU A N   1 
ATOM   3167 C CA  . GLU B  2 157 ? 3.530   -10.139 35.645  1.00 21.78 ? 154 GLU A CA  1 
ATOM   3168 C C   . GLU B  2 157 ? 2.469   -9.518  36.564  1.00 20.80 ? 154 GLU A C   1 
ATOM   3169 O O   . GLU B  2 157 ? 2.113   -10.156 37.547  1.00 21.86 ? 154 GLU A O   1 
ATOM   3170 C CB  . GLU B  2 157 ? 4.919   -9.560  35.925  1.00 24.81 ? 154 GLU A CB  1 
ATOM   3171 C CG  . GLU B  2 157 ? 6.054   -10.337 35.248  1.00 27.98 ? 154 GLU A CG  1 
ATOM   3172 C CD  . GLU B  2 157 ? 7.386   -9.582  35.186  1.00 31.92 ? 154 GLU A CD  1 
ATOM   3173 O OE1 . GLU B  2 157 ? 7.508   -8.402  35.594  1.00 38.03 ? 154 GLU A OE1 1 
ATOM   3174 O OE2 . GLU B  2 157 ? 8.311   -10.147 34.595  1.00 33.18 ? 154 GLU A OE2 1 
ATOM   3175 N N   . ILE B  2 158 ? 2.041   -8.286  36.299  1.00 19.64 ? 155 ILE A N   1 
ATOM   3176 C CA  . ILE B  2 158 ? 1.004   -7.652  37.108  1.00 21.89 ? 155 ILE A CA  1 
ATOM   3177 C C   . ILE B  2 158 ? -0.274  -8.507  37.089  1.00 21.70 ? 155 ILE A C   1 
ATOM   3178 O O   . ILE B  2 158 ? -0.802  -8.820  38.156  1.00 23.23 ? 155 ILE A O   1 
ATOM   3179 C CB  . ILE B  2 158 ? 0.715   -6.210  36.691  1.00 22.32 ? 155 ILE A CB  1 
ATOM   3180 C CG1 . ILE B  2 158 ? 1.956   -5.326  36.898  1.00 23.75 ? 155 ILE A CG1 1 
ATOM   3181 C CG2 . ILE B  2 158 ? -0.479  -5.636  37.472  1.00 23.00 ? 155 ILE A CG2 1 
ATOM   3182 C CD1 . ILE B  2 158 ? 1.856   -3.951  36.306  1.00 24.64 ? 155 ILE A CD1 1 
ATOM   3183 N N   . SER B  2 159 ? -0.709  -8.921  35.883  1.00 20.89 ? 156 SER A N   1 
ATOM   3184 C CA  . SER B  2 159 ? -1.959  -9.681  35.775  1.00 21.62 ? 156 SER A CA  1 
ATOM   3185 C C   . SER B  2 159 ? -1.803  -11.047 36.432  1.00 21.70 ? 156 SER A C   1 
ATOM   3186 O O   . SER B  2 159 ? -2.768  -11.496 37.017  1.00 22.38 ? 156 SER A O   1 
ATOM   3187 C CB  . SER B  2 159 ? -2.478  -9.764  34.328  1.00 21.19 ? 156 SER A CB  1 
ATOM   3188 O OG  . SER B  2 159 ? -1.475  -10.320 33.531  1.00 23.18 ? 156 SER A OG  1 
ATOM   3189 N N   . ALA B  2 160 ? -0.626  -11.713 36.346  1.00 22.14 ? 157 ALA A N   1 
ATOM   3190 C CA  . ALA B  2 160 ? -0.428  -12.991 37.025  1.00 23.23 ? 157 ALA A CA  1 
ATOM   3191 C C   . ALA B  2 160 ? -0.535  -12.841 38.553  1.00 24.32 ? 157 ALA A C   1 
ATOM   3192 O O   . ALA B  2 160 ? -1.120  -13.675 39.215  1.00 25.97 ? 157 ALA A O   1 
ATOM   3193 C CB  . ALA B  2 160 ? 0.880   -13.658 36.616  1.00 23.85 ? 157 ALA A CB  1 
ATOM   3194 N N   . ALA B  2 161 ? 0.032   -11.796 39.113  1.00 25.23 ? 158 ALA A N   1 
ATOM   3195 C CA  . ALA B  2 161 ? -0.039  -11.532 40.550  1.00 25.46 ? 158 ALA A CA  1 
ATOM   3196 C C   . ALA B  2 161 ? -1.401  -11.010 41.023  1.00 26.52 ? 158 ALA A C   1 
ATOM   3197 O O   . ALA B  2 161 ? -1.675  -11.185 42.212  1.00 27.48 ? 158 ALA A O   1 
ATOM   3198 C CB  . ALA B  2 161 ? 1.035   -10.548 40.894  1.00 26.34 ? 158 ALA A CB  1 
ATOM   3199 N N   . ALA B  2 162 ? -2.191  -10.277 40.189  1.00 25.27 ? 159 ALA A N   1 
ATOM   3200 C CA  . ALA B  2 162 ? -3.262  -9.419  40.697  1.00 28.02 ? 159 ALA A CA  1 
ATOM   3201 C C   . ALA B  2 162 ? -4.656  -9.697  40.137  1.00 27.22 ? 159 ALA A C   1 
ATOM   3202 O O   . ALA B  2 162 ? -5.579  -9.042  40.617  1.00 27.56 ? 159 ALA A O   1 
ATOM   3203 C CB  . ALA B  2 162 ? -2.909  -7.931  40.508  1.00 29.43 ? 159 ALA A CB  1 
ATOM   3204 N N   . MET B  2 163 ? -4.801  -10.509 39.071  1.00 24.56 ? 160 MET A N   1 
ATOM   3205 C CA  . MET B  2 163 ? -6.061  -10.653 38.365  1.00 23.67 ? 160 MET A CA  1 
ATOM   3206 C C   . MET B  2 163 ? -6.385  -12.128 38.216  1.00 24.45 ? 160 MET A C   1 
ATOM   3207 O O   . MET B  2 163 ? -5.486  -12.990 38.176  1.00 23.16 ? 160 MET A O   1 
ATOM   3208 C CB  . MET B  2 163 ? -5.962  -9.982  36.992  1.00 22.94 ? 160 MET A CB  1 
ATOM   3209 C CG  . MET B  2 163 ? -5.886  -8.443  37.057  1.00 24.29 ? 160 MET A CG  1 
ATOM   3210 S SD  . MET B  2 163 ? -5.510  -7.712  35.448  1.00 26.61 ? 160 MET A SD  1 
ATOM   3211 C CE  . MET B  2 163 ? -6.923  -8.225  34.465  1.00 24.03 ? 160 MET A CE  1 
ATOM   3212 N N   . GLN B  2 164 ? -7.682  -12.415 38.094  1.00 24.97 ? 161 GLN A N   1 
ATOM   3213 C CA  . GLN B  2 164 ? -8.155  -13.780 37.980  1.00 27.46 ? 161 GLN A CA  1 
ATOM   3214 C C   . GLN B  2 164 ? -7.850  -14.300 36.566  1.00 25.11 ? 161 GLN A C   1 
ATOM   3215 O O   . GLN B  2 164 ? -7.903  -13.536 35.594  1.00 23.48 ? 161 GLN A O   1 
ATOM   3216 C CB  . GLN B  2 164 ? -9.640  -13.932 38.303  1.00 29.81 ? 161 GLN A CB  1 
ATOM   3217 C CG  . GLN B  2 164 ? -9.966  -13.603 39.756  1.00 32.35 ? 161 GLN A CG  1 
ATOM   3218 C CD  . GLN B  2 164 ? -11.441 -13.705 40.042  1.00 35.69 ? 161 GLN A CD  1 
ATOM   3219 O OE1 . GLN B  2 164 ? -12.264 -13.122 39.321  1.00 35.11 ? 161 GLN A OE1 1 
ATOM   3220 N NE2 . GLN B  2 164 ? -11.777 -14.403 41.129  1.00 37.82 ? 161 GLN A NE2 1 
ATOM   3221 N N   . PRO B  2 165 ? -7.587  -15.614 36.403  1.00 25.61 ? 162 PRO A N   1 
ATOM   3222 C CA  . PRO B  2 165 ? -7.282  -16.156 35.071  1.00 24.58 ? 162 PRO A CA  1 
ATOM   3223 C C   . PRO B  2 165 ? -8.390  -16.020 34.018  1.00 24.86 ? 162 PRO A C   1 
ATOM   3224 O O   . PRO B  2 165 ? -8.089  -16.095 32.818  1.00 22.77 ? 162 PRO A O   1 
ATOM   3225 C CB  . PRO B  2 165 ? -6.966  -17.614 35.372  1.00 25.46 ? 162 PRO A CB  1 
ATOM   3226 C CG  . PRO B  2 165 ? -7.591  -17.899 36.717  1.00 28.48 ? 162 PRO A CG  1 
ATOM   3227 C CD  . PRO B  2 165 ? -7.504  -16.641 37.465  1.00 27.23 ? 162 PRO A CD  1 
ATOM   3228 N N   . THR B  2 166 ? -9.648  -15.895 34.463  1.00 25.18 ? 163 THR A N   1 
ATOM   3229 C CA  . THR B  2 166 ? -10.795 -15.667 33.584  1.00 24.16 ? 163 THR A CA  1 
ATOM   3230 C C   . THR B  2 166 ? -10.953 -14.223 33.127  1.00 24.39 ? 163 THR A C   1 
ATOM   3231 O O   . THR B  2 166 ? -11.794 -14.004 32.255  1.00 22.73 ? 163 THR A O   1 
ATOM   3232 C CB  . THR B  2 166 ? -12.057 -16.128 34.301  1.00 25.07 ? 163 THR A CB  1 
ATOM   3233 O OG1 . THR B  2 166 ? -12.122 -15.496 35.578  1.00 25.92 ? 163 THR A OG1 1 
ATOM   3234 C CG2 . THR B  2 166 ? -12.042 -17.632 34.497  1.00 26.49 ? 163 THR A CG2 1 
ATOM   3235 N N   . HIS B  2 167 ? -10.188 -13.253 33.700  1.00 22.83 ? 164 HIS A N   1 
ATOM   3236 C CA  . HIS B  2 167 ? -10.388 -11.856 33.417  1.00 22.87 ? 164 HIS A CA  1 
ATOM   3237 C C   . HIS B  2 167 ? -10.180 -11.617 31.923  1.00 21.35 ? 164 HIS A C   1 
ATOM   3238 O O   . HIS B  2 167 ? -9.130  -11.984 31.399  1.00 20.28 ? 164 HIS A O   1 
ATOM   3239 C CB  . HIS B  2 167 ? -9.554  -10.914 34.326  1.00 23.87 ? 164 HIS A CB  1 
ATOM   3240 C CG  . HIS B  2 167 ? -10.141 -9.550  34.291  1.00 23.97 ? 164 HIS A CG  1 
ATOM   3241 N ND1 . HIS B  2 167 ? -10.181 -8.794  33.137  1.00 22.94 ? 164 HIS A ND1 1 
ATOM   3242 C CD2 . HIS B  2 167 ? -10.788 -8.832  35.244  1.00 26.87 ? 164 HIS A CD2 1 
ATOM   3243 C CE1 . HIS B  2 167 ? -10.820 -7.663  33.373  1.00 24.72 ? 164 HIS A CE1 1 
ATOM   3244 N NE2 . HIS B  2 167 ? -11.230 -7.679  34.639  1.00 27.44 ? 164 HIS A NE2 1 
ATOM   3245 N N   . PRO B  2 168 ? -11.169 -11.056 31.179  1.00 20.00 ? 165 PRO A N   1 
ATOM   3246 C CA  . PRO B  2 168 ? -10.979 -10.841 29.747  1.00 20.63 ? 165 PRO A CA  1 
ATOM   3247 C C   . PRO B  2 168 ? -9.721  -10.077 29.349  1.00 20.21 ? 165 PRO A C   1 
ATOM   3248 O O   . PRO B  2 168 ? -9.100  -10.407 28.333  1.00 19.50 ? 165 PRO A O   1 
ATOM   3249 C CB  . PRO B  2 168 ? -12.228 -10.138 29.295  1.00 21.05 ? 165 PRO A CB  1 
ATOM   3250 C CG  . PRO B  2 168 ? -13.249 -10.488 30.363  1.00 22.25 ? 165 PRO A CG  1 
ATOM   3251 C CD  . PRO B  2 168 ? -12.524 -10.671 31.643  1.00 21.94 ? 165 PRO A CD  1 
ATOM   3252 N N   . ILE B  2 169 ? -9.289  -9.143  30.201  1.00 19.42 ? 166 ILE A N   1 
ATOM   3253 C CA  . ILE B  2 169 ? -8.042  -8.415  29.948  1.00 18.92 ? 166 ILE A CA  1 
ATOM   3254 C C   . ILE B  2 169 ? -6.818  -9.353  30.068  1.00 17.27 ? 166 ILE A C   1 
ATOM   3255 O O   . ILE B  2 169 ? -5.898  -9.231  29.259  1.00 16.88 ? 166 ILE A O   1 
ATOM   3256 C CB  . ILE B  2 169 ? -7.944  -7.157  30.831  1.00 17.67 ? 166 ILE A CB  1 
ATOM   3257 C CG1 . ILE B  2 169 ? -9.055  -6.132  30.590  1.00 18.56 ? 166 ILE A CG1 1 
ATOM   3258 C CG2 . ILE B  2 169 ? -6.560  -6.481  30.672  1.00 18.22 ? 166 ILE A CG2 1 
ATOM   3259 C CD1 . ILE B  2 169 ? -9.225  -5.163  31.760  1.00 19.67 ? 166 ILE A CD1 1 
ATOM   3260 N N   . ARG B  2 170 ? -6.763  -10.208 31.102  1.00 17.14 ? 167 ARG A N   1 
ATOM   3261 C CA  . ARG B  2 170 ? -5.680  -11.145 31.273  1.00 17.36 ? 167 ARG A CA  1 
ATOM   3262 C C   . ARG B  2 170 ? -5.648  -12.133 30.094  1.00 17.33 ? 167 ARG A C   1 
ATOM   3263 O O   . ARG B  2 170 ? -4.573  -12.383 29.541  1.00 18.05 ? 167 ARG A O   1 
ATOM   3264 C CB  . ARG B  2 170 ? -5.840  -11.866 32.626  1.00 19.27 ? 167 ARG A CB  1 
ATOM   3265 C CG  . ARG B  2 170 ? -4.734  -12.902 32.864  1.00 19.33 ? 167 ARG A CG  1 
ATOM   3266 C CD  . ARG B  2 170 ? -4.613  -13.319 34.312  1.00 22.41 ? 167 ARG A CD  1 
ATOM   3267 N NE  . ARG B  2 170 ? -3.669  -14.445 34.409  1.00 23.02 ? 167 ARG A NE  1 
ATOM   3268 C CZ  . ARG B  2 170 ? -3.528  -15.179 35.492  1.00 26.06 ? 167 ARG A CZ  1 
ATOM   3269 N NH1 . ARG B  2 170 ? -4.194  -14.860 36.579  1.00 24.62 ? 167 ARG A NH1 1 
ATOM   3270 N NH2 . ARG B  2 170 ? -2.796  -16.282 35.495  1.00 26.61 ? 167 ARG A NH2 1 
ATOM   3271 N N   . LEU B  2 171 ? -6.842  -12.610 29.680  1.00 15.60 ? 168 LEU A N   1 
ATOM   3272 C CA  . LEU B  2 171 ? -6.930  -13.514 28.533  1.00 16.65 ? 168 LEU A CA  1 
ATOM   3273 C C   . LEU B  2 171 ? -6.499  -12.833 27.241  1.00 16.17 ? 168 LEU A C   1 
ATOM   3274 O O   . LEU B  2 171 ? -5.760  -13.446 26.472  1.00 15.37 ? 168 LEU A O   1 
ATOM   3275 C CB  . LEU B  2 171 ? -8.347  -14.049 28.426  1.00 17.42 ? 168 LEU A CB  1 
ATOM   3276 C CG  . LEU B  2 171 ? -8.728  -15.079 29.485  1.00 19.16 ? 168 LEU A CG  1 
ATOM   3277 C CD1 . LEU B  2 171 ? -10.237 -15.271 29.491  1.00 20.04 ? 168 LEU A CD1 1 
ATOM   3278 C CD2 . LEU B  2 171 ? -8.000  -16.409 29.231  1.00 19.97 ? 168 LEU A CD2 1 
ATOM   3279 N N   . GLY B  2 172 ? -7.010  -11.619 26.989  1.00 16.31 ? 169 GLY A N   1 
ATOM   3280 C CA  . GLY B  2 172 ? -6.637  -10.814 25.814  1.00 15.87 ? 169 GLY A CA  1 
ATOM   3281 C C   . GLY B  2 172 ? -5.144  -10.517 25.748  1.00 16.51 ? 169 GLY A C   1 
ATOM   3282 O O   . GLY B  2 172 ? -4.522  -10.573 24.677  1.00 14.11 ? 169 GLY A O   1 
ATOM   3283 N N   . LEU B  2 173 ? -4.557  -10.220 26.913  1.00 16.62 ? 170 LEU A N   1 
ATOM   3284 C CA  . LEU B  2 173 ? -3.116  -10.058 27.023  1.00 16.39 ? 170 LEU A CA  1 
ATOM   3285 C C   . LEU B  2 173 ? -2.387  -11.331 26.600  1.00 15.94 ? 170 LEU A C   1 
ATOM   3286 O O   . LEU B  2 173 ? -1.413  -11.247 25.837  1.00 14.62 ? 170 LEU A O   1 
ATOM   3287 C CB  . LEU B  2 173 ? -2.714  -9.588  28.424  1.00 17.73 ? 170 LEU A CB  1 
ATOM   3288 C CG  . LEU B  2 173 ? -1.231  -9.697  28.814  1.00 17.16 ? 170 LEU A CG  1 
ATOM   3289 C CD1 . LEU B  2 173 ? -0.453  -8.725  27.921  1.00 16.51 ? 170 LEU A CD1 1 
ATOM   3290 C CD2 . LEU B  2 173 ? -1.047  -9.460  30.305  1.00 19.70 ? 170 LEU A CD2 1 
ATOM   3291 N N   . ALA B  2 174 ? -2.808  -12.474 27.149  1.00 16.69 ? 171 ALA A N   1 
ATOM   3292 C CA  . ALA B  2 174 ? -2.205  -13.771 26.818  1.00 16.58 ? 171 ALA A CA  1 
ATOM   3293 C C   . ALA B  2 174 ? -2.287  -14.043 25.323  1.00 16.43 ? 171 ALA A C   1 
ATOM   3294 O O   . ALA B  2 174 ? -1.286  -14.462 24.696  1.00 16.05 ? 171 ALA A O   1 
ATOM   3295 C CB  . ALA B  2 174 ? -2.862  -14.878 27.614  1.00 17.59 ? 171 ALA A CB  1 
ATOM   3296 N N   . LEU B  2 175 ? -3.473  -13.758 24.756  1.00 15.69 ? 172 LEU A N   1 
ATOM   3297 C CA  . LEU B  2 175 ? -3.661  -13.938 23.316  1.00 15.39 ? 172 LEU A CA  1 
ATOM   3298 C C   . LEU B  2 175 ? -2.656  -13.123 22.511  1.00 14.77 ? 172 LEU A C   1 
ATOM   3299 O O   . LEU B  2 175 ? -1.994  -13.675 21.632  1.00 14.35 ? 172 LEU A O   1 
ATOM   3300 C CB  . LEU B  2 175 ? -5.105  -13.593 22.969  1.00 16.34 ? 172 LEU A CB  1 
ATOM   3301 C CG  . LEU B  2 175 ? -5.501  -13.806 21.496  1.00 16.18 ? 172 LEU A CG  1 
ATOM   3302 C CD1 . LEU B  2 175 ? -5.449  -15.224 20.996  1.00 15.74 ? 172 LEU A CD1 1 
ATOM   3303 C CD2 . LEU B  2 175 ? -6.833  -13.133 21.218  1.00 16.49 ? 172 LEU A CD2 1 
ATOM   3304 N N   . ASN B  2 176 ? -2.547  -11.815 22.814  1.00 15.19 ? 173 ASN A N   1 
ATOM   3305 C CA  . ASN B  2 176 ? -1.699  -10.911 22.048  1.00 16.64 ? 173 ASN A CA  1 
ATOM   3306 C C   . ASN B  2 176 ? -0.207  -11.149 22.304  1.00 15.76 ? 173 ASN A C   1 
ATOM   3307 O O   . ASN B  2 176 ? 0.569   -11.094 21.363  1.00 16.28 ? 173 ASN A O   1 
ATOM   3308 C CB  . ASN B  2 176 ? -2.092  -9.461  22.286  1.00 16.31 ? 173 ASN A CB  1 
ATOM   3309 C CG  . ASN B  2 176 ? -3.431  -9.115  21.702  1.00 15.51 ? 173 ASN A CG  1 
ATOM   3310 O OD1 . ASN B  2 176 ? -4.177  -10.005 21.263  1.00 15.86 ? 173 ASN A OD1 1 
ATOM   3311 N ND2 . ASN B  2 176 ? -3.734  -7.821  21.762  1.00 14.17 ? 173 ASN A ND2 1 
ATOM   3312 N N   . PHE B  2 177 ? 0.163   -11.433 23.547  1.00 15.90 ? 174 PHE A N   1 
ATOM   3313 C CA  . PHE B  2 177 ? 1.546   -11.789 23.858  1.00 15.59 ? 174 PHE A CA  1 
ATOM   3314 C C   . PHE B  2 177 ? 1.956   -13.087 23.146  1.00 15.12 ? 174 PHE A C   1 
ATOM   3315 O O   . PHE B  2 177 ? 3.099   -13.142 22.653  1.00 14.76 ? 174 PHE A O   1 
ATOM   3316 C CB  . PHE B  2 177 ? 1.784   -11.836 25.365  1.00 16.79 ? 174 PHE A CB  1 
ATOM   3317 C CG  . PHE B  2 177 ? 3.192   -11.633 25.885  1.00 16.78 ? 174 PHE A CG  1 
ATOM   3318 C CD1 . PHE B  2 177 ? 4.269   -11.212 25.103  1.00 17.04 ? 174 PHE A CD1 1 
ATOM   3319 C CD2 . PHE B  2 177 ? 3.383   -11.765 27.259  1.00 17.28 ? 174 PHE A CD2 1 
ATOM   3320 C CE1 . PHE B  2 177 ? 5.512   -10.996 25.672  1.00 19.23 ? 174 PHE A CE1 1 
ATOM   3321 C CE2 . PHE B  2 177 ? 4.640   -11.584 27.814  1.00 19.52 ? 174 PHE A CE2 1 
ATOM   3322 C CZ  . PHE B  2 177 ? 5.695   -11.185 27.027  1.00 19.51 ? 174 PHE A CZ  1 
ATOM   3323 N N   A SER B  2 178 ? 1.063   -14.089 23.115  0.50 14.61 ? 175 SER A N   1 
ATOM   3324 N N   B SER B  2 178 ? 1.046   -14.095 23.057  0.50 15.72 ? 175 SER A N   1 
ATOM   3325 C CA  A SER B  2 178 ? 1.277   -15.322 22.364  0.50 14.53 ? 175 SER A CA  1 
ATOM   3326 C CA  B SER B  2 178 ? 1.280   -15.347 22.320  0.50 16.48 ? 175 SER A CA  1 
ATOM   3327 C C   A SER B  2 178 ? 1.540   -15.035 20.886  0.50 14.36 ? 175 SER A C   1 
ATOM   3328 C C   B SER B  2 178 ? 1.552   -15.038 20.858  0.50 15.34 ? 175 SER A C   1 
ATOM   3329 O O   A SER B  2 178 ? 2.534   -15.536 20.364  0.50 14.04 ? 175 SER A O   1 
ATOM   3330 O O   B SER B  2 178 ? 2.523   -15.556 20.317  0.50 14.81 ? 175 SER A O   1 
ATOM   3331 C CB  A SER B  2 178 ? 0.159   -16.307 22.567  0.50 13.99 ? 175 SER A CB  1 
ATOM   3332 C CB  B SER B  2 178 ? 0.183   -16.432 22.419  0.50 17.09 ? 175 SER A CB  1 
ATOM   3333 O OG  A SER B  2 178 ? 0.260   -17.368 21.653  0.50 13.48 ? 175 SER A OG  1 
ATOM   3334 O OG  B SER B  2 178 ? -1.046  -16.080 21.783  0.50 19.19 ? 175 SER A OG  1 
ATOM   3335 N N   . VAL B  2 179 ? 0.764   -14.114 20.279  1.00 14.23 ? 176 VAL A N   1 
ATOM   3336 C CA  . VAL B  2 179 ? 0.925   -13.766 18.872  1.00 15.10 ? 176 VAL A CA  1 
ATOM   3337 C C   . VAL B  2 179 ? 2.250   -13.030 18.657  1.00 14.75 ? 176 VAL A C   1 
ATOM   3338 O O   . VAL B  2 179 ? 2.973   -13.311 17.687  1.00 14.73 ? 176 VAL A O   1 
ATOM   3339 C CB  . VAL B  2 179 ? -0.277  -13.000 18.305  1.00 15.25 ? 176 VAL A CB  1 
ATOM   3340 C CG1 . VAL B  2 179 ? 0.049   -12.349 16.938  1.00 15.57 ? 176 VAL A CG1 1 
ATOM   3341 C CG2 . VAL B  2 179 ? -1.490  -13.933 18.222  1.00 17.10 ? 176 VAL A CG2 1 
ATOM   3342 N N   . PHE B  2 180 ? 2.604   -12.160 19.603  1.00 14.92 ? 177 PHE A N   1 
ATOM   3343 C CA  . PHE B  2 180 ? 3.898   -11.514 19.572  1.00 14.53 ? 177 PHE A CA  1 
ATOM   3344 C C   . PHE B  2 180 ? 5.038   -12.536 19.499  1.00 14.86 ? 177 PHE A C   1 
ATOM   3345 O O   . PHE B  2 180 ? 5.934   -12.395 18.667  1.00 14.47 ? 177 PHE A O   1 
ATOM   3346 C CB  . PHE B  2 180 ? 3.989   -10.591 20.792  1.00 14.36 ? 177 PHE A CB  1 
ATOM   3347 C CG  . PHE B  2 180 ? 5.359   -9.975  20.908  1.00 15.36 ? 177 PHE A CG  1 
ATOM   3348 C CD1 . PHE B  2 180 ? 5.658   -8.839  20.156  1.00 15.41 ? 177 PHE A CD1 1 
ATOM   3349 C CD2 . PHE B  2 180 ? 6.317   -10.507 21.804  1.00 16.30 ? 177 PHE A CD2 1 
ATOM   3350 C CE1 . PHE B  2 180 ? 6.888   -8.199  20.296  1.00 17.10 ? 177 PHE A CE1 1 
ATOM   3351 C CE2 . PHE B  2 180 ? 7.576   -9.889  21.884  1.00 18.22 ? 177 PHE A CE2 1 
ATOM   3352 C CZ  . PHE B  2 180 ? 7.856   -8.756  21.108  1.00 17.57 ? 177 PHE A CZ  1 
ATOM   3353 N N   . TYR B  2 181 ? 5.021   -13.535 20.387  1.00 15.08 ? 178 TYR A N   1 
ATOM   3354 C CA  . TYR B  2 181 ? 6.031   -14.566 20.357  1.00 16.79 ? 178 TYR A CA  1 
ATOM   3355 C C   . TYR B  2 181 ? 6.013   -15.282 19.021  1.00 17.21 ? 178 TYR A C   1 
ATOM   3356 O O   . TYR B  2 181 ? 7.079   -15.552 18.491  1.00 19.41 ? 178 TYR A O   1 
ATOM   3357 C CB  . TYR B  2 181 ? 5.855   -15.609 21.472  1.00 17.65 ? 178 TYR A CB  1 
ATOM   3358 C CG  . TYR B  2 181 ? 6.529   -15.138 22.749  1.00 20.54 ? 178 TYR A CG  1 
ATOM   3359 C CD1 . TYR B  2 181 ? 7.893   -15.335 22.900  1.00 25.36 ? 178 TYR A CD1 1 
ATOM   3360 C CD2 . TYR B  2 181 ? 5.841   -14.568 23.800  1.00 22.41 ? 178 TYR A CD2 1 
ATOM   3361 C CE1 . TYR B  2 181 ? 8.575   -14.949 24.050  1.00 28.43 ? 178 TYR A CE1 1 
ATOM   3362 C CE2 . TYR B  2 181 ? 6.506   -14.183 24.967  1.00 24.17 ? 178 TYR A CE2 1 
ATOM   3363 C CZ  . TYR B  2 181 ? 7.879   -14.343 25.075  1.00 27.90 ? 178 TYR A CZ  1 
ATOM   3364 O OH  . TYR B  2 181 ? 8.601   -13.989 26.199  1.00 28.89 ? 178 TYR A OH  1 
ATOM   3365 N N   . TYR B  2 182 ? 4.809   -15.618 18.528  1.00 15.88 ? 179 TYR A N   1 
ATOM   3366 C CA  . TYR B  2 182 ? 4.731   -16.461 17.340  1.00 17.02 ? 179 TYR A CA  1 
ATOM   3367 C C   . TYR B  2 182 ? 5.308   -15.721 16.130  1.00 17.59 ? 179 TYR A C   1 
ATOM   3368 O O   . TYR B  2 182 ? 6.151   -16.277 15.422  1.00 18.47 ? 179 TYR A O   1 
ATOM   3369 C CB  . TYR B  2 182 ? 3.287   -16.855 17.049  1.00 16.72 ? 179 TYR A CB  1 
ATOM   3370 C CG  . TYR B  2 182 ? 3.179   -17.932 15.994  1.00 18.43 ? 179 TYR A CG  1 
ATOM   3371 C CD1 . TYR B  2 182 ? 3.135   -17.604 14.646  1.00 19.32 ? 179 TYR A CD1 1 
ATOM   3372 C CD2 . TYR B  2 182 ? 3.170   -19.292 16.359  1.00 19.57 ? 179 TYR A CD2 1 
ATOM   3373 C CE1 . TYR B  2 182 ? 3.079   -18.595 13.682  1.00 20.41 ? 179 TYR A CE1 1 
ATOM   3374 C CE2 . TYR B  2 182 ? 3.111   -20.278 15.396  1.00 20.87 ? 179 TYR A CE2 1 
ATOM   3375 C CZ  . TYR B  2 182 ? 3.048   -19.924 14.065  1.00 21.32 ? 179 TYR A CZ  1 
ATOM   3376 O OH  . TYR B  2 182 ? 2.910   -20.889 13.125  1.00 23.39 ? 179 TYR A OH  1 
ATOM   3377 N N   . GLU B  2 183 ? 4.810   -14.515 15.875  1.00 18.09 ? 180 GLU A N   1 
ATOM   3378 C CA  . GLU B  2 183 ? 5.053   -13.878 14.590  1.00 21.84 ? 180 GLU A CA  1 
ATOM   3379 C C   . GLU B  2 183 ? 6.080   -12.748 14.629  1.00 20.96 ? 180 GLU A C   1 
ATOM   3380 O O   . GLU B  2 183 ? 6.682   -12.540 13.589  1.00 23.44 ? 180 GLU A O   1 
ATOM   3381 C CB  . GLU B  2 183 ? 3.733   -13.572 13.886  1.00 23.80 ? 180 GLU A CB  1 
ATOM   3382 C CG  . GLU B  2 183 ? 3.124   -12.218 14.135  1.00 25.46 ? 180 GLU A CG  1 
ATOM   3383 C CD  . GLU B  2 183 ? 1.770   -12.024 13.442  1.00 26.71 ? 180 GLU A CD  1 
ATOM   3384 O OE1 . GLU B  2 183 ? 1.115   -12.876 12.821  1.00 27.88 ? 180 GLU A OE1 1 
ATOM   3385 O OE2 . GLU B  2 183 ? 1.358   -10.918 13.577  1.00 25.25 ? 180 GLU A OE2 1 
ATOM   3386 N N   . ILE B  2 184 ? 6.309   -12.083 15.767  1.00 18.45 ? 181 ILE A N   1 
ATOM   3387 C CA  . ILE B  2 184 ? 7.360   -11.077 15.865  1.00 18.26 ? 181 ILE A CA  1 
ATOM   3388 C C   . ILE B  2 184 ? 8.674   -11.761 16.248  1.00 18.48 ? 181 ILE A C   1 
ATOM   3389 O O   . ILE B  2 184 ? 9.657   -11.483 15.604  1.00 20.28 ? 181 ILE A O   1 
ATOM   3390 C CB  . ILE B  2 184 ? 6.977   -9.921  16.808  1.00 16.97 ? 181 ILE A CB  1 
ATOM   3391 C CG1 . ILE B  2 184 ? 5.620   -9.311  16.422  1.00 16.46 ? 181 ILE A CG1 1 
ATOM   3392 C CG2 . ILE B  2 184 ? 8.095   -8.874  16.879  1.00 18.18 ? 181 ILE A CG2 1 
ATOM   3393 C CD1 . ILE B  2 184 ? 5.497   -8.773  14.991  1.00 16.88 ? 181 ILE A CD1 1 
ATOM   3394 N N   . LEU B  2 185 ? 8.674   -12.627 17.264  1.00 18.94 ? 182 LEU A N   1 
ATOM   3395 C CA  . LEU B  2 185 ? 9.881   -13.322 17.712  1.00 22.12 ? 182 LEU A CA  1 
ATOM   3396 C C   . LEU B  2 185 ? 10.189  -14.648 16.996  1.00 25.09 ? 182 LEU A C   1 
ATOM   3397 O O   . LEU B  2 185 ? 11.290  -15.159 17.208  1.00 25.36 ? 182 LEU A O   1 
ATOM   3398 C CB  . LEU B  2 185 ? 9.818   -13.518 19.233  1.00 22.92 ? 182 LEU A CB  1 
ATOM   3399 C CG  . LEU B  2 185 ? 9.768   -12.264 20.090  1.00 23.56 ? 182 LEU A CG  1 
ATOM   3400 C CD1 . LEU B  2 185 ? 9.779   -12.674 21.556  1.00 24.06 ? 182 LEU A CD1 1 
ATOM   3401 C CD2 . LEU B  2 185 ? 10.875  -11.269 19.797  1.00 25.43 ? 182 LEU A CD2 1 
ATOM   3402 N N   A ASN B  2 186 ? 9.252   -15.195 16.185  0.50 23.64 ? 183 ASN A N   1 
ATOM   3403 N N   B ASN B  2 186 ? 9.232   -15.226 16.226  0.50 23.87 ? 183 ASN A N   1 
ATOM   3404 C CA  A ASN B  2 186 ? 9.368   -16.506 15.557  0.50 24.49 ? 183 ASN A CA  1 
ATOM   3405 C CA  B ASN B  2 186 ? 9.415   -16.499 15.555  0.50 24.95 ? 183 ASN A CA  1 
ATOM   3406 C C   A ASN B  2 186 ? 9.724   -17.589 16.576  0.50 24.27 ? 183 ASN A C   1 
ATOM   3407 C C   B ASN B  2 186 ? 9.696   -17.632 16.546  0.50 24.55 ? 183 ASN A C   1 
ATOM   3408 O O   A ASN B  2 186 ? 10.713  -18.314 16.406  0.50 25.00 ? 183 ASN A O   1 
ATOM   3409 O O   B ASN B  2 186 ? 10.613  -18.439 16.317  0.50 25.27 ? 183 ASN A O   1 
ATOM   3410 C CB  A ASN B  2 186 ? 10.264  -16.465 14.329  0.50 27.49 ? 183 ASN A CB  1 
ATOM   3411 C CB  B ASN B  2 186 ? 10.489  -16.409 14.484  0.50 28.53 ? 183 ASN A CB  1 
ATOM   3412 C CG  A ASN B  2 186 ? 9.841   -15.360 13.393  0.50 26.66 ? 183 ASN A CG  1 
ATOM   3413 C CG  B ASN B  2 186 ? 10.082  -17.269 13.327  0.50 28.68 ? 183 ASN A CG  1 
ATOM   3414 O OD1 A ASN B  2 186 ? 8.702   -15.333 12.903  0.50 26.39 ? 183 ASN A OD1 1 
ATOM   3415 O OD1 B ASN B  2 186 ? 8.952   -17.131 12.858  0.50 30.22 ? 183 ASN A OD1 1 
ATOM   3416 N ND2 A ASN B  2 186 ? 10.750  -14.428 13.141  0.50 27.01 ? 183 ASN A ND2 1 
ATOM   3417 N ND2 B ASN B  2 186 ? 10.953  -18.159 12.908  0.50 31.23 ? 183 ASN A ND2 1 
ATOM   3418 N N   . SER B  2 187 ? 8.895   -17.661 17.615  1.00 21.93 ? 184 SER A N   1 
ATOM   3419 C CA  . SER B  2 187 ? 9.021   -18.558 18.760  1.00 22.53 ? 184 SER A CA  1 
ATOM   3420 C C   . SER B  2 187 ? 7.709   -19.319 18.927  1.00 20.60 ? 184 SER A C   1 
ATOM   3421 O O   . SER B  2 187 ? 6.971   -19.056 19.859  1.00 19.27 ? 184 SER A O   1 
ATOM   3422 C CB  . SER B  2 187 ? 9.308   -17.794 20.053  1.00 23.75 ? 184 SER A CB  1 
ATOM   3423 O OG  . SER B  2 187 ? 10.582  -17.240 20.004  1.00 26.59 ? 184 SER A OG  1 
ATOM   3424 N N   . PRO B  2 188 ? 7.381   -20.272 18.045  1.00 21.09 ? 185 PRO A N   1 
ATOM   3425 C CA  . PRO B  2 188 ? 6.081   -20.933 18.094  1.00 21.50 ? 185 PRO A CA  1 
ATOM   3426 C C   . PRO B  2 188 ? 5.860   -21.778 19.347  1.00 20.22 ? 185 PRO A C   1 
ATOM   3427 O O   . PRO B  2 188 ? 4.763   -21.750 19.893  1.00 18.67 ? 185 PRO A O   1 
ATOM   3428 C CB  . PRO B  2 188 ? 6.034   -21.720 16.790  1.00 22.07 ? 185 PRO A CB  1 
ATOM   3429 C CG  . PRO B  2 188 ? 7.493   -22.007 16.482  1.00 24.81 ? 185 PRO A CG  1 
ATOM   3430 C CD  . PRO B  2 188 ? 8.201   -20.723 16.902  1.00 22.87 ? 185 PRO A CD  1 
ATOM   3431 N N   . GLU B  2 189 ? 6.895   -22.472 19.823  1.00 21.26 ? 186 GLU A N   1 
ATOM   3432 C CA  . GLU B  2 189 ? 6.811   -23.292 21.018  1.00 22.52 ? 186 GLU A CA  1 
ATOM   3433 C C   . GLU B  2 189 ? 6.364   -22.439 22.228  1.00 22.94 ? 186 GLU A C   1 
ATOM   3434 O O   . GLU B  2 189 ? 5.424   -22.796 22.955  1.00 21.99 ? 186 GLU A O   1 
ATOM   3435 C CB  . GLU B  2 189 ? 8.127   -24.029 21.345  1.00 24.65 ? 186 GLU A CB  1 
ATOM   3436 C CG  . GLU B  2 189 ? 8.681   -24.897 20.219  1.00 26.33 ? 186 GLU A CG  1 
ATOM   3437 C CD  . GLU B  2 189 ? 9.531   -24.318 19.112  1.00 27.44 ? 186 GLU A CD  1 
ATOM   3438 O OE1 . GLU B  2 189 ? 9.613   -23.070 19.064  1.00 24.89 ? 186 GLU A OE1 1 
ATOM   3439 O OE2 . GLU B  2 189 ? 10.073  -25.111 18.293  1.00 28.48 ? 186 GLU A OE2 1 
ATOM   3440 N N   . LYS B  2 190 ? 7.056   -21.296 22.444  1.00 22.99 ? 187 LYS A N   1 
ATOM   3441 C CA  . LYS B  2 190 ? 6.749   -20.350 23.503  1.00 23.61 ? 187 LYS A CA  1 
ATOM   3442 C C   . LYS B  2 190 ? 5.372   -19.721 23.290  1.00 19.72 ? 187 LYS A C   1 
ATOM   3443 O O   . LYS B  2 190 ? 4.640   -19.579 24.249  1.00 20.03 ? 187 LYS A O   1 
ATOM   3444 C CB  . LYS B  2 190 ? 7.794   -19.241 23.638  1.00 25.56 ? 187 LYS A CB  1 
ATOM   3445 C CG  . LYS B  2 190 ? 8.945   -19.632 24.516  1.00 35.53 ? 187 LYS A CG  1 
ATOM   3446 C CD  . LYS B  2 190 ? 9.975   -18.525 24.778  1.00 45.14 ? 187 LYS A CD  1 
ATOM   3447 C CE  . LYS B  2 190 ? 11.181  -18.572 23.832  1.00 58.15 ? 187 LYS A CE  1 
ATOM   3448 N NZ  . LYS B  2 190 ? 12.324  -17.783 24.303  1.00 63.83 ? 187 LYS A NZ  1 
ATOM   3449 N N   . ALA B  2 191 ? 5.030   -19.373 22.058  1.00 20.96 ? 188 ALA A N   1 
ATOM   3450 C CA  . ALA B  2 191 ? 3.713   -18.816 21.738  1.00 17.99 ? 188 ALA A CA  1 
ATOM   3451 C C   . ALA B  2 191 ? 2.606   -19.785 22.139  1.00 18.23 ? 188 ALA A C   1 
ATOM   3452 O O   . ALA B  2 191 ? 1.627   -19.376 22.761  1.00 16.43 ? 188 ALA A O   1 
ATOM   3453 C CB  . ALA B  2 191 ? 3.593   -18.548 20.245  1.00 17.58 ? 188 ALA A CB  1 
HETATM 3454 N N   . CME B  2 192 ? 2.781   -21.048 21.737  1.00 19.47 ? 189 CME A N   1 
HETATM 3455 C CA  . CME B  2 192 ? 1.880   -22.151 22.080  1.00 21.37 ? 189 CME A CA  1 
HETATM 3456 C CB  . CME B  2 192 ? 2.347   -23.394 21.343  1.00 24.19 ? 189 CME A CB  1 
HETATM 3457 S SG  . CME B  2 192 ? 1.219   -24.793 21.492  1.00 27.38 ? 189 CME A SG  1 
HETATM 3458 S SD  . CME B  2 192 ? 1.734   -25.656 23.592  1.00 30.39 ? 189 CME A SD  1 
HETATM 3459 C CE  . CME B  2 192 ? 3.116   -26.774 23.227  1.00 31.10 ? 189 CME A CE  1 
HETATM 3460 C CZ  . CME B  2 192 ? 4.427   -26.047 23.171  1.00 29.25 ? 189 CME A CZ  1 
HETATM 3461 O OH  . CME B  2 192 ? 5.403   -27.049 23.116  1.00 30.51 ? 189 CME A OH  1 
HETATM 3462 C C   . CME B  2 192 ? 1.722   -22.315 23.599  1.00 20.80 ? 189 CME A C   1 
HETATM 3463 O O   . CME B  2 192 ? 0.583   -22.394 24.103  1.00 18.42 ? 189 CME A O   1 
ATOM   3464 N N   A SER B  2 193 ? 2.866   -22.407 24.299  0.50 20.63 ? 190 SER A N   1 
ATOM   3465 N N   B SER B  2 193 ? 2.869   -22.413 24.307  0.50 20.91 ? 190 SER A N   1 
ATOM   3466 C CA  A SER B  2 193 ? 2.912   -22.604 25.742  0.50 20.81 ? 190 SER A CA  1 
ATOM   3467 C CA  B SER B  2 193 ? 2.944   -22.582 25.759  0.50 21.29 ? 190 SER A CA  1 
ATOM   3468 C C   A SER B  2 193 ? 2.110   -21.531 26.481  0.50 20.34 ? 190 SER A C   1 
ATOM   3469 C C   B SER B  2 193 ? 2.137   -21.528 26.507  0.50 20.61 ? 190 SER A C   1 
ATOM   3470 O O   A SER B  2 193 ? 1.255   -21.844 27.316  0.50 20.41 ? 190 SER A O   1 
ATOM   3471 O O   B SER B  2 193 ? 1.341   -21.852 27.397  0.50 20.55 ? 190 SER A O   1 
ATOM   3472 C CB  A SER B  2 193 ? 4.330   -22.600 26.194  0.50 20.93 ? 190 SER A CB  1 
ATOM   3473 C CB  B SER B  2 193 ? 4.370   -22.516 26.217  0.50 21.66 ? 190 SER A CB  1 
ATOM   3474 O OG  A SER B  2 193 ? 4.367   -22.910 27.570  0.50 21.04 ? 190 SER A OG  1 
ATOM   3475 O OG  B SER B  2 193 ? 5.050   -23.687 25.817  0.50 22.73 ? 190 SER A OG  1 
ATOM   3476 N N   . LEU B  2 194 ? 2.364   -20.277 26.102  1.00 19.91 ? 191 LEU A N   1 
ATOM   3477 C CA  . LEU B  2 194 ? 1.739   -19.109 26.720  1.00 19.02 ? 191 LEU A CA  1 
ATOM   3478 C C   . LEU B  2 194 ? 0.205   -19.142 26.551  1.00 17.74 ? 191 LEU A C   1 
ATOM   3479 O O   . LEU B  2 194 ? -0.555  -18.971 27.522  1.00 17.88 ? 191 LEU A O   1 
ATOM   3480 C CB  . LEU B  2 194 ? 2.384   -17.843 26.152  1.00 19.82 ? 191 LEU A CB  1 
ATOM   3481 C CG  . LEU B  2 194 ? 2.243   -16.577 26.994  1.00 20.76 ? 191 LEU A CG  1 
ATOM   3482 C CD1 . LEU B  2 194 ? 3.160   -15.513 26.344  1.00 22.61 ? 191 LEU A CD1 1 
ATOM   3483 C CD2 . LEU B  2 194 ? 0.793   -16.068 27.061  1.00 20.74 ? 191 LEU A CD2 1 
ATOM   3484 N N   . ALA B  2 195 ? -0.252  -19.384 25.302  1.00 17.05 ? 192 ALA A N   1 
ATOM   3485 C CA  . ALA B  2 195 ? -1.676  -19.425 25.012  1.00 17.22 ? 192 ALA A CA  1 
ATOM   3486 C C   . ALA B  2 195 ? -2.376  -20.570 25.745  1.00 17.93 ? 192 ALA A C   1 
ATOM   3487 O O   . ALA B  2 195 ? -3.463  -20.370 26.299  1.00 17.85 ? 192 ALA A O   1 
ATOM   3488 C CB  . ALA B  2 195 ? -1.887  -19.525 23.508  1.00 16.64 ? 192 ALA A CB  1 
ATOM   3489 N N   . LYS B  2 196 ? -1.761  -21.766 25.718  1.00 18.37 ? 193 LYS A N   1 
ATOM   3490 C CA  . LYS B  2 196 ? -2.344  -22.965 26.280  1.00 19.88 ? 193 LYS A CA  1 
ATOM   3491 C C   . LYS B  2 196 ? -2.481  -22.841 27.801  1.00 20.08 ? 193 LYS A C   1 
ATOM   3492 O O   . LYS B  2 196 ? -3.504  -23.264 28.337  1.00 20.04 ? 193 LYS A O   1 
ATOM   3493 C CB  . LYS B  2 196 ? -1.544  -24.221 25.907  1.00 20.51 ? 193 LYS A CB  1 
ATOM   3494 C CG  . LYS B  2 196 ? -2.073  -25.593 26.410  1.00 21.88 ? 193 LYS A CG  1 
ATOM   3495 C CD  . LYS B  2 196 ? -3.537  -25.871 26.125  1.00 21.52 ? 193 LYS A CD  1 
ATOM   3496 C CE  . LYS B  2 196 ? -3.914  -27.201 26.529  1.00 23.12 ? 193 LYS A CE  1 
ATOM   3497 N NZ  . LYS B  2 196 ? -5.351  -27.351 26.608  1.00 23.70 ? 193 LYS A NZ  1 
ATOM   3498 N N   . THR B  2 197 ? -1.437  -22.340 28.474  1.00 20.63 ? 194 THR A N   1 
ATOM   3499 C CA  . THR B  2 197 ? -1.482  -22.123 29.922  1.00 22.19 ? 194 THR A CA  1 
ATOM   3500 C C   . THR B  2 197 ? -2.640  -21.180 30.294  1.00 22.09 ? 194 THR A C   1 
ATOM   3501 O O   . THR B  2 197 ? -3.415  -21.507 31.198  1.00 22.95 ? 194 THR A O   1 
ATOM   3502 C CB  . THR B  2 197 ? -0.133  -21.598 30.428  1.00 22.34 ? 194 THR A CB  1 
ATOM   3503 O OG1 . THR B  2 197 ? 0.809   -22.626 30.158  1.00 22.14 ? 194 THR A OG1 1 
ATOM   3504 C CG2 . THR B  2 197 ? -0.172  -21.307 31.916  1.00 24.17 ? 194 THR A CG2 1 
ATOM   3505 N N   . ALA B  2 198 ? -2.749  -20.046 29.586  1.00 21.14 ? 195 ALA A N   1 
ATOM   3506 C CA  . ALA B  2 198 ? -3.815  -19.076 29.811  1.00 20.05 ? 195 ALA A CA  1 
ATOM   3507 C C   . ALA B  2 198 ? -5.213  -19.667 29.606  1.00 20.82 ? 195 ALA A C   1 
ATOM   3508 O O   . ALA B  2 198 ? -6.093  -19.516 30.492  1.00 20.88 ? 195 ALA A O   1 
ATOM   3509 C CB  . ALA B  2 198 ? -3.625  -17.891 28.903  1.00 20.96 ? 195 ALA A CB  1 
ATOM   3510 N N   . PHE B  2 199 ? -5.395  -20.432 28.522  1.00 19.12 ? 196 PHE A N   1 
ATOM   3511 C CA  . PHE B  2 199 ? -6.626  -21.175 28.301  1.00 20.20 ? 196 PHE A CA  1 
ATOM   3512 C C   . PHE B  2 199 ? -6.948  -22.127 29.458  1.00 21.17 ? 196 PHE A C   1 
ATOM   3513 O O   . PHE B  2 199 ? -8.060  -22.047 29.977  1.00 22.28 ? 196 PHE A O   1 
ATOM   3514 C CB  . PHE B  2 199 ? -6.528  -21.944 26.985  1.00 20.67 ? 196 PHE A CB  1 
ATOM   3515 C CG  . PHE B  2 199 ? -7.796  -22.672 26.585  1.00 22.09 ? 196 PHE A CG  1 
ATOM   3516 C CD1 . PHE B  2 199 ? -8.067  -23.952 27.056  1.00 23.47 ? 196 PHE A CD1 1 
ATOM   3517 C CD2 . PHE B  2 199 ? -8.723  -22.036 25.734  1.00 23.39 ? 196 PHE A CD2 1 
ATOM   3518 C CE1 . PHE B  2 199 ? -9.241  -24.605 26.699  1.00 26.15 ? 196 PHE A CE1 1 
ATOM   3519 C CE2 . PHE B  2 199 ? -9.894  -22.684 25.378  1.00 24.23 ? 196 PHE A CE2 1 
ATOM   3520 C CZ  . PHE B  2 199 ? -10.150 -23.968 25.847  1.00 26.46 ? 196 PHE A CZ  1 
ATOM   3521 N N   . ASP B  2 200 ? -5.971  -22.935 29.909  1.00 21.35 ? 197 ASP A N   1 
ATOM   3522 C CA  . ASP B  2 200 ? -6.190  -23.965 30.916  1.00 22.86 ? 197 ASP A CA  1 
ATOM   3523 C C   . ASP B  2 200 ? -6.494  -23.364 32.278  1.00 23.63 ? 197 ASP A C   1 
ATOM   3524 O O   . ASP B  2 200 ? -7.421  -23.852 32.933  1.00 24.41 ? 197 ASP A O   1 
ATOM   3525 C CB  . ASP B  2 200 ? -5.029  -24.941 30.994  1.00 23.07 ? 197 ASP A CB  1 
ATOM   3526 C CG  . ASP B  2 200 ? -4.883  -25.873 29.796  1.00 23.92 ? 197 ASP A CG  1 
ATOM   3527 O OD1 . ASP B  2 200 ? -5.857  -26.011 29.024  1.00 23.24 ? 197 ASP A OD1 1 
ATOM   3528 O OD2 . ASP B  2 200 ? -3.832  -26.536 29.672  1.00 25.56 ? 197 ASP A OD2 1 
ATOM   3529 N N   . GLU B  2 201 ? -5.781  -22.287 32.629  1.00 24.00 ? 198 GLU A N   1 
ATOM   3530 C CA  . GLU B  2 201 ? -6.028  -21.618 33.900  1.00 24.95 ? 198 GLU A CA  1 
ATOM   3531 C C   . GLU B  2 201 ? -7.430  -20.995 33.960  1.00 25.49 ? 198 GLU A C   1 
ATOM   3532 O O   . GLU B  2 201 ? -8.051  -20.991 35.022  1.00 25.23 ? 198 GLU A O   1 
ATOM   3533 C CB  . GLU B  2 201 ? -4.971  -20.557 34.175  1.00 26.01 ? 198 GLU A CB  1 
ATOM   3534 C CG  . GLU B  2 201 ? -3.580  -21.117 34.470  1.00 29.15 ? 198 GLU A CG  1 
ATOM   3535 C CD  . GLU B  2 201 ? -2.487  -20.038 34.505  1.00 30.08 ? 198 GLU A CD  1 
ATOM   3536 O OE1 . GLU B  2 201 ? -2.626  -18.953 33.942  1.00 31.68 ? 198 GLU A OE1 1 
ATOM   3537 O OE2 . GLU B  2 201 ? -1.443  -20.329 35.082  1.00 33.64 ? 198 GLU A OE2 1 
ATOM   3538 N N   . ALA B  2 202 ? -7.925  -20.458 32.837  1.00 23.50 ? 199 ALA A N   1 
ATOM   3539 C CA  . ALA B  2 202 ? -9.289  -19.946 32.755  1.00 24.30 ? 199 ALA A CA  1 
ATOM   3540 C C   . ALA B  2 202 ? -10.361 -21.037 32.777  1.00 25.64 ? 199 ALA A C   1 
ATOM   3541 O O   . ALA B  2 202 ? -11.380 -20.841 33.437  1.00 24.99 ? 199 ALA A O   1 
ATOM   3542 C CB  . ALA B  2 202 ? -9.416  -19.048 31.556  1.00 24.03 ? 199 ALA A CB  1 
ATOM   3543 N N   . ILE B  2 203 ? -10.150 -22.190 32.089  1.00 27.01 ? 200 ILE A N   1 
ATOM   3544 C CA  . ILE B  2 203 ? -11.062 -23.338 32.143  1.00 30.37 ? 200 ILE A CA  1 
ATOM   3545 C C   . ILE B  2 203 ? -11.352 -23.749 33.581  1.00 32.61 ? 200 ILE A C   1 
ATOM   3546 O O   . ILE B  2 203 ? -12.517 -23.971 33.897  1.00 30.47 ? 200 ILE A O   1 
ATOM   3547 C CB  . ILE B  2 203 ? -10.537 -24.550 31.331  1.00 31.41 ? 200 ILE A CB  1 
ATOM   3548 C CG1 . ILE B  2 203 ? -10.702 -24.302 29.877  1.00 32.80 ? 200 ILE A CG1 1 
ATOM   3549 C CG2 . ILE B  2 203 ? -11.139 -25.919 31.710  1.00 34.32 ? 200 ILE A CG2 1 
ATOM   3550 C CD1 . ILE B  2 203 ? -12.115 -24.463 29.322  1.00 35.14 ? 200 ILE A CD1 1 
ATOM   3551 N N   . ALA B  2 204 ? -10.298 -23.790 34.418  1.00 35.13 ? 201 ALA A N   1 
ATOM   3552 C CA  . ALA B  2 204 ? -10.435 -24.269 35.783  1.00 36.67 ? 201 ALA A CA  1 
ATOM   3553 C C   . ALA B  2 204 ? -11.364 -23.382 36.630  1.00 36.71 ? 201 ALA A C   1 
ATOM   3554 O O   . ALA B  2 204 ? -11.863 -23.911 37.625  1.00 37.70 ? 201 ALA A O   1 
ATOM   3555 C CB  . ALA B  2 204 ? -9.057  -24.457 36.396  1.00 36.43 ? 201 ALA A CB  1 
ATOM   3556 N N   . GLU B  2 205 ? -11.614 -22.100 36.267  1.00 34.67 ? 202 GLU A N   1 
ATOM   3557 C CA  . GLU B  2 205 ? -12.464 -21.200 37.054  1.00 37.10 ? 202 GLU A CA  1 
ATOM   3558 C C   . GLU B  2 205 ? -13.716 -20.679 36.326  1.00 38.75 ? 202 GLU A C   1 
ATOM   3559 O O   . GLU B  2 205 ? -14.333 -19.686 36.749  1.00 38.51 ? 202 GLU A O   1 
ATOM   3560 C CB  . GLU B  2 205 ? -11.515 -20.107 37.547  1.00 37.31 ? 202 GLU A CB  1 
ATOM   3561 C CG  . GLU B  2 205 ? -10.542 -20.606 38.599  1.00 40.79 ? 202 GLU A CG  1 
ATOM   3562 C CD  . GLU B  2 205 ? -9.690  -19.512 39.206  1.00 46.45 ? 202 GLU A CD  1 
ATOM   3563 O OE1 . GLU B  2 205 ? -9.952  -18.257 39.134  1.00 44.38 ? 202 GLU A OE1 1 
ATOM   3564 O OE2 . GLU B  2 205 ? -8.689  -19.999 39.787  1.00 56.69 ? 202 GLU A OE2 1 
ATOM   3565 N N   . LEU B  2 206 ? -14.161 -21.377 35.270  1.00 39.16 ? 203 LEU A N   1 
ATOM   3566 C CA  . LEU B  2 206 ? -15.241 -20.890 34.408  1.00 40.94 ? 203 LEU A CA  1 
ATOM   3567 C C   . LEU B  2 206 ? -16.604 -20.967 35.107  1.00 43.56 ? 203 LEU A C   1 
ATOM   3568 O O   . LEU B  2 206 ? -17.453 -20.085 34.922  1.00 40.03 ? 203 LEU A O   1 
ATOM   3569 C CB  . LEU B  2 206 ? -15.211 -21.698 33.107  1.00 42.58 ? 203 LEU A CB  1 
ATOM   3570 C CG  . LEU B  2 206 ? -15.316 -20.925 31.799  1.00 42.04 ? 203 LEU A CG  1 
ATOM   3571 C CD1 . LEU B  2 206 ? -14.511 -19.644 31.642  1.00 38.35 ? 203 LEU A CD1 1 
ATOM   3572 C CD2 . LEU B  2 206 ? -14.963 -21.936 30.703  1.00 42.38 ? 203 LEU A CD2 1 
ATOM   3573 N N   . ASP B  2 207 ? -16.786 -22.040 35.906  1.00 48.96 ? 204 ASP A N   1 
ATOM   3574 C CA  . ASP B  2 207 ? -17.940 -22.281 36.766  1.00 52.96 ? 204 ASP A CA  1 
ATOM   3575 C C   . ASP B  2 207 ? -18.240 -21.141 37.750  1.00 54.16 ? 204 ASP A C   1 
ATOM   3576 O O   . ASP B  2 207 ? -19.378 -21.092 38.225  1.00 55.09 ? 204 ASP A O   1 
ATOM   3577 C CB  . ASP B  2 207 ? -17.785 -23.586 37.546  1.00 54.16 ? 204 ASP A CB  1 
ATOM   3578 C CG  . ASP B  2 207 ? -16.580 -23.701 38.484  1.00 58.73 ? 204 ASP A CG  1 
ATOM   3579 O OD1 . ASP B  2 207 ? -15.630 -22.870 38.399  1.00 62.20 ? 204 ASP A OD1 1 
ATOM   3580 O OD2 . ASP B  2 207 ? -16.578 -24.628 39.318  1.00 60.75 ? 204 ASP A OD2 1 
ATOM   3581 N N   . THR B  2 208 ? -17.243 -20.298 38.099  1.00 49.27 ? 205 THR A N   1 
ATOM   3582 C CA  . THR B  2 208 ? -17.418 -19.190 39.025  1.00 51.09 ? 205 THR A CA  1 
ATOM   3583 C C   . THR B  2 208 ? -18.114 -17.977 38.385  1.00 49.53 ? 205 THR A C   1 
ATOM   3584 O O   . THR B  2 208 ? -18.562 -17.133 39.146  1.00 56.21 ? 205 THR A O   1 
ATOM   3585 C CB  . THR B  2 208 ? -16.083 -18.804 39.676  1.00 50.74 ? 205 THR A CB  1 
ATOM   3586 O OG1 . THR B  2 208 ? -15.282 -18.112 38.723  1.00 46.87 ? 205 THR A OG1 1 
ATOM   3587 C CG2 . THR B  2 208 ? -15.334 -19.984 40.284  1.00 53.11 ? 205 THR A CG2 1 
ATOM   3588 N N   . LEU B  2 209 ? -18.241 -17.856 37.049  1.00 44.81 ? 206 LEU A N   1 
ATOM   3589 C CA  . LEU B  2 209 ? -18.577 -16.585 36.406  1.00 42.55 ? 206 LEU A CA  1 
ATOM   3590 C C   . LEU B  2 209 ? -20.083 -16.384 36.284  1.00 44.18 ? 206 LEU A C   1 
ATOM   3591 O O   . LEU B  2 209 ? -20.811 -17.343 36.101  1.00 45.88 ? 206 LEU A O   1 
ATOM   3592 C CB  . LEU B  2 209 ? -17.948 -16.526 35.019  1.00 37.64 ? 206 LEU A CB  1 
ATOM   3593 C CG  . LEU B  2 209 ? -16.424 -16.668 34.992  1.00 37.21 ? 206 LEU A CG  1 
ATOM   3594 C CD1 . LEU B  2 209 ? -15.955 -16.557 33.560  1.00 34.36 ? 206 LEU A CD1 1 
ATOM   3595 C CD2 . LEU B  2 209 ? -15.724 -15.617 35.862  1.00 37.59 ? 206 LEU A CD2 1 
ATOM   3596 N N   . SER B  2 210 ? -20.517 -15.113 36.243  1.00 45.09 ? 207 SER A N   1 
ATOM   3597 C CA  . SER B  2 210 ? -21.835 -14.734 35.748  1.00 44.74 ? 207 SER A CA  1 
ATOM   3598 C C   . SER B  2 210 ? -21.962 -15.076 34.265  1.00 45.20 ? 207 SER A C   1 
ATOM   3599 O O   . SER B  2 210 ? -20.958 -15.198 33.550  1.00 45.05 ? 207 SER A O   1 
ATOM   3600 C CB  . SER B  2 210 ? -22.093 -13.252 35.944  1.00 43.09 ? 207 SER A CB  1 
ATOM   3601 O OG  . SER B  2 210 ? -21.197 -12.456 35.179  1.00 39.23 ? 207 SER A OG  1 
ATOM   3602 N N   . GLU B  2 211 ? -23.211 -15.133 33.797  1.00 47.71 ? 208 GLU A N   1 
ATOM   3603 C CA  . GLU B  2 211 ? -23.517 -15.323 32.384  1.00 49.35 ? 208 GLU A CA  1 
ATOM   3604 C C   . GLU B  2 211 ? -22.796 -14.309 31.482  1.00 48.10 ? 208 GLU A C   1 
ATOM   3605 O O   . GLU B  2 211 ? -22.211 -14.719 30.467  1.00 46.79 ? 208 GLU A O   1 
ATOM   3606 C CB  . GLU B  2 211 ? -25.038 -15.344 32.271  1.00 54.43 ? 208 GLU A CB  1 
ATOM   3607 C CG  . GLU B  2 211 ? -25.560 -15.488 30.848  1.00 55.77 ? 208 GLU A CG  1 
ATOM   3608 C CD  . GLU B  2 211 ? -27.025 -15.849 30.859  1.00 62.90 ? 208 GLU A CD  1 
ATOM   3609 O OE1 . GLU B  2 211 ? -27.804 -15.197 31.586  1.00 65.82 ? 208 GLU A OE1 1 
ATOM   3610 O OE2 . GLU B  2 211 ? -27.390 -16.797 30.142  1.00 70.67 ? 208 GLU A OE2 1 
ATOM   3611 N N   . GLU B  2 212 ? -22.791 -13.013 31.855  1.00 46.90 ? 209 GLU A N   1 
ATOM   3612 C CA  . GLU B  2 212 ? -22.170 -11.983 31.009  1.00 48.41 ? 209 GLU A CA  1 
ATOM   3613 C C   . GLU B  2 212 ? -20.633 -12.099 31.019  1.00 40.23 ? 209 GLU A C   1 
ATOM   3614 O O   . GLU B  2 212 ? -19.997 -11.876 30.001  1.00 37.71 ? 209 GLU A O   1 
ATOM   3615 C CB  . GLU B  2 212 ? -22.590 -10.547 31.345  1.00 53.75 ? 209 GLU A CB  1 
ATOM   3616 C CG  . GLU B  2 212 ? -22.376 -9.558  30.194  1.00 55.09 ? 209 GLU A CG  1 
ATOM   3617 C CD  . GLU B  2 212 ? -21.620 -8.255  30.472  1.00 58.03 ? 209 GLU A CD  1 
ATOM   3618 O OE1 . GLU B  2 212 ? -22.047 -7.436  31.329  1.00 54.75 ? 209 GLU A OE1 1 
ATOM   3619 O OE2 . GLU B  2 212 ? -20.573 -8.052  29.797  1.00 64.96 ? 209 GLU A OE2 1 
ATOM   3620 N N   . SER B  2 213 ? -20.051 -12.437 32.176  1.00 38.15 ? 210 SER A N   1 
ATOM   3621 C CA  . SER B  2 213 ? -18.612 -12.666 32.318  1.00 36.32 ? 210 SER A CA  1 
ATOM   3622 C C   . SER B  2 213 ? -18.141 -13.888 31.520  1.00 32.56 ? 210 SER A C   1 
ATOM   3623 O O   . SER B  2 213 ? -17.125 -13.799 30.822  1.00 28.85 ? 210 SER A O   1 
ATOM   3624 C CB  . SER B  2 213 ? -18.223 -12.796 33.795  1.00 37.27 ? 210 SER A CB  1 
ATOM   3625 O OG  . SER B  2 213 ? -18.251 -11.508 34.415  1.00 37.99 ? 210 SER A OG  1 
ATOM   3626 N N   . TYR B  2 214 ? -18.929 -14.978 31.582  1.00 32.99 ? 211 TYR A N   1 
ATOM   3627 C CA  . TYR B  2 214 ? -18.725 -16.195 30.799  1.00 31.74 ? 211 TYR A CA  1 
ATOM   3628 C C   . TYR B  2 214 ? -18.656 -15.879 29.309  1.00 32.17 ? 211 TYR A C   1 
ATOM   3629 O O   . TYR B  2 214 ? -17.721 -16.319 28.656  1.00 31.86 ? 211 TYR A O   1 
ATOM   3630 C CB  . TYR B  2 214 ? -19.840 -17.194 31.138  1.00 35.84 ? 211 TYR A CB  1 
ATOM   3631 C CG  . TYR B  2 214 ? -19.647 -18.573 30.525  1.00 35.63 ? 211 TYR A CG  1 
ATOM   3632 C CD1 . TYR B  2 214 ? -20.080 -18.864 29.223  1.00 34.83 ? 211 TYR A CD1 1 
ATOM   3633 C CD2 . TYR B  2 214 ? -19.075 -19.608 31.277  1.00 35.92 ? 211 TYR A CD2 1 
ATOM   3634 C CE1 . TYR B  2 214 ? -19.876 -20.123 28.662  1.00 34.67 ? 211 TYR A CE1 1 
ATOM   3635 C CE2 . TYR B  2 214 ? -18.898 -20.880 30.739  1.00 35.66 ? 211 TYR A CE2 1 
ATOM   3636 C CZ  . TYR B  2 214 ? -19.293 -21.125 29.430  1.00 35.18 ? 211 TYR A CZ  1 
ATOM   3637 O OH  . TYR B  2 214 ? -19.089 -22.340 28.907  1.00 39.65 ? 211 TYR A OH  1 
ATOM   3638 N N   . LYS B  2 215 ? -19.558 -15.041 28.785  1.00 33.02 ? 212 LYS A N   1 
ATOM   3639 C CA  . LYS B  2 215 ? -19.580 -14.671 27.365  1.00 35.25 ? 212 LYS A CA  1 
ATOM   3640 C C   . LYS B  2 215 ? -18.285 -13.971 26.937  1.00 31.05 ? 212 LYS A C   1 
ATOM   3641 O O   . LYS B  2 215 ? -17.670 -14.300 25.911  1.00 27.83 ? 212 LYS A O   1 
ATOM   3642 C CB  . LYS B  2 215 ? -20.790 -13.767 27.094  1.00 40.11 ? 212 LYS A CB  1 
ATOM   3643 C CG  . LYS B  2 215 ? -21.121 -13.341 25.665  1.00 46.37 ? 212 LYS A CG  1 
ATOM   3644 C CD  . LYS B  2 215 ? -22.061 -12.130 25.603  1.00 52.04 ? 212 LYS A CD  1 
ATOM   3645 C CE  . LYS B  2 215 ? -21.336 -10.804 25.799  1.00 55.51 ? 212 LYS A CE  1 
ATOM   3646 N NZ  . LYS B  2 215 ? -22.196 -9.755  26.362  1.00 59.94 ? 212 LYS A NZ  1 
ATOM   3647 N N   . ASP B  2 216 ? -17.885 -12.980 27.731  1.00 29.10 ? 213 ASP A N   1 
ATOM   3648 C CA  . ASP B  2 216 ? -16.677 -12.215 27.465  1.00 27.76 ? 213 ASP A CA  1 
ATOM   3649 C C   . ASP B  2 216 ? -15.424 -13.096 27.490  1.00 25.49 ? 213 ASP A C   1 
ATOM   3650 O O   . ASP B  2 216 ? -14.535 -12.929 26.615  1.00 25.76 ? 213 ASP A O   1 
ATOM   3651 C CB  . ASP B  2 216 ? -16.550 -11.064 28.464  1.00 29.56 ? 213 ASP A CB  1 
ATOM   3652 C CG  . ASP B  2 216 ? -17.577 -9.936  28.319  1.00 30.62 ? 213 ASP A CG  1 
ATOM   3653 O OD1 . ASP B  2 216 ? -17.949 -9.607  27.197  1.00 33.06 ? 213 ASP A OD1 1 
ATOM   3654 O OD2 . ASP B  2 216 ? -17.900 -9.338  29.318  1.00 37.51 ? 213 ASP A OD2 1 
ATOM   3655 N N   . SER B  2 217 ? -15.326 -13.941 28.535  1.00 24.84 ? 214 SER A N   1 
ATOM   3656 C CA  . SER B  2 217 ? -14.146 -14.758 28.749  1.00 23.35 ? 214 SER A CA  1 
ATOM   3657 C C   . SER B  2 217 ? -14.073 -15.810 27.653  1.00 22.35 ? 214 SER A C   1 
ATOM   3658 O O   . SER B  2 217 ? -13.025 -15.951 27.046  1.00 21.43 ? 214 SER A O   1 
ATOM   3659 C CB  . SER B  2 217 ? -14.147 -15.397 30.087  1.00 24.58 ? 214 SER A CB  1 
ATOM   3660 O OG  . SER B  2 217 ? -14.086 -14.400 31.105  1.00 25.47 ? 214 SER A OG  1 
ATOM   3661 N N   . THR B  2 218 ? -15.197 -16.521 27.425  1.00 23.44 ? 215 THR A N   1 
ATOM   3662 C CA  . THR B  2 218 ? -15.193 -17.605 26.433  1.00 24.58 ? 215 THR A CA  1 
ATOM   3663 C C   . THR B  2 218 ? -14.913 -17.102 25.006  1.00 23.86 ? 215 THR A C   1 
ATOM   3664 O O   . THR B  2 218 ? -14.279 -17.821 24.249  1.00 25.22 ? 215 THR A O   1 
ATOM   3665 C CB  . THR B  2 218 ? -16.428 -18.506 26.512  1.00 25.22 ? 215 THR A CB  1 
ATOM   3666 O OG1 . THR B  2 218 ? -17.570 -17.704 26.321  1.00 26.57 ? 215 THR A OG1 1 
ATOM   3667 C CG2 . THR B  2 218 ? -16.552 -19.246 27.827  1.00 27.05 ? 215 THR A CG2 1 
ATOM   3668 N N   . LEU B  2 219 ? -15.313 -15.886 24.642  1.00 23.16 ? 216 LEU A N   1 
ATOM   3669 C CA  . LEU B  2 219 ? -14.966 -15.295 23.361  1.00 23.27 ? 216 LEU A CA  1 
ATOM   3670 C C   . LEU B  2 219 ? -13.447 -15.229 23.128  1.00 21.87 ? 216 LEU A C   1 
ATOM   3671 O O   . LEU B  2 219 ? -12.966 -15.560 22.044  1.00 20.10 ? 216 LEU A O   1 
ATOM   3672 C CB  . LEU B  2 219 ? -15.633 -13.936 23.221  1.00 25.45 ? 216 LEU A CB  1 
ATOM   3673 C CG  . LEU B  2 219 ? -15.558 -13.323 21.816  1.00 29.51 ? 216 LEU A CG  1 
ATOM   3674 C CD1 . LEU B  2 219 ? -16.887 -12.708 21.396  1.00 34.76 ? 216 LEU A CD1 1 
ATOM   3675 C CD2 . LEU B  2 219 ? -14.497 -12.262 21.729  1.00 31.15 ? 216 LEU A CD2 1 
ATOM   3676 N N   . ILE B  2 220 ? -12.692 -14.823 24.159  1.00 18.98 ? 217 ILE A N   1 
ATOM   3677 C CA  . ILE B  2 220 ? -11.231 -14.749 24.093  1.00 18.83 ? 217 ILE A CA  1 
ATOM   3678 C C   . ILE B  2 220 ? -10.630 -16.145 24.196  1.00 16.60 ? 217 ILE A C   1 
ATOM   3679 O O   . ILE B  2 220 ? -9.653  -16.420 23.524  1.00 17.76 ? 217 ILE A O   1 
ATOM   3680 C CB  . ILE B  2 220 ? -10.618 -13.703 25.052  1.00 19.26 ? 217 ILE A CB  1 
ATOM   3681 C CG1 . ILE B  2 220 ? -11.298 -12.332 24.743  1.00 21.39 ? 217 ILE A CG1 1 
ATOM   3682 C CG2 . ILE B  2 220 ? -9.093  -13.644 24.860  1.00 18.70 ? 217 ILE A CG2 1 
ATOM   3683 C CD1 . ILE B  2 220 ? -10.775 -11.127 25.501  1.00 21.73 ? 217 ILE A CD1 1 
ATOM   3684 N N   . MET B  2 221 ? -11.202 -17.039 24.991  1.00 18.30 ? 218 MET A N   1 
ATOM   3685 C CA  . MET B  2 221 ? -10.745 -18.417 25.079  1.00 18.55 ? 218 MET A CA  1 
ATOM   3686 C C   . MET B  2 221 ? -10.908 -19.122 23.724  1.00 19.61 ? 218 MET A C   1 
ATOM   3687 O O   . MET B  2 221 ? -10.036 -19.887 23.351  1.00 17.40 ? 218 MET A O   1 
ATOM   3688 C CB  . MET B  2 221 ? -11.468 -19.153 26.201  1.00 20.57 ? 218 MET A CB  1 
ATOM   3689 C CG  . MET B  2 221 ? -11.070 -18.620 27.578  1.00 22.01 ? 218 MET A CG  1 
ATOM   3690 S SD  . MET B  2 221 ? -12.164 -19.334 28.787  1.00 24.50 ? 218 MET A SD  1 
ATOM   3691 C CE  . MET B  2 221 ? -11.425 -20.963 28.889  1.00 25.58 ? 218 MET A CE  1 
ATOM   3692 N N   . GLN B  2 222 ? -11.985 -18.832 22.986  1.00 19.04 ? 219 GLN A N   1 
ATOM   3693 C CA  . GLN B  2 222 ? -12.145 -19.339 21.637  1.00 20.84 ? 219 GLN A CA  1 
ATOM   3694 C C   . GLN B  2 222 ? -11.028 -18.876 20.707  1.00 17.96 ? 219 GLN A C   1 
ATOM   3695 O O   . GLN B  2 222 ? -10.524 -19.707 19.952  1.00 19.02 ? 219 GLN A O   1 
ATOM   3696 C CB  . GLN B  2 222 ? -13.539 -19.022 21.096  1.00 25.06 ? 219 GLN A CB  1 
ATOM   3697 C CG  . GLN B  2 222 ? -13.915 -19.759 19.806  1.00 30.17 ? 219 GLN A CG  1 
ATOM   3698 C CD  . GLN B  2 222 ? -13.906 -21.271 19.952  1.00 34.53 ? 219 GLN A CD  1 
ATOM   3699 O OE1 . GLN B  2 222 ? -14.491 -21.819 20.889  1.00 35.64 ? 219 GLN A OE1 1 
ATOM   3700 N NE2 . GLN B  2 222 ? -13.143 -21.954 19.103  1.00 36.28 ? 219 GLN A NE2 1 
ATOM   3701 N N   . LEU B  2 223 ? -10.608 -17.617 20.793  1.00 17.65 ? 220 LEU A N   1 
ATOM   3702 C CA  . LEU B  2 223 ? -9.505  -17.101 19.973  1.00 16.46 ? 220 LEU A CA  1 
ATOM   3703 C C   . LEU B  2 223 ? -8.197  -17.802 20.307  1.00 16.69 ? 220 LEU A C   1 
ATOM   3704 O O   . LEU B  2 223 ? -7.408  -18.067 19.393  1.00 16.98 ? 220 LEU A O   1 
ATOM   3705 C CB  . LEU B  2 223 ? -9.395  -15.598 20.167  1.00 16.84 ? 220 LEU A CB  1 
ATOM   3706 C CG  . LEU B  2 223 ? -10.591 -14.806 19.653  1.00 17.36 ? 220 LEU A CG  1 
ATOM   3707 C CD1 . LEU B  2 223 ? -10.431 -13.349 20.002  1.00 18.38 ? 220 LEU A CD1 1 
ATOM   3708 C CD2 . LEU B  2 223 ? -10.698 -14.939 18.112  1.00 19.01 ? 220 LEU A CD2 1 
ATOM   3709 N N   . LEU B  2 224 ? -7.931  -18.015 21.614  1.00 17.29 ? 221 LEU A N   1 
ATOM   3710 C CA  . LEU B  2 224 ? -6.767  -18.805 22.036  1.00 16.47 ? 221 LEU A CA  1 
ATOM   3711 C C   . LEU B  2 224 ? -6.776  -20.200 21.406  1.00 17.31 ? 221 LEU A C   1 
ATOM   3712 O O   . LEU B  2 224 ? -5.766  -20.606 20.818  1.00 16.59 ? 221 LEU A O   1 
ATOM   3713 C CB  . LEU B  2 224 ? -6.738  -18.873 23.566  1.00 17.37 ? 221 LEU A CB  1 
ATOM   3714 C CG  . LEU B  2 224 ? -6.238  -17.638 24.293  1.00 17.50 ? 221 LEU A CG  1 
ATOM   3715 C CD1 . LEU B  2 224 ? -6.629  -17.757 25.741  1.00 18.87 ? 221 LEU A CD1 1 
ATOM   3716 C CD2 . LEU B  2 224 ? -4.746  -17.385 24.170  1.00 17.09 ? 221 LEU A CD2 1 
ATOM   3717 N N   . ARG B  2 225 ? -7.898  -20.932 21.549  1.00 18.50 ? 222 ARG A N   1 
ATOM   3718 C CA  . ARG B  2 225 ? -8.064  -22.265 21.003  1.00 20.68 ? 222 ARG A CA  1 
ATOM   3719 C C   . ARG B  2 225 ? -7.855  -22.254 19.494  1.00 19.72 ? 222 ARG A C   1 
ATOM   3720 O O   . ARG B  2 225 ? -7.205  -23.157 18.964  1.00 19.12 ? 222 ARG A O   1 
ATOM   3721 C CB  . ARG B  2 225 ? -9.422  -22.901 21.355  1.00 24.96 ? 222 ARG A CB  1 
ATOM   3722 C CG  . ARG B  2 225 ? -9.767  -24.213 20.667  1.00 30.09 ? 222 ARG A CG  1 
ATOM   3723 C CD  . ARG B  2 225 ? -10.887 -24.912 21.366  1.00 35.80 ? 222 ARG A CD  1 
ATOM   3724 N NE  . ARG B  2 225 ? -11.190 -26.207 20.749  1.00 44.09 ? 222 ARG A NE  1 
ATOM   3725 C CZ  . ARG B  2 225 ? -12.269 -26.925 21.053  1.00 51.67 ? 222 ARG A CZ  1 
ATOM   3726 N NH1 . ARG B  2 225 ? -13.065 -26.567 22.051  1.00 55.29 ? 222 ARG A NH1 1 
ATOM   3727 N NH2 . ARG B  2 225 ? -12.568 -27.998 20.344  1.00 55.25 ? 222 ARG A NH2 1 
ATOM   3728 N N   . ASP B  2 226 ? -8.433  -21.255 18.794  1.00 19.16 ? 223 ASP A N   1 
ATOM   3729 C CA  . ASP B  2 226 ? -8.324  -21.202 17.334  1.00 18.87 ? 223 ASP A CA  1 
ATOM   3730 C C   . ASP B  2 226 ? -6.861  -21.001 16.894  1.00 16.94 ? 223 ASP A C   1 
ATOM   3731 O O   . ASP B  2 226 ? -6.443  -21.615 15.919  1.00 18.11 ? 223 ASP A O   1 
ATOM   3732 C CB  . ASP B  2 226 ? -9.164  -20.063 16.771  1.00 19.42 ? 223 ASP A CB  1 
ATOM   3733 C CG  . ASP B  2 226 ? -10.673 -20.233 16.863  1.00 21.79 ? 223 ASP A CG  1 
ATOM   3734 O OD1 . ASP B  2 226 ? -11.133 -21.304 17.159  1.00 23.80 ? 223 ASP A OD1 1 
ATOM   3735 O OD2 . ASP B  2 226 ? -11.374 -19.237 16.686  1.00 26.94 ? 223 ASP A OD2 1 
ATOM   3736 N N   . ASN B  2 227 ? -6.108  -20.157 17.590  1.00 16.54 ? 224 ASN A N   1 
ATOM   3737 C CA  . ASN B  2 227 ? -4.694  -19.952 17.290  1.00 15.86 ? 224 ASN A CA  1 
ATOM   3738 C C   . ASN B  2 227 ? -3.888  -21.232 17.533  1.00 16.03 ? 224 ASN A C   1 
ATOM   3739 O O   . ASN B  2 227 ? -3.113  -21.612 16.652  1.00 16.28 ? 224 ASN A O   1 
ATOM   3740 C CB  . ASN B  2 227 ? -4.105  -18.776 18.041  1.00 15.69 ? 224 ASN A CB  1 
ATOM   3741 C CG  . ASN B  2 227 ? -4.503  -17.428 17.462  1.00 15.62 ? 224 ASN A CG  1 
ATOM   3742 O OD1 . ASN B  2 227 ? -5.225  -17.311 16.449  1.00 16.44 ? 224 ASN A OD1 1 
ATOM   3743 N ND2 . ASN B  2 227 ? -4.009  -16.394 18.111  1.00 15.68 ? 224 ASN A ND2 1 
ATOM   3744 N N   . LEU B  2 228 ? -4.126  -21.898 18.679  1.00 16.14 ? 225 LEU A N   1 
ATOM   3745 C CA  . LEU B  2 228 ? -3.492  -23.187 18.974  1.00 17.67 ? 225 LEU A CA  1 
ATOM   3746 C C   . LEU B  2 228 ? -3.738  -24.212 17.860  1.00 18.49 ? 225 LEU A C   1 
ATOM   3747 O O   . LEU B  2 228 ? -2.807  -24.928 17.485  1.00 18.07 ? 225 LEU A O   1 
ATOM   3748 C CB  . LEU B  2 228 ? -3.941  -23.694 20.348  1.00 18.59 ? 225 LEU A CB  1 
ATOM   3749 C CG  . LEU B  2 228 ? -3.406  -22.882 21.530  1.00 18.86 ? 225 LEU A CG  1 
ATOM   3750 C CD1 . LEU B  2 228 ? -4.101  -23.154 22.830  1.00 19.81 ? 225 LEU A CD1 1 
ATOM   3751 C CD2 . LEU B  2 228 ? -1.900  -23.081 21.682  1.00 19.78 ? 225 LEU A CD2 1 
ATOM   3752 N N   . THR B  2 229 ? -4.985  -24.249 17.341  1.00 18.29 ? 226 THR A N   1 
ATOM   3753 C CA  . THR B  2 229 ? -5.379  -25.192 16.315  1.00 19.19 ? 226 THR A CA  1 
ATOM   3754 C C   . THR B  2 229 ? -4.663  -24.893 14.996  1.00 18.93 ? 226 THR A C   1 
ATOM   3755 O O   . THR B  2 229 ? -4.111  -25.819 14.349  1.00 20.06 ? 226 THR A O   1 
ATOM   3756 C CB  . THR B  2 229 ? -6.908  -25.213 16.221  1.00 20.59 ? 226 THR A CB  1 
ATOM   3757 O OG1 . THR B  2 229 ? -7.390  -25.660 17.499  1.00 21.06 ? 226 THR A OG1 1 
ATOM   3758 C CG2 . THR B  2 229 ? -7.433  -26.193 15.188  1.00 22.07 ? 226 THR A CG2 1 
ATOM   3759 N N   . LEU B  2 230 ? -4.743  -23.622 14.591  1.00 18.39 ? 227 LEU A N   1 
ATOM   3760 C CA  . LEU B  2 230 ? -4.066  -23.076 13.422  1.00 18.41 ? 227 LEU A CA  1 
ATOM   3761 C C   . LEU B  2 230 ? -2.574  -23.397 13.452  1.00 17.77 ? 227 LEU A C   1 
ATOM   3762 O O   . LEU B  2 230 ? -2.056  -23.971 12.514  1.00 17.64 ? 227 LEU A O   1 
ATOM   3763 C CB  . LEU B  2 230 ? -4.330  -21.576 13.342  1.00 17.78 ? 227 LEU A CB  1 
ATOM   3764 C CG  . LEU B  2 230 ? -3.615  -20.827 12.211  1.00 18.98 ? 227 LEU A CG  1 
ATOM   3765 C CD1 . LEU B  2 230 ? -4.077  -21.303 10.841  1.00 19.97 ? 227 LEU A CD1 1 
ATOM   3766 C CD2 . LEU B  2 230 ? -3.779  -19.337 12.320  1.00 17.68 ? 227 LEU A CD2 1 
ATOM   3767 N N   . TRP B  2 231 ? -1.924  -23.109 14.573  1.00 17.69 ? 228 TRP A N   1 
ATOM   3768 C CA  . TRP B  2 231 ? -0.470  -23.202 14.642  1.00 18.49 ? 228 TRP A CA  1 
ATOM   3769 C C   . TRP B  2 231 ? 0.039   -24.636 14.640  1.00 19.29 ? 228 TRP A C   1 
ATOM   3770 O O   . TRP B  2 231 ? 0.948   -24.934 13.863  1.00 21.09 ? 228 TRP A O   1 
ATOM   3771 C CB  . TRP B  2 231 ? -0.004  -22.393 15.865  1.00 17.54 ? 228 TRP A CB  1 
ATOM   3772 C CG  . TRP B  2 231 ? -0.171  -20.915 15.697  1.00 18.02 ? 228 TRP A CG  1 
ATOM   3773 C CD1 . TRP B  2 231 ? -0.295  -20.141 14.578  1.00 18.20 ? 228 TRP A CD1 1 
ATOM   3774 C CD2 . TRP B  2 231 ? -0.176  -19.995 16.801  1.00 17.76 ? 228 TRP A CD2 1 
ATOM   3775 N NE1 . TRP B  2 231 ? -0.387  -18.828 14.925  1.00 17.00 ? 228 TRP A NE1 1 
ATOM   3776 C CE2 . TRP B  2 231 ? -0.326  -18.699 16.272  1.00 17.45 ? 228 TRP A CE2 1 
ATOM   3777 C CE3 . TRP B  2 231 ? -0.083  -20.164 18.178  1.00 18.30 ? 228 TRP A CE3 1 
ATOM   3778 C CZ2 . TRP B  2 231 ? -0.340  -17.569 17.079  1.00 17.89 ? 228 TRP A CZ2 1 
ATOM   3779 C CZ3 . TRP B  2 231 ? -0.168  -19.054 18.996  1.00 18.12 ? 228 TRP A CZ3 1 
ATOM   3780 C CH2 . TRP B  2 231 ? -0.297  -17.761 18.451  1.00 17.26 ? 228 TRP A CH2 1 
ATOM   3781 N N   . THR B  2 232 ? -0.614  -25.547 15.377  1.00 19.24 ? 229 THR A N   1 
ATOM   3782 C CA  . THR B  2 232 ? -0.160  -26.926 15.546  1.00 20.99 ? 229 THR A CA  1 
ATOM   3783 C C   . THR B  2 232 ? -0.673  -27.790 14.414  1.00 22.03 ? 229 THR A C   1 
ATOM   3784 O O   . THR B  2 232 ? 0.092   -28.572 13.858  1.00 21.60 ? 229 THR A O   1 
ATOM   3785 C CB  . THR B  2 232 ? -0.603  -27.486 16.896  1.00 21.44 ? 229 THR A CB  1 
ATOM   3786 O OG1 . THR B  2 232 ? -2.031  -27.400 17.005  1.00 21.01 ? 229 THR A OG1 1 
ATOM   3787 C CG2 . THR B  2 232 ? 0.033   -26.686 18.030  1.00 20.40 ? 229 THR A CG2 1 
ATOM   3788 N N   . GLY B  2 233 ? -1.951  -27.568 14.028  1.00 22.16 ? 230 GLY A N   1 
ATOM   3789 C CA  . GLY B  2 233 ? -2.628  -28.394 13.056  1.00 23.29 ? 230 GLY A CA  1 
ATOM   3790 C C   . GLY B  2 233 ? -2.435  -27.961 11.604  1.00 23.82 ? 230 GLY A C   1 
ATOM   3791 O O   . GLY B  2 233 ? -2.618  -28.765 10.723  1.00 24.26 ? 230 GLY A O   1 
ATOM   3792 N N   . GLY B  2 234 ? -2.096  -26.693 11.369  1.00 23.25 ? 231 GLY A N   1 
ATOM   3793 C CA  . GLY B  2 234 ? -1.980  -26.130 10.039  1.00 25.00 ? 231 GLY A CA  1 
ATOM   3794 C C   . GLY B  2 234 ? -3.276  -25.434 9.626   1.00 24.68 ? 231 GLY A C   1 
ATOM   3795 O O   . GLY B  2 234 ? -4.347  -25.595 10.229  1.00 23.68 ? 231 GLY A O   1 
ATOM   3796 N N   . GLY B  2 235 ? -3.135  -24.613 8.605   1.00 26.01 ? 232 GLY A N   1 
ATOM   3797 C CA  . GLY B  2 235 ? -4.237  -23.813 8.111   1.00 26.28 ? 232 GLY A CA  1 
ATOM   3798 C C   . GLY B  2 235 ? -3.727  -22.572 7.402   1.00 25.47 ? 232 GLY A C   1 
ATOM   3799 O O   . GLY B  2 235 ? -2.674  -22.043 7.762   1.00 25.41 ? 232 GLY A O   1 
ATOM   3800 N N   . GLY B  2 236 ? -4.604  -22.037 6.562   1.00 29.36 ? 233 GLY A N   1 
ATOM   3801 C CA  . GLY B  2 236 ? -4.349  -20.867 5.723   1.00 29.71 ? 233 GLY A CA  1 
ATOM   3802 C C   . GLY B  2 236 ? -4.816  -19.560 6.377   1.00 30.05 ? 233 GLY A C   1 
ATOM   3803 O O   . GLY B  2 236 ? -4.335  -18.501 5.994   1.00 30.85 ? 233 GLY A O   1 
ATOM   3804 N N   . SER B  2 237 ? -5.682  -19.615 7.401   1.00 27.82 ? 234 SER A N   1 
ATOM   3805 C CA  . SER B  2 237 ? -6.392  -18.433 7.883   1.00 26.70 ? 234 SER A CA  1 
ATOM   3806 C C   . SER B  2 237 ? -5.480  -17.575 8.767   1.00 23.52 ? 234 SER A C   1 
ATOM   3807 O O   . SER B  2 237 ? -4.414  -18.030 9.248   1.00 20.66 ? 234 SER A O   1 
ATOM   3808 C CB  . SER B  2 237 ? -7.682  -18.809 8.566   1.00 28.50 ? 234 SER A CB  1 
ATOM   3809 O OG  . SER B  2 237 ? -7.407  -19.376 9.826   1.00 33.86 ? 234 SER A OG  1 
ATOM   3810 N N   . ARG B  2 238 ? -5.930  -16.348 8.970   1.00 21.76 ? 235 ARG A N   1 
ATOM   3811 C CA  . ARG B  2 238 ? -5.182  -15.363 9.725   1.00 20.54 ? 235 ARG A CA  1 
ATOM   3812 C C   . ARG B  2 238 ? -5.417  -15.595 11.212  1.00 19.59 ? 235 ARG A C   1 
ATOM   3813 O O   . ARG B  2 238 ? -6.546  -15.620 11.650  1.00 17.62 ? 235 ARG A O   1 
ATOM   3814 C CB  . ARG B  2 238 ? -5.490  -13.932 9.293   1.00 21.32 ? 235 ARG A CB  1 
ATOM   3815 C CG  . ARG B  2 238 ? -4.643  -12.865 9.984   1.00 19.12 ? 235 ARG A CG  1 
ATOM   3816 C CD  . ARG B  2 238 ? -4.933  -11.428 9.468   1.00 19.22 ? 235 ARG A CD  1 
ATOM   3817 N NE  . ARG B  2 238 ? -4.383  -10.405 10.364  1.00 17.21 ? 235 ARG A NE  1 
ATOM   3818 C CZ  . ARG B  2 238 ? -3.106  -10.075 10.487  1.00 16.25 ? 235 ARG A CZ  1 
ATOM   3819 N NH1 . ARG B  2 238 ? -2.207  -10.672 9.766   1.00 17.02 ? 235 ARG A NH1 1 
ATOM   3820 N NH2 . ARG B  2 238 ? -2.741  -9.198  11.391  1.00 18.21 ? 235 ARG A NH2 1 
ATOM   3821 N N   . ARG B  2 239 ? -4.334  -15.636 11.992  1.00 18.12 ? 236 ARG A N   1 
ATOM   3822 C CA  . ARG B  2 239 ? -4.436  -15.717 13.449  1.00 17.34 ? 236 ARG A CA  1 
ATOM   3823 C C   . ARG B  2 239 ? -5.281  -14.603 14.064  1.00 16.57 ? 236 ARG A C   1 
ATOM   3824 O O   . ARG B  2 239 ? -5.356  -13.507 13.513  1.00 16.30 ? 236 ARG A O   1 
ATOM   3825 C CB  . ARG B  2 239 ? -3.060  -15.778 14.102  1.00 16.97 ? 236 ARG A CB  1 
ATOM   3826 C CG  . ARG B  2 239 ? -2.232  -14.537 14.305  1.00 16.13 ? 236 ARG A CG  1 
ATOM   3827 C CD  . ARG B  2 239 ? -2.115  -13.608 13.105  1.00 16.87 ? 236 ARG A CD  1 
ATOM   3828 N NE  . ARG B  2 239 ? -1.579  -12.280 13.339  1.00 16.63 ? 236 ARG A NE  1 
ATOM   3829 C CZ  . ARG B  2 239 ? -2.225  -11.246 13.934  1.00 16.20 ? 236 ARG A CZ  1 
ATOM   3830 N NH1 . ARG B  2 239 ? -1.532  -10.209 14.296  1.00 15.53 ? 236 ARG A NH1 1 
ATOM   3831 N NH2 . ARG B  2 239 ? -3.556  -11.230 14.118  1.00 15.47 ? 236 ARG A NH2 1 
ATOM   3832 N N   . GLY B  2 240 ? -5.873  -14.887 15.242  1.00 15.77 ? 237 GLY A N   1 
ATOM   3833 C CA  . GLY B  2 240 ? -6.688  -13.935 15.985  1.00 14.73 ? 237 GLY A CA  1 
ATOM   3834 C C   . GLY B  2 240 ? -5.876  -13.139 17.004  1.00 14.81 ? 237 GLY A C   1 
ATOM   3835 O O   . GLY B  2 240 ? -4.985  -13.727 17.662  1.00 15.08 ? 237 GLY A O   1 
HETATM 3836 N N   . TPO B  2 241 ? -6.125  -11.828 17.097  1.00 14.33 ? 238 TPO A N   1 
HETATM 3837 C CA  . TPO B  2 241 ? -5.724  -11.056 18.265  1.00 13.82 ? 238 TPO A CA  1 
HETATM 3838 C CB  . TPO B  2 241 ? -4.620  -10.031 17.958  1.00 14.00 ? 238 TPO A CB  1 
HETATM 3839 C CG2 . TPO B  2 241 ? -3.284  -10.657 17.685  1.00 14.87 ? 238 TPO A CG2 1 
HETATM 3840 O OG1 . TPO B  2 241 ? -5.019  -9.172  16.872  1.00 13.36 ? 238 TPO A OG1 1 
HETATM 3841 P P   . TPO B  2 241 ? -4.285  -7.833  16.452  1.00 15.27 ? 238 TPO A P   1 
HETATM 3842 O O1P . TPO B  2 241 ? -5.274  -7.207  15.511  1.00 13.12 ? 238 TPO A O1P 1 
HETATM 3843 O O2P . TPO B  2 241 ? -4.023  -7.093  17.736  1.00 14.85 ? 238 TPO A O2P 1 
HETATM 3844 O O3P . TPO B  2 241 ? -3.026  -8.220  15.751  1.00 13.61 ? 238 TPO A O3P 1 
HETATM 3845 C C   . TPO B  2 241 ? -6.972  -10.504 18.966  1.00 15.00 ? 238 TPO A C   1 
HETATM 3846 O O   . TPO B  2 241 ? -8.116  -10.654 18.521  1.00 14.58 ? 238 TPO A O   1 
ATOM   3847 N N   . SER B  2 242 ? -6.753  -9.851  20.105  1.00 13.79 ? 239 SER A N   1 
ATOM   3848 C CA  . SER B  2 242 ? -7.805  -9.579  21.025  1.00 15.65 ? 239 SER A CA  1 
ATOM   3849 C C   . SER B  2 242 ? -8.804  -8.576  20.427  1.00 15.24 ? 239 SER A C   1 
ATOM   3850 O O   . SER B  2 242 ? -8.358  -7.599  19.765  1.00 13.51 ? 239 SER A O   1 
ATOM   3851 C CB  . SER B  2 242 ? -7.206  -9.038  22.339  1.00 17.48 ? 239 SER A CB  1 
ATOM   3852 O OG  . SER B  2 242 ? -8.241  -8.874  23.265  1.00 20.32 ? 239 SER A OG  1 
ATOM   3853 N N   . PRO B  2 243 ? -10.119 -8.729  20.737  1.00 17.42 ? 240 PRO A N   1 
ATOM   3854 C CA  . PRO B  2 243 ? -11.059 -7.633  20.493  1.00 18.59 ? 240 PRO A CA  1 
ATOM   3855 C C   . PRO B  2 243 ? -10.614 -6.386  21.262  1.00 18.06 ? 240 PRO A C   1 
ATOM   3856 O O   . PRO B  2 243 ? -9.927  -6.489  22.307  1.00 16.72 ? 240 PRO A O   1 
ATOM   3857 C CB  . PRO B  2 243 ? -12.401 -8.140  20.942  1.00 19.68 ? 240 PRO A CB  1 
ATOM   3858 C CG  . PRO B  2 243 ? -12.029 -9.135  21.985  1.00 19.71 ? 240 PRO A CG  1 
ATOM   3859 C CD  . PRO B  2 243 ? -10.793 -9.823  21.473  1.00 18.24 ? 240 PRO A CD  1 
ATOM   3860 N N   . ALA B  2 244 ? -10.951 -5.232  20.687  1.00 17.77 ? 241 ALA A N   1 
ATOM   3861 C CA  . ALA B  2 244 ? -10.700 -3.941  21.332  1.00 18.54 ? 241 ALA A CA  1 
ATOM   3862 C C   . ALA B  2 244 ? -11.516 -3.791  22.616  1.00 18.02 ? 241 ALA A C   1 
ATOM   3863 O O   . ALA B  2 244 ? -11.039 -3.214  23.603  1.00 17.44 ? 241 ALA A O   1 
ATOM   3864 C CB  . ALA B  2 244 ? -11.018 -2.842  20.348  1.00 18.35 ? 241 ALA A CB  1 
ATOM   3865 N N   . ARG B  2 245 ? -12.767 -4.287  22.582  1.00 20.30 ? 242 ARG A N   1 
ATOM   3866 C CA  . ARG B  2 245 ? -13.661 -4.280  23.731  1.00 21.71 ? 242 ARG A CA  1 
ATOM   3867 C C   . ARG B  2 245 ? -13.616 -5.681  24.333  1.00 21.36 ? 242 ARG A C   1 
ATOM   3868 O O   . ARG B  2 245 ? -14.199 -6.606  23.767  1.00 23.68 ? 242 ARG A O   1 
ATOM   3869 C CB  . ARG B  2 245 ? -15.016 -3.800  23.188  1.00 23.53 ? 242 ARG A CB  1 
ATOM   3870 C CG  . ARG B  2 245 ? -16.113 -3.812  24.207  1.00 24.14 ? 242 ARG A CG  1 
ATOM   3871 C CD  . ARG B  2 245 ? -17.406 -3.119  23.771  1.00 26.50 ? 242 ARG A CD  1 
ATOM   3872 N NE  . ARG B  2 245 ? -17.327 -1.642  23.706  1.00 26.51 ? 242 ARG A NE  1 
ATOM   3873 C CZ  . ARG B  2 245 ? -17.531 -0.859  22.644  1.00 24.84 ? 242 ARG A CZ  1 
ATOM   3874 N NH1 . ARG B  2 245 ? -17.505 -1.373  21.444  1.00 22.74 ? 242 ARG A NH1 1 
ATOM   3875 N NH2 . ARG B  2 245 ? -17.770 0.448   22.762  1.00 24.70 ? 242 ARG A NH2 1 
ATOM   3876 N N   . MET B  2 246 ? -12.866 -5.852  25.422  1.00 20.54 ? 243 MET A N   1 
ATOM   3877 C CA  . MET B  2 246 ? -12.634 -7.163  26.019  1.00 20.94 ? 243 MET A CA  1 
ATOM   3878 C C   . MET B  2 246 ? -13.740 -7.534  27.023  1.00 24.10 ? 243 MET A C   1 
ATOM   3879 O O   . MET B  2 246 ? -14.167 -8.695  27.045  1.00 21.40 ? 243 MET A O   1 
ATOM   3880 C CB  . MET B  2 246 ? -11.248 -7.227  26.655  1.00 20.21 ? 243 MET A CB  1 
ATOM   3881 C CG  . MET B  2 246 ? -10.192 -7.331  25.590  1.00 21.20 ? 243 MET A CG  1 
ATOM   3882 S SD  . MET B  2 246 ? -8.528  -7.057  26.222  1.00 24.06 ? 243 MET A SD  1 
ATOM   3883 C CE  . MET B  2 246 ? -8.467  -5.273  26.139  1.00 23.03 ? 243 MET A CE  1 
ATOM   3884 N N   . ALA B  2 247 ? -14.159 -6.590  27.880  1.00 24.99 ? 244 ALA A N   1 
ATOM   3885 C CA  . ALA B  2 247 ? -15.099 -6.835  28.977  1.00 30.45 ? 244 ALA A CA  1 
ATOM   3886 C C   . ALA B  2 247 ? -16.147 -5.728  28.985  1.00 37.11 ? 244 ALA A C   1 
ATOM   3887 O O   . ALA B  2 247 ? -15.760 -4.551  28.993  1.00 40.35 ? 244 ALA A O   1 
ATOM   3888 C CB  . ALA B  2 247 ? -14.366 -6.949  30.311  1.00 30.02 ? 244 ALA A CB  1 
ATOM   3889 N N   . GLY B  2 248 ? -17.437 -6.107  28.928  1.00 44.19 ? 245 GLY A N   1 
ATOM   3890 C CA  . GLY B  2 248 ? -18.530 -5.186  29.249  1.00 49.80 ? 245 GLY A CA  1 
ATOM   3891 C C   . GLY B  2 248 ? -18.821 -4.163  28.139  1.00 50.07 ? 245 GLY A C   1 
ATOM   3892 O O   . GLY B  2 248 ? -18.421 -4.393  26.993  1.00 53.42 ? 245 GLY A O   1 
ATOM   3893 N N   . ASN B  2 249 ? -19.500 -3.044  28.512  1.00 52.13 ? 246 ASN A N   1 
ATOM   3894 C CA  . ASN B  2 249 ? -19.995 -2.008  27.594  1.00 51.78 ? 246 ASN A CA  1 
ATOM   3895 C C   . ASN B  2 249 ? -18.836 -1.183  26.991  1.00 49.48 ? 246 ASN A C   1 
ATOM   3896 O O   . ASN B  2 249 ? -18.972 -0.782  25.817  1.00 44.22 ? 246 ASN A O   1 
ATOM   3897 C CB  . ASN B  2 249 ? -21.002 -1.057  28.246  1.00 52.48 ? 246 ASN A CB  1 
ATOM   3898 O OXT . ASN B  2 249 ? -17.864 -0.920  27.714  1.00 38.92 ? 246 ASN A OXT 1 
HETATM 3899 C C1  . EDO C  3 .   ? -38.966 -10.730 -12.007 1.00 42.92 ? 301 EDO B C1  1 
HETATM 3900 O O1  . EDO C  3 .   ? -39.108 -11.784 -11.080 1.00 43.45 ? 301 EDO B O1  1 
HETATM 3901 C C2  . EDO C  3 .   ? -40.152 -10.624 -12.913 1.00 43.10 ? 301 EDO B C2  1 
HETATM 3902 O O2  . EDO C  3 .   ? -41.331 -10.346 -12.187 1.00 42.08 ? 301 EDO B O2  1 
HETATM 3903 C C1  . EDO D  3 .   ? -14.694 20.077  -11.041 1.00 43.92 ? 302 EDO B C1  1 
HETATM 3904 O O1  . EDO D  3 .   ? -13.309 20.271  -11.268 1.00 48.07 ? 302 EDO B O1  1 
HETATM 3905 C C2  . EDO D  3 .   ? -14.938 19.826  -9.559  1.00 44.58 ? 302 EDO B C2  1 
HETATM 3906 O O2  . EDO D  3 .   ? -15.068 18.457  -9.180  1.00 40.73 ? 302 EDO B O2  1 
HETATM 3907 C C1  . EDO E  3 .   ? -22.829 11.064  -27.071 1.00 51.48 ? 303 EDO B C1  1 
HETATM 3908 O O1  . EDO E  3 .   ? -22.514 10.214  -28.161 1.00 56.36 ? 303 EDO B O1  1 
HETATM 3909 C C2  . EDO E  3 .   ? -22.657 12.494  -27.417 1.00 49.97 ? 303 EDO B C2  1 
HETATM 3910 O O2  . EDO E  3 .   ? -23.732 13.023  -28.130 1.00 49.49 ? 303 EDO B O2  1 
HETATM 3911 C C1  . EDO F  3 .   ? -24.820 3.137   0.613   1.00 33.56 ? 304 EDO B C1  1 
HETATM 3912 O O1  . EDO F  3 .   ? -26.163 3.428   0.999   1.00 24.84 ? 304 EDO B O1  1 
HETATM 3913 C C2  . EDO F  3 .   ? -23.934 2.704   1.716   1.00 32.13 ? 304 EDO B C2  1 
HETATM 3914 O O2  . EDO F  3 .   ? -24.361 1.481   2.386   1.00 38.07 ? 304 EDO B O2  1 
HETATM 3915 C C1  . EDO G  3 .   ? -25.050 -7.316  -23.962 1.00 24.40 ? 305 EDO B C1  1 
HETATM 3916 O O1  . EDO G  3 .   ? -24.073 -8.161  -24.677 1.00 23.74 ? 305 EDO B O1  1 
HETATM 3917 C C2  . EDO G  3 .   ? -25.815 -6.303  -24.749 1.00 27.12 ? 305 EDO B C2  1 
HETATM 3918 O O2  . EDO G  3 .   ? -25.091 -5.560  -25.768 1.00 26.09 ? 305 EDO B O2  1 
HETATM 3919 C C1  . EDO H  3 .   ? -34.754 7.380   0.511   1.00 40.27 ? 306 EDO B C1  1 
HETATM 3920 O O1  . EDO H  3 .   ? -34.780 8.770   0.719   1.00 36.21 ? 306 EDO B O1  1 
HETATM 3921 C C2  . EDO H  3 .   ? -35.033 6.567   1.724   1.00 42.88 ? 306 EDO B C2  1 
HETATM 3922 O O2  . EDO H  3 .   ? -36.419 6.366   1.898   1.00 49.89 ? 306 EDO B O2  1 
HETATM 3923 C C1  . PEG I  4 .   ? -19.098 -2.804  -6.930  1.00 23.79 ? 307 PEG B C1  1 
HETATM 3924 O O1  . PEG I  4 .   ? -19.078 -2.777  -8.297  1.00 24.44 ? 307 PEG B O1  1 
HETATM 3925 C C2  . PEG I  4 .   ? -20.017 -1.794  -6.413  1.00 26.64 ? 307 PEG B C2  1 
HETATM 3926 O O2  . PEG I  4 .   ? -20.455 -2.023  -5.066  1.00 37.91 ? 307 PEG B O2  1 
HETATM 3927 C C3  . PEG I  4 .   ? -20.824 -0.855  -4.310  1.00 40.58 ? 307 PEG B C3  1 
HETATM 3928 C C4  . PEG I  4 .   ? -19.856 -0.535  -3.219  1.00 52.53 ? 307 PEG B C4  1 
HETATM 3929 O O4  . PEG I  4 .   ? -20.214 0.623   -2.461  1.00 51.02 ? 307 PEG B O4  1 
HETATM 3930 C C1  . EDO J  3 .   ? -9.835  5.036   -24.383 1.00 53.48 ? 308 EDO B C1  1 
HETATM 3931 O O1  . EDO J  3 .   ? -10.410 3.707   -24.327 1.00 51.60 ? 308 EDO B O1  1 
HETATM 3932 C C2  . EDO J  3 .   ? -10.803 6.197   -24.290 1.00 53.38 ? 308 EDO B C2  1 
HETATM 3933 O O2  . EDO J  3 .   ? -12.184 5.897   -24.560 1.00 53.32 ? 308 EDO B O2  1 
HETATM 3934 C C1  . EDO K  3 .   ? 2.413   7.426   -3.118  1.00 45.04 ? 301 EDO A C1  1 
HETATM 3935 O O1  . EDO K  3 .   ? 1.699   8.585   -2.737  1.00 52.53 ? 301 EDO A O1  1 
HETATM 3936 C C2  . EDO K  3 .   ? 2.662   7.236   -4.588  1.00 49.25 ? 301 EDO A C2  1 
HETATM 3937 O O2  . EDO K  3 .   ? 2.646   5.859   -5.035  1.00 43.22 ? 301 EDO A O2  1 
HETATM 3938 C C1  . EDO L  3 .   ? 7.088   -15.221 29.467  1.00 44.54 ? 302 EDO A C1  1 
HETATM 3939 O O1  . EDO L  3 .   ? 7.298   -14.015 28.753  1.00 38.07 ? 302 EDO A O1  1 
HETATM 3940 C C2  . EDO L  3 .   ? 5.969   -16.047 28.988  1.00 43.10 ? 302 EDO A C2  1 
HETATM 3941 O O2  . EDO L  3 .   ? 6.361   -17.276 28.387  1.00 51.68 ? 302 EDO A O2  1 
HETATM 3942 C C1  . EDO M  3 .   ? -13.916 -23.068 24.501  1.00 49.78 ? 303 EDO A C1  1 
HETATM 3943 O O1  . EDO M  3 .   ? -13.538 -22.144 23.505  1.00 46.97 ? 303 EDO A O1  1 
HETATM 3944 C C2  . EDO M  3 .   ? -14.156 -22.398 25.799  1.00 45.12 ? 303 EDO A C2  1 
HETATM 3945 O O2  . EDO M  3 .   ? -14.959 -23.173 26.653  1.00 48.91 ? 303 EDO A O2  1 
HETATM 3946 C C1  . EDO N  3 .   ? 9.013   -6.511  8.127   1.00 54.53 ? 304 EDO A C1  1 
HETATM 3947 O O1  . EDO N  3 .   ? 9.914   -5.469  8.375   1.00 60.77 ? 304 EDO A O1  1 
HETATM 3948 C C2  . EDO N  3 .   ? 8.130   -6.119  7.024   1.00 53.25 ? 304 EDO A C2  1 
HETATM 3949 O O2  . EDO N  3 .   ? 8.750   -6.039  5.763   1.00 49.97 ? 304 EDO A O2  1 
HETATM 3950 C C1  . EDO O  3 .   ? -3.237  9.192   9.504   1.00 53.05 ? 305 EDO A C1  1 
HETATM 3951 O O1  . EDO O  3 .   ? -2.260  9.434   10.490  1.00 48.06 ? 305 EDO A O1  1 
HETATM 3952 C C2  . EDO O  3 .   ? -4.084  10.378  9.246   1.00 54.10 ? 305 EDO A C2  1 
HETATM 3953 O O2  . EDO O  3 .   ? -5.122  10.452  10.198  1.00 57.87 ? 305 EDO A O2  1 
HETATM 3954 C C1  . PEG P  4 .   ? 6.110   -6.344  38.250  0.80 48.48 ? 306 PEG A C1  1 
HETATM 3955 O O1  . PEG P  4 .   ? 6.428   -6.445  36.870  0.80 48.68 ? 306 PEG A O1  1 
HETATM 3956 C C2  . PEG P  4 .   ? 4.736   -6.853  38.515  0.80 47.25 ? 306 PEG A C2  1 
HETATM 3957 O O2  . PEG P  4 .   ? 4.651   -7.532  39.772  0.80 46.05 ? 306 PEG A O2  1 
HETATM 3958 C C3  . PEG P  4 .   ? 4.588   -8.947  39.730  0.80 44.00 ? 306 PEG A C3  1 
HETATM 3959 C C4  . PEG P  4 .   ? 5.977   -9.499  39.604  0.80 45.54 ? 306 PEG A C4  1 
HETATM 3960 O O4  . PEG P  4 .   ? 5.991   -10.902 39.533  0.80 45.79 ? 306 PEG A O4  1 
HETATM 3961 C C1  . EDO Q  3 .   ? -7.207  -25.933 23.721  1.00 37.94 ? 307 EDO A C1  1 
HETATM 3962 O O1  . EDO Q  3 .   ? -5.895  -26.405 23.823  1.00 35.75 ? 307 EDO A O1  1 
HETATM 3963 C C2  . EDO Q  3 .   ? -8.222  -26.915 24.248  1.00 40.05 ? 307 EDO A C2  1 
HETATM 3964 O O2  . EDO Q  3 .   ? -8.837  -27.791 23.307  1.00 41.43 ? 307 EDO A O2  1 
HETATM 3965 C C1  . PEG R  4 .   ? -8.833  -9.093  10.425  0.80 38.69 ? 308 PEG A C1  1 
HETATM 3966 O O1  . PEG R  4 .   ? -9.831  -8.752  11.333  0.80 38.43 ? 308 PEG A O1  1 
HETATM 3967 C C2  . PEG R  4 .   ? -7.479  -9.039  11.040  0.80 37.35 ? 308 PEG A C2  1 
HETATM 3968 O O2  . PEG R  4 .   ? -7.357  -9.916  12.153  0.80 33.78 ? 308 PEG A O2  1 
HETATM 3969 C C3  . PEG R  4 .   ? -7.222  -11.317 11.862  0.80 40.59 ? 308 PEG A C3  1 
HETATM 3970 C C4  . PEG R  4 .   ? -8.111  -12.222 12.676  0.80 35.78 ? 308 PEG A C4  1 
HETATM 3971 O O4  . PEG R  4 .   ? -8.395  -13.473 12.081  0.80 40.67 ? 308 PEG A O4  1 
HETATM 3972 C C1  . PEG S  4 .   ? 8.857   4.959   17.719  1.00 49.78 ? 309 PEG A C1  1 
HETATM 3973 O O1  . PEG S  4 .   ? 7.784   5.549   18.415  1.00 47.64 ? 309 PEG A O1  1 
HETATM 3974 C C2  . PEG S  4 .   ? 9.647   4.040   18.602  1.00 48.65 ? 309 PEG A C2  1 
HETATM 3975 O O2  . PEG S  4 .   ? 10.885  3.623   17.995  1.00 53.35 ? 309 PEG A O2  1 
HETATM 3976 C C3  . PEG S  4 .   ? 12.047  3.465   18.832  1.00 58.97 ? 309 PEG A C3  1 
HETATM 3977 C C4  . PEG S  4 .   ? 11.788  2.751   20.173  1.00 55.72 ? 309 PEG A C4  1 
HETATM 3978 O O4  . PEG S  4 .   ? 12.976  2.311   20.787  1.00 49.35 ? 309 PEG A O4  1 
HETATM 3979 C C1  . EDO T  3 .   ? -0.673  -14.049 9.423   0.80 28.82 ? 310 EDO A C1  1 
HETATM 3980 O O1  . EDO T  3 .   ? 0.233   -13.234 10.269  0.80 30.13 ? 310 EDO A O1  1 
HETATM 3981 C C2  . EDO T  3 .   ? -0.888  -15.486 9.746   0.80 28.93 ? 310 EDO A C2  1 
HETATM 3982 O O2  . EDO T  3 .   ? -1.932  -15.972 10.638  0.80 20.67 ? 310 EDO A O2  1 
HETATM 3983 C C1  . EDO U  3 .   ? -5.784  -5.389  11.089  1.00 25.58 ? 311 EDO A C1  1 
HETATM 3984 O O1  . EDO U  3 .   ? -4.764  -6.341  10.857  1.00 18.15 ? 311 EDO A O1  1 
HETATM 3985 C C2  . EDO U  3 .   ? -6.962  -5.306  10.188  1.00 26.22 ? 311 EDO A C2  1 
HETATM 3986 O O2  . EDO U  3 .   ? -7.242  -6.457  9.269   1.00 31.08 ? 311 EDO A O2  1 
HETATM 3987 C C1  . PEG V  4 .   ? -12.220 -4.331  29.195  0.80 32.41 ? 312 PEG A C1  1 
HETATM 3988 O O1  . PEG V  4 .   ? -12.511 -4.383  27.802  0.80 32.12 ? 312 PEG A O1  1 
HETATM 3989 C C2  . PEG V  4 .   ? -13.173 -3.434  29.971  0.80 35.58 ? 312 PEG A C2  1 
HETATM 3990 O O2  . PEG V  4 .   ? -12.560 -2.596  30.933  0.80 35.38 ? 312 PEG A O2  1 
HETATM 3991 C C3  . PEG V  4 .   ? -11.686 -1.626  30.367  0.80 34.33 ? 312 PEG A C3  1 
HETATM 3992 C C4  . PEG V  4 .   ? -10.374 -1.953  30.877  0.80 36.06 ? 312 PEG A C4  1 
HETATM 3993 O O4  . PEG V  4 .   ? -10.257 -1.753  32.230  0.80 34.49 ? 312 PEG A O4  1 
HETATM 3994 C C1  . PEG W  4 .   ? -8.239  -23.330 6.021   1.00 47.26 ? 313 PEG A C1  1 
HETATM 3995 O O1  . PEG W  4 .   ? -8.899  -22.309 6.731   1.00 46.13 ? 313 PEG A O1  1 
HETATM 3996 C C2  . PEG W  4 .   ? -7.556  -22.824 4.799   1.00 47.88 ? 313 PEG A C2  1 
HETATM 3997 O O2  . PEG W  4 .   ? -6.974  -23.884 4.049   1.00 54.64 ? 313 PEG A O2  1 
HETATM 3998 C C3  . PEG W  4 .   ? -5.931  -24.632 4.681   1.00 52.91 ? 313 PEG A C3  1 
HETATM 3999 C C4  . PEG W  4 .   ? -4.695  -24.718 3.846   1.00 53.76 ? 313 PEG A C4  1 
HETATM 4000 O O4  . PEG W  4 .   ? -3.653  -25.386 4.547   1.00 53.30 ? 313 PEG A O4  1 
HETATM 4001 C C1  . EDO X  3 .   ? -13.154 7.595   8.926   1.00 45.51 ? 314 EDO A C1  1 
HETATM 4002 O O1  . EDO X  3 .   ? -13.175 8.015   10.258  1.00 42.33 ? 314 EDO A O1  1 
HETATM 4003 C C2  . EDO X  3 .   ? -13.096 6.137   8.920   1.00 42.06 ? 314 EDO A C2  1 
HETATM 4004 O O2  . EDO X  3 .   ? -13.939 5.531   9.888   1.00 37.80 ? 314 EDO A O2  1 
HETATM 4005 C C1  A PEG Y  4 .   ? -12.274 -5.015  15.852  0.66 30.28 ? 315 PEG A C1  1 
HETATM 4006 O O1  A PEG Y  4 .   ? -11.165 -4.570  15.079  0.66 30.57 ? 315 PEG A O1  1 
HETATM 4007 C C2  A PEG Y  4 .   ? -11.817 -5.816  17.045  0.66 27.72 ? 315 PEG A C2  1 
HETATM 4008 O O2  A PEG Y  4 .   ? -12.446 -5.282  18.201  0.66 22.26 ? 315 PEG A O2  1 
HETATM 4009 C C3  A PEG Y  4 .   ? -13.734 -5.859  18.352  0.66 22.19 ? 315 PEG A C3  1 
HETATM 4010 C C4  A PEG Y  4 .   ? -14.472 -4.999  19.060  0.66 19.70 ? 315 PEG A C4  1 
HETATM 4011 O O4  A PEG Y  4 .   ? -14.397 -5.360  20.363  0.66 19.10 ? 315 PEG A O4  1 
HETATM 4012 O O   . HOH Z  5 .   ? -24.939 -7.659  -28.050 1.00 32.82 ? 401 HOH B O   1 
HETATM 4013 O O   . HOH Z  5 .   ? -33.116 -6.466  -28.540 1.00 45.01 ? 402 HOH B O   1 
HETATM 4014 O O   . HOH Z  5 .   ? -22.729 -2.925  -5.414  1.00 36.26 ? 403 HOH B O   1 
HETATM 4015 O O   . HOH Z  5 .   ? -27.661 -12.440 -7.460  1.00 42.07 ? 404 HOH B O   1 
HETATM 4016 O O   . HOH Z  5 .   ? -41.355 -3.846  -23.301 1.00 43.07 ? 405 HOH B O   1 
HETATM 4017 O O   . HOH Z  5 .   ? -13.651 14.625  -4.698  1.00 29.36 ? 406 HOH B O   1 
HETATM 4018 O O   . HOH Z  5 .   ? -22.971 20.219  12.807  1.00 37.88 ? 407 HOH B O   1 
HETATM 4019 O O   . HOH Z  5 .   ? -7.948  -2.261  -8.805  1.00 34.63 ? 408 HOH B O   1 
HETATM 4020 O O   . HOH Z  5 .   ? -31.336 3.802   15.618  1.00 35.31 ? 409 HOH B O   1 
HETATM 4021 O O   . HOH Z  5 .   ? -32.163 6.556   -3.181  1.00 17.07 ? 410 HOH B O   1 
HETATM 4022 O O   . HOH Z  5 .   ? -35.703 -0.072  -26.558 1.00 43.86 ? 411 HOH B O   1 
HETATM 4023 O O   . HOH Z  5 .   ? -32.780 -13.049 -7.940  1.00 25.67 ? 412 HOH B O   1 
HETATM 4024 O O   . HOH Z  5 .   ? -8.459  8.530   -20.865 1.00 40.43 ? 413 HOH B O   1 
HETATM 4025 O O   . HOH Z  5 .   ? -13.177 -2.287  -18.763 1.00 38.29 ? 414 HOH B O   1 
HETATM 4026 O O   . HOH Z  5 .   ? -10.422 12.109  -2.319  1.00 29.60 ? 415 HOH B O   1 
HETATM 4027 O O   . HOH Z  5 .   ? -19.484 -0.219  -16.119 1.00 23.83 ? 416 HOH B O   1 
HETATM 4028 O O   . HOH Z  5 .   ? -26.130 12.259  -27.259 1.00 34.71 ? 417 HOH B O   1 
HETATM 4029 O O   . HOH Z  5 .   ? -12.903 9.829   4.202   1.00 47.01 ? 418 HOH B O   1 
HETATM 4030 O O   . HOH Z  5 .   ? -25.481 0.129   -3.608  1.00 21.18 ? 419 HOH B O   1 
HETATM 4031 O O   . HOH Z  5 .   ? -24.834 -13.238 -10.199 1.00 28.67 ? 420 HOH B O   1 
HETATM 4032 O O   . HOH Z  5 .   ? -26.722 -18.202 -14.397 1.00 23.17 ? 421 HOH B O   1 
HETATM 4033 O O   . HOH Z  5 .   ? -9.237  -4.685  -6.917  1.00 52.23 ? 422 HOH B O   1 
HETATM 4034 O O   . HOH Z  5 .   ? -12.001 1.317   2.993   1.00 27.79 ? 423 HOH B O   1 
HETATM 4035 O O   . HOH Z  5 .   ? -16.338 8.780   -23.536 1.00 28.00 ? 424 HOH B O   1 
HETATM 4036 O O   . HOH Z  5 .   ? -16.151 12.624  -21.552 1.00 30.74 ? 425 HOH B O   1 
HETATM 4037 O O   . HOH Z  5 .   ? -39.531 -0.026  -23.067 1.00 40.16 ? 426 HOH B O   1 
HETATM 4038 O O   . HOH Z  5 .   ? -29.495 1.762   6.615   1.00 41.15 ? 427 HOH B O   1 
HETATM 4039 O O   . HOH Z  5 .   ? -8.086  -5.098  2.393   1.00 46.12 ? 428 HOH B O   1 
HETATM 4040 O O   . HOH Z  5 .   ? -16.528 1.114   1.313   1.00 36.63 ? 429 HOH B O   1 
HETATM 4041 O O   . HOH Z  5 .   ? -28.175 19.932  -15.029 1.00 37.00 ? 430 HOH B O   1 
HETATM 4042 O O   . HOH Z  5 .   ? -12.296 14.248  -18.831 1.00 37.00 ? 431 HOH B O   1 
HETATM 4043 O O   . HOH Z  5 .   ? -49.248 -1.290  -4.747  1.00 40.07 ? 432 HOH B O   1 
HETATM 4044 O O   . HOH Z  5 .   ? -31.884 15.801  6.423   1.00 33.98 ? 433 HOH B O   1 
HETATM 4045 O O   B HOH Z  5 .   ? -22.905 0.888   4.539   0.50 24.43 ? 434 HOH B O   1 
HETATM 4046 O O   . HOH Z  5 .   ? -37.140 2.227   -0.085  1.00 26.24 ? 435 HOH B O   1 
HETATM 4047 O O   . HOH Z  5 .   ? -30.587 17.049  -14.642 1.00 23.51 ? 436 HOH B O   1 
HETATM 4048 O O   . HOH Z  5 .   ? -24.724 22.377  12.089  1.00 44.98 ? 437 HOH B O   1 
HETATM 4049 O O   . HOH Z  5 .   ? -15.644 7.556   -29.820 1.00 38.58 ? 438 HOH B O   1 
HETATM 4050 O O   . HOH Z  5 .   ? -11.621 -0.456  -13.579 1.00 20.19 ? 439 HOH B O   1 
HETATM 4051 O O   . HOH Z  5 .   ? -38.520 11.606  -1.085  1.00 42.22 ? 440 HOH B O   1 
HETATM 4052 O O   . HOH Z  5 .   ? -18.862 18.455  7.582   1.00 39.21 ? 441 HOH B O   1 
HETATM 4053 O O   . HOH Z  5 .   ? -35.078 -12.752 -29.321 1.00 29.05 ? 442 HOH B O   1 
HETATM 4054 O O   . HOH Z  5 .   ? -27.477 10.435  0.623   1.00 17.99 ? 443 HOH B O   1 
HETATM 4055 O O   . HOH Z  5 .   ? -16.704 17.215  8.486   1.00 34.66 ? 444 HOH B O   1 
HETATM 4056 O O   . HOH Z  5 .   ? -19.997 2.813   -31.235 1.00 29.32 ? 445 HOH B O   1 
HETATM 4057 O O   . HOH Z  5 .   ? -44.018 -1.926  -2.487  1.00 25.12 ? 446 HOH B O   1 
HETATM 4058 O O   . HOH Z  5 .   ? -19.583 -10.672 -17.533 1.00 20.08 ? 447 HOH B O   1 
HETATM 4059 O O   . HOH Z  5 .   ? -18.027 3.039   1.619   1.00 43.80 ? 448 HOH B O   1 
HETATM 4060 O O   . HOH Z  5 .   ? -43.098 -0.238  -17.658 1.00 32.54 ? 449 HOH B O   1 
HETATM 4061 O O   . HOH Z  5 .   ? -13.497 -2.164  -5.087  1.00 23.89 ? 450 HOH B O   1 
HETATM 4062 O O   . HOH Z  5 .   ? -22.731 -5.947  -13.388 1.00 19.74 ? 451 HOH B O   1 
HETATM 4063 O O   . HOH Z  5 .   ? -25.546 -15.262 -13.079 1.00 25.69 ? 452 HOH B O   1 
HETATM 4064 O O   . HOH Z  5 .   ? -23.310 -12.759 -12.169 1.00 23.79 ? 453 HOH B O   1 
HETATM 4065 O O   . HOH Z  5 .   ? -34.525 -2.298  -26.918 1.00 34.80 ? 454 HOH B O   1 
HETATM 4066 O O   . HOH Z  5 .   ? -4.787  17.172  -10.368 1.00 44.11 ? 455 HOH B O   1 
HETATM 4067 O O   . HOH Z  5 .   ? -27.361 1.925   -1.103  1.00 18.67 ? 456 HOH B O   1 
HETATM 4068 O O   . HOH Z  5 .   ? -8.168  17.697  -8.237  1.00 36.15 ? 457 HOH B O   1 
HETATM 4069 O O   . HOH Z  5 .   ? -41.254 -7.807  1.329   1.00 25.63 ? 458 HOH B O   1 
HETATM 4070 O O   . HOH Z  5 .   ? -21.592 5.215   -11.958 1.00 30.95 ? 459 HOH B O   1 
HETATM 4071 O O   . HOH Z  5 .   ? -39.922 -11.603 -21.402 1.00 26.00 ? 460 HOH B O   1 
HETATM 4072 O O   . HOH Z  5 .   ? -14.086 8.190   2.314   1.00 24.74 ? 461 HOH B O   1 
HETATM 4073 O O   . HOH Z  5 .   ? -25.235 -3.679  -6.068  1.00 27.56 ? 462 HOH B O   1 
HETATM 4074 O O   . HOH Z  5 .   ? -47.618 7.272   -5.231  1.00 37.15 ? 463 HOH B O   1 
HETATM 4075 O O   . HOH Z  5 .   ? -8.471  12.710  -19.008 1.00 34.25 ? 464 HOH B O   1 
HETATM 4076 O O   . HOH Z  5 .   ? -43.219 -6.552  -18.674 1.00 33.53 ? 465 HOH B O   1 
HETATM 4077 O O   . HOH Z  5 .   ? -46.720 -1.886  -11.024 1.00 31.11 ? 466 HOH B O   1 
HETATM 4078 O O   . HOH Z  5 .   ? -23.888 17.332  -13.436 1.00 28.71 ? 467 HOH B O   1 
HETATM 4079 O O   . HOH Z  5 .   ? -8.468  10.646  3.425   1.00 33.54 ? 468 HOH B O   1 
HETATM 4080 O O   . HOH Z  5 .   ? -28.614 -1.410  -29.799 1.00 28.42 ? 469 HOH B O   1 
HETATM 4081 O O   . HOH Z  5 .   ? -27.457 11.291  20.492  1.00 31.57 ? 470 HOH B O   1 
HETATM 4082 O O   . HOH Z  5 .   ? -35.903 -12.531 -5.382  1.00 23.15 ? 471 HOH B O   1 
HETATM 4083 O O   . HOH Z  5 .   ? -35.766 -9.581  -2.004  1.00 23.26 ? 472 HOH B O   1 
HETATM 4084 O O   . HOH Z  5 .   ? -35.204 13.696  -21.878 1.00 42.71 ? 473 HOH B O   1 
HETATM 4085 O O   . HOH Z  5 .   ? -40.618 -14.742 -1.289  1.00 47.74 ? 474 HOH B O   1 
HETATM 4086 O O   . HOH Z  5 .   ? -6.637  8.456   1.929   1.00 44.09 ? 475 HOH B O   1 
HETATM 4087 O O   . HOH Z  5 .   ? -8.891  9.701   -24.207 1.00 37.60 ? 476 HOH B O   1 
HETATM 4088 O O   . HOH Z  5 .   ? -33.441 9.199   3.066   1.00 23.08 ? 477 HOH B O   1 
HETATM 4089 O O   . HOH Z  5 .   ? -19.269 -8.509  -25.079 1.00 39.00 ? 478 HOH B O   1 
HETATM 4090 O O   . HOH Z  5 .   ? -20.198 -6.630  -19.832 1.00 23.92 ? 479 HOH B O   1 
HETATM 4091 O O   . HOH Z  5 .   ? -34.082 3.210   1.538   1.00 39.02 ? 480 HOH B O   1 
HETATM 4092 O O   . HOH Z  5 .   ? -28.947 7.174   2.556   1.00 18.24 ? 481 HOH B O   1 
HETATM 4093 O O   . HOH Z  5 .   ? -41.809 13.974  -10.515 1.00 33.50 ? 482 HOH B O   1 
HETATM 4094 O O   . HOH Z  5 .   ? -23.172 6.035   -9.738  1.00 20.21 ? 483 HOH B O   1 
HETATM 4095 O O   . HOH Z  5 .   ? -15.190 12.725  7.081   1.00 42.10 ? 484 HOH B O   1 
HETATM 4096 O O   . HOH Z  5 .   ? -40.237 -13.574 -5.770  1.00 37.59 ? 485 HOH B O   1 
HETATM 4097 O O   . HOH Z  5 .   ? -38.443 -14.155 -12.337 1.00 24.57 ? 486 HOH B O   1 
HETATM 4098 O O   . HOH Z  5 .   ? -18.039 -5.755  -14.157 1.00 30.83 ? 487 HOH B O   1 
HETATM 4099 O O   . HOH Z  5 .   ? -23.740 2.374   -10.527 1.00 23.10 ? 488 HOH B O   1 
HETATM 4100 O O   . HOH Z  5 .   ? -20.008 -13.937 -18.538 1.00 31.99 ? 489 HOH B O   1 
HETATM 4101 O O   . HOH Z  5 .   ? -15.377 9.840   -21.280 1.00 33.04 ? 490 HOH B O   1 
HETATM 4102 O O   . HOH Z  5 .   ? -5.418  17.120  -13.748 1.00 34.66 ? 491 HOH B O   1 
HETATM 4103 O O   . HOH Z  5 .   ? -22.133 3.623   8.937   1.00 29.83 ? 492 HOH B O   1 
HETATM 4104 O O   . HOH Z  5 .   ? -33.759 -4.138  -19.902 1.00 18.89 ? 493 HOH B O   1 
HETATM 4105 O O   . HOH Z  5 .   ? -4.665  18.385  -19.623 1.00 42.65 ? 494 HOH B O   1 
HETATM 4106 O O   . HOH Z  5 .   ? -39.181 11.097  -15.968 1.00 29.56 ? 495 HOH B O   1 
HETATM 4107 O O   . HOH Z  5 .   ? -32.255 -0.023  -28.402 1.00 36.40 ? 496 HOH B O   1 
HETATM 4108 O O   . HOH Z  5 .   ? -36.190 11.086  0.046   1.00 42.02 ? 497 HOH B O   1 
HETATM 4109 O O   . HOH Z  5 .   ? -20.722 5.877   -8.488  1.00 23.53 ? 498 HOH B O   1 
HETATM 4110 O O   . HOH Z  5 .   ? -20.829 2.217   4.098   1.00 39.77 ? 499 HOH B O   1 
HETATM 4111 O O   . HOH Z  5 .   ? -1.561  -0.432  -10.299 1.00 28.13 ? 500 HOH B O   1 
HETATM 4112 O O   . HOH Z  5 .   ? -27.059 19.040  -18.432 1.00 40.51 ? 501 HOH B O   1 
HETATM 4113 O O   . HOH Z  5 .   ? -25.840 2.499   -8.018  1.00 16.17 ? 502 HOH B O   1 
HETATM 4114 O O   . HOH Z  5 .   ? -28.440 -2.488  -0.974  1.00 26.68 ? 503 HOH B O   1 
HETATM 4115 O O   . HOH Z  5 .   ? -34.533 -1.665  -20.217 1.00 29.66 ? 504 HOH B O   1 
HETATM 4116 O O   . HOH Z  5 .   ? -38.430 -0.186  -17.978 1.00 19.55 ? 505 HOH B O   1 
HETATM 4117 O O   . HOH Z  5 .   ? -27.172 -9.689  -7.908  1.00 27.50 ? 506 HOH B O   1 
HETATM 4118 O O   . HOH Z  5 .   ? -39.623 7.100   -17.216 1.00 32.96 ? 507 HOH B O   1 
HETATM 4119 O O   . HOH Z  5 .   ? -31.623 -5.977  -5.355  1.00 29.81 ? 508 HOH B O   1 
HETATM 4120 O O   . HOH Z  5 .   ? -33.375 2.508   -21.267 1.00 21.64 ? 509 HOH B O   1 
HETATM 4121 O O   . HOH Z  5 .   ? -29.174 3.913   14.156  1.00 38.12 ? 510 HOH B O   1 
HETATM 4122 O O   . HOH Z  5 .   ? -7.757  15.263  -7.052  1.00 29.23 ? 511 HOH B O   1 
HETATM 4123 O O   . HOH Z  5 .   ? -20.480 -6.261  -11.831 1.00 37.54 ? 512 HOH B O   1 
HETATM 4124 O O   . HOH Z  5 .   ? -12.683 12.056  -0.643  1.00 31.62 ? 513 HOH B O   1 
HETATM 4125 O O   . HOH Z  5 .   ? -4.417  -3.497  -10.121 1.00 44.41 ? 514 HOH B O   1 
HETATM 4126 O O   . HOH Z  5 .   ? -40.097 -12.437 -18.867 1.00 34.25 ? 515 HOH B O   1 
HETATM 4127 O O   . HOH Z  5 .   ? -31.884 20.640  1.856   1.00 39.36 ? 516 HOH B O   1 
HETATM 4128 O O   . HOH Z  5 .   ? -19.783 -8.912  -12.548 1.00 34.28 ? 517 HOH B O   1 
HETATM 4129 O O   . HOH Z  5 .   ? -23.451 5.133   -14.010 1.00 17.98 ? 518 HOH B O   1 
HETATM 4130 O O   . HOH Z  5 .   ? -22.902 4.619   -2.212  1.00 14.30 ? 519 HOH B O   1 
HETATM 4131 O O   . HOH Z  5 .   ? -11.864 -5.045  -12.545 1.00 34.02 ? 520 HOH B O   1 
HETATM 4132 O O   . HOH Z  5 .   ? -37.184 -0.568  -0.740  1.00 22.00 ? 521 HOH B O   1 
HETATM 4133 O O   . HOH Z  5 .   ? -27.280 -1.920  -3.377  1.00 18.20 ? 522 HOH B O   1 
HETATM 4134 O O   . HOH Z  5 .   ? -16.204 -3.781  -8.489  1.00 25.41 ? 523 HOH B O   1 
HETATM 4135 O O   . HOH Z  5 .   ? -31.669 5.094   0.482   1.00 24.55 ? 524 HOH B O   1 
HETATM 4136 O O   . HOH Z  5 .   ? -37.256 -6.931  -25.279 1.00 43.35 ? 525 HOH B O   1 
HETATM 4137 O O   A HOH Z  5 .   ? -35.254 -1.568  -8.830  0.50 10.59 ? 526 HOH B O   1 
HETATM 4138 O O   . HOH Z  5 .   ? -46.702 4.609   -8.436  1.00 24.35 ? 527 HOH B O   1 
HETATM 4139 O O   . HOH Z  5 .   ? -33.060 1.292   -18.830 1.00 17.83 ? 528 HOH B O   1 
HETATM 4140 O O   . HOH Z  5 .   ? -47.389 8.496   -7.973  1.00 40.34 ? 529 HOH B O   1 
HETATM 4141 O O   . HOH Z  5 .   ? -24.853 19.296  -12.357 1.00 37.85 ? 530 HOH B O   1 
HETATM 4142 O O   . HOH Z  5 .   ? -40.475 13.713  -3.292  1.00 43.96 ? 531 HOH B O   1 
HETATM 4143 O O   . HOH Z  5 .   ? -27.114 16.161  -26.935 1.00 43.39 ? 532 HOH B O   1 
HETATM 4144 O O   . HOH Z  5 .   ? -26.397 2.300   7.802   1.00 28.18 ? 533 HOH B O   1 
HETATM 4145 O O   . HOH Z  5 .   ? -27.184 -0.507  0.069   1.00 26.06 ? 534 HOH B O   1 
HETATM 4146 O O   . HOH Z  5 .   ? -7.550  1.246   3.677   1.00 32.45 ? 535 HOH B O   1 
HETATM 4147 O O   . HOH Z  5 .   ? -43.030 3.860   -1.999  1.00 33.13 ? 536 HOH B O   1 
HETATM 4148 O O   . HOH Z  5 .   ? -11.057 0.156   -20.793 1.00 27.68 ? 537 HOH B O   1 
HETATM 4149 O O   . HOH Z  5 .   ? -31.031 -4.797  5.211   1.00 38.30 ? 538 HOH B O   1 
HETATM 4150 O O   . HOH Z  5 .   ? -44.319 9.767   -10.078 1.00 31.37 ? 539 HOH B O   1 
HETATM 4151 O O   . HOH Z  5 .   ? -22.555 6.381   -30.147 1.00 31.13 ? 540 HOH B O   1 
HETATM 4152 O O   . HOH Z  5 .   ? -6.387  11.430  -0.968  1.00 36.09 ? 541 HOH B O   1 
HETATM 4153 O O   . HOH Z  5 .   ? -39.814 -1.365  0.577   1.00 37.43 ? 542 HOH B O   1 
HETATM 4154 O O   . HOH Z  5 .   ? -9.202  21.340  -15.767 1.00 42.26 ? 543 HOH B O   1 
HETATM 4155 O O   . HOH Z  5 .   ? -35.270 -1.289  1.244   1.00 19.16 ? 544 HOH B O   1 
HETATM 4156 O O   . HOH Z  5 .   ? -29.178 16.171  -17.342 1.00 33.34 ? 545 HOH B O   1 
HETATM 4157 O O   . HOH Z  5 .   ? -39.887 10.307  0.744   1.00 41.83 ? 546 HOH B O   1 
HETATM 4158 O O   . HOH Z  5 .   ? -39.250 6.652   0.783   1.00 44.72 ? 547 HOH B O   1 
HETATM 4159 O O   . HOH Z  5 .   ? -22.343 2.222   -1.100  1.00 24.43 ? 548 HOH B O   1 
HETATM 4160 O O   . HOH Z  5 .   ? -21.163 -14.162 -27.345 1.00 33.98 ? 549 HOH B O   1 
HETATM 4161 O O   . HOH Z  5 .   ? -7.148  -2.917  3.079   1.00 22.84 ? 550 HOH B O   1 
HETATM 4162 O O   . HOH Z  5 .   ? -14.448 20.883  -20.858 1.00 44.49 ? 551 HOH B O   1 
HETATM 4163 O O   . HOH Z  5 .   ? -21.858 3.660   -27.846 1.00 24.34 ? 552 HOH B O   1 
HETATM 4164 O O   . HOH Z  5 .   ? -14.580 3.695   -24.285 1.00 40.51 ? 553 HOH B O   1 
HETATM 4165 O O   . HOH Z  5 .   ? -3.087  15.868  -13.776 1.00 41.45 ? 554 HOH B O   1 
HETATM 4166 O O   . HOH Z  5 .   ? -2.305  -2.553  -8.825  1.00 51.71 ? 555 HOH B O   1 
HETATM 4167 O O   . HOH Z  5 .   ? -5.608  2.858   5.125   1.00 19.16 ? 556 HOH B O   1 
HETATM 4168 O O   . HOH Z  5 .   ? -16.915 -1.112  -4.749  1.00 30.03 ? 557 HOH B O   1 
HETATM 4169 O O   . HOH Z  5 .   ? -30.483 13.147  -25.967 1.00 35.37 ? 558 HOH B O   1 
HETATM 4170 O O   . HOH Z  5 .   ? -7.866  6.754   0.945   1.00 25.86 ? 559 HOH B O   1 
HETATM 4171 O O   . HOH Z  5 .   ? -14.760 5.660   1.589   1.00 28.57 ? 560 HOH B O   1 
HETATM 4172 O O   . HOH Z  5 .   ? -12.736 1.868   -23.504 1.00 34.76 ? 561 HOH B O   1 
HETATM 4173 O O   . HOH Z  5 .   ? -11.463 4.365   2.187   1.00 26.10 ? 562 HOH B O   1 
HETATM 4174 O O   . HOH Z  5 .   ? -10.223 6.463   2.147   1.00 28.14 ? 563 HOH B O   1 
HETATM 4175 O O   . HOH Z  5 .   ? -13.790 -0.629  2.442   1.00 37.08 ? 564 HOH B O   1 
HETATM 4176 O O   . HOH Z  5 .   ? -32.608 0.567   4.321   1.00 32.85 ? 565 HOH B O   1 
HETATM 4177 O O   . HOH Z  5 .   ? -9.134  3.323   3.996   1.00 34.66 ? 566 HOH B O   1 
HETATM 4178 O O   . HOH Z  5 .   ? -43.121 10.978  -12.831 1.00 41.96 ? 567 HOH B O   1 
HETATM 4179 O O   . HOH Z  5 .   ? -21.683 -6.291  -23.836 1.00 36.99 ? 568 HOH B O   1 
HETATM 4180 O O   . HOH Z  5 .   ? -9.788  18.338  -4.707  1.00 43.71 ? 569 HOH B O   1 
HETATM 4181 O O   . HOH Z  5 .   ? -10.609 13.070  -25.707 1.00 41.63 ? 570 HOH B O   1 
HETATM 4182 O O   . HOH Z  5 .   ? -36.632 -13.207 -0.372  1.00 45.70 ? 571 HOH B O   1 
HETATM 4183 O O   . HOH Z  5 .   ? -13.367 -5.114  -19.959 1.00 34.46 ? 572 HOH B O   1 
HETATM 4184 O O   . HOH Z  5 .   ? -13.907 14.286  -20.961 1.00 28.88 ? 573 HOH B O   1 
HETATM 4185 O O   . HOH Z  5 .   ? -43.505 2.099   -0.393  1.00 33.14 ? 574 HOH B O   1 
HETATM 4186 O O   . HOH Z  5 .   ? -35.628 1.207   -21.996 1.00 25.19 ? 575 HOH B O   1 
HETATM 4187 O O   . HOH Z  5 .   ? -32.587 -6.278  -2.619  1.00 34.01 ? 576 HOH B O   1 
HETATM 4188 O O   . HOH Z  5 .   ? -20.264 -0.890  -20.928 1.00 40.77 ? 577 HOH B O   1 
HETATM 4189 O O   . HOH Z  5 .   ? -47.075 -5.256  -2.220  1.00 38.69 ? 578 HOH B O   1 
HETATM 4190 O O   . HOH Z  5 .   ? -19.638 -5.854  -9.478  1.00 34.58 ? 579 HOH B O   1 
HETATM 4191 O O   . HOH Z  5 .   ? -46.663 -1.031  -3.039  1.00 44.31 ? 580 HOH B O   1 
HETATM 4192 O O   . HOH Z  5 .   ? -25.777 21.039  -14.117 1.00 43.38 ? 581 HOH B O   1 
HETATM 4193 O O   . HOH Z  5 .   ? -9.210  -1.421  -13.018 1.00 24.09 ? 582 HOH B O   1 
HETATM 4194 O O   . HOH Z  5 .   ? -6.741  6.886   3.948   1.00 38.29 ? 583 HOH B O   1 
HETATM 4195 O O   . HOH Z  5 .   ? -40.760 -7.919  -22.847 1.00 39.29 ? 584 HOH B O   1 
HETATM 4196 O O   . HOH Z  5 .   ? -39.028 -15.361 -4.168  1.00 41.39 ? 585 HOH B O   1 
HETATM 4197 O O   . HOH Z  5 .   ? -33.706 -7.922  -1.263  1.00 35.51 ? 586 HOH B O   1 
HETATM 4198 O O   . HOH Z  5 .   ? -33.122 11.642  -26.087 1.00 39.97 ? 587 HOH B O   1 
HETATM 4199 O O   . HOH Z  5 .   ? -15.550 16.376  -1.136  1.00 41.79 ? 588 HOH B O   1 
HETATM 4200 O O   . HOH Z  5 .   ? -22.131 -2.375  -1.919  1.00 36.96 ? 589 HOH B O   1 
HETATM 4201 O O   . HOH Z  5 .   ? -23.617 -0.192  -1.497  1.00 22.36 ? 590 HOH B O   1 
HETATM 4202 O O   . HOH Z  5 .   ? -33.523 14.788  8.259   1.00 40.26 ? 591 HOH B O   1 
HETATM 4203 O O   . HOH Z  5 .   ? -10.901 13.935  -4.190  1.00 31.54 ? 592 HOH B O   1 
HETATM 4204 O O   . HOH Z  5 .   ? -27.659 9.689   3.234   1.00 19.69 ? 593 HOH B O   1 
HETATM 4205 O O   . HOH Z  5 .   ? -14.174 7.675   5.070   1.00 42.53 ? 594 HOH B O   1 
HETATM 4206 O O   . HOH Z  5 .   ? -20.441 2.219   1.181   1.00 33.34 ? 595 HOH B O   1 
HETATM 4207 O O   . HOH Z  5 .   ? -11.761 -5.231  -7.680  1.00 44.91 ? 596 HOH B O   1 
HETATM 4208 O O   . HOH Z  5 .   ? -16.192 8.664   6.751   1.00 31.09 ? 597 HOH B O   1 
HETATM 4209 O O   . HOH Z  5 .   ? -26.271 -4.223  -4.039  1.00 32.57 ? 598 HOH B O   1 
HETATM 4210 O O   . HOH Z  5 .   ? -34.638 0.867   2.731   1.00 34.17 ? 599 HOH B O   1 
HETATM 4211 O O   . HOH Z  5 .   ? -36.087 -2.996  3.034   1.00 25.20 ? 600 HOH B O   1 
HETATM 4212 O O   . HOH Z  5 .   ? -16.494 -6.661  -12.133 1.00 30.83 ? 601 HOH B O   1 
HETATM 4213 O O   . HOH Z  5 .   ? -38.186 13.741  -16.504 1.00 38.46 ? 602 HOH B O   1 
HETATM 4214 O O   . HOH Z  5 .   ? -39.192 3.919   0.849   1.00 43.00 ? 603 HOH B O   1 
HETATM 4215 O O   . HOH Z  5 .   ? -21.174 -6.027  -7.327  1.00 42.26 ? 604 HOH B O   1 
HETATM 4216 O O   . HOH Z  5 .   ? -31.566 7.180   2.829   1.00 24.87 ? 605 HOH B O   1 
HETATM 4217 O O   . HOH Z  5 .   ? -41.789 -10.442 -22.739 1.00 39.02 ? 606 HOH B O   1 
HETATM 4218 O O   . HOH Z  5 .   ? -34.854 -12.039 -1.879  1.00 43.17 ? 607 HOH B O   1 
HETATM 4219 O O   . HOH Z  5 .   ? -14.651 13.584  -2.149  1.00 34.12 ? 608 HOH B O   1 
HETATM 4220 O O   . HOH Z  5 .   ? -30.744 -14.521 -7.316  1.00 29.25 ? 609 HOH B O   1 
HETATM 4221 O O   . HOH Z  5 .   ? -30.300 -7.099  -3.436  1.00 38.85 ? 610 HOH B O   1 
HETATM 4222 O O   . HOH Z  5 .   ? -42.298 -13.698 -3.433  1.00 42.85 ? 611 HOH B O   1 
HETATM 4223 O O   . HOH Z  5 .   ? -35.659 -0.049  -18.967 1.00 34.01 ? 612 HOH B O   1 
HETATM 4224 O O   . HOH Z  5 .   ? -40.632 1.283   -18.381 1.00 25.04 ? 613 HOH B O   1 
HETATM 4225 O O   . HOH Z  5 .   ? -39.884 -7.417  -25.235 1.00 32.53 ? 614 HOH B O   1 
HETATM 4226 O O   . HOH Z  5 .   ? -17.876 2.686   4.832   1.00 43.08 ? 615 HOH B O   1 
HETATM 4227 O O   . HOH Z  5 .   ? -24.196 -5.881  -7.067  1.00 34.56 ? 616 HOH B O   1 
HETATM 4228 O O   . HOH Z  5 .   ? -40.585 -13.901 -14.769 1.00 33.05 ? 617 HOH B O   1 
HETATM 4229 O O   . HOH Z  5 .   ? -28.033 -5.843  -3.039  1.00 34.98 ? 618 HOH B O   1 
HETATM 4230 O O   . HOH Z  5 .   ? -34.791 8.905   5.310   1.00 36.18 ? 619 HOH B O   1 
HETATM 4231 O O   . HOH Z  5 .   ? -38.809 28.397  0.447   1.00 36.49 ? 620 HOH B O   1 
HETATM 4232 O O   . HOH Z  5 .   ? -40.616 1.467   -21.223 1.00 42.86 ? 621 HOH B O   1 
HETATM 4233 O O   . HOH Z  5 .   ? -8.817  15.549  -4.554  1.00 36.09 ? 622 HOH B O   1 
HETATM 4234 O O   . HOH Z  5 .   ? -25.373 -8.253  -6.302  1.00 31.94 ? 623 HOH B O   1 
HETATM 4235 O O   . HOH Z  5 .   ? -24.284 -4.303  -1.764  1.00 41.22 ? 624 HOH B O   1 
HETATM 4236 O O   . HOH Z  5 .   ? -23.412 -10.299 -5.710  1.00 37.16 ? 625 HOH B O   1 
HETATM 4237 O O   C HOH AA 5 .   ? -11.409 -7.830  16.702  0.33 12.24 ? 401 HOH A O   1 
HETATM 4238 O O   . HOH AA 5 .   ? -14.565 9.661   11.112  1.00 24.55 ? 402 HOH A O   1 
HETATM 4239 O O   . HOH AA 5 .   ? 6.871   6.747   20.358  1.00 41.89 ? 403 HOH A O   1 
HETATM 4240 O O   . HOH AA 5 .   ? 6.925   -2.258  31.053  1.00 31.07 ? 404 HOH A O   1 
HETATM 4241 O O   . HOH AA 5 .   ? 3.078   -21.700 29.911  1.00 31.82 ? 405 HOH A O   1 
HETATM 4242 O O   A HOH AA 5 .   ? 14.760  -7.071  19.972  0.50 24.22 ? 406 HOH A O   1 
HETATM 4243 O O   . HOH AA 5 .   ? -13.433 -6.616  36.320  1.00 38.60 ? 407 HOH A O   1 
HETATM 4244 O O   . HOH AA 5 .   ? -4.802  10.361  16.837  1.00 36.49 ? 408 HOH A O   1 
HETATM 4245 O O   . HOH AA 5 .   ? 8.996   2.676   27.367  1.00 27.16 ? 409 HOH A O   1 
HETATM 4246 O O   . HOH AA 5 .   ? 8.762   -17.502 27.634  1.00 42.94 ? 410 HOH A O   1 
HETATM 4247 O O   . HOH AA 5 .   ? -8.969  -16.713 40.877  1.00 41.52 ? 411 HOH A O   1 
HETATM 4248 O O   . HOH AA 5 .   ? -8.567  8.727   7.896   1.00 28.13 ? 412 HOH A O   1 
HETATM 4249 O O   . HOH AA 5 .   ? 1.542   -8.935  15.148  1.00 14.92 ? 413 HOH A O   1 
HETATM 4250 O O   . HOH AA 5 .   ? -14.393 -10.753 25.316  1.00 32.04 ? 414 HOH A O   1 
HETATM 4251 O O   . HOH AA 5 .   ? -11.173 11.681  9.072   1.00 40.34 ? 415 HOH A O   1 
HETATM 4252 O O   . HOH AA 5 .   ? -1.771  -25.805 31.008  1.00 30.65 ? 416 HOH A O   1 
HETATM 4253 O O   . HOH AA 5 .   ? 4.980   0.391   36.272  1.00 37.83 ? 417 HOH A O   1 
HETATM 4254 O O   . HOH AA 5 .   ? -13.561 -3.543  36.772  1.00 38.61 ? 418 HOH A O   1 
HETATM 4255 O O   . HOH AA 5 .   ? 8.549   -1.734  6.019   1.00 21.73 ? 419 HOH A O   1 
HETATM 4256 O O   . HOH AA 5 .   ? -10.881 -2.010  34.726  1.00 38.99 ? 420 HOH A O   1 
HETATM 4257 O O   . HOH AA 5 .   ? -12.177 -11.397 37.389  1.00 28.65 ? 421 HOH A O   1 
HETATM 4258 O O   . HOH AA 5 .   ? -3.373  -16.823 32.664  1.00 40.59 ? 422 HOH A O   1 
HETATM 4259 O O   . HOH AA 5 .   ? -7.759  -6.904  6.005   1.00 47.98 ? 423 HOH A O   1 
HETATM 4260 O O   . HOH AA 5 .   ? -3.649  9.662   1.625   1.00 28.97 ? 424 HOH A O   1 
HETATM 4261 O O   . HOH AA 5 .   ? -21.645 7.417   29.408  1.00 49.66 ? 425 HOH A O   1 
HETATM 4262 O O   . HOH AA 5 .   ? -16.314 -3.318  31.218  1.00 46.69 ? 426 HOH A O   1 
HETATM 4263 O O   . HOH AA 5 .   ? 1.675   -15.308 12.071  1.00 30.88 ? 427 HOH A O   1 
HETATM 4264 O O   . HOH AA 5 .   ? -7.617  3.896   35.320  1.00 35.98 ? 428 HOH A O   1 
HETATM 4265 O O   . HOH AA 5 .   ? -5.430  -26.862 12.239  1.00 25.31 ? 429 HOH A O   1 
HETATM 4266 O O   . HOH AA 5 .   ? -17.592 1.413   25.493  1.00 22.39 ? 430 HOH A O   1 
HETATM 4267 O O   . HOH AA 5 .   ? -8.890  11.189  14.538  1.00 29.89 ? 431 HOH A O   1 
HETATM 4268 O O   . HOH AA 5 .   ? 12.010  0.718   10.425  1.00 34.15 ? 432 HOH A O   1 
HETATM 4269 O O   . HOH AA 5 .   ? -8.776  17.795  26.257  1.00 40.06 ? 433 HOH A O   1 
HETATM 4270 O O   . HOH AA 5 .   ? -18.185 5.878   31.772  1.00 32.14 ? 434 HOH A O   1 
HETATM 4271 O O   . HOH AA 5 .   ? -7.758  -8.098  15.457  1.00 16.65 ? 435 HOH A O   1 
HETATM 4272 O O   . HOH AA 5 .   ? -19.958 2.492   25.087  1.00 32.92 ? 436 HOH A O   1 
HETATM 4273 O O   . HOH AA 5 .   ? 3.772   12.410  8.818   1.00 46.71 ? 437 HOH A O   1 
HETATM 4274 O O   . HOH AA 5 .   ? -9.981  12.718  31.269  1.00 31.08 ? 438 HOH A O   1 
HETATM 4275 O O   . HOH AA 5 .   ? 10.880  7.577   -3.407  1.00 36.76 ? 439 HOH A O   1 
HETATM 4276 O O   . HOH AA 5 .   ? 4.572   10.529  14.472  1.00 43.97 ? 440 HOH A O   1 
HETATM 4277 O O   . HOH AA 5 .   ? -9.246  6.023   9.748   1.00 24.62 ? 441 HOH A O   1 
HETATM 4278 O O   . HOH AA 5 .   ? -17.435 -0.858  17.053  1.00 29.62 ? 442 HOH A O   1 
HETATM 4279 O O   . HOH AA 5 .   ? -12.254 13.520  13.155  1.00 36.96 ? 443 HOH A O   1 
HETATM 4280 O O   . HOH AA 5 .   ? 11.915  -15.945 21.934  1.00 35.85 ? 444 HOH A O   1 
HETATM 4281 O O   . HOH AA 5 .   ? 3.678   -12.000 38.700  1.00 28.40 ? 445 HOH A O   1 
HETATM 4282 O O   . HOH AA 5 .   ? -4.794  -2.489  21.856  1.00 16.85 ? 446 HOH A O   1 
HETATM 4283 O O   . HOH AA 5 .   ? -0.662  10.113  3.976   1.00 26.07 ? 447 HOH A O   1 
HETATM 4284 O O   . HOH AA 5 .   ? 8.643   -3.752  4.356   1.00 39.77 ? 448 HOH A O   1 
HETATM 4285 O O   . HOH AA 5 .   ? 9.671   -10.244 13.219  1.00 35.76 ? 449 HOH A O   1 
HETATM 4286 O O   . HOH AA 5 .   ? -10.644 -10.216 17.713  1.00 29.22 ? 450 HOH A O   1 
HETATM 4287 O O   . HOH AA 5 .   ? -6.588  -21.542 37.214  1.00 33.48 ? 451 HOH A O   1 
HETATM 4288 O O   . HOH AA 5 .   ? 0.109   10.742  9.114   1.00 37.32 ? 452 HOH A O   1 
HETATM 4289 O O   . HOH AA 5 .   ? -14.127 -15.840 19.627  1.00 25.14 ? 453 HOH A O   1 
HETATM 4290 O O   . HOH AA 5 .   ? -5.756  -17.153 31.976  1.00 18.91 ? 454 HOH A O   1 
HETATM 4291 O O   . HOH AA 5 .   ? -13.264 -13.065 35.323  1.00 28.59 ? 455 HOH A O   1 
HETATM 4292 O O   . HOH AA 5 .   ? -14.988 -12.682 32.980  1.00 26.56 ? 456 HOH A O   1 
HETATM 4293 O O   . HOH AA 5 .   ? 5.252   8.110   -0.137  1.00 30.08 ? 457 HOH A O   1 
HETATM 4294 O O   . HOH AA 5 .   ? 6.386   -5.149  3.022   1.00 38.13 ? 458 HOH A O   1 
HETATM 4295 O O   . HOH AA 5 .   ? 7.143   -18.734 14.075  1.00 36.14 ? 459 HOH A O   1 
HETATM 4296 O O   . HOH AA 5 .   ? -6.380  10.706  31.128  1.00 29.32 ? 460 HOH A O   1 
HETATM 4297 O O   . HOH AA 5 .   ? 0.269   -18.068 29.938  1.00 19.81 ? 461 HOH A O   1 
HETATM 4298 O O   . HOH AA 5 .   ? -9.452  -0.293  36.434  1.00 37.37 ? 462 HOH A O   1 
HETATM 4299 O O   . HOH AA 5 .   ? -15.403 14.726  10.793  1.00 28.64 ? 463 HOH A O   1 
HETATM 4300 O O   . HOH AA 5 .   ? 3.933   4.415   25.531  1.00 25.07 ? 464 HOH A O   1 
HETATM 4301 O O   . HOH AA 5 .   ? -10.401 -0.272  10.038  1.00 47.32 ? 465 HOH A O   1 
HETATM 4302 O O   . HOH AA 5 .   ? -6.744  -0.683  20.314  1.00 17.48 ? 466 HOH A O   1 
HETATM 4303 O O   . HOH AA 5 .   ? -6.488  -1.829  23.769  1.00 18.80 ? 467 HOH A O   1 
HETATM 4304 O O   . HOH AA 5 .   ? -7.117  -22.200 8.789   1.00 31.92 ? 468 HOH A O   1 
HETATM 4305 O O   . HOH AA 5 .   ? -5.750  -6.814  19.862  1.00 14.82 ? 469 HOH A O   1 
HETATM 4306 O O   . HOH AA 5 .   ? -3.656  -13.587 40.210  1.00 34.00 ? 470 HOH A O   1 
HETATM 4307 O O   . HOH AA 5 .   ? -5.067  -8.177  12.972  1.00 16.18 ? 471 HOH A O   1 
HETATM 4308 O O   . HOH AA 5 .   ? -18.975 -15.684 23.951  1.00 39.89 ? 472 HOH A O   1 
HETATM 4309 O O   . HOH AA 5 .   ? -0.777  -24.851 7.247   1.00 27.38 ? 473 HOH A O   1 
HETATM 4310 O O   . HOH AA 5 .   ? 1.367   -8.899  2.844   1.00 34.76 ? 474 HOH A O   1 
HETATM 4311 O O   . HOH AA 5 .   ? -9.610  -10.476 37.995  1.00 30.78 ? 475 HOH A O   1 
HETATM 4312 O O   . HOH AA 5 .   ? -4.102  2.944   43.595  1.00 17.65 ? 476 HOH A O   1 
HETATM 4313 O O   . HOH AA 5 .   ? -8.482  15.100  19.445  1.00 29.35 ? 477 HOH A O   1 
HETATM 4314 O O   . HOH AA 5 .   ? -14.665 -14.437 39.277  1.00 42.59 ? 478 HOH A O   1 
HETATM 4315 O O   . HOH AA 5 .   ? 9.393   -11.196 27.978  1.00 38.06 ? 479 HOH A O   1 
HETATM 4316 O O   . HOH AA 5 .   ? 11.253  3.693   -11.392 1.00 42.78 ? 480 HOH A O   1 
HETATM 4317 O O   . HOH AA 5 .   ? -9.609  -27.233 17.922  1.00 32.58 ? 481 HOH A O   1 
HETATM 4318 O O   . HOH AA 5 .   ? 0.122   12.494  24.573  1.00 35.55 ? 482 HOH A O   1 
HETATM 4319 O O   . HOH AA 5 .   ? -7.326  5.492   33.391  1.00 27.80 ? 483 HOH A O   1 
HETATM 4320 O O   . HOH AA 5 .   ? -18.716 -13.140 36.924  1.00 38.16 ? 484 HOH A O   1 
HETATM 4321 O O   . HOH AA 5 .   ? -5.102  6.499   33.611  1.00 25.49 ? 485 HOH A O   1 
HETATM 4322 O O   . HOH AA 5 .   ? -15.502 3.009   8.891   1.00 25.54 ? 486 HOH A O   1 
HETATM 4323 O O   . HOH AA 5 .   ? 1.327   -2.570  11.393  1.00 15.64 ? 487 HOH A O   1 
HETATM 4324 O O   . HOH AA 5 .   ? 1.767   11.157  15.833  1.00 31.74 ? 488 HOH A O   1 
HETATM 4325 O O   . HOH AA 5 .   ? 13.652  -13.864 17.827  1.00 44.53 ? 489 HOH A O   1 
HETATM 4326 O O   . HOH AA 5 .   ? -9.404  3.526   41.676  1.00 37.88 ? 490 HOH A O   1 
HETATM 4327 O O   . HOH AA 5 .   ? -5.833  -9.209  6.033   1.00 41.40 ? 491 HOH A O   1 
HETATM 4328 O O   . HOH AA 5 .   ? 0.028   -5.798  9.440   1.00 17.37 ? 492 HOH A O   1 
HETATM 4329 O O   . HOH AA 5 .   ? -7.387  -5.372  22.437  1.00 20.38 ? 493 HOH A O   1 
HETATM 4330 O O   . HOH AA 5 .   ? -14.431 -14.294 41.912  1.00 35.84 ? 494 HOH A O   1 
HETATM 4331 O O   . HOH AA 5 .   ? 4.485   -7.879  8.994   1.00 22.62 ? 495 HOH A O   1 
HETATM 4332 O O   . HOH AA 5 .   ? -4.735  15.581  17.529  1.00 30.06 ? 496 HOH A O   1 
HETATM 4333 O O   . HOH AA 5 .   ? 5.586   0.844   32.895  1.00 44.97 ? 497 HOH A O   1 
HETATM 4334 O O   . HOH AA 5 .   ? -7.478  18.022  24.110  1.00 41.02 ? 498 HOH A O   1 
HETATM 4335 O O   . HOH AA 5 .   ? 7.712   0.837   12.429  1.00 41.42 ? 499 HOH A O   1 
HETATM 4336 O O   . HOH AA 5 .   ? 10.872  4.665   14.996  1.00 46.77 ? 500 HOH A O   1 
HETATM 4337 O O   . HOH AA 5 .   ? 9.105   -5.650  31.598  1.00 31.03 ? 501 HOH A O   1 
HETATM 4338 O O   . HOH AA 5 .   ? -8.288  -27.181 29.748  1.00 37.13 ? 502 HOH A O   1 
HETATM 4339 O O   . HOH AA 5 .   ? -6.452  16.261  20.635  1.00 36.38 ? 503 HOH A O   1 
HETATM 4340 O O   . HOH AA 5 .   ? -16.869 -3.835  20.256  1.00 26.77 ? 504 HOH A O   1 
HETATM 4341 O O   . HOH AA 5 .   ? 8.230   -0.789  26.865  1.00 22.63 ? 505 HOH A O   1 
HETATM 4342 O O   . HOH AA 5 .   ? -5.096  8.713   5.253   1.00 36.19 ? 506 HOH A O   1 
HETATM 4343 O O   . HOH AA 5 .   ? 2.555   -1.437  -8.995  1.00 37.95 ? 507 HOH A O   1 
HETATM 4344 O O   . HOH AA 5 .   ? -5.875  -0.385  43.176  1.00 22.65 ? 508 HOH A O   1 
HETATM 4345 O O   . HOH AA 5 .   ? -0.144  -17.284 12.387  1.00 21.72 ? 509 HOH A O   1 
HETATM 4346 O O   . HOH AA 5 .   ? -0.905  -13.068 33.203  1.00 25.59 ? 510 HOH A O   1 
HETATM 4347 O O   . HOH AA 5 .   ? -7.227  -18.071 14.598  1.00 29.56 ? 511 HOH A O   1 
HETATM 4348 O O   . HOH AA 5 .   ? 1.831   9.554   4.918   1.00 37.78 ? 512 HOH A O   1 
HETATM 4349 O O   . HOH AA 5 .   ? 6.386   4.844   24.635  1.00 26.22 ? 513 HOH A O   1 
HETATM 4350 O O   . HOH AA 5 .   ? -8.982  -6.823  13.237  1.00 24.02 ? 514 HOH A O   1 
HETATM 4351 O O   . HOH AA 5 .   ? 12.451  -11.187 16.042  1.00 41.29 ? 515 HOH A O   1 
HETATM 4352 O O   . HOH AA 5 .   ? -12.873 -0.319  10.431  1.00 33.05 ? 516 HOH A O   1 
HETATM 4353 O O   . HOH AA 5 .   ? 9.616   -21.072 21.097  1.00 23.62 ? 517 HOH A O   1 
HETATM 4354 O O   . HOH AA 5 .   ? 2.426   6.946   38.834  1.00 43.36 ? 518 HOH A O   1 
HETATM 4355 O O   . HOH AA 5 .   ? -5.521  -3.432  25.965  1.00 17.53 ? 519 HOH A O   1 
HETATM 4356 O O   . HOH AA 5 .   ? 5.029   11.538  24.610  1.00 45.81 ? 520 HOH A O   1 
HETATM 4357 O O   . HOH AA 5 .   ? -8.036  -1.041  4.820   1.00 35.45 ? 521 HOH A O   1 
HETATM 4358 O O   . HOH AA 5 .   ? -6.044  -3.069  14.191  1.00 13.22 ? 522 HOH A O   1 
HETATM 4359 O O   . HOH AA 5 .   ? 8.251   4.537   5.594   1.00 43.47 ? 523 HOH A O   1 
HETATM 4360 O O   . HOH AA 5 .   ? -7.951  -4.132  39.223  1.00 18.29 ? 524 HOH A O   1 
HETATM 4361 O O   . HOH AA 5 .   ? -6.815  -24.133 10.636  1.00 31.34 ? 525 HOH A O   1 
HETATM 4362 O O   . HOH AA 5 .   ? 13.075  -13.725 14.734  1.00 50.75 ? 526 HOH A O   1 
HETATM 4363 O O   . HOH AA 5 .   ? -2.046  -13.281 30.678  1.00 17.97 ? 527 HOH A O   1 
HETATM 4364 O O   . HOH AA 5 .   ? -13.411 -17.307 17.469  1.00 30.77 ? 528 HOH A O   1 
HETATM 4365 O O   . HOH AA 5 .   ? -9.080  -3.056  7.870   1.00 42.41 ? 529 HOH A O   1 
HETATM 4366 O O   . HOH AA 5 .   ? 0.183   -9.393  11.330  1.00 25.09 ? 530 HOH A O   1 
HETATM 4367 O O   . HOH AA 5 .   ? -14.612 -2.513  16.259  1.00 34.62 ? 531 HOH A O   1 
HETATM 4368 O O   . HOH AA 5 .   ? -18.849 8.851   7.016   1.00 20.22 ? 532 HOH A O   1 
HETATM 4369 O O   . HOH AA 5 .   ? -0.498  -22.681 10.371  1.00 37.85 ? 533 HOH A O   1 
HETATM 4370 O O   A HOH AA 5 .   ? -2.479  -16.745 20.711  0.50 10.16 ? 534 HOH A O   1 
HETATM 4371 O O   . HOH AA 5 .   ? -17.634 2.084   32.705  1.00 23.98 ? 535 HOH A O   1 
HETATM 4372 O O   . HOH AA 5 .   ? -18.853 6.114   8.252   1.00 27.82 ? 536 HOH A O   1 
HETATM 4373 O O   . HOH AA 5 .   ? -5.392  -6.858  4.137   1.00 33.39 ? 537 HOH A O   1 
HETATM 4374 O O   . HOH AA 5 .   ? -4.300  -16.880 38.752  1.00 38.98 ? 538 HOH A O   1 
HETATM 4375 O O   . HOH AA 5 .   ? 13.928  -0.219  23.361  1.00 32.15 ? 539 HOH A O   1 
HETATM 4376 O O   . HOH AA 5 .   ? 0.444   -25.237 28.777  1.00 37.59 ? 540 HOH A O   1 
HETATM 4377 O O   . HOH AA 5 .   ? -10.469 2.850   36.412  1.00 32.48 ? 541 HOH A O   1 
HETATM 4378 O O   . HOH AA 5 .   ? -11.596 -7.335  14.050  1.00 40.01 ? 542 HOH A O   1 
HETATM 4379 O O   . HOH AA 5 .   ? -15.463 2.066   35.270  1.00 28.47 ? 543 HOH A O   1 
HETATM 4380 O O   . HOH AA 5 .   ? 8.613   -6.023  34.168  1.00 35.94 ? 544 HOH A O   1 
HETATM 4381 O O   . HOH AA 5 .   ? -0.839  11.873  21.589  1.00 31.12 ? 545 HOH A O   1 
HETATM 4382 O O   . HOH AA 5 .   ? -8.082  -22.697 13.662  1.00 39.72 ? 546 HOH A O   1 
HETATM 4383 O O   . HOH AA 5 .   ? 4.850   -3.162  38.119  1.00 39.55 ? 547 HOH A O   1 
HETATM 4384 O O   . HOH AA 5 .   ? -8.075  -10.737 15.082  1.00 17.35 ? 548 HOH A O   1 
HETATM 4385 O O   . HOH AA 5 .   ? 6.450   -0.580  29.267  1.00 34.57 ? 549 HOH A O   1 
HETATM 4386 O O   . HOH AA 5 .   ? -7.364  -26.845 33.526  1.00 34.48 ? 550 HOH A O   1 
HETATM 4387 O O   . HOH AA 5 .   ? 6.385   8.944   10.879  1.00 44.33 ? 551 HOH A O   1 
HETATM 4388 O O   . HOH AA 5 .   ? -5.980  -2.687  41.948  1.00 32.72 ? 552 HOH A O   1 
HETATM 4389 O O   . HOH AA 5 .   ? -1.272  -16.658 38.494  1.00 40.29 ? 553 HOH A O   1 
HETATM 4390 O O   . HOH AA 5 .   ? -12.718 -4.960  32.902  1.00 33.96 ? 554 HOH A O   1 
HETATM 4391 O O   . HOH AA 5 .   ? -2.452  -12.515 7.287   1.00 30.01 ? 555 HOH A O   1 
HETATM 4392 O O   . HOH AA 5 .   ? -16.171 6.474   7.944   1.00 34.45 ? 556 HOH A O   1 
HETATM 4393 O O   . HOH AA 5 .   ? -7.536  9.377   13.399  1.00 33.20 ? 557 HOH A O   1 
HETATM 4394 O O   . HOH AA 5 .   ? 0.820   1.836   40.123  1.00 43.03 ? 558 HOH A O   1 
HETATM 4395 O O   . HOH AA 5 .   ? -8.793  10.618  38.133  1.00 32.37 ? 559 HOH A O   1 
HETATM 4396 O O   . HOH AA 5 .   ? 7.520   7.492   8.930   1.00 43.69 ? 560 HOH A O   1 
HETATM 4397 O O   . HOH AA 5 .   ? -0.124  -15.673 33.782  1.00 23.06 ? 561 HOH A O   1 
HETATM 4398 O O   . HOH AA 5 .   ? 5.788   2.827   31.180  1.00 35.06 ? 562 HOH A O   1 
HETATM 4399 O O   . HOH AA 5 .   ? -17.562 -2.308  33.789  1.00 54.26 ? 563 HOH A O   1 
HETATM 4400 O O   . HOH AA 5 .   ? -15.844 -10.221 32.620  1.00 35.23 ? 564 HOH A O   1 
HETATM 4401 O O   . HOH AA 5 .   ? -5.855  -3.159  19.987  1.00 33.99 ? 565 HOH A O   1 
HETATM 4402 O O   . HOH AA 5 .   ? -5.326  9.370   33.185  1.00 30.85 ? 566 HOH A O   1 
HETATM 4403 O O   . HOH AA 5 .   ? -9.443  -16.780 15.543  1.00 32.42 ? 567 HOH A O   1 
HETATM 4404 O O   . HOH AA 5 .   ? -5.917  -27.662 3.651   1.00 35.18 ? 568 HOH A O   1 
HETATM 4405 O O   . HOH AA 5 .   ? 6.154   -5.164  -8.381  1.00 42.86 ? 569 HOH A O   1 
HETATM 4406 O O   . HOH AA 5 .   ? -2.250  10.135  13.770  1.00 40.26 ? 570 HOH A O   1 
HETATM 4407 O O   . HOH AA 5 .   ? 5.273   -9.808  42.626  1.00 39.01 ? 571 HOH A O   1 
HETATM 4408 O O   . HOH AA 5 .   ? 12.058  -14.387 25.177  1.00 45.36 ? 572 HOH A O   1 
HETATM 4409 O O   . HOH AA 5 .   ? -10.868 4.059   10.463  1.00 30.91 ? 573 HOH A O   1 
HETATM 4410 O O   . HOH AA 5 .   ? 7.109   -14.973 32.697  1.00 41.85 ? 574 HOH A O   1 
HETATM 4411 O O   . HOH AA 5 .   ? -0.787  -23.679 35.159  1.00 34.87 ? 575 HOH A O   1 
HETATM 4412 O O   . HOH AA 5 .   ? -10.531 -14.481 14.608  1.00 30.28 ? 576 HOH A O   1 
HETATM 4413 O O   . HOH AA 5 .   ? -7.238  11.792  17.038  1.00 31.67 ? 577 HOH A O   1 
HETATM 4414 O O   . HOH AA 5 .   ? -9.832  13.221  13.211  1.00 42.76 ? 578 HOH A O   1 
HETATM 4415 O O   . HOH AA 5 .   ? 0.927   -3.171  8.767   1.00 15.38 ? 579 HOH A O   1 
HETATM 4416 O O   . HOH AA 5 .   ? -9.423  -2.789  10.488  1.00 39.36 ? 580 HOH A O   1 
HETATM 4417 O O   . HOH AA 5 .   ? -8.209  -4.259  13.029  1.00 22.26 ? 581 HOH A O   1 
HETATM 4418 O O   . HOH AA 5 .   ? -9.505  5.680   7.001   1.00 31.13 ? 582 HOH A O   1 
HETATM 4419 O O   . HOH AA 5 .   ? -17.508 -17.703 22.301  1.00 38.93 ? 583 HOH A O   1 
HETATM 4420 O O   . HOH AA 5 .   ? 5.882   7.330   23.546  1.00 41.37 ? 584 HOH A O   1 
HETATM 4421 O O   . HOH AA 5 .   ? -7.511  4.585   5.372   1.00 25.77 ? 585 HOH A O   1 
HETATM 4422 O O   . HOH AA 5 .   ? -14.989 -8.898  18.797  1.00 42.08 ? 586 HOH A O   1 
HETATM 4423 O O   . HOH AA 5 .   ? 13.585  -7.951  15.848  1.00 54.11 ? 587 HOH A O   1 
HETATM 4424 O O   . HOH AA 5 .   ? 4.010   10.210  3.677   1.00 33.53 ? 588 HOH A O   1 
HETATM 4425 O O   . HOH AA 5 .   ? -10.438 -11.766 15.457  1.00 27.74 ? 589 HOH A O   1 
HETATM 4426 O O   . HOH AA 5 .   ? 14.054  1.377   -0.918  1.00 40.55 ? 590 HOH A O   1 
HETATM 4427 O O   . HOH AA 5 .   ? -4.917  9.256   14.487  1.00 31.33 ? 591 HOH A O   1 
HETATM 4428 O O   . HOH AA 5 .   ? -1.331  -16.222 31.260  1.00 35.86 ? 592 HOH A O   1 
HETATM 4429 O O   . HOH AA 5 .   ? -16.263 4.073   6.545   1.00 35.81 ? 593 HOH A O   1 
HETATM 4430 O O   . HOH AA 5 .   ? 4.550   -9.612  11.268  1.00 26.92 ? 594 HOH A O   1 
HETATM 4431 O O   . HOH AA 5 .   ? 5.737   -8.768  6.701   1.00 41.69 ? 595 HOH A O   1 
HETATM 4432 O O   . HOH AA 5 .   ? 1.687   -8.035  9.074   1.00 23.62 ? 596 HOH A O   1 
HETATM 4433 O O   . HOH AA 5 .   ? 11.250  -3.031  3.965   1.00 44.31 ? 597 HOH A O   1 
HETATM 4434 O O   . HOH AA 5 .   ? -13.071 -11.145 18.701  1.00 37.73 ? 598 HOH A O   1 
HETATM 4435 O O   . HOH AA 5 .   ? 2.800   -18.759 30.493  1.00 27.70 ? 599 HOH A O   1 
HETATM 4436 O O   . HOH AA 5 .   ? -14.141 4.986   5.535   1.00 33.62 ? 600 HOH A O   1 
HETATM 4437 O O   . HOH AA 5 .   ? -0.226  -11.412 5.574   1.00 44.75 ? 601 HOH A O   1 
HETATM 4438 O O   . HOH AA 5 .   ? -1.406  -10.861 3.149   1.00 47.96 ? 602 HOH A O   1 
HETATM 4439 O O   . HOH AA 5 .   ? 3.860   10.399  0.807   1.00 47.64 ? 603 HOH A O   1 
HETATM 4440 O O   . HOH AA 5 .   ? 4.410   -15.688 11.252  1.00 36.95 ? 604 HOH A O   1 
HETATM 4441 O O   . HOH AA 5 .   ? -7.397  14.481  17.169  1.00 39.06 ? 605 HOH A O   1 
HETATM 4442 O O   . HOH AA 5 .   ? 2.449   -8.571  5.135   1.00 43.38 ? 606 HOH A O   1 
HETATM 4443 O O   . HOH AA 5 .   ? 1.568   -10.007 7.057   1.00 37.21 ? 607 HOH A O   1 
HETATM 4444 O O   . HOH AA 5 .   ? -14.318 -13.606 17.990  1.00 26.95 ? 608 HOH A O   1 
HETATM 4445 O O   . HOH AA 5 .   ? 3.102   -18.916 33.373  1.00 43.50 ? 609 HOH A O   1 
HETATM 4446 O O   . HOH AA 5 .   ? -10.832 17.034  16.017  1.00 40.34 ? 610 HOH A O   1 
HETATM 4447 O O   . HOH AA 5 .   ? -8.637  16.048  14.696  1.00 38.57 ? 611 HOH A O   1 
HETATM 4448 O O   . HOH AA 5 .   ? -16.957 -12.902 17.474  1.00 47.38 ? 612 HOH A 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   . ASP A 5   ? 0.3875 0.8454 0.7707 -0.1709 0.0887  0.0891  2   ASP B N   
2    C CA  . ASP A 5   ? 0.4069 0.8869 0.7803 -0.1617 0.1036  0.0856  2   ASP B CA  
3    C C   . ASP A 5   ? 0.3678 0.8140 0.7182 -0.1383 0.0983  0.0802  2   ASP B C   
4    O O   . ASP A 5   ? 0.3418 0.7726 0.6972 -0.1222 0.0868  0.0712  2   ASP B O   
5    C CB  . ASP A 5   ? 0.4508 0.9880 0.8543 -0.1564 0.1133  0.0721  2   ASP B CB  
6    C CG  . ASP A 5   ? 0.4898 1.0500 0.8861 -0.1415 0.1269  0.0629  2   ASP B CG  
7    O OD1 . ASP A 5   ? 0.4211 0.9777 0.8199 -0.1169 0.1223  0.0491  2   ASP B OD1 
8    O OD2 . ASP A 5   ? 0.5850 1.1664 0.9727 -0.1551 0.1417  0.0695  2   ASP B OD2 
9    N N   . LYS A 6   ? 0.3832 0.8220 0.7091 -0.1367 0.1073  0.0852  3   LYS B N   
10   C CA  . LYS A 6   ? 0.3779 0.7813 0.6784 -0.1196 0.1024  0.0835  3   LYS B CA  
11   C C   . LYS A 6   ? 0.3512 0.7675 0.6599 -0.0957 0.1023  0.0661  3   LYS B C   
12   O O   . LYS A 6   ? 0.3044 0.6938 0.6083 -0.0808 0.0910  0.0608  3   LYS B O   
13   C CB  . LYS A 6   ? 0.4274 0.8229 0.7001 -0.1257 0.1116  0.0934  3   LYS B CB  
14   C CG  . LYS A 6   ? 0.4746 0.8241 0.7205 -0.1173 0.1026  0.0989  3   LYS B CG  
15   C CD  . LYS A 6   ? 0.5176 0.8632 0.7371 -0.1150 0.1104  0.1028  3   LYS B CD  
16   C CE  . LYS A 6   ? 0.5221 0.8783 0.7409 -0.0945 0.1138  0.0867  3   LYS B CE  
17   N NZ  . LYS A 6   ? 0.5413 0.9173 0.7451 -0.0953 0.1268  0.0853  3   LYS B NZ  
18   N N   . ASN A 7   ? 0.3338 0.7921 0.6553 -0.0927 0.1149  0.0571  4   ASN B N   
19   C CA  . ASN A 7   ? 0.3270 0.8001 0.6580 -0.0700 0.1157  0.0399  4   ASN B CA  
20   C C   . ASN A 7   ? 0.2805 0.7497 0.6327 -0.0585 0.1016  0.0317  4   ASN B C   
21   O O   . ASN A 7   ? 0.2624 0.7121 0.6089 -0.0395 0.0936  0.0237  4   ASN B O   
22   C CB  . ASN A 7   ? 0.3490 0.8709 0.6923 -0.0706 0.1323  0.0314  4   ASN B CB  
23   C CG  . ASN A 7   ? 0.3715 0.9068 0.7259 -0.0456 0.1320  0.0124  4   ASN B CG  
24   O OD1 . ASN A 7   ? 0.4006 0.9670 0.7853 -0.0386 0.1309  0.0018  4   ASN B OD1 
25   N ND2 . ASN A 7   ? 0.3828 0.8925 0.7137 -0.0318 0.1312  0.0080  4   ASN B ND2 
26   N N   . GLU A 8   ? 0.2589 0.7440 0.6334 -0.0714 0.0976  0.0350  5   GLU B N   
27   C CA  . GLU A 8   ? 0.2451 0.7263 0.6382 -0.0631 0.0830  0.0287  5   GLU B CA  
28   C C   . GLU A 8   ? 0.1984 0.6289 0.5704 -0.0571 0.0683  0.0330  5   GLU B C   
29   O O   . GLU A 8   ? 0.1731 0.5932 0.5483 -0.0407 0.0577  0.0249  5   GLU B O   
30   C CB  . GLU A 8   ? 0.2657 0.7760 0.6842 -0.0829 0.0837  0.0328  5   GLU B CB  
31   C CG  . GLU A 8   ? 0.2975 0.8033 0.7340 -0.0811 0.0676  0.0292  5   GLU B CG  
32   C CD  . GLU A 8   ? 0.3382 0.8847 0.8058 -0.0991 0.0700  0.0299  5   GLU B CD  
33   O OE1 . GLU A 8   ? 0.3458 0.9223 0.8211 -0.1171 0.0837  0.0354  5   GLU B OE1 
34   O OE2 . GLU A 8   ? 0.3688 0.9164 0.8529 -0.0942 0.0563  0.0242  5   GLU B OE2 
35   N N   . LEU A 9   ? 0.1848 0.5855 0.5377 -0.0715 0.0667  0.0459  6   LEU B N   
36   C CA  . LEU A 9   ? 0.1682 0.5235 0.5005 -0.0662 0.0549  0.0494  6   LEU B CA  
37   C C   . LEU A 9   ? 0.1517 0.4885 0.4648 -0.0470 0.0546  0.0439  6   LEU B C   
38   O O   . LEU A 9   ? 0.1308 0.4430 0.4365 -0.0361 0.0436  0.0405  6   LEU B O   
39   C CB  . LEU A 9   ? 0.1963 0.5262 0.5117 -0.0833 0.0554  0.0636  6   LEU B CB  
40   C CG  . LEU A 9   ? 0.2211 0.5539 0.5507 -0.1029 0.0509  0.0700  6   LEU B CG  
41   C CD1 . LEU A 9   ? 0.2433 0.5534 0.5554 -0.1195 0.0536  0.0849  6   LEU B CD1 
42   C CD2 . LEU A 9   ? 0.2395 0.5515 0.5734 -0.0977 0.0355  0.0648  6   LEU B CD2 
43   N N   . VAL A 10  ? 0.1421 0.4904 0.4461 -0.0441 0.0665  0.0430  7   VAL B N   
44   C CA  . VAL A 10  ? 0.1439 0.4757 0.4301 -0.0275 0.0664  0.0373  7   VAL B CA  
45   C C   . VAL A 10  ? 0.1379 0.4800 0.4391 -0.0095 0.0605  0.0240  7   VAL B C   
46   O O   . VAL A 10  ? 0.1321 0.4476 0.4206 0.0023  0.0519  0.0213  7   VAL B O   
47   C CB  . VAL A 10  ? 0.1509 0.4932 0.4231 -0.0300 0.0800  0.0388  7   VAL B CB  
48   C CG1 . VAL A 10  ? 0.1435 0.4760 0.4020 -0.0126 0.0808  0.0295  7   VAL B CG1 
49   C CG2 . VAL A 10  ? 0.1644 0.4852 0.4161 -0.0450 0.0815  0.0537  7   VAL B CG2 
50   N N   . GLN A 11  ? 0.1529 0.5333 0.4804 -0.0079 0.0647  0.0162  8   GLN B N   
51   C CA  . GLN A 11  ? 0.1556 0.5469 0.5009 0.0097  0.0570  0.0041  8   GLN B CA  
52   C C   . GLN A 11  ? 0.1461 0.5152 0.4930 0.0121  0.0404  0.0060  8   GLN B C   
53   O O   . GLN A 11  ? 0.1345 0.4860 0.4755 0.0276  0.0310  0.0007  8   GLN B O   
54   C CB  . GLN A 11  ? 0.2018 0.6422 0.5780 0.0118  0.0645  -0.0053 8   GLN B CB  
55   C CG  . GLN A 11  ? 0.2378 0.7035 0.6123 0.0132  0.0812  -0.0109 8   GLN B CG  
56   C CD  . GLN A 11  ? 0.2796 0.7219 0.6322 0.0294  0.0819  -0.0173 8   GLN B CD  
57   O OE1 . GLN A 11  ? 0.3609 0.7993 0.7200 0.0488  0.0748  -0.0283 8   GLN B OE1 
58   N NE2 . GLN A 11  ? 0.2743 0.6980 0.5998 0.0214  0.0889  -0.0099 8   GLN B NE2 
59   N N   . LYS A 12  ? 0.1604 0.5264 0.5117 -0.0037 0.0363  0.0138  9   LYS B N   
60   C CA  . LYS A 12  ? 0.1774 0.5235 0.5286 -0.0025 0.0209  0.0145  9   LYS B CA  
61   C C   . LYS A 12  ? 0.1622 0.4652 0.4832 0.0033  0.0152  0.0183  9   LYS B C   
62   O O   . LYS A 12  ? 0.1222 0.4097 0.4391 0.0128  0.0034  0.0151  9   LYS B O   
63   C CB  . LYS A 12  ? 0.2331 0.5869 0.5968 -0.0213 0.0182  0.0203  9   LYS B CB  
64   C CG  . LYS A 12  ? 0.3336 0.6676 0.6963 -0.0239 0.0027  0.0209  9   LYS B CG  
65   C CD  . LYS A 12  ? 0.4508 0.8052 0.8375 -0.0212 -0.0091 0.0142  9   LYS B CD  
66   C CE  . LYS A 12  ? 0.5492 0.8847 0.9324 -0.0324 -0.0210 0.0169  9   LYS B CE  
67   N NZ  . LYS A 12  ? 0.6360 0.9289 0.9904 -0.0318 -0.0269 0.0205  9   LYS B NZ  
68   N N   . ALA A 13  ? 0.1348 0.4208 0.4353 -0.0032 0.0232  0.0253  10  ALA B N   
69   C CA  . ALA A 13  ? 0.1380 0.3886 0.4119 0.0020  0.0196  0.0283  10  ALA B CA  
70   C C   . ALA A 13  ? 0.1266 0.3702 0.3931 0.0192  0.0169  0.0212  10  ALA B C   
71   O O   . ALA A 13  ? 0.1225 0.3413 0.3752 0.0249  0.0080  0.0214  10  ALA B O   
72   C CB  . ALA A 13  ? 0.1485 0.3876 0.4052 -0.0069 0.0284  0.0365  10  ALA B CB  
73   N N   . LYS A 14  ? 0.1273 0.3920 0.4025 0.0267  0.0244  0.0147  11  LYS B N   
74   C CA  . LYS A 14  ? 0.1298 0.3865 0.3993 0.0433  0.0212  0.0071  11  LYS B CA  
75   C C   . LYS A 14  ? 0.1288 0.3832 0.4091 0.0538  0.0072  0.0025  11  LYS B C   
76   O O   . LYS A 14  ? 0.1312 0.3616 0.3975 0.0636  -0.0012 0.0014  11  LYS B O   
77   C CB  . LYS A 14  ? 0.1435 0.4274 0.4239 0.0491  0.0323  -0.0008 11  LYS B CB  
78   C CG  . LYS A 14  ? 0.1529 0.4360 0.4168 0.0421  0.0452  0.0024  11  LYS B CG  
79   C CD  . LYS A 14  ? 0.1788 0.4926 0.4556 0.0492  0.0554  -0.0081 11  LYS B CD  
80   C CE  . LYS A 14  ? 0.2185 0.5282 0.4757 0.0479  0.0658  -0.0086 11  LYS B CE  
81   N NZ  . LYS A 14  ? 0.2538 0.5969 0.5254 0.0551  0.0761  -0.0208 11  LYS B NZ  
82   N N   . LEU A 15  ? 0.1209 0.4015 0.4263 0.0507  0.0043  0.0003  12  LEU B N   
83   C CA  . LEU A 15  ? 0.1222 0.4045 0.4397 0.0592  -0.0101 -0.0034 12  LEU B CA  
84   C C   . LEU A 15  ? 0.1121 0.3630 0.4103 0.0548  -0.0212 0.0029  12  LEU B C   
85   O O   . LEU A 15  ? 0.1127 0.3460 0.4018 0.0654  -0.0324 0.0017  12  LEU B O   
86   C CB  . LEU A 15  ? 0.1322 0.4520 0.4811 0.0535  -0.0101 -0.0064 12  LEU B CB  
87   C CG  . LEU A 15  ? 0.1635 0.4973 0.5327 0.0656  -0.0238 -0.0129 12  LEU B CG  
88   C CD1 . LEU A 15  ? 0.1866 0.5246 0.5615 0.0859  -0.0255 -0.0216 12  LEU B CD1 
89   C CD2 . LEU A 15  ? 0.1529 0.5286 0.5544 0.0564  -0.0210 -0.0156 12  LEU B CD2 
90   N N   . ALA A 16  ? 0.0983 0.3413 0.3887 0.0395  -0.0177 0.0097  13  ALA B N   
91   C CA  . ALA A 16  ? 0.1022 0.3172 0.3737 0.0349  -0.0259 0.0142  13  ALA B CA  
92   C C   . ALA A 16  ? 0.1150 0.3011 0.3601 0.0428  -0.0269 0.0158  13  ALA B C   
93   O O   . ALA A 16  ? 0.1287 0.2963 0.3608 0.0461  -0.0371 0.0165  13  ALA B O   
94   C CB  . ALA A 16  ? 0.0986 0.3088 0.3664 0.0192  -0.0203 0.0201  13  ALA B CB  
95   N N   . GLU A 17  ? 0.1146 0.2976 0.3508 0.0440  -0.0163 0.0166  14  GLU B N   
96   C CA  . GLU A 17  ? 0.1237 0.2811 0.3361 0.0498  -0.0169 0.0180  14  GLU B CA  
97   C C   . GLU A 17  ? 0.1410 0.2913 0.3526 0.0630  -0.0273 0.0139  14  GLU B C   
98   O O   . GLU A 17  ? 0.1464 0.2734 0.3393 0.0646  -0.0345 0.0167  14  GLU B O   
99   C CB  . GLU A 17  ? 0.1326 0.2915 0.3383 0.0503  -0.0052 0.0177  14  GLU B CB  
100  C CG  . GLU A 17  ? 0.1450 0.2777 0.3264 0.0539  -0.0062 0.0194  14  GLU B CG  
101  C CD  . GLU A 17  ? 0.1689 0.3006 0.3404 0.0528  0.0041  0.0193  14  GLU B CD  
102  O OE1 . GLU A 17  ? 0.1742 0.3263 0.3565 0.0511  0.0128  0.0172  14  GLU B OE1 
103  O OE2 . GLU A 17  ? 0.1737 0.2850 0.3259 0.0526  0.0031  0.0217  14  GLU B OE2 
104  N N   . GLN A 18  ? 0.1589 0.3286 0.3896 0.0723  -0.0279 0.0075  15  GLN B N   
105  C CA  . GLN A 18  ? 0.1857 0.3480 0.4179 0.0862  -0.0396 0.0038  15  GLN B CA  
106  C C   . GLN A 18  ? 0.1753 0.3293 0.4051 0.0856  -0.0542 0.0070  15  GLN B C   
107  O O   . GLN A 18  ? 0.1946 0.3263 0.4089 0.0922  -0.0643 0.0090  15  GLN B O   
108  C CB  . GLN A 18  ? 0.2306 0.4194 0.4885 0.0978  -0.0386 -0.0051 15  GLN B CB  
109  C CG  . GLN A 18  ? 0.3253 0.5075 0.5775 0.1083  -0.0327 -0.0110 15  GLN B CG  
110  C CD  . GLN A 18  ? 0.4041 0.6096 0.6646 0.1032  -0.0163 -0.0147 15  GLN B CD  
111  O OE1 . GLN A 18  ? 0.5966 0.7889 0.8383 0.0973  -0.0077 -0.0121 15  GLN B OE1 
112  N NE2 . GLN A 18  ? 0.3788 0.6203 0.6675 0.1058  -0.0123 -0.0212 15  GLN B NE2 
113  N N   . ALA A 19  ? 0.1459 0.3164 0.3889 0.0766  -0.0555 0.0077  16  ALA B N   
114  C CA  . ALA A 19  ? 0.1528 0.3170 0.3922 0.0738  -0.0687 0.0099  16  ALA B CA  
115  C C   . ALA A 19  ? 0.1558 0.2927 0.3668 0.0654  -0.0697 0.0157  16  ALA B C   
116  O O   . ALA A 19  ? 0.1533 0.2837 0.3576 0.0635  -0.0807 0.0168  16  ALA B O   
117  C CB  . ALA A 19  ? 0.1375 0.3288 0.4012 0.0659  -0.0694 0.0076  16  ALA B CB  
118  N N   . GLU A 20  ? 0.1582 0.2826 0.3543 0.0606  -0.0586 0.0184  17  GLU B N   
119  C CA  . GLU A 20  ? 0.1760 0.2802 0.3492 0.0525  -0.0566 0.0226  17  GLU B CA  
120  C C   . GLU A 20  ? 0.1714 0.2816 0.3504 0.0426  -0.0583 0.0221  17  GLU B C   
121  O O   . GLU A 20  ? 0.1798 0.2768 0.3436 0.0390  -0.0638 0.0228  17  GLU B O   
122  C CB  . GLU A 20  ? 0.2381 0.3199 0.3886 0.0574  -0.0651 0.0253  17  GLU B CB  
123  C CG  . GLU A 20  ? 0.2690 0.3412 0.4138 0.0664  -0.0642 0.0256  17  GLU B CG  
124  C CD  . GLU A 20  ? 0.3176 0.3651 0.4378 0.0680  -0.0727 0.0302  17  GLU B CD  
125  O OE1 . GLU A 20  ? 0.4052 0.4400 0.5063 0.0607  -0.0687 0.0336  17  GLU B OE1 
126  O OE2 . GLU A 20  ? 0.4480 0.4911 0.5690 0.0756  -0.0844 0.0306  17  GLU B OE2 
127  N N   . ARG A 21  ? 0.1470 0.2783 0.3487 0.0378  -0.0544 0.0202  18  ARG B N   
128  C CA  . ARG A 21  ? 0.1473 0.2830 0.3562 0.0269  -0.0558 0.0197  18  ARG B CA  
129  C C   . ARG A 21  ? 0.1414 0.2723 0.3470 0.0189  -0.0440 0.0231  18  ARG B C   
130  O O   . ARG A 21  ? 0.1177 0.2642 0.3392 0.0132  -0.0371 0.0243  18  ARG B O   
131  C CB  . ARG A 21  ? 0.1591 0.3211 0.3951 0.0262  -0.0609 0.0162  18  ARG B CB  
132  C CG  . ARG A 21  ? 0.1612 0.3221 0.3955 0.0324  -0.0761 0.0136  18  ARG B CG  
133  C CD  . ARG A 21  ? 0.1672 0.3539 0.4276 0.0314  -0.0828 0.0098  18  ARG B CD  
134  N NE  . ARG A 21  ? 0.1538 0.3500 0.4266 0.0172  -0.0819 0.0088  18  ARG B NE  
135  C CZ  . ARG A 21  ? 0.1490 0.3475 0.4255 0.0109  -0.0928 0.0059  18  ARG B CZ  
136  N NH1 . ARG A 21  ? 0.1548 0.3446 0.4192 0.0168  -0.1061 0.0042  18  ARG B NH1 
137  N NH2 . ARG A 21  ? 0.1432 0.3507 0.4335 -0.0025 -0.0906 0.0051  18  ARG B NH2 
138  N N   . TYR A 22  ? 0.1394 0.2490 0.3234 0.0183  -0.0420 0.0251  19  TYR B N   
139  C CA  . TYR A 22  ? 0.1519 0.2554 0.3305 0.0140  -0.0317 0.0291  19  TYR B CA  
140  C C   . TYR A 22  ? 0.1380 0.2408 0.3244 0.0034  -0.0308 0.0303  19  TYR B C   
141  O O   . TYR A 22  ? 0.1387 0.2423 0.3271 -0.0012 -0.0228 0.0348  19  TYR B O   
142  C CB  . TYR A 22  ? 0.1531 0.2375 0.3090 0.0173  -0.0298 0.0305  19  TYR B CB  
143  C CG  . TYR A 22  ? 0.1798 0.2627 0.3279 0.0257  -0.0299 0.0306  19  TYR B CG  
144  C CD1 . TYR A 22  ? 0.1836 0.2746 0.3367 0.0288  -0.0226 0.0316  19  TYR B CD1 
145  C CD2 . TYR A 22  ? 0.1745 0.2466 0.3087 0.0301  -0.0377 0.0295  19  TYR B CD2 
146  C CE1 . TYR A 22  ? 0.2015 0.2873 0.3466 0.0367  -0.0235 0.0307  19  TYR B CE1 
147  C CE2 . TYR A 22  ? 0.1872 0.2537 0.3132 0.0369  -0.0389 0.0304  19  TYR B CE2 
148  C CZ  . TYR A 22  ? 0.2147 0.2872 0.3469 0.0406  -0.0322 0.0305  19  TYR B CZ  
149  O OH  . TYR A 22  ? 0.2505 0.3138 0.3736 0.0471  -0.0345 0.0306  19  TYR B OH  
150  N N   . ASP A 23  ? 0.1437 0.2434 0.3332 -0.0009 -0.0392 0.0266  20  ASP B N   
151  C CA  . ASP A 23  ? 0.1603 0.2581 0.3592 -0.0117 -0.0396 0.0274  20  ASP B CA  
152  C C   . ASP A 23  ? 0.1594 0.2791 0.3799 -0.0186 -0.0351 0.0305  20  ASP B C   
153  O O   . ASP A 23  ? 0.1631 0.2809 0.3871 -0.0271 -0.0294 0.0358  20  ASP B O   
154  C CB  . ASP A 23  ? 0.1849 0.2756 0.3827 -0.0151 -0.0503 0.0212  20  ASP B CB  
155  C CG  . ASP A 23  ? 0.2150 0.2855 0.3913 -0.0106 -0.0535 0.0171  20  ASP B CG  
156  O OD1 . ASP A 23  ? 0.2175 0.2759 0.3826 -0.0083 -0.0471 0.0195  20  ASP B OD1 
157  O OD2 . ASP A 23  ? 0.2393 0.3074 0.4117 -0.0111 -0.0628 0.0109  20  ASP B OD2 
158  N N   . ASP A 24  ? 0.1532 0.2943 0.3879 -0.0147 -0.0381 0.0275  21  ASP B N   
159  C CA  . ASP A 24  ? 0.1374 0.3057 0.3945 -0.0198 -0.0327 0.0290  21  ASP B CA  
160  C C   . ASP A 24  ? 0.1345 0.3067 0.3873 -0.0185 -0.0198 0.0341  21  ASP B C   
161  O O   . ASP A 24  ? 0.1525 0.3353 0.4144 -0.0288 -0.0127 0.0389  21  ASP B O   
162  C CB  . ASP A 24  ? 0.1296 0.3207 0.4025 -0.0120 -0.0383 0.0235  21  ASP B CB  
163  C CG  . ASP A 24  ? 0.1378 0.3333 0.4197 -0.0146 -0.0518 0.0185  21  ASP B CG  
164  O OD1 . ASP A 24  ? 0.1562 0.3381 0.4341 -0.0248 -0.0562 0.0185  21  ASP B OD1 
165  O OD2 . ASP A 24  ? 0.1231 0.3340 0.4152 -0.0060 -0.0583 0.0145  21  ASP B OD2 
166  N N   . MET A 25  ? 0.1207 0.2831 0.3580 -0.0074 -0.0173 0.0335  22  MET B N   
167  C CA  . MET A 25  ? 0.1285 0.2939 0.3596 -0.0056 -0.0063 0.0371  22  MET B CA  
168  C C   . MET A 25  ? 0.1198 0.2714 0.3416 -0.0155 -0.0012 0.0446  22  MET B C   
169  O O   . MET A 25  ? 0.1243 0.2875 0.3499 -0.0216 0.0075  0.0494  22  MET B O   
170  C CB  . MET A 25  ? 0.1303 0.2823 0.3442 0.0066  -0.0068 0.0349  22  MET B CB  
171  C CG  . MET A 25  ? 0.1302 0.2882 0.3392 0.0105  0.0030  0.0358  22  MET B CG  
172  S SD  . MET A 25  ? 0.1315 0.2684 0.3191 0.0221  -0.0004 0.0335  22  MET B SD  
173  C CE  . MET A 25  ? 0.1540 0.3006 0.3382 0.0235  0.0117  0.0339  22  MET B CE  
174  N N   . ALA A 26  ? 0.1268 0.2549 0.3366 -0.0168 -0.0069 0.0454  23  ALA B N   
175  C CA  . ALA A 26  ? 0.1360 0.2478 0.3373 -0.0238 -0.0045 0.0519  23  ALA B CA  
176  C C   . ALA A 26  ? 0.1483 0.2665 0.3634 -0.0380 -0.0040 0.0568  23  ALA B C   
177  O O   . ALA A 26  ? 0.1651 0.2807 0.3769 -0.0451 0.0019  0.0651  23  ALA B O   
178  C CB  . ALA A 26  ? 0.1427 0.2303 0.3302 -0.0198 -0.0112 0.0491  23  ALA B CB  
179  N N   . ALA A 27  ? 0.1481 0.2733 0.3774 -0.0431 -0.0108 0.0525  24  ALA B N   
180  C CA  . ALA A 27  ? 0.1653 0.2986 0.4096 -0.0584 -0.0109 0.0567  24  ALA B CA  
181  C C   . ALA A 27  ? 0.1657 0.3259 0.4205 -0.0645 0.0000  0.0622  24  ALA B C   
182  O O   . ALA A 27  ? 0.1806 0.3394 0.4363 -0.0776 0.0043  0.0711  24  ALA B O   
183  C CB  . ALA A 27  ? 0.1793 0.3193 0.4380 -0.0626 -0.0206 0.0499  24  ALA B CB  
184  N N   . CYS A 28  ? 0.1613 0.3443 0.4220 -0.0547 0.0045  0.0569  25  CYS B N   
185  C CA  . CYS A 28  ? 0.1565 0.3678 0.4265 -0.0584 0.0159  0.0595  25  CYS B CA  
186  C C   . CYS A 28  ? 0.1667 0.3672 0.4188 -0.0613 0.0245  0.0683  25  CYS B C   
187  O O   . CYS A 28  ? 0.1676 0.3793 0.4228 -0.0745 0.0317  0.0763  25  CYS B O   
188  C CB  . CYS A 28  ? 0.1479 0.3815 0.4261 -0.0443 0.0181  0.0504  25  CYS B CB  
189  S SG  . CYS A 28  ? 0.1643 0.4216 0.4690 -0.0419 0.0089  0.0413  25  CYS B SG  
190  N N   . MET A 29  ? 0.1599 0.3390 0.3928 -0.0502 0.0230  0.0676  26  MET B N   
191  C CA  . MET A 29  ? 0.1699 0.3403 0.3855 -0.0510 0.0299  0.0749  26  MET B CA  
192  C C   . MET A 29  ? 0.1851 0.3334 0.3923 -0.0621 0.0272  0.0856  26  MET B C   
193  O O   . MET A 29  ? 0.1831 0.3327 0.3816 -0.0687 0.0335  0.0945  26  MET B O   
194  C CB  . MET A 29  ? 0.1639 0.3222 0.3636 -0.0365 0.0292  0.0702  26  MET B CB  
195  C CG  . MET A 29  ? 0.1649 0.3424 0.3704 -0.0257 0.0325  0.0610  26  MET B CG  
196  S SD  . MET A 29  ? 0.1709 0.3849 0.3896 -0.0308 0.0449  0.0602  26  MET B SD  
197  C CE  . MET A 29  ? 0.1777 0.3864 0.3760 -0.0380 0.0539  0.0702  26  MET B CE  
198  N N   . LYS A 30  ? 0.2036 0.3320 0.4131 -0.0642 0.0175  0.0846  27  LYS B N   
199  C CA  . LYS A 30  ? 0.2288 0.3352 0.4340 -0.0753 0.0134  0.0938  27  LYS B CA  
200  C C   . LYS A 30  ? 0.2485 0.3709 0.4651 -0.0933 0.0182  0.1023  27  LYS B C   
201  O O   . LYS A 30  ? 0.2499 0.3634 0.4574 -0.1027 0.0209  0.1142  27  LYS B O   
202  C CB  . LYS A 30  ? 0.2574 0.3418 0.4646 -0.0730 0.0020  0.0876  27  LYS B CB  
203  C CG  . LYS A 30  ? 0.2996 0.3563 0.5042 -0.0826 -0.0050 0.0940  27  LYS B CG  
204  C CD  . LYS A 30  ? 0.3293 0.3652 0.5331 -0.0763 -0.0156 0.0840  27  LYS B CD  
205  C CE  . LYS A 30  ? 0.3854 0.3880 0.5825 -0.0791 -0.0231 0.0874  27  LYS B CE  
206  N NZ  . LYS A 30  ? 0.4106 0.4071 0.6176 -0.0963 -0.0269 0.0931  27  LYS B NZ  
207  N N   . SER A 31  ? 0.2362 0.3846 0.4722 -0.0980 0.0195  0.0965  28  SER B N   
208  C CA  . SER A 31  ? 0.2622 0.4320 0.5115 -0.1162 0.0252  0.1037  28  SER B CA  
209  C C   . SER A 31  ? 0.2533 0.4431 0.4954 -0.1198 0.0382  0.1108  28  SER B C   
210  O O   . SER A 31  ? 0.2642 0.4517 0.5020 -0.1359 0.0417  0.1234  28  SER B O   
211  C CB  . SER A 31  ? 0.2737 0.4714 0.5470 -0.1185 0.0237  0.0947  28  SER B CB  
212  O OG  . SER A 31  ? 0.3156 0.4920 0.5932 -0.1209 0.0111  0.0909  28  SER B OG  
213  N N   . VAL A 32  ? 0.2288 0.4334 0.4666 -0.1049 0.0442  0.1031  29  VAL B N   
214  C CA  . VAL A 32  ? 0.2279 0.4506 0.4562 -0.1057 0.0564  0.1071  29  VAL B CA  
215  C C   . VAL A 32  ? 0.2445 0.4403 0.4496 -0.1109 0.0556  0.1203  29  VAL B C   
216  O O   . VAL A 32  ? 0.2701 0.4749 0.4696 -0.1251 0.0625  0.1314  29  VAL B O   
217  C CB  . VAL A 32  ? 0.2173 0.4537 0.4435 -0.0872 0.0606  0.0948  29  VAL B CB  
218  C CG1 . VAL A 32  ? 0.2258 0.4757 0.4376 -0.0871 0.0722  0.0977  29  VAL B CG1 
219  C CG2 . VAL A 32  ? 0.2052 0.4706 0.4554 -0.0813 0.0612  0.0825  29  VAL B CG2 
220  N N   . THR A 33  ? 0.2446 0.4093 0.4370 -0.0999 0.0468  0.1194  30  THR B N   
221  C CA  . THR A 33  ? 0.2575 0.3958 0.4296 -0.1018 0.0438  0.1310  30  THR B CA  
222  C C   . THR A 33  ? 0.2816 0.4068 0.4536 -0.1205 0.0409  0.1454  30  THR B C   
223  O O   . THR A 33  ? 0.2969 0.4211 0.4552 -0.1299 0.0450  0.1583  30  THR B O   
224  C CB  . THR A 33  ? 0.2529 0.3630 0.4173 -0.0871 0.0340  0.1255  30  THR B CB  
225  O OG1 . THR A 33  ? 0.2248 0.3481 0.3872 -0.0727 0.0378  0.1144  30  THR B OG1 
226  C CG2 . THR A 33  ? 0.2612 0.3451 0.4080 -0.0874 0.0294  0.1366  30  THR B CG2 
227  N N   . GLU A 34  ? 0.2815 0.3977 0.4679 -0.1270 0.0336  0.1433  31  GLU B N   
228  C CA  . GLU A 34  ? 0.3248 0.4244 0.5127 -0.1455 0.0289  0.1558  31  GLU B CA  
229  C C   . GLU A 34  ? 0.3509 0.4774 0.5423 -0.1655 0.0393  0.1665  31  GLU B C   
230  O O   . GLU A 34  ? 0.3642 0.4742 0.5506 -0.1828 0.0363  0.1811  31  GLU B O   
231  C CB  . GLU A 34  ? 0.3434 0.4298 0.5467 -0.1475 0.0187  0.1482  31  GLU B CB  
232  C CG  . GLU A 34  ? 0.3522 0.4038 0.5476 -0.1327 0.0072  0.1419  31  GLU B CG  
233  C CD  . GLU A 34  ? 0.3537 0.3969 0.5619 -0.1299 -0.0019 0.1296  31  GLU B CD  
234  O OE1 . GLU A 34  ? 0.3363 0.4028 0.5615 -0.1364 -0.0004 0.1237  31  GLU B OE1 
235  O OE2 . GLU A 34  ? 0.3620 0.3758 0.5630 -0.1203 -0.0110 0.1251  31  GLU B OE2 
236  N N   . GLN A 35  ? 0.3472 0.5146 0.5475 -0.1643 0.0515  0.1596  32  GLN B N   
237  C CA  . GLN A 35  ? 0.3589 0.5562 0.5608 -0.1827 0.0635  0.1689  32  GLN B CA  
238  C C   . GLN A 35  ? 0.3738 0.5621 0.5496 -0.1873 0.0680  0.1832  32  GLN B C   
239  O O   . GLN A 35  ? 0.3938 0.5986 0.5655 -0.2063 0.0762  0.1952  32  GLN B O   
240  C CB  . GLN A 35  ? 0.3494 0.5942 0.5665 -0.1779 0.0761  0.1566  32  GLN B CB  
241  C CG  . GLN A 35  ? 0.3661 0.6269 0.6102 -0.1729 0.0721  0.1425  32  GLN B CG  
242  C CD  . GLN A 35  ? 0.4183 0.7295 0.6812 -0.1713 0.0845  0.1321  32  GLN B CD  
243  O OE1 . GLN A 35  ? 0.4691 0.8024 0.7232 -0.1700 0.0967  0.1323  32  GLN B OE1 
244  N NE2 . GLN A 35  ? 0.4085 0.7394 0.6979 -0.1715 0.0811  0.1226  32  GLN B NE2 
245  N N   . GLY A 36  ? 0.3691 0.5351 0.5276 -0.1708 0.0632  0.1816  33  GLY B N   
246  C CA  . GLY A 36  ? 0.4064 0.5536 0.5397 -0.1742 0.0620  0.1964  33  GLY B CA  
247  C C   . GLY A 36  ? 0.4091 0.5835 0.5284 -0.1702 0.0742  0.1947  33  GLY B C   
248  O O   . GLY A 36  ? 0.4872 0.6472 0.5841 -0.1711 0.0724  0.2058  33  GLY B O   
249  N N   . ALA A 37  ? 0.3598 0.5720 0.4918 -0.1653 0.0856  0.1806  34  ALA B N   
250  C CA  . ALA A 37  ? 0.3377 0.5746 0.4575 -0.1585 0.0966  0.1748  34  ALA B CA  
251  C C   . ALA A 37  ? 0.3167 0.5360 0.4281 -0.1364 0.0903  0.1643  34  ALA B C   
252  O O   . ALA A 37  ? 0.2646 0.4656 0.3866 -0.1244 0.0809  0.1561  34  ALA B O   
253  C CB  . ALA A 37  ? 0.3270 0.6093 0.4650 -0.1604 0.1102  0.1627  34  ALA B CB  
254  N N   . GLU A 38  ? 0.3196 0.5443 0.4100 -0.1326 0.0953  0.1652  35  GLU B N   
255  C CA  . GLU A 38  ? 0.3222 0.5353 0.4043 -0.1138 0.0909  0.1548  35  GLU B CA  
256  C C   . GLU A 38  ? 0.2948 0.5266 0.3946 -0.1002 0.0951  0.1351  35  GLU B C   
257  O O   . GLU A 38  ? 0.2948 0.5585 0.4062 -0.1042 0.1057  0.1285  35  GLU B O   
258  C CB  . GLU A 38  ? 0.3385 0.5588 0.3959 -0.1137 0.0962  0.1578  35  GLU B CB  
259  C CG  . GLU A 38  ? 0.3777 0.5721 0.4142 -0.1203 0.0876  0.1758  35  GLU B CG  
260  C CD  . GLU A 38  ? 0.3966 0.6030 0.4081 -0.1211 0.0932  0.1778  35  GLU B CD  
261  O OE1 . GLU A 38  ? 0.4049 0.6055 0.4097 -0.1073 0.0899  0.1682  35  GLU B OE1 
262  O OE2 . GLU A 38  ? 0.4320 0.6563 0.4315 -0.1359 0.1019  0.1870  35  GLU B OE2 
263  N N   . LEU A 39  ? 0.2749 0.4873 0.3766 -0.0848 0.0865  0.1264  36  LEU B N   
264  C CA  . LEU A 39  ? 0.2544 0.4772 0.3694 -0.0707 0.0876  0.1092  36  LEU B CA  
265  C C   . LEU A 39  ? 0.2637 0.4992 0.3661 -0.0621 0.0946  0.0997  36  LEU B C   
266  O O   . LEU A 39  ? 0.2645 0.4897 0.3463 -0.0621 0.0935  0.1047  36  LEU B O   
267  C CB  . LEU A 39  ? 0.2322 0.4284 0.3515 -0.0598 0.0756  0.1052  36  LEU B CB  
268  C CG  . LEU A 39  ? 0.2326 0.4115 0.3622 -0.0663 0.0671  0.1123  36  LEU B CG  
269  C CD1 . LEU A 39  ? 0.2135 0.3705 0.3453 -0.0537 0.0570  0.1053  36  LEU B CD1 
270  C CD2 . LEU A 39  ? 0.2259 0.4241 0.3760 -0.0756 0.0705  0.1114  36  LEU B CD2 
271  N N   . SER A 40  ? 0.2517 0.5094 0.3671 -0.0542 0.1008  0.0853  37  SER B N   
272  C CA  . SER A 40  ? 0.2369 0.4999 0.3439 -0.0417 0.1043  0.0720  37  SER B CA  
273  C C   . SER A 40  ? 0.2158 0.4508 0.3181 -0.0292 0.0935  0.0671  37  SER B C   
274  O O   . SER A 40  ? 0.1945 0.4105 0.3035 -0.0283 0.0842  0.0714  37  SER B O   
275  C CB  . SER A 40  ? 0.2348 0.5269 0.3598 -0.0352 0.1123  0.0574  37  SER B CB  
276  O OG  . SER A 40  ? 0.2121 0.4971 0.3565 -0.0254 0.1043  0.0504  37  SER B OG  
277  N N   . ASN A 41  ? 0.2323 0.4654 0.3226 -0.0200 0.0950  0.0573  38  ASN B N   
278  C CA  . ASN A 41  ? 0.2667 0.4758 0.3522 -0.0093 0.0857  0.0519  38  ASN B CA  
279  C C   . ASN A 41  ? 0.2162 0.4206 0.3208 -0.0009 0.0798  0.0452  38  ASN B C   
280  O O   . ASN A 41  ? 0.2172 0.4007 0.3216 0.0017  0.0707  0.0480  38  ASN B O   
281  C CB  . ASN A 41  ? 0.3233 0.5320 0.3940 -0.0021 0.0884  0.0414  38  ASN B CB  
282  C CG  . ASN A 41  ? 0.4470 0.6530 0.4952 -0.0095 0.0900  0.0486  38  ASN B CG  
283  O OD1 . ASN A 41  ? 0.5024 0.7077 0.5453 -0.0197 0.0895  0.0624  38  ASN B OD1 
284  N ND2 . ASN A 41  ? 0.5185 0.7223 0.5522 -0.0045 0.0911  0.0395  38  ASN B ND2 
285  N N   . GLU A 42  ? 0.2319 0.4578 0.3530 0.0033  0.0850  0.0362  39  GLU B N   
286  C CA  . GLU A 42  ? 0.2326 0.4576 0.3730 0.0111  0.0787  0.0303  39  GLU B CA  
287  C C   . GLU A 42  ? 0.1867 0.4039 0.3366 0.0034  0.0722  0.0402  39  GLU B C   
288  O O   . GLU A 42  ? 0.1703 0.3702 0.3231 0.0087  0.0629  0.0393  39  GLU B O   
289  C CB  . GLU A 42  ? 0.2617 0.5165 0.4200 0.0164  0.0860  0.0192  39  GLU B CB  
290  C CG  . GLU A 42  ? 0.3190 0.5729 0.4962 0.0278  0.0780  0.0113  39  GLU B CG  
291  C CD  . GLU A 42  ? 0.3500 0.6368 0.5486 0.0343  0.0847  -0.0002 39  GLU B CD  
292  O OE1 . GLU A 42  ? 0.3235 0.6393 0.5334 0.0244  0.0939  0.0024  39  GLU B OE1 
293  O OE2 . GLU A 42  ? 0.4401 0.7220 0.6438 0.0494  0.0798  -0.0115 39  GLU B OE2 
294  N N   . GLU A 43  ? 0.1583 0.3860 0.3104 -0.0098 0.0770  0.0499  40  GLU B N   
295  C CA  . GLU A 43  ? 0.1545 0.3739 0.3149 -0.0186 0.0712  0.0591  40  GLU B CA  
296  C C   . GLU A 43  ? 0.1573 0.3462 0.3034 -0.0184 0.0627  0.0659  40  GLU B C   
297  O O   . GLU A 43  ? 0.1471 0.3227 0.2999 -0.0175 0.0545  0.0665  40  GLU B O   
298  C CB  . GLU A 43  ? 0.1672 0.4050 0.3320 -0.0339 0.0789  0.0681  40  GLU B CB  
299  C CG  . GLU A 43  ? 0.1742 0.4473 0.3581 -0.0354 0.0876  0.0609  40  GLU B CG  
300  C CD  . GLU A 43  ? 0.2129 0.5092 0.3946 -0.0507 0.0991  0.0687  40  GLU B CD  
301  O OE1 . GLU A 43  ? 0.2235 0.5063 0.3882 -0.0619 0.0992  0.0821  40  GLU B OE1 
302  O OE2 . GLU A 43  ? 0.2071 0.5367 0.4044 -0.0513 0.1078  0.0613  40  GLU B OE2 
303  N N   . ARG A 44  ? 0.1604 0.3395 0.2872 -0.0184 0.0642  0.0697  41  ARG B N   
304  C CA  . ARG A 44  ? 0.1794 0.3335 0.2944 -0.0160 0.0564  0.0741  41  ARG B CA  
305  C C   . ARG A 44  ? 0.1592 0.3017 0.2765 -0.0054 0.0498  0.0654  41  ARG B C   
306  O O   . ARG A 44  ? 0.1638 0.2906 0.2820 -0.0045 0.0425  0.0674  41  ARG B O   
307  C CB  . ARG A 44  ? 0.2101 0.3584 0.3052 -0.0157 0.0580  0.0772  41  ARG B CB  
308  C CG  . ARG A 44  ? 0.2471 0.3944 0.3353 -0.0266 0.0591  0.0904  41  ARG B CG  
309  C CD  . ARG A 44  ? 0.2532 0.3957 0.3214 -0.0264 0.0591  0.0944  41  ARG B CD  
310  N NE  . ARG A 44  ? 0.2583 0.4200 0.3181 -0.0284 0.0683  0.0905  41  ARG B NE  
311  C CZ  . ARG A 44  ? 0.3034 0.4820 0.3612 -0.0380 0.0760  0.0961  41  ARG B CZ  
312  N NH1 . ARG A 44  ? 0.3116 0.4871 0.3733 -0.0483 0.0746  0.1084  41  ARG B NH1 
313  N NH2 . ARG A 44  ? 0.3038 0.5020 0.3541 -0.0384 0.0851  0.0897  41  ARG B NH2 
314  N N   . ASN A 45  ? 0.1658 0.3153 0.2828 0.0026  0.0522  0.0557  42  ASN B N   
315  C CA  . ASN A 45  ? 0.1422 0.2789 0.2591 0.0120  0.0454  0.0487  42  ASN B CA  
316  C C   . ASN A 45  ? 0.1291 0.2660 0.2615 0.0128  0.0396  0.0476  42  ASN B C   
317  O O   . ASN A 45  ? 0.1359 0.2570 0.2647 0.0159  0.0323  0.0471  42  ASN B O   
318  C CB  . ASN A 45  ? 0.1758 0.3167 0.2896 0.0204  0.0478  0.0389  42  ASN B CB  
319  C CG  . ASN A 45  ? 0.1945 0.3277 0.2895 0.0204  0.0499  0.0386  42  ASN B CG  
320  O OD1 . ASN A 45  ? 0.2049 0.3262 0.2891 0.0164  0.0471  0.0451  42  ASN B OD1 
321  N ND2 . ASN A 45  ? 0.2136 0.3559 0.3054 0.0246  0.0552  0.0306  42  ASN B ND2 
322  N N   . LEU A 46  ? 0.1206 0.2765 0.2695 0.0094  0.0428  0.0468  43  LEU B N   
323  C CA  . LEU A 46  ? 0.1237 0.2818 0.2882 0.0086  0.0366  0.0458  43  LEU B CA  
324  C C   . LEU A 46  ? 0.1339 0.2752 0.2947 0.0018  0.0311  0.0529  43  LEU B C   
325  O O   . LEU A 46  ? 0.1366 0.2671 0.2991 0.0046  0.0232  0.0506  43  LEU B O   
326  C CB  . LEU A 46  ? 0.1240 0.3093 0.3082 0.0047  0.0417  0.0438  43  LEU B CB  
327  C CG  . LEU A 46  ? 0.1178 0.3213 0.3101 0.0148  0.0457  0.0336  43  LEU B CG  
328  C CD1 . LEU A 46  ? 0.1312 0.3668 0.3415 0.0086  0.0543  0.0325  43  LEU B CD1 
329  C CD2 . LEU A 46  ? 0.1149 0.3121 0.3141 0.0265  0.0361  0.0262  43  LEU B CD2 
330  N N   . LEU A 47  ? 0.1403 0.2794 0.2959 -0.0071 0.0349  0.0614  44  LEU B N   
331  C CA  . LEU A 47  ? 0.1544 0.2752 0.3062 -0.0121 0.0293  0.0674  44  LEU B CA  
332  C C   . LEU A 47  ? 0.1394 0.2413 0.2785 -0.0045 0.0238  0.0650  44  LEU B C   
333  O O   . LEU A 47  ? 0.1205 0.2106 0.2611 -0.0038 0.0172  0.0634  44  LEU B O   
334  C CB  . LEU A 47  ? 0.1742 0.2939 0.3198 -0.0213 0.0336  0.0777  44  LEU B CB  
335  C CG  . LEU A 47  ? 0.1878 0.2866 0.3300 -0.0256 0.0272  0.0844  44  LEU B CG  
336  C CD1 . LEU A 47  ? 0.2377 0.3358 0.3945 -0.0331 0.0231  0.0847  44  LEU B CD1 
337  C CD2 . LEU A 47  ? 0.2143 0.3082 0.3453 -0.0313 0.0299  0.0951  44  LEU B CD2 
338  N N   . SER A 48  ? 0.1335 0.2341 0.2603 0.0002  0.0269  0.0641  45  SER B N   
339  C CA  . SER A 48  ? 0.1509 0.2373 0.2657 0.0056  0.0231  0.0623  45  SER B CA  
340  C C   . SER A 48  ? 0.1523 0.2336 0.2685 0.0113  0.0176  0.0554  45  SER B C   
341  O O   . SER A 48  ? 0.1545 0.2246 0.2664 0.0125  0.0127  0.0546  45  SER B O   
342  C CB  . SER A 48  ? 0.1613 0.2496 0.2638 0.0077  0.0273  0.0624  45  SER B CB  
343  O OG  . SER A 48  ? 0.1574 0.2342 0.2494 0.0112  0.0239  0.0612  45  SER B OG  
344  N N   . VAL A 49  ? 0.1229 0.2135 0.2451 0.0151  0.0182  0.0505  46  VAL B N   
345  C CA  . VAL A 49  ? 0.1289 0.2141 0.2514 0.0206  0.0117  0.0453  46  VAL B CA  
346  C C   . VAL A 49  ? 0.1243 0.2074 0.2551 0.0178  0.0057  0.0451  46  VAL B C   
347  O O   . VAL A 49  ? 0.1229 0.1955 0.2467 0.0201  -0.0002 0.0429  46  VAL B O   
348  C CB  . VAL A 49  ? 0.1302 0.2249 0.2587 0.0268  0.0125  0.0400  46  VAL B CB  
349  C CG1 . VAL A 49  ? 0.1331 0.2233 0.2650 0.0323  0.0038  0.0361  46  VAL B CG1 
350  C CG2 . VAL A 49  ? 0.1386 0.2289 0.2549 0.0306  0.0161  0.0381  46  VAL B CG2 
351  N N   . ALA A 50  ? 0.1333 0.2272 0.2782 0.0121  0.0072  0.0468  47  ALA B N   
352  C CA  . ALA A 50  ? 0.1442 0.2371 0.2984 0.0085  0.0010  0.0456  47  ALA B CA  
353  C C   . ALA A 50  ? 0.1402 0.2156 0.2844 0.0070  -0.0027 0.0464  47  ALA B C   
354  O O   . ALA A 50  ? 0.1404 0.2083 0.2803 0.0094  -0.0090 0.0421  47  ALA B O   
355  C CB  . ALA A 50  ? 0.1585 0.2654 0.3288 0.0002  0.0041  0.0485  47  ALA B CB  
356  N N   . TYR A 51  ? 0.1389 0.2080 0.2781 0.0038  0.0012  0.0515  48  TYR B N   
357  C CA  . TYR A 51  ? 0.1527 0.2064 0.2848 0.0040  -0.0022 0.0512  48  TYR B CA  
358  C C   . TYR A 51  ? 0.1631 0.2105 0.2815 0.0105  -0.0031 0.0475  48  TYR B C   
359  O O   . TYR A 51  ? 0.1747 0.2134 0.2890 0.0118  -0.0071 0.0435  48  TYR B O   
360  C CB  . TYR A 51  ? 0.1607 0.2094 0.2934 -0.0006 0.0006  0.0585  48  TYR B CB  
361  C CG  . TYR A 51  ? 0.1836 0.2311 0.3283 -0.0092 -0.0017 0.0614  48  TYR B CG  
362  C CD1 . TYR A 51  ? 0.1995 0.2341 0.3472 -0.0106 -0.0087 0.0572  48  TYR B CD1 
363  C CD2 . TYR A 51  ? 0.1799 0.2399 0.3328 -0.0167 0.0030  0.0673  48  TYR B CD2 
364  C CE1 . TYR A 51  ? 0.2189 0.2495 0.3770 -0.0199 -0.0118 0.0599  48  TYR B CE1 
365  C CE2 . TYR A 51  ? 0.2080 0.2668 0.3717 -0.0268 0.0008  0.0708  48  TYR B CE2 
366  C CZ  . TYR A 51  ? 0.2077 0.2508 0.3743 -0.0287 -0.0071 0.0674  48  TYR B CZ  
367  O OH  . TYR A 51  ? 0.2096 0.2499 0.3865 -0.0398 -0.0100 0.0706  48  TYR B OH  
368  N N   A LYS A 52  ? 0.1569 0.2086 0.2680 0.0137  0.0005  0.0482  49  LYS B N   
369  N N   B LYS A 52  ? 0.1677 0.2195 0.2789 0.0137  0.0005  0.0482  49  LYS B N   
370  C CA  A LYS A 52  ? 0.1672 0.2135 0.2652 0.0175  -0.0003 0.0456  49  LYS B CA  
371  C CA  B LYS A 52  ? 0.1881 0.2344 0.2861 0.0175  -0.0003 0.0456  49  LYS B CA  
372  C C   A LYS A 52  ? 0.1676 0.2106 0.2627 0.0189  -0.0063 0.0407  49  LYS B C   
373  C C   B LYS A 52  ? 0.1785 0.2216 0.2736 0.0189  -0.0063 0.0407  49  LYS B C   
374  O O   A LYS A 52  ? 0.1621 0.1997 0.2480 0.0197  -0.0080 0.0379  49  LYS B O   
375  O O   B LYS A 52  ? 0.1711 0.2087 0.2570 0.0197  -0.0080 0.0379  49  LYS B O   
376  C CB  A LYS A 52  ? 0.1884 0.2377 0.2791 0.0195  0.0032  0.0468  49  LYS B CB  
377  C CB  B LYS A 52  ? 0.2332 0.2830 0.3246 0.0194  0.0034  0.0470  49  LYS B CB  
378  C CG  A LYS A 52  ? 0.2036 0.2472 0.2804 0.0206  0.0028  0.0456  49  LYS B CG  
379  C CG  B LYS A 52  ? 0.2793 0.3233 0.3567 0.0208  0.0027  0.0456  49  LYS B CG  
380  C CD  A LYS A 52  ? 0.2265 0.2708 0.2947 0.0203  0.0065  0.0475  49  LYS B CD  
381  C CD  B LYS A 52  ? 0.3288 0.3742 0.3990 0.0201  0.0071  0.0481  49  LYS B CD  
382  C CE  A LYS A 52  ? 0.1982 0.2383 0.2537 0.0193  0.0056  0.0462  49  LYS B CE  
383  C CE  B LYS A 52  ? 0.3049 0.3477 0.3651 0.0193  0.0066  0.0469  49  LYS B CE  
384  N NZ  A LYS A 52  ? 0.1872 0.2246 0.2336 0.0181  0.0068  0.0469  49  LYS B NZ  
385  N NZ  B LYS A 52  ? 0.2838 0.3275 0.3493 0.0201  0.0061  0.0461  49  LYS B NZ  
386  N N   . ASN A 53  ? 0.1536 0.2019 0.2569 0.0193  -0.0094 0.0395  50  ASN B N   
387  C CA  . ASN A 53  ? 0.1634 0.2094 0.2641 0.0206  -0.0166 0.0357  50  ASN B CA  
388  C C   . ASN A 53  ? 0.1553 0.1979 0.2592 0.0175  -0.0209 0.0322  50  ASN B C   
389  O O   . ASN A 53  ? 0.1652 0.2027 0.2591 0.0181  -0.0255 0.0284  50  ASN B O   
390  C CB  . ASN A 53  ? 0.1579 0.2121 0.2680 0.0235  -0.0196 0.0353  50  ASN B CB  
391  C CG  . ASN A 53  ? 0.1868 0.2381 0.2883 0.0280  -0.0179 0.0366  50  ASN B CG  
392  O OD1 . ASN A 53  ? 0.2154 0.2725 0.3218 0.0293  -0.0123 0.0376  50  ASN B OD1 
393  N ND2 . ASN A 53  ? 0.1869 0.2283 0.2743 0.0298  -0.0229 0.0364  50  ASN B ND2 
394  N N   . VAL A 54  ? 0.1354 0.1801 0.2521 0.0134  -0.0196 0.0333  51  VAL B N   
395  C CA  . VAL A 54  ? 0.1473 0.1865 0.2681 0.0099  -0.0247 0.0292  51  VAL B CA  
396  C C   . VAL A 54  ? 0.1529 0.1812 0.2618 0.0122  -0.0236 0.0260  51  VAL B C   
397  O O   . VAL A 54  ? 0.1617 0.1851 0.2638 0.0128  -0.0282 0.0194  51  VAL B O   
398  C CB  . VAL A 54  ? 0.1392 0.1811 0.2759 0.0034  -0.0240 0.0323  51  VAL B CB  
399  C CG1 . VAL A 54  ? 0.1523 0.1826 0.2917 -0.0008 -0.0293 0.0281  51  VAL B CG1 
400  C CG2 . VAL A 54  ? 0.1382 0.1955 0.2888 0.0010  -0.0252 0.0333  51  VAL B CG2 
401  N N   . VAL A 55  ? 0.1619 0.1886 0.2681 0.0140  -0.0177 0.0300  52  VAL B N   
402  C CA  . VAL A 55  ? 0.1651 0.1851 0.2631 0.0173  -0.0167 0.0262  52  VAL B CA  
403  C C   . VAL A 55  ? 0.1627 0.1862 0.2463 0.0200  -0.0160 0.0228  52  VAL B C   
404  O O   . VAL A 55  ? 0.1970 0.2180 0.2737 0.0219  -0.0167 0.0161  52  VAL B O   
405  C CB  . VAL A 55  ? 0.1556 0.1738 0.2563 0.0187  -0.0123 0.0314  52  VAL B CB  
406  C CG1 . VAL A 55  ? 0.1462 0.1722 0.2404 0.0203  -0.0070 0.0362  52  VAL B CG1 
407  C CG2 . VAL A 55  ? 0.1738 0.1844 0.2728 0.0231  -0.0136 0.0259  52  VAL B CG2 
408  N N   . GLY A 56  ? 0.1547 0.1833 0.2335 0.0198  -0.0143 0.0271  53  GLY B N   
409  C CA  . GLY A 56  ? 0.1699 0.1995 0.2337 0.0203  -0.0138 0.0262  53  GLY B CA  
410  C C   . GLY A 56  ? 0.1774 0.2050 0.2323 0.0194  -0.0193 0.0207  53  GLY B C   
411  O O   . GLY A 56  ? 0.1828 0.2115 0.2241 0.0188  -0.0178 0.0184  53  GLY B O   
412  N N   . ALA A 57  ? 0.1985 0.2251 0.2604 0.0184  -0.0256 0.0191  54  ALA B N   
413  C CA  . ALA A 57  ? 0.2002 0.2251 0.2535 0.0172  -0.0324 0.0135  54  ALA B CA  
414  C C   . ALA A 57  ? 0.1931 0.2158 0.2404 0.0175  -0.0308 0.0052  54  ALA B C   
415  O O   . ALA A 57  ? 0.2077 0.2314 0.2392 0.0166  -0.0318 0.0009  54  ALA B O   
416  C CB  . ALA A 57  ? 0.2026 0.2288 0.2688 0.0157  -0.0396 0.0127  54  ALA B CB  
417  N N   . ARG A 58  ? 0.1919 0.2114 0.2508 0.0189  -0.0282 0.0031  55  ARG B N   
418  C CA  . ARG A 58  ? 0.2025 0.2186 0.2589 0.0215  -0.0269 -0.0059 55  ARG B CA  
419  C C   . ARG A 58  ? 0.1973 0.2201 0.2451 0.0246  -0.0196 -0.0067 55  ARG B C   
420  O O   . ARG A 58  ? 0.2054 0.2315 0.2436 0.0262  -0.0182 -0.0153 55  ARG B O   
421  C CB  . ARG A 58  ? 0.2210 0.2280 0.2929 0.0223  -0.0284 -0.0073 55  ARG B CB  
422  C CG  . ARG A 58  ? 0.2298 0.2297 0.3082 0.0182  -0.0363 -0.0116 55  ARG B CG  
423  C CD  . ARG A 58  ? 0.2133 0.2194 0.2988 0.0135  -0.0391 -0.0040 55  ARG B CD  
424  N NE  . ARG A 58  ? 0.2140 0.2164 0.3110 0.0081  -0.0461 -0.0063 55  ARG B NE  
425  C CZ  . ARG A 58  ? 0.2141 0.2251 0.3204 0.0043  -0.0490 -0.0011 55  ARG B CZ  
426  N NH1 . ARG A 58  ? 0.2008 0.2211 0.3111 0.0056  -0.0445 0.0073  55  ARG B NH1 
427  N NH2 . ARG A 58  ? 0.2371 0.2483 0.3508 -0.0009 -0.0567 -0.0052 55  ARG B NH2 
428  N N   . ARG A 59  ? 0.1903 0.2171 0.2409 0.0249  -0.0148 0.0015  56  ARG B N   
429  C CA  . ARG A 59  ? 0.1875 0.2233 0.2313 0.0263  -0.0083 0.0014  56  ARG B CA  
430  C C   . ARG A 59  ? 0.2003 0.2425 0.2259 0.0224  -0.0073 -0.0002 56  ARG B C   
431  O O   . ARG A 59  ? 0.2139 0.2647 0.2328 0.0235  -0.0032 -0.0071 56  ARG B O   
432  C CB  . ARG A 59  ? 0.1830 0.2214 0.2322 0.0259  -0.0048 0.0106  56  ARG B CB  
433  C CG  . ARG A 59  ? 0.1883 0.2217 0.2524 0.0291  -0.0051 0.0132  56  ARG B CG  
434  C CD  . ARG A 59  ? 0.1839 0.2203 0.2505 0.0274  -0.0022 0.0225  56  ARG B CD  
435  N NE  . ARG A 59  ? 0.1906 0.2364 0.2523 0.0283  0.0024  0.0229  56  ARG B NE  
436  C CZ  . ARG A 59  ? 0.1907 0.2410 0.2482 0.0254  0.0050  0.0287  56  ARG B CZ  
437  N NH1 . ARG A 59  ? 0.1717 0.2176 0.2285 0.0226  0.0041  0.0340  56  ARG B NH1 
438  N NH2 . ARG A 59  ? 0.1601 0.2205 0.2141 0.0251  0.0086  0.0281  56  ARG B NH2 
439  N N   A SER A 60  ? 0.1992 0.2375 0.2174 0.0182  -0.0114 0.0057  57  SER B N   
440  N N   B SER A 60  ? 0.1992 0.2375 0.2174 0.0182  -0.0115 0.0056  57  SER B N   
441  C CA  A SER A 60  ? 0.2148 0.2547 0.2136 0.0134  -0.0130 0.0064  57  SER B CA  
442  C CA  B SER A 60  ? 0.2147 0.2549 0.2133 0.0134  -0.0128 0.0063  57  SER B CA  
443  C C   A SER A 60  ? 0.2247 0.2672 0.2137 0.0131  -0.0148 -0.0036 57  SER B C   
444  C C   B SER A 60  ? 0.2247 0.2673 0.2137 0.0131  -0.0148 -0.0037 57  SER B C   
445  O O   A SER A 60  ? 0.2423 0.2933 0.2162 0.0099  -0.0107 -0.0068 57  SER B O   
446  O O   B SER A 60  ? 0.2423 0.2933 0.2160 0.0099  -0.0107 -0.0068 57  SER B O   
447  C CB  A SER A 60  ? 0.2204 0.2523 0.2167 0.0113  -0.0199 0.0142  57  SER B CB  
448  C CB  B SER A 60  ? 0.2215 0.2539 0.2161 0.0110  -0.0195 0.0141  57  SER B CB  
449  O OG  A SER A 60  ? 0.2291 0.2595 0.2259 0.0103  -0.0171 0.0222  57  SER B OG  
450  O OG  B SER A 60  ? 0.2498 0.2820 0.2235 0.0056  -0.0209 0.0170  57  SER B OG  
451  N N   . ALA A 61  ? 0.2221 0.2581 0.2195 0.0154  -0.0209 -0.0087 58  ALA B N   
452  C CA  . ALA A 61  ? 0.2385 0.2748 0.2263 0.0150  -0.0243 -0.0195 58  ALA B CA  
453  C C   . ALA A 61  ? 0.2379 0.2814 0.2262 0.0192  -0.0171 -0.0304 58  ALA B C   
454  O O   . ALA A 61  ? 0.2429 0.2943 0.2153 0.0176  -0.0148 -0.0382 58  ALA B O   
455  C CB  . ALA A 61  ? 0.2422 0.2697 0.2417 0.0158  -0.0325 -0.0229 58  ALA B CB  
456  N N   . TRP A 62  ? 0.2244 0.2665 0.2301 0.0245  -0.0136 -0.0301 59  TRP B N   
457  C CA  . TRP A 62  ? 0.2386 0.2876 0.2485 0.0309  -0.0076 -0.0401 59  TRP B CA  
458  C C   . TRP A 62  ? 0.2394 0.3066 0.2370 0.0289  0.0008  -0.0412 59  TRP B C   
459  O O   . TRP A 62  ? 0.2543 0.3318 0.2459 0.0318  0.0048  -0.0536 59  TRP B O   
460  C CB  . TRP A 62  ? 0.2307 0.2738 0.2609 0.0367  -0.0070 -0.0365 59  TRP B CB  
461  C CG  . TRP A 62  ? 0.2387 0.2860 0.2761 0.0456  -0.0036 -0.0478 59  TRP B CG  
462  C CD1 . TRP A 62  ? 0.2632 0.2994 0.3072 0.0518  -0.0077 -0.0593 59  TRP B CD1 
463  C CD2 . TRP A 62  ? 0.2342 0.2987 0.2734 0.0496  0.0041  -0.0497 59  TRP B CD2 
464  N NE1 . TRP A 62  ? 0.2637 0.3083 0.3140 0.0612  -0.0032 -0.0685 59  TRP B NE1 
465  C CE2 . TRP A 62  ? 0.2527 0.3167 0.3011 0.0600  0.0042  -0.0630 59  TRP B CE2 
466  C CE3 . TRP A 62  ? 0.2314 0.3119 0.2665 0.0454  0.0103  -0.0419 59  TRP B CE3 
467  C CZ2 . TRP A 62  ? 0.2465 0.3282 0.3019 0.0675  0.0104  -0.0688 59  TRP B CZ2 
468  C CZ3 . TRP A 62  ? 0.2357 0.3343 0.2769 0.0508  0.0167  -0.0473 59  TRP B CZ3 
469  C CH2 . TRP A 62  ? 0.2371 0.3378 0.2889 0.0622  0.0169  -0.0608 59  TRP B CH2 
470  N N   . ARG A 63  ? 0.2373 0.3091 0.2311 0.0235  0.0035  -0.0294 60  ARG B N   
471  C CA  . ARG A 63  ? 0.2414 0.3308 0.2239 0.0189  0.0114  -0.0287 60  ARG B CA  
472  C C   . ARG A 63  ? 0.2566 0.3517 0.2161 0.0121  0.0116  -0.0326 60  ARG B C   
473  O O   . ARG A 63  ? 0.2591 0.3720 0.2107 0.0110  0.0190  -0.0404 60  ARG B O   
474  C CB  . ARG A 63  ? 0.2526 0.3421 0.2354 0.0134  0.0129  -0.0152 60  ARG B CB  
475  C CG  . ARG A 63  ? 0.2473 0.3370 0.2498 0.0193  0.0145  -0.0122 60  ARG B CG  
476  C CD  . ARG A 63  ? 0.2553 0.3487 0.2553 0.0130  0.0171  -0.0015 60  ARG B CD  
477  N NE  . ARG A 63  ? 0.2560 0.3344 0.2478 0.0076  0.0117  0.0082  60  ARG B NE  
478  C CZ  . ARG A 63  ? 0.2472 0.3133 0.2486 0.0103  0.0074  0.0137  60  ARG B CZ  
479  N NH1 . ARG A 63  ? 0.2299 0.2935 0.2479 0.0170  0.0068  0.0122  60  ARG B NH1 
480  N NH2 . ARG A 63  ? 0.2623 0.3178 0.2564 0.0063  0.0031  0.0211  60  ARG B NH2 
481  N N   . VAL A 64  ? 0.2507 0.3323 0.1997 0.0079  0.0033  -0.0277 61  VAL B N   
482  C CA  . VAL A 64  ? 0.2690 0.3541 0.1941 0.0012  0.0016  -0.0303 61  VAL B CA  
483  C C   . VAL A 64  ? 0.2720 0.3647 0.1945 0.0061  0.0037  -0.0476 61  VAL B C   
484  O O   . VAL A 64  ? 0.2844 0.3923 0.1891 0.0017  0.0096  -0.0539 61  VAL B O   
485  C CB  . VAL A 64  ? 0.2730 0.3418 0.1904 -0.0024 -0.0098 -0.0217 61  VAL B CB  
486  C CG1 . VAL A 64  ? 0.3093 0.3798 0.2024 -0.0079 -0.0141 -0.0258 61  VAL B CG1 
487  C CG2 . VAL A 64  ? 0.2757 0.3377 0.1912 -0.0071 -0.0113 -0.0062 61  VAL B CG2 
488  N N   . VAL A 65  ? 0.2728 0.3542 0.2108 0.0139  -0.0015 -0.0554 62  VAL B N   
489  C CA  . VAL A 65  ? 0.3048 0.3887 0.2396 0.0188  -0.0016 -0.0732 62  VAL B CA  
490  C C   . VAL A 65  ? 0.3288 0.4303 0.2700 0.0256  0.0093  -0.0848 62  VAL B C   
491  O O   . VAL A 65  ? 0.3740 0.4894 0.3016 0.0258  0.0143  -0.0980 62  VAL B O   
492  C CB  . VAL A 65  ? 0.3134 0.3781 0.2625 0.0235  -0.0112 -0.0777 62  VAL B CB  
493  C CG1 . VAL A 65  ? 0.3423 0.4056 0.2891 0.0290  -0.0123 -0.0972 62  VAL B CG1 
494  C CG2 . VAL A 65  ? 0.3185 0.3723 0.2604 0.0165  -0.0217 -0.0683 62  VAL B CG2 
495  N N   . SER A 66  ? 0.3267 0.4304 0.2874 0.0308  0.0131  -0.0797 63  SER B N   
496  C CA  . SER A 66  ? 0.3472 0.4700 0.3176 0.0380  0.0225  -0.0888 63  SER B CA  
497  C C   . SER A 66  ? 0.3577 0.5065 0.3105 0.0300  0.0324  -0.0894 63  SER B C   
498  O O   . SER A 66  ? 0.3903 0.5583 0.3404 0.0343  0.0397  -0.1043 63  SER B O   
499  C CB  . SER A 66  ? 0.3284 0.4468 0.3209 0.0431  0.0223  -0.0796 63  SER B CB  
500  O OG  . SER A 66  ? 0.4146 0.5519 0.4197 0.0511  0.0297  -0.0871 63  SER B OG  
501  N N   . SER A 67  ? 0.3588 0.5079 0.2989 0.0181  0.0324  -0.0737 64  SER B N   
502  C CA  . SER A 67  ? 0.3907 0.5603 0.3101 0.0067  0.0402  -0.0712 64  SER B CA  
503  C C   . SER A 67  ? 0.4289 0.6057 0.3246 0.0030  0.0414  -0.0823 64  SER B C   
504  O O   . SER A 67  ? 0.4696 0.6725 0.3562 0.0003  0.0518  -0.0915 64  SER B O   
505  C CB  . SER A 67  ? 0.4173 0.5772 0.3270 -0.0050 0.0369  -0.0515 64  SER B CB  
506  O OG  . SER A 67  ? 0.4909 0.6666 0.3775 -0.0184 0.0430  -0.0470 64  SER B OG  
507  N N   . ILE A 68  ? 0.4195 0.5758 0.3052 0.0022  0.0309  -0.0820 65  ILE B N   
508  C CA  . ILE A 68  ? 0.4571 0.6180 0.3197 -0.0009 0.0300  -0.0934 65  ILE B CA  
509  C C   . ILE A 68  ? 0.4863 0.6609 0.3576 0.0106  0.0366  -0.1166 65  ILE B C   
510  O O   . ILE A 68  ? 0.5411 0.7364 0.3936 0.0071  0.0442  -0.1278 65  ILE B O   
511  C CB  . ILE A 68  ? 0.4519 0.5886 0.3053 -0.0033 0.0157  -0.0887 65  ILE B CB  
512  C CG1 . ILE A 68  ? 0.4561 0.5831 0.2946 -0.0150 0.0096  -0.0675 65  ILE B CG1 
513  C CG2 . ILE A 68  ? 0.4765 0.6163 0.3097 -0.0039 0.0132  -0.1044 65  ILE B CG2 
514  C CD1 . ILE A 68  ? 0.4639 0.5672 0.3053 -0.0143 -0.0052 -0.0601 65  ILE B CD1 
515  N N   . GLU A 69  ? 0.4697 0.6327 0.3679 0.0240  0.0335  -0.1237 66  GLU B N   
516  C CA  . GLU A 69  ? 0.5122 0.6838 0.4223 0.0375  0.0381  -0.1457 66  GLU B CA  
517  C C   . GLU A 69  ? 0.5356 0.7422 0.4464 0.0392  0.0528  -0.1545 66  GLU B C   
518  O O   . GLU A 69  ? 0.5433 0.7662 0.4468 0.0444  0.0590  -0.1743 66  GLU B O   
519  C CB  . GLU A 69  ? 0.4961 0.6490 0.4364 0.0499  0.0325  -0.1455 66  GLU B CB  
520  C CG  . GLU A 69  ? 0.5076 0.6572 0.4610 0.0652  0.0323  -0.1676 66  GLU B CG  
521  C CD  . GLU A 69  ? 0.5148 0.6404 0.4951 0.0751  0.0244  -0.1633 66  GLU B CD  
522  O OE1 . GLU A 69  ? 0.5455 0.6598 0.5354 0.0708  0.0203  -0.1446 66  GLU B OE1 
523  O OE2 . GLU A 69  ? 0.5578 0.6749 0.5486 0.0876  0.0220  -0.1803 66  GLU B OE2 
524  N N   . GLN A 70  ? 0.5764 0.7945 0.4972 0.0352  0.0580  -0.1405 67  GLN B N   
525  C CA  . GLN A 70  ? 0.6144 0.8684 0.5389 0.0344  0.0715  -0.1453 67  GLN B CA  
526  C C   . GLN A 70  ? 0.6702 0.9473 0.5642 0.0190  0.0801  -0.1448 67  GLN B C   
527  O O   . GLN A 70  ? 0.6906 1.0006 0.5841 0.0208  0.0922  -0.1586 67  GLN B O   
528  C CB  . GLN A 70  ? 0.6018 0.8601 0.5430 0.0314  0.0731  -0.1289 67  GLN B CB  
529  C CG  . GLN A 70  ? 0.6199 0.8614 0.5911 0.0457  0.0664  -0.1279 67  GLN B CG  
530  C CD  . GLN A 70  ? 0.7039 0.9390 0.6839 0.0392  0.0638  -0.1075 67  GLN B CD  
531  O OE1 . GLN A 70  ? 0.7966 1.0428 0.7645 0.0252  0.0682  -0.0954 67  GLN B OE1 
532  N NE2 . GLN A 70  ? 0.7033 0.9186 0.7037 0.0487  0.0563  -0.1032 67  GLN B NE2 
533  N N   . LYS A 71  ? 0.7415 1.0026 0.6106 0.0043  0.0737  -0.1293 68  LYS B N   
534  C CA  . LYS A 71  ? 0.8390 1.1157 0.6748 -0.0127 0.0792  -0.1244 68  LYS B CA  
535  C C   . LYS A 71  ? 0.8998 1.1955 0.7193 -0.0098 0.0857  -0.1465 68  LYS B C   
536  O O   . LYS A 71  ? 1.0149 1.3419 0.8174 -0.0193 0.0979  -0.1504 68  LYS B O   
537  C CB  . LYS A 71  ? 0.8980 1.1463 0.7121 -0.0248 0.0668  -0.1053 68  LYS B CB  
538  C CG  . LYS A 71  ? 0.9826 1.2400 0.7667 -0.0450 0.0702  -0.0894 68  LYS B CG  
539  C CD  . LYS A 71  ? 0.9683 1.2158 0.7576 -0.0542 0.0681  -0.0672 68  LYS B CD  
540  C CE  . LYS A 71  ? 0.9704 1.2419 0.7810 -0.0535 0.0794  -0.0682 68  LYS B CE  
541  N NZ  . LYS A 71  ? 0.9158 1.1769 0.7608 -0.0375 0.0757  -0.0717 68  LYS B NZ  
542  N N   . THR A 72  ? 0.8840 1.1604 0.7075 0.0022  0.0774  -0.1607 69  THR B N   
543  C CA  . THR A 72  ? 0.8679 1.1604 0.6891 0.0127  0.0835  -0.1878 69  THR B CA  
544  C C   . THR A 72  ? 0.8864 1.1852 0.7435 0.0319  0.0874  -0.2019 69  THR B C   
545  O O   . THR A 72  ? 0.8937 1.2254 0.7548 0.0379  0.1002  -0.2193 69  THR B O   
546  C CB  . THR A 72  ? 0.8600 1.1273 0.6656 0.0146  0.0716  -0.1965 69  THR B CB  
547  O OG1 . THR A 72  ? 0.8927 1.1803 0.6981 0.0254  0.0803  -0.2244 69  THR B OG1 
548  C CG2 . THR A 72  ? 0.7840 1.0129 0.6091 0.0220  0.0560  -0.1898 69  THR B CG2 
549  N N   . ALA A 76  ? 0.8973 1.1481 0.6730 0.0463  0.0620  -0.2897 73  ALA B N   
550  C CA  . ALA A 76  ? 0.8955 1.1296 0.7016 0.0667  0.0585  -0.3091 73  ALA B CA  
551  C C   . ALA A 76  ? 0.8651 1.0558 0.6782 0.0680  0.0397  -0.3064 73  ALA B C   
552  O O   . ALA A 76  ? 0.8588 1.0270 0.7016 0.0771  0.0331  -0.3008 73  ALA B O   
553  C CB  . ALA A 76  ? 0.9238 1.1794 0.7220 0.0776  0.0683  -0.3418 73  ALA B CB  
554  N N   . ALA A 77  ? 0.8438 1.0246 0.6296 0.0587  0.0311  -0.3112 74  ALA B N   
555  C CA  . ALA A 77  ? 0.8216 0.9662 0.6107 0.0549  0.0128  -0.3044 74  ALA B CA  
556  C C   . ALA A 77  ? 0.7825 0.9172 0.5785 0.0439  0.0063  -0.2720 74  ALA B C   
557  O O   . ALA A 77  ? 0.7326 0.8403 0.5499 0.0457  -0.0049 -0.2627 74  ALA B O   
558  C CB  . ALA A 77  ? 0.8714 1.0140 0.6281 0.0472  0.0059  -0.3186 74  ALA B CB  
559  N N   . ALA A 78  ? 0.7492 0.9060 0.5271 0.0323  0.0137  -0.2553 75  ALA B N   
560  C CA  . ALA A 78  ? 0.7189 0.8711 0.5043 0.0239  0.0112  -0.2261 75  ALA B CA  
561  C C   . ALA A 78  ? 0.6874 0.8350 0.5082 0.0339  0.0153  -0.2188 75  ALA B C   
562  O O   . ALA A 78  ? 0.6182 0.7471 0.4551 0.0319  0.0073  -0.2004 75  ALA B O   
563  C CB  . ALA A 78  ? 0.7176 0.8953 0.4761 0.0107  0.0203  -0.2137 75  ALA B CB  
564  N N   . GLN A 79  ? 0.6801 0.8475 0.5119 0.0443  0.0280  -0.2330 76  GLN B N   
565  C CA  . GLN A 79  ? 0.6504 0.8159 0.5150 0.0551  0.0316  -0.2282 76  GLN B CA  
566  C C   . GLN A 79  ? 0.6147 0.7467 0.5030 0.0653  0.0194  -0.2326 76  GLN B C   
567  O O   . GLN A 79  ? 0.5837 0.7024 0.4936 0.0670  0.0156  -0.2168 76  GLN B O   
568  C CB  . GLN A 79  ? 0.6967 0.8932 0.5698 0.0652  0.0468  -0.2436 76  GLN B CB  
569  C CG  . GLN A 79  ? 0.6857 0.8918 0.5833 0.0683  0.0524  -0.2287 76  GLN B CG  
570  C CD  . GLN A 79  ? 0.7765 1.0001 0.6986 0.0855  0.0608  -0.2454 76  GLN B CD  
571  O OE1 . GLN A 79  ? 0.8267 1.0570 0.7498 0.0977  0.0640  -0.2705 76  GLN B OE1 
572  N NE2 . GLN A 79  ? 0.8148 1.0468 0.7574 0.0873  0.0642  -0.2315 76  GLN B NE2 
573  N N   . GLN A 80  ? 0.6104 0.7287 0.4935 0.0711  0.0133  -0.2538 77  GLN B N   
574  C CA  . GLN A 80  ? 0.6088 0.6927 0.5114 0.0781  0.0006  -0.2578 77  GLN B CA  
575  C C   . GLN A 80  ? 0.5768 0.6397 0.4819 0.0662  -0.0114 -0.2354 77  GLN B C   
576  O O   . GLN A 80  ? 0.5301 0.5723 0.4587 0.0695  -0.0176 -0.2258 77  GLN B O   
577  C CB  . GLN A 80  ? 0.6543 0.7265 0.5478 0.0843  -0.0044 -0.2851 77  GLN B CB  
578  C CG  . GLN A 80  ? 0.6777 0.7112 0.5902 0.0891  -0.0187 -0.2886 77  GLN B CG  
579  C CD  . GLN A 80  ? 0.7424 0.7607 0.6499 0.0978  -0.0238 -0.3180 77  GLN B CD  
580  O OE1 . GLN A 80  ? 0.7887 0.8221 0.6934 0.1101  -0.0148 -0.3401 77  GLN B OE1 
581  N NE2 . GLN A 80  ? 0.7535 0.7418 0.6610 0.0915  -0.0385 -0.3194 77  GLN B NE2 
582  N N   . MET A 81  ? 0.5803 0.6484 0.4610 0.0528  -0.0154 -0.2284 78  MET B N   
583  C CA  . MET A 81  ? 0.5521 0.6042 0.4364 0.0427  -0.0268 -0.2082 78  MET B CA  
584  C C   . MET A 81  ? 0.4924 0.5471 0.3935 0.0415  -0.0229 -0.1852 78  MET B C   
585  O O   . MET A 81  ? 0.4624 0.4992 0.3821 0.0407  -0.0304 -0.1738 78  MET B O   
586  C CB  . MET A 81  ? 0.5909 0.6509 0.4460 0.0298  -0.0318 -0.2029 78  MET B CB  
587  C CG  . MET A 81  ? 0.5858 0.6304 0.4468 0.0212  -0.0452 -0.1849 78  MET B CG  
588  S SD  . MET A 81  ? 0.6774 0.7314 0.5023 0.0084  -0.0528 -0.1820 78  MET B SD  
589  C CE  . MET A 81  ? 0.6460 0.6982 0.4518 0.0102  -0.0566 -0.2117 78  MET B CE  
590  N N   . ALA A 82  ? 0.4757 0.5535 0.3695 0.0404  -0.0112 -0.1790 79  ALA B N   
591  C CA  . ALA A 82  ? 0.4428 0.5242 0.3514 0.0395  -0.0068 -0.1595 79  ALA B CA  
592  C C   . ALA A 82  ? 0.4300 0.4994 0.3686 0.0508  -0.0068 -0.1607 79  ALA B C   
593  O O   . ALA A 82  ? 0.3884 0.4459 0.3424 0.0491  -0.0110 -0.1446 79  ALA B O   
594  C CB  . ALA A 82  ? 0.4484 0.5573 0.3432 0.0356  0.0057  -0.1562 79  ALA B CB  
595  N N   . ARG A 83  ? 0.4505 0.5218 0.3969 0.0629  -0.0029 -0.1801 80  ARG B N   
596  C CA  . ARG A 83  ? 0.4495 0.5059 0.4228 0.0747  -0.0050 -0.1821 80  ARG B CA  
597  C C   . ARG A 83  ? 0.4277 0.4528 0.4123 0.0719  -0.0181 -0.1757 80  ARG B C   
598  O O   . ARG A 83  ? 0.4160 0.4302 0.4189 0.0728  -0.0205 -0.1617 80  ARG B O   
599  C CB  . ARG A 83  ? 0.4982 0.5577 0.4771 0.0894  -0.0013 -0.2067 80  ARG B CB  
600  C CG  . ARG A 83  ? 0.5338 0.5724 0.5391 0.1027  -0.0063 -0.2097 80  ARG B CG  
601  C CD  . ARG A 83  ? 0.5854 0.6296 0.5980 0.1198  -0.0022 -0.2342 80  ARG B CD  
602  N NE  . ARG A 83  ? 0.6642 0.6905 0.6673 0.1227  -0.0089 -0.2554 80  ARG B NE  
603  C CZ  . ARG A 83  ? 0.7457 0.7879 0.7302 0.1248  -0.0036 -0.2771 80  ARG B CZ  
604  N NH1 . ARG A 83  ? 0.7678 0.8468 0.7383 0.1218  0.0095  -0.2794 80  ARG B NH1 
605  N NH2 . ARG A 83  ? 0.8064 0.8277 0.7844 0.1284  -0.0113 -0.2969 80  ARG B NH2 
606  N N   . GLU A 84  ? 0.4463 0.4586 0.4201 0.0681  -0.0262 -0.1868 81  GLU B N   
607  C CA  . GLU A 84  ? 0.4751 0.4590 0.4604 0.0645  -0.0388 -0.1836 81  GLU B CA  
608  C C   . GLU A 84  ? 0.4444 0.4271 0.4334 0.0530  -0.0428 -0.1604 81  GLU B C   
609  O O   . GLU A 84  ? 0.4268 0.3929 0.4337 0.0515  -0.0484 -0.1503 81  GLU B O   
610  C CB  . GLU A 84  ? 0.5286 0.5015 0.5004 0.0620  -0.0468 -0.2020 81  GLU B CB  
611  C CG  . GLU A 84  ? 0.5724 0.5402 0.5446 0.0752  -0.0444 -0.2271 81  GLU B CG  
612  C CD  . GLU A 84  ? 0.6456 0.6048 0.6009 0.0732  -0.0513 -0.2484 81  GLU B CD  
613  O OE1 . GLU A 84  ? 0.6742 0.6299 0.6193 0.0605  -0.0595 -0.2418 81  GLU B OE1 
614  O OE2 . GLU A 84  ? 0.6607 0.6161 0.6137 0.0843  -0.0496 -0.2720 81  GLU B OE2 
615  N N   . TYR A 85  ? 0.4382 0.4396 0.4107 0.0456  -0.0392 -0.1514 82  TYR B N   
616  C CA  . TYR A 85  ? 0.4019 0.4040 0.3783 0.0370  -0.0423 -0.1306 82  TYR B CA  
617  C C   . TYR A 85  ? 0.3707 0.3750 0.3640 0.0404  -0.0361 -0.1161 82  TYR B C   
618  O O   . TYR A 85  ? 0.3381 0.3324 0.3459 0.0370  -0.0407 -0.1034 82  TYR B O   
619  C CB  . TYR A 85  ? 0.4183 0.4364 0.3710 0.0291  -0.0415 -0.1256 82  TYR B CB  
620  C CG  . TYR A 85  ? 0.4048 0.4193 0.3592 0.0207  -0.0497 -0.1093 82  TYR B CG  
621  C CD1 . TYR A 85  ? 0.4261 0.4265 0.3933 0.0172  -0.0607 -0.1086 82  TYR B CD1 
622  C CD2 . TYR A 85  ? 0.4028 0.4286 0.3462 0.0160  -0.0469 -0.0953 82  TYR B CD2 
623  C CE1 . TYR A 85  ? 0.4332 0.4345 0.4042 0.0107  -0.0678 -0.0950 82  TYR B CE1 
624  C CE2 . TYR A 85  ? 0.4038 0.4265 0.3496 0.0104  -0.0551 -0.0817 82  TYR B CE2 
625  C CZ  . TYR A 85  ? 0.3902 0.4023 0.3515 0.0085  -0.0650 -0.0816 82  TYR B CZ  
626  O OH  . TYR A 85  ? 0.3528 0.3657 0.3181 0.0041  -0.0730 -0.0699 82  TYR B OH  
627  N N   . ARG A 86  ? 0.3679 0.3868 0.3601 0.0469  -0.0258 -0.1189 83  ARG B N   
628  C CA  . ARG A 86  ? 0.3608 0.3823 0.3693 0.0515  -0.0205 -0.1083 83  ARG B CA  
629  C C   . ARG A 86  ? 0.3498 0.3494 0.3796 0.0565  -0.0266 -0.1073 83  ARG B C   
630  O O   . ARG A 86  ? 0.3215 0.3168 0.3632 0.0547  -0.0270 -0.0925 83  ARG B O   
631  C CB  . ARG A 86  ? 0.3859 0.4289 0.3911 0.0579  -0.0094 -0.1145 83  ARG B CB  
632  C CG  . ARG A 86  ? 0.3904 0.4364 0.4137 0.0638  -0.0053 -0.1057 83  ARG B CG  
633  C CD  . ARG A 86  ? 0.4237 0.4928 0.4489 0.0701  0.0046  -0.1108 83  ARG B CD  
634  N NE  . ARG A 86  ? 0.4583 0.5326 0.4866 0.0816  0.0071  -0.1313 83  ARG B NE  
635  C CZ  . ARG A 86  ? 0.4981 0.5554 0.5401 0.0932  0.0017  -0.1430 83  ARG B CZ  
636  N NH1 . ARG A 86  ? 0.4880 0.5215 0.5459 0.0961  -0.0062 -0.1346 83  ARG B NH1 
637  N NH2 . ARG A 86  ? 0.5458 0.6104 0.5849 0.1025  0.0046  -0.1641 83  ARG B NH2 
638  N N   . GLU A 87  ? 0.3891 0.3747 0.4222 0.0627  -0.0311 -0.1230 84  GLU B N   
639  C CA  . GLU A 87  ? 0.4095 0.3707 0.4606 0.0669  -0.0379 -0.1227 84  GLU B CA  
640  C C   . GLU A 87  ? 0.3917 0.3380 0.4487 0.0557  -0.0462 -0.1104 84  GLU B C   
641  O O   . GLU A 87  ? 0.3835 0.3185 0.4551 0.0547  -0.0483 -0.0985 84  GLU B O   
642  C CB  . GLU A 87  ? 0.4512 0.3988 0.5022 0.0761  -0.0416 -0.1443 84  GLU B CB  
643  C CG  . GLU A 87  ? 0.4689 0.4312 0.5221 0.0902  -0.0333 -0.1558 84  GLU B CG  
644  C CD  . GLU A 87  ? 0.5349 0.4910 0.5844 0.1005  -0.0347 -0.1807 84  GLU B CD  
645  O OE1 . GLU A 87  ? 0.5328 0.4717 0.5749 0.0962  -0.0426 -0.1911 84  GLU B OE1 
646  O OE2 . GLU A 87  ? 0.5532 0.5248 0.6073 0.1130  -0.0275 -0.1904 84  GLU B OE2 
647  N N   . LYS A 88  ? 0.4131 0.3623 0.4588 0.0468  -0.0506 -0.1124 85  LYS B N   
648  C CA  . LYS A 88  ? 0.4147 0.3568 0.4672 0.0358  -0.0579 -0.1011 85  LYS B CA  
649  C C   . LYS A 88  ? 0.3643 0.3169 0.4239 0.0325  -0.0532 -0.0816 85  LYS B C   
650  O O   . LYS A 88  ? 0.3671 0.3108 0.4411 0.0280  -0.0561 -0.0710 85  LYS B O   
651  C CB  . LYS A 88  ? 0.4585 0.4063 0.4968 0.0283  -0.0638 -0.1072 85  LYS B CB  
652  C CG  . LYS A 88  ? 0.5214 0.4668 0.5684 0.0174  -0.0720 -0.0970 85  LYS B CG  
653  C CD  . LYS A 88  ? 0.6126 0.5689 0.6446 0.0112  -0.0779 -0.1001 85  LYS B CD  
654  C CE  . LYS A 88  ? 0.7074 0.6540 0.7303 0.0091  -0.0863 -0.1179 85  LYS B CE  
655  N NZ  . LYS A 88  ? 0.7719 0.7280 0.7870 0.0008  -0.0950 -0.1159 85  LYS B NZ  
656  N N   . ILE A 89  ? 0.3367 0.3080 0.3858 0.0344  -0.0456 -0.0775 86  ILE B N   
657  C CA  . ILE A 89  ? 0.3057 0.2868 0.3589 0.0321  -0.0409 -0.0612 86  ILE B CA  
658  C C   . ILE A 89  ? 0.3055 0.2808 0.3731 0.0371  -0.0373 -0.0546 86  ILE B C   
659  O O   . ILE A 89  ? 0.3188 0.2938 0.3955 0.0333  -0.0369 -0.0415 86  ILE B O   
660  C CB  . ILE A 89  ? 0.2984 0.2976 0.3349 0.0317  -0.0347 -0.0592 86  ILE B CB  
661  C CG1 . ILE A 89  ? 0.3160 0.3192 0.3368 0.0255  -0.0403 -0.0624 86  ILE B CG1 
662  C CG2 . ILE A 89  ? 0.2768 0.2838 0.3174 0.0301  -0.0298 -0.0440 86  ILE B CG2 
663  C CD1 . ILE A 89  ? 0.3212 0.3391 0.3214 0.0246  -0.0348 -0.0632 86  ILE B CD1 
664  N N   . GLU A 90  ? 0.3166 0.2899 0.3853 0.0461  -0.0344 -0.0638 87  GLU B N   
665  C CA  . GLU A 90  ? 0.3308 0.2970 0.4128 0.0526  -0.0331 -0.0591 87  GLU B CA  
666  C C   . GLU A 90  ? 0.3285 0.2728 0.4231 0.0485  -0.0405 -0.0531 87  GLU B C   
667  O O   . GLU A 90  ? 0.3224 0.2642 0.4256 0.0478  -0.0394 -0.0404 87  GLU B O   
668  C CB  . GLU A 90  ? 0.3554 0.3216 0.4380 0.0646  -0.0311 -0.0735 87  GLU B CB  
669  C CG  . GLU A 90  ? 0.3825 0.3717 0.4621 0.0701  -0.0219 -0.0728 87  GLU B CG  
670  C CD  . GLU A 90  ? 0.4037 0.4012 0.4826 0.0816  -0.0185 -0.0903 87  GLU B CD  
671  O OE1 . GLU A 90  ? 0.4957 0.4768 0.5798 0.0889  -0.0239 -0.1028 87  GLU B OE1 
672  O OE2 . GLU A 90  ? 0.3945 0.4160 0.4656 0.0820  -0.0104 -0.0929 87  GLU B OE2 
673  N N   . THR A 91  ? 0.3434 0.2722 0.4383 0.0452  -0.0481 -0.0622 88  THR B N   
674  C CA  . THR A 91  ? 0.3561 0.2637 0.4627 0.0388  -0.0555 -0.0561 88  THR B CA  
675  C C   . THR A 91  ? 0.3182 0.2350 0.4297 0.0279  -0.0542 -0.0397 88  THR B C   
676  O O   . THR A 91  ? 0.3109 0.2211 0.4317 0.0247  -0.0541 -0.0274 88  THR B O   
677  C CB  . THR A 91  ? 0.3922 0.2828 0.4971 0.0356  -0.0642 -0.0698 88  THR B CB  
678  O OG1 . THR A 91  ? 0.4072 0.2899 0.5083 0.0475  -0.0644 -0.0857 88  THR B OG1 
679  C CG2 . THR A 91  ? 0.4189 0.2878 0.5357 0.0259  -0.0723 -0.0630 88  THR B CG2 
680  N N   . GLU A 92  ? 0.3033 0.2367 0.4081 0.0229  -0.0529 -0.0392 89  GLU B N   
681  C CA  . GLU A 92  ? 0.2803 0.2252 0.3907 0.0149  -0.0512 -0.0257 89  GLU B CA  
682  C C   . GLU A 92  ? 0.2763 0.2295 0.3887 0.0182  -0.0436 -0.0139 89  GLU B C   
683  O O   . GLU A 92  ? 0.2585 0.2118 0.3798 0.0128  -0.0426 -0.0025 89  GLU B O   
684  C CB  . GLU A 92  ? 0.2834 0.2445 0.3852 0.0123  -0.0515 -0.0274 89  GLU B CB  
685  C CG  . GLU A 92  ? 0.3195 0.2759 0.4190 0.0072  -0.0602 -0.0375 89  GLU B CG  
686  C CD  . GLU A 92  ? 0.3158 0.2876 0.4050 0.0057  -0.0619 -0.0384 89  GLU B CD  
687  O OE1 . GLU A 92  ? 0.3052 0.2894 0.3922 0.0070  -0.0571 -0.0293 89  GLU B OE1 
688  O OE2 . GLU A 92  ? 0.3714 0.3409 0.4543 0.0028  -0.0692 -0.0481 89  GLU B OE2 
689  N N   . LEU A 93  ? 0.2736 0.2348 0.3772 0.0264  -0.0381 -0.0172 90  LEU B N   
690  C CA  . LEU A 93  ? 0.3122 0.2827 0.4163 0.0294  -0.0315 -0.0075 90  LEU B CA  
691  C C   . LEU A 93  ? 0.3082 0.2658 0.4222 0.0306  -0.0328 -0.0005 90  LEU B C   
692  O O   . LEU A 93  ? 0.3110 0.2730 0.4288 0.0265  -0.0301 0.0115  90  LEU B O   
693  C CB  . LEU A 93  ? 0.3411 0.3234 0.4347 0.0365  -0.0263 -0.0141 90  LEU B CB  
694  C CG  . LEU A 93  ? 0.3972 0.3938 0.4873 0.0370  -0.0195 -0.0053 90  LEU B CG  
695  C CD1 . LEU A 93  ? 0.4404 0.4510 0.5176 0.0386  -0.0152 -0.0109 90  LEU B CD1 
696  C CD2 . LEU A 93  ? 0.4572 0.4515 0.5546 0.0425  -0.0179 -0.0010 90  LEU B CD2 
697  N N   A ARG A 94  ? 0.3263 0.2672 0.4437 0.0357  -0.0376 -0.0079 91  ARG B N   
698  N N   B ARG A 94  ? 0.3282 0.2691 0.4456 0.0357  -0.0376 -0.0079 91  ARG B N   
699  C CA  A ARG A 94  ? 0.3635 0.2877 0.4892 0.0372  -0.0411 -0.0009 91  ARG B CA  
700  C CA  B ARG A 94  ? 0.3575 0.2813 0.4832 0.0373  -0.0412 -0.0011 91  ARG B CA  
701  C C   A ARG A 94  ? 0.3784 0.2934 0.5108 0.0250  -0.0444 0.0103  91  ARG B C   
702  C C   B ARG A 94  ? 0.3703 0.2852 0.5027 0.0250  -0.0444 0.0103  91  ARG B C   
703  O O   A ARG A 94  ? 0.3823 0.2946 0.5179 0.0225  -0.0434 0.0230  91  ARG B O   
704  O O   B ARG A 94  ? 0.3726 0.2849 0.5082 0.0226  -0.0434 0.0230  91  ARG B O   
705  C CB  A ARG A 94  ? 0.4016 0.3065 0.5298 0.0461  -0.0472 -0.0128 91  ARG B CB  
706  C CB  B ARG A 94  ? 0.3909 0.2939 0.5195 0.0451  -0.0479 -0.0127 91  ARG B CB  
707  C CG  A ARG A 94  ? 0.4130 0.3312 0.5376 0.0591  -0.0426 -0.0221 91  ARG B CG  
708  C CG  B ARG A 94  ? 0.4016 0.3117 0.5277 0.0593  -0.0453 -0.0242 91  ARG B CG  
709  C CD  A ARG A 94  ? 0.4456 0.3498 0.5740 0.0716  -0.0472 -0.0359 91  ARG B CD  
710  C CD  B ARG A 94  ? 0.4282 0.3178 0.5574 0.0682  -0.0521 -0.0392 91  ARG B CD  
711  N NE  A ARG A 94  ? 0.4352 0.3614 0.5626 0.0819  -0.0404 -0.0399 91  ARG B NE  
712  N NE  B ARG A 94  ? 0.4206 0.3283 0.5452 0.0794  -0.0465 -0.0533 91  ARG B NE  
713  C CZ  A ARG A 94  ? 0.4232 0.3522 0.5576 0.0896  -0.0404 -0.0331 91  ARG B CZ  
714  C CZ  B ARG A 94  ? 0.4180 0.3283 0.5360 0.0827  -0.0462 -0.0706 91  ARG B CZ  
715  N NH1 A ARG A 94  ? 0.3956 0.3011 0.5386 0.0950  -0.0486 -0.0295 91  ARG B NH1 
716  N NH1 B ARG A 94  ? 0.4335 0.3250 0.5497 0.0774  -0.0531 -0.0778 91  ARG B NH1 
717  N NH2 A ARG A 94  ? 0.3708 0.3258 0.5029 0.0910  -0.0328 -0.0296 91  ARG B NH2 
718  N NH2 B ARG A 94  ? 0.4043 0.3369 0.5171 0.0906  -0.0389 -0.0806 91  ARG B NH2 
719  N N   . ASP A 95  ? 0.3676 0.2799 0.5017 0.0170  -0.0481 0.0056  92  ASP B N   
720  C CA  . ASP A 95  ? 0.3719 0.2804 0.5141 0.0038  -0.0507 0.0148  92  ASP B CA  
721  C C   . ASP A 95  ? 0.3290 0.2587 0.4725 -0.0013 -0.0434 0.0268  92  ASP B C   
722  O O   . ASP A 95  ? 0.2984 0.2254 0.4471 -0.0087 -0.0425 0.0388  92  ASP B O   
723  C CB  . ASP A 95  ? 0.4203 0.3252 0.5653 -0.0036 -0.0569 0.0060  92  ASP B CB  
724  C CG  . ASP A 95  ? 0.4596 0.3401 0.6037 -0.0005 -0.0651 -0.0065 92  ASP B CG  
725  O OD1 . ASP A 95  ? 0.5887 0.4530 0.7318 0.0082  -0.0666 -0.0082 92  ASP B OD1 
726  O OD2 . ASP A 95  ? 0.5411 0.4197 0.6850 -0.0053 -0.0704 -0.0161 92  ASP B OD2 
727  N N   . ILE A 96  ? 0.2959 0.2450 0.4331 0.0033  -0.0382 0.0237  93  ILE B N   
728  C CA  . ILE A 96  ? 0.2720 0.2397 0.4094 0.0007  -0.0315 0.0327  93  ILE B CA  
729  C C   . ILE A 96  ? 0.2539 0.2206 0.3892 0.0035  -0.0273 0.0423  93  ILE B C   
730  O O   . ILE A 96  ? 0.2316 0.2036 0.3705 -0.0031 -0.0241 0.0526  93  ILE B O   
731  C CB  . ILE A 96  ? 0.2510 0.2343 0.3808 0.0053  -0.0287 0.0273  93  ILE B CB  
732  C CG1 . ILE A 96  ? 0.3003 0.2866 0.4318 0.0016  -0.0342 0.0197  93  ILE B CG1 
733  C CG2 . ILE A 96  ? 0.2443 0.2434 0.3734 0.0047  -0.0221 0.0353  93  ILE B CG2 
734  C CD1 . ILE A 96  ? 0.2918 0.2852 0.4108 0.0076  -0.0339 0.0125  93  ILE B CD1 
735  N N   . CYS A 97  ? 0.2558 0.2175 0.3851 0.0132  -0.0272 0.0383  94  CYS B N   
736  C CA  . CYS A 97  ? 0.2724 0.2333 0.4000 0.0168  -0.0250 0.0465  94  CYS B CA  
737  C C   . CYS A 97  ? 0.2802 0.2246 0.4129 0.0113  -0.0292 0.0566  94  CYS B C   
738  O O   . CYS A 97  ? 0.3051 0.2552 0.4361 0.0072  -0.0258 0.0680  94  CYS B O   
739  C CB  . CYS A 97  ? 0.2613 0.2226 0.3847 0.0284  -0.0250 0.0390  94  CYS B CB  
740  S SG  . CYS A 97  ? 0.2402 0.2234 0.3545 0.0316  -0.0183 0.0326  94  CYS B SG  
741  N N   . ASN A 98  ? 0.2973 0.2223 0.4349 0.0092  -0.0362 0.0526  95  ASN B N   
742  C CA  . ASN A 98  ? 0.3640 0.2689 0.5055 0.0024  -0.0416 0.0626  95  ASN B CA  
743  C C   . ASN A 98  ? 0.3323 0.2465 0.4770 -0.0124 -0.0379 0.0740  95  ASN B C   
744  O O   . ASN A 98  ? 0.3192 0.2276 0.4623 -0.0180 -0.0380 0.0871  95  ASN B O   
745  C CB  . ASN A 98  ? 0.3958 0.2750 0.5415 0.0034  -0.0508 0.0545  95  ASN B CB  
746  C CG  . ASN A 98  ? 0.4825 0.3507 0.6265 0.0192  -0.0547 0.0448  95  ASN B CG  
747  O OD1 . ASN A 98  ? 0.5014 0.3780 0.6425 0.0287  -0.0520 0.0472  95  ASN B OD1 
748  N ND2 . ASN A 98  ? 0.4893 0.3403 0.6355 0.0224  -0.0611 0.0321  95  ASN B ND2 
749  N N   . ASP A 99  ? 0.3236 0.2538 0.4725 -0.0182 -0.0349 0.0690  96  ASP B N   
750  C CA  . ASP A 99  ? 0.3375 0.2829 0.4918 -0.0310 -0.0301 0.0779  96  ASP B CA  
751  C C   . ASP A 99  ? 0.3008 0.2623 0.4490 -0.0300 -0.0220 0.0870  96  ASP B C   
752  O O   . ASP A 99  ? 0.2881 0.2503 0.4362 -0.0395 -0.0198 0.0991  96  ASP B O   
753  C CB  . ASP A 99  ? 0.3423 0.3056 0.5037 -0.0345 -0.0287 0.0700  96  ASP B CB  
754  C CG  . ASP A 99  ? 0.4261 0.3795 0.5967 -0.0434 -0.0360 0.0652  96  ASP B CG  
755  O OD1 . ASP A 99  ? 0.4938 0.4229 0.6653 -0.0478 -0.0426 0.0673  96  ASP B OD1 
756  O OD2 . ASP A 99  ? 0.4159 0.3846 0.5929 -0.0459 -0.0362 0.0591  96  ASP B OD2 
757  N N   . VAL A 100 ? 0.2598 0.2330 0.4016 -0.0194 -0.0181 0.0813  97  VAL B N   
758  C CA  . VAL A 100 ? 0.2531 0.2415 0.3882 -0.0180 -0.0110 0.0876  97  VAL B CA  
759  C C   . VAL A 100 ? 0.2428 0.2193 0.3715 -0.0180 -0.0129 0.0983  97  VAL B C   
760  O O   . VAL A 100 ? 0.2261 0.2106 0.3509 -0.0246 -0.0085 0.1085  97  VAL B O   
761  C CB  . VAL A 100 ? 0.2438 0.2431 0.3726 -0.0074 -0.0080 0.0793  97  VAL B CB  
762  C CG1 . VAL A 100 ? 0.2473 0.2590 0.3679 -0.0057 -0.0019 0.0846  97  VAL B CG1 
763  C CG2 . VAL A 100 ? 0.2245 0.2351 0.3577 -0.0077 -0.0068 0.0711  97  VAL B CG2 
764  N N   . LEU A 101 ? 0.2473 0.2067 0.3746 -0.0095 -0.0194 0.0952  98  LEU B N   
765  C CA  . LEU A 101 ? 0.2746 0.2212 0.3967 -0.0070 -0.0235 0.1048  98  LEU B CA  
766  C C   . LEU A 101 ? 0.2852 0.2177 0.4078 -0.0194 -0.0267 0.1183  98  LEU B C   
767  O O   . LEU A 101 ? 0.3085 0.2401 0.4233 -0.0222 -0.0266 0.1307  98  LEU B O   
768  C CB  . LEU A 101 ? 0.2778 0.2101 0.4017 0.0060  -0.0303 0.0962  98  LEU B CB  
769  C CG  . LEU A 101 ? 0.2740 0.2228 0.3951 0.0169  -0.0263 0.0860  98  LEU B CG  
770  C CD1 . LEU A 101 ? 0.2808 0.2182 0.4059 0.0290  -0.0322 0.0755  98  LEU B CD1 
771  C CD2 . LEU A 101 ? 0.2506 0.2134 0.3644 0.0186  -0.0226 0.0934  98  LEU B CD2 
772  N N   . SER A 102 ? 0.3143 0.2360 0.4447 -0.0277 -0.0300 0.1165  99  SER B N   
773  C CA  . SER A 102 ? 0.3592 0.2690 0.4905 -0.0429 -0.0324 0.1297  99  SER B CA  
774  C C   . SER A 102 ? 0.3366 0.2705 0.4650 -0.0548 -0.0227 0.1393  99  SER B C   
775  O O   . SER A 102 ? 0.3633 0.2910 0.4850 -0.0642 -0.0231 0.1540  99  SER B O   
776  C CB  . SER A 102 ? 0.4238 0.3198 0.5651 -0.0508 -0.0377 0.1247  99  SER B CB  
777  O OG  . SER A 102 ? 0.5208 0.3869 0.6623 -0.0425 -0.0483 0.1202  99  SER B OG  
778  N N   . LEU A 103 ? 0.3047 0.2651 0.4380 -0.0546 -0.0145 0.1308  100 LEU B N   
779  C CA  . LEU A 103 ? 0.3032 0.2901 0.4350 -0.0631 -0.0042 0.1363  100 LEU B CA  
780  C C   . LEU A 103 ? 0.3033 0.2951 0.4206 -0.0596 -0.0008 0.1444  100 LEU B C   
781  O O   . LEU A 103 ? 0.3115 0.3119 0.4225 -0.0703 0.0041  0.1558  100 LEU B O   
782  C CB  . LEU A 103 ? 0.2620 0.2736 0.4016 -0.0584 0.0021  0.1235  100 LEU B CB  
783  C CG  . LEU A 103 ? 0.2578 0.2717 0.4123 -0.0634 -0.0008 0.1158  100 LEU B CG  
784  C CD1 . LEU A 103 ? 0.2494 0.2862 0.4091 -0.0563 0.0041  0.1047  100 LEU B CD1 
785  C CD2 . LEU A 103 ? 0.2792 0.2970 0.4428 -0.0815 0.0002  0.1243  100 LEU B CD2 
786  N N   . LEU A 104 ? 0.2954 0.2828 0.4072 -0.0453 -0.0035 0.1384  101 LEU B N   
787  C CA  . LEU A 104 ? 0.3061 0.2981 0.4048 -0.0409 -0.0020 0.1444  101 LEU B CA  
788  C C   . LEU A 104 ? 0.3276 0.3004 0.4181 -0.0463 -0.0087 0.1601  101 LEU B C   
789  O O   . LEU A 104 ? 0.3379 0.3198 0.4172 -0.0532 -0.0048 0.1706  101 LEU B O   
790  C CB  . LEU A 104 ? 0.2995 0.2916 0.3974 -0.0257 -0.0043 0.1335  101 LEU B CB  
791  C CG  . LEU A 104 ? 0.2850 0.2960 0.3859 -0.0209 0.0023  0.1208  101 LEU B CG  
792  C CD1 . LEU A 104 ? 0.2954 0.3018 0.3965 -0.0083 -0.0015 0.1110  101 LEU B CD1 
793  C CD2 . LEU A 104 ? 0.2859 0.3173 0.3783 -0.0230 0.0105  0.1223  101 LEU B CD2 
794  N N   . GLU A 105 ? 0.3452 0.2914 0.4406 -0.0435 -0.0189 0.1613  102 GLU B N   
795  C CA  . GLU A 105 ? 0.4132 0.3355 0.5013 -0.0468 -0.0279 0.1761  102 GLU B CA  
796  C C   . GLU A 105 ? 0.4141 0.3334 0.4988 -0.0665 -0.0258 0.1908  102 GLU B C   
797  O O   . GLU A 105 ? 0.4089 0.3244 0.4803 -0.0733 -0.0271 0.2063  102 GLU B O   
798  C CB  . GLU A 105 ? 0.4618 0.3556 0.5574 -0.0362 -0.0398 0.1706  102 GLU B CB  
799  C CG  . GLU A 105 ? 0.5502 0.4235 0.6380 -0.0293 -0.0504 0.1816  102 GLU B CG  
800  C CD  . GLU A 105 ? 0.5399 0.4314 0.6209 -0.0179 -0.0486 0.1801  102 GLU B CD  
801  O OE1 . GLU A 105 ? 0.5487 0.4285 0.6205 -0.0174 -0.0561 0.1938  102 GLU B OE1 
802  O OE2 . GLU A 105 ? 0.5054 0.4204 0.5892 -0.0107 -0.0411 0.1671  102 GLU B OE2 
803  N N   . LYS A 106 ? 0.4081 0.3300 0.5041 -0.0763 -0.0229 0.1862  103 LYS B N   
804  C CA  . LYS A 106 ? 0.4441 0.3638 0.5397 -0.0966 -0.0211 0.1993  103 LYS B CA  
805  C C   . LYS A 106 ? 0.4191 0.3723 0.5083 -0.1076 -0.0077 0.2049  103 LYS B C   
806  O O   . LYS A 106 ? 0.4258 0.3772 0.5066 -0.1240 -0.0063 0.2210  103 LYS B O   
807  C CB  . LYS A 106 ? 0.5162 0.4319 0.6278 -0.1050 -0.0223 0.1921  103 LYS B CB  
808  C CG  . LYS A 106 ? 0.5913 0.4692 0.7088 -0.1052 -0.0358 0.1914  103 LYS B CG  
809  C CD  . LYS A 106 ? 0.6203 0.4994 0.7510 -0.1214 -0.0354 0.1892  103 LYS B CD  
810  C CE  . LYS A 106 ? 0.6717 0.5588 0.7990 -0.1449 -0.0304 0.2068  103 LYS B CE  
811  N NZ  . LYS A 106 ? 0.6752 0.5465 0.8123 -0.1627 -0.0360 0.2102  103 LYS B NZ  
812  N N   . PHE A 107 ? 0.3688 0.3517 0.4622 -0.1001 0.0021  0.1918  104 PHE B N   
813  C CA  . PHE A 107 ? 0.3613 0.3777 0.4522 -0.1093 0.0154  0.1931  104 PHE B CA  
814  C C   . PHE A 107 ? 0.3514 0.3849 0.4300 -0.0989 0.0212  0.1889  104 PHE B C   
815  O O   . PHE A 107 ? 0.3670 0.4135 0.4320 -0.1067 0.0272  0.1982  104 PHE B O   
816  C CB  . PHE A 107 ? 0.3358 0.3737 0.4455 -0.1112 0.0217  0.1801  104 PHE B CB  
817  C CG  . PHE A 107 ? 0.3624 0.3884 0.4849 -0.1246 0.0168  0.1838  104 PHE B CG  
818  C CD1 . PHE A 107 ? 0.3845 0.4186 0.5066 -0.1454 0.0214  0.1971  104 PHE B CD1 
819  C CD2 . PHE A 107 ? 0.3569 0.3642 0.4909 -0.1176 0.0077  0.1738  104 PHE B CD2 
820  C CE1 . PHE A 107 ? 0.4182 0.4405 0.5523 -0.1596 0.0162  0.2008  104 PHE B CE1 
821  C CE2 . PHE A 107 ? 0.3921 0.3870 0.5371 -0.1307 0.0023  0.1765  104 PHE B CE2 
822  C CZ  . PHE A 107 ? 0.4055 0.4076 0.5513 -0.1521 0.0063  0.1901  104 PHE B CZ  
823  N N   . LEU A 108 ? 0.3182 0.3543 0.4013 -0.0826 0.0202  0.1744  105 LEU B N   
824  C CA  . LEU A 108 ? 0.3054 0.3634 0.3816 -0.0747 0.0278  0.1662  105 LEU B CA  
825  C C   . LEU A 108 ? 0.3220 0.3739 0.3797 -0.0712 0.0247  0.1744  105 LEU B C   
826  O O   . LEU A 108 ? 0.3393 0.4091 0.3848 -0.0759 0.0321  0.1774  105 LEU B O   
827  C CB  . LEU A 108 ? 0.2833 0.3447 0.3698 -0.0610 0.0274  0.1493  105 LEU B CB  
828  C CG  . LEU A 108 ? 0.2739 0.3454 0.3781 -0.0637 0.0302  0.1405  105 LEU B CG  
829  C CD1 . LEU A 108 ? 0.2618 0.3301 0.3732 -0.0505 0.0268  0.1264  105 LEU B CD1 
830  C CD2 . LEU A 108 ? 0.2806 0.3820 0.3879 -0.0708 0.0418  0.1387  105 LEU B CD2 
831  N N   . ILE A 109 ? 0.3394 0.3678 0.3954 -0.0629 0.0135  0.1772  106 ILE B N   
832  C CA  . ILE A 109 ? 0.3507 0.3738 0.3912 -0.0582 0.0084  0.1847  106 ILE B CA  
833  C C   . ILE A 109 ? 0.3881 0.4086 0.4136 -0.0724 0.0083  0.2033  106 ILE B C   
834  O O   . ILE A 109 ? 0.3934 0.4299 0.4039 -0.0749 0.0133  0.2063  106 ILE B O   
835  C CB  . ILE A 109 ? 0.3565 0.3577 0.4015 -0.0450 -0.0037 0.1827  106 ILE B CB  
836  C CG1 . ILE A 109 ? 0.3216 0.3303 0.3768 -0.0323 -0.0021 0.1651  106 ILE B CG1 
837  C CG2 . ILE A 109 ? 0.3656 0.3610 0.3964 -0.0416 -0.0111 0.1935  106 ILE B CG2 
838  C CD1 . ILE A 109 ? 0.3291 0.3192 0.3937 -0.0204 -0.0118 0.1597  106 ILE B CD1 
839  N N   . PRO A 110 ? 0.4005 0.4013 0.4278 -0.0828 0.0028  0.2160  107 PRO B N   
840  C CA  . PRO A 110 ? 0.4620 0.4584 0.4718 -0.0971 0.0017  0.2358  107 PRO B CA  
841  C C   . PRO A 110 ? 0.4739 0.5000 0.4745 -0.1116 0.0160  0.2387  107 PRO B C   
842  O O   . PRO A 110 ? 0.5089 0.5364 0.4899 -0.1215 0.0161  0.2537  107 PRO B O   
843  C CB  . PRO A 110 ? 0.4747 0.4411 0.4905 -0.1057 -0.0076 0.2472  107 PRO B CB  
844  C CG  . PRO A 110 ? 0.4532 0.4174 0.4913 -0.0997 -0.0070 0.2311  107 PRO B CG  
845  C CD  . PRO A 110 ? 0.3991 0.3788 0.4427 -0.0823 -0.0037 0.2130  107 PRO B CD  
846  N N   . ASN A 111 ? 0.4563 0.5058 0.4707 -0.1129 0.0274  0.2250  108 ASN B N   
847  C CA  . ASN A 111 ? 0.4645 0.5457 0.4736 -0.1251 0.0419  0.2251  108 ASN B CA  
848  C C   . ASN A 111 ? 0.4155 0.5217 0.4188 -0.1150 0.0504  0.2110  108 ASN B C   
849  O O   . ASN A 111 ? 0.3930 0.5263 0.3898 -0.1236 0.0626  0.2100  108 ASN B O   
850  C CB  . ASN A 111 ? 0.4840 0.5764 0.5125 -0.1354 0.0484  0.2215  108 ASN B CB  
851  C CG  . ASN A 111 ? 0.5464 0.6140 0.5764 -0.1498 0.0404  0.2379  108 ASN B CG  
852  O OD1 . ASN A 111 ? 0.6402 0.6987 0.6524 -0.1627 0.0381  0.2564  108 ASN B OD1 
853  N ND2 . ASN A 111 ? 0.6021 0.6562 0.6517 -0.1485 0.0350  0.2319  108 ASN B ND2 
854  N N   . ALA A 112 ? 0.3775 0.4749 0.3811 -0.0985 0.0442  0.2012  109 ALA B N   
855  C CA  . ALA A 112 ? 0.3663 0.4831 0.3648 -0.0891 0.0507  0.1871  109 ALA B CA  
856  C C   . ALA A 112 ? 0.4103 0.5376 0.3837 -0.0957 0.0537  0.1958  109 ALA B C   
857  O O   . ALA A 112 ? 0.4353 0.5455 0.3953 -0.0960 0.0436  0.2085  109 ALA B O   
858  C CB  . ALA A 112 ? 0.3380 0.4414 0.3433 -0.0725 0.0426  0.1764  109 ALA B CB  
859  N N   . SER A 113 ? 0.4035 0.5588 0.3711 -0.1025 0.0673  0.1904  110 SER B N   
860  C CA  . SER A 113 ? 0.4189 0.5894 0.3614 -0.1108 0.0728  0.1969  110 SER B CA  
861  C C   . SER A 113 ? 0.3970 0.5775 0.3280 -0.1002 0.0745  0.1832  110 SER B C   
862  O O   . SER A 113 ? 0.4004 0.5940 0.3090 -0.1066 0.0787  0.1868  110 SER B O   
863  C CB  . SER A 113 ? 0.4618 0.6593 0.4037 -0.1256 0.0874  0.1987  110 SER B CB  
864  O OG  . SER A 113 ? 0.4379 0.6600 0.3925 -0.1184 0.0987  0.1784  110 SER B OG  
865  N N   . GLN A 114 ? 0.3731 0.5471 0.3176 -0.0855 0.0709  0.1682  111 GLN B N   
866  C CA  . GLN A 114 ? 0.3716 0.5508 0.3072 -0.0758 0.0710  0.1547  111 GLN B CA  
867  C C   . GLN A 114 ? 0.3546 0.5119 0.2963 -0.0650 0.0578  0.1542  111 GLN B C   
868  O O   . GLN A 114 ? 0.3254 0.4685 0.2853 -0.0607 0.0527  0.1549  111 GLN B O   
869  C CB  . GLN A 114 ? 0.3938 0.5879 0.3432 -0.0687 0.0806  0.1351  111 GLN B CB  
870  C CG  . GLN A 114 ? 0.4286 0.6506 0.3747 -0.0763 0.0954  0.1301  111 GLN B CG  
871  C CD  . GLN A 114 ? 0.5006 0.7373 0.4206 -0.0801 0.1007  0.1277  111 GLN B CD  
872  O OE1 . GLN A 114 ? 0.5506 0.8075 0.4588 -0.0913 0.1103  0.1325  111 GLN B OE1 
873  N NE2 . GLN A 114 ? 0.5256 0.7532 0.4352 -0.0719 0.0943  0.1202  111 GLN B NE2 
874  N N   . ALA A 115 ? 0.3572 0.5141 0.2845 -0.0608 0.0528  0.1514  112 ALA B N   
875  C CA  . ALA A 115 ? 0.3669 0.5085 0.3009 -0.0510 0.0415  0.1494  112 ALA B CA  
876  C C   . ALA A 115 ? 0.3472 0.4854 0.3002 -0.0416 0.0433  0.1343  112 ALA B C   
877  O O   . ALA A 115 ? 0.3351 0.4595 0.3013 -0.0356 0.0358  0.1353  112 ALA B O   
878  C CB  . ALA A 115 ? 0.4072 0.5529 0.3237 -0.0495 0.0364  0.1477  112 ALA B CB  
879  N N   . GLU A 116 ? 0.3353 0.4858 0.2894 -0.0403 0.0528  0.1206  113 GLU B N   
880  C CA  . GLU A 116 ? 0.3305 0.4764 0.3007 -0.0318 0.0536  0.1074  113 GLU B CA  
881  C C   . GLU A 116 ? 0.2945 0.4312 0.2842 -0.0305 0.0515  0.1111  113 GLU B C   
882  O O   . GLU A 116 ? 0.2771 0.4022 0.2767 -0.0237 0.0457  0.1073  113 GLU B O   
883  C CB  . GLU A 116 ? 0.3557 0.5146 0.3269 -0.0295 0.0634  0.0929  113 GLU B CB  
884  C CG  . GLU A 116 ? 0.4280 0.5909 0.3830 -0.0275 0.0642  0.0828  113 GLU B CG  
885  C CD  . GLU A 116 ? 0.4707 0.6398 0.4286 -0.0215 0.0709  0.0655  113 GLU B CD  
886  O OE1 . GLU A 116 ? 0.5493 0.7196 0.5238 -0.0167 0.0744  0.0595  113 GLU B OE1 
887  O OE2 . GLU A 116 ? 0.4346 0.6060 0.3770 -0.0212 0.0715  0.0577  113 GLU B OE2 
888  N N   A SER A 117 ? 0.2768 0.4199 0.2708 -0.0379 0.0566  0.1182  114 SER B N   
889  N N   B SER A 117 ? 0.2982 0.4413 0.2923 -0.0379 0.0566  0.1181  114 SER B N   
890  C CA  A SER A 117 ? 0.2541 0.3890 0.2660 -0.0385 0.0545  0.1214  114 SER B CA  
891  C CA  B SER A 117 ? 0.2893 0.4242 0.3013 -0.0385 0.0545  0.1214  114 SER B CA  
892  C C   A SER A 117 ? 0.2594 0.3743 0.2727 -0.0376 0.0436  0.1320  114 SER B C   
893  C C   B SER A 117 ? 0.2777 0.3926 0.2910 -0.0375 0.0436  0.1320  114 SER B C   
894  O O   A SER A 117 ? 0.2482 0.3517 0.2753 -0.0324 0.0389  0.1289  114 SER B O   
895  O O   B SER A 117 ? 0.2654 0.3688 0.2925 -0.0324 0.0389  0.1289  114 SER B O   
896  C CB  A SER A 117 ? 0.2511 0.4000 0.2680 -0.0485 0.0627  0.1259  114 SER B CB  
897  C CB  B SER A 117 ? 0.3095 0.4581 0.3257 -0.0487 0.0626  0.1264  114 SER B CB  
898  O OG  A SER A 117 ? 0.2481 0.3973 0.2523 -0.0599 0.0627  0.1414  114 SER B OG  
899  O OG  B SER A 117 ? 0.3221 0.4923 0.3368 -0.0482 0.0730  0.1154  114 SER B OG  
900  N N   . LYS A 118 ? 0.2802 0.3915 0.2789 -0.0418 0.0392  0.1438  115 LYS B N   
901  C CA  . LYS A 118 ? 0.3006 0.3929 0.3009 -0.0391 0.0278  0.1537  115 LYS B CA  
902  C C   . LYS A 118 ? 0.2844 0.3701 0.2919 -0.0272 0.0216  0.1441  115 LYS B C   
903  O O   . LYS A 118 ? 0.3069 0.3791 0.3269 -0.0222 0.0159  0.1438  115 LYS B O   
904  C CB  . LYS A 118 ? 0.3442 0.4339 0.3267 -0.0444 0.0226  0.1682  115 LYS B CB  
905  C CG  . LYS A 118 ? 0.3991 0.4668 0.3867 -0.0415 0.0102  0.1794  115 LYS B CG  
906  C CD  . LYS A 118 ? 0.4582 0.5209 0.4282 -0.0468 0.0033  0.1959  115 LYS B CD  
907  C CE  . LYS A 118 ? 0.4652 0.5049 0.4414 -0.0403 -0.0107 0.2049  115 LYS B CE  
908  N NZ  . LYS A 118 ? 0.4968 0.5298 0.4550 -0.0465 -0.0182 0.2230  115 LYS B NZ  
909  N N   . VAL A 119 ? 0.2601 0.3558 0.2599 -0.0236 0.0236  0.1356  116 VAL B N   
910  C CA  . VAL A 119 ? 0.2458 0.3386 0.2518 -0.0148 0.0195  0.1260  116 VAL B CA  
911  C C   . VAL A 119 ? 0.2215 0.3099 0.2426 -0.0108 0.0221  0.1167  116 VAL B C   
912  O O   . VAL A 119 ? 0.2320 0.3124 0.2622 -0.0047 0.0168  0.1140  116 VAL B O   
913  C CB  . VAL A 119 ? 0.2453 0.3489 0.2396 -0.0142 0.0215  0.1182  116 VAL B CB  
914  C CG1 . VAL A 119 ? 0.2647 0.3664 0.2652 -0.0078 0.0184  0.1084  116 VAL B CG1 
915  C CG2 . VAL A 119 ? 0.2873 0.3957 0.2661 -0.0175 0.0170  0.1265  116 VAL B CG2 
916  N N   . PHE A 120 ? 0.2161 0.3118 0.2398 -0.0136 0.0300  0.1111  117 PHE B N   
917  C CA  . PHE A 120 ? 0.2043 0.2968 0.2415 -0.0099 0.0314  0.1027  117 PHE B CA  
918  C C   . PHE A 120 ? 0.1922 0.2723 0.2409 -0.0093 0.0261  0.1076  117 PHE B C   
919  O O   . PHE A 120 ? 0.1773 0.2505 0.2341 -0.0037 0.0228  0.1014  117 PHE B O   
920  C CB  . PHE A 120 ? 0.2102 0.3147 0.2499 -0.0130 0.0398  0.0978  117 PHE B CB  
921  C CG  . PHE A 120 ? 0.2448 0.3476 0.2985 -0.0088 0.0402  0.0894  117 PHE B CG  
922  C CD1 . PHE A 120 ? 0.2531 0.3515 0.3196 -0.0110 0.0383  0.0925  117 PHE B CD1 
923  C CD2 . PHE A 120 ? 0.2529 0.3573 0.3060 -0.0030 0.0416  0.0786  117 PHE B CD2 
924  C CE1 . PHE A 120 ? 0.2592 0.3570 0.3374 -0.0072 0.0376  0.0847  117 PHE B CE1 
925  C CE2 . PHE A 120 ? 0.2846 0.3868 0.3491 0.0012  0.0405  0.0719  117 PHE B CE2 
926  C CZ  . PHE A 120 ? 0.2610 0.3610 0.3379 -0.0008 0.0384  0.0749  117 PHE B CZ  
927  N N   . TYR A 121 ? 0.2026 0.2791 0.2510 -0.0157 0.0251  0.1184  118 TYR B N   
928  C CA  . TYR A 121 ? 0.2040 0.2658 0.2625 -0.0163 0.0194  0.1231  118 TYR B CA  
929  C C   . TYR A 121 ? 0.2003 0.2489 0.2591 -0.0091 0.0104  0.1252  118 TYR B C   
930  O O   . TYR A 121 ? 0.2273 0.2644 0.2963 -0.0052 0.0061  0.1219  118 TYR B O   
931  C CB  . TYR A 121 ? 0.2266 0.2869 0.2836 -0.0272 0.0208  0.1351  118 TYR B CB  
932  C CG  . TYR A 121 ? 0.2304 0.3072 0.2916 -0.0347 0.0301  0.1323  118 TYR B CG  
933  C CD1 . TYR A 121 ? 0.2176 0.2996 0.2921 -0.0318 0.0326  0.1216  118 TYR B CD1 
934  C CD2 . TYR A 121 ? 0.2581 0.3471 0.3099 -0.0446 0.0364  0.1404  118 TYR B CD2 
935  C CE1 . TYR A 121 ? 0.2155 0.3153 0.2967 -0.0374 0.0406  0.1185  118 TYR B CE1 
936  C CE2 . TYR A 121 ? 0.2523 0.3610 0.3096 -0.0506 0.0460  0.1364  118 TYR B CE2 
937  C CZ  . TYR A 121 ? 0.2406 0.3550 0.3141 -0.0465 0.0478  0.1252  118 TYR B CZ  
938  O OH  . TYR A 121 ? 0.2405 0.3764 0.3225 -0.0515 0.0565  0.1210  118 TYR B OH  
939  N N   . LEU A 122 ? 0.2207 0.2714 0.2693 -0.0076 0.0073  0.1308  119 LEU B N   
940  C CA  . LEU A 122 ? 0.2170 0.2594 0.2683 0.0009  -0.0014 0.1314  119 LEU B CA  
941  C C   . LEU A 122 ? 0.1977 0.2452 0.2557 0.0087  -0.0006 0.1182  119 LEU B C   
942  O O   . LEU A 122 ? 0.2119 0.2517 0.2789 0.0157  -0.0056 0.1145  119 LEU B O   
943  C CB  . LEU A 122 ? 0.2399 0.2862 0.2793 0.0006  -0.0058 0.1404  119 LEU B CB  
944  C CG  . LEU A 122 ? 0.2756 0.3116 0.3076 -0.0062 -0.0101 0.1562  119 LEU B CG  
945  C CD1 . LEU A 122 ? 0.2976 0.3412 0.3151 -0.0069 -0.0140 0.1641  119 LEU B CD1 
946  C CD2 . LEU A 122 ? 0.2914 0.3057 0.3335 -0.0015 -0.0195 0.1612  119 LEU B CD2 
947  N N   . LYS A 123 ? 0.1949 0.2544 0.2481 0.0071  0.0058  0.1108  120 LYS B N   
948  C CA  . LYS A 123 ? 0.1804 0.2433 0.2379 0.0117  0.0072  0.0996  120 LYS B CA  
949  C C   . LYS A 123 ? 0.1820 0.2367 0.2498 0.0135  0.0073  0.0943  120 LYS B C   
950  O O   . LYS A 123 ? 0.1699 0.2221 0.2433 0.0190  0.0048  0.0881  120 LYS B O   
951  C CB  . LYS A 123 ? 0.1917 0.2641 0.2416 0.0088  0.0132  0.0937  120 LYS B CB  
952  C CG  . LYS A 123 ? 0.1951 0.2690 0.2461 0.0117  0.0139  0.0840  120 LYS B CG  
953  C CD  . LYS A 123 ? 0.1971 0.2749 0.2410 0.0090  0.0188  0.0785  120 LYS B CD  
954  C CE  . LYS A 123 ? 0.1757 0.2493 0.2225 0.0111  0.0190  0.0710  120 LYS B CE  
955  N NZ  . LYS A 123 ? 0.1762 0.2444 0.2322 0.0125  0.0190  0.0699  120 LYS B NZ  
956  N N   . MET A 124 ? 0.2030 0.2554 0.2736 0.0083  0.0104  0.0963  121 MET B N   
957  C CA  A MET A 124 ? 0.1884 0.2336 0.2688 0.0088  0.0093  0.0918  121 MET B CA  
958  C CA  B MET A 124 ? 0.1926 0.2378 0.2730 0.0088  0.0093  0.0918  121 MET B CA  
959  C C   . MET A 124 ? 0.1903 0.2217 0.2772 0.0125  0.0025  0.0934  121 MET B C   
960  O O   . MET A 124 ? 0.1815 0.2080 0.2741 0.0169  0.0003  0.0856  121 MET B O   
961  C CB  A MET A 124 ? 0.1942 0.2427 0.2781 0.0015  0.0133  0.0948  121 MET B CB  
962  C CB  B MET A 124 ? 0.2045 0.2526 0.2888 0.0015  0.0132  0.0946  121 MET B CB  
963  C CG  A MET A 124 ? 0.1893 0.2354 0.2828 0.0014  0.0128  0.0882  121 MET B CG  
964  C CG  B MET A 124 ? 0.2061 0.2513 0.3002 0.0019  0.0123  0.0876  121 MET B CG  
965  S SD  A MET A 124 ? 0.1961 0.2562 0.2941 -0.0062 0.0195  0.0897  121 MET B SD  
966  S SD  B MET A 124 ? 0.2309 0.2827 0.3341 -0.0070 0.0157  0.0904  121 MET B SD  
967  C CE  A MET A 124 ? 0.1785 0.2358 0.2877 -0.0036 0.0160  0.0804  121 MET B CE  
968  C CE  B MET A 124 ? 0.2162 0.2825 0.3085 -0.0093 0.0229  0.0945  121 MET B CE  
969  N N   . LYS A 125 ? 0.2083 0.2326 0.2934 0.0114  -0.0015 0.1032  122 LYS B N   
970  C CA  . LYS A 125 ? 0.2100 0.2185 0.3013 0.0167  -0.0093 0.1045  122 LYS B CA  
971  C C   . LYS A 125 ? 0.2113 0.2239 0.3054 0.0273  -0.0117 0.0956  122 LYS B C   
972  O O   . LYS A 125 ? 0.2207 0.2247 0.3222 0.0333  -0.0152 0.0883  122 LYS B O   
973  C CB  . LYS A 125 ? 0.2185 0.2177 0.3053 0.0134  -0.0142 0.1183  122 LYS B CB  
974  C CG  . LYS A 125 ? 0.2242 0.2031 0.3170 0.0196  -0.0240 0.1213  122 LYS B CG  
975  C CD  . LYS A 125 ? 0.2594 0.2275 0.3451 0.0148  -0.0295 0.1373  122 LYS B CD  
976  C CE  . LYS A 125 ? 0.2777 0.2213 0.3692 0.0216  -0.0410 0.1410  122 LYS B CE  
977  N NZ  . LYS A 125 ? 0.3187 0.2498 0.4011 0.0154  -0.0471 0.1587  122 LYS B NZ  
978  N N   . GLY A 126 ? 0.2031 0.2295 0.2914 0.0291  -0.0099 0.0957  123 GLY B N   
979  C CA  . GLY A 126 ? 0.2085 0.2444 0.2998 0.0368  -0.0106 0.0874  123 GLY B CA  
980  C C   . GLY A 126 ? 0.1972 0.2361 0.2907 0.0374  -0.0065 0.0760  123 GLY B C   
981  O O   . GLY A 126 ? 0.1790 0.2177 0.2785 0.0443  -0.0085 0.0684  123 GLY B O   
982  N N   . ASP A 127 ? 0.1822 0.2235 0.2708 0.0308  -0.0014 0.0751  124 ASP B N   
983  C CA  . ASP A 127 ? 0.1821 0.2252 0.2704 0.0304  0.0013  0.0663  124 ASP B CA  
984  C C   . ASP A 127 ? 0.1839 0.2157 0.2793 0.0331  -0.0020 0.0613  124 ASP B C   
985  O O   . ASP A 127 ? 0.1876 0.2219 0.2833 0.0368  -0.0019 0.0526  124 ASP B O   
986  C CB  . ASP A 127 ? 0.1707 0.2168 0.2539 0.0241  0.0056  0.0673  124 ASP B CB  
987  C CG  . ASP A 127 ? 0.1818 0.2374 0.2563 0.0216  0.0091  0.0687  124 ASP B CG  
988  O OD1 . ASP A 127 ? 0.1792 0.2414 0.2504 0.0233  0.0088  0.0669  124 ASP B OD1 
989  O OD2 . ASP A 127 ? 0.1609 0.2181 0.2323 0.0177  0.0122  0.0706  124 ASP B OD2 
990  N N   . TYR A 128 ? 0.1845 0.2045 0.2844 0.0300  -0.0047 0.0665  125 TYR B N   
991  C CA  . TYR A 128 ? 0.1934 0.2010 0.2995 0.0307  -0.0085 0.0613  125 TYR B CA  
992  C C   . TYR A 128 ? 0.2044 0.2037 0.3154 0.0396  -0.0136 0.0565  125 TYR B C   
993  O O   . TYR A 128 ? 0.2170 0.2110 0.3304 0.0431  -0.0154 0.0466  125 TYR B O   
994  C CB  . TYR A 128 ? 0.1875 0.1876 0.2973 0.0223  -0.0092 0.0675  125 TYR B CB  
995  C CG  . TYR A 128 ? 0.1799 0.1910 0.2882 0.0175  -0.0047 0.0649  125 TYR B CG  
996  C CD1 . TYR A 128 ? 0.1830 0.2061 0.2864 0.0148  0.0005  0.0692  125 TYR B CD1 
997  C CD2 . TYR A 128 ? 0.1945 0.2040 0.3056 0.0169  -0.0064 0.0572  125 TYR B CD2 
998  C CE1 . TYR A 128 ? 0.1770 0.2091 0.2798 0.0126  0.0037  0.0660  125 TYR B CE1 
999  C CE2 . TYR A 128 ? 0.1732 0.1927 0.2834 0.0141  -0.0038 0.0552  125 TYR B CE2 
1000 C CZ  . TYR A 128 ? 0.1777 0.2080 0.2841 0.0129  0.0012  0.0593  125 TYR B CZ  
1001 O OH  . TYR A 128 ? 0.1833 0.2219 0.2896 0.0121  0.0029  0.0567  125 TYR B OH  
1002 N N   . TYR A 129 ? 0.2429 0.2408 0.3551 0.0438  -0.0164 0.0627  126 TYR B N   
1003 C CA  . TYR A 129 ? 0.2258 0.2199 0.3441 0.0548  -0.0212 0.0569  126 TYR B CA  
1004 C C   . TYR A 129 ? 0.2025 0.2153 0.3198 0.0600  -0.0166 0.0459  126 TYR B C   
1005 O O   . TYR A 129 ? 0.2082 0.2199 0.3306 0.0679  -0.0183 0.0356  126 TYR B O   
1006 C CB  . TYR A 129 ? 0.2458 0.2356 0.3664 0.0592  -0.0267 0.0664  126 TYR B CB  
1007 C CG  . TYR A 129 ? 0.2742 0.2392 0.3973 0.0570  -0.0340 0.0748  126 TYR B CG  
1008 C CD1 . TYR A 129 ? 0.2859 0.2319 0.4165 0.0641  -0.0406 0.0677  126 TYR B CD1 
1009 C CD2 . TYR A 129 ? 0.2728 0.2329 0.3899 0.0477  -0.0347 0.0897  126 TYR B CD2 
1010 C CE1 . TYR A 129 ? 0.3238 0.2437 0.4562 0.0612  -0.0485 0.0759  126 TYR B CE1 
1011 C CE2 . TYR A 129 ? 0.3037 0.2403 0.4219 0.0438  -0.0416 0.0989  126 TYR B CE2 
1012 C CZ  . TYR A 129 ? 0.3355 0.2508 0.4615 0.0504  -0.0490 0.0924  126 TYR B CZ  
1013 O OH  . TYR A 129 ? 0.3497 0.2391 0.4763 0.0453  -0.0565 0.1015  126 TYR B OH  
1014 N N   . ARG A 130 ? 0.1739 0.2033 0.2844 0.0551  -0.0109 0.0479  127 ARG B N   
1015 C CA  . ARG A 130 ? 0.1709 0.2177 0.2788 0.0569  -0.0062 0.0393  127 ARG B CA  
1016 C C   . ARG A 130 ? 0.1788 0.2235 0.2832 0.0554  -0.0040 0.0296  127 ARG B C   
1017 O O   . ARG A 130 ? 0.1611 0.2151 0.2664 0.0602  -0.0022 0.0198  127 ARG B O   
1018 C CB  . ARG A 130 ? 0.1710 0.2311 0.2708 0.0500  -0.0017 0.0444  127 ARG B CB  
1019 C CG  . ARG A 130 ? 0.1651 0.2409 0.2599 0.0482  0.0033  0.0371  127 ARG B CG  
1020 C CD  . ARG A 130 ? 0.1377 0.2258 0.2262 0.0423  0.0060  0.0420  127 ARG B CD  
1021 N NE  . ARG A 130 ? 0.1417 0.2211 0.2223 0.0352  0.0071  0.0482  127 ARG B NE  
1022 C CZ  . ARG A 130 ? 0.1464 0.2217 0.2193 0.0300  0.0095  0.0466  127 ARG B CZ  
1023 N NH1 . ARG A 130 ? 0.1440 0.2225 0.2129 0.0290  0.0112  0.0404  127 ARG B NH1 
1024 N NH2 . ARG A 130 ? 0.1374 0.2059 0.2062 0.0260  0.0100  0.0511  127 ARG B NH2 
1025 N N   . TYR A 131 ? 0.1716 0.2060 0.2726 0.0490  -0.0043 0.0322  128 TYR B N   
1026 C CA  . TYR A 131 ? 0.1794 0.2102 0.2771 0.0476  -0.0043 0.0238  128 TYR B CA  
1027 C C   . TYR A 131 ? 0.1953 0.2156 0.2994 0.0546  -0.0086 0.0150  128 TYR B C   
1028 O O   . TYR A 131 ? 0.2146 0.2395 0.3148 0.0569  -0.0073 0.0042  128 TYR B O   
1029 C CB  . TYR A 131 ? 0.1830 0.2071 0.2781 0.0398  -0.0049 0.0285  128 TYR B CB  
1030 C CG  . TYR A 131 ? 0.1849 0.2171 0.2744 0.0344  -0.0011 0.0357  128 TYR B CG  
1031 C CD1 . TYR A 131 ? 0.1691 0.2131 0.2513 0.0339  0.0027  0.0354  128 TYR B CD1 
1032 C CD2 . TYR A 131 ? 0.1828 0.2111 0.2748 0.0293  -0.0014 0.0423  128 TYR B CD2 
1033 C CE1 . TYR A 131 ? 0.1633 0.2113 0.2400 0.0293  0.0052  0.0410  128 TYR B CE1 
1034 C CE2 . TYR A 131 ? 0.1670 0.2022 0.2543 0.0258  0.0020  0.0470  128 TYR B CE2 
1035 C CZ  . TYR A 131 ? 0.1657 0.2090 0.2448 0.0261  0.0049  0.0460  128 TYR B CZ  
1036 O OH  . TYR A 131 ? 0.1529 0.2000 0.2266 0.0230  0.0074  0.0494  128 TYR B OH  
1037 N N   . LEU A 132 ? 0.2087 0.2144 0.3212 0.0578  -0.0139 0.0191  129 LEU B N   
1038 C CA  . LEU A 132 ? 0.2398 0.2330 0.3591 0.0664  -0.0191 0.0100  129 LEU B CA  
1039 C C   . LEU A 132 ? 0.2283 0.2370 0.3504 0.0770  -0.0166 0.0003  129 LEU B C   
1040 O O   . LEU A 132 ? 0.2337 0.2418 0.3567 0.0832  -0.0169 -0.0132 129 LEU B O   
1041 C CB  . LEU A 132 ? 0.2782 0.2505 0.4050 0.0676  -0.0263 0.0183  129 LEU B CB  
1042 C CG  . LEU A 132 ? 0.2934 0.2498 0.4199 0.0568  -0.0293 0.0257  129 LEU B CG  
1043 C CD1 . LEU A 132 ? 0.3037 0.2401 0.4357 0.0568  -0.0362 0.0363  129 LEU B CD1 
1044 C CD2 . LEU A 132 ? 0.3089 0.2555 0.4353 0.0552  -0.0319 0.0145  129 LEU B CD2 
1045 N N   . ALA A 133 ? 0.2252 0.2494 0.3487 0.0786  -0.0139 0.0063  130 ALA B N   
1046 C CA  . ALA A 133 ? 0.2239 0.2672 0.3529 0.0879  -0.0115 -0.0020 130 ALA B CA  
1047 C C   . ALA A 133 ? 0.2235 0.2858 0.3445 0.0849  -0.0039 -0.0125 130 ALA B C   
1048 O O   . ALA A 133 ? 0.2104 0.2871 0.3357 0.0928  -0.0013 -0.0242 130 ALA B O   
1049 C CB  . ALA A 133 ? 0.2250 0.2813 0.3572 0.0882  -0.0114 0.0076  130 ALA B CB  
1050 N N   . GLU A 134 ? 0.2121 0.2740 0.3209 0.0737  -0.0006 -0.0085 131 GLU B N   
1051 C CA  . GLU A 134 ? 0.2123 0.2880 0.3103 0.0692  0.0053  -0.0162 131 GLU B CA  
1052 C C   . GLU A 134 ? 0.2319 0.3040 0.3289 0.0748  0.0046  -0.0308 131 GLU B C   
1053 O O   . GLU A 134 ? 0.2500 0.3394 0.3404 0.0744  0.0103  -0.0396 131 GLU B O   
1054 C CB  . GLU A 134 ? 0.1993 0.2720 0.2845 0.0573  0.0068  -0.0085 131 GLU B CB  
1055 C CG  . GLU A 134 ? 0.1842 0.2628 0.2667 0.0510  0.0089  0.0030  131 GLU B CG  
1056 C CD  . GLU A 134 ? 0.1754 0.2471 0.2473 0.0417  0.0088  0.0099  131 GLU B CD  
1057 O OE1 . GLU A 134 ? 0.1899 0.2511 0.2580 0.0397  0.0062  0.0078  131 GLU B OE1 
1058 O OE2 . GLU A 134 ? 0.2078 0.2848 0.2759 0.0369  0.0109  0.0168  131 GLU B OE2 
1059 N N   . VAL A 135 ? 0.2462 0.2966 0.3488 0.0790  -0.0020 -0.0338 132 VAL B N   
1060 C CA  . VAL A 135 ? 0.2871 0.3311 0.3874 0.0838  -0.0036 -0.0488 132 VAL B CA  
1061 C C   . VAL A 135 ? 0.3320 0.3657 0.4461 0.0976  -0.0085 -0.0580 132 VAL B C   
1062 O O   . VAL A 135 ? 0.3651 0.3947 0.4778 0.1035  -0.0095 -0.0733 132 VAL B O   
1063 C CB  . VAL A 135 ? 0.2894 0.3155 0.3820 0.0747  -0.0081 -0.0461 132 VAL B CB  
1064 C CG1 . VAL A 135 ? 0.2692 0.3053 0.3501 0.0633  -0.0044 -0.0364 132 VAL B CG1 
1065 C CG2 . VAL A 135 ? 0.2894 0.2910 0.3915 0.0737  -0.0160 -0.0381 132 VAL B CG2 
1066 N N   . ALA A 136 ? 0.3287 0.3576 0.4550 0.1037  -0.0122 -0.0498 133 ALA B N   
1067 C CA  . ALA A 136 ? 0.3481 0.3604 0.4872 0.1170  -0.0196 -0.0566 133 ALA B CA  
1068 C C   . ALA A 136 ? 0.3551 0.3891 0.5017 0.1310  -0.0155 -0.0729 133 ALA B C   
1069 O O   . ALA A 136 ? 0.3051 0.3686 0.4500 0.1291  -0.0074 -0.0732 133 ALA B O   
1070 C CB  . ALA A 136 ? 0.3635 0.3627 0.5108 0.1178  -0.0260 -0.0407 133 ALA B CB  
1071 N N   . ALA A 137 ? 0.4075 0.4266 0.5635 0.1449  -0.0215 -0.0862 134 ALA B N   
1072 C CA  . ALA A 137 ? 0.4334 0.4712 0.6015 0.1619  -0.0193 -0.1023 134 ALA B CA  
1073 C C   . ALA A 137 ? 0.5128 0.5279 0.6979 0.1785  -0.0308 -0.1041 134 ALA B C   
1074 O O   . ALA A 137 ? 0.5029 0.4834 0.6880 0.1759  -0.0407 -0.0945 134 ALA B O   
1075 C CB  . ALA A 137 ? 0.4534 0.4994 0.6133 0.1640  -0.0137 -0.1230 134 ALA B CB  
1076 N N   . GLY A 138 ? 0.5503 0.5856 0.7506 0.1958  -0.0298 -0.1162 135 GLY B N   
1077 C CA  . GLY A 138 ? 0.6083 0.6223 0.8253 0.2153  -0.0413 -0.1229 135 GLY B CA  
1078 C C   . GLY A 138 ? 0.6228 0.6173 0.8471 0.2161  -0.0524 -0.1017 135 GLY B C   
1079 O O   . GLY A 138 ? 0.6566 0.6688 0.8782 0.2064  -0.0490 -0.0857 135 GLY B O   
1080 N N   . ASP A 139 ? 0.6741 0.6306 0.9059 0.2271  -0.0662 -0.1016 136 ASP B N   
1081 C CA  . ASP A 139 ? 0.6556 0.5902 0.8927 0.2284  -0.0783 -0.0812 136 ASP B CA  
1082 C C   . ASP A 139 ? 0.6049 0.5289 0.8258 0.2050  -0.0767 -0.0583 136 ASP B C   
1083 O O   . ASP A 139 ? 0.6067 0.5393 0.8273 0.2002  -0.0781 -0.0408 136 ASP B O   
1084 C CB  . ASP A 139 ? 0.6480 0.5448 0.8967 0.2464  -0.0939 -0.0869 136 ASP B CB  
1085 N N   . ASP A 140 ? 0.5935 0.5047 0.8011 0.1904  -0.0727 -0.0597 137 ASP B N   
1086 C CA  . ASP A 140 ? 0.5470 0.4501 0.7409 0.1690  -0.0704 -0.0415 137 ASP B CA  
1087 C C   . ASP A 140 ? 0.4908 0.4277 0.6787 0.1587  -0.0603 -0.0305 137 ASP B C   
1088 O O   . ASP A 140 ? 0.4264 0.3582 0.6079 0.1466  -0.0613 -0.0119 137 ASP B O   
1089 C CB  . ASP A 140 ? 0.5996 0.4919 0.7837 0.1593  -0.0671 -0.0515 137 ASP B CB  
1090 C CG  . ASP A 140 ? 0.6565 0.5429 0.8285 0.1382  -0.0643 -0.0368 137 ASP B CG  
1091 O OD1 . ASP A 140 ? 0.7015 0.5656 0.8734 0.1314  -0.0714 -0.0203 137 ASP B OD1 
1092 O OD2 . ASP A 140 ? 0.6864 0.5916 0.8493 0.1289  -0.0553 -0.0415 137 ASP B OD2 
1093 N N   . LYS A 141 ? 0.4501 0.4216 0.6392 0.1624  -0.0504 -0.0427 138 LYS B N   
1094 C CA  . LYS A 141 ? 0.4143 0.4168 0.5976 0.1526  -0.0411 -0.0347 138 LYS B CA  
1095 C C   . LYS A 141 ? 0.3946 0.4044 0.5847 0.1559  -0.0458 -0.0208 138 LYS B C   
1096 O O   . LYS A 141 ? 0.3265 0.3434 0.5082 0.1434  -0.0428 -0.0066 138 LYS B O   
1097 C CB  . LYS A 141 ? 0.4262 0.4640 0.6107 0.1564  -0.0306 -0.0502 138 LYS B CB  
1098 C CG  . LYS A 141 ? 0.4242 0.4900 0.5999 0.1432  -0.0211 -0.0422 138 LYS B CG  
1099 C CD  . LYS A 141 ? 0.4852 0.5832 0.6589 0.1433  -0.0104 -0.0566 138 LYS B CD  
1100 C CE  . LYS A 141 ? 0.4552 0.5712 0.6150 0.1270  -0.0016 -0.0495 138 LYS B CE  
1101 N NZ  . LYS A 141 ? 0.4437 0.5906 0.6100 0.1267  0.0026  -0.0468 138 LYS B NZ  
1102 N N   . LYS A 142 ? 0.4425 0.4527 0.6479 0.1735  -0.0533 -0.0261 139 LYS B N   
1103 C CA  . LYS A 142 ? 0.4519 0.4679 0.6644 0.1784  -0.0602 -0.0131 139 LYS B CA  
1104 C C   . LYS A 142 ? 0.3861 0.3748 0.5878 0.1666  -0.0669 0.0083  139 LYS B C   
1105 O O   . LYS A 142 ? 0.3511 0.3532 0.5471 0.1581  -0.0652 0.0214  139 LYS B O   
1106 C CB  . LYS A 142 ? 0.5138 0.5292 0.7456 0.2010  -0.0697 -0.0224 139 LYS B CB  
1107 C CG  . LYS A 142 ? 0.6250 0.6495 0.8654 0.2077  -0.0784 -0.0095 139 LYS B CG  
1108 C CD  . LYS A 142 ? 0.7545 0.7397 0.9920 0.2093  -0.0935 0.0076  139 LYS B CD  
1109 C CE  . LYS A 142 ? 0.7974 0.7889 1.0483 0.2243  -0.1057 0.0141  139 LYS B CE  
1110 N NZ  . LYS A 142 ? 0.7865 0.8157 1.0368 0.2178  -0.1005 0.0208  139 LYS B NZ  
1111 N N   . GLY A 143 ? 0.4028 0.3549 0.6010 0.1647  -0.0737 0.0111  140 GLY B N   
1112 C CA  . GLY A 143 ? 0.4010 0.3281 0.5885 0.1515  -0.0789 0.0308  140 GLY B CA  
1113 C C   . GLY A 143 ? 0.3742 0.3146 0.5476 0.1322  -0.0684 0.0393  140 GLY B C   
1114 O O   . GLY A 143 ? 0.3651 0.3061 0.5310 0.1232  -0.0692 0.0556  140 GLY B O   
1115 N N   . ILE A 144 ? 0.3420 0.2938 0.5116 0.1266  -0.0588 0.0276  141 ILE B N   
1116 C CA  . ILE A 144 ? 0.3108 0.2743 0.4684 0.1104  -0.0496 0.0333  141 ILE B CA  
1117 C C   . ILE A 144 ? 0.2682 0.2608 0.4230 0.1078  -0.0438 0.0385  141 ILE B C   
1118 O O   . ILE A 144 ? 0.2325 0.2277 0.3779 0.0962  -0.0410 0.0504  141 ILE B O   
1119 C CB  . ILE A 144 ? 0.3157 0.2819 0.4701 0.1071  -0.0432 0.0190  141 ILE B CB  
1120 C CG1 . ILE A 144 ? 0.3642 0.2988 0.5189 0.1047  -0.0496 0.0173  141 ILE B CG1 
1121 C CG2 . ILE A 144 ? 0.2992 0.2836 0.4430 0.0941  -0.0335 0.0218  141 ILE B CG2 
1122 C CD1 . ILE A 144 ? 0.3736 0.3082 0.5263 0.1048  -0.0463 0.0007  141 ILE B CD1 
1123 N N   . VAL A 145 ? 0.2515 0.2673 0.4141 0.1178  -0.0415 0.0282  142 VAL B N   
1124 C CA  . VAL A 145 ? 0.2422 0.2867 0.4036 0.1149  -0.0367 0.0315  142 VAL B CA  
1125 C C   . VAL A 145 ? 0.2497 0.2897 0.4101 0.1145  -0.0441 0.0471  142 VAL B C   
1126 O O   . VAL A 145 ? 0.2375 0.2882 0.3886 0.1041  -0.0403 0.0555  142 VAL B O   
1127 C CB  . VAL A 145 ? 0.2531 0.3253 0.4255 0.1254  -0.0331 0.0169  142 VAL B CB  
1128 C CG1 . VAL A 145 ? 0.2467 0.3486 0.4205 0.1226  -0.0303 0.0208  142 VAL B CG1 
1129 C CG2 . VAL A 145 ? 0.2401 0.3201 0.4079 0.1220  -0.0241 0.0031  142 VAL B CG2 
1130 N N   . ASP A 146 ? 0.3047 0.3282 0.4737 0.1257  -0.0552 0.0507  143 ASP B N   
1131 C CA  . ASP A 146 ? 0.3359 0.3516 0.5019 0.1252  -0.0640 0.0670  143 ASP B CA  
1132 C C   . ASP A 146 ? 0.3153 0.3147 0.4652 0.1090  -0.0623 0.0818  143 ASP B C   
1133 O O   . ASP A 146 ? 0.2945 0.3029 0.4357 0.1019  -0.0622 0.0929  143 ASP B O   
1134 C CB  . ASP A 146 ? 0.4117 0.4094 0.5897 0.1413  -0.0773 0.0677  143 ASP B CB  
1135 C CG  . ASP A 146 ? 0.4928 0.5143 0.6889 0.1590  -0.0802 0.0552  143 ASP B CG  
1136 O OD1 . ASP A 146 ? 0.4766 0.5325 0.6752 0.1567  -0.0722 0.0491  143 ASP B OD1 
1137 O OD2 . ASP A 146 ? 0.6142 0.6195 0.8226 0.1749  -0.0907 0.0512  143 ASP B OD2 
1138 N N   . GLN A 147 ? 0.3214 0.3003 0.4674 0.1023  -0.0600 0.0806  144 GLN B N   
1139 C CA  . GLN A 147 ? 0.3057 0.2735 0.4389 0.0865  -0.0569 0.0928  144 GLN B CA  
1140 C C   . GLN A 147 ? 0.2730 0.2646 0.3973 0.0762  -0.0461 0.0922  144 GLN B C   
1141 O O   . GLN A 147 ? 0.2734 0.2678 0.3874 0.0669  -0.0445 0.1036  144 GLN B O   
1142 C CB  . GLN A 147 ? 0.3253 0.2701 0.4588 0.0812  -0.0570 0.0901  144 GLN B CB  
1143 C CG  . GLN A 147 ? 0.3796 0.2925 0.5183 0.0868  -0.0688 0.0946  144 GLN B CG  
1144 C CD  . GLN A 147 ? 0.4138 0.3118 0.5441 0.0799  -0.0758 0.1147  144 GLN B CD  
1145 O OE1 . GLN A 147 ? 0.4083 0.3110 0.5277 0.0652  -0.0704 0.1256  144 GLN B OE1 
1146 N NE2 . GLN A 147 ? 0.4835 0.3667 0.6186 0.0912  -0.0879 0.1198  144 GLN B NE2 
1147 N N   . SER A 148 ? 0.2466 0.2548 0.3738 0.0780  -0.0388 0.0788  145 SER B N   
1148 C CA  . SER A 148 ? 0.2329 0.2603 0.3516 0.0689  -0.0297 0.0776  145 SER B CA  
1149 C C   . SER A 148 ? 0.2206 0.2644 0.3358 0.0687  -0.0309 0.0840  145 SER B C   
1150 O O   . SER A 148 ? 0.2213 0.2696 0.3257 0.0592  -0.0274 0.0909  145 SER B O   
1151 C CB  . SER A 148 ? 0.2155 0.2554 0.3368 0.0706  -0.0233 0.0636  145 SER B CB  
1152 O OG  . SER A 148 ? 0.1917 0.2458 0.3040 0.0617  -0.0159 0.0635  145 SER B OG  
1153 N N   . GLN A 149 ? 0.2325 0.2866 0.3576 0.0797  -0.0362 0.0804  146 GLN B N   
1154 C CA  . GLN A 149 ? 0.2392 0.3122 0.3625 0.0796  -0.0383 0.0850  146 GLN B CA  
1155 C C   . GLN A 149 ? 0.2498 0.3122 0.3632 0.0749  -0.0444 0.1008  146 GLN B C   
1156 O O   . GLN A 149 ? 0.2361 0.3104 0.3390 0.0668  -0.0417 0.1054  146 GLN B O   
1157 C CB  . GLN A 149 ? 0.2665 0.3544 0.4053 0.0932  -0.0437 0.0780  146 GLN B CB  
1158 C CG  . GLN A 149 ? 0.2730 0.3861 0.4116 0.0916  -0.0451 0.0805  146 GLN B CG  
1159 C CD  . GLN A 149 ? 0.3101 0.4474 0.4662 0.1030  -0.0470 0.0700  146 GLN B CD  
1160 O OE1 . GLN A 149 ? 0.2992 0.4329 0.4681 0.1146  -0.0487 0.0615  146 GLN B OE1 
1161 N NE2 . GLN A 149 ? 0.3176 0.4811 0.4750 0.0995  -0.0467 0.0698  146 GLN B NE2 
1162 N N   . GLN A 150 ? 0.2797 0.3189 0.3949 0.0788  -0.0522 0.1084  147 GLN B N   
1163 C CA  . GLN A 150 ? 0.3316 0.3585 0.4358 0.0735  -0.0586 0.1250  147 GLN B CA  
1164 C C   . GLN A 150 ? 0.3004 0.3271 0.3892 0.0579  -0.0497 0.1305  147 GLN B C   
1165 O O   . GLN A 150 ? 0.2865 0.3190 0.3628 0.0513  -0.0505 0.1402  147 GLN B O   
1166 C CB  . GLN A 150 ? 0.4029 0.4015 0.5116 0.0796  -0.0691 0.1326  147 GLN B CB  
1167 C CG  . GLN A 150 ? 0.5032 0.5018 0.6241 0.0958  -0.0816 0.1325  147 GLN B CG  
1168 C CD  . GLN A 150 ? 0.6418 0.6099 0.7714 0.1054  -0.0918 0.1338  147 GLN B CD  
1169 O OE1 . GLN A 150 ? 0.7283 0.6698 0.8492 0.0975  -0.0952 0.1452  147 GLN B OE1 
1170 N NE2 . GLN A 150 ? 0.7260 0.6974 0.8732 0.1224  -0.0968 0.1214  147 GLN B NE2 
1171 N N   . ALA A 151 ? 0.2801 0.3022 0.3701 0.0529  -0.0416 0.1234  148 ALA B N   
1172 C CA  . ALA A 151 ? 0.2524 0.2758 0.3314 0.0400  -0.0332 0.1267  148 ALA B CA  
1173 C C   . ALA A 151 ? 0.2368 0.2817 0.3082 0.0359  -0.0264 0.1219  148 ALA B C   
1174 O O   . ALA A 151 ? 0.2406 0.2910 0.2996 0.0279  -0.0236 0.1284  148 ALA B O   
1175 C CB  . ALA A 151 ? 0.2446 0.2587 0.3293 0.0373  -0.0281 0.1195  148 ALA B CB  
1176 N N   . TYR A 152 ? 0.2103 0.2674 0.2886 0.0412  -0.0242 0.1104  149 TYR B N   
1177 C CA  . TYR A 152 ? 0.1929 0.2681 0.2646 0.0372  -0.0194 0.1058  149 TYR B CA  
1178 C C   . TYR A 152 ? 0.2174 0.3026 0.2824 0.0367  -0.0248 0.1129  149 TYR B C   
1179 O O   . TYR A 152 ? 0.2176 0.3108 0.2707 0.0291  -0.0208 0.1135  149 TYR B O   
1180 C CB  . TYR A 152 ? 0.1747 0.2606 0.2553 0.0419  -0.0170 0.0937  149 TYR B CB  
1181 C CG  . TYR A 152 ? 0.1538 0.2347 0.2353 0.0393  -0.0102 0.0855  149 TYR B CG  
1182 C CD1 . TYR A 152 ? 0.1522 0.2298 0.2250 0.0313  -0.0043 0.0857  149 TYR B CD1 
1183 C CD2 . TYR A 152 ? 0.1641 0.2463 0.2551 0.0454  -0.0099 0.0766  149 TYR B CD2 
1184 C CE1 . TYR A 152 ? 0.1387 0.2132 0.2122 0.0297  0.0004  0.0784  149 TYR B CE1 
1185 C CE2 . TYR A 152 ? 0.1418 0.2209 0.2317 0.0428  -0.0047 0.0695  149 TYR B CE2 
1186 C CZ  . TYR A 152 ? 0.1432 0.2176 0.2244 0.0349  -0.0002 0.0711  149 TYR B CZ  
1187 O OH  . TYR A 152 ? 0.1608 0.2321 0.2412 0.0332  0.0032  0.0645  149 TYR B OH  
1188 N N   . GLN A 153 ? 0.2234 0.3083 0.2958 0.0451  -0.0342 0.1173  150 GLN B N   
1189 C CA  . GLN A 153 ? 0.2216 0.3173 0.2882 0.0453  -0.0412 0.1243  150 GLN B CA  
1190 C C   . GLN A 153 ? 0.2480 0.3359 0.2968 0.0363  -0.0417 0.1369  150 GLN B C   
1191 O O   . GLN A 153 ? 0.2242 0.3245 0.2610 0.0305  -0.0415 0.1388  150 GLN B O   
1192 C CB  . GLN A 153 ? 0.2416 0.3362 0.3213 0.0580  -0.0528 0.1274  150 GLN B CB  
1193 C CG  . GLN A 153 ? 0.2496 0.3604 0.3274 0.0603  -0.0615 0.1325  150 GLN B CG  
1194 C CD  . GLN A 153 ? 0.2452 0.3810 0.3228 0.0556  -0.0568 0.1233  150 GLN B CD  
1195 O OE1 . GLN A 153 ? 0.2433 0.3896 0.3308 0.0566  -0.0504 0.1114  150 GLN B OE1 
1196 N NE2 . GLN A 153 ? 0.2772 0.4220 0.3409 0.0484  -0.0594 0.1290  150 GLN B NE2 
1197 N N   . GLU A 154 ? 0.2537 0.3225 0.3007 0.0344  -0.0421 0.1446  151 GLU B N   
1198 C CA  . GLU A 154 ? 0.2912 0.3540 0.3212 0.0242  -0.0409 0.1567  151 GLU B CA  
1199 C C   . GLU A 154 ? 0.2641 0.3377 0.2835 0.0143  -0.0290 0.1505  151 GLU B C   
1200 O O   . GLU A 154 ? 0.2520 0.3348 0.2556 0.0077  -0.0278 0.1546  151 GLU B O   
1201 C CB  . GLU A 154 ? 0.3204 0.3608 0.3512 0.0219  -0.0434 0.1666  151 GLU B CB  
1202 C CG  . GLU A 154 ? 0.3741 0.4116 0.3856 0.0106  -0.0436 0.1816  151 GLU B CG  
1203 C CD  . GLU A 154 ? 0.4552 0.4710 0.4651 0.0048  -0.0460 0.1938  151 GLU B CD  
1204 O OE1 . GLU A 154 ? 0.4653 0.4650 0.4896 0.0104  -0.0490 0.1906  151 GLU B OE1 
1205 O OE2 . GLU A 154 ? 0.5368 0.5522 0.5294 -0.0063 -0.0450 0.2068  151 GLU B OE2 
1206 N N   . ALA A 155 ? 0.2527 0.3257 0.2805 0.0145  -0.0211 0.1395  152 ALA B N   
1207 C CA  . ALA A 155 ? 0.2409 0.3233 0.2613 0.0079  -0.0111 0.1318  152 ALA B CA  
1208 C C   . ALA A 155 ? 0.2363 0.3336 0.2485 0.0070  -0.0115 0.1267  152 ALA B C   
1209 O O   . ALA A 155 ? 0.2188 0.3226 0.2175 0.0005  -0.0067 0.1258  152 ALA B O   
1210 C CB  . ALA A 155 ? 0.2133 0.2921 0.2446 0.0098  -0.0052 0.1215  152 ALA B CB  
1211 N N   . PHE A 156 ? 0.2355 0.3393 0.2564 0.0134  -0.0172 0.1225  153 PHE B N   
1212 C CA  . PHE A 156 ? 0.2459 0.3646 0.2615 0.0113  -0.0180 0.1168  153 PHE B CA  
1213 C C   . PHE A 156 ? 0.2622 0.3876 0.2629 0.0072  -0.0234 0.1251  153 PHE B C   
1214 O O   . PHE A 156 ? 0.2527 0.3872 0.2416 0.0013  -0.0214 0.1206  153 PHE B O   
1215 C CB  . PHE A 156 ? 0.2568 0.3833 0.2881 0.0186  -0.0227 0.1113  153 PHE B CB  
1216 C CG  . PHE A 156 ? 0.2658 0.4091 0.2954 0.0153  -0.0236 0.1045  153 PHE B CG  
1217 C CD1 . PHE A 156 ? 0.2833 0.4280 0.3110 0.0102  -0.0166 0.0948  153 PHE B CD1 
1218 C CD2 . PHE A 156 ? 0.3414 0.4984 0.3707 0.0165  -0.0323 0.1085  153 PHE B CD2 
1219 C CE1 . PHE A 156 ? 0.3027 0.4609 0.3286 0.0052  -0.0178 0.0890  153 PHE B CE1 
1220 C CE2 . PHE A 156 ? 0.3459 0.5195 0.3744 0.0117  -0.0334 0.1019  153 PHE B CE2 
1221 C CZ  . PHE A 156 ? 0.3425 0.5162 0.3699 0.0057  -0.0259 0.0921  153 PHE B CZ  
1222 N N   . GLU A 157 ? 0.2860 0.4062 0.2870 0.0107  -0.0317 0.1370  154 GLU B N   
1223 C CA  . GLU A 157 ? 0.3286 0.4541 0.3139 0.0069  -0.0383 0.1470  154 GLU B CA  
1224 C C   . GLU A 157 ? 0.3152 0.4388 0.2808 -0.0034 -0.0304 0.1502  154 GLU B C   
1225 O O   . GLU A 157 ? 0.3432 0.4774 0.2926 -0.0091 -0.0308 0.1494  154 GLU B O   
1226 C CB  . GLU A 157 ? 0.3640 0.4802 0.3548 0.0138  -0.0500 0.1601  154 GLU B CB  
1227 C CG  . GLU A 157 ? 0.3962 0.5207 0.4061 0.0253  -0.0589 0.1557  154 GLU B CG  
1228 C CD  . GLU A 157 ? 0.4759 0.5866 0.4961 0.0356  -0.0702 0.1658  154 GLU B CD  
1229 O OE1 . GLU A 157 ? 0.4945 0.5862 0.5058 0.0327  -0.0727 0.1785  154 GLU B OE1 
1230 O OE2 . GLU A 157 ? 0.4072 0.5273 0.4454 0.0465  -0.0768 0.1603  154 GLU B OE2 
1231 N N   . ILE A 158 ? 0.3236 0.4358 0.2912 -0.0058 -0.0234 0.1524  155 ILE B N   
1232 C CA  . ILE A 158 ? 0.3421 0.4561 0.2936 -0.0155 -0.0145 0.1547  155 ILE B CA  
1233 C C   . ILE A 158 ? 0.3374 0.4621 0.2834 -0.0182 -0.0059 0.1399  155 ILE B C   
1234 O O   . ILE A 158 ? 0.3709 0.5048 0.2988 -0.0244 -0.0031 0.1388  155 ILE B O   
1235 C CB  . ILE A 158 ? 0.3387 0.4411 0.2970 -0.0179 -0.0089 0.1593  155 ILE B CB  
1236 C CG1 . ILE A 158 ? 0.3523 0.4402 0.3125 -0.0168 -0.0186 0.1751  155 ILE B CG1 
1237 C CG2 . ILE A 158 ? 0.3906 0.5009 0.3359 -0.0277 0.0026  0.1583  155 ILE B CG2 
1238 C CD1 . ILE A 158 ? 0.3599 0.4336 0.3306 -0.0189 -0.0153 0.1788  155 ILE B CD1 
1239 N N   . SER A 159 ? 0.2968 0.4193 0.2574 -0.0133 -0.0029 0.1284  156 SER B N   
1240 C CA  . SER A 159 ? 0.2850 0.4127 0.2419 -0.0151 0.0037  0.1147  156 SER B CA  
1241 C C   . SER A 159 ? 0.2804 0.4178 0.2261 -0.0175 -0.0012 0.1108  156 SER B C   
1242 O O   . SER A 159 ? 0.3144 0.4560 0.2475 -0.0219 0.0035  0.1026  156 SER B O   
1243 C CB  . SER A 159 ? 0.2783 0.3996 0.2524 -0.0098 0.0056  0.1061  156 SER B CB  
1244 O OG  . SER A 159 ? 0.3413 0.4657 0.3116 -0.0111 0.0075  0.0948  156 SER B OG  
1245 N N   . ALA A 160 ? 0.2708 0.4125 0.2223 -0.0143 -0.0111 0.1151  157 ALA B N   
1246 C CA  . ALA A 160 ? 0.2940 0.4473 0.2362 -0.0175 -0.0173 0.1122  157 ALA B CA  
1247 C C   . ALA A 160 ? 0.3214 0.4806 0.2403 -0.0242 -0.0178 0.1166  157 ALA B C   
1248 O O   . ALA A 160 ? 0.3668 0.5340 0.2741 -0.0289 -0.0197 0.1096  157 ALA B O   
1249 C CB  . ALA A 160 ? 0.3048 0.4656 0.2592 -0.0121 -0.0286 0.1173  157 ALA B CB  
1250 N N   . ALA A 161 ? 0.3546 0.5100 0.2660 -0.0257 -0.0167 0.1279  158 ALA B N   
1251 C CA  . ALA A 161 ? 0.4127 0.5753 0.2996 -0.0331 -0.0166 0.1328  158 ALA B CA  
1252 C C   . ALA A 161 ? 0.4249 0.5876 0.3007 -0.0384 -0.0031 0.1273  158 ALA B C   
1253 O O   . ALA A 161 ? 0.4128 0.5844 0.2671 -0.0448 -0.0007 0.1253  158 ALA B O   
1254 C CB  . ALA A 161 ? 0.4175 0.5785 0.2998 -0.0327 -0.0267 0.1506  158 ALA B CB  
1255 N N   . ALA A 162 ? 0.3911 0.5463 0.2810 -0.0358 0.0052  0.1245  159 ALA B N   
1256 C CA  . ALA A 162 ? 0.3964 0.5554 0.2797 -0.0398 0.0179  0.1192  159 ALA B CA  
1257 C C   . ALA A 162 ? 0.3589 0.5188 0.2444 -0.0373 0.0250  0.1003  159 ALA B C   
1258 O O   . ALA A 162 ? 0.3392 0.5067 0.2137 -0.0401 0.0342  0.0920  159 ALA B O   
1259 C CB  . ALA A 162 ? 0.4118 0.5637 0.3095 -0.0390 0.0221  0.1269  159 ALA B CB  
1260 N N   . MET A 163 ? 0.3104 0.4624 0.2106 -0.0318 0.0211  0.0934  160 MET B N   
1261 C CA  . MET A 163 ? 0.3095 0.4562 0.2166 -0.0285 0.0269  0.0785  160 MET B CA  
1262 C C   . MET A 163 ? 0.2905 0.4356 0.1909 -0.0296 0.0217  0.0686  160 MET B C   
1263 O O   . MET A 163 ? 0.2675 0.4150 0.1682 -0.0310 0.0126  0.0732  160 MET B O   
1264 C CB  . MET A 163 ? 0.3038 0.4407 0.2326 -0.0228 0.0271  0.0796  160 MET B CB  
1265 C CG  . MET A 163 ? 0.3172 0.4540 0.2549 -0.0225 0.0321  0.0876  160 MET B CG  
1266 S SD  . MET A 163 ? 0.3860 0.5106 0.3470 -0.0158 0.0306  0.0857  160 MET B SD  
1267 C CE  . MET A 163 ? 0.3653 0.4910 0.3353 -0.0174 0.0364  0.0932  160 MET B CE  
1268 N N   . GLN A 164 ? 0.2822 0.4231 0.1779 -0.0289 0.0270  0.0542  161 GLN B N   
1269 C CA  A GLN A 164 ? 0.2786 0.4137 0.1681 -0.0310 0.0224  0.0435  161 GLN B CA  
1270 C CA  B GLN A 164 ? 0.2875 0.4227 0.1771 -0.0310 0.0223  0.0436  161 GLN B CA  
1271 C C   . GLN A 164 ? 0.2580 0.3829 0.1649 -0.0283 0.0184  0.0438  161 GLN B C   
1272 O O   . GLN A 164 ? 0.2267 0.3466 0.1480 -0.0234 0.0215  0.0469  161 GLN B O   
1273 C CB  A GLN A 164 ? 0.2926 0.4230 0.1711 -0.0302 0.0284  0.0277  161 GLN B CB  
1274 C CB  B GLN A 164 ? 0.3159 0.4470 0.1938 -0.0305 0.0283  0.0280  161 GLN B CB  
1275 C CG  A GLN A 164 ? 0.3136 0.4568 0.1719 -0.0337 0.0329  0.0248  161 GLN B CG  
1276 C CG  B GLN A 164 ? 0.3515 0.4956 0.2083 -0.0347 0.0316  0.0259  161 GLN B CG  
1277 C CD  A GLN A 164 ? 0.3285 0.4755 0.1680 -0.0407 0.0258  0.0211  161 GLN B CD  
1278 C CD  B GLN A 164 ? 0.3768 0.5208 0.2265 -0.0312 0.0411  0.0110  161 GLN B CD  
1279 O OE1 A GLN A 164 ? 0.3454 0.4878 0.1888 -0.0436 0.0168  0.0225  161 GLN B OE1 
1280 O OE1 B GLN A 164 ? 0.3825 0.5198 0.2461 -0.0244 0.0463  0.0057  161 GLN B OE1 
1281 N NE2 A GLN A 164 ? 0.3341 0.4910 0.1529 -0.0440 0.0295  0.0156  161 GLN B NE2 
1282 N NE2 B GLN A 164 ? 0.4107 0.5631 0.2389 -0.0352 0.0430  0.0032  161 GLN B NE2 
1283 N N   . PRO A 165 ? 0.2613 0.3840 0.1666 -0.0326 0.0114  0.0404  162 PRO B N   
1284 C CA  . PRO A 165 ? 0.2553 0.3712 0.1759 -0.0316 0.0084  0.0413  162 PRO B CA  
1285 C C   . PRO A 165 ? 0.2560 0.3558 0.1828 -0.0278 0.0130  0.0344  162 PRO B C   
1286 O O   . PRO A 165 ? 0.2404 0.3359 0.1800 -0.0260 0.0120  0.0376  162 PRO B O   
1287 C CB  . PRO A 165 ? 0.2596 0.3798 0.1753 -0.0391 0.0009  0.0386  162 PRO B CB  
1288 C CG  . PRO A 165 ? 0.2845 0.4157 0.1847 -0.0430 -0.0020 0.0391  162 PRO B CG  
1289 C CD  . PRO A 165 ? 0.2738 0.4031 0.1639 -0.0396 0.0056  0.0367  162 PRO B CD  
1290 N N   . THR A 166 ? 0.2593 0.3511 0.1769 -0.0261 0.0173  0.0244  163 THR B N   
1291 C CA  . THR A 166 ? 0.2852 0.3616 0.2087 -0.0208 0.0205  0.0176  163 THR B CA  
1292 C C   . THR A 166 ? 0.2735 0.3535 0.2085 -0.0133 0.0268  0.0213  163 THR B C   
1293 O O   . THR A 166 ? 0.2564 0.3255 0.1978 -0.0078 0.0286  0.0160  163 THR B O   
1294 C CB  . THR A 166 ? 0.3215 0.3875 0.2313 -0.0208 0.0214  0.0038  163 THR B CB  
1295 O OG1 . THR A 166 ? 0.3588 0.4383 0.2580 -0.0204 0.0261  0.0012  163 THR B OG1 
1296 C CG2 . THR A 166 ? 0.3374 0.3946 0.2376 -0.0295 0.0139  -0.0005 163 THR B CG2 
1297 N N   . HIS A 167 ? 0.2337 0.3284 0.1709 -0.0133 0.0294  0.0302  164 HIS B N   
1298 C CA  . HIS A 167 ? 0.2174 0.3169 0.1648 -0.0086 0.0353  0.0339  164 HIS B CA  
1299 C C   . HIS A 167 ? 0.1949 0.2860 0.1583 -0.0051 0.0330  0.0378  164 HIS B C   
1300 O O   . HIS A 167 ? 0.1752 0.2658 0.1430 -0.0071 0.0281  0.0443  164 HIS B O   
1301 C CB  . HIS A 167 ? 0.2161 0.3300 0.1602 -0.0117 0.0374  0.0441  164 HIS B CB  
1302 C CG  . HIS A 167 ? 0.2266 0.3471 0.1789 -0.0093 0.0445  0.0463  164 HIS B CG  
1303 N ND1 . HIS A 167 ? 0.2263 0.3420 0.1953 -0.0052 0.0453  0.0483  164 HIS B ND1 
1304 C CD2 . HIS A 167 ? 0.2372 0.3702 0.1830 -0.0115 0.0512  0.0468  164 HIS B CD2 
1305 C CE1 . HIS A 167 ? 0.2449 0.3703 0.2189 -0.0052 0.0518  0.0498  164 HIS B CE1 
1306 N NE2 . HIS A 167 ? 0.2533 0.3901 0.2134 -0.0092 0.0562  0.0491  164 HIS B NE2 
1307 N N   . PRO A 168 ? 0.2046 0.2899 0.1768 0.0004  0.0359  0.0330  165 PRO B N   
1308 C CA  . PRO A 168 ? 0.1824 0.2597 0.1673 0.0032  0.0331  0.0363  165 PRO B CA  
1309 C C   . PRO A 168 ? 0.1812 0.2647 0.1752 0.0020  0.0318  0.0471  165 PRO B C   
1310 O O   . PRO A 168 ? 0.1684 0.2467 0.1681 0.0022  0.0279  0.0497  165 PRO B O   
1311 C CB  . PRO A 168 ? 0.1986 0.2736 0.1919 0.0096  0.0364  0.0305  165 PRO B CB  
1312 C CG  . PRO A 168 ? 0.2197 0.2984 0.2042 0.0112  0.0407  0.0214  165 PRO B CG  
1313 C CD  . PRO A 168 ? 0.2112 0.2983 0.1821 0.0050  0.0416  0.0232  165 PRO B CD  
1314 N N   . ILE A 169 ? 0.1789 0.2730 0.1732 0.0004  0.0348  0.0533  166 ILE B N   
1315 C CA  . ILE A 169 ? 0.1793 0.2756 0.1814 -0.0004 0.0325  0.0636  166 ILE B CA  
1316 C C   . ILE A 169 ? 0.1797 0.2766 0.1781 -0.0022 0.0265  0.0678  166 ILE B C   
1317 O O   . ILE A 169 ? 0.1884 0.2827 0.1959 -0.0001 0.0228  0.0716  166 ILE B O   
1318 C CB  . ILE A 169 ? 0.2025 0.3076 0.2048 -0.0030 0.0368  0.0703  166 ILE B CB  
1319 C CG1 . ILE A 169 ? 0.2076 0.3162 0.2183 -0.0011 0.0430  0.0652  166 ILE B CG1 
1320 C CG2 . ILE A 169 ? 0.1992 0.3018 0.2082 -0.0040 0.0324  0.0814  166 ILE B CG2 
1321 C CD1 . ILE A 169 ? 0.2324 0.3534 0.2423 -0.0059 0.0490  0.0708  166 ILE B CD1 
1322 N N   . ARG A 170 ? 0.1898 0.2921 0.1756 -0.0057 0.0253  0.0669  167 ARG B N   
1323 C CA  . ARG A 170 ? 0.1961 0.3022 0.1793 -0.0076 0.0190  0.0695  167 ARG B CA  
1324 C C   . ARG A 170 ? 0.1892 0.2901 0.1782 -0.0071 0.0165  0.0643  167 ARG B C   
1325 O O   . ARG A 170 ? 0.2071 0.3117 0.2043 -0.0058 0.0126  0.0680  167 ARG B O   
1326 C CB  . ARG A 170 ? 0.2098 0.3225 0.1770 -0.0124 0.0182  0.0673  167 ARG B CB  
1327 C CG  . ARG A 170 ? 0.2299 0.3498 0.1955 -0.0149 0.0107  0.0702  167 ARG B CG  
1328 C CD  . ARG A 170 ? 0.2514 0.3803 0.2020 -0.0194 0.0078  0.0721  167 ARG B CD  
1329 N NE  . ARG A 170 ? 0.2562 0.3937 0.2080 -0.0218 -0.0002 0.0731  167 ARG B NE  
1330 C CZ  . ARG A 170 ? 0.2601 0.4062 0.1988 -0.0269 -0.0047 0.0724  167 ARG B CZ  
1331 N NH1 . ARG A 170 ? 0.2771 0.4245 0.1993 -0.0296 -0.0019 0.0723  167 ARG B NH1 
1332 N NH2 . ARG A 170 ? 0.2601 0.4155 0.2021 -0.0297 -0.0120 0.0718  167 ARG B NH2 
1333 N N   . LEU A 171 ? 0.1729 0.2650 0.1581 -0.0079 0.0188  0.0562  168 LEU B N   
1334 C CA  . LEU A 171 ? 0.1824 0.2678 0.1706 -0.0092 0.0165  0.0526  168 LEU B CA  
1335 C C   . LEU A 171 ? 0.1747 0.2581 0.1756 -0.0050 0.0168  0.0558  168 LEU B C   
1336 O O   . LEU A 171 ? 0.1641 0.2512 0.1698 -0.0060 0.0144  0.0568  168 LEU B O   
1337 C CB  . LEU A 171 ? 0.2010 0.2736 0.1810 -0.0103 0.0178  0.0443  168 LEU B CB  
1338 C CG  . LEU A 171 ? 0.2267 0.2990 0.1931 -0.0157 0.0162  0.0390  168 LEU B CG  
1339 C CD1 . LEU A 171 ? 0.2621 0.3199 0.2218 -0.0136 0.0179  0.0300  168 LEU B CD1 
1340 C CD2 . LEU A 171 ? 0.2301 0.3058 0.1942 -0.0233 0.0111  0.0396  168 LEU B CD2 
1341 N N   . GLY A 172 ? 0.1520 0.2311 0.1580 -0.0007 0.0198  0.0563  169 GLY B N   
1342 C CA  . GLY A 172 ? 0.1476 0.2238 0.1648 0.0030  0.0195  0.0584  169 GLY B CA  
1343 C C   . GLY A 172 ? 0.1281 0.2110 0.1530 0.0048  0.0171  0.0640  169 GLY B C   
1344 O O   . GLY A 172 ? 0.1331 0.2159 0.1643 0.0066  0.0155  0.0632  169 GLY B O   
1345 N N   . LEU A 173 ? 0.1508 0.2398 0.1741 0.0045  0.0163  0.0694  170 LEU B N   
1346 C CA  . LEU A 173 ? 0.1370 0.2310 0.1671 0.0072  0.0121  0.0751  170 LEU B CA  
1347 C C   . LEU A 173 ? 0.1366 0.2391 0.1681 0.0068  0.0090  0.0724  170 LEU B C   
1348 O O   . LEU A 173 ? 0.1275 0.2332 0.1688 0.0111  0.0067  0.0724  170 LEU B O   
1349 C CB  . LEU A 173 ? 0.1547 0.2520 0.1792 0.0058  0.0109  0.0826  170 LEU B CB  
1350 C CG  . LEU A 173 ? 0.1632 0.2651 0.1921 0.0090  0.0044  0.0895  170 LEU B CG  
1351 C CD1 . LEU A 173 ? 0.1647 0.2589 0.2065 0.0149  0.0021  0.0915  170 LEU B CD1 
1352 C CD2 . LEU A 173 ? 0.1810 0.2841 0.2003 0.0058  0.0034  0.0979  170 LEU B CD2 
1353 N N   . ALA A 174 ? 0.1444 0.2519 0.1668 0.0015  0.0086  0.0698  171 ALA B N   
1354 C CA  . ALA A 174 ? 0.1376 0.2560 0.1622 -0.0010 0.0059  0.0673  171 ALA B CA  
1355 C C   . ALA A 174 ? 0.1494 0.2660 0.1796 -0.0011 0.0080  0.0627  171 ALA B C   
1356 O O   . ALA A 174 ? 0.1410 0.2689 0.1806 0.0012  0.0066  0.0619  171 ALA B O   
1357 C CB  . ALA A 174 ? 0.1367 0.2577 0.1496 -0.0086 0.0051  0.0642  171 ALA B CB  
1358 N N   . LEU A 175 ? 0.1569 0.2603 0.1811 -0.0032 0.0111  0.0597  172 LEU B N   
1359 C CA  . LEU A 175 ? 0.1464 0.2459 0.1727 -0.0038 0.0126  0.0565  172 LEU B CA  
1360 C C   . LEU A 175 ? 0.1403 0.2438 0.1782 0.0031  0.0126  0.0570  172 LEU B C   
1361 O O   . LEU A 175 ? 0.1372 0.2497 0.1793 0.0028  0.0130  0.0544  172 LEU B O   
1362 C CB  . LEU A 175 ? 0.1398 0.2228 0.1589 -0.0045 0.0142  0.0545  172 LEU B CB  
1363 C CG  . LEU A 175 ? 0.1486 0.2248 0.1654 -0.0067 0.0145  0.0523  172 LEU B CG  
1364 C CD1 . LEU A 175 ? 0.1596 0.2389 0.1692 -0.0156 0.0140  0.0512  172 LEU B CD1 
1365 C CD2 . LEU A 175 ? 0.1699 0.2304 0.1823 -0.0048 0.0144  0.0510  172 LEU B CD2 
1366 N N   . ASN A 176 ? 0.1429 0.2396 0.1854 0.0087  0.0123  0.0597  173 ASN B N   
1367 C CA  . ASN A 176 ? 0.1264 0.2219 0.1790 0.0150  0.0115  0.0592  173 ASN B CA  
1368 C C   . ASN A 176 ? 0.1373 0.2443 0.1992 0.0201  0.0085  0.0601  173 ASN B C   
1369 O O   . ASN A 176 ? 0.1276 0.2387 0.1971 0.0247  0.0084  0.0558  173 ASN B O   
1370 C CB  . ASN A 176 ? 0.1305 0.2146 0.1854 0.0175  0.0116  0.0622  173 ASN B CB  
1371 C CG  . ASN A 176 ? 0.1499 0.2251 0.2002 0.0150  0.0138  0.0595  173 ASN B CG  
1372 O OD1 . ASN A 176 ? 0.1495 0.2237 0.1924 0.0113  0.0148  0.0565  173 ASN B OD1 
1373 N ND2 . ASN A 176 ? 0.1535 0.2219 0.2087 0.0168  0.0139  0.0608  173 ASN B ND2 
1374 N N   . PHE A 177 ? 0.1299 0.2424 0.1909 0.0200  0.0056  0.0651  174 PHE B N   
1375 C CA  . PHE A 177 ? 0.1387 0.2629 0.2091 0.0257  0.0011  0.0663  174 PHE B CA  
1376 C C   . PHE A 177 ? 0.1281 0.2706 0.2029 0.0241  0.0023  0.0601  174 PHE B C   
1377 O O   . PHE A 177 ? 0.1323 0.2855 0.2195 0.0315  0.0005  0.0568  174 PHE B O   
1378 C CB  . PHE A 177 ? 0.1469 0.2736 0.2134 0.0252  -0.0034 0.0738  174 PHE B CB  
1379 C CG  . PHE A 177 ? 0.1505 0.2818 0.2268 0.0336  -0.0105 0.0783  174 PHE B CG  
1380 C CD1 . PHE A 177 ? 0.1450 0.2768 0.2351 0.0432  -0.0130 0.0748  174 PHE B CD1 
1381 C CD2 . PHE A 177 ? 0.1492 0.2829 0.2194 0.0322  -0.0155 0.0862  174 PHE B CD2 
1382 C CE1 . PHE A 177 ? 0.1544 0.2875 0.2535 0.0522  -0.0210 0.0793  174 PHE B CE1 
1383 C CE2 . PHE A 177 ? 0.1700 0.3067 0.2481 0.0402  -0.0239 0.0917  174 PHE B CE2 
1384 C CZ  . PHE A 177 ? 0.1680 0.3027 0.2610 0.0506  -0.0269 0.0885  174 PHE B CZ  
1385 N N   A SER A 178 ? 0.1303 0.2765 0.1957 0.0146  0.0050  0.0584  175 SER B N   
1386 N N   B SER A 178 ? 0.1358 0.2820 0.2011 0.0145  0.0051  0.0583  175 SER B N   
1387 C CA  A SER A 178 ? 0.1266 0.2894 0.1944 0.0096  0.0072  0.0533  175 SER B CA  
1388 C CA  B SER A 178 ? 0.1361 0.2986 0.2034 0.0092  0.0074  0.0532  175 SER B CA  
1389 C C   A SER A 178 ? 0.1252 0.2890 0.1975 0.0124  0.0111  0.0477  175 SER B C   
1390 C C   B SER A 178 ? 0.1302 0.2939 0.2024 0.0124  0.0112  0.0477  175 SER B C   
1391 O O   A SER A 178 ? 0.1186 0.3014 0.2014 0.0156  0.0119  0.0431  175 SER B O   
1392 O O   B SER A 178 ? 0.1228 0.3056 0.2056 0.0156  0.0119  0.0431  175 SER B O   
1393 C CB  A SER A 178 ? 0.1344 0.2943 0.1891 -0.0024 0.0088  0.0532  175 SER B CB  
1394 C CB  B SER A 178 ? 0.1511 0.3107 0.2050 -0.0033 0.0092  0.0528  175 SER B CB  
1395 O OG  A SER A 178 ? 0.1263 0.2981 0.1815 -0.0091 0.0118  0.0491  175 SER B OG  
1396 O OG  B SER A 178 ? 0.1576 0.2997 0.2013 -0.0074 0.0124  0.0517  175 SER B OG  
1397 N N   . VAL A 179 ? 0.1303 0.2754 0.1962 0.0128  0.0131  0.0476  176 VAL B N   
1398 C CA  . VAL A 179 ? 0.1263 0.2707 0.1937 0.0150  0.0161  0.0421  176 VAL B CA  
1399 C C   . VAL A 179 ? 0.1324 0.2824 0.2137 0.0266  0.0143  0.0384  176 VAL B C   
1400 O O   . VAL A 179 ? 0.1070 0.2699 0.1934 0.0291  0.0171  0.0314  176 VAL B O   
1401 C CB  . VAL A 179 ? 0.1373 0.2615 0.1945 0.0123  0.0170  0.0431  176 VAL B CB  
1402 C CG1 . VAL A 179 ? 0.1546 0.2767 0.2136 0.0162  0.0185  0.0376  176 VAL B CG1 
1403 C CG2 . VAL A 179 ? 0.1387 0.2581 0.1824 0.0016  0.0183  0.0448  176 VAL B CG2 
1404 N N   . PHE A 180 ? 0.1303 0.2702 0.2169 0.0333  0.0097  0.0430  177 PHE B N   
1405 C CA  . PHE A 180 ? 0.1345 0.2763 0.2345 0.0448  0.0060  0.0405  177 PHE B CA  
1406 C C   . PHE A 180 ? 0.1287 0.2952 0.2403 0.0497  0.0054  0.0358  177 PHE B C   
1407 O O   . PHE A 180 ? 0.1321 0.3063 0.2538 0.0582  0.0060  0.0276  177 PHE B O   
1408 C CB  . PHE A 180 ? 0.1387 0.2656 0.2394 0.0479  0.0004  0.0493  177 PHE B CB  
1409 C CG  . PHE A 180 ? 0.1505 0.2739 0.2639 0.0599  -0.0056 0.0487  177 PHE B CG  
1410 C CD1 . PHE A 180 ? 0.1567 0.2642 0.2740 0.0654  -0.0068 0.0448  177 PHE B CD1 
1411 C CD2 . PHE A 180 ? 0.1599 0.2943 0.2813 0.0657  -0.0114 0.0521  177 PHE B CD2 
1412 C CE1 . PHE A 180 ? 0.1728 0.2729 0.3013 0.0767  -0.0135 0.0441  177 PHE B CE1 
1413 C CE2 . PHE A 180 ? 0.1819 0.3111 0.3158 0.0785  -0.0184 0.0514  177 PHE B CE2 
1414 C CZ  . PHE A 180 ? 0.1840 0.2944 0.3210 0.0839  -0.0194 0.0474  177 PHE B CZ  
1415 N N   . TYR A 181 ? 0.1313 0.3115 0.2422 0.0447  0.0040  0.0398  178 TYR B N   
1416 C CA  . TYR A 181 ? 0.1222 0.3304 0.2460 0.0482  0.0034  0.0351  178 TYR B CA  
1417 C C   . TYR A 181 ? 0.1120 0.3366 0.2362 0.0437  0.0111  0.0260  178 TYR B C   
1418 O O   . TYR A 181 ? 0.1199 0.3639 0.2580 0.0520  0.0122  0.0179  178 TYR B O   
1419 C CB  . TYR A 181 ? 0.1382 0.3602 0.2603 0.0411  0.0004  0.0403  178 TYR B CB  
1420 C CG  . TYR A 181 ? 0.1554 0.3733 0.2830 0.0493  -0.0086 0.0474  178 TYR B CG  
1421 C CD1 . TYR A 181 ? 0.1885 0.4237 0.3340 0.0612  -0.0144 0.0449  178 TYR B CD1 
1422 C CD2 . TYR A 181 ? 0.1849 0.3835 0.2997 0.0452  -0.0118 0.0567  178 TYR B CD2 
1423 C CE1 . TYR A 181 ? 0.2403 0.4701 0.3896 0.0690  -0.0243 0.0527  178 TYR B CE1 
1424 C CE2 . TYR A 181 ? 0.2097 0.4038 0.3269 0.0516  -0.0202 0.0644  178 TYR B CE2 
1425 C CZ  . TYR A 181 ? 0.2384 0.4462 0.3722 0.0635  -0.0271 0.0632  178 TYR B CZ  
1426 O OH  . TYR A 181 ? 0.2877 0.4908 0.4226 0.0695  -0.0371 0.0723  178 TYR B OH  
1427 N N   . TYR A 182 ? 0.1134 0.3301 0.2219 0.0310  0.0160  0.0276  179 TYR B N   
1428 C CA  . TYR A 182 ? 0.1124 0.3453 0.2175 0.0232  0.0231  0.0215  179 TYR B CA  
1429 C C   . TYR A 182 ? 0.1176 0.3517 0.2272 0.0317  0.0264  0.0127  179 TYR B C   
1430 O O   . TYR A 182 ? 0.1222 0.3820 0.2407 0.0337  0.0309  0.0044  179 TYR B O   
1431 C CB  . TYR A 182 ? 0.1209 0.3390 0.2066 0.0086  0.0258  0.0263  179 TYR B CB  
1432 C CG  . TYR A 182 ? 0.1225 0.3581 0.2025 -0.0029 0.0322  0.0229  179 TYR B CG  
1433 C CD1 . TYR A 182 ? 0.1339 0.3692 0.2078 -0.0034 0.0371  0.0179  179 TYR B CD1 
1434 C CD2 . TYR A 182 ? 0.1390 0.3918 0.2188 -0.0143 0.0330  0.0250  179 TYR B CD2 
1435 C CE1 . TYR A 182 ? 0.1556 0.4085 0.2224 -0.0155 0.0434  0.0159  179 TYR B CE1 
1436 C CE2 . TYR A 182 ? 0.1558 0.4273 0.2311 -0.0267 0.0391  0.0227  179 TYR B CE2 
1437 C CZ  . TYR A 182 ? 0.1598 0.4309 0.2277 -0.0275 0.0447  0.0187  179 TYR B CZ  
1438 O OH  . TYR A 182 ? 0.1855 0.4736 0.2456 -0.0420 0.0509  0.0182  179 TYR B OH  
1439 N N   . GLU A 183 ? 0.1339 0.3419 0.2369 0.0356  0.0246  0.0137  180 GLU B N   
1440 C CA  . GLU A 183 ? 0.1560 0.3613 0.2578 0.0403  0.0277  0.0051  180 GLU B CA  
1441 C C   . GLU A 183 ? 0.1521 0.3482 0.2666 0.0558  0.0231  0.0000  180 GLU B C   
1442 O O   . GLU A 183 ? 0.1476 0.3467 0.2637 0.0613  0.0257  -0.0102 180 GLU B O   
1443 C CB  . GLU A 183 ? 0.1700 0.3571 0.2532 0.0303  0.0296  0.0084  180 GLU B CB  
1444 C CG  . GLU A 183 ? 0.1749 0.3337 0.2535 0.0319  0.0246  0.0145  180 GLU B CG  
1445 C CD  . GLU A 183 ? 0.1913 0.3357 0.2536 0.0233  0.0257  0.0168  180 GLU B CD  
1446 O OE1 . GLU A 183 ? 0.1819 0.3325 0.2322 0.0132  0.0292  0.0177  180 GLU B OE1 
1447 O OE2 . GLU A 183 ? 0.1855 0.3110 0.2473 0.0267  0.0221  0.0183  180 GLU B OE2 
1448 N N   . ILE A 184 ? 0.1474 0.3301 0.2686 0.0619  0.0161  0.0066  181 ILE B N   
1449 C CA  . ILE A 184 ? 0.1559 0.3269 0.2887 0.0760  0.0105  0.0025  181 ILE B CA  
1450 C C   . ILE A 184 ? 0.1681 0.3607 0.3188 0.0874  0.0078  -0.0021 181 ILE B C   
1451 O O   . ILE A 184 ? 0.1563 0.3537 0.3180 0.0994  0.0074  -0.0131 181 ILE B O   
1452 C CB  . ILE A 184 ? 0.1562 0.2986 0.2854 0.0758  0.0041  0.0128  181 ILE B CB  
1453 C CG1 . ILE A 184 ? 0.1606 0.2866 0.2750 0.0653  0.0069  0.0163  181 ILE B CG1 
1454 C CG2 . ILE A 184 ? 0.1702 0.2975 0.3110 0.0893  -0.0028 0.0093  181 ILE B CG2 
1455 C CD1 . ILE A 184 ? 0.1611 0.2829 0.2704 0.0651  0.0101  0.0068  181 ILE B CD1 
1456 N N   . LEU A 185 ? 0.1573 0.3630 0.3114 0.0842  0.0055  0.0053  182 LEU B N   
1457 C CA  . LEU A 185 ? 0.1838 0.4137 0.3563 0.0946  0.0018  0.0017  182 LEU B CA  
1458 C C   . LEU A 185 ? 0.1604 0.4273 0.3391 0.0908  0.0097  -0.0075 182 LEU B C   
1459 O O   . LEU A 185 ? 0.1697 0.4604 0.3668 0.1011  0.0072  -0.0131 182 LEU B O   
1460 C CB  . LEU A 185 ? 0.1912 0.4188 0.3635 0.0922  -0.0055 0.0143  182 LEU B CB  
1461 C CG  . LEU A 185 ? 0.2161 0.4113 0.3836 0.0962  -0.0137 0.0244  182 LEU B CG  
1462 C CD1 . LEU A 185 ? 0.2293 0.4285 0.3947 0.0926  -0.0202 0.0361  182 LEU B CD1 
1463 C CD2 . LEU A 185 ? 0.2397 0.4230 0.4205 0.1130  -0.0202 0.0191  182 LEU B CD2 
1464 N N   . ASN A 186 ? 0.1554 0.4274 0.3198 0.0761  0.0184  -0.0084 183 ASN B N   
1465 C CA  . ASN A 186 ? 0.1685 0.4755 0.3358 0.0684  0.0268  -0.0152 183 ASN B CA  
1466 C C   . ASN A 186 ? 0.1440 0.4761 0.3225 0.0655  0.0237  -0.0111 183 ASN B C   
1467 O O   . ASN A 186 ? 0.1377 0.5035 0.3340 0.0714  0.0257  -0.0195 183 ASN B O   
1468 C CB  . ASN A 186 ? 0.2214 0.5479 0.3993 0.0787  0.0325  -0.0308 183 ASN B CB  
1469 C CG  . ASN A 186 ? 0.3073 0.6071 0.4725 0.0808  0.0341  -0.0349 183 ASN B CG  
1470 O OD1 . ASN A 186 ? 0.4217 0.7108 0.5961 0.0962  0.0302  -0.0426 183 ASN B OD1 
1471 N ND2 . ASN A 186 ? 0.2987 0.5853 0.4430 0.0659  0.0383  -0.0296 183 ASN B ND2 
1472 N N   . SER A 187 ? 0.1416 0.4580 0.3100 0.0567  0.0187  0.0010  184 SER B N   
1473 C CA  . SER A 187 ? 0.1427 0.4761 0.3175 0.0524  0.0137  0.0067  184 SER B CA  
1474 C C   . SER A 187 ? 0.1274 0.4570 0.2843 0.0322  0.0171  0.0133  184 SER B C   
1475 O O   . SER A 187 ? 0.1321 0.4387 0.2764 0.0270  0.0127  0.0221  184 SER B O   
1476 C CB  . SER A 187 ? 0.1631 0.4784 0.3411 0.0624  0.0030  0.0145  184 SER B CB  
1477 O OG  . SER A 187 ? 0.1992 0.5229 0.3967 0.0808  -0.0019 0.0085  184 SER B OG  
1478 N N   . PRO A 188 ? 0.1287 0.4771 0.2815 0.0192  0.0254  0.0092  185 PRO B N   
1479 C CA  . PRO A 188 ? 0.1238 0.4580 0.2557 0.0000  0.0280  0.0158  185 PRO B CA  
1480 C C   . PRO A 188 ? 0.1108 0.4505 0.2415 -0.0096 0.0226  0.0219  185 PRO B C   
1481 O O   . PRO A 188 ? 0.1204 0.4353 0.2343 -0.0183 0.0202  0.0285  185 PRO B O   
1482 C CB  . PRO A 188 ? 0.1233 0.4757 0.2513 -0.0104 0.0376  0.0103  185 PRO B CB  
1483 C CG  . PRO A 188 ? 0.1334 0.5231 0.2853 0.0007  0.0398  0.0006  185 PRO B CG  
1484 C CD  . PRO A 188 ? 0.1267 0.5039 0.2905 0.0220  0.0331  -0.0016 185 PRO B CD  
1485 N N   . GLU A 189 ? 0.0971 0.4690 0.2465 -0.0064 0.0196  0.0190  186 GLU B N   
1486 C CA  . GLU A 189 ? 0.1140 0.4947 0.2633 -0.0157 0.0133  0.0238  186 GLU B CA  
1487 C C   . GLU A 189 ? 0.1205 0.4727 0.2614 -0.0085 0.0048  0.0311  186 GLU B C   
1488 O O   . GLU A 189 ? 0.1159 0.4516 0.2409 -0.0195 0.0022  0.0363  186 GLU B O   
1489 C CB  . GLU A 189 ? 0.1066 0.5313 0.2799 -0.0132 0.0108  0.0190  186 GLU B CB  
1490 C CG  . GLU A 189 ? 0.1022 0.5599 0.2839 -0.0228 0.0205  0.0118  186 GLU B CG  
1491 C CD  . GLU A 189 ? 0.0933 0.5608 0.2850 -0.0094 0.0276  0.0030  186 GLU B CD  
1492 O OE1 . GLU A 189 ? 0.0825 0.5348 0.2797 0.0095  0.0241  0.0011  186 GLU B OE1 
1493 O OE2 . GLU A 189 ? 0.0968 0.5841 0.2875 -0.0198 0.0375  -0.0019 186 GLU B OE2 
1494 N N   . LYS A 190 ? 0.1398 0.4846 0.2899 0.0095  0.0007  0.0312  187 LYS B N   
1495 C CA  . LYS A 190 ? 0.1625 0.4806 0.3041 0.0162  -0.0065 0.0389  187 LYS B CA  
1496 C C   . LYS A 190 ? 0.1474 0.4316 0.2672 0.0088  -0.0025 0.0426  187 LYS B C   
1497 O O   . LYS A 190 ? 0.1535 0.4214 0.2604 0.0043  -0.0061 0.0485  187 LYS B O   
1498 C CB  . LYS A 190 ? 0.2167 0.5295 0.3712 0.0355  -0.0119 0.0392  187 LYS B CB  
1499 C CG  . LYS A 190 ? 0.3160 0.6564 0.4915 0.0462  -0.0199 0.0378  187 LYS B CG  
1500 C CD  . LYS A 190 ? 0.4065 0.7474 0.5995 0.0661  -0.0229 0.0332  187 LYS B CD  
1501 C CE  . LYS A 190 ? 0.4556 0.8284 0.6725 0.0778  -0.0306 0.0299  187 LYS B CE  
1502 N NZ  . LYS A 190 ? 0.5084 0.8714 0.7229 0.0828  -0.0436 0.0407  187 LYS B NZ  
1503 N N   . ALA A 191 ? 0.1425 0.4172 0.2583 0.0082  0.0047  0.0387  188 ALA B N   
1504 C CA  . ALA A 191 ? 0.1265 0.3715 0.2237 0.0019  0.0080  0.0416  188 ALA B CA  
1505 C C   . ALA A 191 ? 0.1253 0.3657 0.2078 -0.0141 0.0085  0.0440  188 ALA B C   
1506 O O   . ALA A 191 ? 0.1445 0.3625 0.2138 -0.0167 0.0069  0.0478  188 ALA B O   
1507 C CB  . ALA A 191 ? 0.1328 0.3744 0.2288 0.0025  0.0146  0.0365  188 ALA B CB  
1508 N N   . OCY A 192 ? 0.1203 0.3817 0.2053 -0.0250 0.0109  0.0411  189 OCY B N   
1509 C CA  . OCY A 192 ? 0.1385 0.3949 0.2101 -0.0414 0.0103  0.0429  189 OCY B CA  
1510 C CB  . OCY A 192 ? 0.1531 0.4347 0.2294 -0.0542 0.0143  0.0398  189 OCY B CB  
1511 S SG  . OCY A 192 ? 0.1970 0.4695 0.2644 -0.0585 0.0228  0.0383  189 OCY B SG  
1512 C CD  . OCY A 192 ? 0.2287 0.5365 0.3019 -0.0755 0.0284  0.0355  189 OCY B CD  
1513 C CE  . OCY A 192 ? 0.2294 0.5694 0.3244 -0.0626 0.0312  0.0291  189 OCY B CE  
1514 O OZ  . OCY A 192 ? 0.3035 0.6797 0.4088 -0.0736 0.0354  0.0258  189 OCY B OZ  
1515 C C   . OCY A 192 ? 0.1406 0.3960 0.2096 -0.0425 0.0032  0.0458  189 OCY B C   
1516 O O   . OCY A 192 ? 0.1582 0.3922 0.2111 -0.0497 0.0019  0.0475  189 OCY B O   
1517 N N   . SER A 193 ? 0.1363 0.4146 0.2206 -0.0346 -0.0019 0.0458  190 SER B N   
1518 C CA  . SER A 193 ? 0.1526 0.4330 0.2339 -0.0352 -0.0097 0.0490  190 SER B CA  
1519 C C   . SER A 193 ? 0.1519 0.4019 0.2184 -0.0299 -0.0109 0.0532  190 SER B C   
1520 O O   . SER A 193 ? 0.1583 0.3967 0.2101 -0.0376 -0.0131 0.0540  190 SER B O   
1521 C CB  . SER A 193 ? 0.1582 0.4647 0.2587 -0.0244 -0.0157 0.0493  190 SER B CB  
1522 O OG  . SER A 193 ? 0.1800 0.4900 0.2752 -0.0274 -0.0239 0.0527  190 SER B OG  
1523 N N   . LEU A 194 ? 0.1514 0.3898 0.2219 -0.0175 -0.0092 0.0551  191 LEU B N   
1524 C CA  . LEU A 194 ? 0.1538 0.3667 0.2124 -0.0130 -0.0093 0.0595  191 LEU B CA  
1525 C C   . LEU A 194 ? 0.1624 0.3538 0.2041 -0.0220 -0.0048 0.0575  191 LEU B C   
1526 O O   . LEU A 194 ? 0.1895 0.3691 0.2185 -0.0247 -0.0062 0.0588  191 LEU B O   
1527 C CB  . LEU A 194 ? 0.1631 0.3687 0.2311 -0.0001 -0.0082 0.0611  191 LEU B CB  
1528 C CG  . LEU A 194 ? 0.1882 0.3762 0.2503 0.0061  -0.0105 0.0675  191 LEU B CG  
1529 C CD1 . LEU A 194 ? 0.1988 0.3815 0.2730 0.0182  -0.0114 0.0690  191 LEU B CD1 
1530 C CD2 . LEU A 194 ? 0.2118 0.3788 0.2587 0.0005  -0.0056 0.0673  191 LEU B CD2 
1531 N N   . ALA A 195 ? 0.1564 0.3429 0.1972 -0.0265 0.0003  0.0541  192 ALA B N   
1532 C CA  . ALA A 195 ? 0.1492 0.3132 0.1752 -0.0333 0.0033  0.0526  192 ALA B CA  
1533 C C   . ALA A 195 ? 0.1673 0.3292 0.1817 -0.0453 0.0005  0.0507  192 ALA B C   
1534 O O   . ALA A 195 ? 0.1698 0.3131 0.1713 -0.0471 0.0000  0.0495  192 ALA B O   
1535 C CB  . ALA A 195 ? 0.1624 0.3233 0.1892 -0.0361 0.0078  0.0507  192 ALA B CB  
1536 N N   . LYS A 196 ? 0.1731 0.3550 0.1928 -0.0537 -0.0015 0.0495  193 LYS B N   
1537 C CA  . LYS A 196 ? 0.1913 0.3727 0.2012 -0.0670 -0.0050 0.0472  193 LYS B CA  
1538 C C   . LYS A 196 ? 0.1913 0.3718 0.1946 -0.0648 -0.0101 0.0472  193 LYS B C   
1539 O O   . LYS A 196 ? 0.2155 0.3796 0.2037 -0.0717 -0.0117 0.0439  193 LYS B O   
1540 C CB  . LYS A 196 ? 0.2172 0.4259 0.2372 -0.0774 -0.0063 0.0461  193 LYS B CB  
1541 C CG  . LYS A 196 ? 0.2501 0.4509 0.2570 -0.0947 -0.0097 0.0435  193 LYS B CG  
1542 C CD  . LYS A 196 ? 0.3411 0.5638 0.3542 -0.1105 -0.0103 0.0425  193 LYS B CD  
1543 C CE  . LYS A 196 ? 0.3661 0.5708 0.3627 -0.1275 -0.0144 0.0400  193 LYS B CE  
1544 N NZ  . LYS A 196 ? 0.4060 0.6182 0.4003 -0.1291 -0.0216 0.0373  193 LYS B NZ  
1545 N N   . THR A 197 ? 0.1781 0.3755 0.1913 -0.0557 -0.0132 0.0506  194 THR B N   
1546 C CA  . THR A 197 ? 0.1881 0.3849 0.1931 -0.0530 -0.0181 0.0523  194 THR B CA  
1547 C C   . THR A 197 ? 0.1885 0.3593 0.1784 -0.0498 -0.0143 0.0514  194 THR B C   
1548 O O   . THR A 197 ? 0.1950 0.3581 0.1701 -0.0551 -0.0162 0.0480  194 THR B O   
1549 C CB  . THR A 197 ? 0.1745 0.3888 0.1926 -0.0418 -0.0222 0.0582  194 THR B CB  
1550 O OG1 . THR A 197 ? 0.1665 0.4078 0.1977 -0.0461 -0.0267 0.0569  194 THR B OG1 
1551 C CG2 . THR A 197 ? 0.1940 0.4064 0.2015 -0.0386 -0.0273 0.0624  194 THR B CG2 
1552 N N   . ALA A 198 ? 0.1722 0.3314 0.1665 -0.0414 -0.0091 0.0535  195 ALA B N   
1553 C CA  . ALA A 198 ? 0.1780 0.3171 0.1621 -0.0375 -0.0051 0.0525  195 ALA B CA  
1554 C C   . ALA A 198 ? 0.2020 0.3232 0.1731 -0.0451 -0.0037 0.0454  195 ALA B C   
1555 O O   . ALA A 198 ? 0.2177 0.3290 0.1765 -0.0453 -0.0032 0.0416  195 ALA B O   
1556 C CB  . ALA A 198 ? 0.1747 0.3072 0.1682 -0.0287 -0.0007 0.0555  195 ALA B CB  
1557 N N   . PHE A 199 ? 0.1931 0.3102 0.1662 -0.0515 -0.0034 0.0435  196 PHE B N   
1558 C CA  . PHE A 199 ? 0.2136 0.3110 0.1743 -0.0596 -0.0040 0.0379  196 PHE B CA  
1559 C C   . PHE A 199 ? 0.2218 0.3203 0.1711 -0.0683 -0.0088 0.0329  196 PHE B C   
1560 O O   . PHE A 199 ? 0.2651 0.3454 0.2016 -0.0684 -0.0089 0.0269  196 PHE B O   
1561 C CB  . PHE A 199 ? 0.2196 0.3156 0.1839 -0.0674 -0.0037 0.0392  196 PHE B CB  
1562 C CG  . PHE A 199 ? 0.2669 0.3374 0.2177 -0.0758 -0.0054 0.0353  196 PHE B CG  
1563 C CD1 . PHE A 199 ? 0.2952 0.3629 0.2372 -0.0894 -0.0101 0.0319  196 PHE B CD1 
1564 C CD2 . PHE A 199 ? 0.2670 0.3150 0.2138 -0.0702 -0.0036 0.0350  196 PHE B CD2 
1565 C CE1 . PHE A 199 ? 0.3215 0.3610 0.2500 -0.0972 -0.0129 0.0284  196 PHE B CE1 
1566 C CE2 . PHE A 199 ? 0.3022 0.3237 0.2364 -0.0764 -0.0067 0.0319  196 PHE B CE2 
1567 C CZ  . PHE A 199 ? 0.3282 0.3435 0.2526 -0.0902 -0.0115 0.0287  196 PHE B CZ  
1568 N N   . ASP A 200 ? 0.2337 0.3540 0.1880 -0.0743 -0.0129 0.0347  197 ASP B N   
1569 C CA  . ASP A 200 ? 0.2566 0.3803 0.2005 -0.0844 -0.0187 0.0298  197 ASP B CA  
1570 C C   . ASP A 200 ? 0.2670 0.3893 0.1997 -0.0785 -0.0195 0.0274  197 ASP B C   
1571 O O   . ASP A 200 ? 0.2758 0.3875 0.1933 -0.0847 -0.0223 0.0198  197 ASP B O   
1572 C CB  . ASP A 200 ? 0.2654 0.4166 0.2205 -0.0923 -0.0234 0.0325  197 ASP B CB  
1573 C CG  . ASP A 200 ? 0.2803 0.4339 0.2419 -0.1035 -0.0225 0.0328  197 ASP B CG  
1574 O OD1 . ASP A 200 ? 0.2720 0.4005 0.2245 -0.1080 -0.0203 0.0308  197 ASP B OD1 
1575 O OD2 . ASP A 200 ? 0.2787 0.4602 0.2541 -0.1080 -0.0245 0.0352  197 ASP B OD2 
1576 N N   . GLU A 201 ? 0.2395 0.3725 0.1790 -0.0676 -0.0173 0.0338  198 GLU B N   
1577 C CA  . GLU A 201 ? 0.2576 0.3905 0.1855 -0.0629 -0.0170 0.0334  198 GLU B CA  
1578 C C   . GLU A 201 ? 0.2548 0.3654 0.1712 -0.0595 -0.0112 0.0260  198 GLU B C   
1579 O O   . GLU A 201 ? 0.2531 0.3609 0.1542 -0.0607 -0.0113 0.0200  198 GLU B O   
1580 C CB  . GLU A 201 ? 0.2482 0.3946 0.1853 -0.0534 -0.0164 0.0434  198 GLU B CB  
1581 C CG  . GLU A 201 ? 0.2592 0.4291 0.2058 -0.0545 -0.0240 0.0496  198 GLU B CG  
1582 C CD  . GLU A 201 ? 0.2807 0.4594 0.2390 -0.0440 -0.0247 0.0599  198 GLU B CD  
1583 O OE1 . GLU A 201 ? 0.2850 0.4529 0.2480 -0.0368 -0.0189 0.0627  198 GLU B OE1 
1584 O OE2 . GLU A 201 ? 0.3144 0.5110 0.2777 -0.0429 -0.0323 0.0653  198 GLU B OE2 
1585 N N   . ALA A 202 ? 0.2466 0.3434 0.1704 -0.0547 -0.0065 0.0262  199 ALA B N   
1586 C CA  . ALA A 202 ? 0.2597 0.3359 0.1758 -0.0504 -0.0021 0.0186  199 ALA B CA  
1587 C C   . ALA A 202 ? 0.2885 0.3474 0.1908 -0.0582 -0.0057 0.0078  199 ALA B C   
1588 O O   . ALA A 202 ? 0.3123 0.3625 0.2028 -0.0553 -0.0040 -0.0010 199 ALA B O   
1589 C CB  . ALA A 202 ? 0.2398 0.3062 0.1672 -0.0441 0.0017  0.0216  199 ALA B CB  
1590 N N   . ILE A 203 ? 0.2769 0.3313 0.1807 -0.0682 -0.0106 0.0083  200 ILE B N   
1591 C CA  . ILE A 203 ? 0.3015 0.3387 0.1921 -0.0784 -0.0158 -0.0008 200 ILE B CA  
1592 C C   . ILE A 203 ? 0.3254 0.3708 0.2026 -0.0823 -0.0190 -0.0076 200 ILE B C   
1593 O O   . ILE A 203 ? 0.3297 0.3577 0.1923 -0.0821 -0.0196 -0.0191 200 ILE B O   
1594 C CB  . ILE A 203 ? 0.3023 0.3407 0.1982 -0.0914 -0.0203 0.0036  200 ILE B CB  
1595 C CG1 . ILE A 203 ? 0.2970 0.3238 0.2015 -0.0894 -0.0176 0.0094  200 ILE B CG1 
1596 C CG2 . ILE A 203 ? 0.3279 0.3507 0.2098 -0.1052 -0.0271 -0.0049 200 ILE B CG2 
1597 C CD1 . ILE A 203 ? 0.3162 0.3093 0.2115 -0.0865 -0.0181 0.0039  200 ILE B CD1 
1598 N N   . ALA A 204 ? 0.3178 0.3902 0.1996 -0.0849 -0.0214 -0.0010 201 ALA B N   
1599 C CA  . ALA A 204 ? 0.3369 0.4197 0.2051 -0.0903 -0.0261 -0.0061 201 ALA B CA  
1600 C C   . ALA A 204 ? 0.3365 0.4166 0.1920 -0.0814 -0.0210 -0.0116 201 ALA B C   
1601 O O   . ALA A 204 ? 0.3479 0.4264 0.1864 -0.0860 -0.0239 -0.0209 201 ALA B O   
1602 C CB  . ALA A 204 ? 0.3289 0.4417 0.2058 -0.0937 -0.0313 0.0032  201 ALA B CB  
1603 N N   . GLU A 205 ? 0.3292 0.4100 0.1926 -0.0697 -0.0133 -0.0064 202 GLU B N   
1604 C CA  . GLU A 205 ? 0.3559 0.4374 0.2091 -0.0619 -0.0067 -0.0111 202 GLU B CA  
1605 C C   . GLU A 205 ? 0.3247 0.3870 0.1807 -0.0531 0.0000  -0.0185 202 GLU B C   
1606 O O   . GLU A 205 ? 0.3222 0.3903 0.1791 -0.0449 0.0073  -0.0181 202 GLU B O   
1607 C CB  . GLU A 205 ? 0.3925 0.4972 0.2495 -0.0589 -0.0056 0.0016  202 GLU B CB  
1608 C CG  . GLU A 205 ? 0.4796 0.5993 0.3217 -0.0666 -0.0124 0.0013  202 GLU B CG  
1609 C CD  . GLU A 205 ? 0.5649 0.7056 0.4145 -0.0681 -0.0187 0.0153  202 GLU B CD  
1610 O OE1 . GLU A 205 ? 0.6794 0.8292 0.5244 -0.0764 -0.0275 0.0140  202 GLU B OE1 
1611 O OE2 . GLU A 205 ? 0.5764 0.7239 0.4373 -0.0611 -0.0159 0.0269  202 GLU B OE2 
1612 N N   . LEU A 206 ? 0.3218 0.3608 0.1763 -0.0559 -0.0034 -0.0266 203 LEU B N   
1613 C CA  . LEU A 206 ? 0.3235 0.3416 0.1792 -0.0469 0.0006  -0.0352 203 LEU B CA  
1614 C C   . LEU A 206 ? 0.3465 0.3639 0.1891 -0.0404 0.0056  -0.0490 203 LEU B C   
1615 O O   . LEU A 206 ? 0.3488 0.3585 0.1967 -0.0296 0.0110  -0.0549 203 LEU B O   
1616 C CB  . LEU A 206 ? 0.3324 0.3228 0.1873 -0.0520 -0.0058 -0.0396 203 LEU B CB  
1617 C CG  . LEU A 206 ? 0.3240 0.3106 0.1937 -0.0532 -0.0071 -0.0278 203 LEU B CG  
1618 C CD1 . LEU A 206 ? 0.3437 0.3042 0.2069 -0.0636 -0.0150 -0.0311 203 LEU B CD1 
1619 C CD2 . LEU A 206 ? 0.3045 0.2872 0.1859 -0.0403 -0.0015 -0.0251 203 LEU B CD2 
1620 N N   . ASP A 207 ? 0.3669 0.3944 0.1933 -0.0469 0.0037  -0.0544 204 ASP B N   
1621 C CA  . ASP A 207 ? 0.3982 0.4312 0.2097 -0.0420 0.0094  -0.0675 204 ASP B CA  
1622 C C   . ASP A 207 ? 0.4034 0.4565 0.2218 -0.0327 0.0202  -0.0622 204 ASP B C   
1623 O O   . ASP A 207 ? 0.4373 0.4934 0.2476 -0.0263 0.0271  -0.0745 204 ASP B O   
1624 C CB  . ASP A 207 ? 0.4164 0.4593 0.2084 -0.0524 0.0043  -0.0717 204 ASP B CB  
1625 C CG  . ASP A 207 ? 0.3977 0.4665 0.1914 -0.0587 0.0019  -0.0553 204 ASP B CG  
1626 O OD1 . ASP A 207 ? 0.3681 0.4389 0.1769 -0.0620 -0.0026 -0.0426 204 ASP B OD1 
1627 O OD2 . ASP A 207 ? 0.4066 0.4933 0.1861 -0.0598 0.0046  -0.0556 204 ASP B OD2 
1628 N N   . THR A 208 ? 0.3887 0.4568 0.2202 -0.0332 0.0214  -0.0448 205 THR B N   
1629 C CA  . THR A 208 ? 0.4040 0.4905 0.2427 -0.0274 0.0302  -0.0368 205 THR B CA  
1630 C C   . THR A 208 ? 0.3540 0.4316 0.2124 -0.0178 0.0345  -0.0362 205 THR B C   
1631 O O   . THR A 208 ? 0.3510 0.4428 0.2181 -0.0135 0.0417  -0.0299 205 THR B O   
1632 C CB  . THR A 208 ? 0.4105 0.5132 0.2536 -0.0333 0.0268  -0.0182 205 THR B CB  
1633 O OG1 . THR A 208 ? 0.4881 0.5830 0.3492 -0.0330 0.0220  -0.0087 205 THR B OG1 
1634 C CG2 . THR A 208 ? 0.4616 0.5743 0.2876 -0.0426 0.0201  -0.0165 205 THR B CG2 
1635 N N   . LEU A 209 ? 0.3264 0.3817 0.1926 -0.0159 0.0292  -0.0395 206 LEU B N   
1636 C CA  . LEU A 209 ? 0.3082 0.3546 0.1917 -0.0068 0.0316  -0.0386 206 LEU B CA  
1637 C C   . LEU A 209 ? 0.3305 0.3718 0.2125 0.0035  0.0370  -0.0547 206 LEU B C   
1638 O O   . LEU A 209 ? 0.3388 0.3609 0.2116 0.0048  0.0329  -0.0677 206 LEU B O   
1639 C CB  . LEU A 209 ? 0.3011 0.3258 0.1906 -0.0097 0.0233  -0.0349 206 LEU B CB  
1640 C CG  . LEU A 209 ? 0.2872 0.3009 0.1922 -0.0011 0.0238  -0.0332 206 LEU B CG  
1641 C CD1 . LEU A 209 ? 0.2686 0.3011 0.1892 0.0039  0.0300  -0.0234 206 LEU B CD1 
1642 C CD2 . LEU A 209 ? 0.2899 0.2845 0.1966 -0.0069 0.0156  -0.0278 206 LEU B CD2 
1643 N N   . SER A 210 ? 0.3259 0.3854 0.2175 0.0106  0.0460  -0.0541 207 SER B N   
1644 C CA  . SER A 210 ? 0.3554 0.4161 0.2496 0.0219  0.0522  -0.0699 207 SER B CA  
1645 C C   . SER A 210 ? 0.3728 0.4085 0.2790 0.0309  0.0461  -0.0748 207 SER B C   
1646 O O   . SER A 210 ? 0.3649 0.3921 0.2819 0.0292  0.0411  -0.0630 207 SER B O   
1647 C CB  . SER A 210 ? 0.3459 0.4353 0.2503 0.0256  0.0634  -0.0665 207 SER B CB  
1648 O OG  . SER A 210 ? 0.3242 0.4140 0.2490 0.0284  0.0624  -0.0550 207 SER B OG  
1649 N N   . GLU A 211 ? 0.4111 0.4363 0.3151 0.0409  0.0468  -0.0925 208 GLU B N   
1650 C CA  . GLU A 211 ? 0.4562 0.4582 0.3716 0.0522  0.0409  -0.0986 208 GLU B CA  
1651 C C   . GLU A 211 ? 0.4323 0.4465 0.3704 0.0586  0.0433  -0.0888 208 GLU B C   
1652 O O   . GLU A 211 ? 0.4439 0.4393 0.3899 0.0602  0.0353  -0.0820 208 GLU B O   
1653 C CB  . GLU A 211 ? 0.5174 0.5153 0.4276 0.0638  0.0439  -0.1210 208 GLU B CB  
1654 C CG  . GLU A 211 ? 0.5791 0.5526 0.5006 0.0788  0.0374  -0.1310 208 GLU B CG  
1655 C CD  . GLU A 211 ? 0.6628 0.6179 0.5714 0.0866  0.0353  -0.1535 208 GLU B CD  
1656 O OE1 . GLU A 211 ? 0.7458 0.7115 0.6680 0.1029  0.0404  -0.1663 208 GLU B OE1 
1657 O OE2 . GLU A 211 ? 0.6229 0.5585 0.5104 0.0772  0.0299  -0.1587 208 GLU B OE2 
1658 N N   . GLU A 212 ? 0.4148 0.4611 0.3620 0.0599  0.0539  -0.0865 209 GLU B N   
1659 C CA  . GLU A 212 ? 0.3882 0.4497 0.3571 0.0645  0.0569  -0.0781 209 GLU B CA  
1660 C C   . GLU A 212 ? 0.3339 0.3898 0.3064 0.0550  0.0513  -0.0591 209 GLU B C   
1661 O O   . GLU A 212 ? 0.3308 0.3818 0.3183 0.0596  0.0474  -0.0537 209 GLU B O   
1662 C CB  . GLU A 212 ? 0.4231 0.5212 0.3979 0.0637  0.0699  -0.0784 209 GLU B CB  
1663 C CG  . GLU A 212 ? 0.5054 0.6167 0.4789 0.0739  0.0779  -0.0985 209 GLU B CG  
1664 C CD  . GLU A 212 ? 0.6001 0.7089 0.5499 0.0714  0.0807  -0.1117 209 GLU B CD  
1665 O OE1 . GLU A 212 ? 0.5440 0.6496 0.4741 0.0587  0.0790  -0.1050 209 GLU B OE1 
1666 O OE2 . GLU A 212 ? 0.6535 0.7631 0.6056 0.0841  0.0838  -0.1314 209 GLU B OE2 
1667 N N   . SER A 213 ? 0.3010 0.3576 0.2598 0.0426  0.0503  -0.0501 210 SER B N   
1668 C CA  . SER A 213 ? 0.2742 0.3267 0.2358 0.0343  0.0453  -0.0341 210 SER B CA  
1669 C C   . SER A 213 ? 0.2580 0.2826 0.2144 0.0315  0.0349  -0.0322 210 SER B C   
1670 O O   . SER A 213 ? 0.2257 0.2486 0.1859 0.0257  0.0314  -0.0202 210 SER B O   
1671 C CB  . SER A 213 ? 0.2746 0.3433 0.2265 0.0240  0.0487  -0.0256 210 SER B CB  
1672 O OG  . SER A 213 ? 0.2922 0.3625 0.2515 0.0185  0.0455  -0.0106 210 SER B OG  
1673 N N   . TYR A 214 ? 0.2812 0.2841 0.2281 0.0345  0.0300  -0.0436 211 TYR B N   
1674 C CA  . TYR A 214 ? 0.2949 0.2720 0.2330 0.0277  0.0204  -0.0405 211 TYR B CA  
1675 C C   . TYR A 214 ? 0.2797 0.2478 0.2284 0.0278  0.0153  -0.0294 211 TYR B C   
1676 O O   . TYR A 214 ? 0.2618 0.2274 0.2075 0.0180  0.0119  -0.0192 211 TYR B O   
1677 C CB  . TYR A 214 ? 0.3163 0.2686 0.2435 0.0320  0.0155  -0.0552 211 TYR B CB  
1678 C CG  . TYR A 214 ? 0.3289 0.2519 0.2453 0.0230  0.0051  -0.0522 211 TYR B CG  
1679 C CD1 . TYR A 214 ? 0.3324 0.2323 0.2533 0.0262  -0.0024 -0.0480 211 TYR B CD1 
1680 C CD2 . TYR A 214 ? 0.3349 0.2534 0.2361 0.0102  0.0023  -0.0530 211 TYR B CD2 
1681 C CE1 . TYR A 214 ? 0.3454 0.2176 0.2549 0.0164  -0.0116 -0.0445 211 TYR B CE1 
1682 C CE2 . TYR A 214 ? 0.3466 0.2394 0.2387 0.0002  -0.0069 -0.0501 211 TYR B CE2 
1683 C CZ  . TYR A 214 ? 0.3526 0.2217 0.2481 0.0028  -0.0135 -0.0455 211 TYR B CZ  
1684 O OH  . TYR A 214 ? 0.3589 0.2032 0.2442 -0.0090 -0.0221 -0.0411 211 TYR B OH  
1685 N N   . LYS A 215 ? 0.3065 0.2721 0.2676 0.0391  0.0149  -0.0321 212 LYS B N   
1686 C CA  . LYS A 215 ? 0.3200 0.2759 0.2893 0.0402  0.0091  -0.0231 212 LYS B CA  
1687 C C   . LYS A 215 ? 0.2701 0.2449 0.2462 0.0332  0.0125  -0.0102 212 LYS B C   
1688 O O   . LYS A 215 ? 0.2490 0.2158 0.2227 0.0265  0.0080  -0.0014 212 LYS B O   
1689 C CB  . LYS A 215 ? 0.3689 0.3219 0.3517 0.0547  0.0074  -0.0291 212 LYS B CB  
1690 C CG  . LYS A 215 ? 0.4713 0.3930 0.4494 0.0626  -0.0024 -0.0362 212 LYS B CG  
1691 C CD  . LYS A 215 ? 0.5758 0.4753 0.5365 0.0590  -0.0058 -0.0451 212 LYS B CD  
1692 C CE  . LYS A 215 ? 0.7316 0.5951 0.6869 0.0668  -0.0170 -0.0519 212 LYS B CE  
1693 N NZ  . LYS A 215 ? 0.7467 0.5842 0.6896 0.0548  -0.0263 -0.0403 212 LYS B NZ  
1694 N N   . ASP A 216 ? 0.2494 0.2490 0.2340 0.0350  0.0205  -0.0096 213 ASP B N   
1695 C CA  . ASP A 216 ? 0.2397 0.2558 0.2310 0.0294  0.0235  0.0015  213 ASP B CA  
1696 C C   . ASP A 216 ? 0.2232 0.2386 0.2045 0.0186  0.0216  0.0083  213 ASP B C   
1697 O O   . ASP A 216 ? 0.2176 0.2344 0.2029 0.0146  0.0195  0.0169  213 ASP B O   
1698 C CB  . ASP A 216 ? 0.2436 0.2839 0.2424 0.0311  0.0320  0.0013  213 ASP B CB  
1699 C CG  . ASP A 216 ? 0.2608 0.3107 0.2750 0.0404  0.0351  -0.0033 213 ASP B CG  
1700 O OD1 . ASP A 216 ? 0.2663 0.3055 0.2880 0.0460  0.0297  -0.0039 213 ASP B OD1 
1701 O OD2 . ASP A 216 ? 0.2808 0.3500 0.2989 0.0415  0.0428  -0.0063 213 ASP B OD2 
1702 N N   . SER A 217 ? 0.2233 0.2396 0.1926 0.0144  0.0227  0.0037  214 SER B N   
1703 C CA  . SER A 217 ? 0.2255 0.2466 0.1871 0.0045  0.0210  0.0093  214 SER B CA  
1704 C C   . SER A 217 ? 0.2215 0.2257 0.1778 -0.0017 0.0142  0.0112  214 SER B C   
1705 O O   . SER A 217 ? 0.2137 0.2249 0.1725 -0.0077 0.0129  0.0191  214 SER B O   
1706 C CB  . SER A 217 ? 0.2421 0.2695 0.1917 0.0013  0.0230  0.0036  214 SER B CB  
1707 O OG  . SER A 217 ? 0.2392 0.2855 0.1929 0.0047  0.0298  0.0049  214 SER B OG  
1708 N N   . THR A 218 ? 0.2382 0.2209 0.1871 -0.0003 0.0101  0.0040  215 THR B N   
1709 C CA  . THR A 218 ? 0.2490 0.2128 0.1902 -0.0083 0.0033  0.0063  215 THR B CA  
1710 C C   . THR A 218 ? 0.2496 0.2114 0.1982 -0.0084 0.0015  0.0150  215 THR B C   
1711 O O   . THR A 218 ? 0.2392 0.1996 0.1838 -0.0182 -0.0011 0.0208  215 THR B O   
1712 C CB  . THR A 218 ? 0.2775 0.2142 0.2082 -0.0068 -0.0021 -0.0029 215 THR B CB  
1713 O OG1 . THR A 218 ? 0.2868 0.2139 0.2242 0.0058  -0.0027 -0.0072 215 THR B OG1 
1714 C CG2 . THR A 218 ? 0.2960 0.2337 0.2160 -0.0096 -0.0012 -0.0124 215 THR B CG2 
1715 N N   . LEU A 219 ? 0.2346 0.1996 0.1940 0.0015  0.0032  0.0156  216 LEU B N   
1716 C CA  . LEU A 219 ? 0.2565 0.2226 0.2223 0.0014  0.0017  0.0234  216 LEU B CA  
1717 C C   . LEU A 219 ? 0.2311 0.2156 0.2003 -0.0056 0.0047  0.0303  216 LEU B C   
1718 O O   . LEU A 219 ? 0.2325 0.2148 0.1993 -0.0116 0.0025  0.0354  216 LEU B O   
1719 C CB  . LEU A 219 ? 0.2764 0.2482 0.2550 0.0125  0.0034  0.0222  216 LEU B CB  
1720 C CG  . LEU A 219 ? 0.3247 0.2992 0.3106 0.0136  0.0017  0.0286  216 LEU B CG  
1721 C CD1 . LEU A 219 ? 0.3892 0.3409 0.3669 0.0133  -0.0061 0.0298  216 LEU B CD1 
1722 C CD2 . LEU A 219 ? 0.3586 0.3467 0.3598 0.0224  0.0048  0.0274  216 LEU B CD2 
1723 N N   . ILE A 220 ? 0.2139 0.2166 0.1881 -0.0047 0.0094  0.0305  217 ILE B N   
1724 C CA  . ILE A 220 ? 0.1936 0.2136 0.1733 -0.0084 0.0113  0.0365  217 ILE B CA  
1725 C C   . ILE A 220 ? 0.1875 0.2098 0.1594 -0.0185 0.0091  0.0372  217 ILE B C   
1726 O O   . ILE A 220 ? 0.1860 0.2184 0.1618 -0.0226 0.0091  0.0415  217 ILE B O   
1727 C CB  . ILE A 220 ? 0.1849 0.2210 0.1724 -0.0039 0.0156  0.0381  217 ILE B CB  
1728 C CG1 . ILE A 220 ? 0.2088 0.2440 0.2057 0.0042  0.0178  0.0375  217 ILE B CG1 
1729 C CG2 . ILE A 220 ? 0.1753 0.2259 0.1694 -0.0060 0.0158  0.0444  217 ILE B CG2 
1730 C CD1 . ILE A 220 ? 0.2134 0.2627 0.2170 0.0070  0.0223  0.0397  217 ILE B CD1 
1731 N N   . MET A 221 ? 0.1935 0.2085 0.1552 -0.0225 0.0074  0.0322  218 MET B N   
1732 C CA  . MET A 221 ? 0.2162 0.2316 0.1701 -0.0338 0.0042  0.0321  218 MET B CA  
1733 C C   . MET A 221 ? 0.2240 0.2289 0.1747 -0.0411 0.0015  0.0355  218 MET B C   
1734 O O   . MET A 221 ? 0.2256 0.2424 0.1774 -0.0500 0.0012  0.0389  218 MET B O   
1735 C CB  . MET A 221 ? 0.2334 0.2377 0.1754 -0.0364 0.0021  0.0244  218 MET B CB  
1736 C CG  . MET A 221 ? 0.2346 0.2539 0.1766 -0.0325 0.0051  0.0219  218 MET B CG  
1737 S SD  . MET A 221 ? 0.2814 0.2875 0.2072 -0.0354 0.0027  0.0104  218 MET B SD  
1738 C CE  . MET A 221 ? 0.2924 0.2971 0.2095 -0.0513 -0.0037 0.0104  218 MET B CE  
1739 N N   . GLN A 222 ? 0.2342 0.2181 0.1811 -0.0371 -0.0007 0.0347  219 GLN B N   
1740 C CA  . GLN A 222 ? 0.2467 0.2192 0.1886 -0.0433 -0.0037 0.0394  219 GLN B CA  
1741 C C   . GLN A 222 ? 0.2234 0.2143 0.1741 -0.0433 -0.0002 0.0450  219 GLN B C   
1742 O O   . GLN A 222 ? 0.2155 0.2099 0.1619 -0.0536 -0.0006 0.0488  219 GLN B O   
1743 C CB  . GLN A 222 ? 0.2616 0.2075 0.1976 -0.0374 -0.0083 0.0379  219 GLN B CB  
1744 C CG  . GLN A 222 ? 0.3064 0.2308 0.2315 -0.0396 -0.0128 0.0314  219 GLN B CG  
1745 C CD  . GLN A 222 ? 0.3307 0.2347 0.2555 -0.0272 -0.0161 0.0258  219 GLN B CD  
1746 O OE1 . GLN A 222 ? 0.3573 0.2565 0.2871 -0.0194 -0.0178 0.0285  219 GLN B OE1 
1747 N NE2 . GLN A 222 ? 0.3413 0.2339 0.2604 -0.0250 -0.0177 0.0168  219 GLN B NE2 
1748 N N   . LEU A 223 ? 0.2091 0.2125 0.1716 -0.0329 0.0032  0.0450  220 LEU B N   
1749 C CA  . LEU A 223 ? 0.1848 0.2044 0.1559 -0.0317 0.0061  0.0485  220 LEU B CA  
1750 C C   . LEU A 223 ? 0.1850 0.2263 0.1607 -0.0378 0.0084  0.0494  220 LEU B C   
1751 O O   . LEU A 223 ? 0.1690 0.2211 0.1467 -0.0420 0.0100  0.0513  220 LEU B O   
1752 C CB  . LEU A 223 ? 0.1809 0.2062 0.1635 -0.0200 0.0083  0.0478  220 LEU B CB  
1753 C CG  . LEU A 223 ? 0.2067 0.2160 0.1884 -0.0136 0.0059  0.0468  220 LEU B CG  
1754 C CD1 . LEU A 223 ? 0.1969 0.2142 0.1907 -0.0043 0.0084  0.0458  220 LEU B CD1 
1755 C CD2 . LEU A 223 ? 0.2379 0.2400 0.2145 -0.0164 0.0033  0.0498  220 LEU B CD2 
1756 N N   . LEU A 224 ? 0.1869 0.2364 0.1646 -0.0376 0.0084  0.0476  221 LEU B N   
1757 C CA  . LEU A 224 ? 0.1925 0.2631 0.1751 -0.0433 0.0088  0.0483  221 LEU B CA  
1758 C C   . LEU A 224 ? 0.2046 0.2761 0.1802 -0.0569 0.0077  0.0490  221 LEU B C   
1759 O O   . LEU A 224 ? 0.1705 0.2620 0.1533 -0.0606 0.0099  0.0502  221 LEU B O   
1760 C CB  . LEU A 224 ? 0.1913 0.2670 0.1733 -0.0420 0.0074  0.0466  221 LEU B CB  
1761 C CG  . LEU A 224 ? 0.1989 0.2810 0.1891 -0.0308 0.0090  0.0481  221 LEU B CG  
1762 C CD1 . LEU A 224 ? 0.2291 0.3092 0.2125 -0.0302 0.0080  0.0462  221 LEU B CD1 
1763 C CD2 . LEU A 224 ? 0.1970 0.2999 0.2001 -0.0272 0.0092  0.0512  221 LEU B CD2 
1764 N N   . ARG A 225 ? 0.2225 0.2725 0.1846 -0.0643 0.0042  0.0477  222 ARG B N   
1765 C CA  . ARG A 225 ? 0.2431 0.2896 0.1964 -0.0796 0.0024  0.0495  222 ARG B CA  
1766 C C   . ARG A 225 ? 0.2400 0.2894 0.1929 -0.0828 0.0050  0.0538  222 ARG B C   
1767 O O   . ARG A 225 ? 0.2203 0.2869 0.1743 -0.0940 0.0071  0.0557  222 ARG B O   
1768 C CB  . ARG A 225 ? 0.2789 0.2955 0.2166 -0.0863 -0.0030 0.0477  222 ARG B CB  
1769 C CG  . ARG A 225 ? 0.3171 0.3259 0.2441 -0.1043 -0.0056 0.0511  222 ARG B CG  
1770 C CD  . ARG A 225 ? 0.3525 0.3319 0.2649 -0.1116 -0.0122 0.0481  222 ARG B CD  
1771 N NE  . ARG A 225 ? 0.3724 0.3399 0.2731 -0.1303 -0.0154 0.0531  222 ARG B NE  
1772 C CZ  . ARG A 225 ? 0.4114 0.3593 0.3019 -0.1348 -0.0174 0.0593  222 ARG B CZ  
1773 N NH1 . ARG A 225 ? 0.4424 0.3743 0.3315 -0.1213 -0.0183 0.0605  222 ARG B NH1 
1774 N NH2 . ARG A 225 ? 0.4662 0.4109 0.3472 -0.1544 -0.0191 0.0651  222 ARG B NH2 
1775 N N   . ASP A 226 ? 0.2310 0.2648 0.1814 -0.0741 0.0047  0.0549  223 ASP B N   
1776 C CA  . ASP A 226 ? 0.2413 0.2748 0.1871 -0.0778 0.0062  0.0589  223 ASP B CA  
1777 C C   . ASP A 226 ? 0.2146 0.2790 0.1730 -0.0757 0.0122  0.0579  223 ASP B C   
1778 O O   . ASP A 226 ? 0.2071 0.2819 0.1614 -0.0852 0.0149  0.0602  223 ASP B O   
1779 C CB  . ASP A 226 ? 0.2549 0.2649 0.1949 -0.0692 0.0029  0.0601  223 ASP B CB  
1780 C CG  . ASP A 226 ? 0.2881 0.2661 0.2152 -0.0711 -0.0039 0.0607  223 ASP B CG  
1781 O OD1 . ASP A 226 ? 0.3185 0.2881 0.2373 -0.0821 -0.0064 0.0609  223 ASP B OD1 
1782 O OD2 . ASP A 226 ? 0.3110 0.2727 0.2370 -0.0615 -0.0071 0.0605  223 ASP B OD2 
1783 N N   . ASN A 227 ? 0.2040 0.2826 0.1771 -0.0636 0.0140  0.0546  224 ASN B N   
1784 C CA  . ASN A 227 ? 0.1885 0.2952 0.1754 -0.0594 0.0185  0.0523  224 ASN B CA  
1785 C C   . ASN A 227 ? 0.1828 0.3128 0.1739 -0.0701 0.0201  0.0518  224 ASN B C   
1786 O O   . ASN A 227 ? 0.1825 0.3333 0.1781 -0.0739 0.0245  0.0506  224 ASN B O   
1787 C CB  . ASN A 227 ? 0.1662 0.2788 0.1668 -0.0448 0.0184  0.0501  224 ASN B CB  
1788 C CG  . ASN A 227 ? 0.1679 0.2658 0.1686 -0.0349 0.0181  0.0499  224 ASN B CG  
1789 O OD1 . ASN A 227 ? 0.1747 0.2589 0.1656 -0.0376 0.0175  0.0512  224 ASN B OD1 
1790 N ND2 . ASN A 227 ? 0.1507 0.2518 0.1622 -0.0242 0.0179  0.0490  224 ASN B ND2 
1791 N N   . LEU A 228 ? 0.1896 0.3176 0.1789 -0.0757 0.0167  0.0520  225 LEU B N   
1792 C CA  . LEU A 228 ? 0.1948 0.3453 0.1881 -0.0880 0.0171  0.0515  225 LEU B CA  
1793 C C   . LEU A 228 ? 0.2123 0.3626 0.1948 -0.1050 0.0193  0.0545  225 LEU B C   
1794 O O   . LEU A 228 ? 0.2190 0.3989 0.2102 -0.1119 0.0233  0.0534  225 LEU B O   
1795 C CB  . LEU A 228 ? 0.2058 0.3515 0.1969 -0.0913 0.0120  0.0506  225 LEU B CB  
1796 C CG  . LEU A 228 ? 0.2030 0.3576 0.2051 -0.0776 0.0101  0.0488  225 LEU B CG  
1797 C CD1 . LEU A 228 ? 0.2074 0.3507 0.2016 -0.0805 0.0052  0.0477  225 LEU B CD1 
1798 C CD2 . LEU A 228 ? 0.2077 0.3974 0.2283 -0.0739 0.0111  0.0474  225 LEU B CD2 
1799 N N   . THR A 229 ? 0.2156 0.3350 0.1802 -0.1108 0.0168  0.0584  226 THR B N   
1800 C CA  . THR A 229 ? 0.2519 0.3658 0.2025 -0.1277 0.0179  0.0634  226 THR B CA  
1801 C C   . THR A 229 ? 0.2398 0.3750 0.1942 -0.1261 0.0248  0.0632  226 THR B C   
1802 O O   . THR A 229 ? 0.2564 0.4140 0.2108 -0.1395 0.0295  0.0643  226 THR B O   
1803 C CB  . THR A 229 ? 0.2734 0.3451 0.2044 -0.1304 0.0115  0.0678  226 THR B CB  
1804 O OG1 . THR A 229 ? 0.2721 0.3284 0.2008 -0.1319 0.0060  0.0655  226 THR B OG1 
1805 C CG2 . THR A 229 ? 0.3017 0.3611 0.2148 -0.1484 0.0107  0.0752  226 THR B CG2 
1806 N N   . LEU A 230 ? 0.2420 0.3711 0.1997 -0.1104 0.0255  0.0611  227 LEU B N   
1807 C CA  . LEU A 230 ? 0.2266 0.3744 0.1885 -0.1055 0.0315  0.0585  227 LEU B CA  
1808 C C   . LEU A 230 ? 0.2228 0.4115 0.2039 -0.1039 0.0376  0.0525  227 LEU B C   
1809 O O   . LEU A 230 ? 0.2275 0.4396 0.2080 -0.1127 0.0439  0.0514  227 LEU B O   
1810 C CB  . LEU A 230 ? 0.2222 0.3552 0.1871 -0.0878 0.0296  0.0562  227 LEU B CB  
1811 C CG  . LEU A 230 ? 0.2259 0.3742 0.1939 -0.0815 0.0347  0.0520  227 LEU B CG  
1812 C CD1 . LEU A 230 ? 0.2491 0.3953 0.1978 -0.0958 0.0370  0.0564  227 LEU B CD1 
1813 C CD2 . LEU A 230 ? 0.2093 0.3426 0.1823 -0.0650 0.0317  0.0493  227 LEU B CD2 
1814 N N   . TRP A 231 ? 0.2159 0.4139 0.2132 -0.0934 0.0354  0.0488  228 TRP B N   
1815 C CA  . TRP A 231 ? 0.1877 0.4229 0.2061 -0.0871 0.0393  0.0426  228 TRP B CA  
1816 C C   . TRP A 231 ? 0.2058 0.4702 0.2296 -0.1027 0.0419  0.0424  228 TRP B C   
1817 O O   . TRP A 231 ? 0.1934 0.4942 0.2348 -0.0991 0.0466  0.0365  228 TRP B O   
1818 C CB  . TRP A 231 ? 0.1603 0.3920 0.1921 -0.0704 0.0346  0.0404  228 TRP B CB  
1819 C CG  . TRP A 231 ? 0.1510 0.3635 0.1824 -0.0553 0.0336  0.0393  228 TRP B CG  
1820 C CD1 . TRP A 231 ? 0.1527 0.3578 0.1782 -0.0518 0.0366  0.0375  228 TRP B CD1 
1821 C CD2 . TRP A 231 ? 0.1440 0.3429 0.1814 -0.0426 0.0288  0.0400  228 TRP B CD2 
1822 N NE1 . TRP A 231 ? 0.1544 0.3431 0.1836 -0.0379 0.0336  0.0366  228 TRP B NE1 
1823 C CE2 . TRP A 231 ? 0.1413 0.3260 0.1779 -0.0323 0.0293  0.0385  228 TRP B CE2 
1824 C CE3 . TRP A 231 ? 0.1388 0.3383 0.1817 -0.0399 0.0242  0.0418  228 TRP B CE3 
1825 C CZ2 . TRP A 231 ? 0.1349 0.3056 0.1767 -0.0205 0.0256  0.0394  228 TRP B CZ2 
1826 C CZ3 . TRP A 231 ? 0.1379 0.3222 0.1833 -0.0283 0.0208  0.0432  228 TRP B CZ3 
1827 C CH2 . TRP A 231 ? 0.1320 0.3021 0.1774 -0.0190 0.0218  0.0423  228 TRP B CH2 
1828 N N   . THR A 232 ? 0.2244 0.4740 0.2348 -0.1195 0.0385  0.0482  229 THR B N   
1829 C CA  . THR A 232 ? 0.2521 0.5255 0.2647 -0.1387 0.0404  0.0493  229 THR B CA  
1830 C C   . THR A 232 ? 0.3036 0.5757 0.2995 -0.1577 0.0454  0.0543  229 THR B C   
1831 O O   . THR A 232 ? 0.3297 0.6196 0.3254 -0.1767 0.0471  0.0564  229 THR B O   
1832 C CB  . THR A 232 ? 0.2520 0.5092 0.2600 -0.1466 0.0324  0.0519  229 THR B CB  
1833 O OG1 . THR A 232 ? 0.2574 0.4703 0.2438 -0.1494 0.0277  0.0570  229 THR B OG1 
1834 C CG2 . THR A 232 ? 0.2350 0.4992 0.2584 -0.1303 0.0277  0.0478  229 THR B CG2 
1835 N N   . GLY A 233 ? 0.3085 0.5638 0.2909 -0.1543 0.0478  0.0563  230 GLY B N   
1836 C CA  . GLY A 233 ? 0.3566 0.6158 0.3227 -0.1719 0.0533  0.0613  230 GLY B CA  
1837 C C   . GLY A 233 ? 0.3683 0.5852 0.3077 -0.1870 0.0467  0.0720  230 GLY B C   
1838 O O   . GLY A 233 ? 0.3705 0.5880 0.2939 -0.2043 0.0500  0.0782  230 GLY B O   
1839 N N   . GLY A 234 ? 0.3606 0.5408 0.2946 -0.1799 0.0375  0.0738  231 GLY B N   
1840 C CA  . GLY A 234 ? 0.3733 0.5094 0.2839 -0.1898 0.0296  0.0824  231 GLY B CA  
1841 C C   . GLY A 234 ? 0.3782 0.4852 0.2739 -0.1804 0.0267  0.0861  231 GLY B C   
1842 O O   . GLY A 234 ? 0.3932 0.4615 0.2711 -0.1851 0.0186  0.0927  231 GLY B O   
1843 N N   . GLY A 235 ? 0.3862 0.5098 0.2888 -0.1671 0.0320  0.0816  232 GLY B N   
1844 C CA  . GLY A 235 ? 0.4186 0.5196 0.3067 -0.1605 0.0292  0.0850  232 GLY B CA  
1845 C C   . GLY A 235 ? 0.4090 0.4882 0.3047 -0.1394 0.0232  0.0811  232 GLY B C   
1846 O O   . GLY A 235 ? 0.3540 0.4333 0.2636 -0.1309 0.0214  0.0765  232 GLY B O   
1847 N N   . GLY A 236 ? 0.4017 0.4671 0.2888 -0.1315 0.0209  0.0825  233 GLY B N   
1848 C CA  . GLY A 236 ? 0.3870 0.4296 0.2777 -0.1142 0.0146  0.0806  233 GLY B CA  
1849 C C   . GLY A 236 ? 0.4084 0.4611 0.3022 -0.1031 0.0171  0.0765  233 GLY B C   
1850 O O   . GLY A 236 ? 0.4085 0.4864 0.3022 -0.1074 0.0243  0.0737  233 GLY B O   
1851 N N   . SER A 237 ? 0.3931 0.4269 0.2900 -0.0891 0.0111  0.0752  234 SER B N   
1852 C CA  . SER A 237 ? 0.4383 0.4789 0.3409 -0.0772 0.0119  0.0702  234 SER B CA  
1853 C C   . SER A 237 ? 0.3532 0.4149 0.2791 -0.0652 0.0172  0.0612  234 SER B C   
1854 O O   . SER A 237 ? 0.3974 0.4725 0.3339 -0.0668 0.0208  0.0593  234 SER B O   
1855 C CB  . SER A 237 ? 0.4719 0.4838 0.3686 -0.0692 0.0022  0.0735  234 SER B CB  
1856 O OG  . SER A 237 ? 0.5585 0.5538 0.4617 -0.0645 -0.0022 0.0741  234 SER B OG  
1857 N N   . ARG A 238 ? 0.3083 0.3729 0.2417 -0.0537 0.0170  0.0560  235 ARG B N   
1858 C CA  . ARG A 238 ? 0.2739 0.3520 0.2277 -0.0416 0.0199  0.0486  235 ARG B CA  
1859 C C   . ARG A 238 ? 0.2504 0.3235 0.2153 -0.0378 0.0184  0.0499  235 ARG B C   
1860 O O   . ARG A 238 ? 0.2321 0.2848 0.1923 -0.0374 0.0132  0.0539  235 ARG B O   
1861 C CB  . ARG A 238 ? 0.3030 0.3743 0.2604 -0.0313 0.0168  0.0448  235 ARG B CB  
1862 C CG  . ARG A 238 ? 0.2689 0.3465 0.2458 -0.0190 0.0177  0.0387  235 ARG B CG  
1863 C CD  . ARG A 238 ? 0.2983 0.3662 0.2773 -0.0117 0.0133  0.0358  235 ARG B CD  
1864 N NE  . ARG A 238 ? 0.2635 0.3325 0.2604 -0.0019 0.0131  0.0321  235 ARG B NE  
1865 C CZ  . ARG A 238 ? 0.2263 0.3079 0.2345 0.0036  0.0165  0.0260  235 ARG B CZ  
1866 N NH1 . ARG A 238 ? 0.2165 0.3140 0.2218 0.0017  0.0213  0.0209  235 ARG B NH1 
1867 N NH2 . ARG A 238 ? 0.2213 0.2999 0.2440 0.0110  0.0151  0.0253  235 ARG B NH2 
1868 N N   . ARG A 239 ? 0.2026 0.2951 0.1822 -0.0341 0.0227  0.0458  236 ARG B N   
1869 C CA  . ARG A 239 ? 0.1964 0.2875 0.1854 -0.0308 0.0214  0.0468  236 ARG B CA  
1870 C C   . ARG A 239 ? 0.1744 0.2476 0.1670 -0.0221 0.0172  0.0477  236 ARG B C   
1871 O O   . ARG A 239 ? 0.1782 0.2475 0.1740 -0.0153 0.0161  0.0455  236 ARG B O   
1872 C CB  . ARG A 239 ? 0.1791 0.2924 0.1846 -0.0249 0.0246  0.0425  236 ARG B CB  
1873 C CG  . ARG A 239 ? 0.1672 0.2822 0.1861 -0.0118 0.0241  0.0385  236 ARG B CG  
1874 C CD  . ARG A 239 ? 0.1684 0.2822 0.1849 -0.0082 0.0250  0.0339  236 ARG B CD  
1875 N NE  . ARG A 239 ? 0.1592 0.2699 0.1889 0.0032  0.0230  0.0308  236 ARG B NE  
1876 C CZ  . ARG A 239 ? 0.1581 0.2527 0.1907 0.0077  0.0193  0.0336  236 ARG B CZ  
1877 N NH1 . ARG A 239 ? 0.1731 0.2537 0.1968 0.0035  0.0169  0.0379  236 ARG B NH1 
1878 N NH2 . ARG A 239 ? 0.1431 0.2359 0.1876 0.0161  0.0176  0.0316  236 ARG B NH2 
1879 N N   . GLY A 240 ? 0.1745 0.2399 0.1676 -0.0223 0.0153  0.0497  237 GLY B N   
1880 C CA  . GLY A 240 ? 0.1822 0.2350 0.1799 -0.0144 0.0127  0.0499  237 GLY B CA  
1881 C C   . GLY A 240 ? 0.1706 0.2338 0.1822 -0.0072 0.0144  0.0487  237 GLY B C   
1882 O O   . GLY A 240 ? 0.1598 0.2359 0.1757 -0.0085 0.0160  0.0487  237 GLY B O   
1883 N N   . TPO A 241 ? 0.1555 0.2130 0.1739 -0.0001 0.0133  0.0484  238 TPO B N   
1884 C CA  . TPO A 241 ? 0.1424 0.2033 0.1702 0.0048  0.0140  0.0495  238 TPO B CA  
1885 C CB  . TPO A 241 ? 0.1314 0.1974 0.1701 0.0105  0.0140  0.0486  238 TPO B CB  
1886 C CG2 . TPO A 241 ? 0.1506 0.2296 0.1930 0.0111  0.0151  0.0466  238 TPO B CG2 
1887 O OG1 . TPO A 241 ? 0.1419 0.2010 0.1802 0.0120  0.0125  0.0462  238 TPO B OG1 
1888 P P   . TPO A 241 ? 0.1610 0.2193 0.2095 0.0173  0.0111  0.0440  238 TPO B P   
1889 O O1P . TPO A 241 ? 0.1398 0.1974 0.1971 0.0198  0.0110  0.0478  238 TPO B O1P 
1890 O O2P . TPO A 241 ? 0.1386 0.2057 0.1891 0.0193  0.0121  0.0397  238 TPO B O2P 
1891 O O3P . TPO A 241 ? 0.1427 0.1928 0.1878 0.0168  0.0085  0.0422  238 TPO B O3P 
1892 C C   . TPO A 241 ? 0.1461 0.1972 0.1724 0.0063  0.0133  0.0502  238 TPO B C   
1893 O O   . TPO A 241 ? 0.1339 0.1748 0.1540 0.0054  0.0114  0.0492  238 TPO B O   
1894 N N   . SER A 242 ? 0.1555 0.2108 0.1877 0.0088  0.0147  0.0519  239 SER B N   
1895 C CA  . SER A 242 ? 0.1693 0.2211 0.2002 0.0097  0.0158  0.0516  239 SER B CA  
1896 C C   . SER A 242 ? 0.1550 0.2005 0.1904 0.0133  0.0147  0.0498  239 SER B C   
1897 O O   . SER A 242 ? 0.1509 0.1972 0.1938 0.0152  0.0135  0.0502  239 SER B O   
1898 C CB  . SER A 242 ? 0.1991 0.2591 0.2346 0.0106  0.0179  0.0549  239 SER B CB  
1899 O OG  . SER A 242 ? 0.2289 0.2890 0.2622 0.0109  0.0203  0.0538  239 SER B OG  
1900 N N   . PRO A 243 ? 0.1712 0.2110 0.2035 0.0149  0.0144  0.0469  240 PRO B N   
1901 C CA  . PRO A 243 ? 0.1968 0.2358 0.2374 0.0196  0.0136  0.0450  240 PRO B CA  
1902 C C   . PRO A 243 ? 0.1856 0.2358 0.2374 0.0202  0.0171  0.0471  240 PRO B C   
1903 O O   . PRO A 243 ? 0.1901 0.2465 0.2406 0.0178  0.0203  0.0499  240 PRO B O   
1904 C CB  . PRO A 243 ? 0.2208 0.2535 0.2570 0.0225  0.0131  0.0404  240 PRO B CB  
1905 C CG  . PRO A 243 ? 0.2468 0.2799 0.2731 0.0185  0.0156  0.0402  240 PRO B CG  
1906 C CD  . PRO A 243 ? 0.2097 0.2448 0.2321 0.0130  0.0149  0.0444  240 PRO B CD  
1907 N N   . ALA A 244 ? 0.2081 0.2602 0.2704 0.0223  0.0154  0.0467  241 ALA B N   
1908 C CA  . ALA A 244 ? 0.2013 0.2634 0.2751 0.0212  0.0184  0.0489  241 ALA B CA  
1909 C C   . ALA A 244 ? 0.1856 0.2575 0.2612 0.0217  0.0238  0.0474  241 ALA B C   
1910 O O   . ALA A 244 ? 0.2028 0.2830 0.2807 0.0180  0.0280  0.0515  241 ALA B O   
1911 C CB  . ALA A 244 ? 0.2175 0.2805 0.3025 0.0226  0.0147  0.0475  241 ALA B CB  
1912 N N   . ARG A 245 ? 0.1761 0.2463 0.2501 0.0265  0.0234  0.0414  242 ARG B N   
1913 C CA  . ARG A 245 ? 0.1802 0.2600 0.2547 0.0286  0.0289  0.0371  242 ARG B CA  
1914 C C   . ARG A 245 ? 0.2192 0.2907 0.2779 0.0277  0.0294  0.0353  242 ARG B C   
1915 O O   . ARG A 245 ? 0.2346 0.2938 0.2870 0.0312  0.0254  0.0308  242 ARG B O   
1916 C CB  . ARG A 245 ? 0.1747 0.2581 0.2606 0.0357  0.0269  0.0307  242 ARG B CB  
1917 C CG  . ARG A 245 ? 0.2107 0.3040 0.2987 0.0410  0.0320  0.0228  242 ARG B CG  
1918 C CD  . ARG A 245 ? 0.1972 0.2995 0.3013 0.0495  0.0304  0.0159  242 ARG B CD  
1919 N NE  . ARG A 245 ? 0.1923 0.3141 0.3145 0.0467  0.0328  0.0182  242 ARG B NE  
1920 C CZ  . ARG A 245 ? 0.1825 0.3056 0.3175 0.0485  0.0263  0.0190  242 ARG B CZ  
1921 N NH1 . ARG A 245 ? 0.1726 0.2770 0.3016 0.0519  0.0169  0.0198  242 ARG B NH1 
1922 N NH2 . ARG A 245 ? 0.1651 0.3082 0.3177 0.0451  0.0288  0.0200  242 ARG B NH2 
1923 N N   . MET A 246 ? 0.2141 0.2915 0.2659 0.0225  0.0332  0.0395  243 MET B N   
1924 C CA  . MET A 246 ? 0.2388 0.3109 0.2760 0.0201  0.0331  0.0382  243 MET B CA  
1925 C C   . MET A 246 ? 0.2373 0.3135 0.2689 0.0228  0.0372  0.0302  243 MET B C   
1926 O O   . MET A 246 ? 0.2341 0.2990 0.2556 0.0236  0.0345  0.0250  243 MET B O   
1927 C CB  . MET A 246 ? 0.2315 0.3089 0.2639 0.0143  0.0339  0.0459  243 MET B CB  
1928 C CG  . MET A 246 ? 0.2529 0.3243 0.2885 0.0130  0.0291  0.0510  243 MET B CG  
1929 S SD  . MET A 246 ? 0.2839 0.3624 0.3188 0.0089  0.0291  0.0603  243 MET B SD  
1930 C CE  . MET A 246 ? 0.3256 0.4072 0.3743 0.0090  0.0307  0.0644  243 MET B CE  
1931 N N   . ALA A 247 ? 0.2709 0.3631 0.3081 0.0232  0.0439  0.0289  244 ALA B N   
1932 C CA  . ALA A 247 ? 0.2672 0.3675 0.2982 0.0256  0.0495  0.0202  244 ALA B CA  
1933 C C   . ALA A 247 ? 0.2933 0.4080 0.3391 0.0313  0.0544  0.0143  244 ALA B C   
1934 O O   . ALA A 247 ? 0.2523 0.3809 0.3090 0.0276  0.0578  0.0205  244 ALA B O   
1935 C CB  . ALA A 247 ? 0.3020 0.4128 0.3212 0.0183  0.0540  0.0249  244 ALA B CB  
1936 N N   . GLY A 248 ? 0.3508 0.4629 0.3976 0.0401  0.0546  0.0020  245 GLY B N   
1937 C CA  . GLY A 248 ? 0.3394 0.4698 0.4005 0.0471  0.0603  -0.0065 245 GLY B CA  
1938 C C   . GLY A 248 ? 0.3954 0.5276 0.4763 0.0517  0.0557  -0.0046 245 GLY B C   
1939 O O   . GLY A 248 ? 0.3858 0.5009 0.4662 0.0508  0.0475  0.0015  245 GLY B O   
1940 N N   . ASN A 249 ? 0.4034 0.5593 0.5015 0.0560  0.0616  -0.0103 246 ASN B N   
1941 C CA  . ASN A 249 ? 0.4508 0.6161 0.5705 0.0597  0.0583  -0.0095 246 ASN B CA  
1942 C C   . ASN A 249 ? 0.3934 0.5623 0.5178 0.0483  0.0576  0.0038  246 ASN B C   
1943 O O   . ASN A 249 ? 0.4067 0.5833 0.5238 0.0378  0.0638  0.0113  246 ASN B O   
1944 C CB  . ASN A 249 ? 0.5022 0.6984 0.6407 0.0652  0.0663  -0.0189 246 ASN B CB  
1945 C CG  . ASN A 249 ? 0.6361 0.8313 0.7773 0.0802  0.0658  -0.0347 246 ASN B CG  
1946 O OD1 . ASN A 249 ? 0.6644 0.8317 0.7951 0.0874  0.0570  -0.0381 246 ASN B OD1 
1947 N ND2 . ASN A 249 ? 0.6583 0.8841 0.8144 0.0852  0.0749  -0.0447 246 ASN B ND2 
1948 O OXT . ASN A 249 ? 0.4199 0.5839 0.5553 0.0503  0.0504  0.0060  246 ASN B OXT 
1949 N N   . ASP B 5   ? 0.8100 0.5254 0.6581 0.2062  0.0239  -0.0867 2   ASP A N   
1950 C CA  . ASP B 5   ? 0.8106 0.5450 0.6571 0.2141  0.0375  -0.0903 2   ASP A CA  
1951 C C   . ASP B 5   ? 0.7367 0.5136 0.6107 0.1980  0.0398  -0.0841 2   ASP A C   
1952 O O   . ASP B 5   ? 0.6950 0.5007 0.5978 0.1919  0.0380  -0.0758 2   ASP A O   
1953 C CB  . ASP B 5   ? 0.8353 0.5787 0.6854 0.2395  0.0511  -0.0901 2   ASP A CB  
1954 C CG  . ASP B 5   ? 0.8831 0.6554 0.7398 0.2483  0.0678  -0.0905 2   ASP A CG  
1955 O OD1 . ASP B 5   ? 0.8227 0.6389 0.7132 0.2470  0.0746  -0.0825 2   ASP A OD1 
1956 O OD2 . ASP B 5   ? 1.0279 0.7779 0.8552 0.2561  0.0738  -0.0985 2   ASP A OD2 
1957 N N   . LYS B 6   ? 0.7168 0.4966 0.5799 0.1933  0.0444  -0.0883 3   LYS A N   
1958 C CA  . LYS B 6   ? 0.6582 0.4697 0.5399 0.1776  0.0454  -0.0840 3   LYS A CA  
1959 C C   . LYS B 6   ? 0.6041 0.4587 0.5163 0.1838  0.0577  -0.0767 3   LYS A C   
1960 O O   . LYS B 6   ? 0.5434 0.4252 0.4818 0.1725  0.0541  -0.0697 3   LYS A O   
1961 C CB  . LYS B 6   ? 0.6761 0.4753 0.5344 0.1734  0.0470  -0.0904 3   LYS A CB  
1962 C CG  . LYS B 6   ? 0.6777 0.5075 0.5508 0.1621  0.0515  -0.0864 3   LYS A CG  
1963 C CD  . LYS B 6   ? 0.7139 0.5248 0.5614 0.1543  0.0470  -0.0925 3   LYS A CD  
1964 C CE  . LYS B 6   ? 0.7057 0.5453 0.5661 0.1463  0.0533  -0.0881 3   LYS A CE  
1965 N NZ  . LYS B 6   ? 0.7254 0.5524 0.5705 0.1333  0.0435  -0.0915 3   LYS A NZ  
1966 N N   . ASN B 7   ? 0.6550 0.5150 0.5635 0.2023  0.0719  -0.0782 4   ASN A N   
1967 C CA  . ASN B 7   ? 0.6318 0.5338 0.5707 0.2088  0.0842  -0.0710 4   ASN A CA  
1968 C C   . ASN B 7   ? 0.5858 0.5090 0.5549 0.2079  0.0781  -0.0635 4   ASN A C   
1969 O O   . ASN B 7   ? 0.5482 0.5063 0.5459 0.1984  0.0785  -0.0565 4   ASN A O   
1970 C CB  . ASN B 7   ? 0.7403 0.6433 0.6694 0.2299  0.1011  -0.0736 4   ASN A CB  
1971 C CG  . ASN B 7   ? 0.8131 0.7636 0.7778 0.2336  0.1137  -0.0650 4   ASN A CG  
1972 O OD1 . ASN B 7   ? 0.8687 0.8356 0.8527 0.2474  0.1180  -0.0611 4   ASN A OD1 
1973 N ND2 . ASN B 7   ? 0.8913 0.8651 0.8674 0.2202  0.1179  -0.0612 4   ASN A ND2 
1974 N N   . GLU B 8   ? 0.5613 0.4604 0.5216 0.2161  0.0707  -0.0649 5   GLU A N   
1975 C CA  . GLU B 8   ? 0.5580 0.4707 0.5411 0.2158  0.0632  -0.0580 5   GLU A CA  
1976 C C   . GLU B 8   ? 0.5006 0.4243 0.4971 0.1937  0.0514  -0.0532 5   GLU A C   
1977 O O   . GLU B 8   ? 0.4440 0.3981 0.4677 0.1902  0.0497  -0.0461 5   GLU A O   
1978 C CB  . GLU B 8   ? 0.6393 0.5148 0.6020 0.2289  0.0576  -0.0615 5   GLU A CB  
1979 C CG  . GLU B 8   ? 0.6816 0.5623 0.6610 0.2291  0.0481  -0.0545 5   GLU A CG  
1980 C CD  . GLU B 8   ? 0.7589 0.6189 0.7290 0.2509  0.0488  -0.0554 5   GLU A CD  
1981 O OE1 . GLU B 8   ? 0.8261 0.6470 0.7652 0.2596  0.0494  -0.0631 5   GLU A OE1 
1982 O OE2 . GLU B 8   ? 0.8268 0.7096 0.8202 0.2597  0.0483  -0.0486 5   GLU A OE2 
1983 N N   . LEU B 9   ? 0.4914 0.3884 0.4678 0.1802  0.0425  -0.0571 6   LEU A N   
1984 C CA  . LEU B 9   ? 0.4555 0.3619 0.4417 0.1599  0.0331  -0.0532 6   LEU A CA  
1985 C C   . LEU B 9   ? 0.4045 0.3468 0.4112 0.1511  0.0383  -0.0497 6   LEU A C   
1986 O O   . LEU B 9   ? 0.3480 0.3100 0.3731 0.1410  0.0330  -0.0439 6   LEU A O   
1987 C CB  . LEU B 9   ? 0.4811 0.3558 0.4432 0.1482  0.0248  -0.0585 6   LEU A CB  
1988 C CG  . LEU B 9   ? 0.5293 0.3690 0.4754 0.1499  0.0155  -0.0596 6   LEU A CG  
1989 C CD1 . LEU B 9   ? 0.5485 0.3563 0.4697 0.1397  0.0082  -0.0661 6   LEU A CD1 
1990 C CD2 . LEU B 9   ? 0.5036 0.3534 0.4665 0.1416  0.0077  -0.0513 6   LEU A CD2 
1991 N N   . VAL B 10  ? 0.4164 0.3643 0.4173 0.1546  0.0484  -0.0531 7   VAL A N   
1992 C CA  . VAL B 10  ? 0.3915 0.3703 0.4095 0.1465  0.0541  -0.0496 7   VAL A CA  
1993 C C   . VAL B 10  ? 0.3830 0.3964 0.4319 0.1516  0.0582  -0.0424 7   VAL A C   
1994 O O   . VAL B 10  ? 0.3530 0.3891 0.4204 0.1398  0.0547  -0.0376 7   VAL A O   
1995 C CB  . VAL B 10  ? 0.3863 0.3597 0.3877 0.1495  0.0644  -0.0542 7   VAL A CB  
1996 C CG1 . VAL B 10  ? 0.3566 0.3624 0.3768 0.1443  0.0732  -0.0494 7   VAL A CG1 
1997 C CG2 . VAL B 10  ? 0.4131 0.3579 0.3886 0.1393  0.0563  -0.0602 7   VAL A CG2 
1998 N N   . GLN B 11  ? 0.3994 0.4163 0.4534 0.1693  0.0649  -0.0419 8   GLN A N   
1999 C CA  . GLN B 11  ? 0.4012 0.4517 0.4864 0.1753  0.0672  -0.0349 8   GLN A CA  
2000 C C   . GLN B 11  ? 0.3702 0.4243 0.4673 0.1675  0.0533  -0.0303 8   GLN A C   
2001 O O   . GLN B 11  ? 0.3246 0.4084 0.4464 0.1607  0.0508  -0.0246 8   GLN A O   
2002 C CB  . GLN B 11  ? 0.4491 0.5024 0.5370 0.1978  0.0775  -0.0353 8   GLN A CB  
2003 C CG  . GLN B 11  ? 0.5066 0.5626 0.5854 0.2061  0.0938  -0.0384 8   GLN A CG  
2004 C CD  . GLN B 11  ? 0.5434 0.6337 0.6434 0.1953  0.1013  -0.0333 8   GLN A CD  
2005 O OE1 . GLN B 11  ? 0.6019 0.7281 0.7343 0.1969  0.1045  -0.0263 8   GLN A OE1 
2006 N NE2 . GLN B 11  ? 0.5489 0.6280 0.6316 0.1833  0.1027  -0.0364 8   GLN A NE2 
2007 N N   . LYS B 12  ? 0.3704 0.3936 0.4485 0.1670  0.0440  -0.0326 9   LYS A N   
2008 C CA  . LYS B 12  ? 0.3644 0.3879 0.4495 0.1591  0.0316  -0.0279 9   LYS A CA  
2009 C C   . LYS B 12  ? 0.3139 0.3491 0.4043 0.1396  0.0266  -0.0261 9   LYS A C   
2010 O O   . LYS B 12  ? 0.2665 0.3193 0.3725 0.1338  0.0202  -0.0209 9   LYS A O   
2011 C CB  . LYS B 12  ? 0.4228 0.4092 0.4853 0.1620  0.0244  -0.0300 9   LYS A CB  
2012 C CG  . LYS B 12  ? 0.4971 0.4823 0.5651 0.1571  0.0132  -0.0240 9   LYS A CG  
2013 C CD  . LYS B 12  ? 0.6043 0.5562 0.6547 0.1630  0.0065  -0.0234 9   LYS A CD  
2014 C CE  . LYS B 12  ? 0.6117 0.5681 0.6688 0.1556  -0.0035 -0.0160 9   LYS A CE  
2015 N NZ  . LYS B 12  ? 0.6329 0.5641 0.6787 0.1650  -0.0093 -0.0130 9   LYS A NZ  
2016 N N   . ALA B 13  ? 0.2966 0.3209 0.3725 0.1305  0.0291  -0.0307 10  ALA A N   
2017 C CA  . ALA B 13  ? 0.2783 0.3126 0.3579 0.1140  0.0253  -0.0295 10  ALA A CA  
2018 C C   . ALA B 13  ? 0.2501 0.3180 0.3533 0.1109  0.0286  -0.0253 10  ALA A C   
2019 O O   . ALA B 13  ? 0.2439 0.3228 0.3557 0.1005  0.0220  -0.0221 10  ALA A O   
2020 C CB  . ALA B 13  ? 0.2918 0.3084 0.3517 0.1072  0.0272  -0.0352 10  ALA A CB  
2021 N N   . LYS B 14  ? 0.2626 0.3454 0.3749 0.1191  0.0391  -0.0253 11  LYS A N   
2022 C CA  . LYS B 14  ? 0.2599 0.3753 0.3968 0.1156  0.0429  -0.0207 11  LYS A CA  
2023 C C   . LYS B 14  ? 0.2372 0.3726 0.3967 0.1177  0.0351  -0.0149 11  LYS A C   
2024 O O   . LYS B 14  ? 0.2157 0.3706 0.3909 0.1075  0.0301  -0.0113 11  LYS A O   
2025 C CB  . LYS B 14  ? 0.2898 0.4166 0.4317 0.1257  0.0573  -0.0210 11  LYS A CB  
2026 C CG  . LYS B 14  ? 0.3045 0.4150 0.4243 0.1233  0.0656  -0.0259 11  LYS A CG  
2027 C CD  . LYS B 14  ? 0.3526 0.4667 0.4697 0.1373  0.0807  -0.0270 11  LYS A CD  
2028 C CE  . LYS B 14  ? 0.3884 0.5191 0.5112 0.1306  0.0907  -0.0244 11  LYS A CE  
2029 N NZ  . LYS B 14  ? 0.4234 0.5571 0.5412 0.1444  0.1069  -0.0250 11  LYS A NZ  
2030 N N   . LEU B 15  ? 0.2456 0.3733 0.4043 0.1310  0.0332  -0.0144 12  LEU A N   
2031 C CA  . LEU B 15  ? 0.2501 0.3919 0.4261 0.1349  0.0241  -0.0091 12  LEU A CA  
2032 C C   . LEU B 15  ? 0.2379 0.3716 0.4072 0.1222  0.0115  -0.0076 12  LEU A C   
2033 O O   . LEU B 15  ? 0.2307 0.3842 0.4162 0.1164  0.0043  -0.0034 12  LEU A O   
2034 C CB  . LEU B 15  ? 0.2787 0.4069 0.4493 0.1529  0.0249  -0.0094 12  LEU A CB  
2035 C CG  . LEU B 15  ? 0.3180 0.4676 0.5115 0.1631  0.0192  -0.0034 12  LEU A CG  
2036 C CD1 . LEU B 15  ? 0.2971 0.4873 0.5229 0.1642  0.0244  0.0007  12  LEU A CD1 
2037 C CD2 . LEU B 15  ? 0.3484 0.4790 0.5316 0.1826  0.0220  -0.0048 12  LEU A CD2 
2038 N N   . ALA B 16  ? 0.2345 0.3392 0.3797 0.1177  0.0090  -0.0109 13  ALA A N   
2039 C CA  . ALA B 16  ? 0.2288 0.3243 0.3650 0.1058  -0.0004 -0.0095 13  ALA A CA  
2040 C C   . ALA B 16  ? 0.2122 0.3242 0.3559 0.0923  -0.0017 -0.0092 13  ALA A C   
2041 O O   . ALA B 16  ? 0.1935 0.3115 0.3404 0.0859  -0.0103 -0.0062 13  ALA A O   
2042 C CB  . ALA B 16  ? 0.2376 0.3029 0.3500 0.1026  -0.0005 -0.0131 13  ALA A CB  
2043 N N   . GLU B 17  ? 0.2037 0.3205 0.3476 0.0885  0.0065  -0.0123 14  GLU A N   
2044 C CA  . GLU B 17  ? 0.2013 0.3309 0.3509 0.0762  0.0057  -0.0120 14  GLU A CA  
2045 C C   . GLU B 17  ? 0.1878 0.3437 0.3606 0.0747  0.0008  -0.0073 14  GLU A C   
2046 O O   . GLU B 17  ? 0.1564 0.3158 0.3297 0.0654  -0.0073 -0.0061 14  GLU A O   
2047 C CB  . GLU B 17  ? 0.2083 0.3397 0.3554 0.0738  0.0158  -0.0148 14  GLU A CB  
2048 C CG  . GLU B 17  ? 0.1950 0.3326 0.3428 0.0604  0.0138  -0.0147 14  GLU A CG  
2049 C CD  . GLU B 17  ? 0.2041 0.3399 0.3457 0.0571  0.0229  -0.0169 14  GLU A CD  
2050 O OE1 . GLU B 17  ? 0.1950 0.3264 0.3317 0.0651  0.0318  -0.0187 14  GLU A OE1 
2051 O OE2 . GLU B 17  ? 0.2239 0.3600 0.3626 0.0466  0.0202  -0.0170 14  GLU A OE2 
2052 N N   . GLN B 18  ? 0.2059 0.3791 0.3968 0.0843  0.0052  -0.0049 15  GLN A N   
2053 C CA  . GLN B 18  ? 0.2403 0.4412 0.4570 0.0836  -0.0003 0.0000  15  GLN A CA  
2054 C C   . GLN B 18  ? 0.2176 0.4157 0.4329 0.0831  -0.0144 0.0025  15  GLN A C   
2055 O O   . GLN B 18  ? 0.2254 0.4370 0.4509 0.0747  -0.0232 0.0048  15  GLN A O   
2056 C CB  . GLN B 18  ? 0.2735 0.4949 0.5116 0.0968  0.0068  0.0029  15  GLN A CB  
2057 C CG  . GLN B 18  ? 0.3346 0.5645 0.5774 0.0982  0.0218  0.0019  15  GLN A CG  
2058 C CD  . GLN B 18  ? 0.3965 0.6397 0.6478 0.0828  0.0231  0.0033  15  GLN A CD  
2059 O OE1 . GLN B 18  ? 0.4894 0.7496 0.7573 0.0735  0.0139  0.0068  15  GLN A OE1 
2060 N NE2 . GLN B 18  ? 0.4508 0.6835 0.6883 0.0799  0.0337  0.0004  15  GLN A NE2 
2061 N N   . ALA B 19  ? 0.2220 0.4007 0.4229 0.0919  -0.0166 0.0022  16  ALA A N   
2062 C CA  . ALA B 19  ? 0.2013 0.3719 0.3951 0.0926  -0.0287 0.0050  16  ALA A CA  
2063 C C   . ALA B 19  ? 0.1840 0.3388 0.3584 0.0807  -0.0342 0.0037  16  ALA A C   
2064 O O   . ALA B 19  ? 0.2011 0.3493 0.3681 0.0816  -0.0435 0.0066  16  ALA A O   
2065 C CB  . ALA B 19  ? 0.2194 0.3715 0.4024 0.1055  -0.0280 0.0057  16  ALA A CB  
2066 N N   . GLU B 20  ? 0.1715 0.3179 0.3354 0.0719  -0.0281 -0.0003 17  GLU A N   
2067 C CA  A GLU B 20  ? 0.1670 0.2990 0.3128 0.0621  -0.0311 -0.0019 17  GLU A CA  
2068 C CA  B GLU B 20  ? 0.1707 0.3029 0.3166 0.0622  -0.0313 -0.0018 17  GLU A CA  
2069 C C   . GLU B 20  ? 0.1748 0.2849 0.3029 0.0657  -0.0326 -0.0007 17  GLU A C   
2070 O O   . GLU B 20  ? 0.1715 0.2739 0.2881 0.0615  -0.0383 0.0011  17  GLU A O   
2071 C CB  A GLU B 20  ? 0.1706 0.3141 0.3211 0.0544  -0.0400 -0.0005 17  GLU A CB  
2072 C CB  B GLU B 20  ? 0.1808 0.3236 0.3305 0.0545  -0.0406 -0.0003 17  GLU A CB  
2073 C CG  A GLU B 20  ? 0.1638 0.3271 0.3322 0.0486  -0.0383 -0.0012 17  GLU A CG  
2074 C CG  B GLU B 20  ? 0.1774 0.3360 0.3402 0.0466  -0.0388 -0.0019 17  GLU A CG  
2075 C CD  A GLU B 20  ? 0.1678 0.3380 0.3380 0.0392  -0.0483 -0.0008 17  GLU A CD  
2076 C CD  B GLU B 20  ? 0.1879 0.3561 0.3556 0.0396  -0.0501 -0.0005 17  GLU A CD  
2077 O OE1 A GLU B 20  ? 0.1525 0.3077 0.3035 0.0342  -0.0519 -0.0025 17  GLU A OE1 
2078 O OE1 B GLU B 20  ? 0.1940 0.3603 0.3578 0.0428  -0.0598 0.0020  17  GLU A OE1 
2079 O OE2 A GLU B 20  ? 0.1567 0.3470 0.3474 0.0375  -0.0530 0.0015  17  GLU A OE2 
2080 O OE2 B GLU B 20  ? 0.1570 0.3329 0.3311 0.0311  -0.0495 -0.0018 17  GLU A OE2 
2081 N N   . ARG B 21  ? 0.1929 0.2923 0.3183 0.0741  -0.0274 -0.0014 18  ARG A N   
2082 C CA  . ARG B 21  ? 0.2111 0.2874 0.3203 0.0769  -0.0282 -0.0002 18  ARG A CA  
2083 C C   . ARG B 21  ? 0.2135 0.2758 0.3114 0.0712  -0.0217 -0.0047 18  ARG A C   
2084 O O   . ARG B 21  ? 0.2148 0.2661 0.3088 0.0766  -0.0168 -0.0075 18  ARG A O   
2085 C CB  . ARG B 21  ? 0.2427 0.3153 0.3563 0.0904  -0.0290 0.0021  18  ARG A CB  
2086 C CG  . ARG B 21  ? 0.2434 0.3256 0.3634 0.0943  -0.0386 0.0076  18  ARG A CG  
2087 C CD  . ARG B 21  ? 0.2483 0.3260 0.3715 0.1082  -0.0405 0.0105  18  ARG A CD  
2088 N NE  . ARG B 21  ? 0.2724 0.3205 0.3761 0.1108  -0.0398 0.0115  18  ARG A NE  
2089 C CZ  . ARG B 21  ? 0.2880 0.3203 0.3800 0.1139  -0.0462 0.0168  18  ARG A CZ  
2090 N NH1 . ARG B 21  ? 0.2791 0.3209 0.3730 0.1138  -0.0548 0.0217  18  ARG A NH1 
2091 N NH2 . ARG B 21  ? 0.3028 0.3074 0.3790 0.1165  -0.0444 0.0174  18  ARG A NH2 
2092 N N   . TYR B 22  ? 0.1964 0.2583 0.2879 0.0608  -0.0222 -0.0056 19  TYR A N   
2093 C CA  . TYR B 22  ? 0.2016 0.2557 0.2854 0.0546  -0.0173 -0.0099 19  TYR A CA  
2094 C C   . TYR B 22  ? 0.2159 0.2484 0.2871 0.0541  -0.0173 -0.0097 19  TYR A C   
2095 O O   . TYR B 22  ? 0.2171 0.2411 0.2831 0.0525  -0.0138 -0.0139 19  TYR A O   
2096 C CB  . TYR B 22  ? 0.1847 0.2461 0.2666 0.0452  -0.0181 -0.0106 19  TYR A CB  
2097 C CG  . TYR B 22  ? 0.1787 0.2585 0.2726 0.0444  -0.0184 -0.0113 19  TYR A CG  
2098 C CD1 . TYR B 22  ? 0.1990 0.2860 0.3003 0.0458  -0.0126 -0.0142 19  TYR A CD1 
2099 C CD2 . TYR B 22  ? 0.1858 0.2748 0.2827 0.0417  -0.0246 -0.0089 19  TYR A CD2 
2100 C CE1 . TYR B 22  ? 0.1965 0.3006 0.3105 0.0437  -0.0124 -0.0138 19  TYR A CE1 
2101 C CE2 . TYR B 22  ? 0.2038 0.3084 0.3123 0.0392  -0.0261 -0.0094 19  TYR A CE2 
2102 C CZ  . TYR B 22  ? 0.2209 0.3337 0.3391 0.0395  -0.0198 -0.0115 19  TYR A CZ  
2103 O OH  . TYR B 22  ? 0.2526 0.3808 0.3835 0.0357  -0.0205 -0.0110 19  TYR A OH  
2104 N N   . ASP B 23  ? 0.2256 0.2481 0.2910 0.0547  -0.0215 -0.0047 20  ASP A N   
2105 C CA  . ASP B 23  ? 0.2566 0.2572 0.3111 0.0534  -0.0218 -0.0039 20  ASP A CA  
2106 C C   . ASP B 23  ? 0.2567 0.2447 0.3091 0.0625  -0.0199 -0.0073 20  ASP A C   
2107 O O   . ASP B 23  ? 0.2605 0.2332 0.3046 0.0601  -0.0184 -0.0111 20  ASP A O   
2108 C CB  . ASP B 23  ? 0.2842 0.2756 0.3323 0.0525  -0.0260 0.0033  20  ASP A CB  
2109 C CG  . ASP B 23  ? 0.2912 0.2906 0.3370 0.0440  -0.0266 0.0068  20  ASP A CG  
2110 O OD1 . ASP B 23  ? 0.2778 0.2845 0.3250 0.0374  -0.0240 0.0038  20  ASP A OD1 
2111 O OD2 . ASP B 23  ? 0.3432 0.3399 0.3838 0.0448  -0.0294 0.0128  20  ASP A OD2 
2112 N N   . ASP B 24  ? 0.2508 0.2462 0.3107 0.0733  -0.0200 -0.0062 21  ASP A N   
2113 C CA  . ASP B 24  ? 0.2560 0.2425 0.3148 0.0847  -0.0168 -0.0096 21  ASP A CA  
2114 C C   . ASP B 24  ? 0.2525 0.2426 0.3111 0.0840  -0.0102 -0.0163 21  ASP A C   
2115 O O   . ASP B 24  ? 0.2764 0.2475 0.3235 0.0879  -0.0079 -0.0207 21  ASP A O   
2116 C CB  . ASP B 24  ? 0.2652 0.2649 0.3361 0.0970  -0.0176 -0.0067 21  ASP A CB  
2117 C CG  . ASP B 24  ? 0.2866 0.2775 0.3542 0.1017  -0.0245 -0.0002 21  ASP A CG  
2118 O OD1 . ASP B 24  ? 0.2989 0.2697 0.3529 0.0957  -0.0277 0.0025  21  ASP A OD1 
2119 O OD2 . ASP B 24  ? 0.2996 0.3046 0.3788 0.1111  -0.0268 0.0026  21  ASP A OD2 
2120 N N   . MET B 25  ? 0.2360 0.2483 0.3051 0.0790  -0.0077 -0.0170 22  MET A N   
2121 C CA  . MET B 25  ? 0.2528 0.2696 0.3211 0.0781  -0.0012 -0.0223 22  MET A CA  
2122 C C   . MET B 25  ? 0.2406 0.2384 0.2934 0.0705  -0.0020 -0.0263 22  MET A C   
2123 O O   . MET B 25  ? 0.2736 0.2604 0.3171 0.0745  0.0020  -0.0313 22  MET A O   
2124 C CB  . MET B 25  ? 0.2285 0.2695 0.3096 0.0718  0.0001  -0.0211 22  MET A CB  
2125 C CG  . MET B 25  ? 0.2213 0.2706 0.3044 0.0722  0.0077  -0.0247 22  MET A CG  
2126 S SD  . MET B 25  ? 0.2018 0.2745 0.2977 0.0621  0.0067  -0.0224 22  MET A SD  
2127 C CE  . MET B 25  ? 0.2234 0.2985 0.3169 0.0647  0.0174  -0.0261 22  MET A CE  
2128 N N   . ALA B 26  ? 0.2431 0.2376 0.2930 0.0604  -0.0071 -0.0238 23  ALA A N   
2129 C CA  . ALA B 26  ? 0.2399 0.2210 0.2793 0.0518  -0.0091 -0.0265 23  ALA A CA  
2130 C C   . ALA B 26  ? 0.2723 0.2270 0.2990 0.0544  -0.0118 -0.0283 23  ALA A C   
2131 O O   . ALA B 26  ? 0.2881 0.2297 0.3044 0.0524  -0.0121 -0.0334 23  ALA A O   
2132 C CB  . ALA B 26  ? 0.2182 0.2062 0.2609 0.0417  -0.0128 -0.0221 23  ALA A CB  
2133 N N   . ALA B 27  ? 0.2998 0.2447 0.3257 0.0595  -0.0143 -0.0243 24  ALA A N   
2134 C CA  . ALA B 27  ? 0.3284 0.2445 0.3407 0.0631  -0.0172 -0.0258 24  ALA A CA  
2135 C C   . ALA B 27  ? 0.3354 0.2413 0.3388 0.0739  -0.0128 -0.0330 24  ALA A C   
2136 O O   . ALA B 27  ? 0.3554 0.2378 0.3434 0.0721  -0.0153 -0.0380 24  ALA A O   
2137 C CB  . ALA B 27  ? 0.3355 0.2429 0.3478 0.0680  -0.0204 -0.0196 24  ALA A CB  
2138 N N   . CYS B 28  ? 0.3272 0.2514 0.3400 0.0844  -0.0063 -0.0335 25  CYS A N   
2139 C CA  . CYS B 28  ? 0.3452 0.2632 0.3503 0.0960  0.0003  -0.0395 25  CYS A CA  
2140 C C   . CYS B 28  ? 0.3301 0.2424 0.3238 0.0897  0.0019  -0.0457 25  CYS A C   
2141 O O   . CYS B 28  ? 0.3622 0.2500 0.3369 0.0946  0.0019  -0.0518 25  CYS A O   
2142 C CB  . CYS B 28  ? 0.3521 0.2972 0.3742 0.1061  0.0078  -0.0375 25  CYS A CB  
2143 S SG  . CYS B 28  ? 0.3617 0.3104 0.3944 0.1189  0.0059  -0.0317 25  CYS A SG  
2144 N N   . MET B 29  ? 0.2902 0.2228 0.2935 0.0796  0.0022  -0.0441 26  MET A N   
2145 C CA  . MET B 29  ? 0.2908 0.2218 0.2850 0.0747  0.0038  -0.0490 26  MET A CA  
2146 C C   . MET B 29  ? 0.3123 0.2217 0.2930 0.0651  -0.0048 -0.0518 26  MET A C   
2147 O O   . MET B 29  ? 0.3073 0.2029 0.2726 0.0658  -0.0050 -0.0577 26  MET A O   
2148 C CB  . MET B 29  ? 0.2562 0.2142 0.2644 0.0686  0.0070  -0.0462 26  MET A CB  
2149 C CG  . MET B 29  ? 0.2543 0.2329 0.2751 0.0771  0.0157  -0.0442 26  MET A CG  
2150 S SD  . MET B 29  ? 0.2945 0.2636 0.3041 0.0928  0.0257  -0.0489 26  MET A SD  
2151 C CE  . MET B 29  ? 0.3189 0.2729 0.3064 0.0883  0.0269  -0.0552 26  MET A CE  
2152 N N   . LYS B 30  ? 0.3246 0.2310 0.3108 0.0567  -0.0117 -0.0473 27  LYS A N   
2153 C CA  . LYS B 30  ? 0.3575 0.2420 0.3331 0.0477  -0.0202 -0.0489 27  LYS A CA  
2154 C C   . LYS B 30  ? 0.3736 0.2260 0.3290 0.0550  -0.0225 -0.0548 27  LYS A C   
2155 O O   . LYS B 30  ? 0.3717 0.2064 0.3121 0.0515  -0.0272 -0.0607 27  LYS A O   
2156 C CB  . LYS B 30  ? 0.3628 0.2518 0.3494 0.0385  -0.0249 -0.0413 27  LYS A CB  
2157 C CG  . LYS B 30  ? 0.3748 0.2448 0.3556 0.0264  -0.0339 -0.0408 27  LYS A CG  
2158 C CD  . LYS B 30  ? 0.3718 0.2510 0.3650 0.0176  -0.0357 -0.0317 27  LYS A CD  
2159 C CE  . LYS B 30  ? 0.3988 0.2724 0.3947 0.0031  -0.0425 -0.0286 27  LYS A CE  
2160 N NZ  . LYS B 30  ? 0.4624 0.3046 0.4459 0.0009  -0.0487 -0.0294 27  LYS A NZ  
2161 N N   . SER B 31  ? 0.3864 0.2305 0.3399 0.0667  -0.0193 -0.0537 28  SER A N   
2162 C CA  . SER B 31  ? 0.4198 0.2319 0.3525 0.0764  -0.0205 -0.0595 28  SER A CA  
2163 C C   . SER B 31  ? 0.4372 0.2427 0.3541 0.0850  -0.0151 -0.0678 28  SER A C   
2164 O O   . SER B 31  ? 0.4416 0.2179 0.3365 0.0845  -0.0206 -0.0745 28  SER A O   
2165 C CB  . SER B 31  ? 0.4460 0.2534 0.3813 0.0892  -0.0174 -0.0562 28  SER A CB  
2166 O OG  . SER B 31  ? 0.4872 0.2897 0.4289 0.0800  -0.0244 -0.0492 28  SER A OG  
2167 N N   . VAL B 32  ? 0.4127 0.2449 0.3401 0.0914  -0.0051 -0.0670 29  VAL A N   
2168 C CA  . VAL B 32  ? 0.4297 0.2596 0.3431 0.0988  0.0019  -0.0732 29  VAL A CA  
2169 C C   . VAL B 32  ? 0.4356 0.2535 0.3351 0.0872  -0.0059 -0.0778 29  VAL A C   
2170 O O   . VAL B 32  ? 0.4986 0.2889 0.3725 0.0916  -0.0083 -0.0854 29  VAL A O   
2171 C CB  . VAL B 32  ? 0.4081 0.2721 0.3391 0.1036  0.0135  -0.0696 29  VAL A CB  
2172 C CG1 . VAL B 32  ? 0.4341 0.2969 0.3502 0.1086  0.0212  -0.0746 29  VAL A CG1 
2173 C CG2 . VAL B 32  ? 0.4110 0.2880 0.3562 0.1169  0.0208  -0.0655 29  VAL A CG2 
2174 N N   . THR B 33  ? 0.3941 0.2309 0.3092 0.0732  -0.0107 -0.0734 30  THR A N   
2175 C CA  . THR B 33  ? 0.3941 0.2250 0.3006 0.0622  -0.0186 -0.0767 30  THR A CA  
2176 C C   . THR B 33  ? 0.4517 0.2485 0.3395 0.0577  -0.0303 -0.0817 30  THR A C   
2177 O O   . THR B 33  ? 0.4682 0.2462 0.3347 0.0581  -0.0347 -0.0888 30  THR A O   
2178 C CB  . THR B 33  ? 0.3413 0.1981 0.2700 0.0494  -0.0217 -0.0702 30  THR A CB  
2179 O OG1 . THR B 33  ? 0.3155 0.1999 0.2587 0.0534  -0.0119 -0.0663 30  THR A OG1 
2180 C CG2 . THR B 33  ? 0.3361 0.1895 0.2590 0.0389  -0.0306 -0.0728 30  THR A CG2 
2181 N N   . GLU B 34  ? 0.4646 0.2521 0.3588 0.0538  -0.0354 -0.0780 31  GLU A N   
2182 C CA  . GLU B 34  ? 0.5097 0.2640 0.3887 0.0475  -0.0473 -0.0814 31  GLU A CA  
2183 C C   . GLU B 34  ? 0.5556 0.2739 0.4039 0.0599  -0.0476 -0.0906 31  GLU A C   
2184 O O   . GLU B 34  ? 0.6081 0.2962 0.4391 0.0536  -0.0592 -0.0955 31  GLU A O   
2185 C CB  . GLU B 34  ? 0.4997 0.2524 0.3922 0.0416  -0.0505 -0.0739 31  GLU A CB  
2186 C CG  . GLU B 34  ? 0.4774 0.2571 0.3942 0.0266  -0.0533 -0.0658 31  GLU A CG  
2187 C CD  . GLU B 34  ? 0.4636 0.2481 0.3947 0.0224  -0.0532 -0.0567 31  GLU A CD  
2188 O OE1 . GLU B 34  ? 0.5013 0.2750 0.4281 0.0324  -0.0496 -0.0554 31  GLU A OE1 
2189 O OE2 . GLU B 34  ? 0.4874 0.2893 0.4347 0.0097  -0.0559 -0.0505 31  GLU A OE2 
2190 N N   . GLN B 35  ? 0.5674 0.2877 0.4078 0.0773  -0.0355 -0.0933 32  GLN A N   
2191 C CA  . GLN B 35  ? 0.5931 0.2804 0.4016 0.0908  -0.0342 -0.1028 32  GLN A CA  
2192 C C   . GLN B 35  ? 0.5894 0.2661 0.3768 0.0881  -0.0384 -0.1102 32  GLN A C   
2193 O O   . GLN B 35  ? 0.5960 0.2390 0.3518 0.0968  -0.0406 -0.1190 32  GLN A O   
2194 C CB  . GLN B 35  ? 0.6327 0.3291 0.4399 0.1110  -0.0184 -0.1031 32  GLN A CB  
2195 C CG  . GLN B 35  ? 0.6690 0.3721 0.4929 0.1175  -0.0147 -0.0968 32  GLN A CG  
2196 C CD  . GLN B 35  ? 0.7390 0.4510 0.5625 0.1387  0.0002  -0.0974 32  GLN A CD  
2197 O OE1 . GLN B 35  ? 0.7981 0.5142 0.6103 0.1481  0.0098  -0.1016 32  GLN A OE1 
2198 N NE2 . GLN B 35  ? 0.7280 0.4447 0.5649 0.1462  0.0023  -0.0922 32  GLN A NE2 
2199 N N   . GLY B 36  ? 0.5691 0.2733 0.3717 0.0777  -0.0390 -0.1068 33  GLY A N   
2200 C CA  . GLY B 36  ? 0.5986 0.2930 0.3840 0.0715  -0.0470 -0.1124 33  GLY A CA  
2201 C C   . GLY B 36  ? 0.6217 0.3207 0.3908 0.0837  -0.0357 -0.1161 33  GLY A C   
2202 O O   . GLY B 36  ? 0.6701 0.3623 0.4245 0.0790  -0.0424 -0.1201 33  GLY A O   
2203 N N   . ALA B 37  ? 0.5845 0.2955 0.3567 0.0986  -0.0192 -0.1142 34  ALA A N   
2204 C CA  . ALA B 37  ? 0.5790 0.2986 0.3393 0.1091  -0.0062 -0.1156 34  ALA A CA  
2205 C C   . ALA B 37  ? 0.5185 0.2759 0.3050 0.1001  -0.0019 -0.1079 34  ALA A C   
2206 O O   . ALA B 37  ? 0.4867 0.2678 0.3029 0.0916  -0.0034 -0.1009 34  ALA A O   
2207 C CB  . ALA B 37  ? 0.5885 0.3067 0.3433 0.1285  0.0098  -0.1162 34  ALA A CB  
2208 N N   . GLU B 38  ? 0.5230 0.2835 0.2958 0.1020  0.0029  -0.1092 35  GLU A N   
2209 C CA  . GLU B 38  ? 0.5073 0.3002 0.3009 0.0957  0.0087  -0.1021 35  GLU A CA  
2210 C C   . GLU B 38  ? 0.4661 0.2869 0.2848 0.1016  0.0234  -0.0951 35  GLU A C   
2211 O O   . GLU B 38  ? 0.4664 0.2819 0.2779 0.1155  0.0344  -0.0966 35  GLU A O   
2212 C CB  . GLU B 38  ? 0.5529 0.3413 0.3239 0.0998  0.0143  -0.1040 35  GLU A CB  
2213 C CG  . GLU B 38  ? 0.5634 0.3390 0.3206 0.0898  -0.0013 -0.1075 35  GLU A CG  
2214 C CD  . GLU B 38  ? 0.5915 0.3608 0.3236 0.0952  0.0047  -0.1088 35  GLU A CD  
2215 O OE1 . GLU B 38  ? 0.6375 0.3762 0.3342 0.1038  0.0030  -0.1166 35  GLU A OE1 
2216 O OE2 . GLU B 38  ? 0.5717 0.3635 0.3180 0.0904  0.0093  -0.1025 35  GLU A OE2 
2217 N N   . LEU B 39  ? 0.4228 0.2721 0.2699 0.0916  0.0228  -0.0879 36  LEU A N   
2218 C CA  . LEU B 39  ? 0.4065 0.2842 0.2792 0.0944  0.0341  -0.0810 36  LEU A CA  
2219 C C   . LEU B 39  ? 0.4246 0.3140 0.2927 0.0991  0.0475  -0.0786 36  LEU A C   
2220 O O   . LEU B 39  ? 0.4186 0.3031 0.2727 0.0947  0.0457  -0.0795 36  LEU A O   
2221 C CB  . LEU B 39  ? 0.3646 0.2638 0.2651 0.0820  0.0273  -0.0750 36  LEU A CB  
2222 C CG  . LEU B 39  ? 0.3619 0.2512 0.2678 0.0757  0.0149  -0.0757 36  LEU A CG  
2223 C CD1 . LEU B 39  ? 0.3259 0.2392 0.2585 0.0655  0.0113  -0.0689 36  LEU A CD1 
2224 C CD2 . LEU B 39  ? 0.3791 0.2549 0.2823 0.0847  0.0160  -0.0774 36  LEU A CD2 
2225 N N   . SER B 40  ? 0.4197 0.3275 0.3026 0.1073  0.0608  -0.0743 37  SER A N   
2226 C CA  . SER B 40  ? 0.3966 0.3258 0.2880 0.1077  0.0737  -0.0686 37  SER A CA  
2227 C C   . SER B 40  ? 0.3707 0.3230 0.2865 0.0939  0.0693  -0.0623 37  SER A C   
2228 O O   . SER B 40  ? 0.3338 0.2900 0.2637 0.0860  0.0581  -0.0616 37  SER A O   
2229 C CB  . SER B 40  ? 0.4134 0.3578 0.3171 0.1199  0.0884  -0.0655 37  SER A CB  
2230 O OG  . SER B 40  ? 0.3532 0.3196 0.2885 0.1167  0.0853  -0.0606 37  SER A OG  
2231 N N   . ASN B 41  ? 0.3599 0.3276 0.2807 0.0914  0.0789  -0.0571 38  ASN A N   
2232 C CA  . ASN B 41  ? 0.3505 0.3392 0.2938 0.0793  0.0759  -0.0509 38  ASN A CA  
2233 C C   . ASN B 41  ? 0.3094 0.3191 0.2828 0.0775  0.0736  -0.0470 38  ASN A C   
2234 O O   . ASN B 41  ? 0.2901 0.3056 0.2755 0.0682  0.0636  -0.0456 38  ASN A O   
2235 C CB  . ASN B 41  ? 0.3810 0.3807 0.3243 0.0771  0.0874  -0.0454 38  ASN A CB  
2236 C CG  . ASN B 41  ? 0.4635 0.4430 0.3777 0.0757  0.0863  -0.0479 38  ASN A CG  
2237 O OD1 . ASN B 41  ? 0.4885 0.4467 0.3829 0.0764  0.0761  -0.0541 38  ASN A OD1 
2238 N ND2 . ASN B 41  ? 0.4975 0.4835 0.4090 0.0731  0.0960  -0.0424 38  ASN A ND2 
2239 N N   . GLU B 42  ? 0.3152 0.3356 0.2993 0.0873  0.0829  -0.0454 39  GLU A N   
2240 C CA  A GLU B 42  ? 0.2964 0.3361 0.3079 0.0872  0.0801  -0.0417 39  GLU A CA  
2241 C CA  B GLU B 42  ? 0.2908 0.3301 0.3020 0.0878  0.0804  -0.0418 39  GLU A CA  
2242 C C   . GLU B 42  ? 0.2858 0.3120 0.2951 0.0856  0.0668  -0.0452 39  GLU A C   
2243 O O   . GLU B 42  ? 0.2492 0.2878 0.2764 0.0784  0.0593  -0.0419 39  GLU A O   
2244 C CB  A GLU B 42  ? 0.3221 0.3756 0.3451 0.0999  0.0921  -0.0393 39  GLU A CB  
2245 C CB  B GLU B 42  ? 0.3129 0.3598 0.3286 0.1022  0.0928  -0.0410 39  GLU A CB  
2246 C CG  A GLU B 42  ? 0.3293 0.4099 0.3851 0.0974  0.0893  -0.0335 39  GLU A CG  
2247 C CG  B GLU B 42  ? 0.3153 0.3800 0.3566 0.1073  0.0911  -0.0377 39  GLU A CG  
2248 C CD  A GLU B 42  ? 0.3525 0.4514 0.4259 0.1103  0.0991  -0.0303 39  GLU A CD  
2249 C CD  B GLU B 42  ? 0.3290 0.4077 0.3784 0.1215  0.1060  -0.0354 39  GLU A CD  
2250 O OE1 A GLU B 42  ? 0.3970 0.4799 0.4567 0.1237  0.1017  -0.0348 39  GLU A OE1 
2251 O OE1 B GLU B 42  ? 0.3225 0.4224 0.3845 0.1183  0.1164  -0.0298 39  GLU A OE1 
2252 O OE2 A GLU B 42  ? 0.3587 0.4868 0.4604 0.1063  0.1016  -0.0236 39  GLU A OE2 
2253 O OE2 B GLU B 42  ? 0.3537 0.4204 0.3951 0.1356  0.1078  -0.0391 39  GLU A OE2 
2254 N N   . GLU B 43  ? 0.2992 0.2997 0.2861 0.0919  0.0639  -0.0515 40  GLU A N   
2255 C CA  . GLU B 43  ? 0.3153 0.3007 0.2988 0.0896  0.0519  -0.0543 40  GLU A CA  
2256 C C   . GLU B 43  ? 0.2810 0.2657 0.2657 0.0758  0.0411  -0.0538 40  GLU A C   
2257 O O   . GLU B 43  ? 0.2524 0.2406 0.2484 0.0709  0.0333  -0.0517 40  GLU A O   
2258 C CB  . GLU B 43  ? 0.3426 0.2986 0.3002 0.0984  0.0511  -0.0613 40  GLU A CB  
2259 C CG  . GLU B 43  ? 0.3703 0.3245 0.3267 0.1144  0.0607  -0.0622 40  GLU A CG  
2260 C CD  . GLU B 43  ? 0.4490 0.3743 0.3741 0.1255  0.0646  -0.0697 40  GLU A CD  
2261 O OE1 . GLU B 43  ? 0.4542 0.3572 0.3567 0.1197  0.0569  -0.0749 40  GLU A OE1 
2262 O OE2 . GLU B 43  ? 0.4800 0.4041 0.4026 0.1408  0.0745  -0.0705 40  GLU A OE2 
2263 N N   . ARG B 44  ? 0.2790 0.2591 0.2514 0.0706  0.0409  -0.0552 41  ARG A N   
2264 C CA  . ARG B 44  ? 0.2806 0.2642 0.2566 0.0591  0.0323  -0.0540 41  ARG A CA  
2265 C C   . ARG B 44  ? 0.2619 0.2682 0.2613 0.0534  0.0319  -0.0481 41  ARG A C   
2266 O O   . ARG B 44  ? 0.2311 0.2394 0.2375 0.0472  0.0236  -0.0470 41  ARG A O   
2267 C CB  . ARG B 44  ? 0.3251 0.3046 0.2877 0.0550  0.0328  -0.0549 41  ARG A CB  
2268 C CG  . ARG B 44  ? 0.3383 0.2942 0.2781 0.0558  0.0258  -0.0609 41  ARG A CG  
2269 C CD  . ARG B 44  ? 0.3526 0.3018 0.2757 0.0536  0.0256  -0.0620 41  ARG A CD  
2270 N NE  . ARG B 44  ? 0.3733 0.3170 0.2810 0.0616  0.0372  -0.0626 41  ARG A NE  
2271 C CZ  . ARG B 44  ? 0.4128 0.3375 0.2987 0.0702  0.0400  -0.0677 41  ARG A CZ  
2272 N NH1 . ARG B 44  ? 0.4162 0.3216 0.2907 0.0712  0.0301  -0.0735 41  ARG A NH1 
2273 N NH2 . ARG B 44  ? 0.4566 0.3798 0.3300 0.0777  0.0527  -0.0668 41  ARG A NH2 
2274 N N   . ASN B 45  ? 0.2472 0.2699 0.2578 0.0553  0.0407  -0.0443 42  ASN A N   
2275 C CA  . ASN B 45  ? 0.2206 0.2635 0.2523 0.0495  0.0392  -0.0392 42  ASN A CA  
2276 C C   . ASN B 45  ? 0.2040 0.2512 0.2481 0.0513  0.0334  -0.0379 42  ASN A C   
2277 O O   . ASN B 45  ? 0.2085 0.2629 0.2614 0.0448  0.0269  -0.0356 42  ASN A O   
2278 C CB  . ASN B 45  ? 0.2313 0.2916 0.2748 0.0499  0.0487  -0.0349 42  ASN A CB  
2279 C CG  . ASN B 45  ? 0.2760 0.3331 0.3091 0.0442  0.0522  -0.0342 42  ASN A CG  
2280 O OD1 . ASN B 45  ? 0.3214 0.3678 0.3431 0.0387  0.0456  -0.0361 42  ASN A OD1 
2281 N ND2 . ASN B 45  ? 0.2883 0.3558 0.3263 0.0458  0.0629  -0.0306 42  ASN A ND2 
2282 N N   . LEU B 46  ? 0.2082 0.2496 0.2510 0.0609  0.0360  -0.0393 43  LEU A N   
2283 C CA  . LEU B 46  ? 0.1996 0.2419 0.2515 0.0639  0.0307  -0.0377 43  LEU A CA  
2284 C C   . LEU B 46  ? 0.2027 0.2310 0.2464 0.0575  0.0209  -0.0389 43  LEU A C   
2285 O O   . LEU B 46  ? 0.1910 0.2261 0.2443 0.0535  0.0152  -0.0355 43  LEU A O   
2286 C CB  . LEU B 46  ? 0.2146 0.2494 0.2628 0.0768  0.0361  -0.0395 43  LEU A CB  
2287 C CG  . LEU B 46  ? 0.2173 0.2712 0.2790 0.0849  0.0467  -0.0368 43  LEU A CG  
2288 C CD1 . LEU B 46  ? 0.2504 0.2921 0.3027 0.0996  0.0527  -0.0398 43  LEU A CD1 
2289 C CD2 . LEU B 46  ? 0.2054 0.2852 0.2934 0.0829  0.0444  -0.0306 43  LEU A CD2 
2290 N N   . LEU B 47  ? 0.2133 0.2224 0.2393 0.0563  0.0190  -0.0435 44  LEU A N   
2291 C CA  . LEU B 47  ? 0.2201 0.2190 0.2410 0.0488  0.0102  -0.0441 44  LEU A CA  
2292 C C   . LEU B 47  ? 0.1963 0.2091 0.2260 0.0399  0.0069  -0.0409 44  LEU A C   
2293 O O   . LEU B 47  ? 0.1792 0.1942 0.2145 0.0356  0.0017  -0.0380 44  LEU A O   
2294 C CB  . LEU B 47  ? 0.2452 0.2244 0.2473 0.0480  0.0079  -0.0495 44  LEU A CB  
2295 C CG  . LEU B 47  ? 0.2533 0.2231 0.2523 0.0396  -0.0016 -0.0499 44  LEU A CG  
2296 C CD1 . LEU B 47  ? 0.2851 0.2432 0.2846 0.0408  -0.0056 -0.0487 44  LEU A CD1 
2297 C CD2 . LEU B 47  ? 0.3144 0.2700 0.2974 0.0372  -0.0054 -0.0549 44  LEU A CD2 
2298 N N   . SER B 48  ? 0.2121 0.2325 0.2410 0.0377  0.0103  -0.0412 45  SER A N   
2299 C CA  . SER B 48  ? 0.2088 0.2383 0.2420 0.0305  0.0074  -0.0393 45  SER A CA  
2300 C C   . SER B 48  ? 0.2010 0.2449 0.2485 0.0292  0.0062  -0.0350 45  SER A C   
2301 O O   . SER B 48  ? 0.2090 0.2554 0.2585 0.0249  0.0014  -0.0332 45  SER A O   
2302 C CB  . SER B 48  ? 0.2345 0.2653 0.2614 0.0295  0.0116  -0.0405 45  SER A CB  
2303 O OG  . SER B 48  ? 0.2384 0.2754 0.2674 0.0237  0.0089  -0.0389 45  SER A OG  
2304 N N   . VAL B 49  ? 0.1893 0.2428 0.2462 0.0333  0.0104  -0.0332 46  VAL A N   
2305 C CA  . VAL B 49  ? 0.1655 0.2325 0.2359 0.0323  0.0077  -0.0293 46  VAL A CA  
2306 C C   . VAL B 49  ? 0.1571 0.2190 0.2277 0.0336  0.0021  -0.0276 46  VAL A C   
2307 O O   . VAL B 49  ? 0.1419 0.2092 0.2159 0.0302  -0.0026 -0.0250 46  VAL A O   
2308 C CB  . VAL B 49  ? 0.1668 0.2471 0.2500 0.0368  0.0129  -0.0274 46  VAL A CB  
2309 C CG1 . VAL B 49  ? 0.1726 0.2656 0.2701 0.0376  0.0081  -0.0235 46  VAL A CG1 
2310 C CG2 . VAL B 49  ? 0.1814 0.2688 0.2660 0.0323  0.0179  -0.0271 46  VAL A CG2 
2311 N N   . ALA B 50  ? 0.1791 0.2299 0.2451 0.0391  0.0029  -0.0288 47  ALA A N   
2312 C CA  . ALA B 50  ? 0.1720 0.2157 0.2375 0.0407  -0.0017 -0.0263 47  ALA A CA  
2313 C C   . ALA B 50  ? 0.1690 0.2088 0.2295 0.0330  -0.0061 -0.0250 47  ALA A C   
2314 O O   . ALA B 50  ? 0.1754 0.2204 0.2389 0.0311  -0.0094 -0.0212 47  ALA A O   
2315 C CB  . ALA B 50  ? 0.1843 0.2124 0.2427 0.0472  -0.0003 -0.0284 47  ALA A CB  
2316 N N   . TYR B 51  ? 0.1814 0.2132 0.2340 0.0289  -0.0062 -0.0279 48  TYR A N   
2317 C CA  . TYR B 51  ? 0.1712 0.2021 0.2216 0.0223  -0.0096 -0.0262 48  TYR A CA  
2318 C C   . TYR B 51  ? 0.1729 0.2165 0.2263 0.0191  -0.0097 -0.0249 48  TYR A C   
2319 O O   . TYR B 51  ? 0.1811 0.2270 0.2346 0.0161  -0.0116 -0.0217 48  TYR A O   
2320 C CB  . TYR B 51  ? 0.1867 0.2063 0.2298 0.0193  -0.0110 -0.0296 48  TYR A CB  
2321 C CG  . TYR B 51  ? 0.2063 0.2100 0.2451 0.0200  -0.0135 -0.0295 48  TYR A CG  
2322 C CD1 . TYR B 51  ? 0.2100 0.2108 0.2512 0.0156  -0.0166 -0.0246 48  TYR A CD1 
2323 C CD2 . TYR B 51  ? 0.2243 0.2138 0.2549 0.0249  -0.0127 -0.0339 48  TYR A CD2 
2324 C CE1 . TYR B 51  ? 0.2343 0.2178 0.2707 0.0146  -0.0196 -0.0239 48  TYR A CE1 
2325 C CE2 . TYR B 51  ? 0.2475 0.2182 0.2716 0.0253  -0.0162 -0.0342 48  TYR A CE2 
2326 C CZ  . TYR B 51  ? 0.2462 0.2135 0.2737 0.0197  -0.0199 -0.0290 48  TYR A CZ  
2327 O OH  . TYR B 51  ? 0.2672 0.2138 0.2877 0.0186  -0.0239 -0.0288 48  TYR A OH  
2328 N N   . LYS B 52  ? 0.1604 0.2109 0.2152 0.0197  -0.0075 -0.0269 49  LYS A N   
2329 C CA  A LYS B 52  ? 0.1694 0.2281 0.2249 0.0170  -0.0085 -0.0260 49  LYS A CA  
2330 C CA  B LYS B 52  ? 0.1682 0.2266 0.2235 0.0169  -0.0086 -0.0260 49  LYS A CA  
2331 C CA  C LYS B 52  ? 0.1658 0.2248 0.2215 0.0171  -0.0084 -0.0261 49  LYS A CA  
2332 C C   . LYS B 52  ? 0.1577 0.2212 0.2165 0.0177  -0.0114 -0.0223 49  LYS A C   
2333 O O   . LYS B 52  ? 0.1588 0.2239 0.2138 0.0159  -0.0133 -0.0209 49  LYS A O   
2334 C CB  A LYS B 52  ? 0.1706 0.2336 0.2274 0.0167  -0.0059 -0.0280 49  LYS A CB  
2335 C CB  B LYS B 52  ? 0.1667 0.2291 0.2221 0.0161  -0.0062 -0.0281 49  LYS A CB  
2336 C CB  C LYS B 52  ? 0.1616 0.2266 0.2203 0.0169  -0.0062 -0.0274 49  LYS A CB  
2337 C CG  A LYS B 52  ? 0.1832 0.2515 0.2397 0.0135  -0.0075 -0.0276 49  LYS A CG  
2338 C CG  B LYS B 52  ? 0.1744 0.2382 0.2251 0.0129  -0.0080 -0.0284 49  LYS A CG  
2339 C CG  C LYS B 52  ? 0.1727 0.2429 0.2307 0.0134  -0.0084 -0.0269 49  LYS A CG  
2340 C CD  A LYS B 52  ? 0.1848 0.2486 0.2325 0.0113  -0.0077 -0.0295 49  LYS A CD  
2341 C CD  B LYS B 52  ? 0.1934 0.2571 0.2413 0.0110  -0.0062 -0.0301 49  LYS A CD  
2342 C CD  C LYS B 52  ? 0.1732 0.2512 0.2391 0.0120  -0.0081 -0.0262 49  LYS A CD  
2343 C CE  A LYS B 52  ? 0.1716 0.2368 0.2167 0.0088  -0.0099 -0.0294 49  LYS A CE  
2344 C CE  B LYS B 52  ? 0.1956 0.2568 0.2361 0.0094  -0.0087 -0.0306 49  LYS A CE  
2345 C CE  C LYS B 52  ? 0.1817 0.2598 0.2446 0.0070  -0.0097 -0.0267 49  LYS A CE  
2346 N NZ  A LYS B 52  ? 0.1627 0.2264 0.2066 0.0061  -0.0081 -0.0303 49  LYS A NZ  
2347 N NZ  B LYS B 52  ? 0.1899 0.2502 0.2281 0.0108  -0.0098 -0.0303 49  LYS A NZ  
2348 N NZ  C LYS B 52  ? 0.1883 0.2751 0.2617 0.0036  -0.0096 -0.0251 49  LYS A NZ  
2349 N N   . ASN B 53  ? 0.1570 0.2227 0.2220 0.0214  -0.0119 -0.0209 50  ASN A N   
2350 C CA  . ASN B 53  ? 0.1634 0.2332 0.2308 0.0230  -0.0160 -0.0173 50  ASN A CA  
2351 C C   . ASN B 53  ? 0.1624 0.2245 0.2239 0.0231  -0.0173 -0.0138 50  ASN A C   
2352 O O   . ASN B 53  ? 0.1626 0.2260 0.2199 0.0227  -0.0201 -0.0108 50  ASN A O   
2353 C CB  . ASN B 53  ? 0.1615 0.2382 0.2393 0.0276  -0.0164 -0.0164 50  ASN A CB  
2354 C CG  . ASN B 53  ? 0.1881 0.2760 0.2735 0.0251  -0.0161 -0.0177 50  ASN A CG  
2355 O OD1 . ASN B 53  ? 0.2103 0.3033 0.2963 0.0222  -0.0212 -0.0166 50  ASN A OD1 
2356 N ND2 . ASN B 53  ? 0.1901 0.2805 0.2795 0.0254  -0.0106 -0.0199 50  ASN A ND2 
2357 N N   . VAL B 54  ? 0.1606 0.2133 0.2207 0.0238  -0.0156 -0.0138 51  VAL A N   
2358 C CA  . VAL B 54  ? 0.1741 0.2185 0.2295 0.0224  -0.0167 -0.0096 51  VAL A CA  
2359 C C   . VAL B 54  ? 0.1696 0.2173 0.2211 0.0172  -0.0157 -0.0082 51  VAL A C   
2360 O O   . VAL B 54  ? 0.1891 0.2376 0.2364 0.0167  -0.0161 -0.0036 51  VAL A O   
2361 C CB  . VAL B 54  ? 0.1690 0.1999 0.2230 0.0231  -0.0162 -0.0103 51  VAL A CB  
2362 C CG1 . VAL B 54  ? 0.1945 0.2156 0.2443 0.0187  -0.0173 -0.0055 51  VAL A CG1 
2363 C CG2 . VAL B 54  ? 0.1838 0.2109 0.2403 0.0307  -0.0167 -0.0107 51  VAL A CG2 
2364 N N   . VAL B 55  ? 0.1577 0.2078 0.2097 0.0142  -0.0140 -0.0119 52  VAL A N   
2365 C CA  . VAL B 55  ? 0.1489 0.2042 0.1990 0.0110  -0.0126 -0.0107 52  VAL A CA  
2366 C C   . VAL B 55  ? 0.1519 0.2137 0.1975 0.0131  -0.0128 -0.0106 52  VAL A C   
2367 O O   . VAL B 55  ? 0.1500 0.2149 0.1913 0.0128  -0.0112 -0.0077 52  VAL A O   
2368 C CB  . VAL B 55  ? 0.1563 0.2124 0.2082 0.0082  -0.0120 -0.0144 52  VAL A CB  
2369 C CG1 . VAL B 55  ? 0.1491 0.2084 0.1991 0.0099  -0.0117 -0.0192 52  VAL A CG1 
2370 C CG2 . VAL B 55  ? 0.1614 0.2235 0.2151 0.0049  -0.0107 -0.0111 52  VAL A CG2 
2371 N N   . GLY B 56  ? 0.1367 0.2004 0.1831 0.0149  -0.0146 -0.0138 53  GLY A N   
2372 C CA  . GLY B 56  ? 0.1559 0.2229 0.1970 0.0157  -0.0164 -0.0148 53  GLY A CA  
2373 C C   . GLY B 56  ? 0.1685 0.2346 0.2028 0.0177  -0.0186 -0.0108 53  GLY A C   
2374 O O   . GLY B 56  ? 0.1904 0.2562 0.2152 0.0188  -0.0190 -0.0110 53  GLY A O   
2375 N N   . ALA B 57  ? 0.1770 0.2408 0.2141 0.0193  -0.0204 -0.0074 54  ALA A N   
2376 C CA  . ALA B 57  ? 0.1977 0.2588 0.2263 0.0217  -0.0228 -0.0028 54  ALA A CA  
2377 C C   . ALA B 57  ? 0.2094 0.2690 0.2293 0.0211  -0.0181 0.0009  54  ALA A C   
2378 O O   . ALA B 57  ? 0.2115 0.2698 0.2193 0.0234  -0.0185 0.0026  54  ALA A O   
2379 C CB  . ALA B 57  ? 0.2083 0.2657 0.2411 0.0242  -0.0253 0.0006  54  ALA A CB  
2380 N N   . ARG B 58  ? 0.1784 0.2386 0.2044 0.0179  -0.0135 0.0019  55  ARG A N   
2381 C CA  . ARG B 58  ? 0.1658 0.2287 0.1889 0.0163  -0.0081 0.0061  55  ARG A CA  
2382 C C   . ARG B 58  ? 0.1572 0.2263 0.1763 0.0179  -0.0055 0.0028  55  ARG A C   
2383 O O   . ARG B 58  ? 0.1684 0.2399 0.1792 0.0204  -0.0015 0.0061  55  ARG A O   
2384 C CB  . ARG B 58  ? 0.1660 0.2281 0.1988 0.0112  -0.0057 0.0089  55  ARG A CB  
2385 C CG  . ARG B 58  ? 0.1794 0.2323 0.2114 0.0097  -0.0065 0.0148  55  ARG A CG  
2386 C CD  . ARG B 58  ? 0.1844 0.2301 0.2176 0.0127  -0.0116 0.0118  55  ARG A CD  
2387 N NE  . ARG B 58  ? 0.2035 0.2375 0.2353 0.0125  -0.0130 0.0170  55  ARG A NE  
2388 C CZ  . ARG B 58  ? 0.2141 0.2416 0.2467 0.0170  -0.0171 0.0155  55  ARG A CZ  
2389 N NH1 . ARG B 58  ? 0.2189 0.2511 0.2574 0.0199  -0.0189 0.0089  55  ARG A NH1 
2390 N NH2 . ARG B 58  ? 0.2243 0.2401 0.2520 0.0185  -0.0187 0.0211  55  ARG A NH2 
2391 N N   . ARG B 59  ? 0.1589 0.2297 0.1823 0.0175  -0.0073 -0.0033 56  ARG A N   
2392 C CA  . ARG B 59  ? 0.1515 0.2256 0.1699 0.0200  -0.0055 -0.0066 56  ARG A CA  
2393 C C   . ARG B 59  ? 0.1657 0.2351 0.1688 0.0245  -0.0073 -0.0076 56  ARG A C   
2394 O O   . ARG B 59  ? 0.1609 0.2319 0.1553 0.0285  -0.0032 -0.0066 56  ARG A O   
2395 C CB  . ARG B 59  ? 0.1521 0.2257 0.1756 0.0186  -0.0077 -0.0123 56  ARG A CB  
2396 C CG  . ARG B 59  ? 0.1530 0.2295 0.1878 0.0150  -0.0066 -0.0121 56  ARG A CG  
2397 C CD  . ARG B 59  ? 0.1537 0.2271 0.1904 0.0141  -0.0089 -0.0175 56  ARG A CD  
2398 N NE  . ARG B 59  ? 0.1438 0.2176 0.1745 0.0167  -0.0086 -0.0205 56  ARG A NE  
2399 C CZ  . ARG B 59  ? 0.1492 0.2181 0.1762 0.0168  -0.0104 -0.0246 56  ARG A CZ  
2400 N NH1 . ARG B 59  ? 0.1288 0.1947 0.1591 0.0143  -0.0119 -0.0258 56  ARG A NH1 
2401 N NH2 . ARG B 59  ? 0.1432 0.2105 0.1636 0.0197  -0.0102 -0.0267 56  ARG A NH2 
2402 N N   . SER B 60  ? 0.1745 0.2387 0.1746 0.0242  -0.0134 -0.0091 57  SER A N   
2403 C CA  . SER B 60  ? 0.2033 0.2612 0.1881 0.0274  -0.0176 -0.0102 57  SER A CA  
2404 C C   . SER B 60  ? 0.1906 0.2464 0.1631 0.0312  -0.0144 -0.0048 57  SER A C   
2405 O O   . SER B 60  ? 0.2109 0.2620 0.1670 0.0357  -0.0135 -0.0058 57  SER A O   
2406 C CB  . SER B 60  ? 0.2326 0.2881 0.2201 0.0255  -0.0260 -0.0117 57  SER A CB  
2407 O OG  . SER B 60  ? 0.3634 0.4204 0.3593 0.0222  -0.0279 -0.0164 57  SER A OG  
2408 N N   . ALA B 61  ? 0.1934 0.2506 0.1715 0.0296  -0.0131 0.0010  58  ALA A N   
2409 C CA  . ALA B 61  ? 0.2048 0.2590 0.1704 0.0326  -0.0093 0.0077  58  ALA A CA  
2410 C C   . ALA B 61  ? 0.2023 0.2626 0.1653 0.0345  0.0007  0.0103  58  ALA A C   
2411 O O   . ALA B 61  ? 0.2131 0.2706 0.1592 0.0398  0.0045  0.0126  58  ALA A O   
2412 C CB  . ALA B 61  ? 0.2018 0.2542 0.1743 0.0301  -0.0099 0.0137  58  ALA A CB  
2413 N N   . TRP B 62  ? 0.1882 0.2574 0.1677 0.0308  0.0045  0.0096  59  TRP A N   
2414 C CA  . TRP B 62  ? 0.1929 0.2720 0.1751 0.0325  0.0132  0.0121  59  TRP A CA  
2415 C C   . TRP B 62  ? 0.2026 0.2797 0.1696 0.0403  0.0148  0.0075  59  TRP A C   
2416 O O   . TRP B 62  ? 0.2151 0.2962 0.1731 0.0458  0.0227  0.0112  59  TRP A O   
2417 C CB  . TRP B 62  ? 0.1730 0.2611 0.1759 0.0270  0.0137  0.0109  59  TRP A CB  
2418 C CG  . TRP B 62  ? 0.1839 0.2859 0.1947 0.0278  0.0219  0.0150  59  TRP A CG  
2419 C CD1 . TRP B 62  ? 0.1919 0.3025 0.2124 0.0234  0.0279  0.0234  59  TRP A CD1 
2420 C CD2 . TRP B 62  ? 0.1911 0.3002 0.2012 0.0337  0.0249  0.0113  59  TRP A CD2 
2421 N NE1 . TRP B 62  ? 0.1940 0.3202 0.2232 0.0258  0.0345  0.0253  59  TRP A NE1 
2422 C CE2 . TRP B 62  ? 0.2062 0.3314 0.2280 0.0333  0.0331  0.0180  59  TRP A CE2 
2423 C CE3 . TRP B 62  ? 0.2006 0.3034 0.2009 0.0395  0.0214  0.0037  59  TRP A CE3 
2424 C CZ2 . TRP B 62  ? 0.2161 0.3532 0.2415 0.0399  0.0378  0.0167  59  TRP A CZ2 
2425 C CZ3 . TRP B 62  ? 0.2157 0.3262 0.2161 0.0461  0.0258  0.0022  59  TRP A CZ3 
2426 C CH2 . TRP B 62  ? 0.2326 0.3612 0.2466 0.0468  0.0338  0.0085  59  TRP A CH2 
2427 N N   . ARG B 63  ? 0.1965 0.2666 0.1599 0.0411  0.0078  -0.0004 60  ARG A N   
2428 C CA  . ARG B 63  ? 0.2193 0.2828 0.1659 0.0483  0.0078  -0.0055 60  ARG A CA  
2429 C C   . ARG B 63  ? 0.2576 0.3102 0.1795 0.0543  0.0073  -0.0047 60  ARG A C   
2430 O O   . ARG B 63  ? 0.2629 0.3130 0.1689 0.0626  0.0130  -0.0051 60  ARG A O   
2431 C CB  . ARG B 63  ? 0.2222 0.2781 0.1694 0.0463  -0.0001 -0.0132 60  ARG A CB  
2432 C CG  . ARG B 63  ? 0.2114 0.2760 0.1767 0.0430  0.0014  -0.0146 60  ARG A CG  
2433 C CD  . ARG B 63  ? 0.2415 0.2971 0.2036 0.0422  -0.0044 -0.0214 60  ARG A CD  
2434 N NE  . ARG B 63  ? 0.2420 0.2904 0.2040 0.0367  -0.0123 -0.0234 60  ARG A NE  
2435 C CZ  . ARG B 63  ? 0.2357 0.2882 0.2129 0.0303  -0.0147 -0.0233 60  ARG A CZ  
2436 N NH1 . ARG B 63  ? 0.2307 0.2918 0.2220 0.0282  -0.0109 -0.0213 60  ARG A NH1 
2437 N NH2 . ARG B 63  ? 0.2613 0.3093 0.2394 0.0263  -0.0212 -0.0251 60  ARG A NH2 
2438 N N   . VAL B 64  ? 0.2516 0.2974 0.1696 0.0511  0.0004  -0.0034 61  VAL A N   
2439 C CA  . VAL B 64  ? 0.2823 0.3168 0.1758 0.0563  -0.0016 -0.0019 61  VAL A CA  
2440 C C   . VAL B 64  ? 0.2864 0.3262 0.1723 0.0610  0.0102  0.0061  61  VAL A C   
2441 O O   . VAL B 64  ? 0.3195 0.3520 0.1820 0.0696  0.0143  0.0055  61  VAL A O   
2442 C CB  . VAL B 64  ? 0.2812 0.3103 0.1759 0.0518  -0.0121 -0.0011 61  VAL A CB  
2443 C CG1 . VAL B 64  ? 0.3248 0.3427 0.1943 0.0571  -0.0145 0.0020  61  VAL A CG1 
2444 C CG2 . VAL B 64  ? 0.2691 0.2937 0.1691 0.0477  -0.0232 -0.0086 61  VAL A CG2 
2445 N N   . VAL B 65  ? 0.2642 0.3154 0.1685 0.0557  0.0160  0.0134  62  VAL A N   
2446 C CA  . VAL B 65  ? 0.2883 0.3450 0.1871 0.0583  0.0275  0.0228  62  VAL A CA  
2447 C C   . VAL B 65  ? 0.3130 0.3813 0.2130 0.0644  0.0390  0.0231  62  VAL A C   
2448 O O   . VAL B 65  ? 0.3510 0.4177 0.2317 0.0726  0.0475  0.0265  62  VAL A O   
2449 C CB  . VAL B 65  ? 0.2660 0.3284 0.1820 0.0500  0.0293  0.0311  62  VAL A CB  
2450 C CG1 . VAL B 65  ? 0.2923 0.3603 0.2028 0.0513  0.0418  0.0421  62  VAL A CG1 
2451 C CG2 . VAL B 65  ? 0.2604 0.3105 0.1717 0.0473  0.0185  0.0310  62  VAL A CG2 
2452 N N   . SER B 66  ? 0.3203 0.3981 0.2389 0.0623  0.0384  0.0185  63  SER A N   
2453 C CA  . SER B 66  ? 0.3563 0.4452 0.2776 0.0694  0.0471  0.0176  63  SER A CA  
2454 C C   . SER B 66  ? 0.4141 0.4900 0.3065 0.0817  0.0481  0.0119  63  SER A C   
2455 O O   . SER B 66  ? 0.4786 0.5604 0.3613 0.0910  0.0595  0.0153  63  SER A O   
2456 C CB  . SER B 66  ? 0.3517 0.4473 0.2934 0.0653  0.0422  0.0122  63  SER A CB  
2457 O OG  . SER B 66  ? 0.3772 0.4856 0.3440 0.0554  0.0430  0.0177  63  SER A OG  
2458 N N   . SER B 67  ? 0.4132 0.4708 0.2915 0.0816  0.0363  0.0035  64  SER A N   
2459 C CA  . SER B 67  ? 0.4649 0.5042 0.3124 0.0918  0.0340  -0.0030 64  SER A CA  
2460 C C   . SER B 67  ? 0.5485 0.5797 0.3692 0.0989  0.0395  0.0016  64  SER A C   
2461 O O   . SER B 67  ? 0.5932 0.6191 0.3922 0.1110  0.0472  0.0002  64  SER A O   
2462 C CB  . SER B 67  ? 0.5153 0.5378 0.3567 0.0869  0.0189  -0.0114 64  SER A CB  
2463 O OG  . SER B 67  ? 0.5978 0.5991 0.4074 0.0954  0.0146  -0.0181 64  SER A OG  
2464 N N   . ILE B 68  ? 0.4989 0.5278 0.3192 0.0925  0.0357  0.0071  65  ILE A N   
2465 C CA  . ILE B 68  ? 0.5444 0.5652 0.3390 0.0985  0.0410  0.0130  65  ILE A CA  
2466 C C   . ILE B 68  ? 0.5871 0.6247 0.3854 0.1044  0.0597  0.0219  65  ILE A C   
2467 O O   . ILE B 68  ? 0.6911 0.7211 0.4614 0.1158  0.0678  0.0231  65  ILE A O   
2468 C CB  . ILE B 68  ? 0.4887 0.5050 0.2851 0.0905  0.0333  0.0184  65  ILE A CB  
2469 C CG1 . ILE B 68  ? 0.5085 0.5081 0.2959 0.0875  0.0152  0.0100  65  ILE A CG1 
2470 C CG2 . ILE B 68  ? 0.5392 0.5506 0.3129 0.0959  0.0419  0.0278  65  ILE A CG2 
2471 C CD1 . ILE B 68  ? 0.4755 0.4753 0.2751 0.0791  0.0060  0.0140  65  ILE A CD1 
2472 N N   . GLU B 69  ? 0.5787 0.6386 0.4107 0.0967  0.0662  0.0279  66  GLU A N   
2473 C CA  . GLU B 69  ? 0.6031 0.6841 0.4471 0.0994  0.0834  0.0376  66  GLU A CA  
2474 C C   . GLU B 69  ? 0.7143 0.7993 0.5452 0.1142  0.0937  0.0343  66  GLU A C   
2475 O O   . GLU B 69  ? 0.7328 0.8301 0.5603 0.1205  0.1093  0.0428  66  GLU A O   
2476 C CB  . GLU B 69  ? 0.5503 0.6505 0.4334 0.0861  0.0826  0.0422  66  GLU A CB  
2477 C CG  . GLU B 69  ? 0.5413 0.6651 0.4444 0.0830  0.0975  0.0544  66  GLU A CG  
2478 C CD  . GLU B 69  ? 0.5036 0.6445 0.4441 0.0700  0.0948  0.0572  66  GLU A CD  
2479 O OE1 . GLU B 69  ? 0.5440 0.6802 0.4966 0.0639  0.0825  0.0498  66  GLU A OE1 
2480 O OE2 . GLU B 69  ? 0.5150 0.6758 0.4736 0.0662  0.1058  0.0672  66  GLU A OE2 
2481 N N   . GLN B 70  ? 0.7865 0.8597 0.6077 0.1204  0.0858  0.0227  67  GLN A N   
2482 C CA  . GLN B 70  ? 0.8041 0.8669 0.5970 0.1371  0.0917  0.0171  67  GLN A CA  
2483 C C   . GLN B 70  ? 0.7686 0.7993 0.5199 0.1425  0.0822  0.0103  67  GLN A C   
2484 O O   . GLN B 70  ? 0.8713 0.8941 0.5931 0.1542  0.0916  0.0129  67  GLN A O   
2485 C CB  . GLN B 70  ? 0.7996 0.8616 0.6009 0.1410  0.0865  0.0077  67  GLN A CB  
2486 C CG  . GLN B 70  ? 0.8514 0.9438 0.6889 0.1398  0.0956  0.0129  67  GLN A CG  
2487 C CD  . GLN B 70  ? 0.8286 0.9349 0.7014 0.1226  0.0882  0.0160  67  GLN A CD  
2488 O OE1 . GLN B 70  ? 0.8257 0.9213 0.7037 0.1154  0.0748  0.0089  67  GLN A OE1 
2489 N NE2 . GLN B 70  ? 0.8723 1.0018 0.7692 0.1159  0.0971  0.0268  67  GLN A NE2 
2490 N N   . ALA B 75  ? 0.7594 0.7979 0.3889 0.1694  0.1747  0.0893  72  ALA A N   
2491 C CA  . ALA B 75  ? 0.7850 0.8361 0.4165 0.1657  0.1927  0.1075  72  ALA A CA  
2492 C C   . ALA B 75  ? 0.7191 0.7969 0.4030 0.1465  0.1938  0.1170  72  ALA A C   
2493 O O   . ALA B 75  ? 0.6564 0.7349 0.3665 0.1354  0.1772  0.1095  72  ALA A O   
2494 C CB  . ALA B 75  ? 0.8199 0.8424 0.4106 0.1669  0.1875  0.1123  72  ALA A CB  
2495 N N   . ALA B 76  ? 0.6884 0.7876 0.3860 0.1429  0.2140  0.1335  73  ALA A N   
2496 C CA  . ALA B 76  ? 0.6297 0.7570 0.3775 0.1254  0.2179  0.1434  73  ALA A CA  
2497 C C   . ALA B 76  ? 0.5805 0.6929 0.3402 0.1085  0.1991  0.1433  73  ALA A C   
2498 O O   . ALA B 76  ? 0.5150 0.6394 0.3119 0.0965  0.1894  0.1395  73  ALA A O   
2499 C CB  . ALA B 76  ? 0.6294 0.7777 0.3835 0.1239  0.2425  0.1626  73  ALA A CB  
2500 N N   . ALA B 77  ? 0.6050 0.6915 0.3324 0.1085  0.1949  0.1484  74  ALA A N   
2501 C CA  . ALA B 77  ? 0.6001 0.6709 0.3350 0.0948  0.1787  0.1500  74  ALA A CA  
2502 C C   . ALA B 77  ? 0.5668 0.6271 0.3101 0.0930  0.1558  0.1332  74  ALA A C   
2503 O O   . ALA B 77  ? 0.5396 0.6043 0.3134 0.0798  0.1457  0.1323  74  ALA A O   
2504 C CB  . ALA B 77  ? 0.6566 0.7011 0.3501 0.0990  0.1793  0.1584  74  ALA A CB  
2505 N N   . ALA B 78  ? 0.5719 0.6187 0.2883 0.1062  0.1486  0.1201  75  ALA A N   
2506 C CA  . ALA B 78  ? 0.5728 0.6107 0.2946 0.1058  0.1288  0.1042  75  ALA A CA  
2507 C C   . ALA B 78  ? 0.5004 0.5612 0.2637 0.0992  0.1280  0.0984  75  ALA A C   
2508 O O   . ALA B 78  ? 0.4667 0.5253 0.2500 0.0907  0.1127  0.0910  75  ALA A O   
2509 C CB  . ALA B 78  ? 0.6242 0.6440 0.3069 0.1216  0.1252  0.0934  75  ALA A CB  
2510 N N   . GLN B 79  ? 0.4806 0.5632 0.2550 0.1048  0.1443  0.1012  76  GLN A N   
2511 C CA  A GLN B 79  ? 0.4390 0.5450 0.2508 0.1005  0.1447  0.0966  76  GLN A CA  
2512 C CA  B GLN B 79  ? 0.4405 0.5452 0.2520 0.1003  0.1435  0.0959  76  GLN A CA  
2513 C C   . GLN B 79  ? 0.4019 0.5209 0.2517 0.0825  0.1414  0.1038  76  GLN A C   
2514 O O   . GLN B 79  ? 0.3794 0.5028 0.2538 0.0750  0.1301  0.0964  76  GLN A O   
2515 C CB  A GLN B 79  ? 0.4518 0.5809 0.2683 0.1106  0.1648  0.1016  76  GLN A CB  
2516 C CB  B GLN B 79  ? 0.4560 0.5809 0.2699 0.1122  0.1604  0.0969  76  GLN A CB  
2517 C CG  A GLN B 79  ? 0.4779 0.5964 0.2628 0.1298  0.1675  0.0914  76  GLN A CG  
2518 C CG  B GLN B 79  ? 0.4482 0.5734 0.2675 0.1189  0.1518  0.0823  76  GLN A CG  
2519 C CD  A GLN B 79  ? 0.5099 0.6475 0.2899 0.1425  0.1907  0.0995  76  GLN A CD  
2520 C CD  B GLN B 79  ? 0.4209 0.5709 0.2849 0.1094  0.1498  0.0818  76  GLN A CD  
2521 O OE1 A GLN B 79  ? 0.5050 0.6743 0.3205 0.1377  0.2027  0.1081  76  GLN A OE1 
2522 O OE1 B GLN B 79  ? 0.4099 0.5543 0.2898 0.0989  0.1345  0.0757  76  GLN A OE1 
2523 N NE2 A GLN B 79  ? 0.5470 0.6665 0.2829 0.1587  0.1979  0.0978  76  GLN A NE2 
2524 N NE2 B GLN B 79  ? 0.4258 0.6036 0.3092 0.1141  0.1651  0.0879  76  GLN A NE2 
2525 N N   . GLN B 80  ? 0.4062 0.5298 0.2583 0.0758  0.1521  0.1187  77  GLN A N   
2526 C CA  . GLN B 80  ? 0.3847 0.5170 0.2688 0.0585  0.1497  0.1268  77  GLN A CA  
2527 C C   . GLN B 80  ? 0.3663 0.4763 0.2487 0.0513  0.1301  0.1200  77  GLN A C   
2528 O O   . GLN B 80  ? 0.3325 0.4489 0.2438 0.0402  0.1222  0.1177  77  GLN A O   
2529 C CB  . GLN B 80  ? 0.4077 0.5442 0.2879 0.0536  0.1651  0.1446  77  GLN A CB  
2530 C CG  . GLN B 80  ? 0.4044 0.5444 0.3130 0.0347  0.1621  0.1540  77  GLN A CG  
2531 C CD  . GLN B 80  ? 0.4386 0.5903 0.3534 0.0273  0.1797  0.1729  77  GLN A CD  
2532 O OE1 . GLN B 80  ? 0.4548 0.6180 0.3570 0.0358  0.1976  0.1809  77  GLN A OE1 
2533 N NE2 . GLN B 80  ? 0.4495 0.5960 0.3825 0.0107  0.1745  0.1805  77  GLN A NE2 
2534 N N   . MET B 81  ? 0.3895 0.4744 0.2385 0.0576  0.1227  0.1179  78  MET A N   
2535 C CA  . MET B 81  ? 0.3859 0.4518 0.2340 0.0527  0.1043  0.1116  78  MET A CA  
2536 C C   . MET B 81  ? 0.3379 0.4079 0.2030 0.0523  0.0920  0.0971  78  MET A C   
2537 O O   . MET B 81  ? 0.3149 0.3844 0.2017 0.0428  0.0826  0.0947  78  MET A O   
2538 C CB  . MET B 81  ? 0.4401 0.4811 0.2493 0.0616  0.0976  0.1108  78  MET A CB  
2539 C CG  . MET B 81  ? 0.4666 0.4899 0.2743 0.0593  0.0772  0.1028  78  MET A CG  
2540 S SD  . MET B 81  ? 0.5742 0.5712 0.3354 0.0708  0.0692  0.1028  78  MET A SD  
2541 C CE  . MET B 81  ? 0.5819 0.5732 0.3199 0.0723  0.0863  0.1210  78  MET A CE  
2542 N N   . ALA B 82  ? 0.3296 0.4023 0.1839 0.0627  0.0927  0.0879  79  ALA A N   
2543 C CA  . ALA B 82  ? 0.3075 0.3834 0.1758 0.0627  0.0825  0.0749  79  ALA A CA  
2544 C C   . ALA B 82  ? 0.2761 0.3726 0.1820 0.0532  0.0849  0.0757  79  ALA A C   
2545 O O   . ALA B 82  ? 0.2580 0.3529 0.1806 0.0468  0.0737  0.0691  79  ALA A O   
2546 C CB  . ALA B 82  ? 0.3237 0.3974 0.1715 0.0758  0.0852  0.0668  79  ALA A CB  
2547 N N   . ARG B 83  ? 0.2776 0.3940 0.1966 0.0522  0.0997  0.0847  80  ARG A N   
2548 C CA  . ARG B 83  ? 0.2530 0.3904 0.2080 0.0427  0.1013  0.0864  80  ARG A CA  
2549 C C   . ARG B 83  ? 0.2401 0.3710 0.2116 0.0284  0.0932  0.0904  80  ARG A C   
2550 O O   . ARG B 83  ? 0.2150 0.3480 0.2055 0.0224  0.0838  0.0836  80  ARG A O   
2551 C CB  . ARG B 83  ? 0.2591 0.4218 0.2284 0.0428  0.1188  0.0976  80  ARG A CB  
2552 C CG  . ARG B 83  ? 0.2342 0.4193 0.2429 0.0318  0.1178  0.0992  80  ARG A CG  
2553 C CD  . ARG B 83  ? 0.2392 0.4529 0.2644 0.0326  0.1350  0.1105  80  ARG A CD  
2554 N NE  . ARG B 83  ? 0.2623 0.4753 0.2795 0.0283  0.1468  0.1250  80  ARG A NE  
2555 C CZ  . ARG B 83  ? 0.2656 0.4770 0.2947 0.0135  0.1476  0.1361  80  ARG A CZ  
2556 N NH1 . ARG B 83  ? 0.2529 0.4601 0.3026 0.0003  0.1349  0.1333  80  ARG A NH1 
2557 N NH2 . ARG B 83  ? 0.2906 0.5012 0.3081 0.0122  0.1605  0.1496  80  ARG A NH2 
2558 N N   . GLU B 84  ? 0.2641 0.3846 0.2252 0.0241  0.0966  0.1007  81  GLU A N   
2559 C CA  . GLU B 84  ? 0.2711 0.3828 0.2455 0.0112  0.0900  0.1055  81  GLU A CA  
2560 C C   . GLU B 84  ? 0.2665 0.3597 0.2363 0.0115  0.0737  0.0949  81  GLU A C   
2561 O O   . GLU B 84  ? 0.2575 0.3487 0.2454 0.0029  0.0663  0.0926  81  GLU A O   
2562 C CB  . GLU B 84  ? 0.3061 0.4083 0.2677 0.0073  0.0975  0.1197  81  GLU A CB  
2563 C CG  . GLU B 84  ? 0.3264 0.4501 0.2992 0.0037  0.1150  0.1324  81  GLU A CG  
2564 C CD  . GLU B 84  ? 0.3661 0.4810 0.3239 0.0003  0.1249  0.1479  81  GLU A CD  
2565 O OE1 . GLU B 84  ? 0.3866 0.4766 0.3175 0.0047  0.1186  0.1480  81  GLU A OE1 
2566 O OE2 . GLU B 84  ? 0.3799 0.5125 0.3524 -0.0067 0.1388  0.1606  81  GLU A OE2 
2567 N N   . TYR B 85  ? 0.2830 0.3644 0.2297 0.0219  0.0682  0.0876  82  TYR A N   
2568 C CA  . TYR B 85  ? 0.2689 0.3376 0.2139 0.0232  0.0535  0.0773  82  TYR A CA  
2569 C C   . TYR B 85  ? 0.2419 0.3209 0.2070 0.0212  0.0484  0.0671  82  TYR A C   
2570 O O   . TYR B 85  ? 0.2179 0.2917 0.1954 0.0158  0.0397  0.0629  82  TYR A O   
2571 C CB  . TYR B 85  ? 0.2905 0.3455 0.2061 0.0337  0.0488  0.0735  82  TYR A CB  
2572 C CG  . TYR B 85  ? 0.2985 0.3392 0.2115 0.0339  0.0341  0.0676  82  TYR A CG  
2573 C CD1 . TYR B 85  ? 0.3108 0.3425 0.2317 0.0280  0.0293  0.0723  82  TYR A CD1 
2574 C CD2 . TYR B 85  ? 0.3230 0.3587 0.2248 0.0404  0.0251  0.0578  82  TYR A CD2 
2575 C CE1 . TYR B 85  ? 0.3140 0.3355 0.2347 0.0296  0.0168  0.0671  82  TYR A CE1 
2576 C CE2 . TYR B 85  ? 0.3212 0.3481 0.2248 0.0403  0.0121  0.0531  82  TYR A CE2 
2577 C CZ  . TYR B 85  ? 0.3139 0.3342 0.2258 0.0361  0.0085  0.0582  82  TYR A CZ  
2578 O OH  . TYR B 85  ? 0.3036 0.3169 0.2179 0.0376  -0.0032 0.0545  82  TYR A OH  
2579 N N   . ARG B 86  ? 0.2459 0.3383 0.2127 0.0263  0.0543  0.0635  83  ARG A N   
2580 C CA  . ARG B 86  ? 0.2320 0.3349 0.2171 0.0248  0.0508  0.0554  83  ARG A CA  
2581 C C   . ARG B 86  ? 0.2284 0.3393 0.2398 0.0133  0.0497  0.0586  83  ARG A C   
2582 O O   . ARG B 86  ? 0.2126 0.3223 0.2354 0.0103  0.0416  0.0510  83  ARG A O   
2583 C CB  . ARG B 86  ? 0.2417 0.3573 0.2244 0.0332  0.0577  0.0520  83  ARG A CB  
2584 C CG  . ARG B 86  ? 0.2506 0.3772 0.2530 0.0314  0.0541  0.0451  83  ARG A CG  
2585 C CD  . ARG B 86  ? 0.2899 0.4273 0.2909 0.0402  0.0596  0.0417  83  ARG A CD  
2586 N NE  . ARG B 86  ? 0.3454 0.5008 0.3520 0.0428  0.0733  0.0510  83  ARG A NE  
2587 C CZ  . ARG B 86  ? 0.3312 0.5061 0.3615 0.0354  0.0800  0.0599  83  ARG A CZ  
2588 N NH1 . ARG B 86  ? 0.3198 0.4985 0.3728 0.0233  0.0733  0.0606  83  ARG A NH1 
2589 N NH2 . ARG B 86  ? 0.3372 0.5274 0.3671 0.0406  0.0940  0.0682  83  ARG A NH2 
2590 N N   . GLU B 87  ? 0.2394 0.3591 0.2598 0.0071  0.0583  0.0695  84  GLU A N   
2591 C CA  . GLU B 87  ? 0.2306 0.3577 0.2757 -0.0051 0.0569  0.0734  84  GLU A CA  
2592 C C   . GLU B 87  ? 0.2348 0.3418 0.2792 -0.0114 0.0464  0.0715  84  GLU A C   
2593 O O   . GLU B 87  ? 0.2214 0.3281 0.2809 -0.0179 0.0395  0.0669  84  GLU A O   
2594 C CB  . GLU B 87  ? 0.2365 0.3762 0.2895 -0.0108 0.0688  0.0872  84  GLU A CB  
2595 C CG  . GLU B 87  ? 0.2381 0.4033 0.3002 -0.0054 0.0799  0.0895  84  GLU A CG  
2596 C CD  . GLU B 87  ? 0.2543 0.4349 0.3243 -0.0100 0.0938  0.1040  84  GLU A CD  
2597 O OE1 . GLU B 87  ? 0.2713 0.4406 0.3369 -0.0179 0.0955  0.1132  84  GLU A OE1 
2598 O OE2 . GLU B 87  ? 0.2733 0.4781 0.3544 -0.0052 0.1039  0.1069  84  GLU A OE2 
2599 N N   . LYS B 88  ? 0.2602 0.3499 0.2857 -0.0084 0.0450  0.0746  85  LYS A N   
2600 C CA  . LYS B 88  ? 0.2659 0.3359 0.2883 -0.0113 0.0355  0.0727  85  LYS A CA  
2601 C C   . LYS B 88  ? 0.2437 0.3106 0.2689 -0.0074 0.0261  0.0601  85  LYS A C   
2602 O O   . LYS B 88  ? 0.2284 0.2874 0.2629 -0.0125 0.0196  0.0569  85  LYS A O   
2603 C CB  . LYS B 88  ? 0.3180 0.3723 0.3175 -0.0054 0.0352  0.0775  85  LYS A CB  
2604 C CG  . LYS B 88  ? 0.3657 0.3992 0.3594 -0.0056 0.0260  0.0770  85  LYS A CG  
2605 C CD  . LYS B 88  ? 0.4534 0.4748 0.4230 0.0024  0.0254  0.0818  85  LYS A CD  
2606 C CE  . LYS B 88  ? 0.5246 0.5251 0.4846 0.0020  0.0206  0.0882  85  LYS A CE  
2607 N NZ  . LYS B 88  ? 0.5180 0.5098 0.4911 -0.0013 0.0125  0.0828  85  LYS A NZ  
2608 N N   . ILE B 89  ? 0.2164 0.2883 0.2327 0.0013  0.0257  0.0535  86  ILE A N   
2609 C CA  . ILE B 89  ? 0.2215 0.2921 0.2403 0.0046  0.0181  0.0425  86  ILE A CA  
2610 C C   . ILE B 89  ? 0.2064 0.2868 0.2434 -0.0006 0.0174  0.0383  86  ILE A C   
2611 O O   . ILE B 89  ? 0.1880 0.2628 0.2301 -0.0018 0.0109  0.0318  86  ILE A O   
2612 C CB  . ILE B 89  ? 0.2285 0.3001 0.2323 0.0136  0.0175  0.0374  86  ILE A CB  
2613 C CG1 . ILE B 89  ? 0.2479 0.3075 0.2333 0.0184  0.0149  0.0406  86  ILE A CG1 
2614 C CG2 . ILE B 89  ? 0.2308 0.3031 0.2394 0.0155  0.0109  0.0269  86  ILE A CG2 
2615 C CD1 . ILE B 89  ? 0.2537 0.3128 0.2209 0.0265  0.0149  0.0373  86  ILE A CD1 
2616 N N   . GLU B 90  ? 0.2102 0.3061 0.2554 -0.0022 0.0242  0.0417  87  GLU A N   
2617 C CA  . GLU B 90  ? 0.2242 0.3315 0.2872 -0.0070 0.0231  0.0388  87  GLU A CA  
2618 C C   . GLU B 90  ? 0.2218 0.3217 0.2965 -0.0172 0.0179  0.0405  87  GLU A C   
2619 O O   . GLU B 90  ? 0.2067 0.3057 0.2890 -0.0194 0.0118  0.0339  87  GLU A O   
2620 C CB  . GLU B 90  ? 0.2502 0.3778 0.3229 -0.0071 0.0318  0.0446  87  GLU A CB  
2621 C CG  . GLU B 90  ? 0.2912 0.4304 0.3641 0.0010  0.0333  0.0384  87  GLU A CG  
2622 C CD  . GLU B 90  ? 0.3032 0.4611 0.3797 0.0053  0.0443  0.0450  87  GLU A CD  
2623 O OE1 . GLU B 90  ? 0.4517 0.6224 0.5441 -0.0022 0.0493  0.0539  87  GLU A OE1 
2624 O OE2 . GLU B 90  ? 0.2943 0.4534 0.3573 0.0159  0.0481  0.0418  87  GLU A OE2 
2625 N N   . THR B 91  ? 0.2225 0.3150 0.2962 -0.0230 0.0201  0.0492  88  THR A N   
2626 C CA  . THR B 91  ? 0.2327 0.3136 0.3145 -0.0329 0.0145  0.0511  88  THR A CA  
2627 C C   . THR B 91  ? 0.2351 0.2977 0.3087 -0.0291 0.0060  0.0423  88  THR A C   
2628 O O   . THR B 91  ? 0.2156 0.2734 0.2961 -0.0332 0.0000  0.0369  88  THR A O   
2629 C CB  . THR B 91  ? 0.2484 0.3226 0.3282 -0.0394 0.0190  0.0630  88  THR A CB  
2630 O OG1 . THR B 91  ? 0.2249 0.3208 0.3171 -0.0435 0.0276  0.0705  88  THR A OG1 
2631 C CG2 . THR B 91  ? 0.2629 0.3190 0.3469 -0.0494 0.0123  0.0647  88  THR A CG2 
2632 N N   . GLU B 92  ? 0.2445 0.2988 0.3039 -0.0207 0.0056  0.0406  89  GLU A N   
2633 C CA  . GLU B 92  ? 0.2359 0.2774 0.2900 -0.0158 -0.0011 0.0328  89  GLU A CA  
2634 C C   . GLU B 92  ? 0.2290 0.2780 0.2889 -0.0139 -0.0037 0.0234  89  GLU A C   
2635 O O   . GLU B 92  ? 0.2116 0.2513 0.2733 -0.0151 -0.0086 0.0181  89  GLU A O   
2636 C CB  . GLU B 92  ? 0.2346 0.2717 0.2759 -0.0070 -0.0016 0.0326  89  GLU A CB  
2637 C CG  . GLU B 92  ? 0.2582 0.2839 0.2901 -0.0071 -0.0004 0.0417  89  GLU A CG  
2638 C CD  . GLU B 92  ? 0.2683 0.2902 0.2874 0.0019  -0.0027 0.0415  89  GLU A CD  
2639 O OE1 . GLU B 92  ? 0.2352 0.2623 0.2545 0.0073  -0.0061 0.0339  89  GLU A OE1 
2640 O OE2 . GLU B 92  ? 0.2856 0.2987 0.2943 0.0029  -0.0018 0.0494  89  GLU A OE2 
2641 N N   . LEU B 93  ? 0.2262 0.2902 0.2870 -0.0108 -0.0002 0.0217  90  LEU A N   
2642 C CA  . LEU B 93  ? 0.2167 0.2866 0.2805 -0.0083 -0.0025 0.0136  90  LEU A CA  
2643 C C   . LEU B 93  ? 0.2255 0.2964 0.3000 -0.0150 -0.0057 0.0119  90  LEU A C   
2644 O O   . LEU B 93  ? 0.2646 0.3280 0.3378 -0.0142 -0.0103 0.0051  90  LEU A O   
2645 C CB  . LEU B 93  ? 0.2448 0.3272 0.3051 -0.0031 0.0020  0.0134  90  LEU A CB  
2646 C CG  . LEU B 93  ? 0.2568 0.3412 0.3139 0.0019  -0.0002 0.0054  90  LEU A CG  
2647 C CD1 . LEU B 93  ? 0.2826 0.3715 0.3297 0.0083  0.0031  0.0054  90  LEU A CD1 
2648 C CD2 . LEU B 93  ? 0.3074 0.3999 0.3743 -0.0007 -0.0011 0.0030  90  LEU A CD2 
2649 N N   . ARG B 94  ? 0.2143 0.2933 0.2989 -0.0220 -0.0037 0.0183  91  ARG A N   
2650 C CA  . ARG B 94  ? 0.2513 0.3315 0.3474 -0.0300 -0.0086 0.0173  91  ARG A CA  
2651 C C   . ARG B 94  ? 0.2463 0.3053 0.3381 -0.0343 -0.0152 0.0147  91  ARG A C   
2652 O O   . ARG B 94  ? 0.2531 0.3070 0.3461 -0.0363 -0.0214 0.0085  91  ARG A O   
2653 C CB  . ARG B 94  ? 0.3009 0.3950 0.4113 -0.0382 -0.0052 0.0264  91  ARG A CB  
2654 C CG  . ARG B 94  ? 0.3369 0.4537 0.4537 -0.0331 0.0009  0.0278  91  ARG A CG  
2655 C CD  . ARG B 94  ? 0.4081 0.5429 0.5424 -0.0408 0.0054  0.0374  91  ARG A CD  
2656 N NE  . ARG B 94  ? 0.4284 0.5800 0.5610 -0.0324 0.0154  0.0410  91  ARG A NE  
2657 C CZ  . ARG B 94  ? 0.5120 0.6839 0.6542 -0.0276 0.0184  0.0404  91  ARG A CZ  
2658 N NH1 . ARG B 94  ? 0.5189 0.7027 0.6786 -0.0324 0.0126  0.0389  91  ARG A NH1 
2659 N NH2 . ARG B 94  ? 0.5943 0.7742 0.7277 -0.0172 0.0270  0.0414  91  ARG A NH2 
2660 N N   . ASP B 95  ? 0.2345 0.2801 0.3195 -0.0346 -0.0142 0.0191  92  ASP A N   
2661 C CA  . ASP B 95  ? 0.2407 0.2632 0.3190 -0.0366 -0.0198 0.0168  92  ASP A CA  
2662 C C   . ASP B 95  ? 0.2203 0.2343 0.2896 -0.0281 -0.0225 0.0073  92  ASP A C   
2663 O O   . ASP B 95  ? 0.2393 0.2394 0.3054 -0.0300 -0.0281 0.0019  92  ASP A O   
2664 C CB  . ASP B 95  ? 0.2664 0.2763 0.3386 -0.0374 -0.0178 0.0244  92  ASP A CB  
2665 C CG  . ASP B 95  ? 0.3004 0.3134 0.3811 -0.0485 -0.0157 0.0346  92  ASP A CG  
2666 O OD1 . ASP B 95  ? 0.3331 0.3590 0.4271 -0.0563 -0.0167 0.0355  92  ASP A OD1 
2667 O OD2 . ASP B 95  ? 0.3591 0.3641 0.4337 -0.0489 -0.0125 0.0424  92  ASP A OD2 
2668 N N   . ILE B 96  ? 0.1938 0.2166 0.2592 -0.0195 -0.0187 0.0052  93  ILE A N   
2669 C CA  . ILE B 96  ? 0.1929 0.2115 0.2524 -0.0121 -0.0198 -0.0025 93  ILE A CA  
2670 C C   . ILE B 96  ? 0.1884 0.2109 0.2499 -0.0138 -0.0223 -0.0086 93  ILE A C   
2671 O O   . ILE B 96  ? 0.1987 0.2088 0.2541 -0.0120 -0.0253 -0.0145 93  ILE A O   
2672 C CB  . ILE B 96  ? 0.1846 0.2122 0.2412 -0.0047 -0.0162 -0.0025 93  ILE A CB  
2673 C CG1 . ILE B 96  ? 0.1937 0.2147 0.2461 -0.0017 -0.0156 0.0030  93  ILE A CG1 
2674 C CG2 . ILE B 96  ? 0.1939 0.2219 0.2478 0.0013  -0.0164 -0.0097 93  ILE A CG2 
2675 C CD1 . ILE B 96  ? 0.1975 0.2293 0.2472 0.0027  -0.0133 0.0053  93  ILE A CD1 
2676 N N   . CYS B 97  ? 0.1691 0.2077 0.2374 -0.0160 -0.0208 -0.0073 94  CYS A N   
2677 C CA  . CYS B 97  ? 0.1808 0.2236 0.2507 -0.0170 -0.0240 -0.0123 94  CYS A CA  
2678 C C   . CYS B 97  ? 0.1906 0.2225 0.2617 -0.0239 -0.0309 -0.0140 94  CYS A C   
2679 O O   . CYS B 97  ? 0.1895 0.2131 0.2535 -0.0221 -0.0348 -0.0206 94  CYS A O   
2680 C CB  . CYS B 97  ? 0.1706 0.2328 0.2484 -0.0170 -0.0214 -0.0098 94  CYS A CB  
2681 S SG  . CYS B 97  ? 0.1871 0.2574 0.2587 -0.0083 -0.0154 -0.0104 94  CYS A SG  
2682 N N   . ASN B 98  ? 0.2159 0.2452 0.2937 -0.0317 -0.0326 -0.0083 95  ASN A N   
2683 C CA  . ASN B 98  ? 0.2472 0.2634 0.3259 -0.0401 -0.0407 -0.0097 95  ASN A CA  
2684 C C   . ASN B 98  ? 0.2528 0.2432 0.3157 -0.0363 -0.0442 -0.0159 95  ASN A C   
2685 O O   . ASN B 98  ? 0.2492 0.2281 0.3063 -0.0387 -0.0514 -0.0216 95  ASN A O   
2686 C CB  . ASN B 98  ? 0.2962 0.3150 0.3863 -0.0506 -0.0414 -0.0010 95  ASN A CB  
2687 C CG  . ASN B 98  ? 0.3459 0.3916 0.4537 -0.0551 -0.0387 0.0049  95  ASN A CG  
2688 O OD1 . ASN B 98  ? 0.3811 0.4415 0.4932 -0.0515 -0.0393 0.0015  95  ASN A OD1 
2689 N ND2 . ASN B 98  ? 0.3709 0.4229 0.4887 -0.0623 -0.0352 0.0143  95  ASN A ND2 
2690 N N   . ASP B 99  ? 0.2671 0.2489 0.3226 -0.0295 -0.0395 -0.0151 96  ASP A N   
2691 C CA  . ASP B 99  ? 0.2987 0.2584 0.3398 -0.0232 -0.0412 -0.0211 96  ASP A CA  
2692 C C   . ASP B 99  ? 0.2902 0.2507 0.3235 -0.0166 -0.0409 -0.0291 96  ASP A C   
2693 O O   . ASP B 99  ? 0.2900 0.2325 0.3116 -0.0158 -0.0456 -0.0352 96  ASP A O   
2694 C CB  . ASP B 99  ? 0.3253 0.2799 0.3624 -0.0154 -0.0361 -0.0185 96  ASP A CB  
2695 C CG  . ASP B 99  ? 0.4364 0.3746 0.4715 -0.0192 -0.0382 -0.0128 96  ASP A CG  
2696 O OD1 . ASP B 99  ? 0.4597 0.3905 0.4981 -0.0302 -0.0433 -0.0096 96  ASP A OD1 
2697 O OD2 . ASP B 99  ? 0.4652 0.3986 0.4962 -0.0114 -0.0350 -0.0108 96  ASP A OD2 
2698 N N   . VAL B 100 ? 0.2722 0.2510 0.3097 -0.0118 -0.0353 -0.0289 97  VAL A N   
2699 C CA  . VAL B 100 ? 0.2587 0.2392 0.2889 -0.0060 -0.0338 -0.0350 97  VAL A CA  
2700 C C   . VAL B 100 ? 0.2468 0.2240 0.2738 -0.0108 -0.0406 -0.0388 97  VAL A C   
2701 O O   . VAL B 100 ? 0.2433 0.2070 0.2569 -0.0073 -0.0427 -0.0449 97  VAL A O   
2702 C CB  . VAL B 100 ? 0.2432 0.2428 0.2792 -0.0022 -0.0278 -0.0333 97  VAL A CB  
2703 C CG1 . VAL B 100 ? 0.2612 0.2617 0.2893 0.0021  -0.0264 -0.0385 97  VAL A CG1 
2704 C CG2 . VAL B 100 ? 0.2609 0.2629 0.2988 0.0029  -0.0227 -0.0305 97  VAL A CG2 
2705 N N   . LEU B 101 ? 0.2275 0.2187 0.2670 -0.0180 -0.0438 -0.0348 98  LEU A N   
2706 C CA  . LEU B 101 ? 0.2409 0.2329 0.2807 -0.0228 -0.0517 -0.0375 98  LEU A CA  
2707 C C   . LEU B 101 ? 0.2754 0.2449 0.3059 -0.0279 -0.0608 -0.0415 98  LEU A C   
2708 O O   . LEU B 101 ? 0.2786 0.2395 0.2985 -0.0272 -0.0672 -0.0473 98  LEU A O   
2709 C CB  . LEU B 101 ? 0.2435 0.2582 0.3018 -0.0286 -0.0522 -0.0313 98  LEU A CB  
2710 C CG  . LEU B 101 ? 0.2321 0.2650 0.2943 -0.0222 -0.0451 -0.0297 98  LEU A CG  
2711 C CD1 . LEU B 101 ? 0.1996 0.2549 0.2794 -0.0258 -0.0430 -0.0228 98  LEU A CD1 
2712 C CD2 . LEU B 101 ? 0.2202 0.2516 0.2726 -0.0168 -0.0467 -0.0352 98  LEU A CD2 
2713 N N   . SER B 102 ? 0.2692 0.2270 0.3010 -0.0322 -0.0618 -0.0386 99  SER A N   
2714 C CA  . SER B 102 ? 0.3272 0.2586 0.3472 -0.0364 -0.0705 -0.0427 99  SER A CA  
2715 C C   . SER B 102 ? 0.3229 0.2321 0.3194 -0.0259 -0.0693 -0.0513 99  SER A C   
2716 O O   . SER B 102 ? 0.3618 0.2524 0.3441 -0.0274 -0.0778 -0.0575 99  SER A O   
2717 C CB  . SER B 102 ? 0.3433 0.2663 0.3692 -0.0425 -0.0705 -0.0366 99  SER A CB  
2718 O OG  . SER B 102 ? 0.4123 0.3067 0.4255 -0.0475 -0.0802 -0.0409 99  SER A OG  
2719 N N   . LEU B 103 ? 0.3114 0.2228 0.3039 -0.0154 -0.0590 -0.0512 100 LEU A N   
2720 C CA  . LEU B 103 ? 0.3276 0.2237 0.3011 -0.0042 -0.0548 -0.0579 100 LEU A CA  
2721 C C   . LEU B 103 ? 0.3182 0.2165 0.2819 -0.0017 -0.0563 -0.0630 100 LEU A C   
2722 O O   . LEU B 103 ? 0.3178 0.1951 0.2609 0.0029  -0.0589 -0.0699 100 LEU A O   
2723 C CB  . LEU B 103 ? 0.3189 0.2249 0.2967 0.0053  -0.0435 -0.0552 100 LEU A CB  
2724 C CG  . LEU B 103 ? 0.3308 0.2291 0.3127 0.0061  -0.0423 -0.0509 100 LEU A CG  
2725 C CD1 . LEU B 103 ? 0.3330 0.2462 0.3218 0.0151  -0.0327 -0.0481 100 LEU A CD1 
2726 C CD2 . LEU B 103 ? 0.3589 0.2253 0.3235 0.0093  -0.0467 -0.0555 100 LEU A CD2 
2727 N N   . LEU B 104 ? 0.2866 0.2084 0.2631 -0.0041 -0.0545 -0.0596 101 LEU A N   
2728 C CA  . LEU B 104 ? 0.3083 0.2341 0.2770 -0.0021 -0.0561 -0.0630 101 LEU A CA  
2729 C C   . LEU B 104 ? 0.3558 0.2682 0.3157 -0.0083 -0.0693 -0.0672 101 LEU A C   
2730 O O   . LEU B 104 ? 0.3438 0.2401 0.2825 -0.0032 -0.0716 -0.0735 101 LEU A O   
2731 C CB  . LEU B 104 ? 0.3009 0.2529 0.2860 -0.0033 -0.0521 -0.0578 101 LEU A CB  
2732 C CG  . LEU B 104 ? 0.2882 0.2515 0.2776 0.0031  -0.0406 -0.0551 101 LEU A CG  
2733 C CD1 . LEU B 104 ? 0.2756 0.2615 0.2811 0.0003  -0.0388 -0.0498 101 LEU A CD1 
2734 C CD2 . LEU B 104 ? 0.2892 0.2462 0.2631 0.0109  -0.0349 -0.0589 101 LEU A CD2 
2735 N N   . GLU B 105 ? 0.3344 0.2523 0.3096 -0.0190 -0.0777 -0.0637 102 GLU A N   
2736 C CA  . GLU B 105 ? 0.3728 0.2811 0.3442 -0.0270 -0.0922 -0.0669 102 GLU A CA  
2737 C C   . GLU B 105 ? 0.3698 0.2441 0.3184 -0.0265 -0.0987 -0.0738 102 GLU A C   
2738 O O   . GLU B 105 ? 0.3978 0.2556 0.3276 -0.0259 -0.1079 -0.0804 102 GLU A O   
2739 C CB  . GLU B 105 ? 0.3680 0.2957 0.3658 -0.0392 -0.0981 -0.0599 102 GLU A CB  
2740 C CG  . GLU B 105 ? 0.4048 0.3403 0.4080 -0.0455 -0.1110 -0.0611 102 GLU A CG  
2741 C CD  . GLU B 105 ? 0.3903 0.3428 0.3931 -0.0377 -0.1075 -0.0614 102 GLU A CD  
2742 O OE1 . GLU B 105 ? 0.4435 0.3929 0.4418 -0.0406 -0.1198 -0.0647 102 GLU A OE1 
2743 O OE2 . GLU B 105 ? 0.3329 0.2988 0.3381 -0.0295 -0.0949 -0.0589 102 GLU A OE2 
2744 N N   . LYS B 106 ? 0.3746 0.2359 0.3220 -0.0261 -0.0948 -0.0726 103 LYS A N   
2745 C CA  . LYS B 106 ? 0.4422 0.2684 0.3677 -0.0257 -0.1017 -0.0789 103 LYS A CA  
2746 C C   . LYS B 106 ? 0.4397 0.2462 0.3367 -0.0107 -0.0949 -0.0867 103 LYS A C   
2747 O O   . LYS B 106 ? 0.4479 0.2256 0.3201 -0.0090 -0.1030 -0.0944 103 LYS A O   
2748 C CB  . LYS B 106 ? 0.4791 0.2986 0.4147 -0.0308 -0.1005 -0.0737 103 LYS A CB  
2749 C CG  . LYS B 106 ? 0.6088 0.3902 0.5234 -0.0320 -0.1088 -0.0792 103 LYS A CG  
2750 C CD  . LYS B 106 ? 0.6381 0.4102 0.5620 -0.0386 -0.1093 -0.0731 103 LYS A CD  
2751 C CE  . LYS B 106 ? 0.7473 0.4764 0.6455 -0.0390 -0.1192 -0.0803 103 LYS A CE  
2752 N NZ  . LYS B 106 ? 0.7881 0.5031 0.6904 -0.0427 -0.1185 -0.0747 103 LYS A NZ  
2753 N N   . PHE B 107 ? 0.3985 0.2191 0.2978 0.0002  -0.0801 -0.0847 104 PHE A N   
2754 C CA  . PHE B 107 ? 0.4097 0.2141 0.2855 0.0146  -0.0712 -0.0904 104 PHE A CA  
2755 C C   . PHE B 107 ? 0.3995 0.2189 0.2711 0.0213  -0.0632 -0.0908 104 PHE A C   
2756 O O   . PHE B 107 ? 0.4469 0.2492 0.2936 0.0277  -0.0638 -0.0970 104 PHE A O   
2757 C CB  . PHE B 107 ? 0.4021 0.2078 0.2844 0.0223  -0.0603 -0.0873 104 PHE A CB  
2758 C CG  . PHE B 107 ? 0.4204 0.2055 0.3022 0.0174  -0.0675 -0.0869 104 PHE A CG  
2759 C CD1 . PHE B 107 ? 0.4670 0.2156 0.3219 0.0222  -0.0730 -0.0946 104 PHE A CD1 
2760 C CD2 . PHE B 107 ? 0.4044 0.2041 0.3098 0.0084  -0.0685 -0.0787 104 PHE A CD2 
2761 C CE1 . PHE B 107 ? 0.4876 0.2134 0.3400 0.0171  -0.0805 -0.0942 104 PHE A CE1 
2762 C CE2 . PHE B 107 ? 0.4379 0.2166 0.3413 0.0033  -0.0750 -0.0775 104 PHE A CE2 
2763 C CZ  . PHE B 107 ? 0.4716 0.2128 0.3489 0.0076  -0.0810 -0.0851 104 PHE A CZ  
2764 N N   . LEU B 108 ? 0.3559 0.2047 0.2492 0.0201  -0.0556 -0.0841 105 LEU A N   
2765 C CA  . LEU B 108 ? 0.3473 0.2083 0.2371 0.0280  -0.0444 -0.0834 105 LEU A CA  
2766 C C   . LEU B 108 ? 0.3590 0.2196 0.2378 0.0260  -0.0505 -0.0856 105 LEU A C   
2767 O O   . LEU B 108 ? 0.3772 0.2260 0.2338 0.0338  -0.0461 -0.0896 105 LEU A O   
2768 C CB  . LEU B 108 ? 0.3268 0.2156 0.2416 0.0273  -0.0355 -0.0759 105 LEU A CB  
2769 C CG  . LEU B 108 ? 0.3168 0.2065 0.2415 0.0307  -0.0298 -0.0732 105 LEU A CG  
2770 C CD1 . LEU B 108 ? 0.3029 0.2183 0.2512 0.0275  -0.0252 -0.0661 105 LEU A CD1 
2771 C CD2 . LEU B 108 ? 0.3533 0.2319 0.2635 0.0434  -0.0199 -0.0765 105 LEU A CD2 
2772 N N   . ILE B 109 ? 0.3319 0.2048 0.2249 0.0163  -0.0605 -0.0830 106 ILE A N   
2773 C CA  . ILE B 109 ? 0.3343 0.2088 0.2185 0.0154  -0.0670 -0.0845 106 ILE A CA  
2774 C C   . ILE B 109 ? 0.3826 0.2283 0.2375 0.0174  -0.0767 -0.0925 106 ILE A C   
2775 O O   . ILE B 109 ? 0.3796 0.2165 0.2127 0.0246  -0.0736 -0.0952 106 ILE A O   
2776 C CB  . ILE B 109 ? 0.3063 0.2029 0.2141 0.0063  -0.0751 -0.0797 106 ILE A CB  
2777 C CG1 . ILE B 109 ? 0.2788 0.2009 0.2082 0.0068  -0.0646 -0.0728 106 ILE A CG1 
2778 C CG2 . ILE B 109 ? 0.3190 0.2140 0.2164 0.0059  -0.0849 -0.0819 106 ILE A CG2 
2779 C CD1 . ILE B 109 ? 0.2528 0.1968 0.2077 -0.0011 -0.0698 -0.0674 106 ILE A CD1 
2780 N N   . PRO B 110 ? 0.4324 0.2606 0.2833 0.0116  -0.0883 -0.0962 107 PRO A N   
2781 C CA  . PRO B 110 ? 0.4713 0.2697 0.2916 0.0133  -0.0995 -0.1046 107 PRO A CA  
2782 C C   . PRO B 110 ? 0.5050 0.2785 0.2928 0.0267  -0.0897 -0.1105 107 PRO A C   
2783 O O   . PRO B 110 ? 0.5398 0.2907 0.2976 0.0307  -0.0965 -0.1171 107 PRO A O   
2784 C CB  . PRO B 110 ? 0.5003 0.2860 0.3268 0.0024  -0.1139 -0.1064 107 PRO A CB  
2785 C CG  . PRO B 110 ? 0.4714 0.2759 0.3271 -0.0019 -0.1059 -0.0991 107 PRO A CG  
2786 C CD  . PRO B 110 ? 0.4311 0.2659 0.3050 0.0021  -0.0926 -0.0925 107 PRO A CD  
2787 N N   . ASN B 111 ? 0.4987 0.2766 0.2918 0.0340  -0.0744 -0.1083 108 ASN A N   
2788 C CA  . ASN B 111 ? 0.5452 0.3053 0.3124 0.0480  -0.0622 -0.1125 108 ASN A CA  
2789 C C   . ASN B 111 ? 0.4957 0.2715 0.2605 0.0560  -0.0469 -0.1088 108 ASN A C   
2790 O O   . ASN B 111 ? 0.5038 0.2667 0.2474 0.0679  -0.0355 -0.1117 108 ASN A O   
2791 C CB  . ASN B 111 ? 0.5845 0.3412 0.3592 0.0531  -0.0537 -0.1118 108 ASN A CB  
2792 C CG  . ASN B 111 ? 0.7038 0.4256 0.4565 0.0542  -0.0637 -0.1195 108 ASN A CG  
2793 O OD1 . ASN B 111 ? 0.8862 0.5896 0.6205 0.0667  -0.0549 -0.1235 108 ASN A OD1 
2794 N ND2 . ASN B 111 ? 0.7547 0.4673 0.5094 0.0416  -0.0816 -0.1213 108 ASN A ND2 
2795 N N   . ALA B 112 ? 0.4609 0.2626 0.2461 0.0501  -0.0460 -0.1025 109 ALA A N   
2796 C CA  . ALA B 112 ? 0.4347 0.2521 0.2218 0.0556  -0.0314 -0.0976 109 ALA A CA  
2797 C C   . ALA B 112 ? 0.4725 0.2712 0.2257 0.0621  -0.0311 -0.1015 109 ALA A C   
2798 O O   . ALA B 112 ? 0.5027 0.2986 0.2490 0.0574  -0.0429 -0.1023 109 ALA A O   
2799 C CB  . ALA B 112 ? 0.3940 0.2393 0.2094 0.0474  -0.0325 -0.0906 109 ALA A CB  
2800 N N   . SER B 113 ? 0.4877 0.2747 0.2199 0.0735  -0.0173 -0.1033 110 SER A N   
2801 C CA  . SER B 113 ? 0.5164 0.2803 0.2102 0.0817  -0.0157 -0.1076 110 SER A CA  
2802 C C   . SER B 113 ? 0.5099 0.2857 0.2001 0.0832  -0.0055 -0.1013 110 SER A C   
2803 O O   . SER B 113 ? 0.5411 0.2973 0.1977 0.0896  -0.0044 -0.1040 110 SER A O   
2804 C CB  . SER B 113 ? 0.5410 0.2838 0.2114 0.0941  -0.0061 -0.1131 110 SER A CB  
2805 O OG  . SER B 113 ? 0.5200 0.2825 0.2059 0.1004  0.0138  -0.1071 110 SER A OG  
2806 N N   . GLN B 114 ? 0.4823 0.2864 0.2032 0.0777  0.0015  -0.0933 111 GLN A N   
2807 C CA  . GLN B 114 ? 0.4846 0.2995 0.2048 0.0772  0.0103  -0.0866 111 GLN A CA  
2808 C C   . GLN B 114 ? 0.4365 0.2715 0.1833 0.0669  0.0017  -0.0817 111 GLN A C   
2809 O O   . GLN B 114 ? 0.4071 0.2552 0.1799 0.0608  -0.0048 -0.0816 111 GLN A O   
2810 C CB  . GLN B 114 ? 0.5148 0.3443 0.2453 0.0820  0.0308  -0.0809 111 GLN A CB  
2811 C CG  . GLN B 114 ? 0.6141 0.4252 0.3157 0.0945  0.0427  -0.0846 111 GLN A CG  
2812 C CD  . GLN B 114 ? 0.6720 0.5017 0.3895 0.0996  0.0629  -0.0787 111 GLN A CD  
2813 O OE1 . GLN B 114 ? 0.6580 0.5109 0.4096 0.0951  0.0651  -0.0750 111 GLN A OE1 
2814 N NE2 . GLN B 114 ? 0.7024 0.5222 0.3947 0.1093  0.0774  -0.0779 111 GLN A NE2 
2815 N N   . ALA B 115 ? 0.4300 0.2665 0.1690 0.0659  0.0034  -0.0772 112 ALA A N   
2816 C CA  . ALA B 115 ? 0.4259 0.2782 0.1854 0.0583  -0.0040 -0.0728 112 ALA A CA  
2817 C C   . ALA B 115 ? 0.3998 0.2764 0.1927 0.0535  0.0039  -0.0678 112 ALA A C   
2818 O O   . ALA B 115 ? 0.3594 0.2488 0.1741 0.0477  -0.0047 -0.0671 112 ALA A O   
2819 C CB  . ALA B 115 ? 0.4318 0.2783 0.1743 0.0595  -0.0023 -0.0685 112 ALA A CB  
2820 N N   . GLU B 116 ? 0.4069 0.2901 0.2036 0.0563  0.0199  -0.0642 113 GLU A N   
2821 C CA  . GLU B 116 ? 0.3876 0.2937 0.2154 0.0515  0.0261  -0.0592 113 GLU A CA  
2822 C C   . GLU B 116 ? 0.3526 0.2668 0.2008 0.0491  0.0188  -0.0622 113 GLU A C   
2823 O O   . GLU B 116 ? 0.3524 0.2815 0.2225 0.0431  0.0145  -0.0596 113 GLU A O   
2824 C CB  . GLU B 116 ? 0.4367 0.3507 0.2687 0.0552  0.0432  -0.0554 113 GLU A CB  
2825 C CG  . GLU B 116 ? 0.4797 0.3946 0.3034 0.0541  0.0538  -0.0489 113 GLU A CG  
2826 C CD  . GLU B 116 ? 0.5277 0.4549 0.3603 0.0572  0.0715  -0.0442 113 GLU A CD  
2827 O OE1 . GLU B 116 ? 0.4615 0.4039 0.3164 0.0583  0.0753  -0.0441 113 GLU A OE1 
2828 O OE2 . GLU B 116 ? 0.6061 0.5291 0.4246 0.0580  0.0823  -0.0392 113 GLU A OE2 
2829 N N   . SER B 117 ? 0.3813 0.2835 0.2198 0.0542  0.0178  -0.0676 114 SER A N   
2830 C CA  . SER B 117 ? 0.3553 0.2618 0.2106 0.0519  0.0115  -0.0698 114 SER A CA  
2831 C C   . SER B 117 ? 0.3351 0.2406 0.1956 0.0450  -0.0043 -0.0717 114 SER A C   
2832 O O   . SER B 117 ? 0.3050 0.2234 0.1877 0.0397  -0.0085 -0.0697 114 SER A O   
2833 C CB  . SER B 117 ? 0.3798 0.2720 0.2233 0.0594  0.0148  -0.0746 114 SER A CB  
2834 O OG  . SER B 117 ? 0.4270 0.2942 0.2403 0.0635  0.0088  -0.0809 114 SER A OG  
2835 N N   . LYS B 118 ? 0.3631 0.2544 0.2035 0.0453  -0.0128 -0.0748 115 LYS A N   
2836 C CA  . LYS B 118 ? 0.3522 0.2451 0.1990 0.0390  -0.0280 -0.0761 115 LYS A CA  
2837 C C   . LYS B 118 ? 0.3128 0.2274 0.1824 0.0340  -0.0282 -0.0703 115 LYS A C   
2838 O O   . LYS B 118 ? 0.2872 0.2135 0.1769 0.0285  -0.0346 -0.0691 115 LYS A O   
2839 C CB  . LYS B 118 ? 0.4048 0.2799 0.2255 0.0410  -0.0375 -0.0800 115 LYS A CB  
2840 C CG  . LYS B 118 ? 0.4422 0.3188 0.2709 0.0346  -0.0549 -0.0820 115 LYS A CG  
2841 C CD  . LYS B 118 ? 0.5238 0.3777 0.3245 0.0366  -0.0671 -0.0880 115 LYS A CD  
2842 C CE  . LYS B 118 ? 0.5106 0.3689 0.3250 0.0285  -0.0848 -0.0896 115 LYS A CE  
2843 N NZ  . LYS B 118 ? 0.5357 0.3751 0.3241 0.0304  -0.0980 -0.0945 115 LYS A NZ  
2844 N N   . VAL B 119 ? 0.3007 0.2190 0.1657 0.0360  -0.0203 -0.0665 116 VAL A N   
2845 C CA  . VAL B 119 ? 0.2852 0.2202 0.1679 0.0324  -0.0198 -0.0615 116 VAL A CA  
2846 C C   . VAL B 119 ? 0.2682 0.2191 0.1751 0.0293  -0.0147 -0.0589 116 VAL A C   
2847 O O   . VAL B 119 ? 0.2399 0.2034 0.1634 0.0256  -0.0193 -0.0569 116 VAL A O   
2848 C CB  . VAL B 119 ? 0.2976 0.2289 0.1679 0.0346  -0.0127 -0.0579 116 VAL A CB  
2849 C CG1 . VAL B 119 ? 0.2748 0.2198 0.1611 0.0312  -0.0104 -0.0530 116 VAL A CG1 
2850 C CG2 . VAL B 119 ? 0.3240 0.2393 0.1699 0.0379  -0.0202 -0.0599 116 VAL A CG2 
2851 N N   . PHE B 120 ? 0.2744 0.2254 0.1826 0.0316  -0.0051 -0.0586 117 PHE A N   
2852 C CA  . PHE B 120 ? 0.2510 0.2164 0.1808 0.0294  -0.0012 -0.0561 117 PHE A CA  
2853 C C   . PHE B 120 ? 0.2444 0.2130 0.1859 0.0260  -0.0101 -0.0574 117 PHE A C   
2854 O O   . PHE B 120 ? 0.2330 0.2150 0.1915 0.0225  -0.0112 -0.0542 117 PHE A O   
2855 C CB  . PHE B 120 ? 0.2818 0.2449 0.2098 0.0343  0.0085  -0.0565 117 PHE A CB  
2856 C CG  . PHE B 120 ? 0.2820 0.2600 0.2313 0.0333  0.0125  -0.0535 117 PHE A CG  
2857 C CD1 . PHE B 120 ? 0.2740 0.2528 0.2330 0.0325  0.0074  -0.0545 117 PHE A CD1 
2858 C CD2 . PHE B 120 ? 0.3136 0.3046 0.2735 0.0324  0.0204  -0.0490 117 PHE A CD2 
2859 C CE1 . PHE B 120 ? 0.2812 0.2725 0.2577 0.0323  0.0102  -0.0514 117 PHE A CE1 
2860 C CE2 . PHE B 120 ? 0.3246 0.3292 0.3036 0.0318  0.0225  -0.0464 117 PHE A CE2 
2861 C CZ  . PHE B 120 ? 0.2945 0.2989 0.2808 0.0323  0.0172  -0.0476 117 PHE A CZ  
2862 N N   . TYR B 121 ? 0.2460 0.2008 0.1768 0.0266  -0.0167 -0.0618 118 TYR A N   
2863 C CA  . TYR B 121 ? 0.2349 0.1913 0.1771 0.0220  -0.0249 -0.0623 118 TYR A CA  
2864 C C   . TYR B 121 ? 0.2198 0.1859 0.1712 0.0168  -0.0337 -0.0606 118 TYR A C   
2865 O O   . TYR B 121 ? 0.1985 0.1749 0.1666 0.0122  -0.0365 -0.0579 118 TYR A O   
2866 C CB  . TYR B 121 ? 0.2572 0.1934 0.1844 0.0235  -0.0298 -0.0676 118 TYR A CB  
2867 C CG  . TYR B 121 ? 0.2690 0.1956 0.1880 0.0305  -0.0208 -0.0695 118 TYR A CG  
2868 C CD1 . TYR B 121 ? 0.2581 0.1960 0.1933 0.0317  -0.0137 -0.0659 118 TYR A CD1 
2869 C CD2 . TYR B 121 ? 0.2954 0.2013 0.1895 0.0368  -0.0197 -0.0748 118 TYR A CD2 
2870 C CE1 . TYR B 121 ? 0.2632 0.1937 0.1925 0.0394  -0.0060 -0.0674 118 TYR A CE1 
2871 C CE2 . TYR B 121 ? 0.3111 0.2085 0.1972 0.0451  -0.0104 -0.0766 118 TYR A CE2 
2872 C CZ  . TYR B 121 ? 0.3022 0.2132 0.2076 0.0465  -0.0036 -0.0727 118 TYR A CZ  
2873 O OH  . TYR B 121 ? 0.3127 0.2176 0.2125 0.0559  0.0054  -0.0740 118 TYR A OH  
2874 N N   . LEU B 122 ? 0.2399 0.2022 0.1800 0.0181  -0.0379 -0.0618 119 LEU A N   
2875 C CA  . LEU B 122 ? 0.2372 0.2110 0.1874 0.0150  -0.0459 -0.0598 119 LEU A CA  
2876 C C   . LEU B 122 ? 0.2133 0.2040 0.1785 0.0150  -0.0399 -0.0550 119 LEU A C   
2877 O O   . LEU B 122 ? 0.1900 0.1945 0.1713 0.0121  -0.0433 -0.0523 119 LEU A O   
2878 C CB  . LEU B 122 ? 0.2620 0.2265 0.1951 0.0178  -0.0525 -0.0622 119 LEU A CB  
2879 C CG  . LEU B 122 ? 0.2938 0.2428 0.2137 0.0164  -0.0632 -0.0672 119 LEU A CG  
2880 C CD1 . LEU B 122 ? 0.3150 0.2530 0.2138 0.0208  -0.0686 -0.0692 119 LEU A CD1 
2881 C CD2 . LEU B 122 ? 0.2854 0.2450 0.2241 0.0093  -0.0741 -0.0664 119 LEU A CD2 
2882 N N   . LYS B 123 ? 0.1968 0.1861 0.1565 0.0180  -0.0308 -0.0538 120 LYS A N   
2883 C CA  . LYS B 123 ? 0.1876 0.1896 0.1594 0.0175  -0.0257 -0.0499 120 LYS A CA  
2884 C C   . LYS B 123 ? 0.1760 0.1878 0.1641 0.0145  -0.0243 -0.0480 120 LYS A C   
2885 O O   . LYS B 123 ? 0.1831 0.2066 0.1829 0.0132  -0.0252 -0.0452 120 LYS A O   
2886 C CB  . LYS B 123 ? 0.1930 0.1909 0.1575 0.0193  -0.0169 -0.0488 120 LYS A CB  
2887 C CG  . LYS B 123 ? 0.1914 0.1990 0.1659 0.0180  -0.0129 -0.0455 120 LYS A CG  
2888 C CD  . LYS B 123 ? 0.2001 0.2050 0.1705 0.0178  -0.0050 -0.0439 120 LYS A CD  
2889 C CE  . LYS B 123 ? 0.1923 0.2079 0.1766 0.0152  -0.0022 -0.0413 120 LYS A CE  
2890 N NZ  . LYS B 123 ? 0.1765 0.1995 0.1731 0.0148  -0.0024 -0.0413 120 LYS A NZ  
2891 N N   . MET B 124 ? 0.2027 0.2086 0.1902 0.0143  -0.0221 -0.0493 121 MET A N   
2892 C CA  . MET B 124 ? 0.1980 0.2104 0.1987 0.0120  -0.0212 -0.0471 121 MET A CA  
2893 C C   . MET B 124 ? 0.1809 0.1990 0.1914 0.0076  -0.0280 -0.0456 121 MET A C   
2894 O O   . MET B 124 ? 0.1621 0.1913 0.1848 0.0056  -0.0267 -0.0417 121 MET A O   
2895 C CB  . MET B 124 ? 0.2098 0.2122 0.2059 0.0142  -0.0181 -0.0490 121 MET A CB  
2896 C CG  . MET B 124 ? 0.2419 0.2492 0.2497 0.0133  -0.0163 -0.0461 121 MET A CG  
2897 S SD  . MET B 124 ? 0.2804 0.2744 0.2808 0.0188  -0.0122 -0.0488 121 MET A SD  
2898 C CE  . MET B 124 ? 0.2432 0.2484 0.2593 0.0186  -0.0100 -0.0437 121 MET A CE  
2899 N N   . LYS B 125 ? 0.1919 0.2032 0.1971 0.0057  -0.0355 -0.0483 122 LYS A N   
2900 C CA  . LYS B 125 ? 0.1948 0.2145 0.2121 0.0003  -0.0426 -0.0462 122 LYS A CA  
2901 C C   . LYS B 125 ? 0.1853 0.2230 0.2138 0.0012  -0.0415 -0.0424 122 LYS A C   
2902 O O   . LYS B 125 ? 0.1784 0.2288 0.2215 -0.0019 -0.0409 -0.0381 122 LYS A O   
2903 C CB  . LYS B 125 ? 0.2049 0.2141 0.2134 -0.0016 -0.0522 -0.0502 122 LYS A CB  
2904 C CG  . LYS B 125 ? 0.1950 0.2135 0.2183 -0.0088 -0.0613 -0.0480 122 LYS A CG  
2905 C CD  . LYS B 125 ? 0.2219 0.2266 0.2345 -0.0115 -0.0727 -0.0528 122 LYS A CD  
2906 C CE  . LYS B 125 ? 0.2297 0.2471 0.2607 -0.0197 -0.0821 -0.0498 122 LYS A CE  
2907 N NZ  . LYS B 125 ? 0.2570 0.2614 0.2789 -0.0237 -0.0957 -0.0545 122 LYS A NZ  
2908 N N   . GLY B 126 ? 0.1840 0.2210 0.2038 0.0061  -0.0404 -0.0438 123 GLY A N   
2909 C CA  . GLY B 126 ? 0.1845 0.2341 0.2101 0.0094  -0.0388 -0.0411 123 GLY A CA  
2910 C C   . GLY B 126 ? 0.1570 0.2135 0.1890 0.0098  -0.0314 -0.0380 123 GLY A C   
2911 O O   . GLY B 126 ? 0.1767 0.2463 0.2194 0.0101  -0.0306 -0.0346 123 GLY A O   
2912 N N   . ASP B 127 ? 0.1509 0.1995 0.1772 0.0100  -0.0266 -0.0388 124 ASP A N   
2913 C CA  . ASP B 127 ? 0.1681 0.2218 0.1990 0.0103  -0.0214 -0.0363 124 ASP A CA  
2914 C C   . ASP B 127 ? 0.1845 0.2461 0.2270 0.0071  -0.0214 -0.0326 124 ASP A C   
2915 O O   . ASP B 127 ? 0.1547 0.2249 0.2014 0.0083  -0.0187 -0.0295 124 ASP A O   
2916 C CB  . ASP B 127 ? 0.1788 0.2251 0.2044 0.0108  -0.0174 -0.0374 124 ASP A CB  
2917 C CG  . ASP B 127 ? 0.1836 0.2236 0.1991 0.0129  -0.0152 -0.0393 124 ASP A CG  
2918 O OD1 . ASP B 127 ? 0.2090 0.2495 0.2203 0.0147  -0.0162 -0.0392 124 ASP A OD1 
2919 O OD2 . ASP B 127 ? 0.1805 0.2148 0.1924 0.0131  -0.0121 -0.0404 124 ASP A OD2 
2920 N N   . TYR B 128 ? 0.1905 0.2471 0.2358 0.0031  -0.0242 -0.0328 125 TYR A N   
2921 C CA  . TYR B 128 ? 0.1713 0.2320 0.2259 -0.0008 -0.0238 -0.0285 125 TYR A CA  
2922 C C   . TYR B 128 ? 0.1829 0.2572 0.2489 -0.0037 -0.0257 -0.0248 125 TYR A C   
2923 O O   . TYR B 128 ? 0.1699 0.2525 0.2435 -0.0053 -0.0223 -0.0196 125 TYR A O   
2924 C CB  . TYR B 128 ? 0.1844 0.2316 0.2361 -0.0035 -0.0259 -0.0299 125 TYR A CB  
2925 C CG  . TYR B 128 ? 0.1709 0.2128 0.2174 0.0007  -0.0212 -0.0305 125 TYR A CG  
2926 C CD1 . TYR B 128 ? 0.1714 0.2078 0.2095 0.0048  -0.0192 -0.0345 125 TYR A CD1 
2927 C CD2 . TYR B 128 ? 0.1828 0.2265 0.2334 0.0007  -0.0187 -0.0264 125 TYR A CD2 
2928 C CE1 . TYR B 128 ? 0.1899 0.2255 0.2270 0.0084  -0.0149 -0.0344 125 TYR A CE1 
2929 C CE2 . TYR B 128 ? 0.1725 0.2142 0.2206 0.0049  -0.0157 -0.0267 125 TYR A CE2 
2930 C CZ  . TYR B 128 ? 0.1759 0.2152 0.2189 0.0085  -0.0138 -0.0306 125 TYR A CZ  
2931 O OH  . TYR B 128 ? 0.2009 0.2414 0.2448 0.0121  -0.0109 -0.0305 125 TYR A OH  
2932 N N   . TYR B 129 ? 0.1561 0.2336 0.2238 -0.0041 -0.0308 -0.0267 126 TYR A N   
2933 C CA  . TYR B 129 ? 0.1621 0.2571 0.2431 -0.0049 -0.0318 -0.0229 126 TYR A CA  
2934 C C   . TYR B 129 ? 0.1382 0.2428 0.2179 0.0023  -0.0256 -0.0213 126 TYR A C   
2935 O O   . TYR B 129 ? 0.1318 0.2513 0.2220 0.0028  -0.0222 -0.0164 126 TYR A O   
2936 C CB  . TYR B 129 ? 0.1776 0.2748 0.2613 -0.0061 -0.0401 -0.0253 126 TYR A CB  
2937 C CG  . TYR B 129 ? 0.1919 0.2854 0.2827 -0.0151 -0.0475 -0.0249 126 TYR A CG  
2938 C CD1 . TYR B 129 ? 0.1955 0.3032 0.3047 -0.0221 -0.0477 -0.0186 126 TYR A CD1 
2939 C CD2 . TYR B 129 ? 0.2114 0.2862 0.2897 -0.0170 -0.0545 -0.0306 126 TYR A CD2 
2940 C CE1 . TYR B 129 ? 0.2163 0.3194 0.3325 -0.0320 -0.0559 -0.0180 126 TYR A CE1 
2941 C CE2 . TYR B 129 ? 0.2433 0.3113 0.3257 -0.0256 -0.0628 -0.0309 126 TYR A CE2 
2942 C CZ  . TYR B 129 ? 0.2444 0.3261 0.3463 -0.0338 -0.0640 -0.0246 126 TYR A CZ  
2943 O OH  . TYR B 129 ? 0.2342 0.3096 0.3419 -0.0438 -0.0730 -0.0243 126 TYR A OH  
2944 N N   . ARG B 130 ? 0.1278 0.2232 0.1940 0.0079  -0.0239 -0.0251 127 ARG A N   
2945 C CA  . ARG B 130 ? 0.1215 0.2208 0.1829 0.0144  -0.0191 -0.0245 127 ARG A CA  
2946 C C   . ARG B 130 ? 0.1355 0.2376 0.1980 0.0139  -0.0135 -0.0208 127 ARG A C   
2947 O O   . ARG B 130 ? 0.1404 0.2515 0.2040 0.0183  -0.0094 -0.0182 127 ARG A O   
2948 C CB  . ARG B 130 ? 0.1355 0.2219 0.1820 0.0183  -0.0192 -0.0288 127 ARG A CB  
2949 C CG  . ARG B 130 ? 0.1273 0.2132 0.1662 0.0243  -0.0155 -0.0288 127 ARG A CG  
2950 C CD  . ARG B 130 ? 0.1386 0.2116 0.1638 0.0272  -0.0169 -0.0325 127 ARG A CD  
2951 N NE  . ARG B 130 ? 0.1445 0.2069 0.1647 0.0228  -0.0168 -0.0343 127 ARG A NE  
2952 C CZ  . ARG B 130 ? 0.1463 0.2050 0.1644 0.0207  -0.0145 -0.0342 127 ARG A CZ  
2953 N NH1 . ARG B 130 ? 0.1332 0.1942 0.1499 0.0226  -0.0129 -0.0329 127 ARG A NH1 
2954 N NH2 . ARG B 130 ? 0.1494 0.2022 0.1663 0.0174  -0.0140 -0.0353 127 ARG A NH2 
2955 N N   . TYR B 131 ? 0.1478 0.2416 0.2085 0.0098  -0.0134 -0.0208 128 TYR A N   
2956 C CA  . TYR B 131 ? 0.1441 0.2393 0.2048 0.0094  -0.0093 -0.0168 128 TYR A CA  
2957 C C   . TYR B 131 ? 0.1417 0.2489 0.2136 0.0065  -0.0069 -0.0107 128 TYR A C   
2958 O O   . TYR B 131 ? 0.1923 0.3054 0.2624 0.0095  -0.0018 -0.0069 128 TYR A O   
2959 C CB  . TYR B 131 ? 0.1555 0.2395 0.2126 0.0069  -0.0104 -0.0178 128 TYR A CB  
2960 C CG  . TYR B 131 ? 0.1482 0.2234 0.1971 0.0091  -0.0116 -0.0228 128 TYR A CG  
2961 C CD1 . TYR B 131 ? 0.1454 0.2199 0.1871 0.0129  -0.0110 -0.0251 128 TYR A CD1 
2962 C CD2 . TYR B 131 ? 0.1371 0.2040 0.1853 0.0076  -0.0127 -0.0246 128 TYR A CD2 
2963 C CE1 . TYR B 131 ? 0.1393 0.2063 0.1750 0.0133  -0.0116 -0.0285 128 TYR A CE1 
2964 C CE2 . TYR B 131 ? 0.1286 0.1902 0.1715 0.0093  -0.0123 -0.0280 128 TYR A CE2 
2965 C CZ  . TYR B 131 ? 0.1385 0.2006 0.1758 0.0113  -0.0117 -0.0295 128 TYR A CZ  
2966 O OH  . TYR B 131 ? 0.1672 0.2245 0.2005 0.0116  -0.0108 -0.0318 128 TYR A OH  
2967 N N   . LEU B 132 ? 0.1329 0.2438 0.2157 0.0006  -0.0105 -0.0094 129 LEU A N   
2968 C CA  . LEU B 132 ? 0.1444 0.2702 0.2418 -0.0035 -0.0085 -0.0029 129 LEU A CA  
2969 C C   . LEU B 132 ? 0.1310 0.2736 0.2328 0.0032  -0.0041 -0.0010 129 LEU A C   
2970 O O   . LEU B 132 ? 0.1394 0.2935 0.2465 0.0041  0.0025  0.0051  129 LEU A O   
2971 C CB  . LEU B 132 ? 0.1510 0.2770 0.2598 -0.0121 -0.0153 -0.0026 129 LEU A CB  
2972 C CG  . LEU B 132 ? 0.1823 0.2909 0.2869 -0.0186 -0.0190 -0.0032 129 LEU A CG  
2973 C CD1 . LEU B 132 ? 0.1966 0.3020 0.3092 -0.0269 -0.0275 -0.0044 129 LEU A CD1 
2974 C CD2 . LEU B 132 ? 0.2117 0.3194 0.3179 -0.0219 -0.0139 0.0037  129 LEU A CD2 
2975 N N   . ALA B 133 ? 0.1343 0.2769 0.2322 0.0089  -0.0071 -0.0060 130 ALA A N   
2976 C CA  . ALA B 133 ? 0.1423 0.2989 0.2433 0.0172  -0.0036 -0.0050 130 ALA A CA  
2977 C C   . ALA B 133 ? 0.1458 0.2999 0.2336 0.0252  0.0040  -0.0044 130 ALA A C   
2978 O O   . ALA B 133 ? 0.1385 0.3064 0.2302 0.0318  0.0101  -0.0009 130 ALA A O   
2979 C CB  . ALA B 133 ? 0.1445 0.2963 0.2401 0.0220  -0.0095 -0.0107 130 ALA A CB  
2980 N N   . GLU B 134 ? 0.1386 0.2758 0.2114 0.0248  0.0036  -0.0074 131 GLU A N   
2981 C CA  . GLU B 134 ? 0.1687 0.3008 0.2272 0.0310  0.0088  -0.0071 131 GLU A CA  
2982 C C   . GLU B 134 ? 0.1898 0.3326 0.2524 0.0310  0.0163  0.0002  131 GLU A C   
2983 O O   . GLU B 134 ? 0.1946 0.3368 0.2453 0.0387  0.0216  0.0007  131 GLU A O   
2984 C CB  . GLU B 134 ? 0.1755 0.2899 0.2205 0.0290  0.0056  -0.0108 131 GLU A CB  
2985 C CG  . GLU B 134 ? 0.1718 0.2744 0.2096 0.0296  0.0002  -0.0173 131 GLU A CG  
2986 C CD  . GLU B 134 ? 0.1806 0.2705 0.2112 0.0261  -0.0029 -0.0198 131 GLU A CD  
2987 O OE1 . GLU B 134 ? 0.1611 0.2502 0.1924 0.0234  -0.0021 -0.0171 131 GLU A OE1 
2988 O OE2 . GLU B 134 ? 0.2031 0.2841 0.2265 0.0270  -0.0056 -0.0241 131 GLU A OE2 
2989 N N   . VAL B 135 ? 0.1790 0.3292 0.2558 0.0225  0.0167  0.0058  132 VAL A N   
2990 C CA  . VAL B 135 ? 0.2153 0.3744 0.2955 0.0211  0.0244  0.0141  132 VAL A CA  
2991 C C   . VAL B 135 ? 0.2205 0.4022 0.3227 0.0178  0.0284  0.0208  132 VAL A C   
2992 O O   . VAL B 135 ? 0.2316 0.4239 0.3368 0.0183  0.0370  0.0284  132 VAL A O   
2993 C CB  . VAL B 135 ? 0.2479 0.3940 0.3238 0.0139  0.0224  0.0165  132 VAL A CB  
2994 C CG1 . VAL B 135 ? 0.2410 0.3691 0.2987 0.0178  0.0181  0.0101  132 VAL A CG1 
2995 C CG2 . VAL B 135 ? 0.3006 0.4453 0.3910 0.0032  0.0165  0.0176  132 VAL A CG2 
2996 N N   . ALA B 136 ? 0.2068 0.3961 0.3239 0.0141  0.0221  0.0186  133 ALA A N   
2997 C CA  . ALA B 136 ? 0.2303 0.4421 0.3722 0.0082  0.0234  0.0255  133 ALA A CA  
2998 C C   . ALA B 136 ? 0.2644 0.4980 0.4127 0.0187  0.0324  0.0291  133 ALA A C   
2999 O O   . ALA B 136 ? 0.2903 0.5198 0.4261 0.0303  0.0328  0.0234  133 ALA A O   
3000 C CB  . ALA B 136 ? 0.2419 0.4531 0.3951 0.0019  0.0119  0.0210  133 ALA A CB  
3001 N N   . ALA B 137 ? 0.3106 0.5668 0.4785 0.0146  0.0397  0.0389  134 ALA A N   
3002 C CA  . ALA B 137 ? 0.3963 0.6778 0.5746 0.0246  0.0497  0.0438  134 ALA A CA  
3003 C C   . ALA B 137 ? 0.4870 0.7968 0.6983 0.0142  0.0517  0.0539  134 ALA A C   
3004 O O   . ALA B 137 ? 0.6167 0.9303 0.8331 0.0058  0.0584  0.0626  134 ALA A O   
3005 C CB  . ALA B 137 ? 0.4088 0.6853 0.5668 0.0341  0.0624  0.0467  134 ALA A CB  
3006 N N   . GLY B 138 ? 0.6144 0.9415 0.8473 0.0129  0.0441  0.0527  135 GLY A N   
3007 C CA  . GLY B 138 ? 0.6210 0.9815 0.8889 0.0052  0.0465  0.0628  135 GLY A CA  
3008 C C   . GLY B 138 ? 0.6903 1.0592 0.9781 -0.0015 0.0312  0.0593  135 GLY A C   
3009 O O   . GLY B 138 ? 0.7448 1.1031 1.0209 0.0074  0.0232  0.0501  135 GLY A O   
3010 N N   . ASP B 139 ? 0.7250 1.1104 1.0410 -0.0176 0.0265  0.0668  136 ASP A N   
3011 C CA  . ASP B 139 ? 0.6813 1.0728 1.0157 -0.0263 0.0097  0.0637  136 ASP A CA  
3012 C C   . ASP B 139 ? 0.5321 0.8859 0.8403 -0.0293 -0.0037 0.0520  136 ASP A C   
3013 O O   . ASP B 139 ? 0.5478 0.8978 0.8527 -0.0243 -0.0147 0.0445  136 ASP A O   
3014 C CB  . ASP B 139 ? 0.6303 1.0484 1.0011 -0.0435 0.0074  0.0747  136 ASP A CB  
3015 N N   . ASP B 140 ? 0.4889 0.8146 0.7757 -0.0348 -0.0016 0.0504  137 ASP A N   
3016 C CA  . ASP B 140 ? 0.4016 0.6936 0.6658 -0.0378 -0.0129 0.0403  137 ASP A CA  
3017 C C   . ASP B 140 ? 0.3375 0.6134 0.5762 -0.0226 -0.0127 0.0306  137 ASP A C   
3018 O O   . ASP B 140 ? 0.2472 0.5005 0.4708 -0.0243 -0.0223 0.0227  137 ASP A O   
3019 C CB  . ASP B 140 ? 0.4424 0.7113 0.6956 -0.0487 -0.0123 0.0421  137 ASP A CB  
3020 C CG  . ASP B 140 ? 0.5187 0.7718 0.7483 -0.0406 -0.0012 0.0417  137 ASP A CG  
3021 O OD1 . ASP B 140 ? 0.6077 0.8751 0.8356 -0.0296 0.0100  0.0447  137 ASP A OD1 
3022 O OD2 . ASP B 140 ? 0.4934 0.7203 0.7062 -0.0449 -0.0042 0.0387  137 ASP A OD2 
3023 N N   . LYS B 141 ? 0.3009 0.5855 0.5326 -0.0085 -0.0020 0.0312  138 LYS A N   
3024 C CA  . LYS B 141 ? 0.2977 0.5642 0.5042 0.0044  -0.0021 0.0224  138 LYS A CA  
3025 C C   . LYS B 141 ? 0.2445 0.5095 0.4516 0.0078  -0.0139 0.0160  138 LYS A C   
3026 O O   . LYS B 141 ? 0.2097 0.4509 0.3962 0.0100  -0.0197 0.0081  138 LYS A O   
3027 C CB  . LYS B 141 ? 0.3638 0.6400 0.5635 0.0193  0.0101  0.0241  138 LYS A CB  
3028 C CG  . LYS B 141 ? 0.4322 0.6851 0.6034 0.0308  0.0092  0.0151  138 LYS A CG  
3029 C CD  . LYS B 141 ? 0.5154 0.7677 0.6717 0.0438  0.0208  0.0157  138 LYS A CD  
3030 C CE  . LYS B 141 ? 0.5043 0.7275 0.6309 0.0488  0.0196  0.0081  138 LYS A CE  
3031 N NZ  . LYS B 141 ? 0.4706 0.6886 0.5853 0.0619  0.0185  0.0028  138 LYS A NZ  
3032 N N   . LYS B 142 ? 0.2496 0.5416 0.4808 0.0090  -0.0167 0.0201  139 LYS A N   
3033 C CA  . LYS B 142 ? 0.2879 0.5814 0.5220 0.0123  -0.0291 0.0152  139 LYS A CA  
3034 C C   . LYS B 142 ? 0.2182 0.4889 0.4428 0.0012  -0.0423 0.0095  139 LYS A C   
3035 O O   . LYS B 142 ? 0.2079 0.4596 0.4131 0.0066  -0.0486 0.0021  139 LYS A O   
3036 C CB  . LYS B 142 ? 0.3387 0.6681 0.6057 0.0123  -0.0318 0.0219  139 LYS A CB  
3037 C CG  . LYS B 142 ? 0.4668 0.7995 0.7349 0.0201  -0.0438 0.0173  139 LYS A CG  
3038 C CD  . LYS B 142 ? 0.5263 0.8949 0.8298 0.0180  -0.0508 0.0234  139 LYS A CD  
3039 C CE  . LYS B 142 ? 0.6058 0.9740 0.9048 0.0290  -0.0623 0.0184  139 LYS A CE  
3040 N NZ  . LYS B 142 ? 0.6628 0.9976 0.9358 0.0249  -0.0751 0.0095  139 LYS A NZ  
3041 N N   . GLY B 143 ? 0.2165 0.4873 0.4527 -0.0138 -0.0456 0.0130  140 GLY A N   
3042 C CA  . GLY B 143 ? 0.2146 0.4614 0.4402 -0.0243 -0.0572 0.0077  140 GLY A CA  
3043 C C   . GLY B 143 ? 0.2006 0.4154 0.3948 -0.0198 -0.0545 0.0003  140 GLY A C   
3044 O O   . GLY B 143 ? 0.1979 0.3933 0.3759 -0.0192 -0.0632 -0.0068 140 GLY A O   
3045 N N   . ILE B 144 ? 0.1692 0.3797 0.3553 -0.0167 -0.0424 0.0025  141 ILE A N   
3046 C CA  . ILE B 144 ? 0.1708 0.3552 0.3316 -0.0133 -0.0393 -0.0030 141 ILE A CA  
3047 C C   . ILE B 144 ? 0.1680 0.3430 0.3114 -0.0020 -0.0405 -0.0096 141 ILE A C   
3048 O O   . ILE B 144 ? 0.1777 0.3312 0.3032 -0.0019 -0.0444 -0.0156 141 ILE A O   
3049 C CB  . ILE B 144 ? 0.1575 0.3423 0.3158 -0.0127 -0.0275 0.0018  141 ILE A CB  
3050 C CG1 . ILE B 144 ? 0.1766 0.3597 0.3451 -0.0256 -0.0285 0.0070  141 ILE A CG1 
3051 C CG2 . ILE B 144 ? 0.1393 0.3039 0.2743 -0.0062 -0.0234 -0.0033 141 ILE A CG2 
3052 C CD1 . ILE B 144 ? 0.1826 0.3708 0.3527 -0.0261 -0.0173 0.0143  141 ILE A CD1 
3053 N N   . VAL B 145 ? 0.1691 0.3594 0.3170 0.0078  -0.0360 -0.0077 142 VAL A N   
3054 C CA  . VAL B 145 ? 0.1727 0.3533 0.3040 0.0187  -0.0368 -0.0129 142 VAL A CA  
3055 C C   . VAL B 145 ? 0.1673 0.3405 0.2948 0.0175  -0.0488 -0.0172 142 VAL A C   
3056 O O   . VAL B 145 ? 0.1694 0.3223 0.2763 0.0209  -0.0506 -0.0225 142 VAL A O   
3057 C CB  . VAL B 145 ? 0.1910 0.3890 0.3280 0.0303  -0.0300 -0.0098 142 VAL A CB  
3058 C CG1 . VAL B 145 ? 0.2115 0.3991 0.3325 0.0418  -0.0328 -0.0146 142 VAL A CG1 
3059 C CG2 . VAL B 145 ? 0.1687 0.3696 0.3030 0.0330  -0.0178 -0.0063 142 VAL A CG2 
3060 N N   A ASP B 146 ? 0.1583 0.3484 0.3052 0.0129  -0.0571 -0.0147 143 ASP A N   
3061 N N   B ASP B 146 ? 0.1779 0.3681 0.3250 0.0127  -0.0570 -0.0146 143 ASP A N   
3062 C CA  A ASP B 146 ? 0.1624 0.3457 0.3054 0.0114  -0.0705 -0.0187 143 ASP A CA  
3063 C CA  B ASP B 146 ? 0.1972 0.3809 0.3408 0.0110  -0.0704 -0.0185 143 ASP A CA  
3064 C C   A ASP B 146 ? 0.1761 0.3319 0.2998 0.0043  -0.0749 -0.0242 143 ASP A C   
3065 C C   B ASP B 146 ? 0.1958 0.3520 0.3199 0.0042  -0.0751 -0.0241 143 ASP A C   
3066 O O   A ASP B 146 ? 0.1874 0.3258 0.2916 0.0084  -0.0801 -0.0294 143 ASP A O   
3067 O O   B ASP B 146 ? 0.2070 0.3465 0.3123 0.0083  -0.0806 -0.0293 143 ASP A O   
3068 C CB  A ASP B 146 ? 0.1564 0.3645 0.3266 0.0059  -0.0797 -0.0144 143 ASP A CB  
3069 C CB  B ASP B 146 ? 0.2186 0.4262 0.3896 0.0042  -0.0793 -0.0141 143 ASP A CB  
3070 C CG  A ASP B 146 ? 0.1440 0.3810 0.3335 0.0156  -0.0771 -0.0095 143 ASP A CG  
3071 C CG  B ASP B 146 ? 0.2551 0.4573 0.4222 0.0035  -0.0951 -0.0182 143 ASP A CG  
3072 O OD1 A ASP B 146 ? 0.1422 0.3764 0.3200 0.0283  -0.0694 -0.0104 143 ASP A OD1 
3073 O OD1 B ASP B 146 ? 0.2799 0.4757 0.4330 0.0144  -0.0975 -0.0213 143 ASP A OD1 
3074 O OD2 A ASP B 146 ? 0.1324 0.3956 0.3499 0.0104  -0.0822 -0.0042 143 ASP A OD2 
3075 O OD2 B ASP B 146 ? 0.2961 0.4986 0.4726 -0.0081 -0.1055 -0.0182 143 ASP A OD2 
3076 N N   . GLN B 147 ? 0.1738 0.3244 0.3008 -0.0049 -0.0716 -0.0228 144 GLN A N   
3077 C CA  . GLN B 147 ? 0.1967 0.3214 0.3054 -0.0097 -0.0741 -0.0279 144 GLN A CA  
3078 C C   . GLN B 147 ? 0.1897 0.2966 0.2753 -0.0018 -0.0667 -0.0319 144 GLN A C   
3079 O O   . GLN B 147 ? 0.2061 0.2938 0.2733 -0.0007 -0.0706 -0.0371 144 GLN A O   
3080 C CB  . GLN B 147 ? 0.2049 0.3268 0.3212 -0.0195 -0.0713 -0.0250 144 GLN A CB  
3081 C CG  . GLN B 147 ? 0.2268 0.3591 0.3630 -0.0310 -0.0803 -0.0215 144 GLN A CG  
3082 C CD  . GLN B 147 ? 0.2936 0.4098 0.4200 -0.0356 -0.0946 -0.0274 144 GLN A CD  
3083 O OE1 . GLN B 147 ? 0.3030 0.3931 0.4070 -0.0349 -0.0961 -0.0335 144 GLN A OE1 
3084 N NE2 . GLN B 147 ? 0.3571 0.4890 0.4987 -0.0387 -0.1054 -0.0260 144 GLN A NE2 
3085 N N   . SER B 148 ? 0.1709 0.2840 0.2572 0.0034  -0.0564 -0.0294 145 SER A N   
3086 C CA  . SER B 148 ? 0.1699 0.2681 0.2374 0.0094  -0.0501 -0.0324 145 SER A CA  
3087 C C   . SER B 148 ? 0.1875 0.2776 0.2411 0.0161  -0.0544 -0.0358 145 SER A C   
3088 O O   . SER B 148 ? 0.1695 0.2414 0.2051 0.0169  -0.0545 -0.0396 145 SER A O   
3089 C CB  . SER B 148 ? 0.1524 0.2587 0.2229 0.0137  -0.0405 -0.0292 145 SER A CB  
3090 O OG  . SER B 148 ? 0.1504 0.2421 0.2042 0.0175  -0.0358 -0.0320 145 SER A OG  
3091 N N   . GLN B 149 ? 0.1797 0.2838 0.2419 0.0211  -0.0580 -0.0339 146 GLN A N   
3092 C CA  . GLN B 149 ? 0.2069 0.3035 0.2557 0.0288  -0.0621 -0.0361 146 GLN A CA  
3093 C C   . GLN B 149 ? 0.2124 0.2952 0.2495 0.0259  -0.0720 -0.0399 146 GLN A C   
3094 O O   . GLN B 149 ? 0.2151 0.2803 0.2313 0.0300  -0.0719 -0.0426 146 GLN A O   
3095 C CB  . GLN B 149 ? 0.2169 0.3332 0.2795 0.0360  -0.0640 -0.0329 146 GLN A CB  
3096 C CG  . GLN B 149 ? 0.2659 0.3732 0.3138 0.0455  -0.0690 -0.0347 146 GLN A CG  
3097 C CD  . GLN B 149 ? 0.3118 0.4345 0.3687 0.0562  -0.0681 -0.0318 146 GLN A CD  
3098 O OE1 . GLN B 149 ? 0.3375 0.4496 0.3798 0.0652  -0.0710 -0.0330 146 GLN A OE1 
3099 N NE2 . GLN B 149 ? 0.2906 0.4374 0.3701 0.0563  -0.0638 -0.0277 146 GLN A NE2 
3100 N N   . GLN B 150 ? 0.2129 0.3025 0.2621 0.0186  -0.0802 -0.0398 147 GLN A N   
3101 C CA  A GLN B 150 ? 0.2405 0.3162 0.2775 0.0158  -0.0914 -0.0439 147 GLN A CA  
3102 C CA  B GLN B 150 ? 0.2274 0.3029 0.2637 0.0162  -0.0913 -0.0440 147 GLN A CA  
3103 C C   . GLN B 150 ? 0.2359 0.2869 0.2504 0.0143  -0.0864 -0.0481 147 GLN A C   
3104 O O   . GLN B 150 ? 0.2501 0.2835 0.2435 0.0170  -0.0908 -0.0518 147 GLN A O   
3105 C CB  A GLN B 150 ? 0.2643 0.3522 0.3204 0.0069  -0.1020 -0.0428 147 GLN A CB  
3106 C CB  B GLN B 150 ? 0.2321 0.3195 0.2866 0.0079  -0.1028 -0.0431 147 GLN A CB  
3107 C CG  A GLN B 150 ? 0.3114 0.3789 0.3525 0.0009  -0.1125 -0.0481 147 GLN A CG  
3108 C CG  B GLN B 150 ? 0.2293 0.3431 0.3065 0.0106  -0.1094 -0.0389 147 GLN A CG  
3109 C CD  A GLN B 150 ? 0.3404 0.4185 0.3988 -0.0080 -0.1269 -0.0474 147 GLN A CD  
3110 C CD  B GLN B 150 ? 0.2508 0.3797 0.3509 -0.0001 -0.1203 -0.0368 147 GLN A CD  
3111 O OE1 A GLN B 150 ? 0.3335 0.4072 0.3849 -0.0073 -0.1404 -0.0502 147 GLN A OE1 
3112 O OE1 B GLN B 150 ? 0.2827 0.3967 0.3762 -0.0091 -0.1273 -0.0401 147 GLN A OE1 
3113 N NE2 A GLN B 150 ? 0.3400 0.4306 0.4202 -0.0172 -0.1246 -0.0435 147 GLN A NE2 
3114 N NE2 B GLN B 150 ? 0.2499 0.4084 0.3775 0.0007  -0.1227 -0.0313 147 GLN A NE2 
3115 N N   . ALA B 151 ? 0.2070 0.2574 0.2264 0.0104  -0.0774 -0.0471 148 ALA A N   
3116 C CA  . ALA B 151 ? 0.2172 0.2477 0.2191 0.0098  -0.0718 -0.0504 148 ALA A CA  
3117 C C   . ALA B 151 ? 0.2072 0.2286 0.1925 0.0167  -0.0643 -0.0509 148 ALA A C   
3118 O O   . ALA B 151 ? 0.2237 0.2277 0.1886 0.0190  -0.0639 -0.0539 148 ALA A O   
3119 C CB  . ALA B 151 ? 0.2056 0.2399 0.2189 0.0049  -0.0654 -0.0485 148 ALA A CB  
3120 N N   . TYR B 152 ? 0.1819 0.2142 0.1749 0.0201  -0.0586 -0.0476 149 TYR A N   
3121 C CA  . TYR B 152 ? 0.1928 0.2157 0.1711 0.0253  -0.0529 -0.0474 149 TYR A CA  
3122 C C   . TYR B 152 ? 0.2076 0.2199 0.1692 0.0303  -0.0593 -0.0488 149 TYR A C   
3123 O O   . TYR B 152 ? 0.2218 0.2182 0.1644 0.0322  -0.0552 -0.0496 149 TYR A O   
3124 C CB  . TYR B 152 ? 0.1884 0.2227 0.1765 0.0282  -0.0477 -0.0443 149 TYR A CB  
3125 C CG  . TYR B 152 ? 0.1888 0.2280 0.1854 0.0251  -0.0397 -0.0428 149 TYR A CG  
3126 C CD1 . TYR B 152 ? 0.2076 0.2370 0.1970 0.0225  -0.0337 -0.0437 149 TYR A CD1 
3127 C CD2 . TYR B 152 ? 0.1832 0.2372 0.1941 0.0259  -0.0376 -0.0400 149 TYR A CD2 
3128 C CE1 . TYR B 152 ? 0.1914 0.2260 0.1888 0.0203  -0.0279 -0.0421 149 TYR A CE1 
3129 C CE2 . TYR B 152 ? 0.1794 0.2365 0.1953 0.0237  -0.0312 -0.0385 149 TYR A CE2 
3130 C CZ  . TYR B 152 ? 0.1811 0.2283 0.1903 0.0209  -0.0271 -0.0397 149 TYR A CZ  
3131 O OH  . TYR B 152 ? 0.1877 0.2390 0.2024 0.0193  -0.0225 -0.0380 149 TYR A OH  
3132 N N   . GLN B 153 ? 0.2099 0.2314 0.1788 0.0323  -0.0690 -0.0484 150 GLN A N   
3133 C CA  . GLN B 153 ? 0.2481 0.2600 0.2011 0.0379  -0.0768 -0.0493 150 GLN A CA  
3134 C C   . GLN B 153 ? 0.2685 0.2606 0.2001 0.0360  -0.0805 -0.0531 150 GLN A C   
3135 O O   . GLN B 153 ? 0.3042 0.2794 0.2129 0.0405  -0.0799 -0.0536 150 GLN A O   
3136 C CB  . GLN B 153 ? 0.2510 0.2808 0.2208 0.0398  -0.0879 -0.0480 150 GLN A CB  
3137 C CG  . GLN B 153 ? 0.2732 0.2961 0.2291 0.0476  -0.0968 -0.0481 150 GLN A CG  
3138 C CD  . GLN B 153 ? 0.3119 0.3222 0.2511 0.0552  -0.0901 -0.0464 150 GLN A CD  
3139 O OE1 . GLN B 153 ? 0.3799 0.3711 0.2951 0.0593  -0.0929 -0.0470 150 GLN A OE1 
3140 N NE2 . GLN B 153 ? 0.2974 0.3161 0.2469 0.0572  -0.0816 -0.0441 150 GLN A NE2 
3141 N N   . GLU B 154 ? 0.2815 0.2739 0.2188 0.0299  -0.0842 -0.0557 151 GLU A N   
3142 C CA  . GLU B 154 ? 0.3119 0.2835 0.2269 0.0291  -0.0872 -0.0602 151 GLU A CA  
3143 C C   . GLU B 154 ? 0.3084 0.2651 0.2059 0.0311  -0.0738 -0.0604 151 GLU A C   
3144 O O   . GLU B 154 ? 0.3182 0.2568 0.1904 0.0351  -0.0732 -0.0619 151 GLU A O   
3145 C CB  . GLU B 154 ? 0.3256 0.2975 0.2487 0.0222  -0.0944 -0.0632 151 GLU A CB  
3146 C CG  . GLU B 154 ? 0.3842 0.3310 0.2797 0.0230  -0.0992 -0.0688 151 GLU A CG  
3147 C CD  . GLU B 154 ? 0.4171 0.3584 0.3161 0.0162  -0.1075 -0.0726 151 GLU A CD  
3148 O OE1 . GLU B 154 ? 0.3829 0.3404 0.3076 0.0095  -0.1095 -0.0703 151 GLU A OE1 
3149 O OE2 . GLU B 154 ? 0.4739 0.3921 0.3468 0.0181  -0.1121 -0.0779 151 GLU A OE2 
3150 N N   . ALA B 155 ? 0.2770 0.2426 0.1888 0.0285  -0.0632 -0.0584 152 ALA A N   
3151 C CA  . ALA B 155 ? 0.2888 0.2462 0.1907 0.0298  -0.0504 -0.0574 152 ALA A CA  
3152 C C   . ALA B 155 ? 0.2997 0.2494 0.1866 0.0341  -0.0470 -0.0548 152 ALA A C   
3153 O O   . ALA B 155 ? 0.3233 0.2589 0.1912 0.0360  -0.0404 -0.0548 152 ALA A O   
3154 C CB  . ALA B 155 ? 0.2534 0.2248 0.1756 0.0265  -0.0421 -0.0548 152 ALA A CB  
3155 N N   . PHE B 156 ? 0.2807 0.2388 0.1753 0.0361  -0.0512 -0.0522 153 PHE A N   
3156 C CA  . PHE B 156 ? 0.2881 0.2375 0.1694 0.0401  -0.0484 -0.0493 153 PHE A CA  
3157 C C   . PHE B 156 ? 0.3178 0.2490 0.1728 0.0446  -0.0538 -0.0502 153 PHE A C   
3158 O O   . PHE B 156 ? 0.3177 0.2343 0.1538 0.0463  -0.0473 -0.0477 153 PHE A O   
3159 C CB  . PHE B 156 ? 0.2994 0.2615 0.1952 0.0429  -0.0527 -0.0472 153 PHE A CB  
3160 C CG  . PHE B 156 ? 0.3193 0.2712 0.2025 0.0474  -0.0504 -0.0441 153 PHE A CG  
3161 C CD1 . PHE B 156 ? 0.3401 0.2888 0.2239 0.0446  -0.0409 -0.0418 153 PHE A CD1 
3162 C CD2 . PHE B 156 ? 0.4035 0.3469 0.2731 0.0542  -0.0586 -0.0434 153 PHE A CD2 
3163 C CE1 . PHE B 156 ? 0.3631 0.2987 0.2336 0.0477  -0.0395 -0.0390 153 PHE A CE1 
3164 C CE2 . PHE B 156 ? 0.4336 0.3640 0.2895 0.0587  -0.0567 -0.0404 153 PHE A CE2 
3165 C CZ  . PHE B 156 ? 0.3997 0.3258 0.2563 0.0551  -0.0471 -0.0382 153 PHE A CZ  
3166 N N   . GLU B 157 ? 0.3123 0.2445 0.1663 0.0460  -0.0663 -0.0532 154 GLU A N   
3167 C CA  . GLU B 157 ? 0.3618 0.2763 0.1896 0.0506  -0.0740 -0.0546 154 GLU A CA  
3168 C C   . GLU B 157 ? 0.3629 0.2592 0.1680 0.0500  -0.0667 -0.0568 154 GLU A C   
3169 O O   . GLU B 157 ? 0.3913 0.2695 0.1698 0.0541  -0.0641 -0.0553 154 GLU A O   
3170 C CB  . GLU B 157 ? 0.3952 0.3172 0.2304 0.0511  -0.0906 -0.0574 154 GLU A CB  
3171 C CG  . GLU B 157 ? 0.4230 0.3627 0.2774 0.0545  -0.0976 -0.0545 154 GLU A CG  
3172 C CD  . GLU B 157 ? 0.4608 0.4173 0.3346 0.0525  -0.1124 -0.0562 154 GLU A CD  
3173 O OE1 . GLU B 157 ? 0.5392 0.4930 0.4127 0.0469  -0.1188 -0.0601 154 GLU A OE1 
3174 O OE2 . GLU B 157 ? 0.4647 0.4391 0.3570 0.0559  -0.1168 -0.0534 154 GLU A OE2 
3175 N N   . ILE B 158 ? 0.3441 0.2441 0.1579 0.0459  -0.0639 -0.0601 155 ILE A N   
3176 C CA  . ILE B 158 ? 0.3850 0.2687 0.1781 0.0470  -0.0557 -0.0625 155 ILE A CA  
3177 C C   . ILE B 158 ? 0.3859 0.2662 0.1724 0.0479  -0.0395 -0.0575 155 ILE A C   
3178 O O   . ILE B 158 ? 0.4200 0.2830 0.1797 0.0517  -0.0340 -0.0566 155 ILE A O   
3179 C CB  . ILE B 158 ? 0.3851 0.2730 0.1901 0.0434  -0.0549 -0.0666 155 ILE A CB  
3180 C CG1 . ILE B 158 ? 0.4022 0.2896 0.2106 0.0411  -0.0718 -0.0713 155 ILE A CG1 
3181 C CG2 . ILE B 158 ? 0.4062 0.2778 0.1898 0.0468  -0.0439 -0.0687 155 ILE A CG2 
3182 C CD1 . ILE B 158 ? 0.4071 0.2987 0.2303 0.0361  -0.0727 -0.0745 155 ILE A CD1 
3183 N N   . SER B 159 ? 0.3623 0.2589 0.1725 0.0439  -0.0326 -0.0540 156 SER A N   
3184 C CA  . SER B 159 ? 0.3727 0.2680 0.1807 0.0427  -0.0183 -0.0491 156 SER A CA  
3185 C C   . SER B 159 ? 0.3847 0.2668 0.1732 0.0452  -0.0183 -0.0448 156 SER A C   
3186 O O   . SER B 159 ? 0.4013 0.2737 0.1753 0.0452  -0.0074 -0.0411 156 SER A O   
3187 C CB  . SER B 159 ? 0.3514 0.2656 0.1879 0.0374  -0.0129 -0.0468 156 SER A CB  
3188 O OG  . SER B 159 ? 0.3696 0.2924 0.2187 0.0370  -0.0215 -0.0463 156 SER A OG  
3189 N N   . ALA B 160 ? 0.3906 0.2721 0.1786 0.0478  -0.0299 -0.0446 157 ALA A N   
3190 C CA  . ALA B 160 ? 0.4168 0.2824 0.1833 0.0515  -0.0310 -0.0404 157 ALA A CA  
3191 C C   . ALA B 160 ? 0.4489 0.2932 0.1821 0.0561  -0.0310 -0.0409 157 ALA A C   
3192 O O   . ALA B 160 ? 0.4818 0.3108 0.1942 0.0571  -0.0235 -0.0360 157 ALA A O   
3193 C CB  . ALA B 160 ? 0.4207 0.2910 0.1943 0.0553  -0.0437 -0.0404 157 ALA A CB  
3194 N N   . ALA B 161 ? 0.4634 0.3051 0.1900 0.0586  -0.0397 -0.0466 158 ALA A N   
3195 C CA  . ALA B 161 ? 0.4852 0.3049 0.1773 0.0637  -0.0409 -0.0483 158 ALA A CA  
3196 C C   . ALA B 161 ? 0.5050 0.3175 0.1849 0.0633  -0.0245 -0.0478 158 ALA A C   
3197 O O   . ALA B 161 ? 0.5350 0.3270 0.1820 0.0681  -0.0209 -0.0467 158 ALA A O   
3198 C CB  . ALA B 161 ? 0.4971 0.3162 0.1876 0.0656  -0.0573 -0.0552 158 ALA A CB  
3199 N N   . ALA B 162 ? 0.4761 0.3044 0.1797 0.0589  -0.0154 -0.0489 159 ALA A N   
3200 C CA  . ALA B 162 ? 0.5160 0.3391 0.2093 0.0609  -0.0029 -0.0505 159 ALA A CA  
3201 C C   . ALA B 162 ? 0.4963 0.3321 0.2059 0.0570  0.0152  -0.0448 159 ALA A C   
3202 O O   . ALA B 162 ? 0.5045 0.3372 0.2055 0.0602  0.0268  -0.0454 159 ALA A O   
3203 C CB  . ALA B 162 ? 0.5304 0.3563 0.2314 0.0615  -0.0106 -0.0585 159 ALA A CB  
3204 N N   . MET B 163 ? 0.4493 0.3002 0.1835 0.0507  0.0167  -0.0402 160 MET A N   
3205 C CA  . MET B 163 ? 0.4260 0.2922 0.1811 0.0456  0.0306  -0.0356 160 MET A CA  
3206 C C   . MET B 163 ? 0.4366 0.3008 0.1916 0.0406  0.0353  -0.0278 160 MET A C   
3207 O O   . MET B 163 ? 0.4253 0.2813 0.1734 0.0407  0.0256  -0.0269 160 MET A O   
3208 C CB  . MET B 163 ? 0.3989 0.2857 0.1869 0.0417  0.0260  -0.0387 160 MET A CB  
3209 C CG  . MET B 163 ? 0.4150 0.3031 0.2050 0.0455  0.0235  -0.0454 160 MET A CG  
3210 S SD  . MET B 163 ? 0.4257 0.3345 0.2507 0.0408  0.0158  -0.0483 160 MET A SD  
3211 C CE  . MET B 163 ? 0.3788 0.3062 0.2281 0.0355  0.0288  -0.0420 160 MET A CE  
3212 N N   . GLN B 164 ? 0.4375 0.3097 0.2016 0.0360  0.0499  -0.0219 161 GLN A N   
3213 C CA  . GLN B 164 ? 0.4701 0.3391 0.2342 0.0294  0.0553  -0.0138 161 GLN A CA  
3214 C C   . GLN B 164 ? 0.4278 0.3087 0.2175 0.0232  0.0470  -0.0142 161 GLN A C   
3215 O O   . GLN B 164 ? 0.3934 0.2917 0.2070 0.0220  0.0442  -0.0182 161 GLN A O   
3216 C CB  . GLN B 164 ? 0.4961 0.3720 0.2645 0.0252  0.0734  -0.0067 161 GLN A CB  
3217 C CG  . GLN B 164 ? 0.5429 0.4047 0.2815 0.0322  0.0838  -0.0051 161 GLN A CG  
3218 C CD  . GLN B 164 ? 0.5790 0.4517 0.3252 0.0286  0.1033  0.0027  161 GLN A CD  
3219 O OE1 . GLN B 164 ? 0.5546 0.4501 0.3293 0.0260  0.1091  0.0026  161 GLN A OE1 
3220 N NE2 . GLN B 164 ? 0.6199 0.4771 0.3401 0.0289  0.1136  0.0100  161 GLN A NE2 
3221 N N   . PRO B 165 ? 0.4397 0.3099 0.2233 0.0194  0.0436  -0.0098 162 PRO A N   
3222 C CA  . PRO B 165 ? 0.4174 0.2955 0.2211 0.0148  0.0358  -0.0107 162 PRO A CA  
3223 C C   . PRO B 165 ? 0.4052 0.3026 0.2369 0.0064  0.0419  -0.0089 162 PRO A C   
3224 O O   . PRO B 165 ? 0.3700 0.2763 0.2189 0.0043  0.0345  -0.0116 162 PRO A O   
3225 C CB  . PRO B 165 ? 0.4417 0.2990 0.2267 0.0134  0.0331  -0.0057 162 PRO A CB  
3226 C CG  . PRO B 165 ? 0.4926 0.3354 0.2541 0.0132  0.0438  0.0005  162 PRO A CG  
3227 C CD  . PRO B 165 ? 0.4777 0.3248 0.2321 0.0204  0.0463  -0.0040 162 PRO A CD  
3228 N N   . THR B 166 ? 0.4058 0.3095 0.2416 0.0020  0.0550  -0.0037 163 THR A N   
3229 C CA  . THR B 166 ? 0.3764 0.3011 0.2405 -0.0055 0.0608  -0.0015 163 THR A CA  
3230 C C   . THR B 166 ? 0.3670 0.3106 0.2488 -0.0008 0.0609  -0.0070 163 THR A C   
3231 O O   . THR B 166 ? 0.3318 0.2935 0.2382 -0.0059 0.0632  -0.0057 163 THR A O   
3232 C CB  . THR B 166 ? 0.3877 0.3140 0.2510 -0.0117 0.0754  0.0072  163 THR A CB  
3233 O OG1 . THR B 166 ? 0.4067 0.3271 0.2508 -0.0038 0.0843  0.0074  163 THR A OG1 
3234 C CG2 . THR B 166 ? 0.4163 0.3240 0.2661 -0.0193 0.0746  0.0138  163 THR A CG2 
3235 N N   . HIS B 167 ? 0.3533 0.2917 0.2225 0.0085  0.0578  -0.0128 164 HIS A N   
3236 C CA  . HIS B 167 ? 0.3451 0.2968 0.2272 0.0131  0.0587  -0.0176 164 HIS A CA  
3237 C C   . HIS B 167 ? 0.3130 0.2790 0.2193 0.0098  0.0501  -0.0203 164 HIS A C   
3238 O O   . HIS B 167 ? 0.3020 0.2625 0.2060 0.0099  0.0395  -0.0230 164 HIS A O   
3239 C CB  . HIS B 167 ? 0.3686 0.3080 0.2301 0.0225  0.0551  -0.0236 164 HIS A CB  
3240 C CG  . HIS B 167 ? 0.3635 0.3130 0.2344 0.0271  0.0602  -0.0268 164 HIS A CG  
3241 N ND1 . HIS B 167 ? 0.3376 0.3021 0.2320 0.0261  0.0555  -0.0297 164 HIS A ND1 
3242 C CD2 . HIS B 167 ? 0.4053 0.3513 0.2644 0.0336  0.0706  -0.0273 164 HIS A CD2 
3243 C CE1 . HIS B 167 ? 0.3575 0.3268 0.2549 0.0316  0.0619  -0.0317 164 HIS A CE1 
3244 N NE2 . HIS B 167 ? 0.4023 0.3611 0.2791 0.0366  0.0716  -0.0304 164 HIS A NE2 
3245 N N   . PRO B 168 ? 0.2819 0.2666 0.2116 0.0074  0.0546  -0.0192 165 PRO A N   
3246 C CA  . PRO B 168 ? 0.2794 0.2756 0.2289 0.0046  0.0462  -0.0214 165 PRO A CA  
3247 C C   . PRO B 168 ? 0.2761 0.2689 0.2227 0.0097  0.0361  -0.0276 165 PRO A C   
3248 O O   . PRO B 168 ? 0.2641 0.2591 0.2176 0.0075  0.0280  -0.0289 165 PRO A O   
3249 C CB  . PRO B 168 ? 0.2711 0.2864 0.2423 0.0037  0.0528  -0.0194 165 PRO A CB  
3250 C CG  . PRO B 168 ? 0.2874 0.3038 0.2543 0.0028  0.0659  -0.0139 165 PRO A CG  
3251 C CD  . PRO B 168 ? 0.2997 0.2959 0.2379 0.0076  0.0678  -0.0151 165 PRO A CD  
3252 N N   . ILE B 169 ? 0.2726 0.2583 0.2070 0.0163  0.0366  -0.0313 166 ILE A N   
3253 C CA  . ILE B 169 ? 0.2683 0.2503 0.2003 0.0196  0.0265  -0.0366 166 ILE A CA  
3254 C C   . ILE B 169 ? 0.2546 0.2267 0.1750 0.0193  0.0181  -0.0371 166 ILE A C   
3255 O O   . ILE B 169 ? 0.2454 0.2220 0.1738 0.0192  0.0099  -0.0391 166 ILE A O   
3256 C CB  . ILE B 169 ? 0.2585 0.2333 0.1797 0.0258  0.0278  -0.0407 166 ILE A CB  
3257 C CG1 . ILE B 169 ? 0.2624 0.2468 0.1958 0.0282  0.0352  -0.0406 166 ILE A CG1 
3258 C CG2 . ILE B 169 ? 0.2680 0.2378 0.1865 0.0272  0.0160  -0.0455 166 ILE A CG2 
3259 C CD1 . ILE B 169 ? 0.2865 0.2587 0.2023 0.0357  0.0397  -0.0442 166 ILE A CD1 
3260 N N   . ARG B 170 ? 0.2638 0.2225 0.1650 0.0202  0.0204  -0.0351 167 ARG A N   
3261 C CA  . ARG B 170 ? 0.2739 0.2224 0.1633 0.0214  0.0126  -0.0351 167 ARG A CA  
3262 C C   . ARG B 170 ? 0.2678 0.2216 0.1690 0.0172  0.0100  -0.0328 167 ARG A C   
3263 O O   . ARG B 170 ? 0.2760 0.2305 0.1793 0.0195  0.0017  -0.0347 167 ARG A O   
3264 C CB  . ARG B 170 ? 0.3120 0.2433 0.1767 0.0233  0.0168  -0.0324 167 ARG A CB  
3265 C CG  . ARG B 170 ? 0.3216 0.2404 0.1722 0.0259  0.0082  -0.0319 167 ARG A CG  
3266 C CD  . ARG B 170 ? 0.3765 0.2761 0.1988 0.0298  0.0096  -0.0302 167 ARG A CD  
3267 N NE  . ARG B 170 ? 0.3920 0.2801 0.2026 0.0325  0.0013  -0.0287 167 ARG A NE  
3268 C CZ  . ARG B 170 ? 0.4455 0.3144 0.2304 0.0356  0.0015  -0.0257 167 ARG A CZ  
3269 N NH1 . ARG B 170 ? 0.4362 0.2958 0.2036 0.0364  0.0096  -0.0241 167 ARG A NH1 
3270 N NH2 . ARG B 170 ? 0.4595 0.3171 0.2344 0.0384  -0.0054 -0.0237 167 ARG A NH2 
3271 N N   . LEU B 171 ? 0.2415 0.1999 0.1513 0.0114  0.0170  -0.0290 168 LEU A N   
3272 C CA  . LEU B 171 ? 0.2509 0.2118 0.1699 0.0068  0.0138  -0.0275 168 LEU A CA  
3273 C C   . LEU B 171 ? 0.2348 0.2091 0.1706 0.0077  0.0082  -0.0308 168 LEU A C   
3274 O O   . LEU B 171 ? 0.2254 0.1975 0.1609 0.0089  0.0021  -0.0318 168 LEU A O   
3275 C CB  . LEU B 171 ? 0.2573 0.2213 0.1834 -0.0009 0.0213  -0.0226 168 LEU A CB  
3276 C CG  . LEU B 171 ? 0.2901 0.2388 0.1991 -0.0038 0.0267  -0.0176 168 LEU A CG  
3277 C CD1 . LEU B 171 ? 0.2941 0.2518 0.2155 -0.0121 0.0360  -0.0120 168 LEU A CD1 
3278 C CD2 . LEU B 171 ? 0.3103 0.2421 0.2064 -0.0043 0.0197  -0.0169 168 LEU A CD2 
3279 N N   . GLY B 172 ? 0.2279 0.2147 0.1768 0.0077  0.0110  -0.0319 169 GLY A N   
3280 C CA  . GLY B 172 ? 0.2136 0.2122 0.1771 0.0086  0.0065  -0.0343 169 GLY A CA  
3281 C C   . GLY B 172 ? 0.2235 0.2205 0.1832 0.0132  -0.0006 -0.0372 169 GLY A C   
3282 O O   . GLY B 172 ? 0.1886 0.1916 0.1557 0.0138  -0.0049 -0.0379 169 GLY A O   
3283 N N   . LEU B 173 ? 0.2314 0.2207 0.1793 0.0166  -0.0019 -0.0388 170 LEU A N   
3284 C CA  . LEU B 173 ? 0.2296 0.2183 0.1749 0.0204  -0.0096 -0.0410 170 LEU A CA  
3285 C C   . LEU B 173 ? 0.2263 0.2118 0.1674 0.0225  -0.0135 -0.0400 170 LEU A C   
3286 O O   . LEU B 173 ? 0.2041 0.1979 0.1536 0.0249  -0.0182 -0.0408 170 LEU A O   
3287 C CB  . LEU B 173 ? 0.2545 0.2334 0.1856 0.0233  -0.0117 -0.0431 170 LEU A CB  
3288 C CG  . LEU B 173 ? 0.2496 0.2267 0.1758 0.0270  -0.0213 -0.0448 170 LEU A CG  
3289 C CD1 . LEU B 173 ? 0.2306 0.2219 0.1749 0.0257  -0.0261 -0.0460 170 LEU A CD1 
3290 C CD2 . LEU B 173 ? 0.2926 0.2560 0.1997 0.0297  -0.0238 -0.0467 170 LEU A CD2 
3291 N N   . ALA B 174 ? 0.2446 0.2174 0.1721 0.0223  -0.0113 -0.0380 171 ALA A N   
3292 C CA  . ALA B 174 ? 0.2482 0.2134 0.1683 0.0252  -0.0150 -0.0371 171 ALA A CA  
3293 C C   . ALA B 174 ? 0.2401 0.2127 0.1714 0.0240  -0.0153 -0.0372 171 ALA A C   
3294 O O   . ALA B 174 ? 0.2344 0.2091 0.1664 0.0293  -0.0196 -0.0382 171 ALA A O   
3295 C CB  . ALA B 174 ? 0.2725 0.2203 0.1757 0.0234  -0.0117 -0.0341 171 ALA A CB  
3296 N N   . LEU B 175 ? 0.2262 0.2038 0.1663 0.0178  -0.0108 -0.0363 172 LEU A N   
3297 C CA  . LEU B 175 ? 0.2175 0.2009 0.1662 0.0164  -0.0120 -0.0367 172 LEU A CA  
3298 C C   . LEU B 175 ? 0.2019 0.1983 0.1608 0.0207  -0.0147 -0.0383 172 LEU A C   
3299 O O   . LEU B 175 ? 0.1971 0.1935 0.1545 0.0247  -0.0171 -0.0390 172 LEU A O   
3300 C CB  . LEU B 175 ? 0.2245 0.2134 0.1828 0.0091  -0.0079 -0.0351 172 LEU A CB  
3301 C CG  . LEU B 175 ? 0.2188 0.2120 0.1840 0.0067  -0.0103 -0.0354 172 LEU A CG  
3302 C CD1 . LEU B 175 ? 0.2220 0.2007 0.1753 0.0062  -0.0137 -0.0357 172 LEU A CD1 
3303 C CD2 . LEU B 175 ? 0.2148 0.2183 0.1936 0.0007  -0.0074 -0.0338 172 LEU A CD2 
3304 N N   . ASN B 176 ? 0.2009 0.2073 0.1691 0.0200  -0.0140 -0.0388 173 ASN A N   
3305 C CA  . ASN B 176 ? 0.2112 0.2303 0.1908 0.0220  -0.0159 -0.0392 173 ASN A CA  
3306 C C   . ASN B 176 ? 0.1997 0.2214 0.1779 0.0277  -0.0202 -0.0397 173 ASN A C   
3307 O O   . ASN B 176 ? 0.2007 0.2318 0.1860 0.0307  -0.0209 -0.0391 173 ASN A O   
3308 C CB  . ASN B 176 ? 0.2018 0.2274 0.1905 0.0188  -0.0145 -0.0393 173 ASN A CB  
3309 C CG  . ASN B 176 ? 0.1889 0.2170 0.1835 0.0150  -0.0108 -0.0383 173 ASN A CG  
3310 O OD1 . ASN B 176 ? 0.1953 0.2201 0.1873 0.0131  -0.0097 -0.0375 173 ASN A OD1 
3311 N ND2 . ASN B 176 ? 0.1677 0.2007 0.1699 0.0138  -0.0097 -0.0384 173 ASN A ND2 
3312 N N   . PHE B 177 ? 0.2070 0.2211 0.1761 0.0296  -0.0228 -0.0404 174 PHE A N   
3313 C CA  . PHE B 177 ? 0.2023 0.2195 0.1706 0.0358  -0.0281 -0.0405 174 PHE A CA  
3314 C C   . PHE B 177 ? 0.1995 0.2130 0.1620 0.0419  -0.0282 -0.0400 174 PHE A C   
3315 O O   . PHE B 177 ? 0.1887 0.2134 0.1588 0.0477  -0.0303 -0.0395 174 PHE A O   
3316 C CB  . PHE B 177 ? 0.2245 0.2322 0.1814 0.0370  -0.0321 -0.0414 174 PHE A CB  
3317 C CG  . PHE B 177 ? 0.2206 0.2356 0.1815 0.0414  -0.0398 -0.0418 174 PHE A CG  
3318 C CD1 . PHE B 177 ? 0.2119 0.2453 0.1903 0.0431  -0.0424 -0.0408 174 PHE A CD1 
3319 C CD2 . PHE B 177 ? 0.2353 0.2390 0.1823 0.0431  -0.0447 -0.0428 174 PHE A CD2 
3320 C CE1 . PHE B 177 ? 0.2345 0.2769 0.2194 0.0460  -0.0503 -0.0407 174 PHE A CE1 
3321 C CE2 . PHE B 177 ? 0.2602 0.2707 0.2109 0.0467  -0.0537 -0.0432 174 PHE A CE2 
3322 C CZ  . PHE B 177 ? 0.2464 0.2773 0.2177 0.0478  -0.0568 -0.0421 174 PHE A CZ  
3323 N N   A SER B 178 ? 0.2024 0.2006 0.1520 0.0408  -0.0259 -0.0400 175 SER A N   
3324 N N   B SER B 178 ? 0.2164 0.2147 0.1662 0.0408  -0.0258 -0.0400 175 SER A N   
3325 C CA  A SER B 178 ? 0.2072 0.1969 0.1480 0.0462  -0.0263 -0.0402 175 SER A CA  
3326 C CA  B SER B 178 ? 0.2320 0.2216 0.1727 0.0463  -0.0262 -0.0402 175 SER A CA  
3327 C C   A SER B 178 ? 0.1978 0.1993 0.1483 0.0481  -0.0243 -0.0405 175 SER A C   
3328 C C   B SER B 178 ? 0.2103 0.2119 0.1609 0.0482  -0.0243 -0.0405 175 SER A C   
3329 O O   A SER B 178 ? 0.1930 0.1978 0.1426 0.0567  -0.0252 -0.0407 175 SER A O   
3330 O O   B SER B 178 ? 0.2029 0.2076 0.1524 0.0567  -0.0251 -0.0408 175 SER A O   
3331 C CB  A SER B 178 ? 0.2118 0.1818 0.1381 0.0419  -0.0248 -0.0398 175 SER A CB  
3332 C CB  B SER B 178 ? 0.2515 0.2208 0.1771 0.0424  -0.0249 -0.0399 175 SER A CB  
3333 O OG  A SER B 178 ? 0.2116 0.1715 0.1289 0.0460  -0.0258 -0.0407 175 SER A OG  
3334 O OG  B SER B 178 ? 0.2755 0.2466 0.2070 0.0340  -0.0217 -0.0397 175 SER A OG  
3335 N N   . VAL B 179 ? 0.1903 0.1997 0.1506 0.0412  -0.0215 -0.0402 176 VAL A N   
3336 C CA  . VAL B 179 ? 0.1958 0.2149 0.1629 0.0426  -0.0195 -0.0399 176 VAL A CA  
3337 C C   . VAL B 179 ? 0.1810 0.2183 0.1611 0.0472  -0.0192 -0.0384 176 VAL A C   
3338 O O   . VAL B 179 ? 0.1784 0.2219 0.1592 0.0537  -0.0173 -0.0378 176 VAL A O   
3339 C CB  . VAL B 179 ? 0.1949 0.2166 0.1680 0.0347  -0.0176 -0.0394 176 VAL A CB  
3340 C CG1 . VAL B 179 ? 0.1927 0.2260 0.1731 0.0364  -0.0156 -0.0383 176 VAL A CG1 
3341 C CG2 . VAL B 179 ? 0.2270 0.2334 0.1894 0.0305  -0.0184 -0.0404 176 VAL A CG2 
3342 N N   . PHE B 180 ? 0.1775 0.2224 0.1669 0.0441  -0.0212 -0.0377 177 PHE A N   
3343 C CA  . PHE B 180 ? 0.1621 0.2244 0.1656 0.0468  -0.0224 -0.0358 177 PHE A CA  
3344 C C   . PHE B 180 ? 0.1661 0.2316 0.1670 0.0572  -0.0236 -0.0355 177 PHE A C   
3345 O O   . PHE B 180 ? 0.1525 0.2335 0.1637 0.0620  -0.0210 -0.0333 177 PHE A O   
3346 C CB  . PHE B 180 ? 0.1576 0.2216 0.1666 0.0413  -0.0267 -0.0361 177 PHE A CB  
3347 C CG  . PHE B 180 ? 0.1590 0.2407 0.1838 0.0424  -0.0301 -0.0341 177 PHE A CG  
3348 C CD1 . PHE B 180 ? 0.1497 0.2456 0.1902 0.0375  -0.0279 -0.0312 177 PHE A CD1 
3349 C CD2 . PHE B 180 ? 0.1703 0.2543 0.1947 0.0477  -0.0361 -0.0344 177 PHE A CD2 
3350 C CE1 . PHE B 180 ? 0.1596 0.2729 0.2173 0.0362  -0.0314 -0.0285 177 PHE A CE1 
3351 C CE2 . PHE B 180 ? 0.1820 0.2855 0.2247 0.0475  -0.0402 -0.0320 177 PHE A CE2 
3352 C CZ  . PHE B 180 ? 0.1629 0.2815 0.2230 0.0412  -0.0375 -0.0289 177 PHE A CZ  
3353 N N   . TYR B 181 ? 0.1780 0.2294 0.1654 0.0614  -0.0272 -0.0372 178 TYR A N   
3354 C CA  . TYR B 181 ? 0.2010 0.2529 0.1842 0.0729  -0.0288 -0.0371 178 TYR A CA  
3355 C C   . TYR B 181 ? 0.2096 0.2583 0.1859 0.0795  -0.0237 -0.0376 178 TYR A C   
3356 O O   . TYR B 181 ? 0.2314 0.2924 0.2136 0.0892  -0.0219 -0.0363 178 TYR A O   
3357 C CB  . TYR B 181 ? 0.2245 0.2564 0.1898 0.0763  -0.0335 -0.0385 178 TYR A CB  
3358 C CG  . TYR B 181 ? 0.2569 0.2954 0.2281 0.0759  -0.0400 -0.0378 178 TYR A CG  
3359 C CD1 . TYR B 181 ? 0.3099 0.3628 0.2907 0.0850  -0.0443 -0.0364 178 TYR A CD1 
3360 C CD2 . TYR B 181 ? 0.2851 0.3151 0.2513 0.0677  -0.0424 -0.0386 178 TYR A CD2 
3361 C CE1 . TYR B 181 ? 0.3450 0.4041 0.3310 0.0848  -0.0524 -0.0359 178 TYR A CE1 
3362 C CE2 . TYR B 181 ? 0.3058 0.3390 0.2736 0.0681  -0.0497 -0.0386 178 TYR A CE2 
3363 C CZ  . TYR B 181 ? 0.3445 0.3926 0.3229 0.0760  -0.0555 -0.0373 178 TYR A CZ  
3364 O OH  . TYR B 181 ? 0.3550 0.4071 0.3356 0.0765  -0.0649 -0.0374 178 TYR A OH  
3365 N N   . TYR B 182 ? 0.2027 0.2347 0.1660 0.0747  -0.0218 -0.0395 179 TYR A N   
3366 C CA  . TYR B 182 ? 0.2243 0.2471 0.1753 0.0814  -0.0189 -0.0410 179 TYR A CA  
3367 C C   . TYR B 182 ? 0.2210 0.2634 0.1839 0.0841  -0.0134 -0.0390 179 TYR A C   
3368 O O   . TYR B 182 ? 0.2320 0.2782 0.1914 0.0956  -0.0102 -0.0389 179 TYR A O   
3369 C CB  . TYR B 182 ? 0.2318 0.2345 0.1689 0.0736  -0.0196 -0.0432 179 TYR A CB  
3370 C CG  . TYR B 182 ? 0.2652 0.2513 0.1839 0.0804  -0.0191 -0.0459 179 TYR A CG  
3371 C CD1 . TYR B 182 ? 0.2747 0.2664 0.1931 0.0822  -0.0157 -0.0462 179 TYR A CD1 
3372 C CD2 . TYR B 182 ? 0.2940 0.2565 0.1931 0.0859  -0.0225 -0.0481 179 TYR A CD2 
3373 C CE1 . TYR B 182 ? 0.3012 0.2752 0.1992 0.0895  -0.0158 -0.0494 179 TYR A CE1 
3374 C CE2 . TYR B 182 ? 0.3231 0.2672 0.2028 0.0928  -0.0229 -0.0512 179 TYR A CE2 
3375 C CZ  . TYR B 182 ? 0.3273 0.2769 0.2060 0.0945  -0.0197 -0.0523 179 TYR A CZ  
3376 O OH  . TYR B 182 ? 0.3681 0.2963 0.2243 0.1011  -0.0210 -0.0562 179 TYR A OH  
3377 N N   . GLU B 183 ? 0.2198 0.2726 0.1948 0.0744  -0.0118 -0.0372 180 GLU A N   
3378 C CA  . GLU B 183 ? 0.2611 0.3264 0.2421 0.0755  -0.0062 -0.0349 180 GLU A CA  
3379 C C   . GLU B 183 ? 0.2338 0.3249 0.2376 0.0742  -0.0035 -0.0301 180 GLU A C   
3380 O O   . GLU B 183 ? 0.2600 0.3630 0.2677 0.0790  0.0025  -0.0273 180 GLU A O   
3381 C CB  . GLU B 183 ? 0.2921 0.3468 0.2655 0.0679  -0.0062 -0.0360 180 GLU A CB  
3382 C CG  . GLU B 183 ? 0.3056 0.3688 0.2929 0.0569  -0.0066 -0.0337 180 GLU A CG  
3383 C CD  . GLU B 183 ? 0.3272 0.3804 0.3072 0.0508  -0.0076 -0.0347 180 GLU A CD  
3384 O OE1 . GLU B 183 ? 0.3520 0.3907 0.3167 0.0524  -0.0092 -0.0374 180 GLU A OE1 
3385 O OE2 . GLU B 183 ? 0.3026 0.3629 0.2936 0.0440  -0.0075 -0.0327 180 GLU A OE2 
3386 N N   . ILE B 184 ? 0.1952 0.2937 0.2122 0.0680  -0.0079 -0.0292 181 ILE A N   
3387 C CA  . ILE B 184 ? 0.1775 0.2995 0.2167 0.0655  -0.0072 -0.0247 181 ILE A CA  
3388 C C   . ILE B 184 ? 0.1737 0.3082 0.2200 0.0756  -0.0084 -0.0236 181 ILE A C   
3389 O O   . ILE B 184 ? 0.1848 0.3401 0.2456 0.0795  -0.0036 -0.0193 181 ILE A O   
3390 C CB  . ILE B 184 ? 0.1580 0.2803 0.2066 0.0537  -0.0123 -0.0245 181 ILE A CB  
3391 C CG1 . ILE B 184 ? 0.1579 0.2680 0.1994 0.0460  -0.0108 -0.0255 181 ILE A CG1 
3392 C CG2 . ILE B 184 ? 0.1580 0.3029 0.2297 0.0496  -0.0129 -0.0197 181 ILE A CG2 
3393 C CD1 . ILE B 184 ? 0.1605 0.2767 0.2041 0.0453  -0.0045 -0.0221 181 ILE A CD1 
3394 N N   . LEU B 185 ? 0.1867 0.3094 0.2234 0.0799  -0.0144 -0.0269 182 LEU A N   
3395 C CA  . LEU B 185 ? 0.2214 0.3548 0.2641 0.0907  -0.0170 -0.0259 182 LEU A CA  
3396 C C   . LEU B 185 ? 0.2663 0.3923 0.2945 0.1058  -0.0126 -0.0273 182 LEU A C   
3397 O O   . LEU B 185 ? 0.2630 0.4017 0.2989 0.1167  -0.0135 -0.0258 182 LEU A O   
3398 C CB  . LEU B 185 ? 0.2364 0.3598 0.2747 0.0884  -0.0267 -0.0282 182 LEU A CB  
3399 C CG  . LEU B 185 ? 0.2380 0.3682 0.2891 0.0760  -0.0324 -0.0274 182 LEU A CG  
3400 C CD1 . LEU B 185 ? 0.2518 0.3695 0.2930 0.0769  -0.0417 -0.0299 182 LEU A CD1 
3401 C CD2 . LEU B 185 ? 0.2428 0.4020 0.3214 0.0728  -0.0325 -0.0226 182 LEU A CD2 
3402 N N   A ASN B 186 ? 0.2617 0.3673 0.2693 0.1068  -0.0086 -0.0303 183 ASN A N   
3403 N N   B ASN B 186 ? 0.2651 0.3699 0.2721 0.1068  -0.0089 -0.0305 183 ASN A N   
3404 C CA  A ASN B 186 ? 0.2840 0.3747 0.2718 0.1205  -0.0058 -0.0330 183 ASN A CA  
3405 C CA  B ASN B 186 ? 0.2893 0.3809 0.2777 0.1208  -0.0058 -0.0329 183 ASN A CA  
3406 C C   A ASN B 186 ? 0.2888 0.3667 0.2666 0.1291  -0.0123 -0.0351 183 ASN A C   
3407 C C   B ASN B 186 ? 0.2931 0.3698 0.2697 0.1293  -0.0122 -0.0352 183 ASN A C   
3408 O O   A ASN B 186 ? 0.2962 0.3801 0.2737 0.1441  -0.0107 -0.0346 183 ASN A O   
3409 O O   B ASN B 186 ? 0.3021 0.3822 0.2759 0.1447  -0.0104 -0.0351 183 ASN A O   
3410 C CB  A ASN B 186 ? 0.3137 0.4227 0.3081 0.1311  0.0033  -0.0303 183 ASN A CB  
3411 C CB  B ASN B 186 ? 0.3238 0.4375 0.3227 0.1317  0.0029  -0.0295 183 ASN A CB  
3412 C CG  A ASN B 186 ? 0.2976 0.4162 0.2993 0.1215  0.0091  -0.0275 183 ASN A CG  
3413 C CG  B ASN B 186 ? 0.3406 0.4347 0.3145 0.1406  0.0081  -0.0329 183 ASN A CG  
3414 O OD1 A ASN B 186 ? 0.3056 0.4054 0.2917 0.1151  0.0087  -0.0303 183 ASN A OD1 
3415 O OD1 B ASN B 186 ? 0.3704 0.4472 0.3307 0.1322  0.0076  -0.0354 183 ASN A OD1 
3416 N ND2 A ASN B 186 ? 0.2840 0.4320 0.3101 0.1201  0.0138  -0.0216 183 ASN A ND2 
3417 N ND2 B ASN B 186 ? 0.3746 0.4701 0.3417 0.1579  0.0123  -0.0334 183 ASN A ND2 
3418 N N   . SER B 187 ? 0.2679 0.3283 0.2371 0.1201  -0.0188 -0.0369 184 SER A N   
3419 C CA  . SER B 187 ? 0.2849 0.3293 0.2420 0.1250  -0.0258 -0.0382 184 SER A CA  
3420 C C   . SER B 187 ? 0.2798 0.2910 0.2119 0.1193  -0.0275 -0.0414 184 SER A C   
3421 O O   . SER B 187 ? 0.2668 0.2693 0.1962 0.1089  -0.0310 -0.0413 184 SER A O   
3422 C CB  . SER B 187 ? 0.2918 0.3478 0.2629 0.1180  -0.0323 -0.0363 184 SER A CB  
3423 O OG  . SER B 187 ? 0.3100 0.3957 0.3048 0.1231  -0.0327 -0.0331 184 SER A OG  
3424 N N   . PRO B 188 ? 0.2988 0.2907 0.2118 0.1254  -0.0250 -0.0441 185 PRO A N   
3425 C CA  . PRO B 188 ? 0.3209 0.2829 0.2129 0.1174  -0.0272 -0.0466 185 PRO A CA  
3426 C C   . PRO B 188 ? 0.3170 0.2570 0.1942 0.1172  -0.0329 -0.0464 185 PRO A C   
3427 O O   . PRO B 188 ? 0.3038 0.2304 0.1751 0.1048  -0.0343 -0.0461 185 PRO A O   
3428 C CB  . PRO B 188 ? 0.3385 0.2861 0.2138 0.1257  -0.0243 -0.0498 185 PRO A CB  
3429 C CG  . PRO B 188 ? 0.3670 0.3288 0.2469 0.1437  -0.0215 -0.0491 185 PRO A CG  
3430 C CD  . PRO B 188 ? 0.3203 0.3179 0.2306 0.1399  -0.0199 -0.0449 185 PRO A CD  
3431 N N   . GLU B 189 ? 0.3327 0.2703 0.2049 0.1309  -0.0358 -0.0458 186 GLU A N   
3432 C CA  . GLU B 189 ? 0.3613 0.2770 0.2175 0.1325  -0.0415 -0.0449 186 GLU A CA  
3433 C C   . GLU B 189 ? 0.3610 0.2843 0.2263 0.1199  -0.0438 -0.0424 186 GLU A C   
3434 O O   . GLU B 189 ? 0.3607 0.2629 0.2118 0.1112  -0.0452 -0.0416 186 GLU A O   
3435 C CB  . GLU B 189 ? 0.3892 0.3057 0.2417 0.1510  -0.0450 -0.0442 186 GLU A CB  
3436 C CG  . GLU B 189 ? 0.4168 0.3252 0.2584 0.1667  -0.0420 -0.0468 186 GLU A CG  
3437 C CD  . GLU B 189 ? 0.4147 0.3528 0.2751 0.1753  -0.0355 -0.0470 186 GLU A CD  
3438 O OE1 . GLU B 189 ? 0.3644 0.3317 0.2495 0.1661  -0.0331 -0.0448 186 GLU A OE1 
3439 O OE2 . GLU B 189 ? 0.4344 0.3647 0.2831 0.1910  -0.0325 -0.0492 186 GLU A OE2 
3440 N N   . LYS B 190 ? 0.3438 0.2970 0.2326 0.1191  -0.0441 -0.0411 187 LYS A N   
3441 C CA  . LYS B 190 ? 0.3463 0.3074 0.2435 0.1086  -0.0466 -0.0396 187 LYS A CA  
3442 C C   . LYS B 190 ? 0.2981 0.2551 0.1961 0.0935  -0.0420 -0.0402 187 LYS A C   
3443 O O   . LYS B 190 ? 0.3079 0.2545 0.1986 0.0856  -0.0428 -0.0393 187 LYS A O   
3444 C CB  . LYS B 190 ? 0.3522 0.3447 0.2743 0.1100  -0.0489 -0.0384 187 LYS A CB  
3445 C CG  . LYS B 190 ? 0.4769 0.4737 0.3993 0.1208  -0.0566 -0.0370 187 LYS A CG  
3446 C CD  . LYS B 190 ? 0.5794 0.6076 0.5282 0.1201  -0.0609 -0.0355 187 LYS A CD  
3447 C CE  . LYS B 190 ? 0.7289 0.7830 0.6976 0.1311  -0.0587 -0.0339 187 LYS A CE  
3448 N NZ  . LYS B 190 ? 0.7830 0.8659 0.7765 0.1317  -0.0654 -0.0314 187 LYS A NZ  
3449 N N   . ALA B 191 ? 0.3085 0.2735 0.2144 0.0905  -0.0371 -0.0413 188 ALA A N   
3450 C CA  . ALA B 191 ? 0.2710 0.2335 0.1789 0.0774  -0.0334 -0.0417 188 ALA A CA  
3451 C C   . ALA B 191 ? 0.2896 0.2250 0.1781 0.0719  -0.0337 -0.0416 188 ALA A C   
3452 O O   . ALA B 191 ? 0.2675 0.2000 0.1567 0.0615  -0.0321 -0.0404 188 ALA A O   
3453 C CB  . ALA B 191 ? 0.2606 0.2319 0.1753 0.0776  -0.0294 -0.0429 188 ALA A CB  
3454 N N   . CME B 192 ? 0.3176 0.2333 0.1890 0.0791  -0.0354 -0.0427 189 CME A N   
3455 C CA  . CME B 192 ? 0.3581 0.2446 0.2091 0.0741  -0.0367 -0.0421 189 CME A CA  
3456 C CB  . CME B 192 ? 0.4064 0.2730 0.2397 0.0847  -0.0391 -0.0444 189 CME A CB  
3457 S SG  . CME B 192 ? 0.4685 0.2958 0.2761 0.0768  -0.0417 -0.0438 189 CME A SG  
3458 S SD  . CME B 192 ? 0.5209 0.3256 0.3083 0.0824  -0.0453 -0.0385 189 CME A SD  
3459 C CE  . CME B 192 ? 0.5407 0.3298 0.3111 0.1038  -0.0502 -0.0409 189 CME A CE  
3460 C CZ  . CME B 192 ? 0.5014 0.3203 0.2895 0.1166  -0.0503 -0.0418 189 CME A CZ  
3461 O OH  . CME B 192 ? 0.5271 0.3316 0.3004 0.1339  -0.0540 -0.0426 189 CME A OH  
3462 C C   . CME B 192 ? 0.3571 0.2336 0.1997 0.0712  -0.0381 -0.0389 189 CME A C   
3463 O O   . CME B 192 ? 0.3319 0.1981 0.1698 0.0598  -0.0358 -0.0367 189 CME A O   
3464 N N   A SER B 193 ? 0.3545 0.2343 0.1950 0.0820  -0.0418 -0.0383 190 SER A N   
3465 N N   B SER B 193 ? 0.3582 0.2379 0.1985 0.0821  -0.0418 -0.0383 190 SER A N   
3466 C CA  A SER B 193 ? 0.3643 0.2332 0.1933 0.0819  -0.0444 -0.0354 190 SER A CA  
3467 C CA  B SER B 193 ? 0.3700 0.2395 0.1993 0.0822  -0.0445 -0.0354 190 SER A CA  
3468 C C   A SER B 193 ? 0.3521 0.2311 0.1896 0.0702  -0.0408 -0.0340 190 SER A C   
3469 C C   B SER B 193 ? 0.3554 0.2346 0.1929 0.0704  -0.0410 -0.0340 190 SER A C   
3470 O O   A SER B 193 ? 0.3626 0.2256 0.1872 0.0632  -0.0385 -0.0311 190 SER A O   
3471 O O   B SER B 193 ? 0.3646 0.2275 0.1886 0.0640  -0.0389 -0.0311 190 SER A O   
3472 C CB  A SER B 193 ? 0.3620 0.2401 0.1931 0.0954  -0.0501 -0.0355 190 SER A CB  
3473 C CB  B SER B 193 ? 0.3701 0.2501 0.2026 0.0953  -0.0502 -0.0355 190 SER A CB  
3474 O OG  A SER B 193 ? 0.3734 0.2370 0.1889 0.0962  -0.0538 -0.0327 190 SER A OG  
3475 O OG  B SER B 193 ? 0.3928 0.2583 0.2124 0.1081  -0.0533 -0.0361 190 SER A OG  
3476 N N   . LEU B 194 ? 0.3309 0.2359 0.1898 0.0684  -0.0398 -0.0358 191 LEU A N   
3477 C CA  . LEU B 194 ? 0.3131 0.2287 0.1808 0.0594  -0.0368 -0.0354 191 LEU A CA  
3478 C C   . LEU B 194 ? 0.2998 0.2081 0.1661 0.0478  -0.0302 -0.0341 191 LEU A C   
3479 O O   . LEU B 194 ? 0.3061 0.2076 0.1655 0.0419  -0.0267 -0.0318 191 LEU A O   
3480 C CB  . LEU B 194 ? 0.3069 0.2490 0.1971 0.0601  -0.0376 -0.0376 191 LEU A CB  
3481 C CG  . LEU B 194 ? 0.3133 0.2651 0.2104 0.0549  -0.0378 -0.0379 191 LEU A CG  
3482 C CD1 . LEU B 194 ? 0.3214 0.2973 0.2402 0.0564  -0.0404 -0.0394 191 LEU A CD1 
3483 C CD2 . LEU B 194 ? 0.3137 0.2627 0.2116 0.0447  -0.0307 -0.0374 191 LEU A CD2 
3484 N N   . ALA B 195 ? 0.2884 0.1984 0.1611 0.0448  -0.0285 -0.0352 192 ALA A N   
3485 C CA  . ALA B 195 ? 0.2910 0.1972 0.1660 0.0335  -0.0238 -0.0337 192 ALA A CA  
3486 C C   . ALA B 195 ? 0.3141 0.1962 0.1708 0.0288  -0.0225 -0.0301 192 ALA A C   
3487 O O   . ALA B 195 ? 0.3128 0.1944 0.1711 0.0196  -0.0172 -0.0270 192 ALA A O   
3488 C CB  . ALA B 195 ? 0.2796 0.1905 0.1623 0.0323  -0.0245 -0.0360 192 ALA A CB  
3489 N N   . LYS B 196 ? 0.3323 0.1942 0.1716 0.0355  -0.0270 -0.0300 193 LYS A N   
3490 C CA  . LYS B 196 ? 0.3668 0.2019 0.1867 0.0309  -0.0266 -0.0262 193 LYS A CA  
3491 C C   . LYS B 196 ? 0.3747 0.2039 0.1844 0.0297  -0.0235 -0.0220 193 LYS A C   
3492 O O   . LYS B 196 ? 0.3805 0.1979 0.1832 0.0201  -0.0186 -0.0173 193 LYS A O   
3493 C CB  . LYS B 196 ? 0.3883 0.2010 0.1899 0.0405  -0.0327 -0.0275 193 LYS A CB  
3494 C CG  . LYS B 196 ? 0.4247 0.2038 0.2028 0.0359  -0.0335 -0.0233 193 LYS A CG  
3495 C CD  . LYS B 196 ? 0.4212 0.1937 0.2028 0.0193  -0.0300 -0.0204 193 LYS A CD  
3496 C CE  . LYS B 196 ? 0.4600 0.1992 0.2192 0.0147  -0.0316 -0.0161 193 LYS A CE  
3497 N NZ  . LYS B 196 ? 0.4659 0.2029 0.2315 -0.0031 -0.0271 -0.0112 193 LYS A NZ  
3498 N N   . THR B 197 ? 0.3799 0.2162 0.1877 0.0394  -0.0267 -0.0234 194 THR A N   
3499 C CA  . THR B 197 ? 0.4059 0.2359 0.2012 0.0397  -0.0248 -0.0202 194 THR A CA  
3500 C C   . THR B 197 ? 0.3970 0.2394 0.2028 0.0294  -0.0161 -0.0186 194 THR A C   
3501 O O   . THR B 197 ? 0.4164 0.2463 0.2094 0.0239  -0.0102 -0.0137 194 THR A O   
3502 C CB  . THR B 197 ? 0.4050 0.2439 0.1999 0.0513  -0.0318 -0.0229 194 THR A CB  
3503 O OG1 . THR B 197 ? 0.4102 0.2364 0.1945 0.0615  -0.0386 -0.0232 194 THR A OG1 
3504 C CG2 . THR B 197 ? 0.4361 0.2669 0.2153 0.0519  -0.0311 -0.0204 194 THR A CG2 
3505 N N   . ALA B 198 ? 0.3697 0.2358 0.1977 0.0275  -0.0150 -0.0223 195 ALA A N   
3506 C CA  . ALA B 198 ? 0.3475 0.2269 0.1873 0.0198  -0.0071 -0.0214 195 ALA A CA  
3507 C C   . ALA B 198 ? 0.3582 0.2325 0.2004 0.0086  -0.0001 -0.0168 195 ALA A C   
3508 O O   . ALA B 198 ? 0.3608 0.2335 0.1989 0.0035  0.0081  -0.0126 195 ALA A O   
3509 C CB  . ALA B 198 ? 0.3439 0.2465 0.2061 0.0204  -0.0084 -0.0258 195 ALA A CB  
3510 N N   . PHE B 199 ? 0.3368 0.2066 0.1832 0.0050  -0.0034 -0.0171 196 PHE A N   
3511 C CA  . PHE B 199 ? 0.3523 0.2148 0.2003 -0.0067 0.0007  -0.0125 196 PHE A CA  
3512 C C   . PHE B 199 ? 0.3791 0.2192 0.2062 -0.0102 0.0048  -0.0060 196 PHE A C   
3513 O O   . PHE B 199 ? 0.3904 0.2342 0.2220 -0.0193 0.0134  -0.0007 196 PHE A O   
3514 C CB  . PHE B 199 ? 0.3601 0.2154 0.2100 -0.0084 -0.0063 -0.0151 196 PHE A CB  
3515 C CG  . PHE B 199 ? 0.3788 0.2274 0.2330 -0.0221 -0.0047 -0.0110 196 PHE A CG  
3516 C CD1 . PHE B 199 ? 0.4111 0.2334 0.2472 -0.0277 -0.0050 -0.0062 196 PHE A CD1 
3517 C CD2 . PHE B 199 ? 0.3809 0.2499 0.2580 -0.0299 -0.0036 -0.0117 196 PHE A CD2 
3518 C CE1 . PHE B 199 ? 0.4449 0.2617 0.2869 -0.0423 -0.0043 -0.0019 196 PHE A CE1 
3519 C CE2 . PHE B 199 ? 0.3906 0.2557 0.2743 -0.0434 -0.0035 -0.0078 196 PHE A CE2 
3520 C CZ  . PHE B 199 ? 0.4330 0.2724 0.3000 -0.0503 -0.0040 -0.0029 196 PHE A CZ  
3521 N N   . ASP B 200 ? 0.3960 0.2145 0.2007 -0.0021 -0.0007 -0.0060 197 ASP A N   
3522 C CA  . ASP B 200 ? 0.4316 0.2242 0.2128 -0.0048 0.0020  0.0007  197 ASP A CA  
3523 C C   . ASP B 200 ? 0.4430 0.2386 0.2164 -0.0044 0.0104  0.0046  197 ASP A C   
3524 O O   . ASP B 200 ? 0.4585 0.2444 0.2244 -0.0132 0.0186  0.0120  197 ASP A O   
3525 C CB  . ASP B 200 ? 0.4497 0.2183 0.2087 0.0057  -0.0069 -0.0005 197 ASP A CB  
3526 C CG  . ASP B 200 ? 0.4649 0.2206 0.2231 0.0051  -0.0138 -0.0030 197 ASP A CG  
3527 O OD1 . ASP B 200 ? 0.4510 0.2104 0.2217 -0.0066 -0.0120 -0.0023 197 ASP A OD1 
3528 O OD2 . ASP B 200 ? 0.4961 0.2359 0.2391 0.0164  -0.0213 -0.0054 197 ASP A OD2 
3529 N N   . GLU B 201 ? 0.4419 0.2516 0.2183 0.0049  0.0086  -0.0002 198 GLU A N   
3530 C CA  . GLU B 201 ? 0.4569 0.2680 0.2232 0.0066  0.0158  0.0021  198 GLU A CA  
3531 C C   . GLU B 201 ? 0.4529 0.2803 0.2353 -0.0031 0.0282  0.0054  198 GLU A C   
3532 O O   . GLU B 201 ? 0.4558 0.2772 0.2256 -0.0051 0.0379  0.0109  198 GLU A O   
3533 C CB  . GLU B 201 ? 0.4666 0.2883 0.2334 0.0175  0.0093  -0.0045 198 GLU A CB  
3534 C CG  . GLU B 201 ? 0.5171 0.3241 0.2665 0.0284  -0.0022 -0.0064 198 GLU A CG  
3535 C CD  . GLU B 201 ? 0.5212 0.3434 0.2783 0.0372  -0.0104 -0.0132 198 GLU A CD  
3536 O OE1 . GLU B 201 ? 0.5275 0.3708 0.3056 0.0351  -0.0093 -0.0173 198 GLU A OE1 
3537 O OE2 . GLU B 201 ? 0.5747 0.3869 0.3166 0.0461  -0.0191 -0.0139 198 GLU A OE2 
3538 N N   . ALA B 202 ? 0.4115 0.2601 0.2211 -0.0080 0.0282  0.0024  199 ALA A N   
3539 C CA  . ALA B 202 ? 0.4095 0.2759 0.2380 -0.0168 0.0389  0.0059  199 ALA A CA  
3540 C C   . ALA B 202 ? 0.4290 0.2870 0.2581 -0.0295 0.0451  0.0144  199 ALA A C   
3541 O O   . ALA B 202 ? 0.4169 0.2825 0.2500 -0.0350 0.0572  0.0204  199 ALA A O   
3542 C CB  . ALA B 202 ? 0.3892 0.2790 0.2447 -0.0172 0.0353  0.0003  199 ALA A CB  
3543 N N   . ILE B 203 ? 0.4532 0.2952 0.2779 -0.0344 0.0373  0.0152  200 ILE A N   
3544 C CA  . ILE B 203 ? 0.5009 0.3297 0.3232 -0.0477 0.0412  0.0234  200 ILE A CA  
3545 C C   . ILE B 203 ? 0.5416 0.3552 0.3423 -0.0491 0.0516  0.0319  200 ILE A C   
3546 O O   . ILE B 203 ? 0.5096 0.3291 0.3190 -0.0606 0.0621  0.0401  200 ILE A O   
3547 C CB  . ILE B 203 ? 0.5253 0.3307 0.3372 -0.0498 0.0294  0.0218  200 ILE A CB  
3548 C CG1 . ILE B 203 ? 0.5307 0.3508 0.3648 -0.0529 0.0220  0.0160  200 ILE A CG1 
3549 C CG2 . ILE B 203 ? 0.5757 0.3552 0.3732 -0.0617 0.0317  0.0308  200 ILE A CG2 
3550 C CD1 . ILE B 203 ? 0.5485 0.3814 0.4053 -0.0692 0.0253  0.0207  200 ILE A CD1 
3551 N N   . ALA B 204 ? 0.5883 0.3845 0.3621 -0.0371 0.0485  0.0301  201 ALA A N   
3552 C CA  . ALA B 204 ? 0.6232 0.3998 0.3704 -0.0368 0.0568  0.0381  201 ALA A CA  
3553 C C   . ALA B 204 ? 0.6156 0.4103 0.3688 -0.0383 0.0725  0.0423  201 ALA A C   
3554 O O   . ALA B 204 ? 0.6387 0.4197 0.3740 -0.0424 0.0828  0.0514  201 ALA A O   
3555 C CB  . ALA B 204 ? 0.6369 0.3923 0.3551 -0.0227 0.0477  0.0344  201 ALA A CB  
3556 N N   . GLU B 205 ? 0.5728 0.3958 0.3486 -0.0348 0.0749  0.0364  202 GLU A N   
3557 C CA  . GLU B 205 ? 0.5967 0.4361 0.3770 -0.0336 0.0899  0.0394  202 GLU A CA  
3558 C C   . GLU B 205 ? 0.5951 0.4653 0.4119 -0.0425 0.0977  0.0413  202 GLU A C   
3559 O O   . GLU B 205 ? 0.5829 0.4717 0.4085 -0.0385 0.1086  0.0414  202 GLU A O   
3560 C CB  . GLU B 205 ? 0.6037 0.4431 0.3707 -0.0185 0.0854  0.0307  202 GLU A CB  
3561 C CG  . GLU B 205 ? 0.6701 0.4806 0.3993 -0.0102 0.0809  0.0313  202 GLU A CG  
3562 C CD  . GLU B 205 ? 0.7465 0.5565 0.4618 0.0033  0.0760  0.0232  202 GLU A CD  
3563 O OE1 . GLU B 205 ? 0.7096 0.5384 0.4383 0.0072  0.0795  0.0179  202 GLU A OE1 
3564 O OE2 . GLU B 205 ? 0.8926 0.6804 0.5811 0.0101  0.0671  0.0225  202 GLU A OE2 
3565 N N   . LEU B 206 ? 0.5919 0.4668 0.4290 -0.0545 0.0922  0.0433  203 LEU A N   
3566 C CA  . LEU B 206 ? 0.5924 0.4973 0.4659 -0.0625 0.0955  0.0441  203 LEU A CA  
3567 C C   . LEU B 206 ? 0.6170 0.5363 0.5018 -0.0712 0.1132  0.0552  203 LEU A C   
3568 O O   . LEU B 206 ? 0.5540 0.5024 0.4646 -0.0709 0.1209  0.0555  203 LEU A O   
3569 C CB  . LEU B 206 ? 0.6100 0.5112 0.4967 -0.0724 0.0823  0.0425  203 LEU A CB  
3570 C CG  . LEU B 206 ? 0.5863 0.5104 0.5006 -0.0716 0.0740  0.0351  203 LEU A CG  
3571 C CD1 . LEU B 206 ? 0.5363 0.4702 0.4507 -0.0569 0.0703  0.0256  203 LEU A CD1 
3572 C CD2 . LEU B 206 ? 0.5961 0.5047 0.5094 -0.0786 0.0598  0.0327  203 LEU A CD2 
3573 N N   . ASP B 207 ? 0.6988 0.5973 0.5641 -0.0785 0.1196  0.0646  204 ASP A N   
3574 C CA  . ASP B 207 ? 0.7449 0.6524 0.6147 -0.0868 0.1381  0.0770  204 ASP A CA  
3575 C C   . ASP B 207 ? 0.7569 0.6792 0.6219 -0.0744 0.1537  0.0770  204 ASP A C   
3576 O O   . ASP B 207 ? 0.7578 0.6985 0.6370 -0.0802 0.1705  0.0866  204 ASP A O   
3577 C CB  . ASP B 207 ? 0.7807 0.6560 0.6213 -0.0940 0.1410  0.0864  204 ASP A CB  
3578 C CG  . ASP B 207 ? 0.8636 0.7071 0.6607 -0.0803 0.1378  0.0831  204 ASP A CG  
3579 O OD1 . ASP B 207 ? 0.9104 0.7536 0.6992 -0.0655 0.1292  0.0719  204 ASP A OD1 
3580 O OD2 . ASP B 207 ? 0.9062 0.7246 0.6775 -0.0845 0.1434  0.0922  204 ASP A OD2 
3581 N N   . THR B 208 ? 0.7050 0.6181 0.5491 -0.0578 0.1486  0.0671  205 THR A N   
3582 C CA  . THR B 208 ? 0.7285 0.6500 0.5627 -0.0447 0.1613  0.0653  205 THR A CA  
3583 C C   . THR B 208 ? 0.6862 0.6418 0.5541 -0.0409 0.1648  0.0608  205 THR A C   
3584 O O   . THR B 208 ? 0.7691 0.7342 0.6326 -0.0314 0.1785  0.0613  205 THR A O   
3585 C CB  . THR B 208 ? 0.7448 0.6407 0.5423 -0.0300 0.1526  0.0567  205 THR A CB  
3586 O OG1 . THR B 208 ? 0.6899 0.5918 0.4994 -0.0243 0.1365  0.0449  205 THR A OG1 
3587 C CG2 . THR B 208 ? 0.7975 0.6594 0.5611 -0.0318 0.1474  0.0608  205 THR A CG2 
3588 N N   . LEU B 209 ? 0.6101 0.5829 0.5093 -0.0469 0.1534  0.0567  206 LEU A N   
3589 C CA  . LEU B 209 ? 0.5643 0.5634 0.4890 -0.0398 0.1527  0.0501  206 LEU A CA  
3590 C C   . LEU B 209 ? 0.5627 0.5947 0.5213 -0.0461 0.1668  0.0584  206 LEU A C   
3591 O O   . LEU B 209 ? 0.5768 0.6156 0.5508 -0.0609 0.1701  0.0678  206 LEU A O   
3592 C CB  . LEU B 209 ? 0.4966 0.4975 0.4360 -0.0422 0.1335  0.0419  206 LEU A CB  
3593 C CG  . LEU B 209 ? 0.5095 0.4831 0.4213 -0.0355 0.1190  0.0336  206 LEU A CG  
3594 C CD1 . LEU B 209 ? 0.4653 0.4452 0.3950 -0.0377 0.1030  0.0267  206 LEU A CD1 
3595 C CD2 . LEU B 209 ? 0.5248 0.4896 0.4137 -0.0201 0.1211  0.0270  206 LEU A CD2 
3596 N N   . SER B 210 ? 0.5624 0.6156 0.5353 -0.0351 0.1729  0.0544  207 SER A N   
3597 C CA  . SER B 210 ? 0.5325 0.6222 0.5453 -0.0390 0.1811  0.0598  207 SER A CA  
3598 C C   . SER B 210 ? 0.5242 0.6263 0.5668 -0.0505 0.1648  0.0582  207 SER A C   
3599 O O   . SER B 210 ? 0.5315 0.6163 0.5637 -0.0505 0.1477  0.0501  207 SER A O   
3600 C CB  . SER B 210 ? 0.5049 0.6096 0.5227 -0.0221 0.1883  0.0542  207 SER A CB  
3601 O OG  . SER B 210 ? 0.4598 0.5565 0.4741 -0.0145 0.1722  0.0423  207 SER A OG  
3602 N N   . GLU B 211 ? 0.5329 0.6668 0.6130 -0.0591 0.1701  0.0655  208 GLU A N   
3603 C CA  . GLU B 211 ? 0.5384 0.6877 0.6488 -0.0692 0.1549  0.0641  208 GLU A CA  
3604 C C   . GLU B 211 ? 0.5234 0.6709 0.6334 -0.0579 0.1408  0.0520  208 GLU A C   
3605 O O   . GLU B 211 ? 0.5105 0.6473 0.6200 -0.0640 0.1238  0.0471  208 GLU A O   
3606 C CB  . GLU B 211 ? 0.5766 0.7639 0.7276 -0.0773 0.1653  0.0745  208 GLU A CB  
3607 C CG  . GLU B 211 ? 0.5754 0.7827 0.7609 -0.0881 0.1498  0.0740  208 GLU A CG  
3608 C CD  . GLU B 211 ? 0.6408 0.8834 0.8658 -0.1005 0.1591  0.0864  208 GLU A CD  
3609 O OE1 . GLU B 211 ? 0.6648 0.9322 0.9039 -0.0920 0.1772  0.0919  208 GLU A OE1 
3610 O OE2 . GLU B 211 ? 0.7326 0.9779 0.9746 -0.1187 0.1480  0.0906  208 GLU A OE2 
3611 N N   . GLU B 212 ? 0.5064 0.6617 0.6140 -0.0415 0.1480  0.0473  209 GLU A N   
3612 C CA  . GLU B 212 ? 0.5256 0.6796 0.6340 -0.0315 0.1355  0.0370  209 GLU A CA  
3613 C C   . GLU B 212 ? 0.4444 0.5651 0.5191 -0.0279 0.1239  0.0284  209 GLU A C   
3614 O O   . GLU B 212 ? 0.4132 0.5295 0.4902 -0.0277 0.1093  0.0220  209 GLU A O   
3615 C CB  . GLU B 212 ? 0.5863 0.7550 0.7008 -0.0152 0.1450  0.0342  209 GLU A CB  
3616 C CG  . GLU B 212 ? 0.5966 0.7724 0.7242 -0.0088 0.1321  0.0269  209 GLU A CG  
3617 C CD  . GLU B 212 ? 0.6454 0.8066 0.7527 0.0076  0.1312  0.0178  209 GLU A CD  
3618 O OE1 . GLU B 212 ? 0.6044 0.7694 0.7065 0.0201  0.1445  0.0178  209 GLU A OE1 
3619 O OE2 . GLU B 212 ? 0.7424 0.8872 0.8384 0.0079  0.1168  0.0106  209 GLU A OE2 
3620 N N   . SER B 213 ? 0.4356 0.5341 0.4797 -0.0247 0.1307  0.0288  210 SER A N   
3621 C CA  . SER B 213 ? 0.4328 0.5013 0.4460 -0.0215 0.1201  0.0220  210 SER A CA  
3622 C C   . SER B 213 ? 0.3890 0.4460 0.4019 -0.0338 0.1071  0.0227  210 SER A C   
3623 O O   . SER B 213 ? 0.3483 0.3940 0.3538 -0.0313 0.0935  0.0155  210 SER A O   
3624 C CB  . SER B 213 ? 0.4624 0.5107 0.4429 -0.0152 0.1302  0.0233  210 SER A CB  
3625 O OG  . SER B 213 ? 0.4735 0.5239 0.4458 -0.0009 0.1375  0.0186  210 SER A OG  
3626 N N   . TYR B 214 ? 0.3900 0.4511 0.4125 -0.0468 0.1116  0.0315  211 TYR A N   
3627 C CA  . TYR B 214 ? 0.3774 0.4274 0.4013 -0.0597 0.0999  0.0330  211 TYR A CA  
3628 C C   . TYR B 214 ? 0.3726 0.4335 0.4162 -0.0613 0.0856  0.0273  211 TYR A C   
3629 O O   . TYR B 214 ? 0.3787 0.4221 0.4098 -0.0617 0.0729  0.0219  211 TYR A O   
3630 C CB  . TYR B 214 ? 0.4226 0.4799 0.4591 -0.0743 0.1087  0.0444  211 TYR A CB  
3631 C CG  . TYR B 214 ? 0.4275 0.4666 0.4596 -0.0884 0.0973  0.0465  211 TYR A CG  
3632 C CD1 . TYR B 214 ? 0.4061 0.4558 0.4613 -0.0983 0.0851  0.0455  211 TYR A CD1 
3633 C CD2 . TYR B 214 ? 0.4508 0.4603 0.4538 -0.0915 0.0984  0.0498  211 TYR A CD2 
3634 C CE1 . TYR B 214 ? 0.4136 0.4425 0.4611 -0.1104 0.0739  0.0464  211 TYR A CE1 
3635 C CE2 . TYR B 214 ? 0.4564 0.4456 0.4528 -0.1035 0.0879  0.0516  211 TYR A CE2 
3636 C CZ  . TYR B 214 ? 0.4400 0.4385 0.4583 -0.1128 0.0756  0.0495  211 TYR A CZ  
3637 O OH  . TYR B 214 ? 0.5076 0.4828 0.5161 -0.1235 0.0647  0.0501  211 TYR A OH  
3638 N N   . LYS B 215 ? 0.3645 0.4534 0.4366 -0.0601 0.0878  0.0280  212 LYS A N   
3639 C CA  . LYS B 215 ? 0.3832 0.4830 0.4733 -0.0611 0.0745  0.0232  212 LYS A CA  
3640 C C   . LYS B 215 ? 0.3405 0.4261 0.4133 -0.0498 0.0654  0.0135  212 LYS A C   
3641 O O   . LYS B 215 ? 0.3037 0.3804 0.3732 -0.0521 0.0524  0.0091  212 LYS A O   
3642 C CB  . LYS B 215 ? 0.4231 0.5558 0.5452 -0.0591 0.0801  0.0263  212 LYS A CB  
3643 C CG  . LYS B 215 ? 0.4896 0.6381 0.6341 -0.0605 0.0674  0.0234  212 LYS A CG  
3644 C CD  . LYS B 215 ? 0.5431 0.7209 0.7132 -0.0522 0.0740  0.0250  212 LYS A CD  
3645 C CE  . LYS B 215 ? 0.5939 0.7651 0.7501 -0.0355 0.0759  0.0179  212 LYS A CE  
3646 N NZ  . LYS B 215 ? 0.6380 0.8302 0.8092 -0.0252 0.0884  0.0204  212 LYS A NZ  
3647 N N   . ASP B 216 ? 0.3200 0.4038 0.3816 -0.0376 0.0726  0.0104  213 ASP A N   
3648 C CA  . ASP B 216 ? 0.3119 0.3839 0.3588 -0.0277 0.0650  0.0021  213 ASP A CA  
3649 C C   . ASP B 216 ? 0.2995 0.3465 0.3224 -0.0291 0.0569  -0.0009 213 ASP A C   
3650 O O   . ASP B 216 ? 0.3059 0.3472 0.3256 -0.0265 0.0462  -0.0064 213 ASP A O   
3651 C CB  . ASP B 216 ? 0.3382 0.4097 0.3754 -0.0156 0.0741  -0.0003 213 ASP A CB  
3652 C CG  . ASP B 216 ? 0.3367 0.4311 0.3956 -0.0098 0.0808  0.0007  213 ASP A CG  
3653 O OD1 . ASP B 216 ? 0.3561 0.4647 0.4354 -0.0115 0.0739  0.0002  213 ASP A OD1 
3654 O OD2 . ASP B 216 ? 0.4257 0.5212 0.4782 -0.0021 0.0921  0.0014  213 ASP A OD2 
3655 N N   . SER B 217 ? 0.3020 0.3344 0.3074 -0.0317 0.0629  0.0029  214 SER A N   
3656 C CA  . SER B 217 ? 0.2995 0.3074 0.2804 -0.0309 0.0561  0.0005  214 SER A CA  
3657 C C   . SER B 217 ? 0.2873 0.2894 0.2726 -0.0396 0.0459  0.0007  214 SER A C   
3658 O O   . SER B 217 ? 0.2822 0.2738 0.2582 -0.0357 0.0362  -0.0045 214 SER A O   
3659 C CB  . SER B 217 ? 0.3269 0.3198 0.2873 -0.0314 0.0646  0.0052  214 SER A CB  
3660 O OG  . SER B 217 ? 0.3408 0.3351 0.2918 -0.0217 0.0729  0.0036  214 SER A OG  
3661 N N   . THR B 218 ? 0.2939 0.3032 0.2936 -0.0513 0.0484  0.0070  215 THR A N   
3662 C CA  . THR B 218 ? 0.3113 0.3108 0.3119 -0.0605 0.0378  0.0070  215 THR A CA  
3663 C C   . THR B 218 ? 0.2958 0.3035 0.3073 -0.0579 0.0268  0.0008  215 THR A C   
3664 O O   . THR B 218 ? 0.3218 0.3140 0.3225 -0.0589 0.0169  -0.0026 215 THR A O   
3665 C CB  . THR B 218 ? 0.3137 0.3174 0.3270 -0.0754 0.0413  0.0152  215 THR A CB  
3666 O OG1 . THR B 218 ? 0.3115 0.3447 0.3535 -0.0778 0.0468  0.0182  215 THR A OG1 
3667 C CG2 . THR B 218 ? 0.3470 0.3365 0.3444 -0.0790 0.0514  0.0221  215 THR A CG2 
3668 N N   . LEU B 219 ? 0.2737 0.3031 0.3033 -0.0532 0.0285  -0.0008 216 LEU A N   
3669 C CA  . LEU B 219 ? 0.2705 0.3063 0.3073 -0.0493 0.0190  -0.0062 216 LEU A CA  
3670 C C   . LEU B 219 ? 0.2648 0.2845 0.2815 -0.0404 0.0132  -0.0124 216 LEU A C   
3671 O O   . LEU B 219 ? 0.2458 0.2592 0.2588 -0.0402 0.0040  -0.0159 216 LEU A O   
3672 C CB  . LEU B 219 ? 0.2835 0.3430 0.3406 -0.0445 0.0232  -0.0060 216 LEU A CB  
3673 C CG  . LEU B 219 ? 0.3287 0.3967 0.3957 -0.0421 0.0135  -0.0098 216 LEU A CG  
3674 C CD1 . LEU B 219 ? 0.3781 0.4707 0.4720 -0.0447 0.0145  -0.0063 216 LEU A CD1 
3675 C CD2 . LEU B 219 ? 0.3534 0.4183 0.4116 -0.0308 0.0129  -0.0149 216 LEU A CD2 
3676 N N   . ILE B 220 ? 0.2348 0.2480 0.2384 -0.0327 0.0185  -0.0137 217 ILE A N   
3677 C CA  . ILE B 220 ? 0.2423 0.2433 0.2298 -0.0245 0.0134  -0.0187 217 ILE A CA  
3678 C C   . ILE B 220 ? 0.2274 0.2069 0.1964 -0.0264 0.0092  -0.0184 217 ILE A C   
3679 O O   . ILE B 220 ? 0.2475 0.2190 0.2082 -0.0217 0.0022  -0.0222 217 ILE A O   
3680 C CB  . ILE B 220 ? 0.2492 0.2517 0.2308 -0.0159 0.0180  -0.0207 217 ILE A CB  
3681 C CG1 . ILE B 220 ? 0.2639 0.2854 0.2636 -0.0138 0.0211  -0.0212 217 ILE A CG1 
3682 C CG2 . ILE B 220 ? 0.2492 0.2428 0.2187 -0.0087 0.0112  -0.0253 217 ILE A CG2 
3683 C CD1 . ILE B 220 ? 0.2696 0.2916 0.2644 -0.0057 0.0242  -0.0241 217 ILE A CD1 
3684 N N   . MET B 221 ? 0.2546 0.2241 0.2166 -0.0328 0.0136  -0.0135 218 MET A N   
3685 C CA  . MET B 221 ? 0.2718 0.2179 0.2151 -0.0351 0.0093  -0.0126 218 MET A CA  
3686 C C   . MET B 221 ? 0.2861 0.2269 0.2323 -0.0403 0.0002  -0.0146 218 MET A C   
3687 O O   . MET B 221 ? 0.2694 0.1922 0.1994 -0.0361 -0.0061 -0.0175 218 MET A O   
3688 C CB  . MET B 221 ? 0.3029 0.2395 0.2390 -0.0424 0.0168  -0.0057 218 MET A CB  
3689 C CG  . MET B 221 ? 0.3257 0.2605 0.2500 -0.0351 0.0245  -0.0047 218 MET A CG  
3690 S SD  . MET B 221 ? 0.3612 0.2895 0.2800 -0.0444 0.0359  0.0049  218 MET A SD  
3691 C CE  . MET B 221 ? 0.3951 0.2895 0.2872 -0.0462 0.0287  0.0064  218 MET A CE  
3692 N N   . GLN B 222 ? 0.2670 0.2233 0.2330 -0.0481 -0.0008 -0.0132 219 GLN A N   
3693 C CA  . GLN B 222 ? 0.2908 0.2424 0.2585 -0.0523 -0.0107 -0.0160 219 GLN A CA  
3694 C C   . GLN B 222 ? 0.2566 0.2078 0.2179 -0.0413 -0.0164 -0.0225 219 GLN A C   
3695 O O   . GLN B 222 ? 0.2805 0.2145 0.2276 -0.0399 -0.0237 -0.0257 219 GLN A O   
3696 C CB  . GLN B 222 ? 0.3298 0.3007 0.3215 -0.0625 -0.0116 -0.0129 219 GLN A CB  
3697 C CG  . GLN B 222 ? 0.3974 0.3599 0.3888 -0.0698 -0.0233 -0.0150 219 GLN A CG  
3698 C CD  . GLN B 222 ? 0.4680 0.4025 0.4415 -0.0777 -0.0279 -0.0137 219 GLN A CD  
3699 O OE1 . GLN B 222 ? 0.4828 0.4135 0.4579 -0.0864 -0.0223 -0.0075 219 GLN A OE1 
3700 N NE2 . GLN B 222 ? 0.5041 0.4167 0.4577 -0.0734 -0.0370 -0.0193 219 GLN A NE2 
3701 N N   . LEU B 223 ? 0.2443 0.2120 0.2141 -0.0335 -0.0127 -0.0242 220 LEU A N   
3702 C CA  . LEU B 223 ? 0.2302 0.1996 0.1957 -0.0237 -0.0166 -0.0290 220 LEU A CA  
3703 C C   . LEU B 223 ? 0.2454 0.1976 0.1911 -0.0158 -0.0181 -0.0313 220 LEU A C   
3704 O O   . LEU B 223 ? 0.2537 0.2000 0.1913 -0.0097 -0.0229 -0.0348 220 LEU A O   
3705 C CB  . LEU B 223 ? 0.2240 0.2129 0.2030 -0.0188 -0.0121 -0.0293 220 LEU A CB  
3706 C CG  . LEU B 223 ? 0.2180 0.2248 0.2168 -0.0238 -0.0116 -0.0275 220 LEU A CG  
3707 C CD1 . LEU B 223 ? 0.2228 0.2441 0.2314 -0.0180 -0.0068 -0.0278 220 LEU A CD1 
3708 C CD2 . LEU B 223 ? 0.2384 0.2454 0.2385 -0.0247 -0.0199 -0.0297 220 LEU A CD2 
3709 N N   . LEU B 224 ? 0.2579 0.2033 0.1958 -0.0144 -0.0136 -0.0291 221 LEU A N   
3710 C CA  . LEU B 224 ? 0.2596 0.1878 0.1785 -0.0068 -0.0159 -0.0305 221 LEU A CA  
3711 C C   . LEU B 224 ? 0.2827 0.1887 0.1864 -0.0086 -0.0216 -0.0314 221 LEU A C   
3712 O O   . LEU B 224 ? 0.2800 0.1776 0.1729 0.0004  -0.0258 -0.0349 221 LEU A O   
3713 C CB  . LEU B 224 ? 0.2755 0.1980 0.1867 -0.0066 -0.0108 -0.0272 221 LEU A CB  
3714 C CG  . LEU B 224 ? 0.2702 0.2070 0.1876 -0.0009 -0.0073 -0.0281 221 LEU A CG  
3715 C CD1 . LEU B 224 ? 0.2929 0.2225 0.2013 -0.0030 -0.0016 -0.0244 221 LEU A CD1 
3716 C CD2 . LEU B 224 ? 0.2660 0.2043 0.1791 0.0097  -0.0118 -0.0316 221 LEU A CD2 
3717 N N   . ARG B 225 ? 0.3012 0.1975 0.2042 -0.0200 -0.0217 -0.0279 222 ARG A N   
3718 C CA  . ARG B 225 ? 0.3421 0.2139 0.2298 -0.0241 -0.0281 -0.0286 222 ARG A CA  
3719 C C   . ARG B 225 ? 0.3301 0.2020 0.2172 -0.0208 -0.0350 -0.0339 222 ARG A C   
3720 O O   . ARG B 225 ? 0.3360 0.1866 0.2040 -0.0149 -0.0403 -0.0373 222 ARG A O   
3721 C CB  . ARG B 225 ? 0.3971 0.2623 0.2890 -0.0397 -0.0274 -0.0232 222 ARG A CB  
3722 C CG  . ARG B 225 ? 0.4755 0.3145 0.3534 -0.0470 -0.0358 -0.0240 222 ARG A CG  
3723 C CD  . ARG B 225 ? 0.5497 0.3803 0.4302 -0.0624 -0.0337 -0.0170 222 ARG A CD  
3724 N NE  . ARG B 225 ? 0.6693 0.4711 0.5347 -0.0706 -0.0430 -0.0177 222 ARG A NE  
3725 C CZ  . ARG B 225 ? 0.7670 0.5599 0.6364 -0.0873 -0.0438 -0.0116 222 ARG A CZ  
3726 N NH1 . ARG B 225 ? 0.8016 0.6117 0.6874 -0.0960 -0.0341 -0.0038 222 ARG A NH1 
3727 N NH2 . ARG B 225 ? 0.8254 0.5920 0.6819 -0.0956 -0.0542 -0.0132 222 ARG A NH2 
3728 N N   . ASP B 226 ? 0.3093 0.2033 0.2153 -0.0240 -0.0349 -0.0345 223 ASP A N   
3729 C CA  . ASP B 226 ? 0.3066 0.2002 0.2102 -0.0212 -0.0414 -0.0391 223 ASP A CA  
3730 C C   . ASP B 226 ? 0.2859 0.1787 0.1790 -0.0059 -0.0407 -0.0431 223 ASP A C   
3731 O O   . ASP B 226 ? 0.3106 0.1890 0.1884 -0.0006 -0.0458 -0.0472 223 ASP A O   
3732 C CB  . ASP B 226 ? 0.2980 0.2162 0.2236 -0.0262 -0.0412 -0.0381 223 ASP A CB  
3733 C CG  . ASP B 226 ? 0.3215 0.2449 0.2613 -0.0409 -0.0432 -0.0342 223 ASP A CG  
3734 O OD1 . ASP B 226 ? 0.3554 0.2616 0.2874 -0.0492 -0.0461 -0.0325 223 ASP A OD1 
3735 O OD2 . ASP B 226 ? 0.3724 0.3185 0.3325 -0.0437 -0.0416 -0.0324 223 ASP A OD2 
3736 N N   . ASN B 227 ? 0.2730 0.1812 0.1741 0.0010  -0.0347 -0.0421 224 ASN A N   
3737 C CA  . ASN B 227 ? 0.2653 0.1766 0.1606 0.0145  -0.0337 -0.0447 224 ASN A CA  
3738 C C   . ASN B 227 ? 0.2826 0.1702 0.1562 0.0223  -0.0360 -0.0463 224 ASN A C   
3739 O O   . ASN B 227 ? 0.2917 0.1726 0.1543 0.0321  -0.0379 -0.0498 224 ASN A O   
3740 C CB  . ASN B 227 ? 0.2514 0.1836 0.1611 0.0182  -0.0284 -0.0429 224 ASN A CB  
3741 C CG  . ASN B 227 ? 0.2372 0.1912 0.1651 0.0152  -0.0264 -0.0424 224 ASN A CG  
3742 O OD1 . ASN B 227 ? 0.2460 0.2017 0.1768 0.0111  -0.0291 -0.0431 224 ASN A OD1 
3743 N ND2 . ASN B 227 ? 0.2292 0.1983 0.1682 0.0176  -0.0227 -0.0411 224 ASN A ND2 
3744 N N   . LEU B 228 ? 0.2909 0.1649 0.1574 0.0184  -0.0357 -0.0436 225 LEU A N   
3745 C CA  . LEU B 228 ? 0.3266 0.1742 0.1705 0.0253  -0.0387 -0.0445 225 LEU A CA  
3746 C C   . LEU B 228 ? 0.3506 0.1747 0.1772 0.0253  -0.0448 -0.0482 225 LEU A C   
3747 O O   . LEU B 228 ? 0.3562 0.1649 0.1654 0.0377  -0.0469 -0.0514 225 LEU A O   
3748 C CB  . LEU B 228 ? 0.3442 0.1795 0.1824 0.0187  -0.0371 -0.0398 225 LEU A CB  
3749 C CG  . LEU B 228 ? 0.3394 0.1909 0.1863 0.0227  -0.0324 -0.0373 225 LEU A CG  
3750 C CD1 . LEU B 228 ? 0.3558 0.1985 0.1983 0.0144  -0.0293 -0.0321 225 LEU A CD1 
3751 C CD2 . LEU B 228 ? 0.3543 0.2043 0.1929 0.0384  -0.0342 -0.0393 225 LEU A CD2 
3752 N N   . THR B 229 ? 0.3473 0.1691 0.1787 0.0119  -0.0480 -0.0479 226 THR A N   
3753 C CA  . THR B 229 ? 0.3724 0.1700 0.1867 0.0093  -0.0557 -0.0516 226 THR A CA  
3754 C C   . THR B 229 ? 0.3697 0.1716 0.1780 0.0211  -0.0570 -0.0571 226 THR A C   
3755 O O   . THR B 229 ? 0.4001 0.1775 0.1845 0.0304  -0.0610 -0.0616 226 THR A O   
3756 C CB  . THR B 229 ? 0.3862 0.1847 0.2115 -0.0094 -0.0595 -0.0490 226 THR A CB  
3757 O OG1 . THR B 229 ? 0.3940 0.1854 0.2208 -0.0183 -0.0566 -0.0432 226 THR A OG1 
3758 C CG2 . THR B 229 ? 0.4197 0.1915 0.2274 -0.0148 -0.0698 -0.0529 226 THR A CG2 
3759 N N   . LEU B 230 ? 0.3465 0.1775 0.1748 0.0207  -0.0534 -0.0564 227 LEU A N   
3760 C CA  . LEU B 230 ? 0.3440 0.1851 0.1705 0.0312  -0.0522 -0.0597 227 LEU A CA  
3761 C C   . LEU B 230 ? 0.3409 0.1786 0.1558 0.0487  -0.0481 -0.0616 227 LEU A C   
3762 O O   . LEU B 230 ? 0.3504 0.1735 0.1463 0.0589  -0.0498 -0.0658 227 LEU A O   
3763 C CB  . LEU B 230 ? 0.3168 0.1901 0.1686 0.0273  -0.0477 -0.0568 227 LEU A CB  
3764 C CG  . LEU B 230 ? 0.3273 0.2141 0.1796 0.0372  -0.0449 -0.0585 227 LEU A CG  
3765 C CD1 . LEU B 230 ? 0.3512 0.2217 0.1859 0.0371  -0.0516 -0.0627 227 LEU A CD1 
3766 C CD2 . LEU B 230 ? 0.2930 0.2089 0.1697 0.0334  -0.0403 -0.0549 227 LEU A CD2 
3767 N N   . TRP B 231 ? 0.3324 0.1820 0.1577 0.0523  -0.0433 -0.0584 228 TRP A N   
3768 C CA  . TRP B 231 ? 0.3421 0.1968 0.1636 0.0688  -0.0394 -0.0591 228 TRP A CA  
3769 C C   . TRP B 231 ? 0.3713 0.1954 0.1663 0.0791  -0.0428 -0.0621 228 TRP A C   
3770 O O   . TRP B 231 ? 0.3986 0.2198 0.1828 0.0938  -0.0410 -0.0651 228 TRP A O   
3771 C CB  . TRP B 231 ? 0.3161 0.1930 0.1573 0.0681  -0.0354 -0.0548 228 TRP A CB  
3772 C CG  . TRP B 231 ? 0.3045 0.2108 0.1693 0.0625  -0.0315 -0.0526 228 TRP A CG  
3773 C CD1 . TRP B 231 ? 0.2999 0.2196 0.1719 0.0619  -0.0297 -0.0533 228 TRP A CD1 
3774 C CD2 . TRP B 231 ? 0.2893 0.2134 0.1720 0.0571  -0.0291 -0.0492 228 TRP A CD2 
3775 N NE1 . TRP B 231 ? 0.2695 0.2131 0.1631 0.0563  -0.0265 -0.0502 228 TRP A NE1 
3776 C CE2 . TRP B 231 ? 0.2720 0.2185 0.1724 0.0533  -0.0262 -0.0481 228 TRP A CE2 
3777 C CE3 . TRP B 231 ? 0.2973 0.2179 0.1800 0.0556  -0.0295 -0.0471 228 TRP A CE3 
3778 C CZ2 . TRP B 231 ? 0.2657 0.2302 0.1837 0.0485  -0.0239 -0.0455 228 TRP A CZ2 
3779 C CZ3 . TRP B 231 ? 0.2835 0.2222 0.1828 0.0504  -0.0272 -0.0447 228 TRP A CZ3 
3780 C CH2 . TRP B 231 ? 0.2597 0.2196 0.1765 0.0469  -0.0246 -0.0441 228 TRP A CH2 
3781 N N   . THR B 232 ? 0.3829 0.1821 0.1659 0.0714  -0.0475 -0.0612 229 THR A N   
3782 C CA  . THR B 232 ? 0.4249 0.1912 0.1814 0.0807  -0.0513 -0.0634 229 THR A CA  
3783 C C   . THR B 232 ? 0.4557 0.1926 0.1887 0.0798  -0.0574 -0.0687 229 THR A C   
3784 O O   . THR B 232 ? 0.4641 0.1815 0.1752 0.0950  -0.0584 -0.0729 229 THR A O   
3785 C CB  . THR B 232 ? 0.4369 0.1881 0.1897 0.0723  -0.0533 -0.0591 229 THR A CB  
3786 O OG1 . THR B 232 ? 0.4306 0.1781 0.1896 0.0525  -0.0558 -0.0569 229 THR A OG1 
3787 C CG2 . THR B 232 ? 0.4089 0.1858 0.1802 0.0755  -0.0484 -0.0547 229 THR A CG2 
3788 N N   . GLY B 233 ? 0.4559 0.1916 0.1944 0.0628  -0.0616 -0.0686 230 GLY A N   
3789 C CA  . GLY B 233 ? 0.4874 0.1933 0.2040 0.0581  -0.0700 -0.0734 230 GLY A CA  
3790 C C   . GLY B 233 ? 0.4939 0.2062 0.2050 0.0654  -0.0703 -0.0784 230 GLY A C   
3791 O O   . GLY B 233 ? 0.5177 0.2009 0.2032 0.0678  -0.0771 -0.0840 230 GLY A O   
3792 N N   . GLY B 234 ? 0.4672 0.2154 0.2006 0.0684  -0.0632 -0.0763 231 GLY A N   
3793 C CA  . GLY B 234 ? 0.4876 0.2448 0.2176 0.0740  -0.0623 -0.0795 231 GLY A CA  
3794 C C   . GLY B 234 ? 0.4752 0.2433 0.2192 0.0570  -0.0674 -0.0782 231 GLY A C   
3795 O O   . GLY B 234 ? 0.4607 0.2251 0.2141 0.0407  -0.0728 -0.0757 231 GLY A O   
3796 N N   . GLY B 235 ? 0.4859 0.2696 0.2327 0.0615  -0.0651 -0.0791 232 GLY A N   
3797 C CA  . GLY B 235 ? 0.4802 0.2774 0.2409 0.0484  -0.0697 -0.0776 232 GLY A CA  
3798 C C   . GLY B 235 ? 0.4574 0.2815 0.2290 0.0557  -0.0624 -0.0757 232 GLY A C   
3799 O O   . GLY B 235 ? 0.4469 0.2897 0.2289 0.0654  -0.0525 -0.0730 232 GLY A O   
3800 N N   . GLY B 236 ? 0.5045 0.3328 0.2781 0.0482  -0.0682 -0.0759 233 GLY A N   
3801 C CA  . GLY B 236 ? 0.4998 0.3491 0.2802 0.0532  -0.0633 -0.0737 233 GLY A CA  
3802 C C   . GLY B 236 ? 0.4825 0.3629 0.2964 0.0438  -0.0596 -0.0673 233 GLY A C   
3803 O O   . GLY B 236 ? 0.4830 0.3830 0.3061 0.0488  -0.0528 -0.0641 233 GLY A O   
3804 N N   . SER B 237 ? 0.4469 0.3315 0.2785 0.0311  -0.0629 -0.0651 234 SER A N   
3805 C CA  . SER B 237 ? 0.4148 0.3248 0.2747 0.0221  -0.0611 -0.0600 234 SER A CA  
3806 C C   . SER B 237 ? 0.3618 0.2928 0.2391 0.0272  -0.0501 -0.0561 234 SER A C   
3807 O O   . SER B 237 ? 0.3290 0.2560 0.1999 0.0355  -0.0448 -0.0568 234 SER A O   
3808 C CB  . SER B 237 ? 0.4344 0.3422 0.3062 0.0076  -0.0678 -0.0588 234 SER A CB  
3809 O OG  . SER B 237 ? 0.5027 0.4061 0.3778 0.0060  -0.0636 -0.0576 234 SER A OG  
3810 N N   . ARG B 238 ? 0.3253 0.2776 0.2240 0.0223  -0.0477 -0.0520 235 ARG A N   
3811 C CA  . ARG B 238 ? 0.2979 0.2693 0.2132 0.0255  -0.0390 -0.0484 235 ARG A CA  
3812 C C   . ARG B 238 ? 0.2818 0.2546 0.2080 0.0198  -0.0374 -0.0473 235 ARG A C   
3813 O O   . ARG B 238 ? 0.2535 0.2273 0.1887 0.0105  -0.0406 -0.0462 235 ARG A O   
3814 C CB  . ARG B 238 ? 0.2968 0.2863 0.2268 0.0238  -0.0373 -0.0448 235 ARG A CB  
3815 C CG  . ARG B 238 ? 0.2583 0.2647 0.2034 0.0265  -0.0293 -0.0413 235 ARG A CG  
3816 C CD  . ARG B 238 ? 0.2510 0.2714 0.2079 0.0251  -0.0280 -0.0375 235 ARG A CD  
3817 N NE  . ARG B 238 ? 0.2158 0.2495 0.1887 0.0246  -0.0223 -0.0345 235 ARG A NE  
3818 C CZ  . ARG B 238 ? 0.2008 0.2410 0.1756 0.0295  -0.0168 -0.0330 235 ARG A CZ  
3819 N NH1 . ARG B 238 ? 0.2156 0.2526 0.1785 0.0366  -0.0145 -0.0336 235 ARG A NH1 
3820 N NH2 . ARG B 238 ? 0.2178 0.2676 0.2066 0.0273  -0.0139 -0.0309 235 ARG A NH2 
3821 N N   . ARG B 239 ? 0.2620 0.2377 0.1890 0.0259  -0.0319 -0.0468 236 ARG A N   
3822 C CA  . ARG B 239 ? 0.2488 0.2261 0.1841 0.0218  -0.0298 -0.0454 236 ARG A CA  
3823 C C   . ARG B 239 ? 0.2274 0.2200 0.1820 0.0144  -0.0279 -0.0424 236 ARG A C   
3824 O O   . ARG B 239 ? 0.2165 0.2220 0.1808 0.0148  -0.0267 -0.0408 236 ARG A O   
3825 C CB  . ARG B 239 ? 0.2436 0.2237 0.1774 0.0304  -0.0256 -0.0453 236 ARG A CB  
3826 C CG  . ARG B 239 ? 0.2215 0.2214 0.1700 0.0335  -0.0209 -0.0429 236 ARG A CG  
3827 C CD  . ARG B 239 ? 0.2254 0.2365 0.1790 0.0351  -0.0193 -0.0415 236 ARG A CD  
3828 N NE  . ARG B 239 ? 0.2113 0.2398 0.1807 0.0346  -0.0155 -0.0383 236 ARG A NE  
3829 C CZ  . ARG B 239 ? 0.1990 0.2351 0.1814 0.0281  -0.0153 -0.0366 236 ARG A CZ  
3830 N NH1 . ARG B 239 ? 0.1830 0.2306 0.1767 0.0282  -0.0129 -0.0344 236 ARG A NH1 
3831 N NH2 . ARG B 239 ? 0.1904 0.2225 0.1748 0.0217  -0.0177 -0.0369 236 ARG A NH2 
3832 N N   . GLY B 240 ? 0.2168 0.2068 0.1756 0.0086  -0.0270 -0.0412 237 GLY A N   
3833 C CA  . GLY B 240 ? 0.1939 0.1968 0.1690 0.0031  -0.0239 -0.0385 237 GLY A CA  
3834 C C   . GLY B 240 ? 0.1907 0.2011 0.1708 0.0071  -0.0190 -0.0378 237 GLY A C   
3835 O O   . GLY B 240 ? 0.1996 0.2025 0.1707 0.0113  -0.0185 -0.0387 237 GLY A O   
3836 N N   . TPO B 241 ? 0.1760 0.1995 0.1691 0.0065  -0.0166 -0.0365 238 TPO A N   
3837 C CA  . TPO B 241 ? 0.1667 0.1944 0.1640 0.0079  -0.0130 -0.0361 238 TPO A CA  
3838 C CB  . TPO B 241 ? 0.1648 0.2005 0.1667 0.0123  -0.0129 -0.0361 238 TPO A CB  
3839 C CG2 . TPO B 241 ? 0.1789 0.2123 0.1736 0.0177  -0.0142 -0.0370 238 TPO A CG2 
3840 O OG1 . TPO B 241 ? 0.1515 0.1950 0.1612 0.0116  -0.0133 -0.0348 238 TPO A OG1 
3841 P P   . TPO B 241 ? 0.1703 0.2223 0.1875 0.0135  -0.0125 -0.0332 238 TPO A P   
3842 O O1P . TPO B 241 ? 0.1400 0.1959 0.1626 0.0119  -0.0133 -0.0315 238 TPO A O1P 
3843 O O2P . TPO B 241 ? 0.1638 0.2159 0.1845 0.0129  -0.0112 -0.0338 238 TPO A O2P 
3844 O O3P . TPO B 241 ? 0.1503 0.2039 0.1630 0.0177  -0.0127 -0.0329 238 TPO A O3P 
3845 C C   . TPO B 241 ? 0.1771 0.2096 0.1833 0.0035  -0.0098 -0.0345 238 TPO A C   
3846 O O   . TPO B 241 ? 0.1685 0.2044 0.1811 -0.0009 -0.0103 -0.0332 238 TPO A O   
3847 N N   . SER B 242 ? 0.1615 0.1945 0.1679 0.0051  -0.0064 -0.0347 239 SER A N   
3848 C CA  . SER B 242 ? 0.1833 0.2180 0.1935 0.0027  -0.0016 -0.0335 239 SER A CA  
3849 C C   . SER B 242 ? 0.1694 0.2157 0.1940 0.0020  -0.0005 -0.0321 239 SER A C   
3850 O O   . SER B 242 ? 0.1446 0.1952 0.1736 0.0048  -0.0026 -0.0327 239 SER A O   
3851 C CB  . SER B 242 ? 0.2105 0.2402 0.2135 0.0062  0.0009  -0.0348 239 SER A CB  
3852 O OG  . SER B 242 ? 0.2460 0.2761 0.2498 0.0051  0.0070  -0.0335 239 SER A OG  
3853 N N   . PRO B 243 ? 0.1925 0.2444 0.2250 -0.0013 0.0033  -0.0298 240 PRO A N   
3854 C CA  . PRO B 243 ? 0.1986 0.2625 0.2452 0.0003  0.0054  -0.0285 240 PRO A CA  
3855 C C   . PRO B 243 ? 0.1938 0.2550 0.2372 0.0063  0.0087  -0.0303 240 PRO A C   
3856 O O   . PRO B 243 ? 0.1841 0.2358 0.2154 0.0079  0.0108  -0.0322 240 PRO A O   
3857 C CB  . PRO B 243 ? 0.2067 0.2783 0.2627 -0.0039 0.0100  -0.0252 240 PRO A CB  
3858 C CG  . PRO B 243 ? 0.2154 0.2755 0.2579 -0.0062 0.0134  -0.0251 240 PRO A CG  
3859 C CD  . PRO B 243 ? 0.2050 0.2533 0.2347 -0.0062 0.0067  -0.0277 240 PRO A CD  
3860 N N   . ALA B 244 ? 0.1850 0.2526 0.2374 0.0095  0.0079  -0.0300 241 ALA A N   
3861 C CA  . ALA B 244 ? 0.1974 0.2603 0.2467 0.0150  0.0104  -0.0319 241 ALA A CA  
3862 C C   . ALA B 244 ? 0.1915 0.2541 0.2391 0.0182  0.0185  -0.0320 241 ALA A C   
3863 O O   . ALA B 244 ? 0.1915 0.2436 0.2275 0.0220  0.0208  -0.0348 241 ALA A O   
3864 C CB  . ALA B 244 ? 0.1901 0.2582 0.2488 0.0179  0.0076  -0.0307 241 ALA A CB  
3865 N N   . ARG B 245 ? 0.2125 0.2871 0.2717 0.0165  0.0229  -0.0287 242 ARG A N   
3866 C CA  . ARG B 245 ? 0.2291 0.3070 0.2888 0.0193  0.0326  -0.0274 242 ARG A CA  
3867 C C   . ARG B 245 ? 0.2281 0.3025 0.2808 0.0130  0.0352  -0.0255 242 ARG A C   
3868 O O   . ARG B 245 ? 0.2513 0.3343 0.3143 0.0062  0.0337  -0.0222 242 ARG A O   
3869 C CB  . ARG B 245 ? 0.2391 0.3352 0.3197 0.0217  0.0352  -0.0240 242 ARG A CB  
3870 C CG  . ARG B 245 ? 0.2420 0.3471 0.3282 0.0250  0.0467  -0.0213 242 ARG A CG  
3871 C CD  . ARG B 245 ? 0.2579 0.3828 0.3662 0.0302  0.0498  -0.0180 242 ARG A CD  
3872 N NE  . ARG B 245 ? 0.2607 0.3802 0.3662 0.0411  0.0496  -0.0210 242 ARG A NE  
3873 C CZ  . ARG B 245 ? 0.2344 0.3590 0.3504 0.0445  0.0429  -0.0206 242 ARG A CZ  
3874 N NH1 . ARG B 245 ? 0.2022 0.3341 0.3278 0.0374  0.0337  -0.0186 242 ARG A NH1 
3875 N NH2 . ARG B 245 ? 0.2343 0.3550 0.3493 0.0555  0.0451  -0.0222 242 ARG A NH2 
3876 N N   . MET B 246 ? 0.2290 0.2888 0.2627 0.0148  0.0376  -0.0278 243 MET A N   
3877 C CA  . MET B 246 ? 0.2402 0.2923 0.2630 0.0097  0.0390  -0.0261 243 MET A CA  
3878 C C   . MET B 246 ? 0.2783 0.3352 0.3020 0.0092  0.0507  -0.0218 243 MET A C   
3879 O O   . MET B 246 ? 0.2427 0.3015 0.2690 0.0018  0.0524  -0.0175 243 MET A O   
3880 C CB  . MET B 246 ? 0.2438 0.2784 0.2457 0.0121  0.0347  -0.0300 243 MET A CB  
3881 C CG  . MET B 246 ? 0.2561 0.2893 0.2600 0.0103  0.0244  -0.0321 243 MET A CG  
3882 S SD  . MET B 246 ? 0.3031 0.3216 0.2893 0.0141  0.0181  -0.0366 243 MET A SD  
3883 C CE  . MET B 246 ? 0.2881 0.3079 0.2789 0.0188  0.0172  -0.0397 243 MET A CE  
3884 N N   . ALA B 247 ? 0.2909 0.3481 0.3106 0.0171  0.0589  -0.0228 244 ALA A N   
3885 C CA  . ALA B 247 ? 0.3597 0.4205 0.3768 0.0187  0.0721  -0.0187 244 ALA A CA  
3886 C C   . ALA B 247 ? 0.4342 0.5099 0.4658 0.0266  0.0798  -0.0180 244 ALA A C   
3887 O O   . ALA B 247 ? 0.4797 0.5483 0.5051 0.0349  0.0773  -0.0231 244 ALA A O   
3888 C CB  . ALA B 247 ? 0.3709 0.4108 0.3589 0.0230  0.0754  -0.0210 244 ALA A CB  
3889 N N   . GLY B 248 ? 0.5102 0.6064 0.5622 0.0236  0.0883  -0.0115 245 GLY A N   
3890 C CA  . GLY B 248 ? 0.5719 0.6836 0.6365 0.0330  0.0992  -0.0097 245 GLY A CA  
3891 C C   . GLY B 248 ? 0.5652 0.6886 0.6487 0.0378  0.0923  -0.0117 245 GLY A C   
3892 O O   . GLY B 248 ? 0.6042 0.7291 0.6962 0.0312  0.0800  -0.0125 245 GLY A O   
3893 N N   . ASN B 249 ? 0.5877 0.7176 0.6753 0.0504  0.1005  -0.0124 246 ASN A N   
3894 C CA  . ASN B 249 ? 0.5732 0.7150 0.6790 0.0573  0.0961  -0.0131 246 ASN A CA  
3895 C C   . ASN B 249 ? 0.5559 0.6770 0.6472 0.0596  0.0835  -0.0199 246 ASN A C   
3896 O O   . ASN B 249 ? 0.4813 0.6108 0.5879 0.0590  0.0748  -0.0193 246 ASN A O   
3897 C CB  . ASN B 249 ? 0.5769 0.7288 0.6885 0.0719  0.1092  -0.0122 246 ASN A CB  
3898 O OXT . ASN B 249 ? 0.4386 0.5362 0.5041 0.0620  0.0826  -0.0251 246 ASN A OXT 
3899 C C1  . EDO C .   ? 0.5314 0.6149 0.4844 -0.1099 -0.0053 0.0433  301 EDO B C1  
3900 O O1  . EDO C .   ? 0.5474 0.6137 0.4896 -0.1232 -0.0064 0.0459  301 EDO B O1  
3901 C C2  . EDO C .   ? 0.5231 0.6318 0.4826 -0.1170 -0.0081 0.0414  301 EDO B C2  
3902 O O2  . EDO C .   ? 0.4970 0.6340 0.4679 -0.1257 -0.0058 0.0440  301 EDO B O2  
3903 C C1  . EDO D .   ? 0.5250 0.4575 0.6865 -0.0934 -0.0267 0.1359  302 EDO B C1  
3904 O O1  . EDO D .   ? 0.5689 0.5167 0.7408 -0.1115 -0.0231 0.1406  302 EDO B O1  
3905 C C2  . EDO D .   ? 0.5328 0.4614 0.6997 -0.0810 -0.0316 0.1182  302 EDO B C2  
3906 O O2  . EDO D .   ? 0.4756 0.4295 0.6424 -0.0699 -0.0249 0.1084  302 EDO B O2  
3907 C C1  . EDO E .   ? 0.6388 0.7462 0.5708 -0.0757 0.0291  0.2028  303 EDO B C1  
3908 O O1  . EDO E .   ? 0.6992 0.8292 0.6130 -0.0817 0.0387  0.1990  303 EDO B O1  
3909 C C2  . EDO E .   ? 0.6269 0.7177 0.5539 -0.0854 0.0225  0.2230  303 EDO B C2  
3910 O O2  . EDO E .   ? 0.6300 0.7091 0.5414 -0.0843 0.0104  0.2363  303 EDO B O2  
3911 C C1  . EDO F .   ? 0.4015 0.4404 0.4334 0.0166  -0.0022 0.0302  304 EDO B C1  
3912 O O1  . EDO F .   ? 0.2898 0.3371 0.3171 0.0159  0.0020  0.0266  304 EDO B O1  
3913 C C2  . EDO F .   ? 0.3878 0.4211 0.4117 0.0151  -0.0080 0.0294  304 EDO B C2  
3914 O O2  . EDO F .   ? 0.4696 0.5005 0.4765 0.0104  -0.0087 0.0324  304 EDO B O2  
3915 C C1  . EDO G .   ? 0.3053 0.4003 0.2216 -0.0027 0.0460  -0.0051 305 EDO B C1  
3916 O O1  . EDO G .   ? 0.2981 0.3955 0.2085 0.0030  0.0524  -0.0202 305 EDO B O1  
3917 C C2  . EDO G .   ? 0.3377 0.4469 0.2457 -0.0105 0.0450  0.0063  305 EDO B C2  
3918 O O2  . EDO G .   ? 0.3203 0.4483 0.2228 -0.0119 0.0526  0.0096  305 EDO B O2  
3919 C C1  . EDO H .   ? 0.4352 0.5828 0.5120 0.0459  0.0261  -0.0089 306 EDO B C1  
3920 O O1  . EDO H .   ? 0.3817 0.5243 0.4697 0.0581  0.0231  -0.0177 306 EDO B O1  
3921 C C2  . EDO H .   ? 0.4687 0.6291 0.5315 0.0373  0.0321  -0.0129 306 EDO B C2  
3922 O O2  . EDO H .   ? 0.5463 0.7349 0.6142 0.0366  0.0381  -0.0178 306 EDO B O2  
3923 C C1  . PEG I .   ? 0.2684 0.3032 0.3323 0.0349  0.0024  0.0372  307 PEG B C1  
3924 O O1  . PEG I .   ? 0.2729 0.3165 0.3392 0.0347  0.0090  0.0358  307 PEG B O1  
3925 C C2  . PEG I .   ? 0.3055 0.3407 0.3660 0.0292  0.0031  0.0412  307 PEG B C2  
3926 O O2  . PEG I .   ? 0.4544 0.4799 0.5060 0.0277  -0.0025 0.0422  307 PEG B O2  
3927 C C3  . PEG I .   ? 0.4865 0.5154 0.5399 0.0248  -0.0027 0.0433  307 PEG B C3  
3928 C C4  . PEG I .   ? 0.6363 0.6648 0.6950 0.0268  -0.0087 0.0419  307 PEG B C4  
3929 O O4  . PEG I .   ? 0.6161 0.6467 0.6756 0.0241  -0.0092 0.0412  307 PEG B O4  
3930 C C1  . EDO J .   ? 0.5302 0.8749 0.6268 -0.0711 0.1396  0.0772  308 EDO B C1  
3931 O O1  . EDO J .   ? 0.5115 0.8479 0.6010 -0.0539 0.1376  0.0620  308 EDO B O1  
3932 C C2  . EDO J .   ? 0.5439 0.8579 0.6264 -0.0810 0.1297  0.0964  308 EDO B C2  
3933 O O2  . EDO J .   ? 0.5589 0.8483 0.6188 -0.0749 0.1227  0.0986  308 EDO B O2  
3934 C C1  . EDO K .   ? 0.5812 0.6191 0.5110 0.0097  0.0589  0.1070  301 EDO A C1  
3935 O O1  . EDO K .   ? 0.6806 0.7015 0.6136 0.0045  0.0501  0.1089  301 EDO A O1  
3936 C C2  . EDO K .   ? 0.6446 0.6790 0.5477 0.0170  0.0683  0.1151  301 EDO A C2  
3937 O O2  . EDO K .   ? 0.5709 0.6119 0.4595 0.0281  0.0704  0.1076  301 EDO A O2  
3938 C C1  . EDO L .   ? 0.5956 0.5850 0.5117 0.0766  -0.0726 -0.0396 302 EDO A C1  
3939 O O1  . EDO L .   ? 0.4987 0.5094 0.4384 0.0703  -0.0714 -0.0404 302 EDO A O1  
3940 C C2  . EDO L .   ? 0.5872 0.5600 0.4903 0.0750  -0.0633 -0.0389 302 EDO A C2  
3941 O O2  . EDO L .   ? 0.6991 0.6669 0.5976 0.0840  -0.0629 -0.0376 302 EDO A O2  
3942 C C1  . EDO M .   ? 0.6855 0.5820 0.6240 -0.0860 0.0009  0.0059  303 EDO A C1  
3943 O O1  . EDO M .   ? 0.6412 0.5535 0.5898 -0.0778 -0.0044 -0.0011 303 EDO A O1  
3944 C C2  . EDO M .   ? 0.6207 0.5304 0.5631 -0.0831 0.0143  0.0109  303 EDO A C2  
3945 O O2  . EDO M .   ? 0.6719 0.5741 0.6124 -0.0947 0.0216  0.0199  303 EDO A O2  
3946 C C1  . EDO N .   ? 0.6048 0.7948 0.6721 0.0597  0.0439  0.0124  304 EDO A C1  
3947 O O1  . EDO N .   ? 0.6683 0.8793 0.7612 0.0512  0.0460  0.0200  304 EDO A O1  
3948 C C2  . EDO N .   ? 0.5993 0.7753 0.6485 0.0586  0.0468  0.0137  304 EDO A C2  
3949 O O2  . EDO N .   ? 0.5563 0.7417 0.6005 0.0649  0.0583  0.0202  304 EDO A O2  
3950 C C1  . EDO O .   ? 0.6609 0.6564 0.6984 -0.0019 -0.0150 0.0252  305 EDO A C1  
3951 O O1  . EDO O .   ? 0.5960 0.5898 0.6403 -0.0098 -0.0157 0.0230  305 EDO A O1  
3952 C C2  . EDO O .   ? 0.6827 0.6598 0.7131 0.0024  -0.0183 0.0280  305 EDO A C2  
3953 O O2  . EDO O .   ? 0.7317 0.7038 0.7630 0.0094  -0.0214 0.0206  305 EDO A O2  
3954 C C1  . PEG P .   ? 0.7132 0.6085 0.5205 0.0442  -0.1233 -0.0727 306 PEG A C1  
3955 O O1  . PEG P .   ? 0.6950 0.6168 0.5377 0.0402  -0.1196 -0.0690 306 PEG A O1  
3956 C C2  . PEG P .   ? 0.7096 0.5899 0.4959 0.0483  -0.1063 -0.0712 306 PEG A C2  
3957 O O2  . PEG P .   ? 0.7130 0.5715 0.4650 0.0552  -0.1085 -0.0712 306 PEG A O2  
3958 C C3  . PEG P .   ? 0.6885 0.5473 0.4359 0.0600  -0.1036 -0.0654 306 PEG A C3  
3959 C C4  . PEG P .   ? 0.6996 0.5709 0.4598 0.0625  -0.1190 -0.0640 306 PEG A C4  
3960 O O4  . PEG P .   ? 0.7052 0.5747 0.4599 0.0684  -0.1152 -0.0586 306 PEG A O4  
3961 C C1  . EDO Q .   ? 0.6129 0.3972 0.4314 -0.0230 -0.0293 -0.0189 307 EDO A C1  
3962 O O1  . EDO Q .   ? 0.5966 0.3656 0.3962 -0.0080 -0.0330 -0.0220 307 EDO A O1  
3963 C C2  . EDO Q .   ? 0.6490 0.4129 0.4598 -0.0376 -0.0283 -0.0123 307 EDO A C2  
3964 O O2  . EDO Q .   ? 0.6738 0.4199 0.4803 -0.0473 -0.0357 -0.0133 307 EDO A O2  
3965 C C1  . PEG R .   ? 0.4725 0.5195 0.4778 0.0065  -0.0359 -0.0312 308 PEG A C1  
3966 O O1  . PEG R .   ? 0.4611 0.5166 0.4825 0.0021  -0.0351 -0.0299 308 PEG A O1  
3967 C C2  . PEG R .   ? 0.4573 0.5030 0.4588 0.0105  -0.0292 -0.0316 308 PEG A C2  
3968 O O2  . PEG R .   ? 0.4140 0.4548 0.4146 0.0084  -0.0275 -0.0337 308 PEG A O2  
3969 C C3  . PEG R .   ? 0.5095 0.5372 0.4956 0.0083  -0.0309 -0.0366 308 PEG A C3  
3970 C C4  . PEG R .   ? 0.4498 0.4717 0.4378 0.0015  -0.0331 -0.0373 308 PEG A C4  
3971 O O4  . PEG R .   ? 0.5212 0.5284 0.4956 -0.0009 -0.0393 -0.0398 308 PEG A O4  
3972 C C1  . PEG S .   ? 0.5376 0.6586 0.6950 -0.0593 -0.0443 0.0080  309 PEG A C1  
3973 O O1  . PEG S .   ? 0.5263 0.6191 0.6645 -0.0585 -0.0491 0.0011  309 PEG A O1  
3974 C C2  . PEG S .   ? 0.5159 0.6515 0.6809 -0.0564 -0.0503 0.0044  309 PEG A C2  
3975 O O2  . PEG S .   ? 0.5578 0.7236 0.7458 -0.0578 -0.0465 0.0120  309 PEG A O2  
3976 C C3  . PEG S .   ? 0.6179 0.7996 0.8232 -0.0623 -0.0563 0.0119  309 PEG A C3  
3977 C C4  . PEG S .   ? 0.5852 0.7557 0.7763 -0.0556 -0.0658 0.0021  309 PEG A C4  
3978 O O4  . PEG S .   ? 0.4919 0.6829 0.7005 -0.0566 -0.0741 0.0030  309 PEG A O4  
3979 C C1  . EDO T .   ? 0.3892 0.3951 0.3105 0.0557  -0.0146 -0.0427 310 EDO A C1  
3980 O O1  . EDO T .   ? 0.3931 0.4179 0.3337 0.0560  -0.0095 -0.0390 310 EDO A O1  
3981 C C2  . EDO T .   ? 0.4030 0.3882 0.3081 0.0576  -0.0192 -0.0473 310 EDO A C2  
3982 O O2  . EDO T .   ? 0.3011 0.2761 0.2080 0.0481  -0.0250 -0.0488 310 EDO A O2  
3983 C C1  . EDO U .   ? 0.2963 0.3598 0.3160 0.0161  -0.0183 -0.0231 311 EDO A C1  
3984 O O1  . EDO U .   ? 0.2063 0.2670 0.2164 0.0188  -0.0167 -0.0246 311 EDO A O1  
3985 C C2  . EDO U .   ? 0.3048 0.3678 0.3235 0.0157  -0.0233 -0.0222 311 EDO A C2  
3986 O O2  . EDO U .   ? 0.3726 0.4295 0.3788 0.0162  -0.0281 -0.0242 311 EDO A O2  
3987 C C1  . PEG V .   ? 0.4092 0.4320 0.3903 0.0334  0.0528  -0.0358 312 PEG A C1  
3988 O O1  . PEG V .   ? 0.3931 0.4309 0.3963 0.0289  0.0479  -0.0336 312 PEG A O1  
3989 C C2  . PEG V .   ? 0.4500 0.4735 0.4281 0.0424  0.0635  -0.0362 312 PEG A C2  
3990 O O2  . PEG V .   ? 0.4620 0.4656 0.4168 0.0497  0.0627  -0.0419 312 PEG A O2  
3991 C C3  . PEG V .   ? 0.4514 0.4470 0.4059 0.0503  0.0518  -0.0467 312 PEG A C3  
3992 C C4  . PEG V .   ? 0.4847 0.4644 0.4210 0.0472  0.0432  -0.0500 312 PEG A C4  
3993 O O4  . PEG V .   ? 0.4791 0.4413 0.3901 0.0531  0.0466  -0.0533 312 PEG A O4  
3994 C C1  . PEG W .   ? 0.7447 0.5365 0.5144 0.0072  -0.1035 -0.0797 313 PEG A C1  
3995 O O1  . PEG W .   ? 0.7083 0.5318 0.5127 -0.0025 -0.0997 -0.0731 313 PEG A O1  
3996 C C2  . PEG W .   ? 0.7578 0.5506 0.5108 0.0211  -0.1010 -0.0826 313 PEG A C2  
3997 O O2  . PEG W .   ? 0.8671 0.6262 0.5828 0.0317  -0.1049 -0.0897 313 PEG A O2  
3998 C C3  . PEG W .   ? 0.8534 0.5995 0.5575 0.0426  -0.0973 -0.0911 313 PEG A C3  
3999 C C4  . PEG W .   ? 0.8748 0.6134 0.5544 0.0633  -0.0897 -0.0948 313 PEG A C4  
4000 O O4  . PEG W .   ? 0.8740 0.6044 0.5468 0.0749  -0.0821 -0.0954 313 PEG A O4  
4001 C C1  . EDO X .   ? 0.5435 0.5802 0.6056 0.0573  -0.0374 0.0101  314 EDO A C1  
4002 O O1  . EDO X .   ? 0.5032 0.5355 0.5697 0.0591  -0.0322 0.0058  314 EDO A O1  
4003 C C2  . EDO X .   ? 0.4934 0.5449 0.5596 0.0513  -0.0373 0.0068  314 EDO A C2  
4004 O O2  . EDO X .   ? 0.4305 0.4954 0.5105 0.0527  -0.0353 0.0024  314 EDO A O2  
4005 C C1  A PEG Y .   ? 0.3281 0.4178 0.4046 0.0060  -0.0124 -0.0241 315 PEG A C1  
4006 O O1  A PEG Y .   ? 0.3372 0.4200 0.4044 0.0083  -0.0151 -0.0246 315 PEG A O1  
4007 C C2  A PEG Y .   ? 0.3003 0.3835 0.3695 0.0037  -0.0077 -0.0260 315 PEG A C2  
4008 O O2  A PEG Y .   ? 0.2278 0.3149 0.3030 0.0060  -0.0009 -0.0255 315 PEG A O2  
4009 C C3  A PEG Y .   ? 0.2192 0.3171 0.3066 0.0023  0.0007  -0.0229 315 PEG A C3  
4010 C C4  A PEG Y .   ? 0.1823 0.2877 0.2785 0.0071  0.0070  -0.0218 315 PEG A C4  
4011 O O4  A PEG Y .   ? 0.1785 0.2792 0.2680 0.0069  0.0145  -0.0223 315 PEG A O4  
# 
