data_9AWE
# 
_entry.id   9AWE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9AWE         pdb_00009awe 10.2210/pdb9awe/pdb 
WWPDB D_1000282156 ?            ?                   
# 
_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       2025-02-05 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9AWE 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              koss@bsd.uchicago.edu 
_pdbx_contact_author.name_first         Anthony 
_pdbx_contact_author.name_last          Kossiakoff 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3174-9359 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Slezak, T.'       1 0000-0002-2931-0331 
'Kossiakoff, A.A.' 2 0000-0003-3174-9359 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Protein Sci.' 
_citation.journal_id_ASTM           PRCIEI 
_citation.journal_id_CSD            0795 
_citation.journal_id_ISSN           1469-896X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            34 
_citation.language                  ? 
_citation.page_first                e70019 
_citation.page_last                 e70019 
_citation.title                     'Engineered protein G variants for multifunctional antibody-based assemblies.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/pro.70019 
_citation.pdbx_database_id_PubMed   39865354 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Slezak, T.'       1 0000-0002-2931-0331 
primary 
;O'Leary, K.M.
;
2 ?                   
primary 'Li, J.'           3 ?                   
primary 'Rohaim, A.'       4 ?                   
primary 'Davydova, E.K.'   5 ?                   
primary 'Kossiakoff, A.A.' 6 0000-0003-3174-9359 
# 
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 'Fab Heavy Chain'                    24177.943 1  ? ? ? ? 
2 polymer man 'Fab Light Chain'                    23397.936 1  ? ? ? ? 
3 polymer man 'Histone chaperone ASF1'             18244.432 1  ? ? ? ? 
4 polymer man 'Immunoglobulin G-binding protein G' 7090.834  1  ? ? ? ? 
5 water   nat water                                18.015    14 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
3 'Anti-silencing function protein 1,yASF1' 
4 'IgG-binding protein G'                   
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;EISEVQLVESGGGLVQPGGSLRLSCAASGFNVSYYSIHWVRQAPGKGLEWVASIYPYYGSTSYADSVKGRFTISADTSKN
TAYLQMNSLRAEDTAVYYCARGYGWALDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVS
WNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
;
;EISEVQLVESGGGLVQPGGSLRLSCAASGFNVSYYSIHWVRQAPGKGLEWVASIYPYYGSTSYADSVKGRFTISADTSKN
TAYLQMNSLRAEDTAVYYCARGYGWALDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVS
WNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
;
B ? 
2 'polypeptide(L)' no no 
;SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPSRFSGSRSGTDFTLTISSLQ
PEDFATYYCQQDGWSLITFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS
QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPSRFSGSRSGTDFTLTISSLQ
PEDFATYYCQQDGWSLITFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS
QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
D ? 
3 'polypeptide(L)' no no 
;SSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSILVGPVPVGVNKFVFSADPPS
AELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGL
E
;
;SSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSILVGPVPVGVNKFVFSADPPS
AELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGL
E
;
A ? 
4 'polypeptide(L)' no no TPAVTTYKLVINGRTLSGYTTTTAVDAATAEKVFKQYAFGNGVDGEWTYDDATKTFTVTEKPEKL 
TPAVTTYKLVINGRTLSGYTTTTAVDAATAEKVFKQYAFGNGVDGEWTYDDATKTFTVTEKPEKL C ? 
# 
_pdbx_entity_nonpoly.entity_id   5 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   ILE n 
1 3   SER n 
1 4   GLU n 
1 5   VAL n 
1 6   GLN n 
1 7   LEU n 
1 8   VAL n 
1 9   GLU n 
1 10  SER n 
1 11  GLY n 
1 12  GLY n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  GLN n 
1 17  PRO n 
1 18  GLY n 
1 19  GLY n 
1 20  SER n 
1 21  LEU n 
1 22  ARG n 
1 23  LEU n 
1 24  SER n 
1 25  CYS n 
1 26  ALA n 
1 27  ALA n 
1 28  SER n 
1 29  GLY n 
1 30  PHE n 
1 31  ASN n 
1 32  VAL n 
1 33  SER n 
1 34  TYR n 
1 35  TYR n 
1 36  SER n 
1 37  ILE n 
1 38  HIS n 
1 39  TRP n 
1 40  VAL n 
1 41  ARG n 
1 42  GLN n 
1 43  ALA n 
1 44  PRO n 
1 45  GLY n 
1 46  LYS n 
1 47  GLY n 
1 48  LEU n 
1 49  GLU n 
1 50  TRP n 
1 51  VAL n 
1 52  ALA n 
1 53  SER n 
1 54  ILE n 
1 55  TYR n 
1 56  PRO n 
1 57  TYR n 
1 58  TYR n 
1 59  GLY n 
1 60  SER n 
1 61  THR n 
1 62  SER n 
1 63  TYR n 
1 64  ALA n 
1 65  ASP n 
1 66  SER n 
1 67  VAL n 
1 68  LYS n 
1 69  GLY n 
1 70  ARG n 
1 71  PHE n 
1 72  THR n 
1 73  ILE n 
1 74  SER n 
1 75  ALA n 
1 76  ASP n 
1 77  THR n 
1 78  SER n 
1 79  LYS n 
1 80  ASN n 
1 81  THR n 
1 82  ALA n 
1 83  TYR n 
1 84  LEU n 
1 85  GLN n 
1 86  MET n 
1 87  ASN n 
1 88  SER n 
1 89  LEU n 
1 90  ARG n 
1 91  ALA n 
1 92  GLU n 
1 93  ASP n 
1 94  THR n 
1 95  ALA n 
1 96  VAL n 
1 97  TYR n 
1 98  TYR n 
1 99  CYS n 
1 100 ALA n 
1 101 ARG n 
1 102 GLY n 
1 103 TYR n 
1 104 GLY n 
1 105 TRP n 
1 106 ALA n 
1 107 LEU n 
1 108 ASP n 
1 109 TYR n 
1 110 TRP n 
1 111 GLY n 
1 112 GLN n 
1 113 GLY n 
1 114 THR n 
1 115 LEU n 
1 116 VAL n 
1 117 THR n 
1 118 VAL n 
1 119 SER n 
1 120 SER n 
1 121 ALA n 
1 122 SER n 
1 123 THR n 
1 124 LYS n 
1 125 GLY n 
1 126 PRO n 
1 127 SER n 
1 128 VAL n 
1 129 PHE n 
1 130 PRO n 
1 131 LEU n 
1 132 ALA n 
1 133 PRO n 
1 134 SER n 
1 135 SER n 
1 136 LYS n 
1 137 SER n 
1 138 THR n 
1 139 SER n 
1 140 GLY n 
1 141 GLY n 
1 142 THR n 
1 143 ALA n 
1 144 ALA n 
1 145 LEU n 
1 146 GLY n 
1 147 CYS n 
1 148 LEU n 
1 149 VAL n 
1 150 LYS n 
1 151 ASP n 
1 152 TYR n 
1 153 PHE n 
1 154 PRO n 
1 155 GLU n 
1 156 PRO n 
1 157 VAL n 
1 158 THR n 
1 159 VAL n 
1 160 SER n 
1 161 TRP n 
1 162 ASN n 
1 163 SER n 
1 164 GLY n 
1 165 ALA n 
1 166 LEU n 
1 167 THR n 
1 168 SER n 
1 169 GLY n 
1 170 VAL n 
1 171 HIS n 
1 172 THR n 
1 173 PHE n 
1 174 PRO n 
1 175 ALA n 
1 176 VAL n 
1 177 LEU n 
1 178 GLN n 
1 179 SER n 
1 180 SER n 
1 181 GLY n 
1 182 LEU n 
1 183 TYR n 
1 184 SER n 
1 185 LEU n 
1 186 SER n 
1 187 SER n 
1 188 VAL n 
1 189 VAL n 
1 190 THR n 
1 191 VAL n 
1 192 PRO n 
1 193 SER n 
1 194 SER n 
1 195 SER n 
1 196 LEU n 
1 197 GLY n 
1 198 THR n 
1 199 GLN n 
1 200 THR n 
1 201 TYR n 
1 202 ILE n 
1 203 CYS n 
1 204 ASN n 
1 205 VAL n 
1 206 ASN n 
1 207 HIS n 
1 208 LYS n 
1 209 PRO n 
1 210 SER n 
1 211 ASN n 
1 212 THR n 
1 213 LYS n 
1 214 VAL n 
1 215 ASP n 
1 216 LYS n 
1 217 LYS n 
1 218 VAL n 
1 219 GLU n 
1 220 PRO n 
1 221 LYS n 
1 222 SER n 
1 223 CYS n 
1 224 ASP n 
1 225 LYS n 
1 226 THR n 
1 227 HIS n 
1 228 THR n 
2 1   SER n 
2 2   ASP n 
2 3   ILE n 
2 4   GLN n 
2 5   MET n 
2 6   THR n 
2 7   GLN n 
2 8   SER n 
2 9   PRO n 
2 10  SER n 
2 11  SER n 
2 12  LEU n 
2 13  SER n 
2 14  ALA n 
2 15  SER n 
2 16  VAL n 
2 17  GLY n 
2 18  ASP n 
2 19  ARG n 
2 20  VAL n 
2 21  THR n 
2 22  ILE n 
2 23  THR n 
2 24  CYS n 
2 25  ARG n 
2 26  ALA n 
2 27  SER n 
2 28  GLN n 
2 29  SER n 
2 30  VAL n 
2 31  SER n 
2 32  SER n 
2 33  ALA n 
2 34  VAL n 
2 35  ALA n 
2 36  TRP n 
2 37  TYR n 
2 38  GLN n 
2 39  GLN n 
2 40  LYS n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  ALA n 
2 45  PRO n 
2 46  LYS n 
2 47  LEU n 
2 48  LEU n 
2 49  ILE n 
2 50  TYR n 
2 51  SER n 
2 52  ALA n 
2 53  SER n 
2 54  SER n 
2 55  LEU n 
2 56  TYR n 
2 57  SER n 
2 58  GLY n 
2 59  VAL n 
2 60  PRO n 
2 61  SER n 
2 62  ARG n 
2 63  PHE n 
2 64  SER n 
2 65  GLY n 
2 66  SER n 
2 67  ARG n 
2 68  SER n 
2 69  GLY n 
2 70  THR n 
2 71  ASP n 
2 72  PHE n 
2 73  THR n 
2 74  LEU n 
2 75  THR n 
2 76  ILE n 
2 77  SER n 
2 78  SER n 
2 79  LEU n 
2 80  GLN n 
2 81  PRO n 
2 82  GLU n 
2 83  ASP n 
2 84  PHE n 
2 85  ALA n 
2 86  THR n 
2 87  TYR n 
2 88  TYR n 
2 89  CYS n 
2 90  GLN n 
2 91  GLN n 
2 92  ASP n 
2 93  GLY n 
2 94  TRP n 
2 95  SER n 
2 96  LEU n 
2 97  ILE n 
2 98  THR n 
2 99  PHE n 
2 100 GLY n 
2 101 GLN n 
2 102 GLY n 
2 103 THR n 
2 104 LYS n 
2 105 VAL n 
2 106 GLU n 
2 107 ILE n 
2 108 LYS n 
2 109 ARG n 
2 110 THR n 
2 111 VAL n 
2 112 ALA n 
2 113 ALA n 
2 114 PRO n 
2 115 SER n 
2 116 VAL n 
2 117 PHE n 
2 118 ILE n 
2 119 PHE n 
2 120 PRO n 
2 121 PRO n 
2 122 SER n 
2 123 ASP n 
2 124 GLU n 
2 125 GLN n 
2 126 LEU n 
2 127 LYS n 
2 128 SER n 
2 129 GLY n 
2 130 THR n 
2 131 ALA n 
2 132 SER n 
2 133 VAL n 
2 134 VAL n 
2 135 CYS n 
2 136 LEU n 
2 137 LEU n 
2 138 ASN n 
2 139 ASN n 
2 140 PHE n 
2 141 TYR n 
2 142 PRO n 
2 143 ARG n 
2 144 GLU n 
2 145 ALA n 
2 146 LYS n 
2 147 VAL n 
2 148 GLN n 
2 149 TRP n 
2 150 LYS n 
2 151 VAL n 
2 152 ASP n 
2 153 ASN n 
2 154 ALA n 
2 155 LEU n 
2 156 GLN n 
2 157 SER n 
2 158 GLY n 
2 159 ASN n 
2 160 SER n 
2 161 GLN n 
2 162 GLU n 
2 163 SER n 
2 164 VAL n 
2 165 THR n 
2 166 GLU n 
2 167 GLN n 
2 168 ASP n 
2 169 SER n 
2 170 LYS n 
2 171 ASP n 
2 172 SER n 
2 173 THR n 
2 174 TYR n 
2 175 SER n 
2 176 LEU n 
2 177 SER n 
2 178 SER n 
2 179 THR n 
2 180 LEU n 
2 181 THR n 
2 182 LEU n 
2 183 SER n 
2 184 LYS n 
2 185 ALA n 
2 186 ASP n 
2 187 TYR n 
2 188 GLU n 
2 189 LYS n 
2 190 HIS n 
2 191 LYS n 
2 192 VAL n 
2 193 TYR n 
2 194 ALA n 
2 195 CYS n 
2 196 GLU n 
2 197 VAL n 
2 198 THR n 
2 199 HIS n 
2 200 GLN n 
2 201 GLY n 
2 202 LEU n 
2 203 SER n 
2 204 SER n 
2 205 PRO n 
2 206 VAL n 
2 207 THR n 
2 208 LYS n 
2 209 SER n 
2 210 PHE n 
2 211 ASN n 
2 212 ARG n 
2 213 GLY n 
2 214 GLU n 
2 215 CYS n 
3 1   SER n 
3 2   SER n 
3 3   ILE n 
3 4   VAL n 
3 5   SER n 
3 6   LEU n 
3 7   LEU n 
3 8   GLY n 
3 9   ILE n 
3 10  LYS n 
3 11  VAL n 
3 12  LEU n 
3 13  ASN n 
3 14  ASN n 
3 15  PRO n 
3 16  ALA n 
3 17  LYS n 
3 18  PHE n 
3 19  THR n 
3 20  ASP n 
3 21  PRO n 
3 22  TYR n 
3 23  GLU n 
3 24  PHE n 
3 25  GLU n 
3 26  ILE n 
3 27  THR n 
3 28  PHE n 
3 29  GLU n 
3 30  CYS n 
3 31  LEU n 
3 32  GLU n 
3 33  SER n 
3 34  LEU n 
3 35  LYS n 
3 36  HIS n 
3 37  ASP n 
3 38  LEU n 
3 39  GLU n 
3 40  TRP n 
3 41  LYS n 
3 42  LEU n 
3 43  THR n 
3 44  TYR n 
3 45  VAL n 
3 46  GLY n 
3 47  SER n 
3 48  SER n 
3 49  ARG n 
3 50  SER n 
3 51  LEU n 
3 52  ASP n 
3 53  HIS n 
3 54  ASP n 
3 55  GLN n 
3 56  GLU n 
3 57  LEU n 
3 58  ASP n 
3 59  SER n 
3 60  ILE n 
3 61  LEU n 
3 62  VAL n 
3 63  GLY n 
3 64  PRO n 
3 65  VAL n 
3 66  PRO n 
3 67  VAL n 
3 68  GLY n 
3 69  VAL n 
3 70  ASN n 
3 71  LYS n 
3 72  PHE n 
3 73  VAL n 
3 74  PHE n 
3 75  SER n 
3 76  ALA n 
3 77  ASP n 
3 78  PRO n 
3 79  PRO n 
3 80  SER n 
3 81  ALA n 
3 82  GLU n 
3 83  LEU n 
3 84  ILE n 
3 85  PRO n 
3 86  ALA n 
3 87  SER n 
3 88  GLU n 
3 89  LEU n 
3 90  VAL n 
3 91  SER n 
3 92  VAL n 
3 93  THR n 
3 94  VAL n 
3 95  ILE n 
3 96  LEU n 
3 97  LEU n 
3 98  SER n 
3 99  CYS n 
3 100 SER n 
3 101 TYR n 
3 102 ASP n 
3 103 GLY n 
3 104 ARG n 
3 105 GLU n 
3 106 PHE n 
3 107 VAL n 
3 108 ARG n 
3 109 VAL n 
3 110 GLY n 
3 111 TYR n 
3 112 TYR n 
3 113 VAL n 
3 114 ASN n 
3 115 ASN n 
3 116 GLU n 
3 117 TYR n 
3 118 ASP n 
3 119 GLU n 
3 120 GLU n 
3 121 GLU n 
3 122 LEU n 
3 123 ARG n 
3 124 GLU n 
3 125 ASN n 
3 126 PRO n 
3 127 PRO n 
3 128 ALA n 
3 129 LYS n 
3 130 VAL n 
3 131 GLN n 
3 132 VAL n 
3 133 ASP n 
3 134 HIS n 
3 135 ILE n 
3 136 VAL n 
3 137 ARG n 
3 138 ASN n 
3 139 ILE n 
3 140 LEU n 
3 141 ALA n 
3 142 GLU n 
3 143 LYS n 
3 144 PRO n 
3 145 ARG n 
3 146 VAL n 
3 147 THR n 
3 148 ARG n 
3 149 PHE n 
3 150 ASN n 
3 151 ILE n 
3 152 VAL n 
3 153 TRP n 
3 154 ASP n 
3 155 ASN n 
3 156 GLU n 
3 157 ASN n 
3 158 GLU n 
3 159 GLY n 
3 160 LEU n 
3 161 GLU n 
4 1   THR n 
4 2   PRO n 
4 3   ALA n 
4 4   VAL n 
4 5   THR n 
4 6   THR n 
4 7   TYR n 
4 8   LYS n 
4 9   LEU n 
4 10  VAL n 
4 11  ILE n 
4 12  ASN n 
4 13  GLY n 
4 14  ARG n 
4 15  THR n 
4 16  LEU n 
4 17  SER n 
4 18  GLY n 
4 19  TYR n 
4 20  THR n 
4 21  THR n 
4 22  THR n 
4 23  THR n 
4 24  ALA n 
4 25  VAL n 
4 26  ASP n 
4 27  ALA n 
4 28  ALA n 
4 29  THR n 
4 30  ALA n 
4 31  GLU n 
4 32  LYS n 
4 33  VAL n 
4 34  PHE n 
4 35  LYS n 
4 36  GLN n 
4 37  TYR n 
4 38  ALA n 
4 39  PHE n 
4 40  GLY n 
4 41  ASN n 
4 42  GLY n 
4 43  VAL n 
4 44  ASP n 
4 45  GLY n 
4 46  GLU n 
4 47  TRP n 
4 48  THR n 
4 49  TYR n 
4 50  ASP n 
4 51  ASP n 
4 52  ALA n 
4 53  THR n 
4 54  LYS n 
4 55  THR n 
4 56  PHE n 
4 57  THR n 
4 58  VAL n 
4 59  THR n 
4 60  GLU n 
4 61  LYS n 
4 62  PRO n 
4 63  GLU n 
4 64  LYS n 
4 65  LEU 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' 1 228 ?     ? ?                            ? ? ? ? ? ? 'Homo sapiens'                9606 ? ? ? ? 
? ? ? ? 'Escherichia coli BL21'      511693 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 215 ?     ? ?                            ? ? ? ? ? ? 'Homo sapiens'                9606 ? ? ? ? 
? ? ? ? 'Escherichia coli BL21'      511693 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 161 human ? 'ASF1, CIA1, YJL115W, J0755' ? ? ? ? ? ? 'Homo sapiens'                9606 ? ? ? ? 
? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 65  ?     ? spg                          ? ? ? ? ? ? 
;Streptococcus sp. 'group G'
;
1320 ? ? ? ? ? ? ? ? '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 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLU 1   -1  ?   ?   ?   B . n 
A 1 2   ILE 2   0   ?   ?   ?   B . n 
A 1 3   SER 3   1   ?   ?   ?   B . n 
A 1 4   GLU 4   2   2   GLU GLU B . n 
A 1 5   VAL 5   3   3   VAL VAL B . n 
A 1 6   GLN 6   4   4   GLN GLN B . n 
A 1 7   LEU 7   5   5   LEU LEU B . n 
A 1 8   VAL 8   6   6   VAL VAL B . n 
A 1 9   GLU 9   7   7   GLU GLU B . n 
A 1 10  SER 10  8   8   SER SER B . n 
A 1 11  GLY 11  9   9   GLY GLY B . n 
A 1 12  GLY 12  10  10  GLY GLY B . n 
A 1 13  GLY 13  11  11  GLY GLY B . n 
A 1 14  LEU 14  12  12  LEU LEU B . n 
A 1 15  VAL 15  13  13  VAL VAL B . n 
A 1 16  GLN 16  14  14  GLN GLN B . n 
A 1 17  PRO 17  15  15  PRO PRO B . n 
A 1 18  GLY 18  16  16  GLY GLY B . n 
A 1 19  GLY 19  17  17  GLY GLY B . n 
A 1 20  SER 20  18  18  SER SER B . n 
A 1 21  LEU 21  19  19  LEU LEU B . n 
A 1 22  ARG 22  20  20  ARG ARG B . n 
A 1 23  LEU 23  21  21  LEU LEU B . n 
A 1 24  SER 24  22  22  SER SER B . n 
A 1 25  CYS 25  23  23  CYS CYS B . n 
A 1 26  ALA 26  24  24  ALA ALA B . n 
A 1 27  ALA 27  25  25  ALA ALA B . n 
A 1 28  SER 28  26  26  SER SER B . n 
A 1 29  GLY 29  27  27  GLY GLY B . n 
A 1 30  PHE 30  28  28  PHE PHE B . n 
A 1 31  ASN 31  29  29  ASN ASN B . n 
A 1 32  VAL 32  30  30  VAL VAL B . n 
A 1 33  SER 33  31  31  SER SER B . n 
A 1 34  TYR 34  32  32  TYR TYR B . n 
A 1 35  TYR 35  33  33  TYR TYR B . n 
A 1 36  SER 36  34  34  SER SER B . n 
A 1 37  ILE 37  35  35  ILE ILE B . n 
A 1 38  HIS 38  36  36  HIS HIS B . n 
A 1 39  TRP 39  37  37  TRP TRP B . n 
A 1 40  VAL 40  38  38  VAL VAL B . n 
A 1 41  ARG 41  39  39  ARG ARG B . n 
A 1 42  GLN 42  40  40  GLN GLN B . n 
A 1 43  ALA 43  41  41  ALA ALA B . n 
A 1 44  PRO 44  42  42  PRO PRO B . n 
A 1 45  GLY 45  43  43  GLY GLY B . n 
A 1 46  LYS 46  44  44  LYS LYS B . n 
A 1 47  GLY 47  45  45  GLY GLY B . n 
A 1 48  LEU 48  46  46  LEU LEU B . n 
A 1 49  GLU 49  47  47  GLU GLU B . n 
A 1 50  TRP 50  48  48  TRP TRP B . n 
A 1 51  VAL 51  49  49  VAL VAL B . n 
A 1 52  ALA 52  50  50  ALA ALA B . n 
A 1 53  SER 53  51  51  SER SER B . n 
A 1 54  ILE 54  52  52  ILE ILE B . n 
A 1 55  TYR 55  53  53  TYR TYR B . n 
A 1 56  PRO 56  54  54  PRO PRO B . n 
A 1 57  TYR 57  55  55  TYR TYR B . n 
A 1 58  TYR 58  56  56  TYR TYR B . n 
A 1 59  GLY 59  57  57  GLY GLY B . n 
A 1 60  SER 60  58  58  SER SER B . n 
A 1 61  THR 61  59  59  THR THR B . n 
A 1 62  SER 62  60  60  SER SER B . n 
A 1 63  TYR 63  61  61  TYR TYR B . n 
A 1 64  ALA 64  62  62  ALA ALA B . n 
A 1 65  ASP 65  63  63  ASP ASP B . n 
A 1 66  SER 66  64  64  SER SER B . n 
A 1 67  VAL 67  65  65  VAL VAL B . n 
A 1 68  LYS 68  66  66  LYS LYS B . n 
A 1 69  GLY 69  67  67  GLY GLY B . n 
A 1 70  ARG 70  68  68  ARG ARG B . n 
A 1 71  PHE 71  69  69  PHE PHE B . n 
A 1 72  THR 72  70  70  THR THR B . n 
A 1 73  ILE 73  71  71  ILE ILE B . n 
A 1 74  SER 74  72  72  SER SER B . n 
A 1 75  ALA 75  73  73  ALA ALA B . n 
A 1 76  ASP 76  74  74  ASP ASP B . n 
A 1 77  THR 77  75  75  THR THR B . n 
A 1 78  SER 78  76  76  SER SER B . n 
A 1 79  LYS 79  77  77  LYS LYS B . n 
A 1 80  ASN 80  78  78  ASN ASN B . n 
A 1 81  THR 81  79  79  THR THR B . n 
A 1 82  ALA 82  80  80  ALA ALA B . n 
A 1 83  TYR 83  81  81  TYR TYR B . n 
A 1 84  LEU 84  82  82  LEU LEU B . n 
A 1 85  GLN 85  83  83  GLN GLN B . n 
A 1 86  MET 86  84  84  MET MET B . n 
A 1 87  ASN 87  85  85  ASN ASN B . n 
A 1 88  SER 88  86  86  SER SER B . n 
A 1 89  LEU 89  87  87  LEU LEU B . n 
A 1 90  ARG 90  88  88  ARG ARG B . n 
A 1 91  ALA 91  89  89  ALA ALA B . n 
A 1 92  GLU 92  90  90  GLU GLU B . n 
A 1 93  ASP 93  91  91  ASP ASP B . n 
A 1 94  THR 94  92  92  THR THR B . n 
A 1 95  ALA 95  93  93  ALA ALA B . n 
A 1 96  VAL 96  94  94  VAL VAL B . n 
A 1 97  TYR 97  95  95  TYR TYR B . n 
A 1 98  TYR 98  96  96  TYR TYR B . n 
A 1 99  CYS 99  97  97  CYS CYS B . n 
A 1 100 ALA 100 98  98  ALA ALA B . n 
A 1 101 ARG 101 99  99  ARG ARG B . n 
A 1 102 GLY 102 100 100 GLY GLY B . n 
A 1 103 TYR 103 101 101 TYR TYR B . n 
A 1 104 GLY 104 102 102 GLY GLY B . n 
A 1 105 TRP 105 103 103 TRP TRP B . n 
A 1 106 ALA 106 104 104 ALA ALA B . n 
A 1 107 LEU 107 105 105 LEU LEU B . n 
A 1 108 ASP 108 106 106 ASP ASP B . n 
A 1 109 TYR 109 107 107 TYR TYR B . n 
A 1 110 TRP 110 108 108 TRP TRP B . n 
A 1 111 GLY 111 109 109 GLY GLY B . n 
A 1 112 GLN 112 110 110 GLN GLN B . n 
A 1 113 GLY 113 111 111 GLY GLY B . n 
A 1 114 THR 114 112 112 THR THR B . n 
A 1 115 LEU 115 113 113 LEU LEU B . n 
A 1 116 VAL 116 114 114 VAL VAL B . n 
A 1 117 THR 117 115 115 THR THR B . n 
A 1 118 VAL 118 116 116 VAL VAL B . n 
A 1 119 SER 119 117 117 SER SER B . n 
A 1 120 SER 120 118 118 SER SER B . n 
A 1 121 ALA 121 119 119 ALA ALA B . n 
A 1 122 SER 122 120 120 SER SER B . n 
A 1 123 THR 123 121 121 THR THR B . n 
A 1 124 LYS 124 122 122 LYS LYS B . n 
A 1 125 GLY 125 123 123 GLY GLY B . n 
A 1 126 PRO 126 124 124 PRO PRO B . n 
A 1 127 SER 127 125 125 SER SER B . n 
A 1 128 VAL 128 126 126 VAL VAL B . n 
A 1 129 PHE 129 127 127 PHE PHE B . n 
A 1 130 PRO 130 128 128 PRO PRO B . n 
A 1 131 LEU 131 129 129 LEU LEU B . n 
A 1 132 ALA 132 130 130 ALA ALA B . n 
A 1 133 PRO 133 131 131 PRO PRO B . n 
A 1 134 SER 134 132 132 SER SER B . n 
A 1 135 SER 135 133 133 SER SER B . n 
A 1 136 LYS 136 134 134 LYS LYS B . n 
A 1 137 SER 137 135 135 SER SER B . n 
A 1 138 THR 138 136 136 THR THR B . n 
A 1 139 SER 139 137 137 SER SER B . n 
A 1 140 GLY 140 138 138 GLY GLY B . n 
A 1 141 GLY 141 139 139 GLY GLY B . n 
A 1 142 THR 142 140 140 THR THR B . n 
A 1 143 ALA 143 141 141 ALA ALA B . n 
A 1 144 ALA 144 142 142 ALA ALA B . n 
A 1 145 LEU 145 143 143 LEU LEU B . n 
A 1 146 GLY 146 144 144 GLY GLY B . n 
A 1 147 CYS 147 145 145 CYS CYS B . n 
A 1 148 LEU 148 146 146 LEU LEU B . n 
A 1 149 VAL 149 147 147 VAL VAL B . n 
A 1 150 LYS 150 148 148 LYS LYS B . n 
A 1 151 ASP 151 149 149 ASP ASP B . n 
A 1 152 TYR 152 150 150 TYR TYR B . n 
A 1 153 PHE 153 151 151 PHE PHE B . n 
A 1 154 PRO 154 152 152 PRO PRO B . n 
A 1 155 GLU 155 153 153 GLU GLU B . n 
A 1 156 PRO 156 154 154 PRO PRO B . n 
A 1 157 VAL 157 155 155 VAL VAL B . n 
A 1 158 THR 158 156 156 THR THR B . n 
A 1 159 VAL 159 157 157 VAL VAL B . n 
A 1 160 SER 160 158 158 SER SER B . n 
A 1 161 TRP 161 159 159 TRP TRP B . n 
A 1 162 ASN 162 160 160 ASN ASN B . n 
A 1 163 SER 163 161 161 SER SER B . n 
A 1 164 GLY 164 162 162 GLY GLY B . n 
A 1 165 ALA 165 163 163 ALA ALA B . n 
A 1 166 LEU 166 164 164 LEU LEU B . n 
A 1 167 THR 167 165 165 THR THR B . n 
A 1 168 SER 168 166 166 SER SER B . n 
A 1 169 GLY 169 167 167 GLY GLY B . n 
A 1 170 VAL 170 168 168 VAL VAL B . n 
A 1 171 HIS 171 169 169 HIS HIS B . n 
A 1 172 THR 172 170 170 THR THR B . n 
A 1 173 PHE 173 171 171 PHE PHE B . n 
A 1 174 PRO 174 172 172 PRO PRO B . n 
A 1 175 ALA 175 173 173 ALA ALA B . n 
A 1 176 VAL 176 174 174 VAL VAL B . n 
A 1 177 LEU 177 175 175 LEU LEU B . n 
A 1 178 GLN 178 176 176 GLN GLN B . n 
A 1 179 SER 179 177 177 SER SER B . n 
A 1 180 SER 180 178 178 SER SER B . n 
A 1 181 GLY 181 179 179 GLY GLY B . n 
A 1 182 LEU 182 180 180 LEU LEU B . n 
A 1 183 TYR 183 181 181 TYR TYR B . n 
A 1 184 SER 184 182 182 SER SER B . n 
A 1 185 LEU 185 183 183 LEU LEU B . n 
A 1 186 SER 186 184 184 SER SER B . n 
A 1 187 SER 187 185 185 SER SER B . n 
A 1 188 VAL 188 186 186 VAL VAL B . n 
A 1 189 VAL 189 187 187 VAL VAL B . n 
A 1 190 THR 190 188 188 THR THR B . n 
A 1 191 VAL 191 189 189 VAL VAL B . n 
A 1 192 PRO 192 190 190 PRO PRO B . n 
A 1 193 SER 193 191 191 SER SER B . n 
A 1 194 SER 194 192 192 SER SER B . n 
A 1 195 SER 195 193 193 SER SER B . n 
A 1 196 LEU 196 194 194 LEU LEU B . n 
A 1 197 GLY 197 195 195 GLY GLY B . n 
A 1 198 THR 198 196 196 THR THR B . n 
A 1 199 GLN 199 197 197 GLN GLN B . n 
A 1 200 THR 200 198 198 THR THR B . n 
A 1 201 TYR 201 199 199 TYR TYR B . n 
A 1 202 ILE 202 200 200 ILE ILE B . n 
A 1 203 CYS 203 201 201 CYS CYS B . n 
A 1 204 ASN 204 202 202 ASN ASN B . n 
A 1 205 VAL 205 203 203 VAL VAL B . n 
A 1 206 ASN 206 204 204 ASN ASN B . n 
A 1 207 HIS 207 205 205 HIS HIS B . n 
A 1 208 LYS 208 206 206 LYS LYS B . n 
A 1 209 PRO 209 207 207 PRO PRO B . n 
A 1 210 SER 210 208 208 SER SER B . n 
A 1 211 ASN 211 209 209 ASN ASN B . n 
A 1 212 THR 212 210 210 THR THR B . n 
A 1 213 LYS 213 211 211 LYS LYS B . n 
A 1 214 VAL 214 212 212 VAL VAL B . n 
A 1 215 ASP 215 213 213 ASP ASP B . n 
A 1 216 LYS 216 214 214 LYS LYS B . n 
A 1 217 LYS 217 215 215 LYS LYS B . n 
A 1 218 VAL 218 216 216 VAL VAL B . n 
A 1 219 GLU 219 217 217 GLU GLU B . n 
A 1 220 PRO 220 218 218 PRO PRO B . n 
A 1 221 LYS 221 219 219 LYS LYS B . n 
A 1 222 SER 222 220 ?   ?   ?   B . n 
A 1 223 CYS 223 221 ?   ?   ?   B . n 
A 1 224 ASP 224 222 ?   ?   ?   B . n 
A 1 225 LYS 225 223 ?   ?   ?   B . n 
A 1 226 THR 226 224 ?   ?   ?   B . n 
A 1 227 HIS 227 225 ?   ?   ?   B . n 
A 1 228 THR 228 226 ?   ?   ?   B . n 
B 2 1   SER 1   0   ?   ?   ?   D . n 
B 2 2   ASP 2   1   ?   ?   ?   D . n 
B 2 3   ILE 3   2   ?   ?   ?   D . n 
B 2 4   GLN 4   3   ?   ?   ?   D . n 
B 2 5   MET 5   4   4   MET MET D . n 
B 2 6   THR 6   5   5   THR THR D . n 
B 2 7   GLN 7   6   6   GLN GLN D . n 
B 2 8   SER 8   7   7   SER SER D . n 
B 2 9   PRO 9   8   8   PRO PRO D . n 
B 2 10  SER 10  9   9   SER SER D . n 
B 2 11  SER 11  10  10  SER SER D . n 
B 2 12  LEU 12  11  11  LEU LEU D . n 
B 2 13  SER 13  12  12  SER SER D . n 
B 2 14  ALA 14  13  13  ALA ALA D . n 
B 2 15  SER 15  14  14  SER SER D . n 
B 2 16  VAL 16  15  15  VAL VAL D . n 
B 2 17  GLY 17  16  16  GLY GLY D . n 
B 2 18  ASP 18  17  17  ASP ASP D . n 
B 2 19  ARG 19  18  18  ARG ARG D . n 
B 2 20  VAL 20  19  19  VAL VAL D . n 
B 2 21  THR 21  20  20  THR THR D . n 
B 2 22  ILE 22  21  21  ILE ILE D . n 
B 2 23  THR 23  22  22  THR THR D . n 
B 2 24  CYS 24  23  23  CYS CYS D . n 
B 2 25  ARG 25  24  24  ARG ARG D . n 
B 2 26  ALA 26  25  25  ALA ALA D . n 
B 2 27  SER 27  26  26  SER SER D . n 
B 2 28  GLN 28  27  27  GLN GLN D . n 
B 2 29  SER 29  28  28  SER SER D . n 
B 2 30  VAL 30  29  29  VAL VAL D . n 
B 2 31  SER 31  30  30  SER SER D . n 
B 2 32  SER 32  31  31  SER SER D . n 
B 2 33  ALA 33  32  32  ALA ALA D . n 
B 2 34  VAL 34  33  33  VAL VAL D . n 
B 2 35  ALA 35  34  34  ALA ALA D . n 
B 2 36  TRP 36  35  35  TRP TRP D . n 
B 2 37  TYR 37  36  36  TYR TYR D . n 
B 2 38  GLN 38  37  37  GLN GLN D . n 
B 2 39  GLN 39  38  38  GLN GLN D . n 
B 2 40  LYS 40  39  39  LYS LYS D . n 
B 2 41  PRO 41  40  40  PRO PRO D . n 
B 2 42  GLY 42  41  41  GLY GLY D . n 
B 2 43  LYS 43  42  42  LYS LYS D . n 
B 2 44  ALA 44  43  43  ALA ALA D . n 
B 2 45  PRO 45  44  44  PRO PRO D . n 
B 2 46  LYS 46  45  45  LYS LYS D . n 
B 2 47  LEU 47  46  46  LEU LEU D . n 
B 2 48  LEU 48  47  47  LEU LEU D . n 
B 2 49  ILE 49  48  48  ILE ILE D . n 
B 2 50  TYR 50  49  49  TYR TYR D . n 
B 2 51  SER 51  50  50  SER SER D . n 
B 2 52  ALA 52  51  51  ALA ALA D . n 
B 2 53  SER 53  52  52  SER SER D . n 
B 2 54  SER 54  53  53  SER SER D . n 
B 2 55  LEU 55  54  54  LEU LEU D . n 
B 2 56  TYR 56  55  55  TYR TYR D . n 
B 2 57  SER 57  56  56  SER SER D . n 
B 2 58  GLY 58  57  57  GLY GLY D . n 
B 2 59  VAL 59  58  58  VAL VAL D . n 
B 2 60  PRO 60  59  59  PRO PRO D . n 
B 2 61  SER 61  60  60  SER SER D . n 
B 2 62  ARG 62  61  61  ARG ARG D . n 
B 2 63  PHE 63  62  62  PHE PHE D . n 
B 2 64  SER 64  63  63  SER SER D . n 
B 2 65  GLY 65  64  64  GLY GLY D . n 
B 2 66  SER 66  65  65  SER SER D . n 
B 2 67  ARG 67  66  66  ARG ARG D . n 
B 2 68  SER 68  67  67  SER SER D . n 
B 2 69  GLY 69  68  68  GLY GLY D . n 
B 2 70  THR 70  69  69  THR THR D . n 
B 2 71  ASP 71  70  70  ASP ASP D . n 
B 2 72  PHE 72  71  71  PHE PHE D . n 
B 2 73  THR 73  72  72  THR THR D . n 
B 2 74  LEU 74  73  73  LEU LEU D . n 
B 2 75  THR 75  74  74  THR THR D . n 
B 2 76  ILE 76  75  75  ILE ILE D . n 
B 2 77  SER 77  76  76  SER SER D . n 
B 2 78  SER 78  77  77  SER SER D . n 
B 2 79  LEU 79  78  78  LEU LEU D . n 
B 2 80  GLN 80  79  79  GLN GLN D . n 
B 2 81  PRO 81  80  80  PRO PRO D . n 
B 2 82  GLU 82  81  81  GLU GLU D . n 
B 2 83  ASP 83  82  82  ASP ASP D . n 
B 2 84  PHE 84  83  83  PHE PHE D . n 
B 2 85  ALA 85  84  84  ALA ALA D . n 
B 2 86  THR 86  85  85  THR THR D . n 
B 2 87  TYR 87  86  86  TYR TYR D . n 
B 2 88  TYR 88  87  87  TYR TYR D . n 
B 2 89  CYS 89  88  88  CYS CYS D . n 
B 2 90  GLN 90  89  89  GLN GLN D . n 
B 2 91  GLN 91  90  90  GLN GLN D . n 
B 2 92  ASP 92  91  91  ASP ASP D . n 
B 2 93  GLY 93  92  92  GLY GLY D . n 
B 2 94  TRP 94  93  93  TRP TRP D . n 
B 2 95  SER 95  94  94  SER SER D . n 
B 2 96  LEU 96  95  95  LEU LEU D . n 
B 2 97  ILE 97  96  96  ILE ILE D . n 
B 2 98  THR 98  97  97  THR THR D . n 
B 2 99  PHE 99  98  98  PHE PHE D . n 
B 2 100 GLY 100 99  99  GLY GLY D . n 
B 2 101 GLN 101 100 100 GLN GLN D . n 
B 2 102 GLY 102 101 101 GLY GLY D . n 
B 2 103 THR 103 102 102 THR THR D . n 
B 2 104 LYS 104 103 103 LYS LYS D . n 
B 2 105 VAL 105 104 104 VAL VAL D . n 
B 2 106 GLU 106 105 105 GLU GLU D . n 
B 2 107 ILE 107 106 106 ILE ILE D . n 
B 2 108 LYS 108 107 107 LYS LYS D . n 
B 2 109 ARG 109 108 108 ARG ARG D . n 
B 2 110 THR 110 109 109 THR THR D . n 
B 2 111 VAL 111 110 110 VAL VAL D . n 
B 2 112 ALA 112 111 111 ALA ALA D . n 
B 2 113 ALA 113 112 112 ALA ALA D . n 
B 2 114 PRO 114 113 113 PRO PRO D . n 
B 2 115 SER 115 114 114 SER SER D . n 
B 2 116 VAL 116 115 115 VAL VAL D . n 
B 2 117 PHE 117 116 116 PHE PHE D . n 
B 2 118 ILE 118 117 117 ILE ILE D . n 
B 2 119 PHE 119 118 118 PHE PHE D . n 
B 2 120 PRO 120 119 119 PRO PRO D . n 
B 2 121 PRO 121 120 120 PRO PRO D . n 
B 2 122 SER 122 121 121 SER SER D . n 
B 2 123 ASP 123 122 122 ASP ASP D . n 
B 2 124 GLU 124 123 123 GLU GLU D . n 
B 2 125 GLN 125 124 124 GLN GLN D . n 
B 2 126 LEU 126 125 125 LEU LEU D . n 
B 2 127 LYS 127 126 126 LYS LYS D . n 
B 2 128 SER 128 127 127 SER SER D . n 
B 2 129 GLY 129 128 128 GLY GLY D . n 
B 2 130 THR 130 129 129 THR THR D . n 
B 2 131 ALA 131 130 130 ALA ALA D . n 
B 2 132 SER 132 131 131 SER SER D . n 
B 2 133 VAL 133 132 132 VAL VAL D . n 
B 2 134 VAL 134 133 133 VAL VAL D . n 
B 2 135 CYS 135 134 134 CYS CYS D . n 
B 2 136 LEU 136 135 135 LEU LEU D . n 
B 2 137 LEU 137 136 136 LEU LEU D . n 
B 2 138 ASN 138 137 137 ASN ASN D . n 
B 2 139 ASN 139 138 138 ASN ASN D . n 
B 2 140 PHE 140 139 139 PHE PHE D . n 
B 2 141 TYR 141 140 140 TYR TYR D . n 
B 2 142 PRO 142 141 141 PRO PRO D . n 
B 2 143 ARG 143 142 142 ARG ARG D . n 
B 2 144 GLU 144 143 143 GLU GLU D . n 
B 2 145 ALA 145 144 144 ALA ALA D . n 
B 2 146 LYS 146 145 145 LYS LYS D . n 
B 2 147 VAL 147 146 146 VAL VAL D . n 
B 2 148 GLN 148 147 147 GLN GLN D . n 
B 2 149 TRP 149 148 148 TRP TRP D . n 
B 2 150 LYS 150 149 149 LYS LYS D . n 
B 2 151 VAL 151 150 150 VAL VAL D . n 
B 2 152 ASP 152 151 151 ASP ASP D . n 
B 2 153 ASN 153 152 152 ASN ASN D . n 
B 2 154 ALA 154 153 153 ALA ALA D . n 
B 2 155 LEU 155 154 154 LEU LEU D . n 
B 2 156 GLN 156 155 155 GLN GLN D . n 
B 2 157 SER 157 156 156 SER SER D . n 
B 2 158 GLY 158 157 157 GLY GLY D . n 
B 2 159 ASN 159 158 158 ASN ASN D . n 
B 2 160 SER 160 159 159 SER SER D . n 
B 2 161 GLN 161 160 160 GLN GLN D . n 
B 2 162 GLU 162 161 161 GLU GLU D . n 
B 2 163 SER 163 162 162 SER SER D . n 
B 2 164 VAL 164 163 163 VAL VAL D . n 
B 2 165 THR 165 164 164 THR THR D . n 
B 2 166 GLU 166 165 165 GLU GLU D . n 
B 2 167 GLN 167 166 166 GLN GLN D . n 
B 2 168 ASP 168 167 167 ASP ASP D . n 
B 2 169 SER 169 168 168 SER SER D . n 
B 2 170 LYS 170 169 169 LYS LYS D . n 
B 2 171 ASP 171 170 170 ASP ASP D . n 
B 2 172 SER 172 171 171 SER SER D . n 
B 2 173 THR 173 172 172 THR THR D . n 
B 2 174 TYR 174 173 173 TYR TYR D . n 
B 2 175 SER 175 174 174 SER SER D . n 
B 2 176 LEU 176 175 175 LEU LEU D . n 
B 2 177 SER 177 176 176 SER SER D . n 
B 2 178 SER 178 177 177 SER SER D . n 
B 2 179 THR 179 178 178 THR THR D . n 
B 2 180 LEU 180 179 179 LEU LEU D . n 
B 2 181 THR 181 180 180 THR THR D . n 
B 2 182 LEU 182 181 181 LEU LEU D . n 
B 2 183 SER 183 182 182 SER SER D . n 
B 2 184 LYS 184 183 183 LYS LYS D . n 
B 2 185 ALA 185 184 184 ALA ALA D . n 
B 2 186 ASP 186 185 185 ASP ASP D . n 
B 2 187 TYR 187 186 186 TYR TYR D . n 
B 2 188 GLU 188 187 187 GLU GLU D . n 
B 2 189 LYS 189 188 188 LYS LYS D . n 
B 2 190 HIS 190 189 189 HIS HIS D . n 
B 2 191 LYS 191 190 190 LYS LYS D . n 
B 2 192 VAL 192 191 191 VAL VAL D . n 
B 2 193 TYR 193 192 192 TYR TYR D . n 
B 2 194 ALA 194 193 193 ALA ALA D . n 
B 2 195 CYS 195 194 194 CYS CYS D . n 
B 2 196 GLU 196 195 195 GLU GLU D . n 
B 2 197 VAL 197 196 196 VAL VAL D . n 
B 2 198 THR 198 197 197 THR THR D . n 
B 2 199 HIS 199 198 198 HIS HIS D . n 
B 2 200 GLN 200 199 199 GLN GLN D . n 
B 2 201 GLY 201 200 200 GLY GLY D . n 
B 2 202 LEU 202 201 201 LEU LEU D . n 
B 2 203 SER 203 202 202 SER SER D . n 
B 2 204 SER 204 203 203 SER SER D . n 
B 2 205 PRO 205 204 204 PRO PRO D . n 
B 2 206 VAL 206 205 205 VAL VAL D . n 
B 2 207 THR 207 206 206 THR THR D . n 
B 2 208 LYS 208 207 207 LYS LYS D . n 
B 2 209 SER 209 208 208 SER SER D . n 
B 2 210 PHE 210 209 209 PHE PHE D . n 
B 2 211 ASN 211 210 210 ASN ASN D . n 
B 2 212 ARG 212 211 211 ARG ARG D . n 
B 2 213 GLY 213 212 212 GLY GLY D . n 
B 2 214 GLU 214 213 ?   ?   ?   D . n 
B 2 215 CYS 215 214 ?   ?   ?   D . n 
C 3 1   SER 1   1   ?   ?   ?   A . n 
C 3 2   SER 2   2   2   SER SER A . n 
C 3 3   ILE 3   3   3   ILE ILE A . n 
C 3 4   VAL 4   4   4   VAL VAL A . n 
C 3 5   SER 5   5   5   SER SER A . n 
C 3 6   LEU 6   6   6   LEU LEU A . n 
C 3 7   LEU 7   7   7   LEU LEU A . n 
C 3 8   GLY 8   8   8   GLY GLY A . n 
C 3 9   ILE 9   9   9   ILE ILE A . n 
C 3 10  LYS 10  10  10  LYS LYS A . n 
C 3 11  VAL 11  11  11  VAL VAL A . n 
C 3 12  LEU 12  12  12  LEU LEU A . n 
C 3 13  ASN 13  13  13  ASN ASN A . n 
C 3 14  ASN 14  14  14  ASN ASN A . n 
C 3 15  PRO 15  15  15  PRO PRO A . n 
C 3 16  ALA 16  16  16  ALA ALA A . n 
C 3 17  LYS 17  17  17  LYS LYS A . n 
C 3 18  PHE 18  18  18  PHE PHE A . n 
C 3 19  THR 19  19  19  THR THR A . n 
C 3 20  ASP 20  20  20  ASP ASP A . n 
C 3 21  PRO 21  21  21  PRO PRO A . n 
C 3 22  TYR 22  22  22  TYR TYR A . n 
C 3 23  GLU 23  23  23  GLU GLU A . n 
C 3 24  PHE 24  24  24  PHE PHE A . n 
C 3 25  GLU 25  25  25  GLU GLU A . n 
C 3 26  ILE 26  26  26  ILE ILE A . n 
C 3 27  THR 27  27  27  THR THR A . n 
C 3 28  PHE 28  28  28  PHE PHE A . n 
C 3 29  GLU 29  29  29  GLU GLU A . n 
C 3 30  CYS 30  30  30  CYS CYS A . n 
C 3 31  LEU 31  31  31  LEU LEU A . n 
C 3 32  GLU 32  32  32  GLU GLU A . n 
C 3 33  SER 33  33  33  SER SER A . n 
C 3 34  LEU 34  34  34  LEU LEU A . n 
C 3 35  LYS 35  35  35  LYS LYS A . n 
C 3 36  HIS 36  36  36  HIS HIS A . n 
C 3 37  ASP 37  37  37  ASP ASP A . n 
C 3 38  LEU 38  38  38  LEU LEU A . n 
C 3 39  GLU 39  39  39  GLU GLU A . n 
C 3 40  TRP 40  40  40  TRP TRP A . n 
C 3 41  LYS 41  41  41  LYS LYS A . n 
C 3 42  LEU 42  42  42  LEU LEU A . n 
C 3 43  THR 43  43  43  THR THR A . n 
C 3 44  TYR 44  44  44  TYR TYR A . n 
C 3 45  VAL 45  45  45  VAL VAL A . n 
C 3 46  GLY 46  46  46  GLY GLY A . n 
C 3 47  SER 47  47  47  SER SER A . n 
C 3 48  SER 48  48  48  SER SER A . n 
C 3 49  ARG 49  49  49  ARG ARG A . n 
C 3 50  SER 50  50  50  SER SER A . n 
C 3 51  LEU 51  51  51  LEU LEU A . n 
C 3 52  ASP 52  52  52  ASP ASP A . n 
C 3 53  HIS 53  53  53  HIS HIS A . n 
C 3 54  ASP 54  54  54  ASP ASP A . n 
C 3 55  GLN 55  55  55  GLN GLN A . n 
C 3 56  GLU 56  56  56  GLU GLU A . n 
C 3 57  LEU 57  57  57  LEU LEU A . n 
C 3 58  ASP 58  58  58  ASP ASP A . n 
C 3 59  SER 59  59  59  SER SER A . n 
C 3 60  ILE 60  60  60  ILE ILE A . n 
C 3 61  LEU 61  61  61  LEU LEU A . n 
C 3 62  VAL 62  62  62  VAL VAL A . n 
C 3 63  GLY 63  63  63  GLY GLY A . n 
C 3 64  PRO 64  64  64  PRO PRO A . n 
C 3 65  VAL 65  65  65  VAL VAL A . n 
C 3 66  PRO 66  66  66  PRO PRO A . n 
C 3 67  VAL 67  67  67  VAL VAL A . n 
C 3 68  GLY 68  68  68  GLY GLY A . n 
C 3 69  VAL 69  69  69  VAL VAL A . n 
C 3 70  ASN 70  70  70  ASN ASN A . n 
C 3 71  LYS 71  71  71  LYS LYS A . n 
C 3 72  PHE 72  72  72  PHE PHE A . n 
C 3 73  VAL 73  73  73  VAL VAL A . n 
C 3 74  PHE 74  74  74  PHE PHE A . n 
C 3 75  SER 75  75  75  SER SER A . n 
C 3 76  ALA 76  76  76  ALA ALA A . n 
C 3 77  ASP 77  77  77  ASP ASP A . n 
C 3 78  PRO 78  78  78  PRO PRO A . n 
C 3 79  PRO 79  79  79  PRO PRO A . n 
C 3 80  SER 80  80  80  SER SER A . n 
C 3 81  ALA 81  81  81  ALA ALA A . n 
C 3 82  GLU 82  82  82  GLU GLU A . n 
C 3 83  LEU 83  83  83  LEU LEU A . n 
C 3 84  ILE 84  84  84  ILE ILE A . n 
C 3 85  PRO 85  85  85  PRO PRO A . n 
C 3 86  ALA 86  86  86  ALA ALA A . n 
C 3 87  SER 87  87  87  SER SER A . n 
C 3 88  GLU 88  88  88  GLU GLU A . n 
C 3 89  LEU 89  89  89  LEU LEU A . n 
C 3 90  VAL 90  90  90  VAL VAL A . n 
C 3 91  SER 91  91  91  SER SER A . n 
C 3 92  VAL 92  92  92  VAL VAL A . n 
C 3 93  THR 93  93  93  THR THR A . n 
C 3 94  VAL 94  94  94  VAL VAL A . n 
C 3 95  ILE 95  95  95  ILE ILE A . n 
C 3 96  LEU 96  96  96  LEU LEU A . n 
C 3 97  LEU 97  97  97  LEU LEU A . n 
C 3 98  SER 98  98  98  SER SER A . n 
C 3 99  CYS 99  99  99  CYS CYS A . n 
C 3 100 SER 100 100 100 SER SER A . n 
C 3 101 TYR 101 101 101 TYR TYR A . n 
C 3 102 ASP 102 102 102 ASP ASP A . n 
C 3 103 GLY 103 103 103 GLY GLY A . n 
C 3 104 ARG 104 104 104 ARG ARG A . n 
C 3 105 GLU 105 105 105 GLU GLU A . n 
C 3 106 PHE 106 106 106 PHE PHE A . n 
C 3 107 VAL 107 107 107 VAL VAL A . n 
C 3 108 ARG 108 108 108 ARG ARG A . n 
C 3 109 VAL 109 109 109 VAL VAL A . n 
C 3 110 GLY 110 110 110 GLY GLY A . n 
C 3 111 TYR 111 111 111 TYR TYR A . n 
C 3 112 TYR 112 112 112 TYR TYR A . n 
C 3 113 VAL 113 113 113 VAL VAL A . n 
C 3 114 ASN 114 114 114 ASN ASN A . n 
C 3 115 ASN 115 115 115 ASN ASN A . n 
C 3 116 GLU 116 116 116 GLU GLU A . n 
C 3 117 TYR 117 117 117 TYR TYR A . n 
C 3 118 ASP 118 118 118 ASP ASP A . n 
C 3 119 GLU 119 119 119 GLU GLU A . n 
C 3 120 GLU 120 120 120 GLU GLU A . n 
C 3 121 GLU 121 121 121 GLU GLU A . n 
C 3 122 LEU 122 122 122 LEU LEU A . n 
C 3 123 ARG 123 123 123 ARG ARG A . n 
C 3 124 GLU 124 124 124 GLU GLU A . n 
C 3 125 ASN 125 125 125 ASN ASN A . n 
C 3 126 PRO 126 126 126 PRO PRO A . n 
C 3 127 PRO 127 127 127 PRO PRO A . n 
C 3 128 ALA 128 128 128 ALA ALA A . n 
C 3 129 LYS 129 129 129 LYS LYS A . n 
C 3 130 VAL 130 130 130 VAL VAL A . n 
C 3 131 GLN 131 131 131 GLN GLN A . n 
C 3 132 VAL 132 132 132 VAL VAL A . n 
C 3 133 ASP 133 133 133 ASP ASP A . n 
C 3 134 HIS 134 134 134 HIS HIS A . n 
C 3 135 ILE 135 135 135 ILE ILE A . n 
C 3 136 VAL 136 136 136 VAL VAL A . n 
C 3 137 ARG 137 137 137 ARG ARG A . n 
C 3 138 ASN 138 138 138 ASN ASN A . n 
C 3 139 ILE 139 139 139 ILE ILE A . n 
C 3 140 LEU 140 140 140 LEU LEU A . n 
C 3 141 ALA 141 141 141 ALA ALA A . n 
C 3 142 GLU 142 142 142 GLU GLU A . n 
C 3 143 LYS 143 143 143 LYS LYS A . n 
C 3 144 PRO 144 144 144 PRO PRO A . n 
C 3 145 ARG 145 145 145 ARG ARG A . n 
C 3 146 VAL 146 146 146 VAL VAL A . n 
C 3 147 THR 147 147 147 THR THR A . n 
C 3 148 ARG 148 148 148 ARG ARG A . n 
C 3 149 PHE 149 149 149 PHE PHE A . n 
C 3 150 ASN 150 150 150 ASN ASN A . n 
C 3 151 ILE 151 151 151 ILE ILE A . n 
C 3 152 VAL 152 152 152 VAL VAL A . n 
C 3 153 TRP 153 153 153 TRP TRP A . n 
C 3 154 ASP 154 154 154 ASP ASP A . n 
C 3 155 ASN 155 155 ?   ?   ?   A . n 
C 3 156 GLU 156 156 ?   ?   ?   A . n 
C 3 157 ASN 157 157 ?   ?   ?   A . n 
C 3 158 GLU 158 158 ?   ?   ?   A . n 
C 3 159 GLY 159 159 ?   ?   ?   A . n 
C 3 160 LEU 160 160 ?   ?   ?   A . n 
C 3 161 GLU 161 161 ?   ?   ?   A . n 
D 4 1   THR 1   2   ?   ?   ?   C . n 
D 4 2   PRO 2   3   ?   ?   ?   C . n 
D 4 3   ALA 3   4   ?   ?   ?   C . n 
D 4 4   VAL 4   5   ?   ?   ?   C . n 
D 4 5   THR 5   6   ?   ?   ?   C . n 
D 4 6   THR 6   7   ?   ?   ?   C . n 
D 4 7   TYR 7   8   ?   ?   ?   C . n 
D 4 8   LYS 8   9   ?   ?   ?   C . n 
D 4 9   LEU 9   10  10  LEU LEU C . n 
D 4 10  VAL 10  11  11  VAL VAL C . n 
D 4 11  ILE 11  12  12  ILE ILE C . n 
D 4 12  ASN 12  13  13  ASN ASN C . n 
D 4 13  GLY 13  14  14  GLY GLY C . n 
D 4 14  ARG 14  15  15  ARG ARG C . n 
D 4 15  THR 15  16  16  THR THR C . n 
D 4 16  LEU 16  17  17  LEU LEU C . n 
D 4 17  SER 17  18  18  SER SER C . n 
D 4 18  GLY 18  19  19  GLY GLY C . n 
D 4 19  TYR 19  20  20  TYR TYR C . n 
D 4 20  THR 20  21  21  THR THR C . n 
D 4 21  THR 21  22  22  THR THR C . n 
D 4 22  THR 22  23  23  THR THR C . n 
D 4 23  THR 23  24  24  THR THR C . n 
D 4 24  ALA 24  25  25  ALA ALA C . n 
D 4 25  VAL 25  26  26  VAL VAL C . n 
D 4 26  ASP 26  27  27  ASP ASP C . n 
D 4 27  ALA 27  28  28  ALA ALA C . n 
D 4 28  ALA 28  29  29  ALA ALA C . n 
D 4 29  THR 29  30  30  THR THR C . n 
D 4 30  ALA 30  31  31  ALA ALA C . n 
D 4 31  GLU 31  32  32  GLU GLU C . n 
D 4 32  LYS 32  33  33  LYS LYS C . n 
D 4 33  VAL 33  34  34  VAL VAL C . n 
D 4 34  PHE 34  35  35  PHE PHE C . n 
D 4 35  LYS 35  36  36  LYS LYS C . n 
D 4 36  GLN 36  37  37  GLN GLN C . n 
D 4 37  TYR 37  38  38  TYR TYR C . n 
D 4 38  ALA 38  39  39  ALA ALA C . n 
D 4 39  PHE 39  40  40  PHE PHE C . n 
D 4 40  GLY 40  41  41  GLY GLY C . n 
D 4 41  ASN 41  42  42  ASN ASN C . n 
D 4 42  GLY 42  43  43  GLY GLY C . n 
D 4 43  VAL 43  44  44  VAL VAL C . n 
D 4 44  ASP 44  45  45  ASP ASP C . n 
D 4 45  GLY 45  46  46  GLY GLY C . n 
D 4 46  GLU 46  47  47  GLU GLU C . n 
D 4 47  TRP 47  48  48  TRP TRP C . n 
D 4 48  THR 48  49  49  THR THR C . n 
D 4 49  TYR 49  50  ?   ?   ?   C . n 
D 4 50  ASP 50  51  51  ASP ASP C . n 
D 4 51  ASP 51  52  52  ASP ASP C . n 
D 4 52  ALA 52  53  53  ALA ALA C . n 
D 4 53  THR 53  54  54  THR THR C . n 
D 4 54  LYS 54  55  55  LYS LYS C . n 
D 4 55  THR 55  56  56  THR THR C . n 
D 4 56  PHE 56  57  57  PHE PHE C . n 
D 4 57  THR 57  58  58  THR THR C . n 
D 4 58  VAL 58  59  59  VAL VAL C . n 
D 4 59  THR 59  60  60  THR THR C . n 
D 4 60  GLU 60  61  61  GLU GLU C . n 
D 4 61  LYS 61  62  62  LYS LYS C . n 
D 4 62  PRO 62  63  63  PRO PRO C . n 
D 4 63  GLU 63  64  ?   ?   ?   C . n 
D 4 64  LYS 64  65  ?   ?   ?   C . n 
D 4 65  LEU 65  66  ?   ?   ?   C . n 
# 
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 
E 5 HOH 1  301 8  HOH HOH B . 
E 5 HOH 2  302 5  HOH HOH B . 
F 5 HOH 1  301 9  HOH HOH D . 
F 5 HOH 2  302 6  HOH HOH D . 
F 5 HOH 3  303 12 HOH HOH D . 
F 5 HOH 4  304 4  HOH HOH D . 
F 5 HOH 5  305 10 HOH HOH D . 
F 5 HOH 6  306 11 HOH HOH D . 
F 5 HOH 7  307 7  HOH HOH D . 
F 5 HOH 8  308 1  HOH HOH D . 
F 5 HOH 9  309 3  HOH HOH D . 
F 5 HOH 10 310 2  HOH HOH D . 
G 5 HOH 1  101 14 HOH HOH C . 
G 5 HOH 2  102 13 HOH HOH C . 
# 
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 LYS 77 ? CG  ? A LYS 79 CG  
2  1 Y 1 B LYS 77 ? CD  ? A LYS 79 CD  
3  1 Y 1 B LYS 77 ? CE  ? A LYS 79 CE  
4  1 Y 1 B LYS 77 ? NZ  ? A LYS 79 NZ  
5  1 Y 1 A LYS 71 ? CG  ? C LYS 71 CG  
6  1 Y 1 A LYS 71 ? CD  ? C LYS 71 CD  
7  1 Y 1 A LYS 71 ? CE  ? C LYS 71 CE  
8  1 Y 1 A LYS 71 ? NZ  ? C LYS 71 NZ  
9  1 Y 1 C ARG 15 ? CG  ? D ARG 14 CG  
10 1 Y 1 C ARG 15 ? CD  ? D ARG 14 CD  
11 1 Y 1 C ARG 15 ? NE  ? D ARG 14 NE  
12 1 Y 1 C ARG 15 ? CZ  ? D ARG 14 CZ  
13 1 Y 1 C ARG 15 ? NH1 ? D ARG 14 NH1 
14 1 Y 1 C ARG 15 ? NH2 ? D ARG 14 NH2 
15 1 Y 1 C LYS 33 ? CG  ? D LYS 32 CG  
16 1 Y 1 C LYS 33 ? CD  ? D LYS 32 CD  
17 1 Y 1 C LYS 33 ? CE  ? D LYS 32 CE  
18 1 Y 1 C LYS 33 ? NZ  ? D LYS 32 NZ  
19 1 Y 1 C LYS 36 ? CG  ? D LYS 35 CG  
20 1 Y 1 C LYS 36 ? CD  ? D LYS 35 CD  
21 1 Y 1 C LYS 36 ? CE  ? D LYS 35 CE  
22 1 Y 1 C LYS 36 ? NZ  ? D LYS 35 NZ  
23 1 Y 1 C VAL 44 ? CG1 ? D VAL 43 CG1 
24 1 Y 1 C VAL 44 ? CG2 ? D VAL 43 CG2 
25 1 Y 1 C GLU 47 ? CG  ? D GLU 46 CG  
26 1 Y 1 C GLU 47 ? CD  ? D GLU 46 CD  
27 1 Y 1 C GLU 47 ? OE1 ? D GLU 46 OE1 
28 1 Y 1 C GLU 47 ? OE2 ? D GLU 46 OE2 
29 1 Y 1 C LYS 55 ? CG  ? D LYS 54 CG  
30 1 Y 1 C LYS 55 ? CD  ? D LYS 54 CD  
31 1 Y 1 C LYS 55 ? CE  ? D LYS 54 CE  
32 1 Y 1 C LYS 55 ? NZ  ? D LYS 54 NZ  
33 1 Y 1 C PHE 57 ? CG  ? D PHE 56 CG  
34 1 Y 1 C PHE 57 ? CD1 ? D PHE 56 CD1 
35 1 Y 1 C PHE 57 ? CD2 ? D PHE 56 CD2 
36 1 Y 1 C PHE 57 ? CE1 ? D PHE 56 CE1 
37 1 Y 1 C PHE 57 ? CE2 ? D PHE 56 CE2 
38 1 Y 1 C PHE 57 ? CZ  ? D PHE 56 CZ  
39 1 Y 1 C LYS 62 ? CG  ? D LYS 61 CG  
40 1 Y 1 C LYS 62 ? CD  ? D LYS 61 CD  
41 1 Y 1 C LYS 62 ? CE  ? D LYS 61 CE  
42 1 Y 1 C LYS 62 ? NZ  ? D LYS 61 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AWE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.869 
_cell.length_a_esd                 ? 
_cell.length_b                     85.660 
_cell.length_b_esd                 ? 
_cell.length_c                     180.110 
_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                         9AWE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 2 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                   9AWE 
_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             3.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.82 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Sodium Cacodylate pH 6.0, 0.1M Calcium acetate hydrate, 10% PEG 8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-11-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9791 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 24-ID-C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9791 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-C 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9AWE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.8 
_reflns.d_resolution_low                               90.05 
_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                                     21810 
_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                           97.38 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.8 
_reflns_shell.d_res_low                                     2.9 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2203 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.704 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9AWE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.80 
_refine.ls_d_res_low                             90.05 
_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                     21781 
_refine.ls_number_reflns_R_free                  1095 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.43 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2526 
_refine.ls_R_factor_R_free                       0.2927 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2503 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 34.23 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.40 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4808 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             14 
_refine_hist.number_atoms_total               4822 
_refine_hist.d_res_high                       2.80 
_refine_hist.d_res_low                        90.05 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009 ? 6710 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.209 ? 6710 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.582 ? 678  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.065 ? 769  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 858  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.80 2.93  . . 128 2597 97.00 . . . . 0.3548 . . . . . . . . . . . 0.3971 
'X-RAY DIFFRACTION' 2.93 3.08  . . 137 2537 96.00 . . . . 0.3354 . . . . . . . . . . . 0.3541 
'X-RAY DIFFRACTION' 3.08 3.27  . . 136 2513 94.00 . . . . 0.3155 . . . . . . . . . . . 0.3942 
'X-RAY DIFFRACTION' 3.27 3.53  . . 132 2624 98.00 . . . . 0.2916 . . . . . . . . . . . 0.3817 
'X-RAY DIFFRACTION' 3.53 3.88  . . 136 2601 96.00 . . . . 0.2599 . . . . . . . . . . . 0.3253 
'X-RAY DIFFRACTION' 3.88 4.44  . . 137 2548 94.00 . . . . 0.2287 . . . . . . . . . . . 0.2685 
'X-RAY DIFFRACTION' 4.44 5.60  . . 148 2609 96.00 . . . . 0.2078 . . . . . . . . . . . 0.2500 
'X-RAY DIFFRACTION' 5.60 90.05 . . 141 2657 92.00 . . . . 0.2205 . . . . . . . . . . . 0.2364 
# 
_struct.entry_id                     9AWE 
_struct.title                        'The crystal structure of an engineered Protein GF with Human Kappa Fab' 
_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        9AWE 
_struct_keywords.text            'antibody, protein G, Fab, ASF1, Histone chaperone, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 4 ? 
E N N 5 ? 
F N N 5 ? 
G 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 PDB 9AWE       9AWE   ? 1 ? 1   
2 PDB 9AWE       9AWE   ? 2 ? 1   
3 UNP ASF1_YEAST P32447 ? 3 
;SIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSILVGPVPVGVNKFVFSADPPSA
ELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEG
;
2   
4 UNP SPG2_STRSG P19909 ? 4 TPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEKPE 368 
# 
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 9AWE B 1 ? 228 ? 9AWE   -1  ? 226 ? -1 226 
2 2 9AWE D 1 ? 215 ? 9AWE   0   ? 214 ? 0  214 
3 3 9AWE A 2 ? 159 ? P32447 2   ? 159 ? 2  159 
4 4 9AWE C 1 ? 63  ? P19909 368 ? 430 ? 2  64  
# 
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 
3 9AWE SER A 1   ? UNP P32447 ?   ?   'expression tag' 1   1  
3 9AWE LEU A 160 ? UNP P32447 ?   ?   'expression tag' 160 2  
3 9AWE GLU A 161 ? UNP P32447 ?   ?   'expression tag' 161 3  
4 9AWE ARG C 14  ? UNP P19909 LYS 381 conflict         15  4  
4 9AWE SER C 17  ? UNP P19909 LYS 384 conflict         18  5  
4 9AWE TYR C 19  ? UNP P19909 GLU 386 conflict         20  6  
4 9AWE THR C 23  ? UNP P19909 GLU 390 conflict         24  7  
4 9AWE PHE C 39  ? UNP P19909 ASN 406 conflict         40  8  
4 9AWE GLY C 40  ? UNP P19909 ASP 407 conflict         41  9  
4 9AWE LYS C 64  ? UNP P19909 ?   ?   'expression tag' 65  10 
4 9AWE LEU C 65  ? UNP P19909 ?   ?   'expression tag' 66  11 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_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 
# 
_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 65  ? LYS A 68  ? ASP B 63  LYS B 66  5 ? 4  
HELX_P HELX_P2  AA2 ARG A 90  ? THR A 94  ? ARG B 88  THR B 92  5 ? 5  
HELX_P HELX_P3  AA3 SER A 163 ? ALA A 165 ? SER B 161 ALA B 163 5 ? 3  
HELX_P HELX_P4  AA4 LYS A 208 ? ASN A 211 ? LYS B 206 ASN B 209 5 ? 4  
HELX_P HELX_P5  AA5 VAL B 30  ? SER B 32  ? VAL D 29  SER D 31  5 ? 3  
HELX_P HELX_P6  AA6 GLN B 80  ? PHE B 84  ? GLN D 79  PHE D 83  5 ? 5  
HELX_P HELX_P7  AA7 SER B 122 ? LYS B 127 ? SER D 121 LYS D 126 1 ? 6  
HELX_P HELX_P8  AA8 LYS B 184 ? HIS B 190 ? LYS D 183 HIS D 189 1 ? 7  
HELX_P HELX_P9  AA9 SER C 80  ? ILE C 84  ? SER A 80  ILE A 84  5 ? 5  
HELX_P HELX_P10 AB1 PRO C 85  ? VAL C 90  ? PRO A 85  VAL A 90  1 ? 6  
HELX_P HELX_P11 AB2 GLU C 119 ? ASN C 125 ? GLU A 119 ASN A 125 1 ? 7  
HELX_P HELX_P12 AB3 GLN C 131 ? ASP C 133 ? GLN A 131 ASP A 133 5 ? 3  
HELX_P HELX_P13 AB4 ASP D 26  ? TYR D 37  ? ASP C 27  TYR C 38  1 ? 12 
HELX_P HELX_P14 AB5 ASN D 41  ? GLY D 45  ? ASN C 42  GLY C 46  5 ? 5  
# 
_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 
disulf1 disulf ? ? A CYS 25  SG ? ? ? 1_555 A CYS 99  SG ? ? B CYS 23  B CYS 97  1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf2 disulf ? ? A CYS 147 SG ? ? ? 1_555 A CYS 203 SG ? ? B CYS 145 B CYS 201 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf3 disulf ? ? B CYS 24  SG ? ? ? 1_555 B CYS 89  SG ? ? D CYS 23  D CYS 88  1_555 ? ? ? ? ? ? ? 2.058 ? ? 
disulf4 disulf ? ? B CYS 135 SG ? ? ? 1_555 B CYS 195 SG ? ? D CYS 134 D CYS 194 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
# 
_struct_conn_type.id          disulf 
_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 CYS A 25  ? CYS A 99  ? CYS B 23  ? 1_555 CYS B 97  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 147 ? CYS A 203 ? CYS B 145 ? 1_555 CYS B 201 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 24  ? CYS B 89  ? CYS D 23  ? 1_555 CYS D 88  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS B 135 ? CYS B 195 ? CYS D 134 ? 1_555 CYS D 194 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 153 A . ? PHE 151 B PRO 154 A ? PRO 152 B 1 -14.29 
2 GLU 155 A . ? GLU 153 B PRO 156 A ? PRO 154 B 1 2.88   
3 SER 8   B . ? SER 7   D PRO 9   B ? PRO 8   D 1 -12.23 
4 TYR 141 B . ? TYR 140 D PRO 142 B ? PRO 141 D 1 -3.54  
5 ASN 14  C . ? ASN 14  A PRO 15  C ? PRO 15  A 1 -3.48  
6 GLY 63  C . ? GLY 63  A PRO 64  C ? PRO 64  A 1 2.52   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 6 ? 
AA7 ? 4 ? 
AA8 ? 6 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 3 ? 
AB4 ? 6 ? 
AB5 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 6   ? VAL A 8   ? GLN B 4   VAL B 6   
AA1 2 LEU A 21  ? SER A 28  ? LEU B 19  SER B 26  
AA1 3 THR A 81  ? MET A 86  ? THR B 79  MET B 84  
AA1 4 PHE A 71  ? ASP A 76  ? PHE B 69  ASP B 74  
AA2 1 GLY A 13  ? VAL A 15  ? GLY B 11  VAL B 13  
AA2 2 THR A 114 ? VAL A 118 ? THR B 112 VAL B 116 
AA2 3 ALA A 95  ? TYR A 103 ? ALA B 93  TYR B 101 
AA2 4 ILE A 37  ? GLN A 42  ? ILE B 35  GLN B 40  
AA2 5 GLU A 49  ? ILE A 54  ? GLU B 47  ILE B 52  
AA2 6 THR A 61  ? TYR A 63  ? THR B 59  TYR B 61  
AA3 1 GLY A 13  ? VAL A 15  ? GLY B 11  VAL B 13  
AA3 2 THR A 114 ? VAL A 118 ? THR B 112 VAL B 116 
AA3 3 ALA A 95  ? TYR A 103 ? ALA B 93  TYR B 101 
AA3 4 ALA A 106 ? TRP A 110 ? ALA B 104 TRP B 108 
AA4 1 SER A 127 ? LEU A 131 ? SER B 125 LEU B 129 
AA4 2 THR A 142 ? TYR A 152 ? THR B 140 TYR B 150 
AA4 3 TYR A 183 ? PRO A 192 ? TYR B 181 PRO B 190 
AA4 4 VAL A 170 ? THR A 172 ? VAL B 168 THR B 170 
AA5 1 SER A 127 ? LEU A 131 ? SER B 125 LEU B 129 
AA5 2 THR A 142 ? TYR A 152 ? THR B 140 TYR B 150 
AA5 3 TYR A 183 ? PRO A 192 ? TYR B 181 PRO B 190 
AA5 4 VAL A 176 ? LEU A 177 ? VAL B 174 LEU B 175 
AA6 1 THR A 158 ? TRP A 161 ? THR B 156 TRP B 159 
AA6 2 ILE A 202 ? HIS A 207 ? ILE B 200 HIS B 205 
AA6 3 THR A 212 ? LYS A 217 ? THR B 210 LYS B 215 
AA6 4 LEU D 16  ? TYR D 19  ? LEU C 17  TYR C 20  
AA6 5 VAL D 10  ? ASN D 12  ? VAL C 11  ASN C 13  
AA6 6 THR D 57  ? THR D 59  ? THR C 58  THR C 60  
AA7 1 THR B 6   ? SER B 8   ? THR D 5   SER D 7   
AA7 2 VAL B 20  ? ARG B 25  ? VAL D 19  ARG D 24  
AA7 3 ASP B 71  ? ILE B 76  ? ASP D 70  ILE D 75  
AA7 4 PHE B 63  ? SER B 68  ? PHE D 62  SER D 67  
AA8 1 SER B 11  ? ALA B 14  ? SER D 10  ALA D 13  
AA8 2 THR B 103 ? ILE B 107 ? THR D 102 ILE D 106 
AA8 3 THR B 86  ? ASP B 92  ? THR D 85  ASP D 91  
AA8 4 VAL B 34  ? GLN B 39  ? VAL D 33  GLN D 38  
AA8 5 LYS B 46  ? TYR B 50  ? LYS D 45  TYR D 49  
AA8 6 SER B 54  ? LEU B 55  ? SER D 53  LEU D 54  
AA9 1 SER B 11  ? ALA B 14  ? SER D 10  ALA D 13  
AA9 2 THR B 103 ? ILE B 107 ? THR D 102 ILE D 106 
AA9 3 THR B 86  ? ASP B 92  ? THR D 85  ASP D 91  
AA9 4 ILE B 97  ? PHE B 99  ? ILE D 96  PHE D 98  
AB1 1 SER B 115 ? PHE B 119 ? SER D 114 PHE D 118 
AB1 2 THR B 130 ? PHE B 140 ? THR D 129 PHE D 139 
AB1 3 TYR B 174 ? SER B 183 ? TYR D 173 SER D 182 
AB1 4 SER B 160 ? VAL B 164 ? SER D 159 VAL D 163 
AB2 1 ALA B 154 ? LEU B 155 ? ALA D 153 LEU D 154 
AB2 2 VAL B 147 ? VAL B 151 ? VAL D 146 VAL D 150 
AB2 3 TYR B 193 ? VAL B 197 ? TYR D 192 VAL D 196 
AB2 4 VAL B 206 ? PHE B 210 ? VAL D 205 PHE D 209 
AB3 1 VAL C 4   ? VAL C 11  ? VAL A 4   VAL A 11  
AB3 2 TYR C 22  ? CYS C 30  ? TYR A 22  CYS A 30  
AB3 3 GLY C 68  ? ALA C 76  ? GLY A 68  ALA A 76  
AB4 1 ALA C 16  ? LYS C 17  ? ALA A 16  LYS A 17  
AB4 2 ILE C 135 ? ILE C 139 ? ILE A 135 ILE A 139 
AB4 3 ARG C 104 ? TYR C 117 ? ARG A 104 TYR A 117 
AB4 4 THR C 93  ? TYR C 101 ? THR A 93  TYR A 101 
AB4 5 LEU C 38  ? VAL C 45  ? LEU A 38  VAL A 45  
AB4 6 ASP C 54  ? VAL C 62  ? ASP A 54  VAL A 62  
AB5 1 ALA C 16  ? LYS C 17  ? ALA A 16  LYS A 17  
AB5 2 ILE C 135 ? ILE C 139 ? ILE A 135 ILE A 139 
AB5 3 ARG C 104 ? TYR C 117 ? ARG A 104 TYR A 117 
AB5 4 ARG C 145 ? ARG C 148 ? ARG A 145 ARG A 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 8   ? N VAL B 6   O ALA A 26  ? O ALA B 24  
AA1 2 3 N LEU A 21  ? N LEU B 19  O MET A 86  ? O MET B 84  
AA1 3 4 O TYR A 83  ? O TYR B 81  N SER A 74  ? N SER B 72  
AA2 1 2 N GLY A 13  ? N GLY B 11  O THR A 117 ? O THR B 115 
AA2 2 3 O THR A 114 ? O THR B 112 N TYR A 97  ? N TYR B 95  
AA2 3 4 O TYR A 98  ? O TYR B 96  N VAL A 40  ? N VAL B 38  
AA2 4 5 N ILE A 37  ? N ILE B 35  O ILE A 54  ? O ILE B 52  
AA2 5 6 N SER A 53  ? N SER B 51  O SER A 62  ? O SER B 60  
AA3 1 2 N GLY A 13  ? N GLY B 11  O THR A 117 ? O THR B 115 
AA3 2 3 O THR A 114 ? O THR B 112 N TYR A 97  ? N TYR B 95  
AA3 3 4 N TYR A 103 ? N TYR B 101 O ALA A 106 ? O ALA B 104 
AA4 1 2 N PHE A 129 ? N PHE B 127 O LEU A 148 ? O LEU B 146 
AA4 2 3 N ALA A 143 ? N ALA B 141 O VAL A 191 ? O VAL B 189 
AA4 3 4 O VAL A 188 ? O VAL B 186 N HIS A 171 ? N HIS B 169 
AA5 1 2 N PHE A 129 ? N PHE B 127 O LEU A 148 ? O LEU B 146 
AA5 2 3 N ALA A 143 ? N ALA B 141 O VAL A 191 ? O VAL B 189 
AA5 3 4 O SER A 184 ? O SER B 182 N VAL A 176 ? N VAL B 174 
AA6 1 2 N SER A 160 ? N SER B 158 O ASN A 204 ? O ASN B 202 
AA6 2 3 N HIS A 207 ? N HIS B 205 O THR A 212 ? O THR B 210 
AA6 3 4 N ASP A 215 ? N ASP B 213 O SER D 17  ? O SER C 18  
AA6 4 5 O GLY D 18  ? O GLY C 19  N ILE D 11  ? N ILE C 12  
AA6 5 6 N VAL D 10  ? N VAL C 11  O VAL D 58  ? O VAL C 59  
AA7 1 2 N SER B 8   ? N SER D 7   O THR B 23  ? O THR D 22  
AA7 2 3 N CYS B 24  ? N CYS D 23  O PHE B 72  ? O PHE D 71  
AA7 3 4 O ASP B 71  ? O ASP D 70  N SER B 68  ? N SER D 67  
AA8 1 2 N LEU B 12  ? N LEU D 11  O LYS B 104 ? O LYS D 103 
AA8 2 3 O THR B 103 ? O THR D 102 N TYR B 87  ? N TYR D 86  
AA8 3 4 O GLN B 90  ? O GLN D 89  N ALA B 35  ? N ALA D 34  
AA8 4 5 N TRP B 36  ? N TRP D 35  O LEU B 48  ? O LEU D 47  
AA8 5 6 N TYR B 50  ? N TYR D 49  O SER B 54  ? O SER D 53  
AA9 1 2 N LEU B 12  ? N LEU D 11  O LYS B 104 ? O LYS D 103 
AA9 2 3 O THR B 103 ? O THR D 102 N TYR B 87  ? N TYR D 86  
AA9 3 4 N GLN B 91  ? N GLN D 90  O THR B 98  ? O THR D 97  
AB1 1 2 N PHE B 117 ? N PHE D 116 O LEU B 136 ? O LEU D 135 
AB1 2 3 N VAL B 133 ? N VAL D 132 O LEU B 180 ? O LEU D 179 
AB1 3 4 O THR B 179 ? O THR D 178 N GLN B 161 ? N GLN D 160 
AB2 1 2 O ALA B 154 ? O ALA D 153 N VAL B 151 ? N VAL D 150 
AB2 2 3 N LYS B 150 ? N LYS D 149 O ALA B 194 ? O ALA D 193 
AB2 3 4 N CYS B 195 ? N CYS D 194 O LYS B 208 ? O LYS D 207 
AB3 1 2 N LYS C 10  ? N LYS A 10  O GLU C 25  ? O GLU A 25  
AB3 2 3 N TYR C 22  ? N TYR A 22  O ALA C 76  ? O ALA A 76  
AB4 1 2 N ALA C 16  ? N ALA A 16  O ARG C 137 ? O ARG A 137 
AB4 2 3 O VAL C 136 ? O VAL A 136 N GLU C 116 ? N GLU A 116 
AB4 3 4 O ARG C 104 ? O ARG A 104 N TYR C 101 ? N TYR A 101 
AB4 4 5 O SER C 98  ? O SER A 98  N LYS C 41  ? N LYS A 41  
AB4 5 6 N LEU C 42  ? N LEU A 42  O LEU C 57  ? O LEU A 57  
AB5 1 2 N ALA C 16  ? N ALA A 16  O ARG C 137 ? O ARG A 137 
AB5 2 3 O VAL C 136 ? O VAL A 136 N GLU C 116 ? N GLU A 116 
AB5 3 4 N GLY C 110 ? N GLY A 110 O ARG C 145 ? O ARG A 145 
# 
_pdbx_entry_details.entry_id                   9AWE 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 TYR B 55  ? ? 57.69   -62.09  
2  1 SER B 58  ? ? 69.22   125.74  
3  1 SER B 137 ? ? -68.62  -117.05 
4  1 ALA D 51  ? ? 63.50   -51.60  
5  1 SER D 77  ? ? -166.77 106.60  
6  1 LEU D 78  ? ? -45.84  160.26  
7  1 ALA D 84  ? ? -162.58 -165.81 
8  1 SER D 121 ? ? 65.02   142.64  
9  1 ASN D 138 ? ? 55.02   80.32   
10 1 GLU D 143 ? ? -53.08  104.73  
11 1 THR D 197 ? ? -114.75 59.39   
12 1 ASN D 210 ? ? -136.06 -155.98 
13 1 ASN A 13  ? ? -95.97  52.79   
14 1 GLU A 32  ? ? 65.17   88.66   
15 1 ASP A 37  ? ? 76.50   160.34  
16 1 ARG A 49  ? ? -16.17  -68.99  
17 1 TYR C 38  ? ? -85.15  32.59   
18 1 ALA C 39  ? ? -101.76 72.89   
19 1 PHE C 40  ? ? -57.92  66.25   
20 1 ASP C 45  ? ? -103.22 79.48   
21 1 GLU C 61  ? ? -120.04 -74.48  
22 1 LYS C 62  ? ? 80.86   136.11  
# 
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 16.592 19.538 30.617  1.1214 0.5236 0.4100 0.0926  0.4028 -0.0375 1.1577 0.4531 1.6672 0.0454  
0.5186  0.7436 0.2435 0.0149  0.1680  -0.3199 0.0817  -0.0208 0.1068  -0.2015 -0.4015 
'X-RAY DIFFRACTION' 2 ? refined 11.217 2.863  27.165  1.0212 0.6182 0.4623 -0.1879 0.2443 0.0336  0.4952 0.2642 1.6167 -0.3449 
-0.0977 0.2407 0.3684 -0.1309 -0.2032 -0.2259 -0.0500 0.3628  0.3312  0.2060  -0.7322 
'X-RAY DIFFRACTION' 3 ? refined 19.674 26.539 -10.482 1.9231 0.5339 0.4817 0.1401  0.2034 -0.0082 0.7519 1.4331 2.6008 -0.7523 
-0.9596 0.2203 0.2623 -0.0266 0.0115  0.1653  0.2063  0.1179  -0.6209 -1.2473 -0.1074 
'X-RAY DIFFRACTION' 4 ? refined 17.448 26.331 57.963  1.6120 0.8726 0.6904 -0.3091 0.2905 -0.1164 6.1035 4.1075 7.2174 -4.1962 
1.3397  0.6674 0.4090 -0.1650 -0.2251 -0.5924 0.5306  -0.1764 0.6940  -0.8412 -0.9506 
# 
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 219 '( CHAIN B AND RESID 2:219 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 D 4  D 212 '( CHAIN D AND RESID 4:212 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 3 3 A 2  A 154 '( CHAIN A AND RESID 2:154 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 4 4 C 10 C 63  '( CHAIN C AND RESID 10:63 )' ? ? ? ? ? 
# 
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 GLU -1  ? A GLU 1   
2  1 Y 1 B ILE 0   ? A ILE 2   
3  1 Y 1 B SER 1   ? A SER 3   
4  1 Y 1 B SER 220 ? A SER 222 
5  1 Y 1 B CYS 221 ? A CYS 223 
6  1 Y 1 B ASP 222 ? A ASP 224 
7  1 Y 1 B LYS 223 ? A LYS 225 
8  1 Y 1 B THR 224 ? A THR 226 
9  1 Y 1 B HIS 225 ? A HIS 227 
10 1 Y 1 B THR 226 ? A THR 228 
11 1 Y 1 D SER 0   ? B SER 1   
12 1 Y 1 D ASP 1   ? B ASP 2   
13 1 Y 1 D ILE 2   ? B ILE 3   
14 1 Y 1 D GLN 3   ? B GLN 4   
15 1 Y 1 D GLU 213 ? B GLU 214 
16 1 Y 1 D CYS 214 ? B CYS 215 
17 1 Y 1 A SER 1   ? C SER 1   
18 1 Y 1 A ASN 155 ? C ASN 155 
19 1 Y 1 A GLU 156 ? C GLU 156 
20 1 Y 1 A ASN 157 ? C ASN 157 
21 1 Y 1 A GLU 158 ? C GLU 158 
22 1 Y 1 A GLY 159 ? C GLY 159 
23 1 Y 1 A LEU 160 ? C LEU 160 
24 1 Y 1 A GLU 161 ? C GLU 161 
25 1 Y 1 C THR 2   ? D THR 1   
26 1 Y 1 C PRO 3   ? D PRO 2   
27 1 Y 1 C ALA 4   ? D ALA 3   
28 1 Y 1 C VAL 5   ? D VAL 4   
29 1 Y 1 C THR 6   ? D THR 5   
30 1 Y 1 C THR 7   ? D THR 6   
31 1 Y 1 C TYR 8   ? D TYR 7   
32 1 Y 1 C LYS 9   ? D LYS 8   
33 1 Y 1 C TYR 50  ? D TYR 49  
34 1 Y 1 C GLU 64  ? D GLU 63  
35 1 Y 1 C LYS 65  ? D LYS 64  
36 1 Y 1 C LEU 66  ? D LEU 65  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R01GM117372 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9AVO 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9AWE 
_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]   0.017280 
_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]   0.011674 
_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]   0.005552 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU A 1 4   ? 36.945  24.165  15.634  1.00 101.87 ? 2   GLU B N   1 
ATOM   2    C CA  . GLU A 1 4   ? 35.756  23.320  15.623  1.00 99.00  ? 2   GLU B CA  1 
ATOM   3    C C   . GLU A 1 4   ? 34.494  24.179  15.788  1.00 96.53  ? 2   GLU B C   1 
ATOM   4    O O   . GLU A 1 4   ? 34.443  25.097  16.611  1.00 96.51  ? 2   GLU B O   1 
ATOM   5    C CB  . GLU A 1 4   ? 35.850  22.251  16.720  1.00 101.81 ? 2   GLU B CB  1 
ATOM   6    C CG  . GLU A 1 4   ? 34.513  21.765  17.266  1.00 106.72 ? 2   GLU B CG  1 
ATOM   7    C CD  . GLU A 1 4   ? 34.608  21.260  18.704  1.00 110.41 ? 2   GLU B CD  1 
ATOM   8    O OE1 . GLU A 1 4   ? 34.686  20.023  18.893  1.00 117.78 ? 2   GLU B OE1 1 
ATOM   9    O OE2 . GLU A 1 4   ? 34.582  22.095  19.642  1.00 105.13 ? 2   GLU B OE2 1 
ATOM   10   N N   . VAL A 1 5   ? 33.492  23.882  14.970  1.00 81.31  ? 3   VAL B N   1 
ATOM   11   C CA  . VAL A 1 5   ? 32.223  24.601  14.986  1.00 75.10  ? 3   VAL B CA  1 
ATOM   12   C C   . VAL A 1 5   ? 31.349  24.131  16.148  1.00 75.15  ? 3   VAL B C   1 
ATOM   13   O O   . VAL A 1 5   ? 31.110  22.928  16.322  1.00 75.03  ? 3   VAL B O   1 
ATOM   14   C CB  . VAL A 1 5   ? 31.523  24.451  13.625  1.00 64.87  ? 3   VAL B CB  1 
ATOM   15   C CG1 . VAL A 1 5   ? 31.556  23.031  13.214  1.00 66.99  ? 3   VAL B CG1 1 
ATOM   16   C CG2 . VAL A 1 5   ? 30.064  24.874  13.707  1.00 63.12  ? 3   VAL B CG2 1 
ATOM   17   N N   . GLN A 1 6   ? 30.869  25.091  16.951  1.00 71.16  ? 4   GLN B N   1 
ATOM   18   C CA  . GLN A 1 6   ? 30.001  24.832  18.092  1.00 67.34  ? 4   GLN B CA  1 
ATOM   19   C C   . GLN A 1 6   ? 28.701  25.612  17.952  1.00 60.62  ? 4   GLN B C   1 
ATOM   20   O O   . GLN A 1 6   ? 28.579  26.509  17.117  1.00 62.40  ? 4   GLN B O   1 
ATOM   21   C CB  . GLN A 1 6   ? 30.692  25.209  19.398  1.00 68.06  ? 4   GLN B CB  1 
ATOM   22   C CG  . GLN A 1 6   ? 31.551  24.091  19.943  1.00 81.07  ? 4   GLN B CG  1 
ATOM   23   C CD  . GLN A 1 6   ? 32.857  24.607  20.516  1.00 89.47  ? 4   GLN B CD  1 
ATOM   24   O OE1 . GLN A 1 6   ? 32.874  25.315  21.544  1.00 88.10  ? 4   GLN B OE1 1 
ATOM   25   N NE2 . GLN A 1 6   ? 33.966  24.282  19.836  1.00 88.66  ? 4   GLN B NE2 1 
ATOM   26   N N   . LEU A 1 7   ? 27.721  25.250  18.771  1.00 57.21  ? 5   LEU B N   1 
ATOM   27   C CA  . LEU A 1 7   ? 26.428  25.926  18.802  1.00 58.44  ? 5   LEU B CA  1 
ATOM   28   C C   . LEU A 1 7   ? 25.922  25.839  20.231  1.00 62.28  ? 5   LEU B C   1 
ATOM   29   O O   . LEU A 1 7   ? 25.852  24.746  20.800  1.00 67.46  ? 5   LEU B O   1 
ATOM   30   C CB  . LEU A 1 7   ? 25.423  25.299  17.828  1.00 58.88  ? 5   LEU B CB  1 
ATOM   31   C CG  . LEU A 1 7   ? 25.413  25.790  16.371  1.00 60.34  ? 5   LEU B CG  1 
ATOM   32   C CD1 . LEU A 1 7   ? 24.089  25.443  15.649  1.00 54.89  ? 5   LEU B CD1 1 
ATOM   33   C CD2 . LEU A 1 7   ? 25.665  27.302  16.344  1.00 59.47  ? 5   LEU B CD2 1 
ATOM   34   N N   . VAL A 1 8   ? 25.605  26.982  20.831  1.00 62.02  ? 6   VAL B N   1 
ATOM   35   C CA  . VAL A 1 8   ? 25.321  27.047  22.258  1.00 57.75  ? 6   VAL B CA  1 
ATOM   36   C C   . VAL A 1 8   ? 24.028  27.814  22.453  1.00 58.43  ? 6   VAL B C   1 
ATOM   37   O O   . VAL A 1 8   ? 23.954  29.002  22.120  1.00 64.62  ? 6   VAL B O   1 
ATOM   38   C CB  . VAL A 1 8   ? 26.466  27.715  23.034  1.00 55.55  ? 6   VAL B CB  1 
ATOM   39   C CG1 . VAL A 1 8   ? 26.403  27.328  24.501  1.00 56.00  ? 6   VAL B CG1 1 
ATOM   40   C CG2 . VAL A 1 8   ? 27.812  27.341  22.433  1.00 56.13  ? 6   VAL B CG2 1 
ATOM   41   N N   . GLU A 1 9   ? 23.019  27.147  22.991  1.00 56.74  ? 7   GLU B N   1 
ATOM   42   C CA  . GLU A 1 9   ? 21.780  27.803  23.386  1.00 61.21  ? 7   GLU B CA  1 
ATOM   43   C C   . GLU A 1 9   ? 21.903  28.473  24.768  1.00 62.39  ? 7   GLU B C   1 
ATOM   44   O O   . GLU A 1 9   ? 22.804  28.185  25.558  1.00 61.30  ? 7   GLU B O   1 
ATOM   45   C CB  . GLU A 1 9   ? 20.638  26.789  23.395  1.00 60.05  ? 7   GLU B CB  1 
ATOM   46   C CG  . GLU A 1 9   ? 20.362  26.144  22.068  1.00 56.44  ? 7   GLU B CG  1 
ATOM   47   C CD  . GLU A 1 9   ? 21.124  24.836  21.876  1.00 59.48  ? 7   GLU B CD  1 
ATOM   48   O OE1 . GLU A 1 9   ? 22.222  24.689  22.466  1.00 59.99  ? 7   GLU B OE1 1 
ATOM   49   O OE2 . GLU A 1 9   ? 20.639  23.962  21.108  1.00 58.39  ? 7   GLU B OE2 1 
ATOM   50   N N   . SER A 1 10  ? 20.954  29.363  25.057  1.00 65.37  ? 8   SER B N   1 
ATOM   51   C CA  . SER A 1 10  ? 20.981  30.240  26.228  1.00 64.11  ? 8   SER B CA  1 
ATOM   52   C C   . SER A 1 10  ? 19.628  30.895  26.409  1.00 64.95  ? 8   SER B C   1 
ATOM   53   O O   . SER A 1 10  ? 18.867  31.069  25.455  1.00 64.25  ? 8   SER B O   1 
ATOM   54   C CB  . SER A 1 10  ? 22.039  31.345  26.128  1.00 61.54  ? 8   SER B CB  1 
ATOM   55   O OG  . SER A 1 10  ? 23.286  30.891  26.613  1.00 70.63  ? 8   SER B OG  1 
ATOM   56   N N   . GLY A 1 11  ? 19.371  31.312  27.647  1.00 70.24  ? 9   GLY B N   1 
ATOM   57   C CA  . GLY A 1 11  ? 18.132  31.968  27.994  1.00 66.83  ? 9   GLY B CA  1 
ATOM   58   C C   . GLY A 1 11  ? 17.039  31.036  28.461  1.00 69.36  ? 9   GLY B C   1 
ATOM   59   O O   . GLY A 1 11  ? 15.885  31.474  28.581  1.00 67.00  ? 9   GLY B O   1 
ATOM   60   N N   . GLY A 1 12  ? 17.356  29.765  28.725  1.00 74.39  ? 10  GLY B N   1 
ATOM   61   C CA  . GLY A 1 12  ? 16.357  28.847  29.246  1.00 73.81  ? 10  GLY B CA  1 
ATOM   62   C C   . GLY A 1 12  ? 16.020  29.112  30.707  1.00 74.87  ? 10  GLY B C   1 
ATOM   63   O O   . GLY A 1 12  ? 16.813  29.663  31.472  1.00 76.01  ? 10  GLY B O   1 
ATOM   64   N N   . GLY A 1 13  ? 14.814  28.722  31.094  1.00 59.22  ? 11  GLY B N   1 
ATOM   65   C CA  . GLY A 1 13  ? 14.446  28.814  32.483  1.00 59.89  ? 11  GLY B CA  1 
ATOM   66   C C   . GLY A 1 13  ? 12.959  28.642  32.689  1.00 63.89  ? 11  GLY B C   1 
ATOM   67   O O   . GLY A 1 13  ? 12.273  28.000  31.891  1.00 60.45  ? 11  GLY B O   1 
ATOM   68   N N   . LEU A 1 14  ? 12.465  29.206  33.789  1.00 61.60  ? 12  LEU B N   1 
ATOM   69   C CA  . LEU A 1 14  ? 11.060  29.080  34.118  1.00 62.42  ? 12  LEU B CA  1 
ATOM   70   C C   . LEU A 1 14  ? 10.363  30.351  33.669  1.00 63.52  ? 12  LEU B C   1 
ATOM   71   O O   . LEU A 1 14  ? 10.952  31.434  33.672  1.00 63.98  ? 12  LEU B O   1 
ATOM   72   C CB  . LEU A 1 14  ? 10.874  28.821  35.618  1.00 63.01  ? 12  LEU B CB  1 
ATOM   73   C CG  . LEU A 1 14  ? 9.500   28.962  36.281  1.00 66.35  ? 12  LEU B CG  1 
ATOM   74   C CD1 . LEU A 1 14  ? 8.474   28.036  35.644  1.00 67.97  ? 12  LEU B CD1 1 
ATOM   75   C CD2 . LEU A 1 14  ? 9.570   28.710  37.789  1.00 73.78  ? 12  LEU B CD2 1 
ATOM   76   N N   . VAL A 1 15  ? 9.118   30.201  33.230  1.00 64.00  ? 13  VAL B N   1 
ATOM   77   C CA  . VAL A 1 15  ? 8.348   31.308  32.679  1.00 65.11  ? 13  VAL B CA  1 
ATOM   78   C C   . VAL A 1 15  ? 6.879   31.029  32.965  1.00 66.01  ? 13  VAL B C   1 
ATOM   79   O O   . VAL A 1 15  ? 6.453   29.875  33.031  1.00 67.29  ? 13  VAL B O   1 
ATOM   80   C CB  . VAL A 1 15  ? 8.634   31.482  31.157  1.00 70.70  ? 13  VAL B CB  1 
ATOM   81   C CG1 . VAL A 1 15  ? 7.463   32.107  30.415  1.00 72.83  ? 13  VAL B CG1 1 
ATOM   82   C CG2 . VAL A 1 15  ? 9.882   32.341  30.917  1.00 72.19  ? 13  VAL B CG2 1 
ATOM   83   N N   . GLN A 1 16  ? 6.112   32.095  33.176  1.00 69.73  ? 14  GLN B N   1 
ATOM   84   C CA  . GLN A 1 16  ? 4.676   32.009  33.385  1.00 73.15  ? 14  GLN B CA  1 
ATOM   85   C C   . GLN A 1 16  ? 3.935   31.761  32.083  1.00 72.35  ? 14  GLN B C   1 
ATOM   86   O O   . GLN A 1 16  ? 4.304   32.313  31.046  1.00 74.54  ? 14  GLN B O   1 
ATOM   87   C CB  . GLN A 1 16  ? 4.145   33.305  33.944  1.00 78.90  ? 14  GLN B CB  1 
ATOM   88   C CG  . GLN A 1 16  ? 4.747   33.773  35.183  1.00 86.88  ? 14  GLN B CG  1 
ATOM   89   C CD  . GLN A 1 16  ? 3.669   34.158  36.147  1.00 94.27  ? 14  GLN B CD  1 
ATOM   90   O OE1 . GLN A 1 16  ? 2.541   33.671  36.067  1.00 88.53  ? 14  GLN B OE1 1 
ATOM   91   N NE2 . GLN A 1 16  ? 3.982   35.093  37.025  1.00 102.30 ? 14  GLN B NE2 1 
ATOM   92   N N   . PRO A 1 17  ? 2.826   31.027  32.134  1.00 72.07  ? 15  PRO B N   1 
ATOM   93   C CA  . PRO A 1 17  ? 1.911   30.984  30.983  1.00 73.54  ? 15  PRO B CA  1 
ATOM   94   C C   . PRO A 1 17  ? 1.597   32.390  30.461  1.00 75.18  ? 15  PRO B C   1 
ATOM   95   O O   . PRO A 1 17  ? 1.447   33.345  31.225  1.00 75.89  ? 15  PRO B O   1 
ATOM   96   C CB  . PRO A 1 17  ? 0.669   30.294  31.558  1.00 73.17  ? 15  PRO B CB  1 
ATOM   97   C CG  . PRO A 1 17  ? 1.230   29.426  32.691  1.00 71.69  ? 15  PRO B CG  1 
ATOM   98   C CD  . PRO A 1 17  ? 2.303   30.287  33.297  1.00 70.33  ? 15  PRO B CD  1 
ATOM   99   N N   . GLY A 1 18  ? 1.525   32.530  29.143  1.00 76.13  ? 16  GLY B N   1 
ATOM   100  C CA  . GLY A 1 18  ? 1.415   33.840  28.538  1.00 75.28  ? 16  GLY B CA  1 
ATOM   101  C C   . GLY A 1 18  ? 2.667   34.687  28.611  1.00 74.79  ? 16  GLY B C   1 
ATOM   102  O O   . GLY A 1 18  ? 2.665   35.805  28.075  1.00 77.19  ? 16  GLY B O   1 
ATOM   103  N N   . GLY A 1 19  ? 3.735   34.192  29.242  1.00 69.78  ? 17  GLY B N   1 
ATOM   104  C CA  . GLY A 1 19  ? 4.955   34.959  29.403  1.00 70.47  ? 17  GLY B CA  1 
ATOM   105  C C   . GLY A 1 19  ? 5.822   35.025  28.150  1.00 75.49  ? 17  GLY B C   1 
ATOM   106  O O   . GLY A 1 19  ? 5.645   34.304  27.163  1.00 75.44  ? 17  GLY B O   1 
ATOM   107  N N   . SER A 1 20  ? 6.797   35.929  28.206  1.00 72.31  ? 18  SER B N   1 
ATOM   108  C CA  . SER A 1 20  ? 7.738   36.156  27.118  1.00 72.01  ? 18  SER B CA  1 
ATOM   109  C C   . SER A 1 20  ? 9.111   35.626  27.511  1.00 70.43  ? 18  SER B C   1 
ATOM   110  O O   . SER A 1 20  ? 9.642   35.998  28.562  1.00 67.37  ? 18  SER B O   1 
ATOM   111  C CB  . SER A 1 20  ? 7.837   37.650  26.779  1.00 70.59  ? 18  SER B CB  1 
ATOM   112  O OG  . SER A 1 20  ? 9.199   38.075  26.720  1.00 69.60  ? 18  SER B OG  1 
ATOM   113  N N   . LEU A 1 21  ? 9.693   34.773  26.661  1.00 70.98  ? 19  LEU B N   1 
ATOM   114  C CA  . LEU A 1 21  ? 11.075  34.343  26.820  1.00 66.96  ? 19  LEU B CA  1 
ATOM   115  C C   . LEU A 1 21  ? 11.826  34.603  25.519  1.00 67.84  ? 19  LEU B C   1 
ATOM   116  O O   . LEU A 1 21  ? 11.215  34.784  24.463  1.00 69.98  ? 19  LEU B O   1 
ATOM   117  C CB  . LEU A 1 21  ? 11.164  32.861  27.212  1.00 68.06  ? 19  LEU B CB  1 
ATOM   118  C CG  . LEU A 1 21  ? 12.514  32.412  27.791  1.00 68.22  ? 19  LEU B CG  1 
ATOM   119  C CD1 . LEU A 1 21  ? 13.002  33.392  28.853  1.00 65.73  ? 19  LEU B CD1 1 
ATOM   120  C CD2 . LEU A 1 21  ? 12.496  30.982  28.309  1.00 65.02  ? 19  LEU B CD2 1 
ATOM   121  N N   . ARG A 1 22  ? 13.161  34.639  25.599  1.00 64.86  ? 20  ARG B N   1 
ATOM   122  C CA  . ARG A 1 22  ? 14.003  34.814  24.414  1.00 64.83  ? 20  ARG B CA  1 
ATOM   123  C C   . ARG A 1 22  ? 15.290  34.010  24.526  1.00 64.98  ? 20  ARG B C   1 
ATOM   124  O O   . ARG A 1 22  ? 16.183  34.347  25.312  1.00 62.26  ? 20  ARG B O   1 
ATOM   125  C CB  . ARG A 1 22  ? 14.340  36.279  24.163  1.00 67.42  ? 20  ARG B CB  1 
ATOM   126  C CG  . ARG A 1 22  ? 14.310  36.602  22.680  1.00 68.30  ? 20  ARG B CG  1 
ATOM   127  C CD  . ARG A 1 22  ? 14.950  37.932  22.335  1.00 69.69  ? 20  ARG B CD  1 
ATOM   128  N NE  . ARG A 1 22  ? 16.242  38.142  22.986  1.00 72.66  ? 20  ARG B NE  1 
ATOM   129  C CZ  . ARG A 1 22  ? 17.190  38.962  22.533  1.00 75.26  ? 20  ARG B CZ  1 
ATOM   130  N NH1 . ARG A 1 22  ? 17.079  39.572  21.353  1.00 72.35  ? 20  ARG B NH1 1 
ATOM   131  N NH2 . ARG A 1 22  ? 18.295  39.146  23.263  1.00 70.59  ? 20  ARG B NH2 1 
ATOM   132  N N   . LEU A 1 23  ? 15.420  33.009  23.665  1.00 67.16  ? 21  LEU B N   1 
ATOM   133  C CA  . LEU A 1 23  ? 16.632  32.215  23.589  1.00 63.69  ? 21  LEU B CA  1 
ATOM   134  C C   . LEU A 1 23  ? 17.611  32.816  22.590  1.00 60.21  ? 21  LEU B C   1 
ATOM   135  O O   . LEU A 1 23  ? 17.247  33.590  21.706  1.00 61.06  ? 21  LEU B O   1 
ATOM   136  C CB  . LEU A 1 23  ? 16.314  30.774  23.206  1.00 61.56  ? 21  LEU B CB  1 
ATOM   137  C CG  . LEU A 1 23  ? 15.003  30.213  23.745  1.00 61.42  ? 21  LEU B CG  1 
ATOM   138  C CD1 . LEU A 1 23  ? 14.946  28.742  23.471  1.00 59.96  ? 21  LEU B CD1 1 
ATOM   139  C CD2 . LEU A 1 23  ? 14.872  30.448  25.229  1.00 66.56  ? 21  LEU B CD2 1 
ATOM   140  N N   . SER A 1 24  ? 18.870  32.429  22.745  1.00 59.65  ? 22  SER B N   1 
ATOM   141  C CA  . SER A 1 24  ? 19.964  32.933  21.932  1.00 61.23  ? 22  SER B CA  1 
ATOM   142  C C   . SER A 1 24  ? 20.853  31.758  21.538  1.00 63.44  ? 22  SER B C   1 
ATOM   143  O O   . SER A 1 24  ? 21.368  31.041  22.404  1.00 64.48  ? 22  SER B O   1 
ATOM   144  C CB  . SER A 1 24  ? 20.743  34.000  22.703  1.00 60.73  ? 22  SER B CB  1 
ATOM   145  O OG  . SER A 1 24  ? 21.696  33.380  23.548  1.00 61.39  ? 22  SER B OG  1 
ATOM   146  N N   . CYS A 1 25  ? 21.010  31.544  20.237  1.00 61.76  ? 23  CYS B N   1 
ATOM   147  C CA  . CYS A 1 25  ? 21.848  30.475  19.704  1.00 59.46  ? 23  CYS B CA  1 
ATOM   148  C C   . CYS A 1 25  ? 23.192  31.096  19.319  1.00 61.42  ? 23  CYS B C   1 
ATOM   149  O O   . CYS A 1 25  ? 23.280  31.832  18.331  1.00 63.62  ? 23  CYS B O   1 
ATOM   150  C CB  . CYS A 1 25  ? 21.148  29.802  18.521  1.00 59.01  ? 23  CYS B CB  1 
ATOM   151  S SG  . CYS A 1 25  ? 22.058  28.463  17.684  1.00 56.29  ? 23  CYS B SG  1 
ATOM   152  N N   . ALA A 1 26  ? 24.223  30.839  20.126  1.00 59.66  ? 24  ALA B N   1 
ATOM   153  C CA  . ALA A 1 26  ? 25.534  31.465  19.966  1.00 58.57  ? 24  ALA B CA  1 
ATOM   154  C C   . ALA A 1 26  ? 26.444  30.564  19.149  1.00 58.37  ? 24  ALA B C   1 
ATOM   155  O O   . ALA A 1 26  ? 26.658  29.405  19.521  1.00 60.42  ? 24  ALA B O   1 
ATOM   156  C CB  . ALA A 1 26  ? 26.181  31.735  21.322  1.00 58.32  ? 24  ALA B CB  1 
ATOM   157  N N   . ALA A 1 27  ? 27.022  31.107  18.078  1.00 58.17  ? 25  ALA B N   1 
ATOM   158  C CA  . ALA A 1 27  ? 27.765  30.320  17.098  1.00 57.82  ? 25  ALA B CA  1 
ATOM   159  C C   . ALA A 1 27  ? 29.272  30.500  17.239  1.00 58.08  ? 25  ALA B C   1 
ATOM   160  O O   . ALA A 1 27  ? 29.751  31.578  17.596  1.00 61.20  ? 25  ALA B O   1 
ATOM   161  C CB  . ALA A 1 27  ? 27.340  30.690  15.674  1.00 58.27  ? 25  ALA B CB  1 
ATOM   162  N N   . SER A 1 28  ? 30.015  29.446  16.939  1.00 57.35  ? 26  SER B N   1 
ATOM   163  C CA  . SER A 1 28  ? 31.466  29.515  16.874  1.00 61.95  ? 26  SER B CA  1 
ATOM   164  C C   . SER A 1 28  ? 31.959  28.577  15.774  1.00 66.45  ? 26  SER B C   1 
ATOM   165  O O   . SER A 1 28  ? 31.377  27.510  15.540  1.00 64.65  ? 26  SER B O   1 
ATOM   166  C CB  . SER A 1 28  ? 32.113  29.161  18.223  1.00 62.42  ? 26  SER B CB  1 
ATOM   167  O OG  . SER A 1 28  ? 33.460  28.734  18.048  1.00 64.73  ? 26  SER B OG  1 
ATOM   168  N N   . GLY A 1 29  ? 33.026  28.990  15.088  1.00 64.66  ? 27  GLY B N   1 
ATOM   169  C CA  . GLY A 1 29  ? 33.543  28.268  13.944  1.00 63.58  ? 27  GLY B CA  1 
ATOM   170  C C   . GLY A 1 29  ? 32.915  28.631  12.617  1.00 60.13  ? 27  GLY B C   1 
ATOM   171  O O   . GLY A 1 29  ? 33.306  28.060  11.592  1.00 58.57  ? 27  GLY B O   1 
ATOM   172  N N   . PHE A 1 30  ? 31.965  29.562  12.595  1.00 59.82  ? 28  PHE B N   1 
ATOM   173  C CA  . PHE A 1 30  ? 31.274  29.899  11.360  1.00 59.60  ? 28  PHE B CA  1 
ATOM   174  C C   . PHE A 1 30  ? 30.418  31.137  11.581  1.00 60.48  ? 28  PHE B C   1 
ATOM   175  O O   . PHE A 1 30  ? 29.978  31.420  12.701  1.00 60.28  ? 28  PHE B O   1 
ATOM   176  C CB  . PHE A 1 30  ? 30.422  28.728  10.870  1.00 58.44  ? 28  PHE B CB  1 
ATOM   177  C CG  . PHE A 1 30  ? 29.131  28.568  11.594  1.00 57.73  ? 28  PHE B CG  1 
ATOM   178  C CD1 . PHE A 1 30  ? 29.086  27.924  12.812  1.00 56.81  ? 28  PHE B CD1 1 
ATOM   179  C CD2 . PHE A 1 30  ? 27.948  29.008  11.033  1.00 58.06  ? 28  PHE B CD2 1 
ATOM   180  C CE1 . PHE A 1 30  ? 27.880  27.753  13.475  1.00 56.26  ? 28  PHE B CE1 1 
ATOM   181  C CE2 . PHE A 1 30  ? 26.737  28.840  11.690  1.00 57.50  ? 28  PHE B CE2 1 
ATOM   182  C CZ  . PHE A 1 30  ? 26.702  28.218  12.908  1.00 56.62  ? 28  PHE B CZ  1 
ATOM   183  N N   . ASN A 1 31  ? 30.172  31.857  10.492  1.00 61.56  ? 29  ASN B N   1 
ATOM   184  C CA  . ASN A 1 31  ? 29.296  33.015  10.502  1.00 62.58  ? 29  ASN B CA  1 
ATOM   185  C C   . ASN A 1 31  ? 27.904  32.625  10.011  1.00 62.04  ? 29  ASN B C   1 
ATOM   186  O O   . ASN A 1 31  ? 27.762  32.043  8.936   1.00 64.42  ? 29  ASN B O   1 
ATOM   187  C CB  . ASN A 1 31  ? 29.890  34.129  9.645   1.00 67.32  ? 29  ASN B CB  1 
ATOM   188  C CG  . ASN A 1 31  ? 29.075  35.392  9.716   1.00 72.43  ? 29  ASN B CG  1 
ATOM   189  O OD1 . ASN A 1 31  ? 28.135  35.569  8.943   1.00 74.10  ? 29  ASN B OD1 1 
ATOM   190  N ND2 . ASN A 1 31  ? 29.381  36.254  10.699  1.00 74.81  ? 29  ASN B ND2 1 
ATOM   191  N N   . VAL A 1 32  ? 26.880  32.975  10.792  1.00 62.33  ? 30  VAL B N   1 
ATOM   192  C CA  . VAL A 1 32  ? 25.505  32.529  10.569  1.00 62.47  ? 30  VAL B CA  1 
ATOM   193  C C   . VAL A 1 32  ? 24.823  33.176  9.364   1.00 68.29  ? 30  VAL B C   1 
ATOM   194  O O   . VAL A 1 32  ? 23.724  32.758  8.979   1.00 66.48  ? 30  VAL B O   1 
ATOM   195  C CB  . VAL A 1 32  ? 24.744  32.792  11.890  1.00 64.93  ? 30  VAL B CB  1 
ATOM   196  C CG1 . VAL A 1 32  ? 25.037  34.193  12.411  1.00 66.33  ? 30  VAL B CG1 1 
ATOM   197  C CG2 . VAL A 1 32  ? 23.254  32.617  11.754  1.00 67.74  ? 30  VAL B CG2 1 
ATOM   198  N N   . SER A 1 33  ? 25.440  34.189  8.749   1.00 76.05  ? 31  SER B N   1 
ATOM   199  C CA  . SER A 1 33  ? 24.811  34.859  7.608   1.00 76.53  ? 31  SER B CA  1 
ATOM   200  C C   . SER A 1 33  ? 24.787  33.959  6.368   1.00 76.97  ? 31  SER B C   1 
ATOM   201  O O   . SER A 1 33  ? 23.807  33.951  5.609   1.00 77.78  ? 31  SER B O   1 
ATOM   202  C CB  . SER A 1 33  ? 25.545  36.165  7.305   1.00 79.07  ? 31  SER B CB  1 
ATOM   203  O OG  . SER A 1 33  ? 24.673  37.143  6.771   1.00 84.18  ? 31  SER B OG  1 
ATOM   204  N N   . TYR A 1 34  ? 25.858  33.206  6.137   1.00 70.57  ? 32  TYR B N   1 
ATOM   205  C CA  . TYR A 1 34  ? 25.886  32.295  5.002   1.00 70.58  ? 32  TYR B CA  1 
ATOM   206  C C   . TYR A 1 34  ? 24.966  31.081  5.163   1.00 70.13  ? 32  TYR B C   1 
ATOM   207  O O   . TYR A 1 34  ? 24.573  30.486  4.153   1.00 66.48  ? 32  TYR B O   1 
ATOM   208  C CB  . TYR A 1 34  ? 27.307  31.781  4.762   1.00 72.23  ? 32  TYR B CB  1 
ATOM   209  C CG  . TYR A 1 34  ? 28.439  32.779  4.910   1.00 76.48  ? 32  TYR B CG  1 
ATOM   210  C CD1 . TYR A 1 34  ? 28.374  34.038  4.315   1.00 82.31  ? 32  TYR B CD1 1 
ATOM   211  C CD2 . TYR A 1 34  ? 29.609  32.427  5.583   1.00 75.29  ? 32  TYR B CD2 1 
ATOM   212  C CE1 . TYR A 1 34  ? 29.431  34.930  4.417   1.00 84.37  ? 32  TYR B CE1 1 
ATOM   213  C CE2 . TYR A 1 34  ? 30.669  33.297  5.680   1.00 77.71  ? 32  TYR B CE2 1 
ATOM   214  C CZ  . TYR A 1 34  ? 30.576  34.550  5.098   1.00 84.49  ? 32  TYR B CZ  1 
ATOM   215  O OH  . TYR A 1 34  ? 31.631  35.426  5.197   1.00 91.92  ? 32  TYR B OH  1 
ATOM   216  N N   . TYR A 1 35  ? 24.631  30.687  6.393   1.00 68.26  ? 33  TYR B N   1 
ATOM   217  C CA  . TYR A 1 35  ? 24.012  29.403  6.660   1.00 59.46  ? 33  TYR B CA  1 
ATOM   218  C C   . TYR A 1 35  ? 22.534  29.540  7.000   1.00 59.36  ? 33  TYR B C   1 
ATOM   219  O O   . TYR A 1 35  ? 22.031  30.622  7.295   1.00 68.59  ? 33  TYR B O   1 
ATOM   220  C CB  . TYR A 1 35  ? 24.710  28.718  7.817   1.00 58.42  ? 33  TYR B CB  1 
ATOM   221  C CG  . TYR A 1 35  ? 26.103  28.236  7.549   1.00 58.26  ? 33  TYR B CG  1 
ATOM   222  C CD1 . TYR A 1 35  ? 26.346  26.938  7.102   1.00 57.31  ? 33  TYR B CD1 1 
ATOM   223  C CD2 . TYR A 1 35  ? 27.181  29.068  7.768   1.00 59.14  ? 33  TYR B CD2 1 
ATOM   224  C CE1 . TYR A 1 35  ? 27.634  26.495  6.891   1.00 57.26  ? 33  TYR B CE1 1 
ATOM   225  C CE2 . TYR A 1 35  ? 28.471  28.628  7.564   1.00 59.09  ? 33  TYR B CE2 1 
ATOM   226  C CZ  . TYR A 1 35  ? 28.697  27.340  7.126   1.00 58.15  ? 33  TYR B CZ  1 
ATOM   227  O OH  . TYR A 1 35  ? 29.995  26.929  6.926   1.00 58.23  ? 33  TYR B OH  1 
ATOM   228  N N   . SER A 1 36  ? 21.838  28.417  6.975   1.00 58.48  ? 34  SER B N   1 
ATOM   229  C CA  . SER A 1 36  ? 20.457  28.364  7.417   1.00 58.57  ? 34  SER B CA  1 
ATOM   230  C C   . SER A 1 36  ? 20.456  27.917  8.872   1.00 59.52  ? 34  SER B C   1 
ATOM   231  O O   . SER A 1 36  ? 21.258  27.058  9.265   1.00 57.10  ? 34  SER B O   1 
ATOM   232  C CB  . SER A 1 36  ? 19.642  27.395  6.551   1.00 60.63  ? 34  SER B CB  1 
ATOM   233  O OG  . SER A 1 36  ? 18.249  27.659  6.654   1.00 60.80  ? 34  SER B OG  1 
ATOM   234  N N   . ILE A 1 37  ? 19.578  28.522  9.677   1.00 59.20  ? 35  ILE B N   1 
ATOM   235  C CA  . ILE A 1 37  ? 19.542  28.284  11.113  1.00 56.97  ? 35  ILE B CA  1 
ATOM   236  C C   . ILE A 1 37  ? 18.106  28.055  11.570  1.00 58.80  ? 35  ILE B C   1 
ATOM   237  O O   . ILE A 1 37  ? 17.182  28.784  11.185  1.00 57.72  ? 35  ILE B O   1 
ATOM   238  C CB  . ILE A 1 37  ? 20.183  29.436  11.893  1.00 57.77  ? 35  ILE B CB  1 
ATOM   239  C CG1 . ILE A 1 37  ? 21.497  29.843  11.233  1.00 58.25  ? 35  ILE B CG1 1 
ATOM   240  C CG2 . ILE A 1 37  ? 20.408  29.034  13.307  1.00 57.08  ? 35  ILE B CG2 1 
ATOM   241  C CD1 . ILE A 1 37  ? 22.631  28.917  11.451  1.00 57.32  ? 35  ILE B CD1 1 
ATOM   242  N N   . HIS A 1 38  ? 17.941  27.043  12.429  1.00 59.32  ? 36  HIS B N   1 
ATOM   243  C CA  . HIS A 1 38  ? 16.661  26.465  12.789  1.00 57.61  ? 36  HIS B CA  1 
ATOM   244  C C   . HIS A 1 38  ? 16.580  26.274  14.297  1.00 57.35  ? 36  HIS B C   1 
ATOM   245  O O   . HIS A 1 38  ? 17.597  26.189  14.990  1.00 56.26  ? 36  HIS B O   1 
ATOM   246  C CB  . HIS A 1 38  ? 16.461  25.123  12.079  1.00 54.68  ? 36  HIS B CB  1 
ATOM   247  C CG  . HIS A 1 38  ? 16.883  25.142  10.642  1.00 59.03  ? 36  HIS B CG  1 
ATOM   248  N ND1 . HIS A 1 38  ? 15.985  25.028  9.605   1.00 55.22  ? 36  HIS B ND1 1 
ATOM   249  C CD2 . HIS A 1 38  ? 18.105  25.283  10.072  1.00 56.13  ? 36  HIS B CD2 1 
ATOM   250  C CE1 . HIS A 1 38  ? 16.636  25.103  8.459   1.00 59.39  ? 36  HIS B CE1 1 
ATOM   251  N NE2 . HIS A 1 38  ? 17.924  25.253  8.715   1.00 56.60  ? 36  HIS B NE2 1 
ATOM   252  N N   . TRP A 1 39  ? 15.346  26.206  14.794  1.00 57.51  ? 37  TRP B N   1 
ATOM   253  C CA  . TRP A 1 39  ? 15.058  25.872  16.179  1.00 56.87  ? 37  TRP B CA  1 
ATOM   254  C C   . TRP A 1 39  ? 14.165  24.648  16.204  1.00 55.82  ? 37  TRP B C   1 
ATOM   255  O O   . TRP A 1 39  ? 13.127  24.620  15.534  1.00 54.92  ? 37  TRP B O   1 
ATOM   256  C CB  . TRP A 1 39  ? 14.370  27.026  16.911  1.00 59.54  ? 37  TRP B CB  1 
ATOM   257  C CG  . TRP A 1 39  ? 15.265  28.184  17.192  1.00 59.22  ? 37  TRP B CG  1 
ATOM   258  C CD1 . TRP A 1 39  ? 15.396  29.317  16.441  1.00 60.35  ? 37  TRP B CD1 1 
ATOM   259  C CD2 . TRP A 1 39  ? 16.118  28.360  18.330  1.00 63.52  ? 37  TRP B CD2 1 
ATOM   260  N NE1 . TRP A 1 39  ? 16.292  30.185  17.023  1.00 58.28  ? 37  TRP B NE1 1 
ATOM   261  C CE2 . TRP A 1 39  ? 16.759  29.622  18.181  1.00 63.94  ? 37  TRP B CE2 1 
ATOM   262  C CE3 . TRP A 1 39  ? 16.396  27.586  19.472  1.00 59.85  ? 37  TRP B CE3 1 
ATOM   263  C CZ2 . TRP A 1 39  ? 17.670  30.120  19.122  1.00 63.70  ? 37  TRP B CZ2 1 
ATOM   264  C CZ3 . TRP A 1 39  ? 17.312  28.081  20.408  1.00 59.15  ? 37  TRP B CZ3 1 
ATOM   265  C CH2 . TRP A 1 39  ? 17.935  29.338  20.224  1.00 61.20  ? 37  TRP B CH2 1 
ATOM   266  N N   . VAL A 1 40  ? 14.573  23.652  16.992  1.00 58.10  ? 38  VAL B N   1 
ATOM   267  C CA  . VAL A 1 40  ? 13.873  22.381  17.163  1.00 56.76  ? 38  VAL B CA  1 
ATOM   268  C C   . VAL A 1 40  ? 13.772  22.086  18.650  1.00 55.22  ? 38  VAL B C   1 
ATOM   269  O O   . VAL A 1 40  ? 14.729  22.316  19.396  1.00 53.24  ? 38  VAL B O   1 
ATOM   270  C CB  . VAL A 1 40  ? 14.599  21.220  16.450  1.00 55.39  ? 38  VAL B CB  1 
ATOM   271  C CG1 . VAL A 1 40  ? 13.616  20.360  15.708  1.00 56.60  ? 38  VAL B CG1 1 
ATOM   272  C CG2 . VAL A 1 40  ? 15.677  21.746  15.497  1.00 52.41  ? 38  VAL B CG2 1 
ATOM   273  N N   . ARG A 1 41  ? 12.627  21.539  19.078  1.00 58.20  ? 39  ARG B N   1 
ATOM   274  C CA  . ARG A 1 41  ? 12.347  21.317  20.494  1.00 58.28  ? 39  ARG B CA  1 
ATOM   275  C C   . ARG A 1 41  ? 11.876  19.888  20.739  1.00 59.70  ? 39  ARG B C   1 
ATOM   276  O O   . ARG A 1 41  ? 11.326  19.238  19.849  1.00 61.68  ? 39  ARG B O   1 
ATOM   277  C CB  . ARG A 1 41  ? 11.301  22.299  21.012  1.00 56.06  ? 39  ARG B CB  1 
ATOM   278  C CG  . ARG A 1 41  ? 9.957   22.232  20.302  1.00 58.85  ? 39  ARG B CG  1 
ATOM   279  C CD  . ARG A 1 41  ? 8.843   22.712  21.233  1.00 59.80  ? 39  ARG B CD  1 
ATOM   280  N NE  . ARG A 1 41  ? 7.562   22.913  20.566  1.00 61.27  ? 39  ARG B NE  1 
ATOM   281  C CZ  . ARG A 1 41  ? 6.785   23.986  20.686  1.00 70.61  ? 39  ARG B CZ  1 
ATOM   282  N NH1 . ARG A 1 41  ? 7.141   25.038  21.420  1.00 68.74  ? 39  ARG B NH1 1 
ATOM   283  N NH2 . ARG A 1 41  ? 5.608   23.999  20.067  1.00 74.54  ? 39  ARG B NH2 1 
ATOM   284  N N   . GLN A 1 42  ? 12.092  19.409  21.964  1.00 58.07  ? 40  GLN B N   1 
ATOM   285  C CA  . GLN A 1 42  ? 11.778  18.037  22.357  1.00 58.06  ? 40  GLN B CA  1 
ATOM   286  C C   . GLN A 1 42  ? 11.137  18.025  23.742  1.00 56.94  ? 40  GLN B C   1 
ATOM   287  O O   . GLN A 1 42  ? 11.842  18.136  24.749  1.00 56.25  ? 40  GLN B O   1 
ATOM   288  C CB  . GLN A 1 42  ? 13.038  17.175  22.374  1.00 55.96  ? 40  GLN B CB  1 
ATOM   289  C CG  . GLN A 1 42  ? 12.805  15.726  22.061  1.00 56.53  ? 40  GLN B CG  1 
ATOM   290  C CD  . GLN A 1 42  ? 14.081  14.925  22.151  1.00 54.60  ? 40  GLN B CD  1 
ATOM   291  O OE1 . GLN A 1 42  ? 15.061  15.356  22.770  1.00 51.19  ? 40  GLN B OE1 1 
ATOM   292  N NE2 . GLN A 1 42  ? 14.139  13.841  21.380  1.00 54.44  ? 40  GLN B NE2 1 
ATOM   293  N N   . ALA A 1 43  ? 9.820   17.840  23.795  1.00 55.22  ? 41  ALA B N   1 
ATOM   294  C CA  . ALA A 1 43  ? 9.133   17.637  25.055  1.00 54.96  ? 41  ALA B CA  1 
ATOM   295  C C   . ALA A 1 43  ? 9.671   16.380  25.741  1.00 57.09  ? 41  ALA B C   1 
ATOM   296  O O   . ALA A 1 43  ? 10.185  15.479  25.079  1.00 62.72  ? 41  ALA B O   1 
ATOM   297  C CB  . ALA A 1 43  ? 7.632   17.517  24.812  1.00 55.72  ? 41  ALA B CB  1 
ATOM   298  N N   . PRO A 1 44  ? 9.583   16.296  27.067  1.00 60.31  ? 42  PRO B N   1 
ATOM   299  C CA  . PRO A 1 44  ? 10.140  15.130  27.778  1.00 61.29  ? 42  PRO B CA  1 
ATOM   300  C C   . PRO A 1 44  ? 9.628   13.800  27.246  1.00 59.56  ? 42  PRO B C   1 
ATOM   301  O O   . PRO A 1 44  ? 8.433   13.506  27.287  1.00 59.34  ? 42  PRO B O   1 
ATOM   302  C CB  . PRO A 1 44  ? 9.702   15.377  29.224  1.00 55.92  ? 42  PRO B CB  1 
ATOM   303  C CG  . PRO A 1 44  ? 9.738   16.862  29.303  1.00 58.85  ? 42  PRO B CG  1 
ATOM   304  C CD  . PRO A 1 44  ? 9.110   17.317  28.019  1.00 60.03  ? 42  PRO B CD  1 
ATOM   305  N N   . GLY A 1 45  ? 10.555  12.990  26.747  1.00 60.43  ? 43  GLY B N   1 
ATOM   306  C CA  . GLY A 1 45  ? 10.192  11.680  26.235  1.00 64.89  ? 43  GLY B CA  1 
ATOM   307  C C   . GLY A 1 45  ? 9.331   11.700  24.991  1.00 62.65  ? 43  GLY B C   1 
ATOM   308  O O   . GLY A 1 45  ? 8.506   10.798  24.797  1.00 58.32  ? 43  GLY B O   1 
ATOM   309  N N   . LYS A 1 46  ? 9.493   12.712  24.145  1.00 62.25  ? 44  LYS B N   1 
ATOM   310  C CA  . LYS A 1 46  ? 8.685   12.862  22.949  1.00 64.05  ? 44  LYS B CA  1 
ATOM   311  C C   . LYS A 1 46  ? 9.594   13.036  21.746  1.00 65.08  ? 44  LYS B C   1 
ATOM   312  O O   . LYS A 1 46  ? 10.804  13.257  21.875  1.00 62.66  ? 44  LYS B O   1 
ATOM   313  C CB  . LYS A 1 46  ? 7.726   14.046  23.077  1.00 61.16  ? 44  LYS B CB  1 
ATOM   314  C CG  . LYS A 1 46  ? 7.030   14.098  24.424  1.00 61.24  ? 44  LYS B CG  1 
ATOM   315  C CD  . LYS A 1 46  ? 6.195   12.857  24.701  1.00 64.53  ? 44  LYS B CD  1 
ATOM   316  C CE  . LYS A 1 46  ? 4.702   13.196  24.631  1.00 70.46  ? 44  LYS B CE  1 
ATOM   317  N NZ  . LYS A 1 46  ? 4.347   14.458  25.388  1.00 69.06  ? 44  LYS B NZ  1 
ATOM   318  N N   . GLY A 1 47  ? 8.991   12.937  20.566  1.00 72.46  ? 45  GLY B N   1 
ATOM   319  C CA  . GLY A 1 47  ? 9.724   13.102  19.327  1.00 72.17  ? 45  GLY B CA  1 
ATOM   320  C C   . GLY A 1 47  ? 10.281  14.504  19.172  1.00 69.97  ? 45  GLY B C   1 
ATOM   321  O O   . GLY A 1 47  ? 10.169  15.365  20.047  1.00 70.05  ? 45  GLY B O   1 
ATOM   322  N N   . LEU A 1 48  ? 10.907  14.726  18.015  1.00 65.11  ? 46  LEU B N   1 
ATOM   323  C CA  . LEU A 1 48  ? 11.454  16.030  17.659  1.00 59.67  ? 46  LEU B CA  1 
ATOM   324  C C   . LEU A 1 48  ? 10.402  16.872  16.950  1.00 58.52  ? 46  LEU B C   1 
ATOM   325  O O   . LEU A 1 48  ? 9.667   16.383  16.086  1.00 57.84  ? 46  LEU B O   1 
ATOM   326  C CB  . LEU A 1 48  ? 12.676  15.885  16.756  1.00 55.07  ? 46  LEU B CB  1 
ATOM   327  C CG  . LEU A 1 48  ? 13.943  15.269  17.348  1.00 55.50  ? 46  LEU B CG  1 
ATOM   328  C CD1 . LEU A 1 48  ? 15.066  15.063  16.255  1.00 50.03  ? 46  LEU B CD1 1 
ATOM   329  C CD2 . LEU A 1 48  ? 14.426  16.062  18.583  1.00 50.72  ? 46  LEU B CD2 1 
ATOM   330  N N   . GLU A 1 49  ? 10.334  18.145  17.318  1.00 59.28  ? 47  GLU B N   1 
ATOM   331  C CA  . GLU A 1 49  ? 9.422   19.079  16.677  1.00 60.79  ? 47  GLU B CA  1 
ATOM   332  C C   . GLU A 1 49  ? 10.189  20.313  16.237  1.00 59.99  ? 47  GLU B C   1 
ATOM   333  O O   . GLU A 1 49  ? 10.916  20.917  17.031  1.00 59.30  ? 47  GLU B O   1 
ATOM   334  C CB  . GLU A 1 49  ? 8.271   19.478  17.596  1.00 56.81  ? 47  GLU B CB  1 
ATOM   335  C CG  . GLU A 1 49  ? 7.088   19.927  16.811  1.00 59.22  ? 47  GLU B CG  1 
ATOM   336  C CD  . GLU A 1 49  ? 5.849   20.093  17.647  1.00 69.60  ? 47  GLU B CD  1 
ATOM   337  O OE1 . GLU A 1 49  ? 5.929   20.630  18.783  1.00 70.56  ? 47  GLU B OE1 1 
ATOM   338  O OE2 . GLU A 1 49  ? 4.789   19.628  17.167  1.00 73.54  ? 47  GLU B OE2 1 
ATOM   339  N N   . TRP A 1 50  ? 10.039  20.666  14.967  1.00 61.54  ? 48  TRP B N   1 
ATOM   340  C CA  . TRP A 1 50  ? 10.632  21.867  14.418  1.00 60.01  ? 48  TRP B CA  1 
ATOM   341  C C   . TRP A 1 50  ? 9.668   23.004  14.677  1.00 59.18  ? 48  TRP B C   1 
ATOM   342  O O   . TRP A 1 50  ? 8.451   22.802  14.676  1.00 59.14  ? 48  TRP B O   1 
ATOM   343  C CB  . TRP A 1 50  ? 10.908  21.684  12.915  1.00 60.73  ? 48  TRP B CB  1 
ATOM   344  C CG  . TRP A 1 50  ? 11.162  22.954  12.121  1.00 60.89  ? 48  TRP B CG  1 
ATOM   345  C CD1 . TRP A 1 50  ? 12.362  23.592  11.943  1.00 59.94  ? 48  TRP B CD1 1 
ATOM   346  C CD2 . TRP A 1 50  ? 10.201  23.707  11.387  1.00 58.06  ? 48  TRP B CD2 1 
ATOM   347  N NE1 . TRP A 1 50  ? 12.200  24.704  11.162  1.00 60.03  ? 48  TRP B NE1 1 
ATOM   348  C CE2 . TRP A 1 50  ? 10.881  24.797  10.805  1.00 61.68  ? 48  TRP B CE2 1 
ATOM   349  C CE3 . TRP A 1 50  ? 8.834   23.564  11.159  1.00 59.05  ? 48  TRP B CE3 1 
ATOM   350  C CZ2 . TRP A 1 50  ? 10.239  25.732  10.007  1.00 64.04  ? 48  TRP B CZ2 1 
ATOM   351  C CZ3 . TRP A 1 50  ? 8.199   24.492  10.389  1.00 64.49  ? 48  TRP B CZ3 1 
ATOM   352  C CH2 . TRP A 1 50  ? 8.897   25.564  9.813   1.00 66.32  ? 48  TRP B CH2 1 
ATOM   353  N N   . VAL A 1 51  ? 10.218  24.192  14.954  1.00 59.54  ? 49  VAL B N   1 
ATOM   354  C CA  . VAL A 1 51  ? 9.421   25.392  15.184  1.00 64.22  ? 49  VAL B CA  1 
ATOM   355  C C   . VAL A 1 51  ? 9.800   26.518  14.233  1.00 64.45  ? 49  VAL B C   1 
ATOM   356  O O   . VAL A 1 51  ? 8.922   27.242  13.751  1.00 67.64  ? 49  VAL B O   1 
ATOM   357  C CB  . VAL A 1 51  ? 9.505   25.892  16.655  1.00 65.45  ? 49  VAL B CB  1 
ATOM   358  C CG1 . VAL A 1 51  ? 8.965   24.850  17.638  1.00 67.60  ? 49  VAL B CG1 1 
ATOM   359  C CG2 . VAL A 1 51  ? 10.923  26.350  17.028  1.00 61.23  ? 49  VAL B CG2 1 
ATOM   360  N N   . ALA A 1 52  ? 11.092  26.712  13.961  1.00 60.93  ? 50  ALA B N   1 
ATOM   361  C CA  . ALA A 1 52  ? 11.454  27.890  13.189  1.00 61.14  ? 50  ALA B CA  1 
ATOM   362  C C   . ALA A 1 52  ? 12.717  27.665  12.379  1.00 62.54  ? 50  ALA B C   1 
ATOM   363  O O   . ALA A 1 52  ? 13.655  26.993  12.815  1.00 59.44  ? 50  ALA B O   1 
ATOM   364  C CB  . ALA A 1 52  ? 11.649  29.119  14.072  1.00 61.68  ? 50  ALA B CB  1 
ATOM   365  N N   . SER A 1 53  ? 12.729  28.275  11.202  1.00 62.52  ? 51  SER B N   1 
ATOM   366  C CA  . SER A 1 53  ? 13.889  28.314  10.345  1.00 58.84  ? 51  SER B CA  1 
ATOM   367  C C   . SER A 1 53  ? 14.147  29.762  9.970   1.00 60.71  ? 51  SER B C   1 
ATOM   368  O O   . SER A 1 53  ? 13.212  30.511  9.677   1.00 62.82  ? 51  SER B O   1 
ATOM   369  C CB  . SER A 1 53  ? 13.653  27.477  9.093   1.00 63.25  ? 51  SER B CB  1 
ATOM   370  O OG  . SER A 1 53  ? 13.786  26.095  9.351   1.00 61.39  ? 51  SER B OG  1 
ATOM   371  N N   . ILE A 1 54  ? 15.410  30.163  10.002  1.00 61.63  ? 52  ILE B N   1 
ATOM   372  C CA  . ILE A 1 54  ? 15.839  31.390  9.354   1.00 62.48  ? 52  ILE B CA  1 
ATOM   373  C C   . ILE A 1 54  ? 16.728  30.975  8.185   1.00 65.84  ? 52  ILE B C   1 
ATOM   374  O O   . ILE A 1 54  ? 17.627  30.136  8.340   1.00 65.61  ? 52  ILE B O   1 
ATOM   375  C CB  . ILE A 1 54  ? 16.561  32.335  10.323  1.00 61.59  ? 52  ILE B CB  1 
ATOM   376  C CG1 . ILE A 1 54  ? 16.837  33.683  9.644   1.00 64.68  ? 52  ILE B CG1 1 
ATOM   377  C CG2 . ILE A 1 54  ? 17.858  31.747  10.800  1.00 60.61  ? 52  ILE B CG2 1 
ATOM   378  C CD1 . ILE A 1 54  ? 15.631  34.569  9.590   1.00 64.54  ? 52  ILE B CD1 1 
ATOM   379  N N   . TYR A 1 55  ? 16.437  31.500  7.001   1.00 67.36  ? 53  TYR B N   1 
ATOM   380  C CA  . TYR A 1 55  ? 17.228  31.188  5.821   1.00 64.22  ? 53  TYR B CA  1 
ATOM   381  C C   . TYR A 1 55  ? 18.209  32.316  5.590   1.00 64.01  ? 53  TYR B C   1 
ATOM   382  O O   . TYR A 1 55  ? 18.097  33.372  6.203   1.00 71.22  ? 53  TYR B O   1 
ATOM   383  C CB  . TYR A 1 55  ? 16.294  30.915  4.637   1.00 66.69  ? 53  TYR B CB  1 
ATOM   384  C CG  . TYR A 1 55  ? 15.549  29.610  4.855   1.00 69.09  ? 53  TYR B CG  1 
ATOM   385  C CD1 . TYR A 1 55  ? 16.119  28.387  4.530   1.00 65.01  ? 53  TYR B CD1 1 
ATOM   386  C CD2 . TYR A 1 55  ? 14.306  29.603  5.466   1.00 69.12  ? 53  TYR B CD2 1 
ATOM   387  C CE1 . TYR A 1 55  ? 15.445  27.200  4.773   1.00 65.83  ? 53  TYR B CE1 1 
ATOM   388  C CE2 . TYR A 1 55  ? 13.626  28.434  5.709   1.00 67.07  ? 53  TYR B CE2 1 
ATOM   389  C CZ  . TYR A 1 55  ? 14.188  27.231  5.365   1.00 68.52  ? 53  TYR B CZ  1 
ATOM   390  O OH  . TYR A 1 55  ? 13.471  26.072  5.648   1.00 67.87  ? 53  TYR B OH  1 
ATOM   391  N N   . PRO A 1 56  ? 19.238  32.114  4.791   1.00 66.27  ? 54  PRO B N   1 
ATOM   392  C CA  . PRO A 1 56  ? 20.263  33.159  4.687   1.00 68.73  ? 54  PRO B CA  1 
ATOM   393  C C   . PRO A 1 56  ? 19.960  34.206  3.625   1.00 69.94  ? 54  PRO B C   1 
ATOM   394  O O   . PRO A 1 56  ? 18.835  34.312  3.118   1.00 67.48  ? 54  PRO B O   1 
ATOM   395  C CB  . PRO A 1 56  ? 21.527  32.362  4.356   1.00 69.41  ? 54  PRO B CB  1 
ATOM   396  C CG  . PRO A 1 56  ? 21.022  31.221  3.560   1.00 66.96  ? 54  PRO B CG  1 
ATOM   397  C CD  . PRO A 1 56  ? 19.650  30.878  4.100   1.00 67.99  ? 54  PRO B CD  1 
ATOM   398  N N   . TYR A 1 57  ? 20.977  35.009  3.318   1.00 72.99  ? 55  TYR B N   1 
ATOM   399  C CA  . TYR A 1 57  ? 20.906  36.084  2.330   1.00 75.00  ? 55  TYR B CA  1 
ATOM   400  C C   . TYR A 1 57  ? 19.815  37.106  2.644   1.00 70.68  ? 55  TYR B C   1 
ATOM   401  O O   . TYR A 1 57  ? 20.131  38.270  2.898   1.00 71.89  ? 55  TYR B O   1 
ATOM   402  C CB  . TYR A 1 57  ? 20.747  35.481  0.928   1.00 73.99  ? 55  TYR B CB  1 
ATOM   403  C CG  . TYR A 1 57  ? 21.829  34.449  0.658   1.00 73.54  ? 55  TYR B CG  1 
ATOM   404  C CD1 . TYR A 1 57  ? 23.131  34.651  1.115   1.00 72.62  ? 55  TYR B CD1 1 
ATOM   405  C CD2 . TYR A 1 57  ? 21.551  33.267  -0.025  1.00 75.09  ? 55  TYR B CD2 1 
ATOM   406  C CE1 . TYR A 1 57  ? 24.120  33.729  0.896   1.00 74.84  ? 55  TYR B CE1 1 
ATOM   407  C CE2 . TYR A 1 57  ? 22.550  32.310  -0.252  1.00 75.02  ? 55  TYR B CE2 1 
ATOM   408  C CZ  . TYR A 1 57  ? 23.836  32.550  0.208   1.00 77.90  ? 55  TYR B CZ  1 
ATOM   409  O OH  . TYR A 1 57  ? 24.835  31.612  0.006   1.00 72.71  ? 55  TYR B OH  1 
ATOM   410  N N   . TYR A 1 58  ? 18.545  36.690  2.670   1.00 69.87  ? 56  TYR B N   1 
ATOM   411  C CA  . TYR A 1 58  ? 17.415  37.613  2.689   1.00 71.23  ? 56  TYR B CA  1 
ATOM   412  C C   . TYR A 1 58  ? 16.561  37.488  3.945   1.00 74.02  ? 56  TYR B C   1 
ATOM   413  O O   . TYR A 1 58  ? 15.369  37.833  3.918   1.00 72.08  ? 56  TYR B O   1 
ATOM   414  C CB  . TYR A 1 58  ? 16.557  37.393  1.446   1.00 71.85  ? 56  TYR B CB  1 
ATOM   415  C CG  . TYR A 1 58  ? 17.346  37.540  0.154   1.00 81.31  ? 56  TYR B CG  1 
ATOM   416  C CD1 . TYR A 1 58  ? 18.442  38.399  0.080   1.00 80.34  ? 56  TYR B CD1 1 
ATOM   417  C CD2 . TYR A 1 58  ? 17.034  36.789  -0.973  1.00 79.84  ? 56  TYR B CD2 1 
ATOM   418  C CE1 . TYR A 1 58  ? 19.184  38.519  -1.075  1.00 81.87  ? 56  TYR B CE1 1 
ATOM   419  C CE2 . TYR A 1 58  ? 17.767  36.920  -2.139  1.00 77.83  ? 56  TYR B CE2 1 
ATOM   420  C CZ  . TYR A 1 58  ? 18.847  37.778  -2.178  1.00 79.73  ? 56  TYR B CZ  1 
ATOM   421  O OH  . TYR A 1 58  ? 19.602  37.931  -3.314  1.00 81.87  ? 56  TYR B OH  1 
ATOM   422  N N   . GLY A 1 59  ? 17.142  37.026  5.055   1.00 73.19  ? 57  GLY B N   1 
ATOM   423  C CA  . GLY A 1 59  ? 16.357  36.754  6.240   1.00 68.44  ? 57  GLY B CA  1 
ATOM   424  C C   . GLY A 1 59  ? 15.393  35.652  5.897   1.00 67.32  ? 57  GLY B C   1 
ATOM   425  O O   . GLY A 1 59  ? 15.841  34.562  5.551   1.00 69.37  ? 57  GLY B O   1 
ATOM   426  N N   . SER A 1 60  ? 14.086  35.922  5.947   1.00 67.93  ? 58  SER B N   1 
ATOM   427  C CA  . SER A 1 60  ? 13.062  35.016  5.421   1.00 69.81  ? 58  SER B CA  1 
ATOM   428  C C   . SER A 1 60  ? 12.953  33.753  6.260   1.00 69.15  ? 58  SER B C   1 
ATOM   429  O O   . SER A 1 60  ? 13.941  33.048  6.495   1.00 69.12  ? 58  SER B O   1 
ATOM   430  C CB  . SER A 1 60  ? 13.335  34.660  3.951   1.00 76.62  ? 58  SER B CB  1 
ATOM   431  O OG  . SER A 1 60  ? 12.139  34.322  3.260   1.00 78.72  ? 58  SER B OG  1 
ATOM   432  N N   . THR A 1 61  ? 11.749  33.457  6.721   1.00 68.77  ? 59  THR B N   1 
ATOM   433  C CA  . THR A 1 61  ? 11.574  32.572  7.856   1.00 64.20  ? 59  THR B CA  1 
ATOM   434  C C   . THR A 1 61  ? 10.466  31.579  7.569   1.00 65.74  ? 59  THR B C   1 
ATOM   435  O O   . THR A 1 61  ? 9.665   31.756  6.652   1.00 71.51  ? 59  THR B O   1 
ATOM   436  C CB  . THR A 1 61  ? 11.214  33.366  9.111   1.00 66.57  ? 59  THR B CB  1 
ATOM   437  O OG1 . THR A 1 61  ? 9.930   33.983  8.922   1.00 65.83  ? 59  THR B OG1 1 
ATOM   438  C CG2 . THR A 1 61  ? 12.245  34.455  9.359   1.00 65.41  ? 59  THR B CG2 1 
ATOM   439  N N   . SER A 1 62  ? 10.424  30.533  8.379   1.00 67.60  ? 60  SER B N   1 
ATOM   440  C CA  . SER A 1 62  ? 9.336   29.573  8.356   1.00 67.78  ? 60  SER B CA  1 
ATOM   441  C C   . SER A 1 62  ? 9.072   29.151  9.788   1.00 67.10  ? 60  SER B C   1 
ATOM   442  O O   . SER A 1 62  ? 9.998   29.064  10.601  1.00 64.66  ? 60  SER B O   1 
ATOM   443  C CB  . SER A 1 62  ? 9.661   28.364  7.478   1.00 67.25  ? 60  SER B CB  1 
ATOM   444  O OG  . SER A 1 62  ? 10.128  28.792  6.212   1.00 71.55  ? 60  SER B OG  1 
ATOM   445  N N   . TYR A 1 63  ? 7.806   28.917  10.097  1.00 64.26  ? 61  TYR B N   1 
ATOM   446  C CA  . TYR A 1 63  ? 7.392   28.668  11.467  1.00 71.42  ? 61  TYR B CA  1 
ATOM   447  C C   . TYR A 1 63  ? 6.369   27.543  11.458  1.00 77.41  ? 61  TYR B C   1 
ATOM   448  O O   . TYR A 1 63  ? 5.455   27.535  10.626  1.00 82.50  ? 61  TYR B O   1 
ATOM   449  C CB  . TYR A 1 63  ? 6.793   29.942  12.131  1.00 72.49  ? 61  TYR B CB  1 
ATOM   450  C CG  . TYR A 1 63  ? 7.759   31.130  12.264  1.00 68.50  ? 61  TYR B CG  1 
ATOM   451  C CD1 . TYR A 1 63  ? 8.899   31.049  13.064  1.00 69.23  ? 61  TYR B CD1 1 
ATOM   452  C CD2 . TYR A 1 63  ? 7.523   32.326  11.601  1.00 67.09  ? 61  TYR B CD2 1 
ATOM   453  C CE1 . TYR A 1 63  ? 9.779   32.122  13.199  1.00 66.51  ? 61  TYR B CE1 1 
ATOM   454  C CE2 . TYR A 1 63  ? 8.411   33.412  11.720  1.00 71.29  ? 61  TYR B CE2 1 
ATOM   455  C CZ  . TYR A 1 63  ? 9.543   33.304  12.520  1.00 69.60  ? 61  TYR B CZ  1 
ATOM   456  O OH  . TYR A 1 63  ? 10.430  34.374  12.635  1.00 65.18  ? 61  TYR B OH  1 
ATOM   457  N N   . ALA A 1 64  ? 6.548   26.576  12.359  1.00 74.79  ? 62  ALA B N   1 
ATOM   458  C CA  . ALA A 1 64  ? 5.523   25.571  12.585  1.00 82.26  ? 62  ALA B CA  1 
ATOM   459  C C   . ALA A 1 64  ? 4.188   26.255  12.845  1.00 98.69  ? 62  ALA B C   1 
ATOM   460  O O   . ALA A 1 64  ? 4.127   27.312  13.482  1.00 100.13 ? 62  ALA B O   1 
ATOM   461  C CB  . ALA A 1 64  ? 5.904   24.683  13.771  1.00 81.80  ? 62  ALA B CB  1 
ATOM   462  N N   . ASP A 1 65  ? 3.113   25.653  12.331  1.00 114.83 ? 63  ASP B N   1 
ATOM   463  C CA  . ASP A 1 65  ? 1.792   26.261  12.469  1.00 116.24 ? 63  ASP B CA  1 
ATOM   464  C C   . ASP A 1 65  ? 1.431   26.513  13.926  1.00 113.09 ? 63  ASP B C   1 
ATOM   465  O O   . ASP A 1 65  ? 0.783   27.516  14.238  1.00 112.45 ? 63  ASP B O   1 
ATOM   466  C CB  . ASP A 1 65  ? 0.738   25.379  11.798  1.00 117.06 ? 63  ASP B CB  1 
ATOM   467  C CG  . ASP A 1 65  ? 0.964   25.236  10.305  1.00 119.23 ? 63  ASP B CG  1 
ATOM   468  O OD1 . ASP A 1 65  ? 2.019   25.698  9.818   1.00 118.98 ? 63  ASP B OD1 1 
ATOM   469  O OD2 . ASP A 1 65  ? 0.097   24.643  9.626   1.00 120.85 ? 63  ASP B OD2 1 
ATOM   470  N N   . SER A 1 66  ? 1.860   25.635  14.831  1.00 103.08 ? 64  SER B N   1 
ATOM   471  C CA  . SER A 1 66  ? 1.460   25.771  16.225  1.00 100.12 ? 64  SER B CA  1 
ATOM   472  C C   . SER A 1 66  ? 2.089   27.001  16.871  1.00 99.90  ? 64  SER B C   1 
ATOM   473  O O   . SER A 1 66  ? 1.462   27.659  17.713  1.00 95.62  ? 64  SER B O   1 
ATOM   474  C CB  . SER A 1 66  ? 1.834   24.504  16.990  1.00 96.96  ? 64  SER B CB  1 
ATOM   475  O OG  . SER A 1 66  ? 3.200   24.532  17.357  1.00 93.81  ? 64  SER B OG  1 
ATOM   476  N N   . VAL A 1 67  ? 3.316   27.337  16.479  1.00 96.53  ? 65  VAL B N   1 
ATOM   477  C CA  . VAL A 1 67  ? 4.043   28.430  17.118  1.00 95.98  ? 65  VAL B CA  1 
ATOM   478  C C   . VAL A 1 67  ? 3.855   29.732  16.346  1.00 98.67  ? 65  VAL B C   1 
ATOM   479  O O   . VAL A 1 67  ? 4.594   30.701  16.559  1.00 96.03  ? 65  VAL B O   1 
ATOM   480  C CB  . VAL A 1 67  ? 5.532   28.068  17.258  1.00 90.11  ? 65  VAL B CB  1 
ATOM   481  C CG1 . VAL A 1 67  ? 5.670   26.656  17.772  1.00 86.65  ? 65  VAL B CG1 1 
ATOM   482  C CG2 . VAL A 1 67  ? 6.223   28.162  15.921  1.00 87.27  ? 65  VAL B CG2 1 
ATOM   483  N N   . LYS A 1 68  ? 2.847   29.769  15.470  1.00 110.00 ? 66  LYS B N   1 
ATOM   484  C CA  . LYS A 1 68  ? 2.644   30.913  14.586  1.00 111.32 ? 66  LYS B CA  1 
ATOM   485  C C   . LYS A 1 68  ? 2.384   32.192  15.376  1.00 112.51 ? 66  LYS B C   1 
ATOM   486  O O   . LYS A 1 68  ? 1.705   32.188  16.413  1.00 110.12 ? 66  LYS B O   1 
ATOM   487  C CB  . LYS A 1 68  ? 1.480   30.643  13.622  1.00 113.69 ? 66  LYS B CB  1 
ATOM   488  C CG  . LYS A 1 68  ? 0.078   30.739  14.246  1.00 117.56 ? 66  LYS B CG  1 
ATOM   489  C CD  . LYS A 1 68  ? -0.865  31.659  13.459  1.00 118.89 ? 66  LYS B CD  1 
ATOM   490  C CE  . LYS A 1 68  ? -0.298  33.060  13.260  1.00 115.67 ? 66  LYS B CE  1 
ATOM   491  N NZ  . LYS A 1 68  ? -1.372  34.027  12.889  1.00 116.00 ? 66  LYS B NZ  1 
ATOM   492  N N   . GLY A 1 69  ? 2.952   33.295  14.888  1.00 103.61 ? 67  GLY B N   1 
ATOM   493  C CA  . GLY A 1 69  ? 2.706   34.592  15.493  1.00 100.47 ? 67  GLY B CA  1 
ATOM   494  C C   . GLY A 1 69  ? 3.267   34.758  16.890  1.00 92.66  ? 67  GLY B C   1 
ATOM   495  O O   . GLY A 1 69  ? 3.795   35.826  17.214  1.00 90.58  ? 67  GLY B O   1 
ATOM   496  N N   . ARG A 1 70  ? 3.147   33.717  17.727  1.00 94.14  ? 68  ARG B N   1 
ATOM   497  C CA  . ARG A 1 70  ? 3.762   33.739  19.051  1.00 86.80  ? 68  ARG B CA  1 
ATOM   498  C C   . ARG A 1 70  ? 5.286   33.736  18.982  1.00 86.48  ? 68  ARG B C   1 
ATOM   499  O O   . ARG A 1 70  ? 5.943   34.349  19.829  1.00 80.96  ? 68  ARG B O   1 
ATOM   500  C CB  . ARG A 1 70  ? 3.272   32.551  19.865  1.00 86.26  ? 68  ARG B CB  1 
ATOM   501  C CG  . ARG A 1 70  ? 1.825   32.213  19.620  1.00 89.57  ? 68  ARG B CG  1 
ATOM   502  C CD  . ARG A 1 70  ? 1.221   31.492  20.821  1.00 84.49  ? 68  ARG B CD  1 
ATOM   503  N NE  . ARG A 1 70  ? 0.331   30.429  20.383  1.00 83.22  ? 68  ARG B NE  1 
ATOM   504  C CZ  . ARG A 1 70  ? 0.688   29.156  20.311  1.00 86.68  ? 68  ARG B CZ  1 
ATOM   505  N NH1 . ARG A 1 70  ? 1.876   28.748  20.733  1.00 84.16  ? 68  ARG B NH1 1 
ATOM   506  N NH2 . ARG A 1 70  ? -0.157  28.276  19.781  1.00 90.06  ? 68  ARG B NH2 1 
ATOM   507  N N   . PHE A 1 71  ? 5.869   33.081  17.985  1.00 86.30  ? 69  PHE B N   1 
ATOM   508  C CA  . PHE A 1 71  ? 7.309   32.880  17.924  1.00 82.55  ? 69  PHE B CA  1 
ATOM   509  C C   . PHE A 1 71  ? 7.924   33.725  16.809  1.00 80.31  ? 69  PHE B C   1 
ATOM   510  O O   . PHE A 1 71  ? 7.324   33.886  15.743  1.00 79.57  ? 69  PHE B O   1 
ATOM   511  C CB  . PHE A 1 71  ? 7.629   31.395  17.710  1.00 83.22  ? 69  PHE B CB  1 
ATOM   512  C CG  . PHE A 1 71  ? 7.395   30.526  18.934  1.00 84.92  ? 69  PHE B CG  1 
ATOM   513  C CD1 . PHE A 1 71  ? 6.325   30.762  19.796  1.00 88.47  ? 69  PHE B CD1 1 
ATOM   514  C CD2 . PHE A 1 71  ? 8.246   29.466  19.213  1.00 80.88  ? 69  PHE B CD2 1 
ATOM   515  C CE1 . PHE A 1 71  ? 6.111   29.966  20.916  1.00 86.48  ? 69  PHE B CE1 1 
ATOM   516  C CE2 . PHE A 1 71  ? 8.035   28.666  20.320  1.00 81.79  ? 69  PHE B CE2 1 
ATOM   517  C CZ  . PHE A 1 71  ? 6.961   28.917  21.179  1.00 83.70  ? 69  PHE B CZ  1 
ATOM   518  N N   . THR A 1 72  ? 9.120   34.270  17.056  1.00 71.74  ? 70  THR B N   1 
ATOM   519  C CA  . THR A 1 72  ? 9.874   34.994  16.037  1.00 69.59  ? 70  THR B CA  1 
ATOM   520  C C   . THR A 1 72  ? 11.323  34.518  16.053  1.00 68.35  ? 70  THR B C   1 
ATOM   521  O O   . THR A 1 72  ? 12.076  34.830  16.983  1.00 67.48  ? 70  THR B O   1 
ATOM   522  C CB  . THR A 1 72  ? 9.786   36.516  16.239  1.00 72.53  ? 70  THR B CB  1 
ATOM   523  O OG1 . THR A 1 72  ? 8.679   37.039  15.485  1.00 72.67  ? 70  THR B OG1 1 
ATOM   524  C CG2 . THR A 1 72  ? 11.056  37.230  15.750  1.00 68.68  ? 70  THR B CG2 1 
ATOM   525  N N   . ILE A 1 73  ? 11.710  33.744  15.024  1.00 67.09  ? 71  ILE B N   1 
ATOM   526  C CA  . ILE A 1 73  ? 13.116  33.444  14.782  1.00 65.63  ? 71  ILE B CA  1 
ATOM   527  C C   . ILE A 1 73  ? 13.743  34.622  14.067  1.00 63.96  ? 71  ILE B C   1 
ATOM   528  O O   . ILE A 1 73  ? 13.087  35.303  13.274  1.00 66.43  ? 71  ILE B O   1 
ATOM   529  C CB  . ILE A 1 73  ? 13.308  32.146  13.971  1.00 64.84  ? 71  ILE B CB  1 
ATOM   530  C CG1 . ILE A 1 73  ? 14.773  31.710  14.003  1.00 61.31  ? 71  ILE B CG1 1 
ATOM   531  C CG2 . ILE A 1 73  ? 12.951  32.346  12.533  1.00 66.12  ? 71  ILE B CG2 1 
ATOM   532  C CD1 . ILE A 1 73  ? 15.018  30.403  13.327  1.00 63.01  ? 71  ILE B CD1 1 
ATOM   533  N N   . SER A 1 74  ? 15.022  34.861  14.349  1.00 63.80  ? 72  SER B N   1 
ATOM   534  C CA  . SER A 1 74  ? 15.758  35.984  13.780  1.00 65.05  ? 72  SER B CA  1 
ATOM   535  C C   . SER A 1 74  ? 17.228  35.820  14.131  1.00 64.44  ? 72  SER B C   1 
ATOM   536  O O   . SER A 1 74  ? 17.608  34.894  14.851  1.00 64.68  ? 72  SER B O   1 
ATOM   537  C CB  . SER A 1 74  ? 15.211  37.311  14.284  1.00 66.71  ? 72  SER B CB  1 
ATOM   538  O OG  . SER A 1 74  ? 14.116  37.697  13.470  1.00 70.33  ? 72  SER B OG  1 
ATOM   539  N N   . ALA A 1 75  ? 18.057  36.716  13.599  1.00 65.50  ? 73  ALA B N   1 
ATOM   540  C CA  . ALA A 1 75  ? 19.498  36.578  13.758  1.00 65.08  ? 73  ALA B CA  1 
ATOM   541  C C   . ALA A 1 75  ? 20.171  37.926  13.582  1.00 67.91  ? 73  ALA B C   1 
ATOM   542  O O   . ALA A 1 75  ? 19.738  38.758  12.779  1.00 68.15  ? 73  ALA B O   1 
ATOM   543  C CB  . ALA A 1 75  ? 20.082  35.593  12.756  1.00 64.10  ? 73  ALA B CB  1 
ATOM   544  N N   . ASP A 1 76  ? 21.237  38.128  14.342  1.00 68.16  ? 74  ASP B N   1 
ATOM   545  C CA  . ASP A 1 76  ? 22.016  39.356  14.283  1.00 71.27  ? 74  ASP B CA  1 
ATOM   546  C C   . ASP A 1 76  ? 23.423  38.966  13.879  1.00 74.33  ? 74  ASP B C   1 
ATOM   547  O O   . ASP A 1 76  ? 24.172  38.414  14.693  1.00 73.62  ? 74  ASP B O   1 
ATOM   548  C CB  . ASP A 1 76  ? 22.028  40.100  15.602  1.00 75.90  ? 74  ASP B CB  1 
ATOM   549  C CG  . ASP A 1 76  ? 22.588  41.486  15.442  1.00 82.91  ? 74  ASP B CG  1 
ATOM   550  O OD1 . ASP A 1 76  ? 21.824  42.436  15.128  1.00 82.78  ? 74  ASP B OD1 1 
ATOM   551  O OD2 . ASP A 1 76  ? 23.834  41.584  15.518  1.00 84.02  ? 74  ASP B OD2 1 
ATOM   552  N N   . THR A 1 77  ? 23.763  39.272  12.624  1.00 78.33  ? 75  THR B N   1 
ATOM   553  C CA  . THR A 1 77  ? 24.983  38.754  12.011  1.00 78.48  ? 75  THR B CA  1 
ATOM   554  C C   . THR A 1 77  ? 26.225  39.370  12.624  1.00 80.85  ? 75  THR B C   1 
ATOM   555  O O   . THR A 1 77  ? 27.267  38.708  12.747  1.00 78.01  ? 75  THR B O   1 
ATOM   556  C CB  . THR A 1 77  ? 24.946  39.022  10.515  1.00 79.34  ? 75  THR B CB  1 
ATOM   557  O OG1 . THR A 1 77  ? 23.883  38.256  9.939   1.00 75.69  ? 75  THR B OG1 1 
ATOM   558  C CG2 . THR A 1 77  ? 26.281  38.669  9.872   1.00 82.18  ? 75  THR B CG2 1 
ATOM   559  N N   . SER A 1 78  ? 26.145  40.657  12.961  1.00 90.20  ? 76  SER B N   1 
ATOM   560  C CA  . SER A 1 78  ? 27.179  41.303  13.755  1.00 90.23  ? 76  SER B CA  1 
ATOM   561  C C   . SER A 1 78  ? 27.539  40.456  14.969  1.00 87.74  ? 76  SER B C   1 
ATOM   562  O O   . SER A 1 78  ? 28.711  40.127  15.193  1.00 87.55  ? 76  SER B O   1 
ATOM   563  C CB  . SER A 1 78  ? 26.685  42.687  14.171  1.00 91.24  ? 76  SER B CB  1 
ATOM   564  O OG  . SER A 1 78  ? 25.995  42.614  15.406  1.00 95.21  ? 76  SER B OG  1 
ATOM   565  N N   . LYS A 1 79  ? 26.532  40.059  15.740  1.00 82.52  ? 77  LYS B N   1 
ATOM   566  C CA  . LYS A 1 79  ? 26.748  39.321  16.972  1.00 79.20  ? 77  LYS B CA  1 
ATOM   567  C C   . LYS A 1 79  ? 26.728  37.799  16.778  1.00 74.85  ? 77  LYS B C   1 
ATOM   568  O O   . LYS A 1 79  ? 26.712  37.070  17.779  1.00 71.12  ? 77  LYS B O   1 
ATOM   569  C CB  . LYS A 1 79  ? 25.713  39.756  18.014  1.00 75.24  ? 77  LYS B CB  1 
ATOM   570  N N   . ASN A 1 80  ? 26.757  37.313  15.531  1.00 72.55  ? 78  ASN B N   1 
ATOM   571  C CA  . ASN A 1 80  ? 26.860  35.885  15.202  1.00 64.87  ? 78  ASN B CA  1 
ATOM   572  C C   . ASN A 1 80  ? 25.971  35.037  16.107  1.00 64.66  ? 78  ASN B C   1 
ATOM   573  O O   . ASN A 1 80  ? 26.430  34.259  16.944  1.00 61.49  ? 78  ASN B O   1 
ATOM   574  C CB  . ASN A 1 80  ? 28.304  35.412  15.283  1.00 63.44  ? 78  ASN B CB  1 
ATOM   575  C CG  . ASN A 1 80  ? 28.564  34.216  14.397  1.00 65.26  ? 78  ASN B CG  1 
ATOM   576  O OD1 . ASN A 1 80  ? 27.627  33.632  13.851  1.00 64.92  ? 78  ASN B OD1 1 
ATOM   577  N ND2 . ASN A 1 80  ? 29.840  33.847  14.228  1.00 63.16  ? 78  ASN B ND2 1 
ATOM   578  N N   . THR A 1 81  ? 24.671  35.227  15.952  1.00 62.96  ? 79  THR B N   1 
ATOM   579  C CA  . THR A 1 81  ? 23.749  34.722  16.952  1.00 61.89  ? 79  THR B CA  1 
ATOM   580  C C   . THR A 1 81  ? 22.359  34.770  16.359  1.00 62.96  ? 79  THR B C   1 
ATOM   581  O O   . THR A 1 81  ? 22.063  35.615  15.506  1.00 66.44  ? 79  THR B O   1 
ATOM   582  C CB  . THR A 1 81  ? 23.800  35.570  18.235  1.00 67.28  ? 79  THR B CB  1 
ATOM   583  O OG1 . THR A 1 81  ? 25.150  35.645  18.718  1.00 66.48  ? 79  THR B OG1 1 
ATOM   584  C CG2 . THR A 1 81  ? 22.912  34.980  19.328  1.00 66.69  ? 79  THR B CG2 1 
ATOM   585  N N   . ALA A 1 82  ? 21.514  33.862  16.812  1.00 61.07  ? 80  ALA B N   1 
ATOM   586  C CA  . ALA A 1 82  ? 20.121  33.878  16.426  1.00 61.29  ? 80  ALA B CA  1 
ATOM   587  C C   . ALA A 1 82  ? 19.274  33.906  17.687  1.00 61.25  ? 80  ALA B C   1 
ATOM   588  O O   . ALA A 1 82  ? 19.781  33.823  18.807  1.00 60.94  ? 80  ALA B O   1 
ATOM   589  C CB  . ALA A 1 82  ? 19.767  32.679  15.533  1.00 60.23  ? 80  ALA B CB  1 
ATOM   590  N N   . TYR A 1 83  ? 17.970  34.036  17.497  1.00 61.65  ? 81  TYR B N   1 
ATOM   591  C CA  . TYR A 1 83  ? 17.066  34.289  18.609  1.00 62.00  ? 81  TYR B CA  1 
ATOM   592  C C   . TYR A 1 83  ? 15.729  33.682  18.258  1.00 64.98  ? 81  TYR B C   1 
ATOM   593  O O   . TYR A 1 83  ? 15.102  34.103  17.278  1.00 64.76  ? 81  TYR B O   1 
ATOM   594  C CB  . TYR A 1 83  ? 16.899  35.800  18.882  1.00 63.68  ? 81  TYR B CB  1 
ATOM   595  C CG  . TYR A 1 83  ? 18.207  36.488  19.145  1.00 64.14  ? 81  TYR B CG  1 
ATOM   596  C CD1 . TYR A 1 83  ? 18.815  36.371  20.373  1.00 63.75  ? 81  TYR B CD1 1 
ATOM   597  C CD2 . TYR A 1 83  ? 18.868  37.197  18.144  1.00 64.99  ? 81  TYR B CD2 1 
ATOM   598  C CE1 . TYR A 1 83  ? 20.017  36.950  20.628  1.00 64.31  ? 81  TYR B CE1 1 
ATOM   599  C CE2 . TYR A 1 83  ? 20.095  37.783  18.393  1.00 66.95  ? 81  TYR B CE2 1 
ATOM   600  C CZ  . TYR A 1 83  ? 20.658  37.656  19.654  1.00 66.00  ? 81  TYR B CZ  1 
ATOM   601  O OH  . TYR A 1 83  ? 21.870  38.226  19.970  1.00 70.50  ? 81  TYR B OH  1 
ATOM   602  N N   . LEU A 1 84  ? 15.291  32.708  19.043  1.00 63.38  ? 82  LEU B N   1 
ATOM   603  C CA  . LEU A 1 84  ? 13.888  32.346  19.041  1.00 63.15  ? 82  LEU B CA  1 
ATOM   604  C C   . LEU A 1 84  ? 13.233  33.165  20.141  1.00 68.15  ? 82  LEU B C   1 
ATOM   605  O O   . LEU A 1 84  ? 13.695  33.162  21.288  1.00 67.45  ? 82  LEU B O   1 
ATOM   606  C CB  . LEU A 1 84  ? 13.673  30.849  19.244  1.00 64.26  ? 82  LEU B CB  1 
ATOM   607  C CG  . LEU A 1 84  ? 12.168  30.550  19.264  1.00 69.48  ? 82  LEU B CG  1 
ATOM   608  C CD1 . LEU A 1 84  ? 11.598  30.761  17.873  1.00 67.33  ? 82  LEU B CD1 1 
ATOM   609  C CD2 . LEU A 1 84  ? 11.832  29.157  19.777  1.00 63.29  ? 82  LEU B CD2 1 
ATOM   610  N N   . GLN A 1 85  ? 12.204  33.914  19.773  1.00 69.40  ? 83  GLN B N   1 
ATOM   611  C CA  . GLN A 1 85  ? 11.478  34.784  20.682  1.00 69.52  ? 83  GLN B CA  1 
ATOM   612  C C   . GLN A 1 85  ? 10.082  34.202  20.823  1.00 72.62  ? 83  GLN B C   1 
ATOM   613  O O   . GLN A 1 85  ? 9.367   34.064  19.826  1.00 74.61  ? 83  GLN B O   1 
ATOM   614  C CB  . GLN A 1 85  ? 11.443  36.219  20.137  1.00 69.59  ? 83  GLN B CB  1 
ATOM   615  C CG  . GLN A 1 85  ? 10.414  37.130  20.791  1.00 72.00  ? 83  GLN B CG  1 
ATOM   616  C CD  . GLN A 1 85  ? 10.774  37.493  22.230  1.00 72.72  ? 83  GLN B CD  1 
ATOM   617  O OE1 . GLN A 1 85  ? 11.725  38.239  22.483  1.00 72.20  ? 83  GLN B OE1 1 
ATOM   618  N NE2 . GLN A 1 85  ? 10.021  36.940  23.184  1.00 73.43  ? 83  GLN B NE2 1 
ATOM   619  N N   . MET A 1 86  ? 9.704   33.824  22.038  1.00 73.37  ? 84  MET B N   1 
ATOM   620  C CA  . MET A 1 86  ? 8.378   33.267  22.277  1.00 76.09  ? 84  MET B CA  1 
ATOM   621  C C   . MET A 1 86  ? 7.593   34.186  23.200  1.00 75.00  ? 84  MET B C   1 
ATOM   622  O O   . MET A 1 86  ? 8.062   34.546  24.287  1.00 73.44  ? 84  MET B O   1 
ATOM   623  C CB  . MET A 1 86  ? 8.457   31.858  22.853  1.00 77.29  ? 84  MET B CB  1 
ATOM   624  C CG  . MET A 1 86  ? 9.480   31.017  22.157  1.00 75.49  ? 84  MET B CG  1 
ATOM   625  S SD  . MET A 1 86  ? 9.944   29.601  23.171  1.00 69.53  ? 84  MET B SD  1 
ATOM   626  C CE  . MET A 1 86  ? 11.704  29.860  23.164  1.00 60.82  ? 84  MET B CE  1 
ATOM   627  N N   . ASN A 1 87  ? 6.413   34.570  22.734  1.00 76.53  ? 85  ASN B N   1 
ATOM   628  C CA  . ASN A 1 87  ? 5.399   35.341  23.426  1.00 73.91  ? 85  ASN B CA  1 
ATOM   629  C C   . ASN A 1 87  ? 4.153   34.473  23.469  1.00 76.44  ? 85  ASN B C   1 
ATOM   630  O O   . ASN A 1 87  ? 4.073   33.460  22.772  1.00 82.01  ? 85  ASN B O   1 
ATOM   631  C CB  . ASN A 1 87  ? 5.134   36.660  22.693  1.00 70.13  ? 85  ASN B CB  1 
ATOM   632  C CG  . ASN A 1 87  ? 6.425   37.380  22.313  1.00 72.86  ? 85  ASN B CG  1 
ATOM   633  O OD1 . ASN A 1 87  ? 7.429   37.289  23.022  1.00 71.72  ? 85  ASN B OD1 1 
ATOM   634  N ND2 . ASN A 1 87  ? 6.407   38.091  21.184  1.00 76.29  ? 85  ASN B ND2 1 
ATOM   635  N N   . SER A 1 88  ? 3.191   34.836  24.312  1.00 77.16  ? 86  SER B N   1 
ATOM   636  C CA  . SER A 1 88  ? 1.924   34.108  24.374  1.00 79.86  ? 86  SER B CA  1 
ATOM   637  C C   . SER A 1 88  ? 2.152   32.616  24.660  1.00 81.20  ? 86  SER B C   1 
ATOM   638  O O   . SER A 1 88  ? 1.359   31.755  24.269  1.00 80.32  ? 86  SER B O   1 
ATOM   639  C CB  . SER A 1 88  ? 1.131   34.326  23.078  1.00 79.11  ? 86  SER B CB  1 
ATOM   640  O OG  . SER A 1 88  ? -0.174  33.789  23.153  1.00 85.02  ? 86  SER B OG  1 
ATOM   641  N N   . LEU A 1 89  ? 3.254   32.326  25.355  1.00 79.36  ? 87  LEU B N   1 
ATOM   642  C CA  . LEU A 1 89  ? 3.687   30.962  25.633  1.00 81.72  ? 87  LEU B CA  1 
ATOM   643  C C   . LEU A 1 89  ? 2.643   30.192  26.436  1.00 82.09  ? 87  LEU B C   1 
ATOM   644  O O   . LEU A 1 89  ? 2.083   30.697  27.409  1.00 82.66  ? 87  LEU B O   1 
ATOM   645  C CB  . LEU A 1 89  ? 4.998   30.991  26.419  1.00 82.35  ? 87  LEU B CB  1 
ATOM   646  C CG  . LEU A 1 89  ? 6.321   30.993  25.657  1.00 81.27  ? 87  LEU B CG  1 
ATOM   647  C CD1 . LEU A 1 89  ? 7.446   31.440  26.577  1.00 80.53  ? 87  LEU B CD1 1 
ATOM   648  C CD2 . LEU A 1 89  ? 6.613   29.628  25.082  1.00 78.99  ? 87  LEU B CD2 1 
ATOM   649  N N   . ARG A 1 90  ? 2.411   28.948  26.051  1.00 82.44  ? 88  ARG B N   1 
ATOM   650  C CA  . ARG A 1 90  ? 1.400   28.105  26.665  1.00 78.57  ? 88  ARG B CA  1 
ATOM   651  C C   . ARG A 1 90  ? 2.107   26.913  27.298  1.00 75.26  ? 88  ARG B C   1 
ATOM   652  O O   . ARG A 1 90  ? 3.285   26.680  27.049  1.00 76.61  ? 88  ARG B O   1 
ATOM   653  C CB  . ARG A 1 90  ? 0.369   27.660  25.613  1.00 83.12  ? 88  ARG B CB  1 
ATOM   654  C CG  . ARG A 1 90  ? 0.175   28.666  24.417  1.00 83.48  ? 88  ARG B CG  1 
ATOM   655  C CD  . ARG A 1 90  ? -0.938  29.691  24.686  1.00 84.73  ? 88  ARG B CD  1 
ATOM   656  N NE  . ARG A 1 90  ? -0.618  30.618  25.768  1.00 89.25  ? 88  ARG B NE  1 
ATOM   657  C CZ  . ARG A 1 90  ? -1.503  31.422  26.350  1.00 87.64  ? 88  ARG B CZ  1 
ATOM   658  N NH1 . ARG A 1 90  ? -2.774  31.425  25.986  1.00 90.09  ? 88  ARG B NH1 1 
ATOM   659  N NH2 . ARG A 1 90  ? -1.112  32.213  27.353  1.00 84.13  ? 88  ARG B NH2 1 
ATOM   660  N N   . ALA A 1 91  ? 1.385   26.136  28.108  1.00 78.34  ? 89  ALA B N   1 
ATOM   661  C CA  . ALA A 1 91  ? 2.012   25.007  28.799  1.00 80.01  ? 89  ALA B CA  1 
ATOM   662  C C   . ALA A 1 91  ? 2.491   23.918  27.840  1.00 82.07  ? 89  ALA B C   1 
ATOM   663  O O   . ALA A 1 91  ? 3.282   23.049  28.229  1.00 76.20  ? 89  ALA B O   1 
ATOM   664  C CB  . ALA A 1 91  ? 1.043   24.401  29.811  1.00 74.03  ? 89  ALA B CB  1 
ATOM   665  N N   . GLU A 1 92  ? 2.021   23.938  26.599  1.00 79.95  ? 90  GLU B N   1 
ATOM   666  C CA  . GLU A 1 92  ? 2.446   22.945  25.630  1.00 80.46  ? 90  GLU B CA  1 
ATOM   667  C C   . GLU A 1 92  ? 3.855   23.208  25.121  1.00 79.66  ? 90  GLU B C   1 
ATOM   668  O O   . GLU A 1 92  ? 4.504   22.276  24.634  1.00 80.95  ? 90  GLU B O   1 
ATOM   669  C CB  . GLU A 1 92  ? 1.424   22.918  24.500  1.00 83.64  ? 90  GLU B CB  1 
ATOM   670  C CG  . GLU A 1 92  ? -0.003  22.901  25.080  1.00 87.06  ? 90  GLU B CG  1 
ATOM   671  C CD  . GLU A 1 92  ? -0.976  23.846  24.379  1.00 93.42  ? 90  GLU B CD  1 
ATOM   672  O OE1 . GLU A 1 92  ? -0.606  25.011  24.094  1.00 91.96  ? 90  GLU B OE1 1 
ATOM   673  O OE2 . GLU A 1 92  ? -2.136  23.430  24.155  1.00 94.73  ? 90  GLU B OE2 1 
ATOM   674  N N   . ASP A 1 93  ? 4.360   24.433  25.266  1.00 74.08  ? 91  ASP B N   1 
ATOM   675  C CA  . ASP A 1 93  ? 5.676   24.799  24.750  1.00 74.48  ? 91  ASP B CA  1 
ATOM   676  C C   . ASP A 1 93  ? 6.829   24.459  25.695  1.00 70.13  ? 91  ASP B C   1 
ATOM   677  O O   . ASP A 1 93  ? 7.978   24.781  25.367  1.00 68.97  ? 91  ASP B O   1 
ATOM   678  C CB  . ASP A 1 93  ? 5.737   26.298  24.398  1.00 77.41  ? 91  ASP B CB  1 
ATOM   679  C CG  . ASP A 1 93  ? 4.776   26.697  23.282  1.00 77.44  ? 91  ASP B CG  1 
ATOM   680  O OD1 . ASP A 1 93  ? 4.859   26.081  22.189  1.00 73.32  ? 91  ASP B OD1 1 
ATOM   681  O OD2 . ASP A 1 93  ? 3.965   27.635  23.495  1.00 77.76  ? 91  ASP B OD2 1 
ATOM   682  N N   . THR A 1 94  ? 6.568   23.818  26.840  1.00 70.30  ? 92  THR B N   1 
ATOM   683  C CA  . THR A 1 94  ? 7.661   23.430  27.733  1.00 66.18  ? 92  THR B CA  1 
ATOM   684  C C   . THR A 1 94  ? 8.442   22.278  27.099  1.00 61.93  ? 92  THR B C   1 
ATOM   685  O O   . THR A 1 94  ? 7.867   21.224  26.799  1.00 62.50  ? 92  THR B O   1 
ATOM   686  C CB  . THR A 1 94  ? 7.140   23.051  29.131  1.00 63.86  ? 92  THR B CB  1 
ATOM   687  O OG1 . THR A 1 94  ? 6.840   21.656  29.206  1.00 61.79  ? 92  THR B OG1 1 
ATOM   688  C CG2 . THR A 1 94  ? 5.885   23.806  29.474  1.00 65.64  ? 92  THR B CG2 1 
ATOM   689  N N   . ALA A 1 95  ? 9.742   22.481  26.878  1.00 56.89  ? 93  ALA B N   1 
ATOM   690  C CA  . ALA A 1 95  ? 10.571  21.464  26.237  1.00 56.93  ? 93  ALA B CA  1 
ATOM   691  C C   . ALA A 1 95  ? 12.030  21.919  26.249  1.00 56.29  ? 93  ALA B C   1 
ATOM   692  O O   . ALA A 1 95  ? 12.357  23.016  26.714  1.00 55.75  ? 93  ALA B O   1 
ATOM   693  C CB  . ALA A 1 95  ? 10.095  21.187  24.810  1.00 59.01  ? 93  ALA B CB  1 
ATOM   694  N N   . VAL A 1 96  ? 12.908  21.048  25.739  1.00 54.39  ? 94  VAL B N   1 
ATOM   695  C CA  . VAL A 1 96  ? 14.309  21.386  25.493  1.00 55.31  ? 94  VAL B CA  1 
ATOM   696  C C   . VAL A 1 96  ? 14.434  21.953  24.083  1.00 58.43  ? 94  VAL B C   1 
ATOM   697  O O   . VAL A 1 96  ? 14.114  21.277  23.097  1.00 57.13  ? 94  VAL B O   1 
ATOM   698  C CB  . VAL A 1 96  ? 15.226  20.169  25.668  1.00 53.12  ? 94  VAL B CB  1 
ATOM   699  C CG1 . VAL A 1 96  ? 16.528  20.390  24.924  1.00 52.59  ? 94  VAL B CG1 1 
ATOM   700  C CG2 . VAL A 1 96  ? 15.519  19.966  27.115  1.00 53.37  ? 94  VAL B CG2 1 
ATOM   701  N N   . TYR A 1 97  ? 14.913  23.186  23.986  1.00 56.69  ? 95  TYR B N   1 
ATOM   702  C CA  . TYR A 1 97  ? 15.000  23.875  22.720  1.00 54.26  ? 95  TYR B CA  1 
ATOM   703  C C   . TYR A 1 97  ? 16.401  23.683  22.164  1.00 55.96  ? 95  TYR B C   1 
ATOM   704  O O   . TYR A 1 97  ? 17.385  23.988  22.844  1.00 56.66  ? 95  TYR B O   1 
ATOM   705  C CB  . TYR A 1 97  ? 14.641  25.339  22.910  1.00 55.27  ? 95  TYR B CB  1 
ATOM   706  C CG  . TYR A 1 97  ? 13.147  25.497  22.910  1.00 55.93  ? 95  TYR B CG  1 
ATOM   707  C CD1 . TYR A 1 97  ? 12.379  25.074  23.993  1.00 56.27  ? 95  TYR B CD1 1 
ATOM   708  C CD2 . TYR A 1 97  ? 12.492  26.034  21.821  1.00 56.40  ? 95  TYR B CD2 1 
ATOM   709  C CE1 . TYR A 1 97  ? 10.987  25.204  23.984  1.00 57.45  ? 95  TYR B CE1 1 
ATOM   710  C CE2 . TYR A 1 97  ? 11.118  26.166  21.795  1.00 57.10  ? 95  TYR B CE2 1 
ATOM   711  C CZ  . TYR A 1 97  ? 10.366  25.756  22.871  1.00 62.17  ? 95  TYR B CZ  1 
ATOM   712  O OH  . TYR A 1 97  ? 8.992   25.909  22.824  1.00 68.12  ? 95  TYR B OH  1 
ATOM   713  N N   . TYR A 1 98  ? 16.479  23.143  20.942  1.00 53.89  ? 96  TYR B N   1 
ATOM   714  C CA  . TYR A 1 98  ? 17.705  22.968  20.179  1.00 52.71  ? 96  TYR B CA  1 
ATOM   715  C C   . TYR A 1 98  ? 17.799  24.025  19.084  1.00 53.24  ? 96  TYR B C   1 
ATOM   716  O O   . TYR A 1 98  ? 16.797  24.410  18.479  1.00 53.69  ? 96  TYR B O   1 
ATOM   717  C CB  . TYR A 1 98  ? 17.737  21.576  19.529  1.00 51.94  ? 96  TYR B CB  1 
ATOM   718  C CG  . TYR A 1 98  ? 18.067  20.437  20.460  1.00 51.44  ? 96  TYR B CG  1 
ATOM   719  C CD1 . TYR A 1 98  ? 19.360  20.239  20.915  1.00 51.16  ? 96  TYR B CD1 1 
ATOM   720  C CD2 . TYR A 1 98  ? 17.075  19.566  20.895  1.00 51.38  ? 96  TYR B CD2 1 
ATOM   721  C CE1 . TYR A 1 98  ? 19.645  19.211  21.770  1.00 50.83  ? 96  TYR B CE1 1 
ATOM   722  C CE2 . TYR A 1 98  ? 17.355  18.540  21.740  1.00 51.08  ? 96  TYR B CE2 1 
ATOM   723  C CZ  . TYR A 1 98  ? 18.636  18.369  22.172  1.00 50.81  ? 96  TYR B CZ  1 
ATOM   724  O OH  . TYR A 1 98  ? 18.928  17.341  23.016  1.00 50.62  ? 96  TYR B OH  1 
ATOM   725  N N   . CYS A 1 99  ? 19.007  24.477  18.805  1.00 54.31  ? 97  CYS B N   1 
ATOM   726  C CA  . CYS A 1 99  ? 19.223  25.304  17.636  1.00 55.00  ? 97  CYS B CA  1 
ATOM   727  C C   . CYS A 1 99  ? 20.267  24.644  16.738  1.00 56.83  ? 97  CYS B C   1 
ATOM   728  O O   . CYS A 1 99  ? 21.153  23.937  17.227  1.00 58.13  ? 97  CYS B O   1 
ATOM   729  C CB  . CYS A 1 99  ? 19.671  26.699  18.040  1.00 58.22  ? 97  CYS B CB  1 
ATOM   730  S SG  . CYS A 1 99  ? 21.408  26.725  18.525  1.00 61.96  ? 97  CYS B SG  1 
ATOM   731  N N   . ALA A 1 100 ? 20.182  24.859  15.423  1.00 53.57  ? 98  ALA B N   1 
ATOM   732  C CA  . ALA A 1 100 ? 21.000  24.002  14.569  1.00 56.95  ? 98  ALA B CA  1 
ATOM   733  C C   . ALA A 1 100 ? 21.241  24.624  13.204  1.00 53.54  ? 98  ALA B C   1 
ATOM   734  O O   . ALA A 1 100 ? 20.350  25.240  12.621  1.00 54.13  ? 98  ALA B O   1 
ATOM   735  C CB  . ALA A 1 100 ? 20.373  22.605  14.388  1.00 52.15  ? 98  ALA B CB  1 
ATOM   736  N N   . ARG A 1 101 ? 22.441  24.385  12.694  1.00 53.42  ? 99  ARG B N   1 
ATOM   737  C CA  . ARG A 1 101 ? 22.869  24.834  11.385  1.00 54.00  ? 99  ARG B CA  1 
ATOM   738  C C   . ARG A 1 101 ? 22.286  23.971  10.259  1.00 53.64  ? 99  ARG B C   1 
ATOM   739  O O   . ARG A 1 101 ? 22.178  22.745  10.378  1.00 52.78  ? 99  ARG B O   1 
ATOM   740  C CB  . ARG A 1 101 ? 24.396  24.802  11.342  1.00 54.06  ? 99  ARG B CB  1 
ATOM   741  C CG  . ARG A 1 101 ? 25.010  25.448  10.155  1.00 54.90  ? 99  ARG B CG  1 
ATOM   742  C CD  . ARG A 1 101 ? 26.485  25.578  10.366  1.00 55.12  ? 99  ARG B CD  1 
ATOM   743  N NE  . ARG A 1 101 ? 27.216  24.519  9.701   1.00 54.65  ? 99  ARG B NE  1 
ATOM   744  C CZ  . ARG A 1 101 ? 28.529  24.372  9.766   1.00 54.79  ? 99  ARG B CZ  1 
ATOM   745  N NH1 . ARG A 1 101 ? 29.289  25.238  10.414  1.00 55.41  ? 99  ARG B NH1 1 
ATOM   746  N NH2 . ARG A 1 101 ? 29.092  23.318  9.186   1.00 54.36  ? 99  ARG B NH2 1 
ATOM   747  N N   . GLY A 1 102 ? 21.937  24.621  9.145   1.00 55.88  ? 100 GLY B N   1 
ATOM   748  C CA  . GLY A 1 102 ? 21.469  23.896  7.959   1.00 54.17  ? 100 GLY B CA  1 
ATOM   749  C C   . GLY A 1 102 ? 22.616  23.295  7.162   1.00 54.01  ? 100 GLY B C   1 
ATOM   750  O O   . GLY A 1 102 ? 23.687  23.879  7.021   1.00 54.55  ? 100 GLY B O   1 
ATOM   751  N N   . TYR A 1 103 ? 22.388  22.083  6.683   1.00 53.32  ? 101 TYR B N   1 
ATOM   752  C CA  . TYR A 1 103 ? 23.260  21.373  5.741   1.00 53.21  ? 101 TYR B CA  1 
ATOM   753  C C   . TYR A 1 103 ? 22.317  21.024  4.605   1.00 53.31  ? 101 TYR B C   1 
ATOM   754  O O   . TYR A 1 103 ? 21.516  20.092  4.731   1.00 52.66  ? 101 TYR B O   1 
ATOM   755  C CB  . TYR A 1 103 ? 23.893  20.126  6.370   1.00 52.32  ? 101 TYR B CB  1 
ATOM   756  C CG  . TYR A 1 103 ? 24.918  19.355  5.514   1.00 52.28  ? 101 TYR B CG  1 
ATOM   757  C CD1 . TYR A 1 103 ? 24.533  18.362  4.630   1.00 52.00  ? 101 TYR B CD1 1 
ATOM   758  C CD2 . TYR A 1 103 ? 26.280  19.580  5.667   1.00 52.58  ? 101 TYR B CD2 1 
ATOM   759  C CE1 . TYR A 1 103 ? 25.484  17.668  3.900   1.00 52.05  ? 101 TYR B CE1 1 
ATOM   760  C CE2 . TYR A 1 103 ? 27.223  18.884  4.952   1.00 52.64  ? 101 TYR B CE2 1 
ATOM   761  C CZ  . TYR A 1 103 ? 26.832  17.940  4.075   1.00 52.39  ? 101 TYR B CZ  1 
ATOM   762  O OH  . TYR A 1 103 ? 27.813  17.278  3.369   1.00 52.56  ? 101 TYR B OH  1 
ATOM   763  N N   . GLY A 1 104 ? 22.368  21.815  3.541   1.00 54.22  ? 102 GLY B N   1 
ATOM   764  C CA  . GLY A 1 104 ? 21.386  21.702  2.487   1.00 54.50  ? 102 GLY B CA  1 
ATOM   765  C C   . GLY A 1 104 ? 20.001  21.696  3.082   1.00 54.24  ? 102 GLY B C   1 
ATOM   766  O O   . GLY A 1 104 ? 19.616  22.649  3.754   1.00 58.47  ? 102 GLY B O   1 
ATOM   767  N N   . TRP A 1 105 ? 19.251  20.630  2.870   1.00 53.62  ? 103 TRP B N   1 
ATOM   768  C CA  . TRP A 1 105 ? 17.980  20.435  3.543   1.00 53.61  ? 103 TRP B CA  1 
ATOM   769  C C   . TRP A 1 105 ? 18.105  19.597  4.810   1.00 53.07  ? 103 TRP B C   1 
ATOM   770  O O   . TRP A 1 105 ? 17.082  19.142  5.341   1.00 55.03  ? 103 TRP B O   1 
ATOM   771  C CB  . TRP A 1 105 ? 16.968  19.767  2.610   1.00 56.14  ? 103 TRP B CB  1 
ATOM   772  C CG  . TRP A 1 105 ? 16.656  20.480  1.328   1.00 59.64  ? 103 TRP B CG  1 
ATOM   773  C CD1 . TRP A 1 105 ? 15.476  21.092  1.012   1.00 62.35  ? 103 TRP B CD1 1 
ATOM   774  C CD2 . TRP A 1 105 ? 17.496  20.604  0.163   1.00 57.48  ? 103 TRP B CD2 1 
ATOM   775  N NE1 . TRP A 1 105 ? 15.544  21.616  -0.257  1.00 65.27  ? 103 TRP B NE1 1 
ATOM   776  C CE2 . TRP A 1 105 ? 16.762  21.321  -0.806  1.00 60.48  ? 103 TRP B CE2 1 
ATOM   777  C CE3 . TRP A 1 105 ? 18.787  20.181  -0.153  1.00 60.58  ? 103 TRP B CE3 1 
ATOM   778  C CZ2 . TRP A 1 105 ? 17.276  21.629  -2.074  1.00 62.02  ? 103 TRP B CZ2 1 
ATOM   779  C CZ3 . TRP A 1 105 ? 19.308  20.499  -1.429  1.00 62.12  ? 103 TRP B CZ3 1 
ATOM   780  C CH2 . TRP A 1 105 ? 18.547  21.220  -2.364  1.00 60.57  ? 103 TRP B CH2 1 
ATOM   781  N N   . ALA A 1 106 ? 19.317  19.365  5.304   1.00 52.09  ? 104 ALA B N   1 
ATOM   782  C CA  . ALA A 1 106 ? 19.456  18.662  6.576   1.00 51.37  ? 104 ALA B CA  1 
ATOM   783  C C   . ALA A 1 106 ? 20.015  19.619  7.644   1.00 51.59  ? 104 ALA B C   1 
ATOM   784  O O   . ALA A 1 106 ? 20.144  20.822  7.426   1.00 52.32  ? 104 ALA B O   1 
ATOM   785  C CB  . ALA A 1 106 ? 20.318  17.404  6.414   1.00 50.78  ? 104 ALA B CB  1 
ATOM   786  N N   . LEU A 1 107 ? 20.345  19.052  8.807   1.00 51.04  ? 105 LEU B N   1 
ATOM   787  C CA  . LEU A 1 107 ? 20.805  19.782  9.990   1.00 51.17  ? 105 LEU B CA  1 
ATOM   788  C C   . LEU A 1 107 ? 22.064  19.109  10.520  1.00 50.72  ? 105 LEU B C   1 
ATOM   789  O O   . LEU A 1 107 ? 21.960  18.110  11.224  1.00 50.17  ? 105 LEU B O   1 
ATOM   790  C CB  . LEU A 1 107 ? 19.721  19.804  11.059  1.00 51.07  ? 105 LEU B CB  1 
ATOM   791  C CG  . LEU A 1 107 ? 18.388  20.414  10.628  1.00 51.59  ? 105 LEU B CG  1 
ATOM   792  C CD1 . LEU A 1 107 ? 17.183  19.909  11.423  1.00 51.40  ? 105 LEU B CD1 1 
ATOM   793  C CD2 . LEU A 1 107 ? 18.505  21.923  10.705  1.00 52.42  ? 105 LEU B CD2 1 
ATOM   794  N N   . ASP A 1 108 ? 23.248  19.643  10.239  1.00 51.06  ? 106 ASP B N   1 
ATOM   795  C CA  . ASP A 1 108 ? 24.414  18.837  10.573  1.00 50.69  ? 106 ASP B CA  1 
ATOM   796  C C   . ASP A 1 108 ? 24.981  19.103  11.971  1.00 53.25  ? 106 ASP B C   1 
ATOM   797  O O   . ASP A 1 108 ? 25.536  18.175  12.582  1.00 54.51  ? 106 ASP B O   1 
ATOM   798  C CB  . ASP A 1 108 ? 25.496  18.974  9.484   1.00 51.09  ? 106 ASP B CB  1 
ATOM   799  C CG  . ASP A 1 108 ? 26.074  20.365  9.357   1.00 51.91  ? 106 ASP B CG  1 
ATOM   800  O OD1 . ASP A 1 108 ? 25.696  21.275  10.146  1.00 52.18  ? 106 ASP B OD1 1 
ATOM   801  O OD2 . ASP A 1 108 ? 26.882  20.544  8.412   1.00 52.39  ? 106 ASP B OD2 1 
ATOM   802  N N   . TYR A 1 109 ? 24.833  20.309  12.530  1.00 54.08  ? 107 TYR B N   1 
ATOM   803  C CA  . TYR A 1 109 ? 25.375  20.612  13.853  1.00 51.12  ? 107 TYR B CA  1 
ATOM   804  C C   . TYR A 1 109 ? 24.281  21.119  14.777  1.00 54.37  ? 107 TYR B C   1 
ATOM   805  O O   . TYR A 1 109 ? 23.387  21.870  14.355  1.00 51.62  ? 107 TYR B O   1 
ATOM   806  C CB  . TYR A 1 109 ? 26.483  21.651  13.798  1.00 51.79  ? 107 TYR B CB  1 
ATOM   807  C CG  . TYR A 1 109 ? 27.853  21.124  13.443  1.00 52.53  ? 107 TYR B CG  1 
ATOM   808  C CD1 . TYR A 1 109 ? 28.262  21.035  12.114  1.00 53.10  ? 107 TYR B CD1 1 
ATOM   809  C CD2 . TYR A 1 109 ? 28.756  20.751  14.429  1.00 52.72  ? 107 TYR B CD2 1 
ATOM   810  C CE1 . TYR A 1 109 ? 29.528  20.587  11.785  1.00 52.20  ? 107 TYR B CE1 1 
ATOM   811  C CE2 . TYR A 1 109 ? 30.023  20.286  14.105  1.00 52.16  ? 107 TYR B CE2 1 
ATOM   812  C CZ  . TYR A 1 109 ? 30.397  20.203  12.786  1.00 51.98  ? 107 TYR B CZ  1 
ATOM   813  O OH  . TYR A 1 109 ? 31.658  19.767  12.464  1.00 53.33  ? 107 TYR B OH  1 
ATOM   814  N N   . TRP A 1 110 ? 24.373  20.716  16.053  1.00 59.26  ? 108 TRP B N   1 
ATOM   815  C CA  . TRP A 1 110 ? 23.335  20.998  17.040  1.00 53.94  ? 108 TRP B CA  1 
ATOM   816  C C   . TRP A 1 110 ? 23.941  21.563  18.321  1.00 56.86  ? 108 TRP B C   1 
ATOM   817  O O   . TRP A 1 110 ? 25.095  21.306  18.678  1.00 58.39  ? 108 TRP B O   1 
ATOM   818  C CB  . TRP A 1 110 ? 22.520  19.741  17.379  1.00 50.42  ? 108 TRP B CB  1 
ATOM   819  C CG  . TRP A 1 110 ? 21.752  19.166  16.253  1.00 50.23  ? 108 TRP B CG  1 
ATOM   820  C CD1 . TRP A 1 110 ? 22.254  18.667  15.079  1.00 50.04  ? 108 TRP B CD1 1 
ATOM   821  C CD2 . TRP A 1 110 ? 20.338  19.004  16.182  1.00 50.27  ? 108 TRP B CD2 1 
ATOM   822  N NE1 . TRP A 1 110 ? 21.229  18.232  14.279  1.00 49.95  ? 108 TRP B NE1 1 
ATOM   823  C CE2 . TRP A 1 110 ? 20.045  18.417  14.941  1.00 50.09  ? 108 TRP B CE2 1 
ATOM   824  C CE3 . TRP A 1 110 ? 19.290  19.314  17.038  1.00 50.53  ? 108 TRP B CE3 1 
ATOM   825  C CZ2 . TRP A 1 110 ? 18.752  18.131  14.546  1.00 50.14  ? 108 TRP B CZ2 1 
ATOM   826  C CZ3 . TRP A 1 110 ? 18.003  19.017  16.645  1.00 50.62  ? 108 TRP B CZ3 1 
ATOM   827  C CH2 . TRP A 1 110 ? 17.746  18.433  15.416  1.00 50.41  ? 108 TRP B CH2 1 
ATOM   828  N N   . GLY A 1 111 ? 23.148  22.355  19.011  1.00 64.01  ? 109 GLY B N   1 
ATOM   829  C CA  . GLY A 1 111 ? 23.490  22.748  20.351  1.00 64.18  ? 109 GLY B CA  1 
ATOM   830  C C   . GLY A 1 111 ? 23.259  21.594  21.297  1.00 65.85  ? 109 GLY B C   1 
ATOM   831  O O   . GLY A 1 111 ? 22.935  20.468  20.902  1.00 64.78  ? 109 GLY B O   1 
ATOM   832  N N   . GLN A 1 112 ? 23.454  21.878  22.581  1.00 61.82  ? 110 GLN B N   1 
ATOM   833  C CA  . GLN A 1 112 ? 23.052  20.902  23.575  1.00 54.77  ? 110 GLN B CA  1 
ATOM   834  C C   . GLN A 1 112 ? 21.643  21.163  24.061  1.00 52.73  ? 110 GLN B C   1 
ATOM   835  O O   . GLN A 1 112 ? 20.964  20.236  24.502  1.00 54.72  ? 110 GLN B O   1 
ATOM   836  C CB  . GLN A 1 112 ? 24.046  20.889  24.728  1.00 55.36  ? 110 GLN B CB  1 
ATOM   837  C CG  . GLN A 1 112 ? 24.888  19.621  24.724  1.00 65.73  ? 110 GLN B CG  1 
ATOM   838  C CD  . GLN A 1 112 ? 26.249  19.769  25.412  1.00 73.20  ? 110 GLN B CD  1 
ATOM   839  O OE1 . GLN A 1 112 ? 26.565  20.817  26.025  1.00 69.30  ? 110 GLN B OE1 1 
ATOM   840  N NE2 . GLN A 1 112 ? 27.071  18.707  25.307  1.00 68.97  ? 110 GLN B NE2 1 
ATOM   841  N N   . GLY A 1 113 ? 21.166  22.386  23.928  1.00 54.45  ? 111 GLY B N   1 
ATOM   842  C CA  . GLY A 1 113 ? 19.795  22.713  24.245  1.00 55.55  ? 111 GLY B CA  1 
ATOM   843  C C   . GLY A 1 113 ? 19.688  23.496  25.543  1.00 54.59  ? 111 GLY B C   1 
ATOM   844  O O   . GLY A 1 113 ? 20.638  23.604  26.325  1.00 53.28  ? 111 GLY B O   1 
ATOM   845  N N   . THR A 1 114 ? 18.513  24.085  25.749  1.00 53.86  ? 112 THR B N   1 
ATOM   846  C CA  . THR A 1 114 ? 18.160  24.565  27.074  1.00 54.71  ? 112 THR B CA  1 
ATOM   847  C C   . THR A 1 114 ? 16.733  24.167  27.392  1.00 54.97  ? 112 THR B C   1 
ATOM   848  O O   . THR A 1 114 ? 15.873  24.114  26.507  1.00 56.96  ? 112 THR B O   1 
ATOM   849  C CB  . THR A 1 114 ? 18.293  26.076  27.241  1.00 55.33  ? 112 THR B CB  1 
ATOM   850  O OG1 . THR A 1 114 ? 17.427  26.746  26.311  1.00 61.51  ? 112 THR B OG1 1 
ATOM   851  C CG2 . THR A 1 114 ? 19.725  26.504  27.065  1.00 60.80  ? 112 THR B CG2 1 
ATOM   852  N N   . LEU A 1 115 ? 16.494  23.884  28.659  1.00 55.06  ? 113 LEU B N   1 
ATOM   853  C CA  . LEU A 1 115 ? 15.170  23.524  29.106  1.00 55.51  ? 113 LEU B CA  1 
ATOM   854  C C   . LEU A 1 115 ? 14.359  24.791  29.355  1.00 56.53  ? 113 LEU B C   1 
ATOM   855  O O   . LEU A 1 115 ? 14.855  25.755  29.945  1.00 57.03  ? 113 LEU B O   1 
ATOM   856  C CB  . LEU A 1 115 ? 15.272  22.662  30.356  1.00 55.52  ? 113 LEU B CB  1 
ATOM   857  C CG  . LEU A 1 115 ? 13.931  22.117  30.792  1.00 56.03  ? 113 LEU B CG  1 
ATOM   858  C CD1 . LEU A 1 115 ? 13.244  21.441  29.623  1.00 55.65  ? 113 LEU B CD1 1 
ATOM   859  C CD2 . LEU A 1 115 ? 14.118  21.183  31.993  1.00 61.15  ? 113 LEU B CD2 1 
ATOM   860  N N   . VAL A 1 116 ? 13.128  24.799  28.864  1.00 56.92  ? 114 VAL B N   1 
ATOM   861  C CA  . VAL A 1 116 ? 12.231  25.933  28.984  1.00 58.00  ? 114 VAL B CA  1 
ATOM   862  C C   . VAL A 1 116 ? 10.963  25.381  29.604  1.00 59.51  ? 114 VAL B C   1 
ATOM   863  O O   . VAL A 1 116 ? 10.248  24.593  28.971  1.00 60.13  ? 114 VAL B O   1 
ATOM   864  C CB  . VAL A 1 116 ? 11.944  26.604  27.634  1.00 58.15  ? 114 VAL B CB  1 
ATOM   865  C CG1 . VAL A 1 116 ? 10.637  27.375  27.677  1.00 59.32  ? 114 VAL B CG1 1 
ATOM   866  C CG2 . VAL A 1 116 ? 13.093  27.510  27.230  1.00 58.87  ? 114 VAL B CG2 1 
ATOM   867  N N   . THR A 1 117 ? 10.698  25.778  30.849  1.00 63.96  ? 115 THR B N   1 
ATOM   868  C CA  . THR A 1 117 ? 9.561   25.326  31.636  1.00 62.31  ? 115 THR B CA  1 
ATOM   869  C C   . THR A 1 117 ? 8.575   26.475  31.767  1.00 62.99  ? 115 THR B C   1 
ATOM   870  O O   . THR A 1 117 ? 8.920   27.543  32.292  1.00 61.99  ? 115 THR B O   1 
ATOM   871  C CB  . THR A 1 117 ? 10.039  24.860  33.004  1.00 62.52  ? 115 THR B CB  1 
ATOM   872  O OG1 . THR A 1 117 ? 11.468  24.714  32.951  1.00 60.70  ? 115 THR B OG1 1 
ATOM   873  C CG2 . THR A 1 117 ? 9.398   23.537  33.369  1.00 64.86  ? 115 THR B CG2 1 
ATOM   874  N N   . VAL A 1 118 ? 7.364   26.272  31.264  1.00 63.77  ? 116 VAL B N   1 
ATOM   875  C CA  . VAL A 1 118 ? 6.314   27.271  31.383  1.00 64.52  ? 116 VAL B CA  1 
ATOM   876  C C   . VAL A 1 118 ? 5.164   26.604  32.121  1.00 69.33  ? 116 VAL B C   1 
ATOM   877  O O   . VAL A 1 118 ? 4.692   25.527  31.728  1.00 71.67  ? 116 VAL B O   1 
ATOM   878  C CB  . VAL A 1 118 ? 5.880   27.857  30.021  1.00 68.77  ? 116 VAL B CB  1 
ATOM   879  C CG1 . VAL A 1 118 ? 7.083   28.161  29.137  1.00 69.03  ? 116 VAL B CG1 1 
ATOM   880  C CG2 . VAL A 1 118 ? 4.917   26.991  29.296  1.00 68.01  ? 116 VAL B CG2 1 
ATOM   881  N N   . SER A 1 119 ? 4.755   27.221  33.221  1.00 70.05  ? 117 SER B N   1 
ATOM   882  C CA  . SER A 1 119 ? 3.807   26.672  34.171  1.00 69.58  ? 117 SER B CA  1 
ATOM   883  C C   . SER A 1 119 ? 3.537   27.757  35.202  1.00 70.58  ? 117 SER B C   1 
ATOM   884  O O   . SER A 1 119 ? 4.279   28.744  35.292  1.00 69.15  ? 117 SER B O   1 
ATOM   885  C CB  . SER A 1 119 ? 4.351   25.398  34.830  1.00 71.24  ? 117 SER B CB  1 
ATOM   886  O OG  . SER A 1 119 ? 3.603   25.051  35.992  1.00 77.60  ? 117 SER B OG  1 
ATOM   887  N N   . SER A 1 120 ? 2.460   27.575  35.971  1.00 73.07  ? 118 SER B N   1 
ATOM   888  C CA  . SER A 1 120 ? 2.197   28.492  37.078  1.00 74.60  ? 118 SER B CA  1 
ATOM   889  C C   . SER A 1 120 ? 2.877   28.067  38.373  1.00 72.18  ? 118 SER B C   1 
ATOM   890  O O   . SER A 1 120 ? 2.868   28.840  39.328  1.00 73.43  ? 118 SER B O   1 
ATOM   891  C CB  . SER A 1 120 ? 0.691   28.646  37.341  1.00 71.68  ? 118 SER B CB  1 
ATOM   892  O OG  . SER A 1 120 ? -0.041  27.495  36.958  1.00 72.88  ? 118 SER B OG  1 
ATOM   893  N N   . ALA A 1 121 ? 3.464   26.876  38.438  1.00 73.59  ? 119 ALA B N   1 
ATOM   894  C CA  . ALA A 1 121 ? 4.175   26.481  39.643  1.00 73.93  ? 119 ALA B CA  1 
ATOM   895  C C   . ALA A 1 121 ? 5.401   27.366  39.871  1.00 73.69  ? 119 ALA B C   1 
ATOM   896  O O   . ALA A 1 121 ? 5.918   28.020  38.961  1.00 75.52  ? 119 ALA B O   1 
ATOM   897  C CB  . ALA A 1 121 ? 4.602   25.017  39.558  1.00 75.75  ? 119 ALA B CB  1 
ATOM   898  N N   . SER A 1 122 ? 5.875   27.363  41.113  1.00 74.70  ? 120 SER B N   1 
ATOM   899  C CA  . SER A 1 122 ? 6.980   28.193  41.561  1.00 74.92  ? 120 SER B CA  1 
ATOM   900  C C   . SER A 1 122 ? 8.204   27.337  41.855  1.00 74.11  ? 120 SER B C   1 
ATOM   901  O O   . SER A 1 122 ? 8.102   26.136  42.119  1.00 76.58  ? 120 SER B O   1 
ATOM   902  C CB  . SER A 1 122 ? 6.585   28.991  42.812  1.00 73.63  ? 120 SER B CB  1 
ATOM   903  O OG  . SER A 1 122 ? 7.704   29.685  43.338  1.00 71.43  ? 120 SER B OG  1 
ATOM   904  N N   . THR A 1 123 ? 9.367   27.979  41.819  1.00 74.65  ? 121 THR B N   1 
ATOM   905  C CA  . THR A 1 123 ? 10.629  27.281  42.038  1.00 79.34  ? 121 THR B CA  1 
ATOM   906  C C   . THR A 1 123 ? 10.801  26.917  43.518  1.00 83.85  ? 121 THR B C   1 
ATOM   907  O O   . THR A 1 123 ? 10.698  27.776  44.401  1.00 81.21  ? 121 THR B O   1 
ATOM   908  C CB  . THR A 1 123 ? 11.786  28.136  41.509  1.00 76.62  ? 121 THR B CB  1 
ATOM   909  O OG1 . THR A 1 123 ? 13.046  27.654  42.001  1.00 75.67  ? 121 THR B OG1 1 
ATOM   910  C CG2 . THR A 1 123 ? 11.593  29.610  41.841  1.00 80.32  ? 121 THR B CG2 1 
ATOM   911  N N   . LYS A 1 124 ? 11.063  25.630  43.775  1.00 90.83  ? 122 LYS B N   1 
ATOM   912  C CA  . LYS A 1 124 ? 11.067  25.038  45.110  1.00 91.46  ? 122 LYS B CA  1 
ATOM   913  C C   . LYS A 1 124 ? 12.054  23.880  45.165  1.00 91.82  ? 122 LYS B C   1 
ATOM   914  O O   . LYS A 1 124 ? 11.960  22.958  44.351  1.00 91.24  ? 122 LYS B O   1 
ATOM   915  C CB  . LYS A 1 124 ? 9.673   24.526  45.482  1.00 92.95  ? 122 LYS B CB  1 
ATOM   916  C CG  . LYS A 1 124 ? 9.521   24.190  46.956  1.00 97.49  ? 122 LYS B CG  1 
ATOM   917  C CD  . LYS A 1 124 ? 8.752   22.887  47.178  1.00 98.22  ? 122 LYS B CD  1 
ATOM   918  C CE  . LYS A 1 124 ? 7.255   23.116  47.310  1.00 99.29  ? 122 LYS B CE  1 
ATOM   919  N NZ  . LYS A 1 124 ? 6.504   21.864  47.032  1.00 100.68 ? 122 LYS B NZ  1 
ATOM   920  N N   . GLY A 1 125 ? 12.976  23.912  46.129  1.00 83.81  ? 123 GLY B N   1 
ATOM   921  C CA  . GLY A 1 125 ? 13.897  22.817  46.355  1.00 79.23  ? 123 GLY B CA  1 
ATOM   922  C C   . GLY A 1 125 ? 13.188  21.522  46.735  1.00 82.73  ? 123 GLY B C   1 
ATOM   923  O O   . GLY A 1 125 ? 11.984  21.513  47.027  1.00 81.03  ? 123 GLY B O   1 
ATOM   924  N N   . PRO A 1 126 ? 13.919  20.402  46.742  1.00 81.28  ? 124 PRO B N   1 
ATOM   925  C CA  . PRO A 1 126 ? 13.286  19.096  46.945  1.00 80.38  ? 124 PRO B CA  1 
ATOM   926  C C   . PRO A 1 126 ? 13.278  18.646  48.399  1.00 83.52  ? 124 PRO B C   1 
ATOM   927  O O   . PRO A 1 126 ? 14.148  18.983  49.204  1.00 82.48  ? 124 PRO B O   1 
ATOM   928  C CB  . PRO A 1 126 ? 14.186  18.173  46.116  1.00 73.08  ? 124 PRO B CB  1 
ATOM   929  C CG  . PRO A 1 126 ? 15.543  18.718  46.429  1.00 71.34  ? 124 PRO B CG  1 
ATOM   930  C CD  . PRO A 1 126 ? 15.359  20.239  46.463  1.00 77.50  ? 124 PRO B CD  1 
ATOM   931  N N   . SER A 1 127 ? 12.271  17.852  48.731  1.00 86.17  ? 125 SER B N   1 
ATOM   932  C CA  . SER A 1 127 ? 12.289  17.083  49.964  1.00 85.90  ? 125 SER B CA  1 
ATOM   933  C C   . SER A 1 127 ? 12.933  15.736  49.673  1.00 83.12  ? 125 SER B C   1 
ATOM   934  O O   . SER A 1 127 ? 12.689  15.141  48.617  1.00 80.51  ? 125 SER B O   1 
ATOM   935  C CB  . SER A 1 127 ? 10.873  16.912  50.499  1.00 85.42  ? 125 SER B CB  1 
ATOM   936  O OG  . SER A 1 127 ? 10.150  18.106  50.259  1.00 89.78  ? 125 SER B OG  1 
ATOM   937  N N   . VAL A 1 128 ? 13.790  15.279  50.570  1.00 74.73  ? 126 VAL B N   1 
ATOM   938  C CA  . VAL A 1 128 ? 14.517  14.036  50.355  1.00 71.96  ? 126 VAL B CA  1 
ATOM   939  C C   . VAL A 1 128 ? 14.212  13.102  51.517  1.00 74.21  ? 126 VAL B C   1 
ATOM   940  O O   . VAL A 1 128 ? 14.799  13.214  52.600  1.00 79.95  ? 126 VAL B O   1 
ATOM   941  C CB  . VAL A 1 128 ? 16.015  14.261  50.202  1.00 72.12  ? 126 VAL B CB  1 
ATOM   942  C CG1 . VAL A 1 128 ? 16.723  12.917  50.137  1.00 72.42  ? 126 VAL B CG1 1 
ATOM   943  C CG2 . VAL A 1 128 ? 16.266  15.057  48.943  1.00 73.66  ? 126 VAL B CG2 1 
ATOM   944  N N   . PHE A 1 129 ? 13.353  12.240  51.310  1.00 70.69  ? 127 PHE B N   1 
ATOM   945  C CA  . PHE A 1 129 ? 12.854  11.180  52.148  1.00 72.26  ? 127 PHE B CA  1 
ATOM   946  C C   . PHE A 1 129 ? 13.564  9.868   51.822  1.00 71.98  ? 127 PHE B C   1 
ATOM   947  O O   . PHE A 1 129 ? 13.927  9.630   50.668  1.00 73.59  ? 127 PHE B O   1 
ATOM   948  C CB  . PHE A 1 129 ? 11.356  11.044  51.919  1.00 73.07  ? 127 PHE B CB  1 
ATOM   949  C CG  . PHE A 1 129 ? 10.594  12.312  52.164  1.00 73.44  ? 127 PHE B CG  1 
ATOM   950  C CD1 . PHE A 1 129 ? 10.901  13.110  53.257  1.00 74.85  ? 127 PHE B CD1 1 
ATOM   951  C CD2 . PHE A 1 129 ? 9.546   12.684  51.336  1.00 73.21  ? 127 PHE B CD2 1 
ATOM   952  C CE1 . PHE A 1 129 ? 10.194  14.257  53.516  1.00 75.78  ? 127 PHE B CE1 1 
ATOM   953  C CE2 . PHE A 1 129 ? 8.829   13.843  51.589  1.00 78.00  ? 127 PHE B CE2 1 
ATOM   954  C CZ  . PHE A 1 129 ? 9.158   14.631  52.682  1.00 80.16  ? 127 PHE B CZ  1 
ATOM   955  N N   . PRO A 1 130 ? 13.797  8.972   52.776  1.00 73.29  ? 128 PRO B N   1 
ATOM   956  C CA  . PRO A 1 130 ? 14.585  7.773   52.486  1.00 73.09  ? 128 PRO B CA  1 
ATOM   957  C C   . PRO A 1 130 ? 13.755  6.628   51.907  1.00 73.58  ? 128 PRO B C   1 
ATOM   958  O O   . PRO A 1 130 ? 12.521  6.658   51.881  1.00 74.32  ? 128 PRO B O   1 
ATOM   959  C CB  . PRO A 1 130 ? 15.150  7.393   53.860  1.00 74.52  ? 128 PRO B CB  1 
ATOM   960  C CG  . PRO A 1 130 ? 14.201  8.043   54.894  1.00 75.94  ? 128 PRO B CG  1 
ATOM   961  C CD  . PRO A 1 130 ? 13.209  8.898   54.125  1.00 75.23  ? 128 PRO B CD  1 
ATOM   962  N N   . LEU A 1 131 ? 14.479  5.629   51.392  1.00 73.56  ? 129 LEU B N   1 
ATOM   963  C CA  . LEU A 1 131 ? 13.939  4.319   51.017  1.00 74.30  ? 129 LEU B CA  1 
ATOM   964  C C   . LEU A 1 131 ? 14.833  3.313   51.740  1.00 75.30  ? 129 LEU B C   1 
ATOM   965  O O   . LEU A 1 131 ? 15.919  2.992   51.242  1.00 75.58  ? 129 LEU B O   1 
ATOM   966  C CB  . LEU A 1 131 ? 13.975  4.097   49.511  1.00 72.76  ? 129 LEU B CB  1 
ATOM   967  C CG  . LEU A 1 131 ? 12.963  4.898   48.708  1.00 71.99  ? 129 LEU B CG  1 
ATOM   968  C CD1 . LEU A 1 131 ? 13.362  4.940   47.252  1.00 70.21  ? 129 LEU B CD1 1 
ATOM   969  C CD2 . LEU A 1 131 ? 11.567  4.356   48.892  1.00 73.42  ? 129 LEU B CD2 1 
ATOM   970  N N   . ALA A 1 132 ? 14.385  2.813   52.896  1.00 76.89  ? 130 ALA B N   1 
ATOM   971  C CA  . ALA A 1 132 ? 15.408  2.196   53.728  1.00 77.77  ? 130 ALA B CA  1 
ATOM   972  C C   . ALA A 1 132 ? 15.419  0.677   53.604  1.00 78.88  ? 130 ALA B C   1 
ATOM   973  O O   . ALA A 1 132 ? 14.357  0.054   53.523  1.00 79.95  ? 130 ALA B O   1 
ATOM   974  C CB  . ALA A 1 132 ? 15.183  2.571   55.191  1.00 79.39  ? 130 ALA B CB  1 
ATOM   975  N N   . PRO A 1 133 ? 16.598  0.054   53.646  1.00 78.83  ? 131 PRO B N   1 
ATOM   976  C CA  . PRO A 1 133 ? 16.682  -1.405  53.496  1.00 79.96  ? 131 PRO B CA  1 
ATOM   977  C C   . PRO A 1 133 ? 16.189  -2.139  54.735  1.00 90.14  ? 131 PRO B C   1 
ATOM   978  O O   . PRO A 1 133 ? 16.020  -1.576  55.820  1.00 88.72  ? 131 PRO B O   1 
ATOM   979  C CB  . PRO A 1 133 ? 18.177  -1.643  53.283  1.00 79.19  ? 131 PRO B CB  1 
ATOM   980  C CG  . PRO A 1 133 ? 18.808  -0.579  54.093  1.00 81.14  ? 131 PRO B CG  1 
ATOM   981  C CD  . PRO A 1 133 ? 17.930  0.646   53.849  1.00 81.11  ? 131 PRO B CD  1 
ATOM   982  N N   . SER A 1 134 ? 16.000  -3.448  54.557  1.00 98.58  ? 132 SER B N   1 
ATOM   983  C CA  . SER A 1 134 ? 15.415  -4.314  55.568  1.00 102.66 ? 132 SER B CA  1 
ATOM   984  C C   . SER A 1 134 ? 16.240  -5.588  55.695  1.00 111.12 ? 132 SER B C   1 
ATOM   985  O O   . SER A 1 134 ? 17.020  -5.937  54.804  1.00 112.18 ? 132 SER B O   1 
ATOM   986  C CB  . SER A 1 134 ? 13.956  -4.631  55.218  1.00 107.02 ? 132 SER B CB  1 
ATOM   987  O OG  . SER A 1 134 ? 13.852  -5.846  54.492  1.00 115.21 ? 132 SER B OG  1 
ATOM   988  N N   . SER A 1 135 ? 16.053  -6.284  56.826  1.00 112.61 ? 133 SER B N   1 
ATOM   989  C CA  . SER A 1 135 ? 16.765  -7.537  57.083  1.00 114.73 ? 133 SER B CA  1 
ATOM   990  C C   . SER A 1 135 ? 16.112  -8.743  56.409  1.00 122.93 ? 133 SER B C   1 
ATOM   991  O O   . SER A 1 135 ? 16.809  -9.713  56.079  1.00 125.54 ? 133 SER B O   1 
ATOM   992  C CB  . SER A 1 135 ? 16.873  -7.792  58.585  1.00 105.16 ? 133 SER B CB  1 
ATOM   993  O OG  . SER A 1 135 ? 18.180  -8.230  58.908  1.00 103.39 ? 133 SER B OG  1 
ATOM   994  N N   . LYS A 1 136 ? 14.791  -8.717  56.213  1.00 125.64 ? 134 LYS B N   1 
ATOM   995  C CA  . LYS A 1 136 ? 14.142  -9.780  55.451  1.00 127.88 ? 134 LYS B CA  1 
ATOM   996  C C   . LYS A 1 136 ? 14.651  -9.826  54.017  1.00 136.77 ? 134 LYS B C   1 
ATOM   997  O O   . LYS A 1 136 ? 14.731  -10.909 53.423  1.00 137.61 ? 134 LYS B O   1 
ATOM   998  C CB  . LYS A 1 136 ? 12.620  -9.593  55.482  1.00 123.34 ? 134 LYS B CB  1 
ATOM   999  C CG  . LYS A 1 136 ? 12.022  -8.783  54.320  1.00 125.73 ? 134 LYS B CG  1 
ATOM   1000 C CD  . LYS A 1 136 ? 11.631  -9.658  53.127  1.00 123.26 ? 134 LYS B CD  1 
ATOM   1001 C CE  . LYS A 1 136 ? 10.777  -8.896  52.133  1.00 112.71 ? 134 LYS B CE  1 
ATOM   1002 N NZ  . LYS A 1 136 ? 9.977   -9.830  51.297  1.00 95.10  ? 134 LYS B NZ  1 
ATOM   1003 N N   . SER A 1 137 ? 15.014  -8.669  53.452  1.00 168.25 ? 135 SER B N   1 
ATOM   1004 C CA  . SER A 1 137 ? 15.323  -8.554  52.029  1.00 167.00 ? 135 SER B CA  1 
ATOM   1005 C C   . SER A 1 137 ? 16.693  -9.121  51.680  1.00 165.88 ? 135 SER B C   1 
ATOM   1006 O O   . SER A 1 137 ? 17.245  -8.803  50.619  1.00 163.91 ? 135 SER B O   1 
ATOM   1007 C CB  . SER A 1 137 ? 15.235  -7.095  51.569  1.00 165.14 ? 135 SER B CB  1 
ATOM   1008 O OG  . SER A 1 137 ? 14.125  -6.898  50.706  1.00 163.47 ? 135 SER B OG  1 
ATOM   1009 N N   . THR A 1 138 ? 17.249  -9.954  52.559  1.00 145.63 ? 136 THR B N   1 
ATOM   1010 C CA  . THR A 1 138 ? 18.414  -10.759 52.204  1.00 140.25 ? 136 THR B CA  1 
ATOM   1011 C C   . THR A 1 138 ? 17.961  -11.779 51.155  1.00 143.00 ? 136 THR B C   1 
ATOM   1012 O O   . THR A 1 138 ? 17.254  -12.745 51.458  1.00 140.80 ? 136 THR B O   1 
ATOM   1013 C CB  . THR A 1 138 ? 19.046  -11.378 53.460  1.00 131.04 ? 136 THR B CB  1 
ATOM   1014 O OG1 . THR A 1 138 ? 20.358  -11.888 53.177  1.00 124.00 ? 136 THR B OG1 1 
ATOM   1015 C CG2 . THR A 1 138 ? 18.178  -12.454 54.134  1.00 127.31 ? 136 THR B CG2 1 
ATOM   1016 N N   . SER A 1 139 ? 18.285  -11.506 49.882  1.00 146.96 ? 137 SER B N   1 
ATOM   1017 C CA  . SER A 1 139 ? 18.094  -12.493 48.822  1.00 147.90 ? 137 SER B CA  1 
ATOM   1018 C C   . SER A 1 139 ? 19.089  -13.626 49.053  1.00 152.41 ? 137 SER B C   1 
ATOM   1019 O O   . SER A 1 139 ? 19.027  -14.308 50.083  1.00 154.80 ? 137 SER B O   1 
ATOM   1020 C CB  . SER A 1 139 ? 18.266  -11.863 47.432  1.00 139.30 ? 137 SER B CB  1 
ATOM   1021 O OG  . SER A 1 139 ? 17.965  -10.478 47.440  1.00 130.87 ? 137 SER B OG  1 
ATOM   1022 N N   . GLY A 1 140 ? 20.017  -13.844 48.123  1.00 145.29 ? 138 GLY B N   1 
ATOM   1023 C CA  . GLY A 1 140 ? 21.223  -14.568 48.493  1.00 145.84 ? 138 GLY B CA  1 
ATOM   1024 C C   . GLY A 1 140 ? 22.047  -13.771 49.487  1.00 140.90 ? 138 GLY B C   1 
ATOM   1025 O O   . GLY A 1 140 ? 22.633  -14.324 50.423  1.00 141.48 ? 138 GLY B O   1 
ATOM   1026 N N   . GLY A 1 141 ? 22.063  -12.454 49.313  1.00 129.09 ? 139 GLY B N   1 
ATOM   1027 C CA  . GLY A 1 141 ? 22.751  -11.545 50.195  1.00 116.71 ? 139 GLY B CA  1 
ATOM   1028 C C   . GLY A 1 141 ? 22.836  -10.191 49.531  1.00 105.37 ? 139 GLY B C   1 
ATOM   1029 O O   . GLY A 1 141 ? 23.895  -9.559  49.546  1.00 99.62  ? 139 GLY B O   1 
ATOM   1030 N N   . THR A 1 142 ? 21.727  -9.742  48.936  1.00 109.53 ? 140 THR B N   1 
ATOM   1031 C CA  . THR A 1 142 ? 21.666  -8.465  48.234  1.00 98.89  ? 140 THR B CA  1 
ATOM   1032 C C   . THR A 1 142 ? 20.474  -7.653  48.723  1.00 99.32  ? 140 THR B C   1 
ATOM   1033 O O   . THR A 1 142 ? 19.369  -8.185  48.879  1.00 107.08 ? 140 THR B O   1 
ATOM   1034 C CB  . THR A 1 142 ? 21.574  -8.669  46.717  1.00 97.99  ? 140 THR B CB  1 
ATOM   1035 O OG1 . THR A 1 142 ? 22.877  -8.976  46.215  1.00 97.05  ? 140 THR B OG1 1 
ATOM   1036 C CG2 . THR A 1 142 ? 21.050  -7.413  46.016  1.00 84.76  ? 140 THR B CG2 1 
ATOM   1037 N N   . ALA A 1 143 ? 20.710  -6.358  48.955  1.00 90.44  ? 141 ALA B N   1 
ATOM   1038 C CA  . ALA A 1 143 ? 19.712  -5.452  49.498  1.00 86.37  ? 141 ALA B CA  1 
ATOM   1039 C C   . ALA A 1 143 ? 19.619  -4.203  48.639  1.00 81.02  ? 141 ALA B C   1 
ATOM   1040 O O   . ALA A 1 143 ? 20.525  -3.890  47.865  1.00 78.49  ? 141 ALA B O   1 
ATOM   1041 C CB  . ALA A 1 143 ? 20.046  -5.051  50.931  1.00 85.55  ? 141 ALA B CB  1 
ATOM   1042 N N   . ALA A 1 144 ? 18.525  -3.462  48.823  1.00 78.88  ? 142 ALA B N   1 
ATOM   1043 C CA  . ALA A 1 144 ? 18.228  -2.278  48.023  1.00 73.89  ? 142 ALA B CA  1 
ATOM   1044 C C   . ALA A 1 144 ? 17.760  -1.130  48.909  1.00 76.28  ? 142 ALA B C   1 
ATOM   1045 O O   . ALA A 1 144 ? 16.738  -1.241  49.594  1.00 75.18  ? 142 ALA B O   1 
ATOM   1046 C CB  . ALA A 1 144 ? 17.166  -2.587  46.974  1.00 73.33  ? 142 ALA B CB  1 
ATOM   1047 N N   . LEU A 1 145 ? 18.491  -0.022  48.873  1.00 75.60  ? 143 LEU B N   1 
ATOM   1048 C CA  . LEU A 1 145 ? 18.101  1.211   49.529  1.00 72.73  ? 143 LEU B CA  1 
ATOM   1049 C C   . LEU A 1 145 ? 18.078  2.335   48.501  1.00 71.17  ? 143 LEU B C   1 
ATOM   1050 O O   . LEU A 1 145 ? 18.745  2.274   47.462  1.00 69.96  ? 143 LEU B O   1 
ATOM   1051 C CB  . LEU A 1 145 ? 19.058  1.571   50.657  1.00 73.26  ? 143 LEU B CB  1 
ATOM   1052 C CG  . LEU A 1 145 ? 20.501  1.654   50.186  1.00 75.29  ? 143 LEU B CG  1 
ATOM   1053 C CD1 . LEU A 1 145 ? 21.106  2.851   50.841  1.00 82.45  ? 143 LEU B CD1 1 
ATOM   1054 C CD2 . LEU A 1 145 ? 21.269  0.418   50.612  1.00 76.56  ? 143 LEU B CD2 1 
ATOM   1055 N N   . GLY A 1 146 ? 17.303  3.373   48.794  1.00 71.67  ? 144 GLY B N   1 
ATOM   1056 C CA  . GLY A 1 146 ? 17.159  4.442   47.830  1.00 69.78  ? 144 GLY B CA  1 
ATOM   1057 C C   . GLY A 1 146 ? 16.760  5.729   48.509  1.00 68.82  ? 144 GLY B C   1 
ATOM   1058 O O   . GLY A 1 146 ? 16.386  5.745   49.680  1.00 70.21  ? 144 GLY B O   1 
ATOM   1059 N N   . CYS A 1 147 ? 16.865  6.815   47.757  1.00 68.04  ? 145 CYS B N   1 
ATOM   1060 C CA  . CYS A 1 147 ? 16.377  8.123   48.172  1.00 69.86  ? 145 CYS B CA  1 
ATOM   1061 C C   . CYS A 1 147 ? 15.101  8.444   47.410  1.00 67.19  ? 145 CYS B C   1 
ATOM   1062 O O   . CYS A 1 147 ? 14.972  8.109   46.234  1.00 66.28  ? 145 CYS B O   1 
ATOM   1063 C CB  . CYS A 1 147 ? 17.416  9.220   47.890  1.00 67.68  ? 145 CYS B CB  1 
ATOM   1064 S SG  . CYS A 1 147 ? 18.608  9.536   49.226  1.00 69.87  ? 145 CYS B SG  1 
ATOM   1065 N N   . LEU A 1 148 ? 14.170  9.119   48.054  1.00 68.04  ? 146 LEU B N   1 
ATOM   1066 C CA  . LEU A 1 148 ? 12.993  9.606   47.350  1.00 67.85  ? 146 LEU B CA  1 
ATOM   1067 C C   . LEU A 1 148 ? 13.082  11.132  47.302  1.00 68.00  ? 146 LEU B C   1 
ATOM   1068 O O   . LEU A 1 148 ? 13.024  11.794  48.342  1.00 68.04  ? 146 LEU B O   1 
ATOM   1069 C CB  . LEU A 1 148 ? 11.723  9.101   48.025  1.00 69.51  ? 146 LEU B CB  1 
ATOM   1070 C CG  . LEU A 1 148 ? 10.417  9.288   47.259  1.00 69.55  ? 146 LEU B CG  1 
ATOM   1071 C CD1 . LEU A 1 148 ? 9.861   10.661  47.376  1.00 69.55  ? 146 LEU B CD1 1 
ATOM   1072 C CD2 . LEU A 1 148 ? 10.704  9.009   45.813  1.00 68.05  ? 146 LEU B CD2 1 
ATOM   1073 N N   . VAL A 1 149 ? 13.273  11.685  46.102  1.00 70.08  ? 147 VAL B N   1 
ATOM   1074 C CA  . VAL A 1 149 ? 13.423  13.127  45.907  1.00 68.69  ? 147 VAL B CA  1 
ATOM   1075 C C   . VAL A 1 149 ? 12.074  13.691  45.478  1.00 70.76  ? 147 VAL B C   1 
ATOM   1076 O O   . VAL A 1 149 ? 11.675  13.527  44.325  1.00 69.03  ? 147 VAL B O   1 
ATOM   1077 C CB  . VAL A 1 149 ? 14.509  13.443  44.875  1.00 63.63  ? 147 VAL B CB  1 
ATOM   1078 C CG1 . VAL A 1 149 ? 14.648  14.932  44.713  1.00 63.64  ? 147 VAL B CG1 1 
ATOM   1079 C CG2 . VAL A 1 149 ? 15.825  12.860  45.323  1.00 63.45  ? 147 VAL B CG2 1 
ATOM   1080 N N   . LYS A 1 150 ? 11.376  14.375  46.397  1.00 71.21  ? 148 LYS B N   1 
ATOM   1081 C CA  . LYS A 1 150 ? 9.973   14.718  46.194  1.00 72.02  ? 148 LYS B CA  1 
ATOM   1082 C C   . LYS A 1 150 ? 9.701   16.217  46.250  1.00 76.14  ? 148 LYS B C   1 
ATOM   1083 O O   . LYS A 1 150 ? 10.323  16.965  47.014  1.00 76.83  ? 148 LYS B O   1 
ATOM   1084 C CB  . LYS A 1 150 ? 9.073   14.022  47.228  1.00 70.74  ? 148 LYS B CB  1 
ATOM   1085 C CG  . LYS A 1 150 ? 7.594   13.949  46.825  1.00 70.62  ? 148 LYS B CG  1 
ATOM   1086 C CD  . LYS A 1 150 ? 6.780   13.191  47.859  1.00 71.68  ? 148 LYS B CD  1 
ATOM   1087 C CE  . LYS A 1 150 ? 5.333   12.959  47.422  1.00 72.52  ? 148 LYS B CE  1 
ATOM   1088 N NZ  . LYS A 1 150 ? 4.626   14.196  47.002  1.00 75.54  ? 148 LYS B NZ  1 
ATOM   1089 N N   . ASP A 1 151 ? 8.729   16.628  45.430  1.00 74.17  ? 149 ASP B N   1 
ATOM   1090 C CA  . ASP A 1 151 ? 8.120   17.958  45.451  1.00 75.23  ? 149 ASP B CA  1 
ATOM   1091 C C   . ASP A 1 151 ? 9.165   19.059  45.232  1.00 78.15  ? 149 ASP B C   1 
ATOM   1092 O O   . ASP A 1 151 ? 9.440   19.896  46.093  1.00 80.96  ? 149 ASP B O   1 
ATOM   1093 C CB  . ASP A 1 151 ? 7.340   18.145  46.749  1.00 73.45  ? 149 ASP B CB  1 
ATOM   1094 C CG  . ASP A 1 151 ? 5.904   17.634  46.644  1.00 77.44  ? 149 ASP B CG  1 
ATOM   1095 O OD1 . ASP A 1 151 ? 5.602   16.847  45.717  1.00 74.43  ? 149 ASP B OD1 1 
ATOM   1096 O OD2 . ASP A 1 151 ? 5.091   17.963  47.544  1.00 83.72  ? 149 ASP B OD2 1 
ATOM   1097 N N   . TYR A 1 152 ? 9.730   19.033  44.031  1.00 76.71  ? 150 TYR B N   1 
ATOM   1098 C CA  . TYR A 1 152 ? 10.616  20.081  43.561  1.00 78.95  ? 150 TYR B CA  1 
ATOM   1099 C C   . TYR A 1 152 ? 10.102  20.603  42.231  1.00 79.58  ? 150 TYR B C   1 
ATOM   1100 O O   . TYR A 1 152 ? 9.382   19.907  41.508  1.00 77.49  ? 150 TYR B O   1 
ATOM   1101 C CB  . TYR A 1 152 ? 12.061  19.585  43.428  1.00 76.55  ? 150 TYR B CB  1 
ATOM   1102 C CG  . TYR A 1 152 ? 12.290  18.571  42.337  1.00 73.47  ? 150 TYR B CG  1 
ATOM   1103 C CD1 . TYR A 1 152 ? 12.629  18.958  41.061  1.00 73.07  ? 150 TYR B CD1 1 
ATOM   1104 C CD2 . TYR A 1 152 ? 12.175  17.218  42.598  1.00 72.59  ? 150 TYR B CD2 1 
ATOM   1105 C CE1 . TYR A 1 152 ? 12.855  18.021  40.069  1.00 73.69  ? 150 TYR B CE1 1 
ATOM   1106 C CE2 . TYR A 1 152 ? 12.390  16.283  41.621  1.00 72.03  ? 150 TYR B CE2 1 
ATOM   1107 C CZ  . TYR A 1 152 ? 12.730  16.685  40.358  1.00 71.07  ? 150 TYR B CZ  1 
ATOM   1108 O OH  . TYR A 1 152 ? 12.937  15.744  39.380  1.00 69.51  ? 150 TYR B OH  1 
ATOM   1109 N N   . PHE A 1 153 ? 10.469  21.852  41.931  1.00 82.75  ? 151 PHE B N   1 
ATOM   1110 C CA  . PHE A 1 153 ? 10.100  22.540  40.706  1.00 82.28  ? 151 PHE B CA  1 
ATOM   1111 C C   . PHE A 1 153 ? 11.151  23.596  40.424  1.00 83.65  ? 151 PHE B C   1 
ATOM   1112 O O   . PHE A 1 153 ? 11.634  24.238  41.367  1.00 81.45  ? 151 PHE B O   1 
ATOM   1113 C CB  . PHE A 1 153 ? 8.737   23.215  40.805  1.00 81.85  ? 151 PHE B CB  1 
ATOM   1114 C CG  . PHE A 1 153 ? 8.105   23.498  39.481  1.00 81.27  ? 151 PHE B CG  1 
ATOM   1115 C CD1 . PHE A 1 153 ? 7.281   22.562  38.877  1.00 79.95  ? 151 PHE B CD1 1 
ATOM   1116 C CD2 . PHE A 1 153 ? 8.351   24.693  38.828  1.00 79.89  ? 151 PHE B CD2 1 
ATOM   1117 C CE1 . PHE A 1 153 ? 6.687   22.824  37.666  1.00 77.64  ? 151 PHE B CE1 1 
ATOM   1118 C CE2 . PHE A 1 153 ? 7.769   24.962  37.616  1.00 77.50  ? 151 PHE B CE2 1 
ATOM   1119 C CZ  . PHE A 1 153 ? 6.934   24.022  37.032  1.00 78.92  ? 151 PHE B CZ  1 
ATOM   1120 N N   . PRO A 1 154 ? 11.554  23.777  39.161  1.00 94.39  ? 152 PRO B N   1 
ATOM   1121 C CA  . PRO A 1 154 ? 11.336  22.900  37.989  1.00 93.14  ? 152 PRO B CA  1 
ATOM   1122 C C   . PRO A 1 154 ? 12.498  21.939  37.758  1.00 91.37  ? 152 PRO B C   1 
ATOM   1123 O O   . PRO A 1 154 ? 13.497  22.026  38.459  1.00 91.95  ? 152 PRO B O   1 
ATOM   1124 C CB  . PRO A 1 154 ? 11.233  23.903  36.842  1.00 92.78  ? 152 PRO B CB  1 
ATOM   1125 C CG  . PRO A 1 154 ? 12.239  24.963  37.247  1.00 92.71  ? 152 PRO B CG  1 
ATOM   1126 C CD  . PRO A 1 154 ? 12.086  25.092  38.750  1.00 93.43  ? 152 PRO B CD  1 
ATOM   1127 N N   . GLU A 1 155 ? 12.416  21.036  36.779  1.00 78.18  ? 153 GLU B N   1 
ATOM   1128 C CA  . GLU A 1 155 ? 13.549  20.184  36.455  1.00 71.76  ? 153 GLU B CA  1 
ATOM   1129 C C   . GLU A 1 155 ? 14.782  21.046  36.195  1.00 69.54  ? 153 GLU B C   1 
ATOM   1130 O O   . GLU A 1 155 ? 14.666  22.236  35.895  1.00 74.26  ? 153 GLU B O   1 
ATOM   1131 C CB  . GLU A 1 155 ? 13.238  19.325  35.236  1.00 64.85  ? 153 GLU B CB  1 
ATOM   1132 C CG  . GLU A 1 155 ? 12.438  18.106  35.588  1.00 67.58  ? 153 GLU B CG  1 
ATOM   1133 C CD  . GLU A 1 155 ? 13.302  16.928  35.958  1.00 67.02  ? 153 GLU B CD  1 
ATOM   1134 O OE1 . GLU A 1 155 ? 13.894  16.954  37.058  1.00 68.19  ? 153 GLU B OE1 1 
ATOM   1135 O OE2 . GLU A 1 155 ? 13.381  15.963  35.174  1.00 68.10  ? 153 GLU B OE2 1 
ATOM   1136 N N   . PRO A 1 156 ? 15.974  20.479  36.324  1.00 65.45  ? 154 PRO B N   1 
ATOM   1137 C CA  . PRO A 1 156 ? 16.314  19.100  36.633  1.00 67.92  ? 154 PRO B CA  1 
ATOM   1138 C C   . PRO A 1 156 ? 16.842  18.897  38.045  1.00 66.45  ? 154 PRO B C   1 
ATOM   1139 O O   . PRO A 1 156 ? 17.318  19.824  38.694  1.00 68.20  ? 154 PRO B O   1 
ATOM   1140 C CB  . PRO A 1 156 ? 17.425  18.819  35.625  1.00 57.20  ? 154 PRO B CB  1 
ATOM   1141 C CG  . PRO A 1 156 ? 18.147  20.174  35.521  1.00 58.82  ? 154 PRO B CG  1 
ATOM   1142 C CD  . PRO A 1 156 ? 17.197  21.240  36.052  1.00 60.03  ? 154 PRO B CD  1 
ATOM   1143 N N   . VAL A 1 157 ? 16.824  17.666  38.531  1.00 65.05  ? 155 VAL B N   1 
ATOM   1144 C CA  . VAL A 1 157 ? 17.586  17.311  39.717  1.00 67.95  ? 155 VAL B CA  1 
ATOM   1145 C C   . VAL A 1 157 ? 18.643  16.300  39.293  1.00 67.80  ? 155 VAL B C   1 
ATOM   1146 O O   . VAL A 1 157 ? 18.459  15.565  38.319  1.00 64.73  ? 155 VAL B O   1 
ATOM   1147 C CB  . VAL A 1 157 ? 16.677  16.757  40.840  1.00 68.38  ? 155 VAL B CB  1 
ATOM   1148 C CG1 . VAL A 1 157 ? 15.894  15.536  40.367  1.00 67.77  ? 155 VAL B CG1 1 
ATOM   1149 C CG2 . VAL A 1 157 ? 17.485  16.431  42.056  1.00 70.61  ? 155 VAL B CG2 1 
ATOM   1150 N N   . THR A 1 158 ? 19.774  16.300  40.001  1.00 68.36  ? 156 THR B N   1 
ATOM   1151 C CA  . THR A 1 158 ? 20.841  15.317  39.830  1.00 67.88  ? 156 THR B CA  1 
ATOM   1152 C C   . THR A 1 158 ? 21.046  14.566  41.142  1.00 69.54  ? 156 THR B C   1 
ATOM   1153 O O   . THR A 1 158 ? 21.001  15.171  42.217  1.00 70.55  ? 156 THR B O   1 
ATOM   1154 C CB  . THR A 1 158 ? 22.156  15.992  39.426  1.00 67.40  ? 156 THR B CB  1 
ATOM   1155 O OG1 . THR A 1 158 ? 23.121  15.813  40.473  1.00 69.06  ? 156 THR B OG1 1 
ATOM   1156 C CG2 . THR A 1 158 ? 21.942  17.481  39.247  1.00 70.43  ? 156 THR B CG2 1 
ATOM   1157 N N   . VAL A 1 159 ? 21.285  13.255  41.067  1.00 69.64  ? 157 VAL B N   1 
ATOM   1158 C CA  . VAL A 1 159 ? 21.435  12.419  42.261  1.00 68.85  ? 157 VAL B CA  1 
ATOM   1159 C C   . VAL A 1 159 ? 22.705  11.587  42.152  1.00 69.59  ? 157 VAL B C   1 
ATOM   1160 O O   . VAL A 1 159 ? 22.863  10.808  41.206  1.00 69.82  ? 157 VAL B O   1 
ATOM   1161 C CB  . VAL A 1 159 ? 20.222  11.504  42.484  1.00 68.44  ? 157 VAL B CB  1 
ATOM   1162 C CG1 . VAL A 1 159 ? 20.453  10.612  43.685  1.00 68.88  ? 157 VAL B CG1 1 
ATOM   1163 C CG2 . VAL A 1 159 ? 18.976  12.339  42.705  1.00 69.68  ? 157 VAL B CG2 1 
ATOM   1164 N N   . SER A 1 160 ? 23.589  11.728  43.136  1.00 71.48  ? 158 SER B N   1 
ATOM   1165 C CA  . SER A 1 160 ? 24.833  10.975  43.219  1.00 70.96  ? 158 SER B CA  1 
ATOM   1166 C C   . SER A 1 160 ? 24.812  10.090  44.454  1.00 76.48  ? 158 SER B C   1 
ATOM   1167 O O   . SER A 1 160 ? 24.343  10.508  45.525  1.00 76.03  ? 158 SER B O   1 
ATOM   1168 C CB  . SER A 1 160 ? 26.043  11.908  43.284  1.00 75.38  ? 158 SER B CB  1 
ATOM   1169 O OG  . SER A 1 160 ? 27.085  11.352  44.064  1.00 77.85  ? 158 SER B OG  1 
ATOM   1170 N N   . TRP A 1 161 ? 25.332  8.873   44.312  1.00 78.68  ? 159 TRP B N   1 
ATOM   1171 C CA  . TRP A 1 161 ? 25.397  7.939   45.427  1.00 77.84  ? 159 TRP B CA  1 
ATOM   1172 C C   . TRP A 1 161 ? 26.818  7.913   45.977  1.00 82.31  ? 159 TRP B C   1 
ATOM   1173 O O   . TRP A 1 161 ? 27.772  7.622   45.239  1.00 82.00  ? 159 TRP B O   1 
ATOM   1174 C CB  . TRP A 1 161 ? 24.924  6.546   45.011  1.00 72.04  ? 159 TRP B CB  1 
ATOM   1175 C CG  . TRP A 1 161 ? 23.432  6.469   45.027  1.00 68.67  ? 159 TRP B CG  1 
ATOM   1176 C CD1 . TRP A 1 161 ? 22.599  6.536   43.951  1.00 68.07  ? 159 TRP B CD1 1 
ATOM   1177 C CD2 . TRP A 1 161 ? 22.584  6.369   46.185  1.00 67.59  ? 159 TRP B CD2 1 
ATOM   1178 N NE1 . TRP A 1 161 ? 21.287  6.455   44.362  1.00 66.88  ? 159 TRP B NE1 1 
ATOM   1179 C CE2 . TRP A 1 161 ? 21.252  6.358   45.728  1.00 64.03  ? 159 TRP B CE2 1 
ATOM   1180 C CE3 . TRP A 1 161 ? 22.825  6.278   47.560  1.00 67.72  ? 159 TRP B CE3 1 
ATOM   1181 C CZ2 . TRP A 1 161 ? 20.165  6.266   46.593  1.00 65.23  ? 159 TRP B CZ2 1 
ATOM   1182 C CZ3 . TRP A 1 161 ? 21.745  6.180   48.419  1.00 67.13  ? 159 TRP B CZ3 1 
ATOM   1183 C CH2 . TRP A 1 161 ? 20.429  6.174   47.931  1.00 67.24  ? 159 TRP B CH2 1 
ATOM   1184 N N   . ASN A 1 162 ? 26.945  8.241   47.270  1.00 79.84  ? 160 ASN B N   1 
ATOM   1185 C CA  . ASN A 1 162 ? 28.217  8.238   47.994  1.00 80.72  ? 160 ASN B CA  1 
ATOM   1186 C C   . ASN A 1 162 ? 29.267  9.066   47.259  1.00 82.97  ? 160 ASN B C   1 
ATOM   1187 O O   . ASN A 1 162 ? 30.409  8.643   47.065  1.00 84.51  ? 160 ASN B O   1 
ATOM   1188 C CB  . ASN A 1 162 ? 28.706  6.807   48.251  1.00 81.30  ? 160 ASN B CB  1 
ATOM   1189 C CG  . ASN A 1 162 ? 27.963  6.127   49.404  1.00 84.80  ? 160 ASN B CG  1 
ATOM   1190 O OD1 . ASN A 1 162 ? 26.930  6.625   49.858  1.00 84.02  ? 160 ASN B OD1 1 
ATOM   1191 N ND2 . ASN A 1 162 ? 28.475  4.973   49.865  1.00 84.08  ? 160 ASN B ND2 1 
ATOM   1192 N N   . SER A 1 163 ? 28.859  10.265  46.837  1.00 83.12  ? 161 SER B N   1 
ATOM   1193 C CA  . SER A 1 163 ? 29.778  11.230  46.234  1.00 85.93  ? 161 SER B CA  1 
ATOM   1194 C C   . SER A 1 163 ? 30.451  10.665  44.984  1.00 90.74  ? 161 SER B C   1 
ATOM   1195 O O   . SER A 1 163 ? 31.636  10.888  44.732  1.00 91.22  ? 161 SER B O   1 
ATOM   1196 C CB  . SER A 1 163 ? 30.805  11.701  47.262  1.00 85.84  ? 161 SER B CB  1 
ATOM   1197 O OG  . SER A 1 163 ? 31.782  10.696  47.476  1.00 90.29  ? 161 SER B OG  1 
ATOM   1198 N N   . GLY A 1 164 ? 29.681  9.936   44.179  1.00 105.92 ? 162 GLY B N   1 
ATOM   1199 C CA  . GLY A 1 164 ? 30.199  9.352   42.963  1.00 105.21 ? 162 GLY B CA  1 
ATOM   1200 C C   . GLY A 1 164 ? 30.983  8.075   43.148  1.00 105.76 ? 162 GLY B C   1 
ATOM   1201 O O   . GLY A 1 164 ? 31.392  7.465   42.149  1.00 105.64 ? 162 GLY B O   1 
ATOM   1202 N N   . ALA A 1 165 ? 31.201  7.640   44.385  1.00 89.61  ? 163 ALA B N   1 
ATOM   1203 C CA  . ALA A 1 165 ? 31.956  6.422   44.600  1.00 87.06  ? 163 ALA B CA  1 
ATOM   1204 C C   . ALA A 1 165 ? 31.103  5.167   44.507  1.00 84.99  ? 163 ALA B C   1 
ATOM   1205 O O   . ALA A 1 165 ? 31.663  4.068   44.544  1.00 86.25  ? 163 ALA B O   1 
ATOM   1206 C CB  . ALA A 1 165 ? 32.652  6.470   45.958  1.00 88.95  ? 163 ALA B CB  1 
ATOM   1207 N N   . LEU A 1 166 ? 29.780  5.285   44.395  1.00 82.67  ? 164 LEU B N   1 
ATOM   1208 C CA  . LEU A 1 166 ? 28.899  4.115   44.269  1.00 78.44  ? 164 LEU B CA  1 
ATOM   1209 C C   . LEU A 1 166 ? 28.187  4.145   42.918  1.00 76.06  ? 164 LEU B C   1 
ATOM   1210 O O   . LEU A 1 166 ? 27.072  4.662   42.793  1.00 72.73  ? 164 LEU B O   1 
ATOM   1211 C CB  . LEU A 1 166 ? 27.895  4.038   45.412  1.00 76.11  ? 164 LEU B CB  1 
ATOM   1212 C CG  . LEU A 1 166 ? 27.001  2.797   45.311  1.00 71.15  ? 164 LEU B CG  1 
ATOM   1213 C CD1 . LEU A 1 166 ? 27.853  1.555   45.248  1.00 74.92  ? 164 LEU B CD1 1 
ATOM   1214 C CD2 . LEU A 1 166 ? 26.016  2.716   46.467  1.00 68.26  ? 164 LEU B CD2 1 
ATOM   1215 N N   . THR A 1 167 ? 28.818  3.538   41.915  1.00 75.04  ? 165 THR B N   1 
ATOM   1216 C CA  . THR A 1 167 ? 28.316  3.575   40.553  1.00 67.84  ? 165 THR B CA  1 
ATOM   1217 C C   . THR A 1 167 ? 27.711  2.254   40.090  1.00 65.32  ? 165 THR B C   1 
ATOM   1218 O O   . THR A 1 167 ? 27.243  2.176   38.956  1.00 70.50  ? 165 THR B O   1 
ATOM   1219 C CB  . THR A 1 167 ? 29.444  3.994   39.603  1.00 67.77  ? 165 THR B CB  1 
ATOM   1220 O OG1 . THR A 1 167 ? 30.544  3.079   39.728  1.00 67.27  ? 165 THR B OG1 1 
ATOM   1221 C CG2 . THR A 1 167 ? 29.927  5.375   39.965  1.00 71.38  ? 165 THR B CG2 1 
ATOM   1222 N N   . SER A 1 168 ? 27.698  1.213   40.908  1.00 65.70  ? 166 SER B N   1 
ATOM   1223 C CA  . SER A 1 168 ? 27.154  -0.061  40.454  1.00 65.70  ? 166 SER B CA  1 
ATOM   1224 C C   . SER A 1 168 ? 25.817  -0.366  41.108  1.00 64.00  ? 166 SER B C   1 
ATOM   1225 O O   . SER A 1 168 ? 25.552  0.029   42.246  1.00 67.16  ? 166 SER B O   1 
ATOM   1226 C CB  . SER A 1 168 ? 28.116  -1.226  40.706  1.00 63.65  ? 166 SER B CB  1 
ATOM   1227 O OG  . SER A 1 168 ? 29.371  -0.988  40.095  1.00 66.05  ? 166 SER B OG  1 
ATOM   1228 N N   . GLY A 1 169 ? 24.981  -1.086  40.364  1.00 63.50  ? 167 GLY B N   1 
ATOM   1229 C CA  . GLY A 1 169 ? 23.662  -1.480  40.817  1.00 64.40  ? 167 GLY B CA  1 
ATOM   1230 C C   . GLY A 1 169 ? 22.672  -0.363  41.072  1.00 63.93  ? 167 GLY B C   1 
ATOM   1231 O O   . GLY A 1 169 ? 21.638  -0.627  41.686  1.00 64.91  ? 167 GLY B O   1 
ATOM   1232 N N   . VAL A 1 170 ? 22.927  0.870   40.592  1.00 63.87  ? 168 VAL B N   1 
ATOM   1233 C CA  . VAL A 1 170 ? 22.118  2.046   40.921  1.00 62.37  ? 168 VAL B CA  1 
ATOM   1234 C C   . VAL A 1 170 ? 21.256  2.437   39.723  1.00 61.71  ? 168 VAL B C   1 
ATOM   1235 O O   . VAL A 1 170 ? 21.716  2.391   38.578  1.00 62.42  ? 168 VAL B O   1 
ATOM   1236 C CB  . VAL A 1 170 ? 23.027  3.217   41.360  1.00 63.03  ? 168 VAL B CB  1 
ATOM   1237 C CG1 . VAL A 1 170 ? 24.411  3.092   40.711  1.00 66.08  ? 168 VAL B CG1 1 
ATOM   1238 C CG2 . VAL A 1 170 ? 22.398  4.563   41.040  1.00 60.72  ? 168 VAL B CG2 1 
ATOM   1239 N N   . HIS A 1 171 ? 20.003  2.827   39.983  1.00 61.51  ? 169 HIS B N   1 
ATOM   1240 C CA  . HIS A 1 171 ? 19.070  3.276   38.946  1.00 60.71  ? 169 HIS B CA  1 
ATOM   1241 C C   . HIS A 1 171 ? 18.343  4.530   39.427  1.00 60.64  ? 169 HIS B C   1 
ATOM   1242 O O   . HIS A 1 171 ? 17.418  4.446   40.244  1.00 61.68  ? 169 HIS B O   1 
ATOM   1243 C CB  . HIS A 1 171 ? 18.055  2.191   38.585  1.00 61.42  ? 169 HIS B CB  1 
ATOM   1244 C CG  . HIS A 1 171 ? 18.670  0.889   38.181  1.00 62.75  ? 169 HIS B CG  1 
ATOM   1245 N ND1 . HIS A 1 171 ? 18.242  -0.322  38.688  1.00 63.15  ? 169 HIS B ND1 1 
ATOM   1246 C CD2 . HIS A 1 171 ? 19.676  0.605   37.321  1.00 61.25  ? 169 HIS B CD2 1 
ATOM   1247 C CE1 . HIS A 1 171 ? 18.971  -1.295  38.172  1.00 63.22  ? 169 HIS B CE1 1 
ATOM   1248 N NE2 . HIS A 1 171 ? 19.847  -0.759  37.337  1.00 68.31  ? 169 HIS B NE2 1 
ATOM   1249 N N   . THR A 1 172 ? 18.748  5.687   38.898  1.00 62.44  ? 170 THR B N   1 
ATOM   1250 C CA  . THR A 1 172 ? 18.010  6.932   39.087  1.00 59.41  ? 170 THR B CA  1 
ATOM   1251 C C   . THR A 1 172 ? 16.902  6.997   38.058  1.00 59.00  ? 170 THR B C   1 
ATOM   1252 O O   . THR A 1 172 ? 17.130  6.700   36.890  1.00 61.98  ? 170 THR B O   1 
ATOM   1253 C CB  . THR A 1 172 ? 18.904  8.145   38.880  1.00 58.45  ? 170 THR B CB  1 
ATOM   1254 O OG1 . THR A 1 172 ? 20.217  7.886   39.384  1.00 58.50  ? 170 THR B OG1 1 
ATOM   1255 C CG2 . THR A 1 172 ? 18.317  9.309   39.644  1.00 60.32  ? 170 THR B CG2 1 
ATOM   1256 N N   . PHE A 1 173 ? 15.739  7.410   38.466  1.00 59.63  ? 171 PHE B N   1 
ATOM   1257 C CA  . PHE A 1 173 ? 14.577  7.224   37.614  1.00 59.59  ? 171 PHE B CA  1 
ATOM   1258 C C   . PHE A 1 173 ? 14.181  8.512   36.899  1.00 61.01  ? 171 PHE B C   1 
ATOM   1259 O O   . PHE A 1 173 ? 14.513  9.613   37.339  1.00 61.23  ? 171 PHE B O   1 
ATOM   1260 C CB  . PHE A 1 173 ? 13.398  6.713   38.440  1.00 60.99  ? 171 PHE B CB  1 
ATOM   1261 C CG  . PHE A 1 173 ? 13.343  5.211   38.551  1.00 64.06  ? 171 PHE B CG  1 
ATOM   1262 C CD1 . PHE A 1 173 ? 13.834  4.548   39.686  1.00 63.80  ? 171 PHE B CD1 1 
ATOM   1263 C CD2 . PHE A 1 173 ? 12.831  4.450   37.501  1.00 63.25  ? 171 PHE B CD2 1 
ATOM   1264 C CE1 . PHE A 1 173 ? 13.781  3.149   39.775  1.00 63.66  ? 171 PHE B CE1 1 
ATOM   1265 C CE2 . PHE A 1 173 ? 12.774  3.053   37.584  1.00 63.95  ? 171 PHE B CE2 1 
ATOM   1266 C CZ  . PHE A 1 173 ? 13.252  2.399   38.719  1.00 63.50  ? 171 PHE B CZ  1 
ATOM   1267 N N   . PRO A 1 174 ? 13.510  8.417   35.748  1.00 65.80  ? 172 PRO B N   1 
ATOM   1268 C CA  . PRO A 1 174 ? 12.901  9.617   35.169  1.00 61.67  ? 172 PRO B CA  1 
ATOM   1269 C C   . PRO A 1 174 ? 11.955  10.245  36.174  1.00 60.49  ? 172 PRO B C   1 
ATOM   1270 O O   . PRO A 1 174 ? 11.193  9.546   36.842  1.00 62.73  ? 172 PRO B O   1 
ATOM   1271 C CB  . PRO A 1 174 ? 12.154  9.069   33.952  1.00 57.69  ? 172 PRO B CB  1 
ATOM   1272 C CG  . PRO A 1 174 ? 12.994  7.891   33.568  1.00 57.67  ? 172 PRO B CG  1 
ATOM   1273 C CD  . PRO A 1 174 ? 13.347  7.253   34.853  1.00 61.34  ? 172 PRO B CD  1 
ATOM   1274 N N   . ALA A 1 175 ? 12.032  11.568  36.304  1.00 61.54  ? 173 ALA B N   1 
ATOM   1275 C CA  . ALA A 1 175 ? 11.094  12.288  37.159  1.00 62.34  ? 173 ALA B CA  1 
ATOM   1276 C C   . ALA A 1 175 ? 9.692   12.211  36.574  1.00 62.67  ? 173 ALA B C   1 
ATOM   1277 O O   . ALA A 1 175 ? 9.510   12.021  35.369  1.00 69.74  ? 173 ALA B O   1 
ATOM   1278 C CB  . ALA A 1 175 ? 11.509  13.752  37.320  1.00 61.60  ? 173 ALA B CB  1 
ATOM   1279 N N   . VAL A 1 176 ? 8.697   12.357  37.437  1.00 61.47  ? 174 VAL B N   1 
ATOM   1280 C CA  . VAL A 1 176 ? 7.292   12.314  37.055  1.00 64.87  ? 174 VAL B CA  1 
ATOM   1281 C C   . VAL A 1 176 ? 6.624   13.631  37.439  1.00 70.48  ? 174 VAL B C   1 
ATOM   1282 O O   . VAL A 1 176 ? 6.914   14.196  38.497  1.00 73.99  ? 174 VAL B O   1 
ATOM   1283 C CB  . VAL A 1 176 ? 6.590   11.113  37.718  1.00 66.74  ? 174 VAL B CB  1 
ATOM   1284 C CG1 . VAL A 1 176 ? 5.221   10.887  37.118  1.00 69.91  ? 174 VAL B CG1 1 
ATOM   1285 C CG2 . VAL A 1 176 ? 7.452   9.870   37.556  1.00 62.91  ? 174 VAL B CG2 1 
ATOM   1286 N N   . LEU A 1 177 ? 5.758   14.137  36.566  1.00 69.07  ? 175 LEU B N   1 
ATOM   1287 C CA  . LEU A 1 177 ? 4.926   15.280  36.912  1.00 73.70  ? 175 LEU B CA  1 
ATOM   1288 C C   . LEU A 1 177 ? 3.692   14.805  37.649  1.00 77.22  ? 175 LEU B C   1 
ATOM   1289 O O   . LEU A 1 177 ? 3.019   13.869  37.213  1.00 80.17  ? 175 LEU B O   1 
ATOM   1290 C CB  . LEU A 1 177 ? 4.485   16.059  35.673  1.00 77.30  ? 175 LEU B CB  1 
ATOM   1291 C CG  . LEU A 1 177 ? 3.674   17.341  35.932  1.00 80.71  ? 175 LEU B CG  1 
ATOM   1292 C CD1 . LEU A 1 177 ? 4.522   18.588  35.702  1.00 80.91  ? 175 LEU B CD1 1 
ATOM   1293 C CD2 . LEU A 1 177 ? 2.364   17.376  35.115  1.00 79.31  ? 175 LEU B CD2 1 
ATOM   1294 N N   . GLN A 1 178 ? 3.381   15.468  38.755  1.00 80.82  ? 176 GLN B N   1 
ATOM   1295 C CA  . GLN A 1 178 ? 2.284   15.070  39.623  1.00 82.78  ? 176 GLN B CA  1 
ATOM   1296 C C   . GLN A 1 178 ? 1.111   16.028  39.470  1.00 84.40  ? 176 GLN B C   1 
ATOM   1297 O O   . GLN A 1 178 ? 1.230   17.102  38.871  1.00 84.79  ? 176 GLN B O   1 
ATOM   1298 C CB  . GLN A 1 178 ? 2.740   15.027  41.083  1.00 83.40  ? 176 GLN B CB  1 
ATOM   1299 C CG  . GLN A 1 178 ? 3.577   13.818  41.449  1.00 83.06  ? 176 GLN B CG  1 
ATOM   1300 C CD  . GLN A 1 178 ? 4.464   14.092  42.649  1.00 84.29  ? 176 GLN B CD  1 
ATOM   1301 O OE1 . GLN A 1 178 ? 4.892   13.166  43.354  1.00 84.79  ? 176 GLN B OE1 1 
ATOM   1302 N NE2 . GLN A 1 178 ? 4.776   15.371  42.873  1.00 82.20  ? 176 GLN B NE2 1 
ATOM   1303 N N   . SER A 1 179 ? -0.037  15.618  40.026  1.00 80.92  ? 177 SER B N   1 
ATOM   1304 C CA  . SER A 1 179 ? -1.222  16.471  39.969  1.00 83.42  ? 177 SER B CA  1 
ATOM   1305 C C   . SER A 1 179 ? -0.932  17.843  40.556  1.00 83.80  ? 177 SER B C   1 
ATOM   1306 O O   . SER A 1 179 ? -1.379  18.863  40.018  1.00 86.37  ? 177 SER B O   1 
ATOM   1307 C CB  . SER A 1 179 ? -2.395  15.828  40.711  1.00 84.48  ? 177 SER B CB  1 
ATOM   1308 O OG  . SER A 1 179 ? -2.012  14.634  41.357  1.00 83.93  ? 177 SER B OG  1 
ATOM   1309 N N   . SER A 1 180 ? -0.178  17.888  41.656  1.00 83.28  ? 178 SER B N   1 
ATOM   1310 C CA  . SER A 1 180 ? 0.193   19.160  42.260  1.00 81.94  ? 178 SER B CA  1 
ATOM   1311 C C   . SER A 1 180 ? 1.021   20.029  41.325  1.00 81.16  ? 178 SER B C   1 
ATOM   1312 O O   . SER A 1 180 ? 1.134   21.235  41.552  1.00 82.20  ? 178 SER B O   1 
ATOM   1313 C CB  . SER A 1 180 ? 0.954   18.902  43.559  1.00 81.88  ? 178 SER B CB  1 
ATOM   1314 O OG  . SER A 1 180 ? 1.694   17.697  43.487  1.00 81.69  ? 178 SER B OG  1 
ATOM   1315 N N   . GLY A 1 181 ? 1.571   19.457  40.264  1.00 80.79  ? 179 GLY B N   1 
ATOM   1316 C CA  . GLY A 1 181 ? 2.473   20.191  39.409  1.00 80.35  ? 179 GLY B CA  1 
ATOM   1317 C C   . GLY A 1 181 ? 3.909   20.147  39.858  1.00 79.14  ? 179 GLY B C   1 
ATOM   1318 O O   . GLY A 1 181 ? 4.741   20.881  39.312  1.00 76.24  ? 179 GLY B O   1 
ATOM   1319 N N   . LEU A 1 182 ? 4.227   19.297  40.827  1.00 82.66  ? 180 LEU B N   1 
ATOM   1320 C CA  . LEU A 1 182 ? 5.567   19.173  41.364  1.00 80.16  ? 180 LEU B CA  1 
ATOM   1321 C C   . LEU A 1 182 ? 6.245   17.910  40.860  1.00 75.60  ? 180 LEU B C   1 
ATOM   1322 O O   . LEU A 1 182 ? 5.603   16.901  40.568  1.00 73.64  ? 180 LEU B O   1 
ATOM   1323 C CB  . LEU A 1 182 ? 5.554   19.168  42.890  1.00 79.44  ? 180 LEU B CB  1 
ATOM   1324 C CG  . LEU A 1 182 ? 5.170   20.457  43.609  1.00 82.75  ? 180 LEU B CG  1 
ATOM   1325 C CD1 . LEU A 1 182 ? 6.250   21.480  43.229  1.00 82.95  ? 180 LEU B CD1 1 
ATOM   1326 C CD2 . LEU A 1 182 ? 3.728   20.957  43.332  1.00 80.63  ? 180 LEU B CD2 1 
ATOM   1327 N N   . TYR A 1 183 ? 7.557   17.989  40.786  1.00 72.66  ? 181 TYR B N   1 
ATOM   1328 C CA  . TYR A 1 183 ? 8.376   16.904  40.298  1.00 73.04  ? 181 TYR B CA  1 
ATOM   1329 C C   . TYR A 1 183 ? 8.836   16.047  41.460  1.00 74.60  ? 181 TYR B C   1 
ATOM   1330 O O   . TYR A 1 183 ? 9.160   16.563  42.533  1.00 75.87  ? 181 TYR B O   1 
ATOM   1331 C CB  . TYR A 1 183 ? 9.568   17.480  39.549  1.00 73.69  ? 181 TYR B CB  1 
ATOM   1332 C CG  . TYR A 1 183 ? 9.206   18.030  38.193  1.00 74.86  ? 181 TYR B CG  1 
ATOM   1333 C CD1 . TYR A 1 183 ? 8.037   17.642  37.539  1.00 76.50  ? 181 TYR B CD1 1 
ATOM   1334 C CD2 . TYR A 1 183 ? 9.960   19.034  37.630  1.00 75.47  ? 181 TYR B CD2 1 
ATOM   1335 C CE1 . TYR A 1 183 ? 7.700   18.167  36.309  1.00 82.50  ? 181 TYR B CE1 1 
ATOM   1336 C CE2 . TYR A 1 183 ? 9.631   19.570  36.412  1.00 83.34  ? 181 TYR B CE2 1 
ATOM   1337 C CZ  . TYR A 1 183 ? 8.503   19.142  35.751  1.00 82.01  ? 181 TYR B CZ  1 
ATOM   1338 O OH  . TYR A 1 183 ? 8.213   19.719  34.531  1.00 79.64  ? 181 TYR B OH  1 
ATOM   1339 N N   . SER A 1 184 ? 8.824   14.732  41.256  1.00 72.74  ? 182 SER B N   1 
ATOM   1340 C CA  . SER A 1 184 ? 9.463   13.826  42.195  1.00 72.07  ? 182 SER B CA  1 
ATOM   1341 C C   . SER A 1 184 ? 10.125  12.691  41.437  1.00 66.72  ? 182 SER B C   1 
ATOM   1342 O O   . SER A 1 184 ? 9.622   12.224  40.414  1.00 65.60  ? 182 SER B O   1 
ATOM   1343 C CB  . SER A 1 184 ? 8.497   13.276  43.268  1.00 73.17  ? 182 SER B CB  1 
ATOM   1344 O OG  . SER A 1 184 ? 7.176   13.144  42.792  1.00 78.43  ? 182 SER B OG  1 
ATOM   1345 N N   . LEU A 1 185 ? 11.256  12.262  41.976  1.00 66.97  ? 183 LEU B N   1 
ATOM   1346 C CA  . LEU A 1 185 ? 12.169  11.312  41.372  1.00 64.46  ? 183 LEU B CA  1 
ATOM   1347 C C   . LEU A 1 185 ? 12.678  10.385  42.468  1.00 63.98  ? 183 LEU B C   1 
ATOM   1348 O O   . LEU A 1 185 ? 12.835  10.803  43.616  1.00 64.40  ? 183 LEU B O   1 
ATOM   1349 C CB  . LEU A 1 185 ? 13.314  12.062  40.703  1.00 62.14  ? 183 LEU B CB  1 
ATOM   1350 C CG  . LEU A 1 185 ? 14.601  11.351  40.317  1.00 64.18  ? 183 LEU B CG  1 
ATOM   1351 C CD1 . LEU A 1 185 ? 15.138  11.971  39.057  1.00 62.72  ? 183 LEU B CD1 1 
ATOM   1352 C CD2 . LEU A 1 185 ? 15.604  11.503  41.469  1.00 65.37  ? 183 LEU B CD2 1 
ATOM   1353 N N   . SER A 1 186 ? 12.936  9.127   42.113  1.00 64.72  ? 184 SER B N   1 
ATOM   1354 C CA  . SER A 1 186 ? 13.453  8.150   43.063  1.00 64.19  ? 184 SER B CA  1 
ATOM   1355 C C   . SER A 1 186 ? 14.749  7.577   42.523  1.00 63.28  ? 184 SER B C   1 
ATOM   1356 O O   . SER A 1 186 ? 14.886  7.384   41.314  1.00 62.45  ? 184 SER B O   1 
ATOM   1357 C CB  . SER A 1 186 ? 12.439  7.044   43.315  1.00 65.47  ? 184 SER B CB  1 
ATOM   1358 O OG  . SER A 1 186 ? 11.132  7.500   42.994  1.00 67.64  ? 184 SER B OG  1 
ATOM   1359 N N   . SER A 1 187 ? 15.704  7.332   43.410  1.00 63.68  ? 185 SER B N   1 
ATOM   1360 C CA  . SER A 1 187 ? 17.013  6.827   43.025  1.00 62.98  ? 185 SER B CA  1 
ATOM   1361 C C   . SER A 1 187 ? 17.356  5.682   43.949  1.00 64.22  ? 185 SER B C   1 
ATOM   1362 O O   . SER A 1 187 ? 17.350  5.864   45.166  1.00 65.23  ? 185 SER B O   1 
ATOM   1363 C CB  . SER A 1 187 ? 18.086  7.915   43.112  1.00 62.14  ? 185 SER B CB  1 
ATOM   1364 O OG  . SER A 1 187 ? 19.361  7.394   42.795  1.00 61.62  ? 185 SER B OG  1 
ATOM   1365 N N   . VAL A 1 188 ? 17.648  4.508   43.386  1.00 64.24  ? 186 VAL B N   1 
ATOM   1366 C CA  . VAL A 1 188 ? 17.799  3.291   44.179  1.00 65.64  ? 186 VAL B CA  1 
ATOM   1367 C C   . VAL A 1 188 ? 19.104  2.614   43.811  1.00 65.23  ? 186 VAL B C   1 
ATOM   1368 O O   . VAL A 1 188 ? 19.627  2.807   42.711  1.00 63.94  ? 186 VAL B O   1 
ATOM   1369 C CB  . VAL A 1 188 ? 16.641  2.308   43.965  1.00 66.58  ? 186 VAL B CB  1 
ATOM   1370 C CG1 . VAL A 1 188 ? 15.378  2.862   44.551  1.00 67.36  ? 186 VAL B CG1 1 
ATOM   1371 C CG2 . VAL A 1 188 ? 16.480  2.002   42.507  1.00 65.51  ? 186 VAL B CG2 1 
ATOM   1372 N N   . VAL A 1 189 ? 19.630  1.812   44.730  1.00 66.45  ? 187 VAL B N   1 
ATOM   1373 C CA  . VAL A 1 189 ? 20.851  1.060   44.469  1.00 66.35  ? 187 VAL B CA  1 
ATOM   1374 C C   . VAL A 1 189 ? 20.777  -0.265  45.209  1.00 68.11  ? 187 VAL B C   1 
ATOM   1375 O O   . VAL A 1 189 ? 20.445  -0.289  46.400  1.00 69.42  ? 187 VAL B O   1 
ATOM   1376 C CB  . VAL A 1 189 ? 22.113  1.847   44.872  1.00 65.79  ? 187 VAL B CB  1 
ATOM   1377 C CG1 . VAL A 1 189 ? 22.017  2.343   46.299  1.00 66.81  ? 187 VAL B CG1 1 
ATOM   1378 C CG2 . VAL A 1 189 ? 23.356  0.998   44.662  1.00 65.92  ? 187 VAL B CG2 1 
ATOM   1379 N N   . THR A 1 190 ? 21.045  -1.374  44.496  1.00 68.27  ? 188 THR B N   1 
ATOM   1380 C CA  . THR A 1 190 ? 21.199  -2.680  45.136  1.00 70.01  ? 188 THR B CA  1 
ATOM   1381 C C   . THR A 1 190 ? 22.629  -2.860  45.604  1.00 70.25  ? 188 THR B C   1 
ATOM   1382 O O   . THR A 1 190 ? 23.579  -2.477  44.916  1.00 69.00  ? 188 THR B O   1 
ATOM   1383 C CB  . THR A 1 190 ? 20.829  -3.856  44.226  1.00 70.33  ? 188 THR B CB  1 
ATOM   1384 O OG1 . THR A 1 190 ? 21.329  -3.636  42.902  1.00 72.26  ? 188 THR B OG1 1 
ATOM   1385 C CG2 . THR A 1 190 ? 19.330  -4.141  44.249  1.00 71.12  ? 188 THR B CG2 1 
ATOM   1386 N N   . VAL A 1 191 ? 22.784  -3.455  46.776  1.00 71.97  ? 189 VAL B N   1 
ATOM   1387 C CA  . VAL A 1 191 ? 24.124  -3.495  47.326  1.00 73.21  ? 189 VAL B CA  1 
ATOM   1388 C C   . VAL A 1 191 ? 24.233  -4.806  48.097  1.00 80.53  ? 189 VAL B C   1 
ATOM   1389 O O   . VAL A 1 191 ? 23.203  -5.423  48.411  1.00 84.63  ? 189 VAL B O   1 
ATOM   1390 C CB  . VAL A 1 191 ? 24.371  -2.243  48.186  1.00 79.04  ? 189 VAL B CB  1 
ATOM   1391 C CG1 . VAL A 1 191 ? 23.830  -2.403  49.645  1.00 80.97  ? 189 VAL B CG1 1 
ATOM   1392 C CG2 . VAL A 1 191 ? 25.799  -1.678  48.039  1.00 79.31  ? 189 VAL B CG2 1 
ATOM   1393 N N   . PRO A 1 192 ? 25.432  -5.298  48.386  1.00 77.83  ? 190 PRO B N   1 
ATOM   1394 C CA  . PRO A 1 192 ? 25.538  -6.497  49.213  1.00 84.76  ? 190 PRO B CA  1 
ATOM   1395 C C   . PRO A 1 192 ? 24.852  -6.330  50.566  1.00 91.20  ? 190 PRO B C   1 
ATOM   1396 O O   . PRO A 1 192 ? 25.083  -5.351  51.283  1.00 95.75  ? 190 PRO B O   1 
ATOM   1397 C CB  . PRO A 1 192 ? 27.050  -6.652  49.366  1.00 87.25  ? 190 PRO B CB  1 
ATOM   1398 C CG  . PRO A 1 192 ? 27.564  -6.158  48.094  1.00 75.69  ? 190 PRO B CG  1 
ATOM   1399 C CD  . PRO A 1 192 ? 26.760  -4.918  47.871  1.00 75.38  ? 190 PRO B CD  1 
ATOM   1400 N N   . SER A 1 193 ? 24.010  -7.308  50.921  1.00 94.35  ? 191 SER B N   1 
ATOM   1401 C CA  . SER A 1 193 ? 23.421  -7.349  52.259  1.00 95.25  ? 191 SER B CA  1 
ATOM   1402 C C   . SER A 1 193 ? 24.470  -7.517  53.348  1.00 100.47 ? 191 SER B C   1 
ATOM   1403 O O   . SER A 1 193 ? 24.186  -7.233  54.518  1.00 99.25  ? 191 SER B O   1 
ATOM   1404 C CB  . SER A 1 193 ? 22.406  -8.485  52.369  1.00 98.02  ? 191 SER B CB  1 
ATOM   1405 O OG  . SER A 1 193 ? 21.087  -8.044  52.117  1.00 103.35 ? 191 SER B OG  1 
ATOM   1406 N N   . SER A 1 194 ? 25.661  -8.002  52.999  1.00 99.89  ? 192 SER B N   1 
ATOM   1407 C CA  . SER A 1 194 ? 26.758  -8.056  53.959  1.00 101.26 ? 192 SER B CA  1 
ATOM   1408 C C   . SER A 1 194 ? 27.142  -6.661  54.424  1.00 105.04 ? 192 SER B C   1 
ATOM   1409 O O   . SER A 1 194 ? 27.048  -6.337  55.613  1.00 105.95 ? 192 SER B O   1 
ATOM   1410 C CB  . SER A 1 194 ? 27.968  -8.738  53.334  1.00 99.04  ? 192 SER B CB  1 
ATOM   1411 O OG  . SER A 1 194 ? 29.012  -7.788  53.172  1.00 100.07 ? 192 SER B OG  1 
ATOM   1412 N N   . SER A 1 195 ? 27.595  -5.821  53.485  1.00 125.31 ? 193 SER B N   1 
ATOM   1413 C CA  . SER A 1 195 ? 28.066  -4.466  53.761  1.00 124.94 ? 193 SER B CA  1 
ATOM   1414 C C   . SER A 1 195 ? 26.978  -3.532  54.265  1.00 123.55 ? 193 SER B C   1 
ATOM   1415 O O   . SER A 1 195 ? 27.287  -2.367  54.537  1.00 122.75 ? 193 SER B O   1 
ATOM   1416 C CB  . SER A 1 195 ? 28.703  -3.854  52.510  1.00 124.09 ? 193 SER B CB  1 
ATOM   1417 O OG  . SER A 1 195 ? 30.113  -3.968  52.550  1.00 125.77 ? 193 SER B OG  1 
ATOM   1418 N N   . LEU A 1 196 ? 25.734  -3.998  54.394  1.00 107.97 ? 194 LEU B N   1 
ATOM   1419 C CA  . LEU A 1 196 ? 24.669  -3.129  54.878  1.00 102.74 ? 194 LEU B CA  1 
ATOM   1420 C C   . LEU A 1 196 ? 25.026  -2.522  56.229  1.00 100.07 ? 194 LEU B C   1 
ATOM   1421 O O   . LEU A 1 196 ? 24.866  -1.316  56.440  1.00 104.97 ? 194 LEU B O   1 
ATOM   1422 C CB  . LEU A 1 196 ? 23.357  -3.905  54.967  1.00 97.86  ? 194 LEU B CB  1 
ATOM   1423 C CG  . LEU A 1 196 ? 22.298  -3.550  53.918  1.00 89.98  ? 194 LEU B CG  1 
ATOM   1424 C CD1 . LEU A 1 196 ? 20.915  -3.897  54.437  1.00 89.97  ? 194 LEU B CD1 1 
ATOM   1425 C CD2 . LEU A 1 196 ? 22.361  -2.085  53.495  1.00 86.29  ? 194 LEU B CD2 1 
ATOM   1426 N N   . GLY A 1 197 ? 25.548  -3.332  57.141  1.00 100.28 ? 195 GLY B N   1 
ATOM   1427 C CA  . GLY A 1 197 ? 25.804  -2.870  58.494  1.00 104.42 ? 195 GLY B CA  1 
ATOM   1428 C C   . GLY A 1 197 ? 27.008  -1.964  58.677  1.00 102.51 ? 195 GLY B C   1 
ATOM   1429 O O   . GLY A 1 197 ? 26.957  -1.021  59.470  1.00 98.85  ? 195 GLY B O   1 
ATOM   1430 N N   . THR A 1 198 ? 28.095  -2.231  57.953  1.00 101.39 ? 196 THR B N   1 
ATOM   1431 C CA  . THR A 1 198 ? 29.366  -1.559  58.192  1.00 100.31 ? 196 THR B CA  1 
ATOM   1432 C C   . THR A 1 198 ? 29.631  -0.413  57.225  1.00 102.77 ? 196 THR B C   1 
ATOM   1433 O O   . THR A 1 198 ? 30.542  0.390   57.463  1.00 102.18 ? 196 THR B O   1 
ATOM   1434 C CB  . THR A 1 198 ? 30.509  -2.574  58.097  1.00 103.02 ? 196 THR B CB  1 
ATOM   1435 O OG1 . THR A 1 198 ? 30.075  -3.831  58.638  1.00 104.99 ? 196 THR B OG1 1 
ATOM   1436 C CG2 . THR A 1 198 ? 31.724  -2.089  58.887  1.00 102.67 ? 196 THR B CG2 1 
ATOM   1437 N N   . GLN A 1 199 ? 28.863  -0.310  56.149  1.00 103.22 ? 197 GLN B N   1 
ATOM   1438 C CA  . GLN A 1 199 ? 29.122  0.659   55.095  1.00 100.67 ? 197 GLN B CA  1 
ATOM   1439 C C   . GLN A 1 199 ? 27.971  1.651   55.019  1.00 98.19  ? 197 GLN B C   1 
ATOM   1440 O O   . GLN A 1 199 ? 26.830  1.267   54.738  1.00 97.42  ? 197 GLN B O   1 
ATOM   1441 C CB  . GLN A 1 199 ? 29.304  -0.039  53.753  1.00 101.21 ? 197 GLN B CB  1 
ATOM   1442 C CG  . GLN A 1 199 ? 29.275  0.918   52.612  1.00 98.17  ? 197 GLN B CG  1 
ATOM   1443 C CD  . GLN A 1 199 ? 30.646  1.221   52.075  1.00 99.11  ? 197 GLN B CD  1 
ATOM   1444 O OE1 . GLN A 1 199 ? 31.639  0.659   52.535  1.00 102.79 ? 197 GLN B OE1 1 
ATOM   1445 N NE2 . GLN A 1 199 ? 30.713  2.105   51.081  1.00 99.13  ? 197 GLN B NE2 1 
ATOM   1446 N N   . THR A 1 200 ? 28.279  2.920   55.251  1.00 99.46  ? 198 THR B N   1 
ATOM   1447 C CA  . THR A 1 200 ? 27.287  3.978   55.176  1.00 95.64  ? 198 THR B CA  1 
ATOM   1448 C C   . THR A 1 200 ? 27.006  4.335   53.724  1.00 92.16  ? 198 THR B C   1 
ATOM   1449 O O   . THR A 1 200 ? 27.907  4.315   52.883  1.00 92.62  ? 198 THR B O   1 
ATOM   1450 C CB  . THR A 1 200 ? 27.786  5.205   55.929  1.00 94.44  ? 198 THR B CB  1 
ATOM   1451 O OG1 . THR A 1 200 ? 28.592  5.983   55.037  1.00 95.96  ? 198 THR B OG1 1 
ATOM   1452 C CG2 . THR A 1 200 ? 28.620  4.795   57.148  1.00 94.32  ? 198 THR B CG2 1 
ATOM   1453 N N   . TYR A 1 201 ? 25.755  4.684   53.436  1.00 89.96  ? 199 TYR B N   1 
ATOM   1454 C CA  . TYR A 1 201 ? 25.325  5.042   52.085  1.00 88.33  ? 199 TYR B CA  1 
ATOM   1455 C C   . TYR A 1 201 ? 24.645  6.406   52.127  1.00 85.84  ? 199 TYR B C   1 
ATOM   1456 O O   . TYR A 1 201 ? 23.656  6.586   52.850  1.00 85.24  ? 199 TYR B O   1 
ATOM   1457 C CB  . TYR A 1 201 ? 24.386  3.959   51.553  1.00 88.49  ? 199 TYR B CB  1 
ATOM   1458 C CG  . TYR A 1 201 ? 25.100  2.635   51.389  1.00 93.61  ? 199 TYR B CG  1 
ATOM   1459 C CD1 . TYR A 1 201 ? 24.541  1.459   51.884  1.00 94.28  ? 199 TYR B CD1 1 
ATOM   1460 C CD2 . TYR A 1 201 ? 26.277  2.540   50.644  1.00 94.48  ? 199 TYR B CD2 1 
ATOM   1461 C CE1 . TYR A 1 201 ? 25.185  0.241   51.740  1.00 93.95  ? 199 TYR B CE1 1 
ATOM   1462 C CE2 . TYR A 1 201 ? 26.911  1.311   50.463  1.00 94.09  ? 199 TYR B CE2 1 
ATOM   1463 C CZ  . TYR A 1 201 ? 26.368  0.170   51.023  1.00 93.70  ? 199 TYR B CZ  1 
ATOM   1464 O OH  . TYR A 1 201 ? 27.010  -1.040  50.848  1.00 96.64  ? 199 TYR B OH  1 
ATOM   1465 N N   . ILE A 1 202 ? 25.182  7.368   51.371  1.00 82.87  ? 200 ILE B N   1 
ATOM   1466 C CA  . ILE A 1 202 ? 24.616  8.709   51.270  1.00 78.84  ? 200 ILE B CA  1 
ATOM   1467 C C   . ILE A 1 202 ? 24.301  8.974   49.810  1.00 76.34  ? 200 ILE B C   1 
ATOM   1468 O O   . ILE A 1 202 ? 25.134  8.708   48.935  1.00 78.27  ? 200 ILE B O   1 
ATOM   1469 C CB  . ILE A 1 202 ? 25.570  9.794   51.803  1.00 78.94  ? 200 ILE B CB  1 
ATOM   1470 C CG1 . ILE A 1 202 ? 26.993  9.522   51.325  1.00 80.61  ? 200 ILE B CG1 1 
ATOM   1471 C CG2 . ILE A 1 202 ? 25.553  9.815   53.315  1.00 76.94  ? 200 ILE B CG2 1 
ATOM   1472 C CD1 . ILE A 1 202 ? 27.869  10.755  51.273  1.00 78.68  ? 200 ILE B CD1 1 
ATOM   1473 N N   . CYS A 1 203 ? 23.108  9.495   49.543  1.00 73.45  ? 201 CYS B N   1 
ATOM   1474 C CA  . CYS A 1 203 ? 22.767  9.972   48.209  1.00 72.28  ? 201 CYS B CA  1 
ATOM   1475 C C   . CYS A 1 203 ? 22.910  11.486  48.189  1.00 74.83  ? 201 CYS B C   1 
ATOM   1476 O O   . CYS A 1 203 ? 22.410  12.175  49.083  1.00 74.68  ? 201 CYS B O   1 
ATOM   1477 C CB  . CYS A 1 203 ? 21.351  9.553   47.810  1.00 69.76  ? 201 CYS B CB  1 
ATOM   1478 S SG  . CYS A 1 203 ? 20.048  10.664  48.342  1.00 66.81  ? 201 CYS B SG  1 
ATOM   1479 N N   . ASN A 1 204 ? 23.631  12.002  47.211  1.00 74.08  ? 202 ASN B N   1 
ATOM   1480 C CA  . ASN A 1 204 ? 23.818  13.435  47.087  1.00 72.96  ? 202 ASN B CA  1 
ATOM   1481 C C   . ASN A 1 204 ? 22.833  13.952  46.055  1.00 74.27  ? 202 ASN B C   1 
ATOM   1482 O O   . ASN A 1 204 ? 22.840  13.508  44.900  1.00 72.96  ? 202 ASN B O   1 
ATOM   1483 C CB  . ASN A 1 204 ? 25.246  13.758  46.691  1.00 75.94  ? 202 ASN B CB  1 
ATOM   1484 C CG  . ASN A 1 204 ? 26.226  12.888  47.396  1.00 76.64  ? 202 ASN B CG  1 
ATOM   1485 O OD1 . ASN A 1 204 ? 27.174  12.406  46.795  1.00 80.04  ? 202 ASN B OD1 1 
ATOM   1486 N ND2 . ASN A 1 204 ? 26.019  12.687  48.685  1.00 77.21  ? 202 ASN B ND2 1 
ATOM   1487 N N   . VAL A 1 205 ? 21.971  14.860  46.488  1.00 73.26  ? 203 VAL B N   1 
ATOM   1488 C CA  . VAL A 1 205 ? 20.921  15.433  45.663  1.00 71.72  ? 203 VAL B CA  1 
ATOM   1489 C C   . VAL A 1 205 ? 21.342  16.856  45.351  1.00 74.36  ? 203 VAL B C   1 
ATOM   1490 O O   . VAL A 1 205 ? 21.819  17.568  46.240  1.00 75.95  ? 203 VAL B O   1 
ATOM   1491 C CB  . VAL A 1 205 ? 19.564  15.381  46.388  1.00 70.97  ? 203 VAL B CB  1 
ATOM   1492 C CG1 . VAL A 1 205 ? 18.513  16.205  45.669  1.00 68.77  ? 203 VAL B CG1 1 
ATOM   1493 C CG2 . VAL A 1 205 ? 19.100  13.952  46.519  1.00 70.81  ? 203 VAL B CG2 1 
ATOM   1494 N N   . ASN A 1 206 ? 21.226  17.250  44.083  1.00 75.32  ? 204 ASN B N   1 
ATOM   1495 C CA  . ASN A 1 206 ? 21.546  18.603  43.634  1.00 75.52  ? 204 ASN B CA  1 
ATOM   1496 C C   . ASN A 1 206 ? 20.414  19.119  42.760  1.00 74.31  ? 204 ASN B C   1 
ATOM   1497 O O   . ASN A 1 206 ? 20.101  18.523  41.723  1.00 72.96  ? 204 ASN B O   1 
ATOM   1498 C CB  . ASN A 1 206 ? 22.867  18.650  42.860  1.00 76.23  ? 204 ASN B CB  1 
ATOM   1499 C CG  . ASN A 1 206 ? 23.378  20.076  42.666  1.00 80.30  ? 204 ASN B CG  1 
ATOM   1500 O OD1 . ASN A 1 206 ? 24.406  20.307  42.029  1.00 83.86  ? 204 ASN B OD1 1 
ATOM   1501 N ND2 . ASN A 1 206 ? 22.653  21.038  43.217  1.00 79.31  ? 204 ASN B ND2 1 
ATOM   1502 N N   . HIS A 1 207 ? 19.817  20.230  43.173  1.00 72.54  ? 205 HIS B N   1 
ATOM   1503 C CA  . HIS A 1 207 ? 18.777  20.909  42.404  1.00 73.84  ? 205 HIS B CA  1 
ATOM   1504 C C   . HIS A 1 207 ? 19.152  22.385  42.252  1.00 74.77  ? 205 HIS B C   1 
ATOM   1505 O O   . HIS A 1 207 ? 18.830  23.206  43.118  1.00 74.18  ? 205 HIS B O   1 
ATOM   1506 C CB  . HIS A 1 207 ? 17.424  20.753  43.075  1.00 71.76  ? 205 HIS B CB  1 
ATOM   1507 C CG  . HIS A 1 207 ? 16.304  21.371  42.306  1.00 71.14  ? 205 HIS B CG  1 
ATOM   1508 N ND1 . HIS A 1 207 ? 15.565  22.429  42.788  1.00 72.37  ? 205 HIS B ND1 1 
ATOM   1509 C CD2 . HIS A 1 207 ? 15.812  21.092  41.076  1.00 68.46  ? 205 HIS B CD2 1 
ATOM   1510 C CE1 . HIS A 1 207 ? 14.648  22.760  41.896  1.00 74.80  ? 205 HIS B CE1 1 
ATOM   1511 N NE2 . HIS A 1 207 ? 14.779  21.967  40.847  1.00 73.20  ? 205 HIS B NE2 1 
ATOM   1512 N N   . LYS A 1 208 ? 19.808  22.719  41.133  1.00 73.15  ? 206 LYS B N   1 
ATOM   1513 C CA  . LYS A 1 208 ? 20.335  24.057  40.876  1.00 72.22  ? 206 LYS B CA  1 
ATOM   1514 C C   . LYS A 1 208 ? 19.285  25.166  40.785  1.00 68.72  ? 206 LYS B C   1 
ATOM   1515 O O   . LYS A 1 208 ? 19.530  26.255  41.319  1.00 68.27  ? 206 LYS B O   1 
ATOM   1516 C CB  . LYS A 1 208 ? 21.169  24.054  39.594  1.00 72.22  ? 206 LYS B CB  1 
ATOM   1517 C CG  . LYS A 1 208 ? 21.778  25.420  39.278  1.00 75.42  ? 206 LYS B CG  1 
ATOM   1518 C CD  . LYS A 1 208 ? 22.512  26.029  40.492  1.00 79.03  ? 206 LYS B CD  1 
ATOM   1519 C CE  . LYS A 1 208 ? 23.668  26.926  40.041  1.00 81.72  ? 206 LYS B CE  1 
ATOM   1520 N NZ  . LYS A 1 208 ? 24.967  26.174  40.002  1.00 84.38  ? 206 LYS B NZ  1 
ATOM   1521 N N   . PRO A 1 209 ? 18.126  24.966  40.099  1.00 68.76  ? 207 PRO B N   1 
ATOM   1522 C CA  . PRO A 1 209 ? 17.118  26.040  40.020  1.00 69.09  ? 207 PRO B CA  1 
ATOM   1523 C C   . PRO A 1 209 ? 16.843  26.794  41.319  1.00 75.75  ? 207 PRO B C   1 
ATOM   1524 O O   . PRO A 1 209 ? 16.628  28.009  41.294  1.00 79.23  ? 207 PRO B O   1 
ATOM   1525 C CB  . PRO A 1 209 ? 15.869  25.293  39.548  1.00 71.13  ? 207 PRO B CB  1 
ATOM   1526 C CG  . PRO A 1 209 ? 16.418  24.249  38.659  1.00 73.21  ? 207 PRO B CG  1 
ATOM   1527 C CD  . PRO A 1 209 ? 17.726  23.810  39.273  1.00 69.74  ? 207 PRO B CD  1 
ATOM   1528 N N   . SER A 1 210 ? 16.843  26.099  42.456  1.00 73.41  ? 208 SER B N   1 
ATOM   1529 C CA  . SER A 1 210 ? 16.630  26.713  43.758  1.00 70.87  ? 208 SER B CA  1 
ATOM   1530 C C   . SER A 1 210 ? 17.903  26.749  44.591  1.00 74.32  ? 208 SER B C   1 
ATOM   1531 O O   . SER A 1 210 ? 17.842  27.037  45.798  1.00 77.00  ? 208 SER B O   1 
ATOM   1532 C CB  . SER A 1 210 ? 15.528  25.970  44.505  1.00 76.22  ? 208 SER B CB  1 
ATOM   1533 O OG  . SER A 1 210 ? 15.860  24.596  44.591  1.00 78.70  ? 208 SER B OG  1 
ATOM   1534 N N   . ASN A 1 211 ? 19.051  26.489  43.964  1.00 73.56  ? 209 ASN B N   1 
ATOM   1535 C CA  . ASN A 1 211 ? 20.358  26.438  44.615  1.00 75.81  ? 209 ASN B CA  1 
ATOM   1536 C C   . ASN A 1 211 ? 20.318  25.522  45.835  1.00 75.74  ? 209 ASN B C   1 
ATOM   1537 O O   . ASN A 1 211 ? 20.558  25.939  46.971  1.00 76.31  ? 209 ASN B O   1 
ATOM   1538 C CB  . ASN A 1 211 ? 20.849  27.839  44.991  1.00 79.22  ? 209 ASN B CB  1 
ATOM   1539 C CG  . ASN A 1 211 ? 22.367  27.983  44.870  1.00 83.96  ? 209 ASN B CG  1 
ATOM   1540 O OD1 . ASN A 1 211 ? 22.999  27.376  43.997  1.00 83.90  ? 209 ASN B OD1 1 
ATOM   1541 N ND2 . ASN A 1 211 ? 22.962  28.763  45.779  1.00 87.57  ? 209 ASN B ND2 1 
ATOM   1542 N N   . THR A 1 212 ? 19.997  24.251  45.576  1.00 79.07  ? 210 THR B N   1 
ATOM   1543 C CA  . THR A 1 212 ? 19.878  23.238  46.618  1.00 80.11  ? 210 THR B CA  1 
ATOM   1544 C C   . THR A 1 212 ? 20.803  22.060  46.332  1.00 78.36  ? 210 THR B C   1 
ATOM   1545 O O   . THR A 1 212 ? 20.793  21.502  45.230  1.00 75.95  ? 210 THR B O   1 
ATOM   1546 C CB  . THR A 1 212 ? 18.427  22.754  46.774  1.00 80.01  ? 210 THR B CB  1 
ATOM   1547 O OG1 . THR A 1 212 ? 17.514  23.843  46.583  1.00 80.42  ? 210 THR B OG1 1 
ATOM   1548 C CG2 . THR A 1 212 ? 18.204  22.166  48.165  1.00 78.07  ? 210 THR B CG2 1 
ATOM   1549 N N   . LYS A 1 213 ? 21.599  21.694  47.342  1.00 80.07  ? 211 LYS B N   1 
ATOM   1550 C CA  . LYS A 1 213 ? 22.491  20.532  47.305  1.00 81.49  ? 211 LYS B CA  1 
ATOM   1551 C C   . LYS A 1 213 ? 22.520  19.919  48.709  1.00 80.95  ? 211 LYS B C   1 
ATOM   1552 O O   . LYS A 1 213 ? 23.136  20.481  49.621  1.00 80.90  ? 211 LYS B O   1 
ATOM   1553 C CB  . LYS A 1 213 ? 23.901  20.922  46.827  1.00 81.58  ? 211 LYS B CB  1 
ATOM   1554 C CG  . LYS A 1 213 ? 24.873  19.729  46.688  1.00 82.70  ? 211 LYS B CG  1 
ATOM   1555 C CD  . LYS A 1 213 ? 25.818  19.849  45.476  1.00 82.52  ? 211 LYS B CD  1 
ATOM   1556 C CE  . LYS A 1 213 ? 27.312  19.913  45.832  1.00 88.43  ? 211 LYS B CE  1 
ATOM   1557 N NZ  . LYS A 1 213 ? 28.156  19.158  44.814  1.00 84.44  ? 211 LYS B NZ  1 
ATOM   1558 N N   . VAL A 1 214 ? 21.843  18.779  48.895  1.00 80.61  ? 212 VAL B N   1 
ATOM   1559 C CA  . VAL A 1 214 ? 21.804  18.093  50.185  1.00 79.83  ? 212 VAL B CA  1 
ATOM   1560 C C   . VAL A 1 214 ? 22.326  16.673  50.036  1.00 75.45  ? 212 VAL B C   1 
ATOM   1561 O O   . VAL A 1 214 ? 22.300  16.082  48.953  1.00 76.57  ? 212 VAL B O   1 
ATOM   1562 C CB  . VAL A 1 214 ? 20.392  18.065  50.805  1.00 77.07  ? 212 VAL B CB  1 
ATOM   1563 C CG1 . VAL A 1 214 ? 19.774  19.429  50.769  1.00 79.41  ? 212 VAL B CG1 1 
ATOM   1564 C CG2 . VAL A 1 214 ? 19.520  17.088  50.057  1.00 74.48  ? 212 VAL B CG2 1 
ATOM   1565 N N   . ASP A 1 215 ? 22.787  16.119  51.150  1.00 73.85  ? 213 ASP B N   1 
ATOM   1566 C CA  . ASP A 1 215 ? 23.314  14.760  51.215  1.00 75.79  ? 213 ASP B CA  1 
ATOM   1567 C C   . ASP A 1 215 ? 22.558  13.974  52.282  1.00 77.07  ? 213 ASP B C   1 
ATOM   1568 O O   . ASP A 1 215 ? 22.762  14.185  53.488  1.00 76.92  ? 213 ASP B O   1 
ATOM   1569 C CB  . ASP A 1 215 ? 24.805  14.791  51.512  1.00 74.98  ? 213 ASP B CB  1 
ATOM   1570 C CG  . ASP A 1 215 ? 25.581  15.464  50.426  1.00 76.29  ? 213 ASP B CG  1 
ATOM   1571 O OD1 . ASP A 1 215 ? 26.765  15.778  50.661  1.00 82.32  ? 213 ASP B OD1 1 
ATOM   1572 O OD2 . ASP A 1 215 ? 25.022  15.639  49.319  1.00 79.36  ? 213 ASP B OD2 1 
ATOM   1573 N N   . LYS A 1 216 ? 21.689  13.070  51.843  1.00 74.47  ? 214 LYS B N   1 
ATOM   1574 C CA  . LYS A 1 216 ? 20.910  12.255  52.760  1.00 79.66  ? 214 LYS B CA  1 
ATOM   1575 C C   . LYS A 1 216 ? 21.622  10.933  52.984  1.00 79.81  ? 214 LYS B C   1 
ATOM   1576 O O   . LYS A 1 216 ? 22.144  10.332  52.039  1.00 79.31  ? 214 LYS B O   1 
ATOM   1577 C CB  . LYS A 1 216 ? 19.504  12.003  52.223  1.00 77.58  ? 214 LYS B CB  1 
ATOM   1578 C CG  . LYS A 1 216 ? 18.578  11.224  53.161  1.00 76.66  ? 214 LYS B CG  1 
ATOM   1579 C CD  . LYS A 1 216 ? 18.706  11.641  54.605  1.00 82.17  ? 214 LYS B CD  1 
ATOM   1580 C CE  . LYS A 1 216 ? 17.351  11.574  55.317  1.00 85.08  ? 214 LYS B CE  1 
ATOM   1581 N NZ  . LYS A 1 216 ? 16.248  12.241  54.568  1.00 80.77  ? 214 LYS B NZ  1 
ATOM   1582 N N   . LYS A 1 217 ? 21.672  10.507  54.242  1.00 80.18  ? 215 LYS B N   1 
ATOM   1583 C CA  . LYS A 1 217 ? 22.166  9.189   54.604  1.00 81.58  ? 215 LYS B CA  1 
ATOM   1584 C C   . LYS A 1 217 ? 20.975  8.272   54.816  1.00 80.85  ? 215 LYS B C   1 
ATOM   1585 O O   . LYS A 1 217 ? 20.066  8.608   55.584  1.00 80.18  ? 215 LYS B O   1 
ATOM   1586 C CB  . LYS A 1 217 ? 23.018  9.235   55.870  1.00 83.85  ? 215 LYS B CB  1 
ATOM   1587 C CG  . LYS A 1 217 ? 23.143  7.870   56.526  1.00 86.77  ? 215 LYS B CG  1 
ATOM   1588 C CD  . LYS A 1 217 ? 23.921  7.904   57.836  1.00 94.77  ? 215 LYS B CD  1 
ATOM   1589 C CE  . LYS A 1 217 ? 25.373  7.461   57.655  1.00 97.33  ? 215 LYS B CE  1 
ATOM   1590 N NZ  . LYS A 1 217 ? 26.262  8.076   58.688  1.00 102.26 ? 215 LYS B NZ  1 
ATOM   1591 N N   . VAL A 1 218 ? 20.976  7.124   54.136  1.00 84.48  ? 216 VAL B N   1 
ATOM   1592 C CA  . VAL A 1 218 ? 19.883  6.159   54.225  1.00 86.84  ? 216 VAL B CA  1 
ATOM   1593 C C   . VAL A 1 218 ? 20.350  4.963   55.050  1.00 87.63  ? 216 VAL B C   1 
ATOM   1594 O O   . VAL A 1 218 ? 21.303  4.265   54.673  1.00 88.41  ? 216 VAL B O   1 
ATOM   1595 C CB  . VAL A 1 218 ? 19.398  5.736   52.836  1.00 78.62  ? 216 VAL B CB  1 
ATOM   1596 C CG1 . VAL A 1 218 ? 18.013  5.112   52.932  1.00 77.32  ? 216 VAL B CG1 1 
ATOM   1597 C CG2 . VAL A 1 218 ? 19.379  6.938   51.951  1.00 75.60  ? 216 VAL B CG2 1 
ATOM   1598 N N   . GLU A 1 219 ? 19.680  4.735   56.170  1.00 83.00  ? 217 GLU B N   1 
ATOM   1599 C CA  . GLU A 1 219 ? 20.079  3.762   57.171  1.00 86.12  ? 217 GLU B CA  1 
ATOM   1600 C C   . GLU A 1 219 ? 18.880  2.923   57.578  1.00 86.19  ? 217 GLU B C   1 
ATOM   1601 O O   . GLU A 1 219 ? 17.732  3.369   57.478  1.00 84.63  ? 217 GLU B O   1 
ATOM   1602 C CB  . GLU A 1 219 ? 20.658  4.457   58.414  1.00 91.62  ? 217 GLU B CB  1 
ATOM   1603 C CG  . GLU A 1 219 ? 22.146  4.823   58.341  1.00 95.87  ? 217 GLU B CG  1 
ATOM   1604 C CD  . GLU A 1 219 ? 23.046  3.690   57.831  1.00 94.78  ? 217 GLU B CD  1 
ATOM   1605 O OE1 . GLU A 1 219 ? 23.253  2.696   58.574  1.00 93.41  ? 217 GLU B OE1 1 
ATOM   1606 O OE2 . GLU A 1 219 ? 23.571  3.821   56.700  1.00 93.93  ? 217 GLU B OE2 1 
ATOM   1607 N N   . PRO A 1 220 ? 19.117  1.703   58.056  1.00 90.35  ? 218 PRO B N   1 
ATOM   1608 C CA  . PRO A 1 220 ? 18.012  0.862   58.539  1.00 87.48  ? 218 PRO B CA  1 
ATOM   1609 C C   . PRO A 1 220 ? 17.393  1.448   59.801  1.00 89.96  ? 218 PRO B C   1 
ATOM   1610 O O   . PRO A 1 220 ? 18.113  1.811   60.736  1.00 90.97  ? 218 PRO B O   1 
ATOM   1611 C CB  . PRO A 1 220 ? 18.700  -0.476  58.827  1.00 84.89  ? 218 PRO B CB  1 
ATOM   1612 C CG  . PRO A 1 220 ? 19.971  -0.432  57.992  1.00 86.51  ? 218 PRO B CG  1 
ATOM   1613 C CD  . PRO A 1 220 ? 20.403  0.987   58.108  1.00 90.20  ? 218 PRO B CD  1 
ATOM   1614 N N   . LYS A 1 221 ? 16.053  1.519   59.820  1.00 89.96  ? 219 LYS B N   1 
ATOM   1615 C CA  . LYS A 1 221 ? 15.230  1.982   60.969  1.00 91.91  ? 219 LYS B CA  1 
ATOM   1616 C C   . LYS A 1 221 ? 16.016  2.483   62.184  1.00 91.07  ? 219 LYS B C   1 
ATOM   1617 O O   . LYS A 1 221 ? 15.939  3.653   62.554  1.00 96.02  ? 219 LYS B O   1 
ATOM   1618 C CB  . LYS A 1 221 ? 14.274  0.864   61.437  1.00 89.80  ? 219 LYS B CB  1 
ATOM   1619 C CG  . LYS A 1 221 ? 13.899  0.890   62.941  1.00 92.21  ? 219 LYS B CG  1 
ATOM   1620 C CD  . LYS A 1 221 ? 14.821  0.041   63.837  1.00 93.75  ? 219 LYS B CD  1 
ATOM   1621 C CE  . LYS A 1 221 ? 14.334  -1.391  63.995  1.00 95.83  ? 219 LYS B CE  1 
ATOM   1622 N NZ  . LYS A 1 221 ? 15.378  -2.196  64.666  1.00 97.04  ? 219 LYS B NZ  1 
ATOM   1623 N N   . MET B 2 5   ? 7.114   12.246  7.549   1.00 77.16  ? 4   MET D N   1 
ATOM   1624 C CA  . MET B 2 5   ? 5.796   12.305  8.186   1.00 78.32  ? 4   MET D CA  1 
ATOM   1625 C C   . MET B 2 5   ? 5.421   11.072  9.051   1.00 77.92  ? 4   MET D C   1 
ATOM   1626 O O   . MET B 2 5   ? 5.236   11.207  10.271  1.00 79.60  ? 4   MET D O   1 
ATOM   1627 C CB  . MET B 2 5   ? 4.705   12.507  7.131   1.00 76.87  ? 4   MET D CB  1 
ATOM   1628 C CG  . MET B 2 5   ? 4.519   13.949  6.685   1.00 78.33  ? 4   MET D CG  1 
ATOM   1629 S SD  . MET B 2 5   ? 2.788   14.478  6.595   1.00 91.28  ? 4   MET D SD  1 
ATOM   1630 C CE  . MET B 2 5   ? 2.937   15.890  5.488   1.00 84.93  ? 4   MET D CE  1 
ATOM   1631 N N   . THR B 2 6   ? 5.280   9.886   8.431   1.00 74.89  ? 5   THR D N   1 
ATOM   1632 C CA  . THR B 2 6   ? 4.717   8.692   9.086   1.00 75.26  ? 5   THR D CA  1 
ATOM   1633 C C   . THR B 2 6   ? 5.764   7.592   9.243   1.00 72.02  ? 5   THR D C   1 
ATOM   1634 O O   . THR B 2 6   ? 6.073   6.882   8.277   1.00 70.82  ? 5   THR D O   1 
ATOM   1635 C CB  . THR B 2 6   ? 3.520   8.148   8.306   1.00 75.20  ? 5   THR D CB  1 
ATOM   1636 O OG1 . THR B 2 6   ? 2.512   9.162   8.192   1.00 79.47  ? 5   THR D OG1 1 
ATOM   1637 C CG2 . THR B 2 6   ? 2.950   6.919   8.991   1.00 71.56  ? 5   THR D CG2 1 
ATOM   1638 N N   . GLN B 2 7   ? 6.248   7.403   10.474  1.00 67.33  ? 6   GLN D N   1 
ATOM   1639 C CA  . GLN B 2 7   ? 7.409   6.567   10.768  1.00 64.30  ? 6   GLN D CA  1 
ATOM   1640 C C   . GLN B 2 7   ? 6.980   5.250   11.408  1.00 66.75  ? 6   GLN D C   1 
ATOM   1641 O O   . GLN B 2 7   ? 6.291   5.248   12.440  1.00 67.09  ? 6   GLN D O   1 
ATOM   1642 C CB  . GLN B 2 7   ? 8.379   7.315   11.694  1.00 61.60  ? 6   GLN D CB  1 
ATOM   1643 C CG  . GLN B 2 7   ? 9.725   6.637   11.952  1.00 57.59  ? 6   GLN D CG  1 
ATOM   1644 C CD  . GLN B 2 7   ? 10.775  7.637   12.421  1.00 54.42  ? 6   GLN D CD  1 
ATOM   1645 O OE1 . GLN B 2 7   ? 10.539  8.842   12.394  1.00 57.15  ? 6   GLN D OE1 1 
ATOM   1646 N NE2 . GLN B 2 7   ? 11.941  7.148   12.830  1.00 52.02  ? 6   GLN D NE2 1 
ATOM   1647 N N   . SER B 2 8   ? 7.396   4.137   10.803  1.00 64.41  ? 7   SER D N   1 
ATOM   1648 C CA  . SER B 2 8   ? 7.189   2.806   11.352  1.00 61.96  ? 7   SER D CA  1 
ATOM   1649 C C   . SER B 2 8   ? 8.500   2.036   11.331  1.00 60.87  ? 7   SER D C   1 
ATOM   1650 O O   . SER B 2 8   ? 9.366   2.316   10.496  1.00 61.83  ? 7   SER D O   1 
ATOM   1651 C CB  . SER B 2 8   ? 6.143   2.024   10.551  1.00 62.23  ? 7   SER D CB  1 
ATOM   1652 O OG  . SER B 2 8   ? 6.654   0.739   10.230  1.00 63.33  ? 7   SER D OG  1 
ATOM   1653 N N   . PRO B 2 9   ? 8.698   1.085   12.267  1.00 61.34  ? 8   PRO D N   1 
ATOM   1654 C CA  . PRO B 2 9   ? 7.917   0.825   13.492  1.00 61.58  ? 8   PRO D CA  1 
ATOM   1655 C C   . PRO B 2 9   ? 8.383   1.720   14.623  1.00 60.93  ? 8   PRO D C   1 
ATOM   1656 O O   . PRO B 2 9   ? 9.568   2.056   14.682  1.00 58.86  ? 8   PRO D O   1 
ATOM   1657 C CB  . PRO B 2 9   ? 8.220   -0.653  13.784  1.00 57.62  ? 8   PRO D CB  1 
ATOM   1658 C CG  . PRO B 2 9   ? 9.663   -0.784  13.356  1.00 57.20  ? 8   PRO D CG  1 
ATOM   1659 C CD  . PRO B 2 9   ? 9.723   0.039   12.064  1.00 60.31  ? 8   PRO D CD  1 
ATOM   1660 N N   . SER B 2 10  ? 7.482   2.098   15.538  1.00 64.53  ? 9   SER D N   1 
ATOM   1661 C CA  . SER B 2 10  ? 7.866   2.927   16.676  1.00 64.66  ? 9   SER D CA  1 
ATOM   1662 C C   . SER B 2 10  ? 8.931   2.266   17.539  1.00 61.97  ? 9   SER D C   1 
ATOM   1663 O O   . SER B 2 10  ? 9.621   2.961   18.299  1.00 61.88  ? 9   SER D O   1 
ATOM   1664 C CB  . SER B 2 10  ? 6.648   3.234   17.549  1.00 71.28  ? 9   SER D CB  1 
ATOM   1665 O OG  . SER B 2 10  ? 5.462   3.338   16.781  1.00 79.98  ? 9   SER D OG  1 
ATOM   1666 N N   . SER B 2 11  ? 9.090   0.947   17.435  1.00 59.69  ? 10  SER D N   1 
ATOM   1667 C CA  . SER B 2 11  ? 9.917   0.211   18.374  1.00 57.93  ? 10  SER D CA  1 
ATOM   1668 C C   . SER B 2 11  ? 10.459  -1.051  17.719  1.00 52.86  ? 10  SER D C   1 
ATOM   1669 O O   . SER B 2 11  ? 9.722   -1.749  17.024  1.00 53.62  ? 10  SER D O   1 
ATOM   1670 C CB  . SER B 2 11  ? 9.087   -0.145  19.609  1.00 56.61  ? 10  SER D CB  1 
ATOM   1671 O OG  . SER B 2 11  ? 9.913   -0.191  20.748  1.00 57.09  ? 10  SER D OG  1 
ATOM   1672 N N   . LEU B 2 12  ? 11.728  -1.366  17.979  1.00 51.75  ? 11  LEU D N   1 
ATOM   1673 C CA  . LEU B 2 12  ? 12.364  -2.534  17.380  1.00 51.26  ? 11  LEU D CA  1 
ATOM   1674 C C   . LEU B 2 12  ? 13.343  -3.216  18.320  1.00 50.94  ? 11  LEU D C   1 
ATOM   1675 O O   . LEU B 2 12  ? 14.343  -2.612  18.700  1.00 53.04  ? 11  LEU D O   1 
ATOM   1676 C CB  . LEU B 2 12  ? 13.079  -2.124  16.109  1.00 51.69  ? 11  LEU D CB  1 
ATOM   1677 C CG  . LEU B 2 12  ? 12.901  -3.267  15.141  1.00 52.52  ? 11  LEU D CG  1 
ATOM   1678 C CD1 . LEU B 2 12  ? 11.417  -3.620  15.104  1.00 53.58  ? 11  LEU D CD1 1 
ATOM   1679 C CD2 . LEU B 2 12  ? 13.359  -2.787  13.792  1.00 55.27  ? 11  LEU D CD2 1 
ATOM   1680 N N   . SER B 2 13  ? 13.094  -4.480  18.660  1.00 51.87  ? 12  SER D N   1 
ATOM   1681 C CA  . SER B 2 13  ? 14.067  -5.278  19.407  1.00 52.21  ? 12  SER D CA  1 
ATOM   1682 C C   . SER B 2 13  ? 14.966  -6.012  18.431  1.00 50.64  ? 12  SER D C   1 
ATOM   1683 O O   . SER B 2 13  ? 14.482  -6.558  17.436  1.00 51.75  ? 12  SER D O   1 
ATOM   1684 C CB  . SER B 2 13  ? 13.412  -6.287  20.363  1.00 53.18  ? 12  SER D CB  1 
ATOM   1685 O OG  . SER B 2 13  ? 13.099  -5.669  21.599  1.00 53.95  ? 12  SER D OG  1 
ATOM   1686 N N   . ALA B 2 14  ? 16.265  -6.028  18.716  1.00 49.56  ? 13  ALA D N   1 
ATOM   1687 C CA  . ALA B 2 14  ? 17.193  -6.658  17.795  1.00 48.61  ? 13  ALA D CA  1 
ATOM   1688 C C   . ALA B 2 14  ? 18.508  -6.938  18.498  1.00 47.91  ? 13  ALA D C   1 
ATOM   1689 O O   . ALA B 2 14  ? 18.758  -6.458  19.600  1.00 49.95  ? 13  ALA D O   1 
ATOM   1690 C CB  . ALA B 2 14  ? 17.414  -5.788  16.558  1.00 51.00  ? 13  ALA D CB  1 
ATOM   1691 N N   . SER B 2 15  ? 19.360  -7.703  17.821  1.00 47.27  ? 14  SER D N   1 
ATOM   1692 C CA  . SER B 2 15  ? 20.653  -8.134  18.318  1.00 46.67  ? 14  SER D CA  1 
ATOM   1693 C C   . SER B 2 15  ? 21.753  -7.561  17.441  1.00 45.12  ? 14  SER D C   1 
ATOM   1694 O O   . SER B 2 15  ? 21.502  -7.046  16.358  1.00 47.67  ? 14  SER D O   1 
ATOM   1695 C CB  . SER B 2 15  ? 20.755  -9.657  18.334  1.00 49.78  ? 14  SER D CB  1 
ATOM   1696 O OG  . SER B 2 15  ? 19.489  -10.227 18.599  1.00 55.26  ? 14  SER D OG  1 
ATOM   1697 N N   . VAL B 2 16  ? 22.986  -7.648  17.940  1.00 45.64  ? 15  VAL D N   1 
ATOM   1698 C CA  . VAL B 2 16  ? 24.166  -7.250  17.185  1.00 43.16  ? 15  VAL D CA  1 
ATOM   1699 C C   . VAL B 2 16  ? 24.275  -8.114  15.937  1.00 49.23  ? 15  VAL D C   1 
ATOM   1700 O O   . VAL B 2 16  ? 23.871  -9.285  15.941  1.00 49.89  ? 15  VAL D O   1 
ATOM   1701 C CB  . VAL B 2 16  ? 25.408  -7.379  18.085  1.00 42.75  ? 15  VAL D CB  1 
ATOM   1702 C CG1 . VAL B 2 16  ? 26.675  -7.508  17.287  1.00 44.14  ? 15  VAL D CG1 1 
ATOM   1703 C CG2 . VAL B 2 16  ? 25.514  -6.203  19.002  1.00 45.49  ? 15  VAL D CG2 1 
ATOM   1704 N N   . GLY B 2 17  ? 24.793  -7.533  14.845  1.00 48.28  ? 16  GLY D N   1 
ATOM   1705 C CA  . GLY B 2 17  ? 24.941  -8.241  13.592  1.00 44.39  ? 16  GLY D CA  1 
ATOM   1706 C C   . GLY B 2 17  ? 23.681  -8.333  12.762  1.00 47.22  ? 16  GLY D C   1 
ATOM   1707 O O   . GLY B 2 17  ? 23.769  -8.604  11.551  1.00 48.39  ? 16  GLY D O   1 
ATOM   1708 N N   . ASP B 2 18  ? 22.516  -8.108  13.360  1.00 44.13  ? 17  ASP D N   1 
ATOM   1709 C CA  . ASP B 2 18  ? 21.270  -8.122  12.617  1.00 50.25  ? 17  ASP D CA  1 
ATOM   1710 C C   . ASP B 2 18  ? 21.224  -7.014  11.567  1.00 50.71  ? 17  ASP D C   1 
ATOM   1711 O O   . ASP B 2 18  ? 22.015  -6.070  11.580  1.00 49.68  ? 17  ASP D O   1 
ATOM   1712 C CB  . ASP B 2 18  ? 20.098  -7.959  13.557  1.00 49.99  ? 17  ASP D CB  1 
ATOM   1713 C CG  . ASP B 2 18  ? 19.817  -9.199  14.323  1.00 57.87  ? 17  ASP D CG  1 
ATOM   1714 O OD1 . ASP B 2 18  ? 20.607  -10.172 14.189  1.00 60.44  ? 17  ASP D OD1 1 
ATOM   1715 O OD2 . ASP B 2 18  ? 18.782  -9.203  15.027  1.00 58.47  ? 17  ASP D OD2 1 
ATOM   1716 N N   . ARG B 2 19  ? 20.243  -7.115  10.674  1.00 49.41  ? 18  ARG D N   1 
ATOM   1717 C CA  . ARG B 2 19  ? 20.067  -6.158  9.582   1.00 46.15  ? 18  ARG D CA  1 
ATOM   1718 C C   . ARG B 2 19  ? 18.706  -5.503  9.730   1.00 45.08  ? 18  ARG D C   1 
ATOM   1719 O O   . ARG B 2 19  ? 17.682  -6.149  9.508   1.00 49.41  ? 18  ARG D O   1 
ATOM   1720 C CB  . ARG B 2 19  ? 20.169  -6.856  8.233   1.00 47.59  ? 18  ARG D CB  1 
ATOM   1721 C CG  . ARG B 2 19  ? 20.571  -5.996  7.097   1.00 42.60  ? 18  ARG D CG  1 
ATOM   1722 C CD  . ARG B 2 19  ? 20.052  -6.559  5.779   1.00 42.72  ? 18  ARG D CD  1 
ATOM   1723 N NE  . ARG B 2 19  ? 20.897  -6.111  4.682   1.00 43.85  ? 18  ARG D NE  1 
ATOM   1724 C CZ  . ARG B 2 19  ? 20.484  -5.313  3.704   1.00 45.87  ? 18  ARG D CZ  1 
ATOM   1725 N NH1 . ARG B 2 19  ? 19.201  -5.018  3.545   1.00 45.10  ? 18  ARG D NH1 1 
ATOM   1726 N NH2 . ARG B 2 19  ? 21.383  -4.773  2.884   1.00 44.95  ? 18  ARG D NH2 1 
ATOM   1727 N N   . VAL B 2 20  ? 18.685  -4.218  10.044  1.00 45.68  ? 19  VAL D N   1 
ATOM   1728 C CA  . VAL B 2 20  ? 17.473  -3.519  10.458  1.00 48.84  ? 19  VAL D CA  1 
ATOM   1729 C C   . VAL B 2 20  ? 17.030  -2.561  9.355   1.00 44.71  ? 19  VAL D C   1 
ATOM   1730 O O   . VAL B 2 20  ? 17.882  -1.987  8.675   1.00 44.34  ? 19  VAL D O   1 
ATOM   1731 C CB  . VAL B 2 20  ? 17.771  -2.779  11.775  1.00 46.46  ? 19  VAL D CB  1 
ATOM   1732 C CG1 . VAL B 2 20  ? 16.516  -2.472  12.511  1.00 49.35  ? 19  VAL D CG1 1 
ATOM   1733 C CG2 . VAL B 2 20  ? 18.677  -3.636  12.643  1.00 48.28  ? 19  VAL D CG2 1 
ATOM   1734 N N   . THR B 2 21  ? 15.708  -2.394  9.152   1.00 44.94  ? 20  THR D N   1 
ATOM   1735 C CA  . THR B 2 21  ? 15.223  -1.353  8.238   1.00 48.01  ? 20  THR D CA  1 
ATOM   1736 C C   . THR B 2 21  ? 14.045  -0.602  8.859   1.00 50.35  ? 20  THR D C   1 
ATOM   1737 O O   . THR B 2 21  ? 13.027  -1.208  9.202   1.00 51.94  ? 20  THR D O   1 
ATOM   1738 C CB  . THR B 2 21  ? 14.774  -1.885  6.854   1.00 49.80  ? 20  THR D CB  1 
ATOM   1739 O OG1 . THR B 2 21  ? 13.341  -1.947  6.771   1.00 48.19  ? 20  THR D OG1 1 
ATOM   1740 C CG2 . THR B 2 21  ? 15.284  -3.298  6.614   1.00 51.55  ? 20  THR D CG2 1 
ATOM   1741 N N   . ILE B 2 22  ? 14.160  0.723   8.920   1.00 49.40  ? 21  ILE D N   1 
ATOM   1742 C CA  . ILE B 2 22  ? 13.123  1.652   9.361   1.00 50.96  ? 21  ILE D CA  1 
ATOM   1743 C C   . ILE B 2 22  ? 12.567  2.374   8.146   1.00 52.98  ? 21  ILE D C   1 
ATOM   1744 O O   . ILE B 2 22  ? 13.303  2.635   7.186   1.00 51.26  ? 21  ILE D O   1 
ATOM   1745 C CB  . ILE B 2 22  ? 13.716  2.650   10.371  1.00 47.42  ? 21  ILE D CB  1 
ATOM   1746 C CG1 . ILE B 2 22  ? 14.558  1.891   11.413  1.00 50.28  ? 21  ILE D CG1 1 
ATOM   1747 C CG2 . ILE B 2 22  ? 12.633  3.532   10.933  1.00 51.79  ? 21  ILE D CG2 1 
ATOM   1748 C CD1 . ILE B 2 22  ? 15.264  2.758   12.451  1.00 50.99  ? 21  ILE D CD1 1 
ATOM   1749 N N   . THR B 2 23  ? 11.271  2.717   8.177   1.00 52.15  ? 22  THR D N   1 
ATOM   1750 C CA  . THR B 2 23  ? 10.602  3.261   6.997   1.00 54.75  ? 22  THR D CA  1 
ATOM   1751 C C   . THR B 2 23  ? 9.797   4.506   7.327   1.00 60.07  ? 22  THR D C   1 
ATOM   1752 O O   . THR B 2 23  ? 9.031   4.532   8.299   1.00 60.62  ? 22  THR D O   1 
ATOM   1753 C CB  . THR B 2 23  ? 9.699   2.212   6.327   1.00 57.93  ? 22  THR D CB  1 
ATOM   1754 O OG1 . THR B 2 23  ? 10.506  1.151   5.802   1.00 56.87  ? 22  THR D OG1 1 
ATOM   1755 C CG2 . THR B 2 23  ? 8.868   2.822   5.191   1.00 59.36  ? 22  THR D CG2 1 
ATOM   1756 N N   . CYS B 2 24  ? 9.978   5.531   6.496   1.00 64.42  ? 23  CYS D N   1 
ATOM   1757 C CA  . CYS B 2 24  ? 9.300   6.815   6.616   1.00 66.25  ? 23  CYS D CA  1 
ATOM   1758 C C   . CYS B 2 24  ? 8.511   7.078   5.331   1.00 65.53  ? 23  CYS D C   1 
ATOM   1759 O O   . CYS B 2 24  ? 9.038   6.904   4.230   1.00 64.68  ? 23  CYS D O   1 
ATOM   1760 C CB  . CYS B 2 24  ? 10.331  7.917   6.891   1.00 63.74  ? 23  CYS D CB  1 
ATOM   1761 S SG  . CYS B 2 24  ? 9.674   9.453   7.536   1.00 71.32  ? 23  CYS D SG  1 
ATOM   1762 N N   . ARG B 2 25  ? 7.241   7.443   5.476   1.00 66.49  ? 24  ARG D N   1 
ATOM   1763 C CA  . ARG B 2 25  ? 6.363   7.787   4.366   1.00 66.88  ? 24  ARG D CA  1 
ATOM   1764 C C   . ARG B 2 25  ? 6.073   9.282   4.424   1.00 75.40  ? 24  ARG D C   1 
ATOM   1765 O O   . ARG B 2 25  ? 5.483   9.770   5.396   1.00 78.06  ? 24  ARG D O   1 
ATOM   1766 C CB  . ARG B 2 25  ? 5.064   6.989   4.437   1.00 69.46  ? 24  ARG D CB  1 
ATOM   1767 C CG  . ARG B 2 25  ? 3.831   7.746   3.940   1.00 73.16  ? 24  ARG D CG  1 
ATOM   1768 C CD  . ARG B 2 25  ? 2.690   6.811   3.563   1.00 77.45  ? 24  ARG D CD  1 
ATOM   1769 N NE  . ARG B 2 25  ? 3.037   5.930   2.447   1.00 80.13  ? 24  ARG D NE  1 
ATOM   1770 C CZ  . ARG B 2 25  ? 2.719   4.642   2.393   1.00 75.58  ? 24  ARG D CZ  1 
ATOM   1771 N NH1 . ARG B 2 25  ? 2.072   4.048   3.386   1.00 72.96  ? 24  ARG D NH1 1 
ATOM   1772 N NH2 . ARG B 2 25  ? 3.063   3.931   1.321   1.00 69.25  ? 24  ARG D NH2 1 
ATOM   1773 N N   . ALA B 2 26  ? 6.493   10.006  3.392   1.00 77.09  ? 25  ALA D N   1 
ATOM   1774 C CA  . ALA B 2 26  ? 6.293   11.444  3.296   1.00 76.79  ? 25  ALA D CA  1 
ATOM   1775 C C   . ALA B 2 26  ? 5.348   11.758  2.148   1.00 75.62  ? 25  ALA D C   1 
ATOM   1776 O O   . ALA B 2 26  ? 5.197   10.967  1.216   1.00 76.29  ? 25  ALA D O   1 
ATOM   1777 C CB  . ALA B 2 26  ? 7.623   12.172  3.075   1.00 75.27  ? 25  ALA D CB  1 
ATOM   1778 N N   . SER B 2 27  ? 4.720   12.930  2.217   1.00 80.68  ? 26  SER D N   1 
ATOM   1779 C CA  . SER B 2 27  ? 3.881   13.385  1.112   1.00 82.64  ? 26  SER D CA  1 
ATOM   1780 C C   . SER B 2 27  ? 4.709   13.674  -0.134  1.00 83.67  ? 26  SER D C   1 
ATOM   1781 O O   . SER B 2 27  ? 4.325   13.280  -1.240  1.00 84.04  ? 26  SER D O   1 
ATOM   1782 C CB  . SER B 2 27  ? 3.110   14.634  1.522   1.00 84.22  ? 26  SER D CB  1 
ATOM   1783 O OG  . SER B 2 27  ? 3.993   15.579  2.105   1.00 83.48  ? 26  SER D OG  1 
ATOM   1784 N N   . GLN B 2 28  ? 5.837   14.370  0.022   1.00 79.20  ? 27  GLN D N   1 
ATOM   1785 C CA  . GLN B 2 28  ? 6.674   14.745  -1.113  1.00 75.36  ? 27  GLN D CA  1 
ATOM   1786 C C   . GLN B 2 28  ? 7.568   13.598  -1.553  1.00 69.28  ? 27  GLN D C   1 
ATOM   1787 O O   . GLN B 2 28  ? 7.961   12.754  -0.753  1.00 69.49  ? 27  GLN D O   1 
ATOM   1788 C CB  . GLN B 2 28  ? 7.545   15.955  -0.779  1.00 73.85  ? 27  GLN D CB  1 
ATOM   1789 C CG  . GLN B 2 28  ? 6.758   17.176  -0.371  1.00 78.30  ? 27  GLN D CG  1 
ATOM   1790 C CD  . GLN B 2 28  ? 5.815   17.655  -1.466  1.00 80.85  ? 27  GLN D CD  1 
ATOM   1791 O OE1 . GLN B 2 28  ? 6.206   18.422  -2.359  1.00 80.64  ? 27  GLN D OE1 1 
ATOM   1792 N NE2 . GLN B 2 28  ? 4.554   17.214  -1.391  1.00 80.28  ? 27  GLN D NE2 1 
ATOM   1793 N N   . SER B 2 29  ? 7.891   13.579  -2.848  1.00 67.54  ? 28  SER D N   1 
ATOM   1794 C CA  . SER B 2 29  ? 8.804   12.588  -3.412  1.00 63.09  ? 28  SER D CA  1 
ATOM   1795 C C   . SER B 2 29  ? 10.184  13.164  -3.685  1.00 60.75  ? 28  SER D C   1 
ATOM   1796 O O   . SER B 2 29  ? 10.991  12.508  -4.354  1.00 60.69  ? 28  SER D O   1 
ATOM   1797 C CB  . SER B 2 29  ? 8.251   11.996  -4.720  1.00 62.88  ? 28  SER D CB  1 
ATOM   1798 O OG  . SER B 2 29  ? 6.830   11.894  -4.727  1.00 64.00  ? 28  SER D OG  1 
ATOM   1799 N N   . VAL B 2 30  ? 10.467  14.380  -3.223  1.00 61.14  ? 29  VAL D N   1 
ATOM   1800 C CA  . VAL B 2 30  ? 11.764  14.981  -3.508  1.00 57.89  ? 29  VAL D CA  1 
ATOM   1801 C C   . VAL B 2 30  ? 12.826  14.295  -2.668  1.00 55.02  ? 29  VAL D C   1 
ATOM   1802 O O   . VAL B 2 30  ? 12.809  14.363  -1.435  1.00 56.48  ? 29  VAL D O   1 
ATOM   1803 C CB  . VAL B 2 30  ? 11.750  16.487  -3.244  1.00 56.59  ? 29  VAL D CB  1 
ATOM   1804 C CG1 . VAL B 2 30  ? 13.130  17.056  -3.531  1.00 53.75  ? 29  VAL D CG1 1 
ATOM   1805 C CG2 . VAL B 2 30  ? 10.691  17.156  -4.099  1.00 59.05  ? 29  VAL D CG2 1 
ATOM   1806 N N   . SER B 2 31  ? 13.766  13.638  -3.326  1.00 52.17  ? 30  SER D N   1 
ATOM   1807 C CA  . SER B 2 31  ? 14.780  12.973  -2.531  1.00 54.80  ? 30  SER D CA  1 
ATOM   1808 C C   . SER B 2 31  ? 15.667  13.971  -1.794  1.00 52.22  ? 30  SER D C   1 
ATOM   1809 O O   . SER B 2 31  ? 16.269  13.615  -0.776  1.00 53.16  ? 30  SER D O   1 
ATOM   1810 C CB  . SER B 2 31  ? 15.630  12.034  -3.395  1.00 50.84  ? 30  SER D CB  1 
ATOM   1811 O OG  . SER B 2 31  ? 16.951  12.525  -3.504  1.00 50.00  ? 30  SER D OG  1 
ATOM   1812 N N   . SER B 2 32  ? 15.736  15.217  -2.251  1.00 52.24  ? 31  SER D N   1 
ATOM   1813 C CA  . SER B 2 32  ? 16.659  16.173  -1.635  1.00 55.35  ? 31  SER D CA  1 
ATOM   1814 C C   . SER B 2 32  ? 16.260  16.541  -0.210  1.00 52.08  ? 31  SER D C   1 
ATOM   1815 O O   . SER B 2 32  ? 17.129  16.841  0.615   1.00 49.98  ? 31  SER D O   1 
ATOM   1816 C CB  . SER B 2 32  ? 16.758  17.431  -2.503  1.00 53.94  ? 31  SER D CB  1 
ATOM   1817 O OG  . SER B 2 32  ? 16.766  17.056  -3.870  1.00 55.74  ? 31  SER D OG  1 
ATOM   1818 N N   . ALA B 2 33  ? 14.969  16.468  0.100   1.00 51.79  ? 32  ALA D N   1 
ATOM   1819 C CA  . ALA B 2 33  ? 14.350  17.051  1.276   1.00 53.23  ? 32  ALA D CA  1 
ATOM   1820 C C   . ALA B 2 33  ? 14.446  16.186  2.531   1.00 58.00  ? 32  ALA D C   1 
ATOM   1821 O O   . ALA B 2 33  ? 14.057  16.648  3.618   1.00 56.54  ? 32  ALA D O   1 
ATOM   1822 C CB  . ALA B 2 33  ? 12.879  17.329  0.967   1.00 57.48  ? 32  ALA D CB  1 
ATOM   1823 N N   . VAL B 2 34  ? 14.948  14.955  2.421   1.00 55.11  ? 33  VAL D N   1 
ATOM   1824 C CA  . VAL B 2 34  ? 14.823  13.951  3.471   1.00 50.13  ? 33  VAL D CA  1 
ATOM   1825 C C   . VAL B 2 34  ? 16.199  13.655  4.044   1.00 49.74  ? 33  VAL D C   1 
ATOM   1826 O O   . VAL B 2 34  ? 17.156  13.447  3.287   1.00 48.14  ? 33  VAL D O   1 
ATOM   1827 C CB  . VAL B 2 34  ? 14.170  12.668  2.939   1.00 47.91  ? 33  VAL D CB  1 
ATOM   1828 C CG1 . VAL B 2 34  ? 14.439  11.531  3.874   1.00 49.32  ? 33  VAL D CG1 1 
ATOM   1829 C CG2 . VAL B 2 34  ? 12.677  12.856  2.776   1.00 49.23  ? 33  VAL D CG2 1 
ATOM   1830 N N   . ALA B 2 35  ? 16.302  13.646  5.381   1.00 48.02  ? 34  ALA D N   1 
ATOM   1831 C CA  . ALA B 2 35  ? 17.478  13.118  6.065   1.00 45.38  ? 34  ALA D CA  1 
ATOM   1832 C C   . ALA B 2 35  ? 17.054  12.204  7.213   1.00 48.20  ? 34  ALA D C   1 
ATOM   1833 O O   . ALA B 2 35  ? 15.873  12.110  7.572   1.00 50.35  ? 34  ALA D O   1 
ATOM   1834 C CB  . ALA B 2 35  ? 18.375  14.236  6.604   1.00 44.53  ? 34  ALA D CB  1 
ATOM   1835 N N   . TRP B 2 36  ? 18.039  11.549  7.821   1.00 44.29  ? 35  TRP D N   1 
ATOM   1836 C CA  . TRP B 2 36  ? 17.812  10.732  8.996   1.00 45.51  ? 35  TRP D CA  1 
ATOM   1837 C C   . TRP B 2 36  ? 18.771  11.165  10.094  1.00 45.91  ? 35  TRP D C   1 
ATOM   1838 O O   . TRP B 2 36  ? 19.933  11.501  9.808   1.00 44.11  ? 35  TRP D O   1 
ATOM   1839 C CB  . TRP B 2 36  ? 18.038  9.268   8.701   1.00 41.47  ? 35  TRP D CB  1 
ATOM   1840 C CG  . TRP B 2 36  ? 17.038  8.689   7.808   1.00 44.50  ? 35  TRP D CG  1 
ATOM   1841 C CD1 . TRP B 2 36  ? 17.130  8.597   6.461   1.00 46.11  ? 35  TRP D CD1 1 
ATOM   1842 C CD2 . TRP B 2 36  ? 15.800  8.066   8.168   1.00 47.01  ? 35  TRP D CD2 1 
ATOM   1843 N NE1 . TRP B 2 36  ? 16.021  7.982   5.947   1.00 44.58  ? 35  TRP D NE1 1 
ATOM   1844 C CE2 . TRP B 2 36  ? 15.193  7.630   6.974   1.00 47.33  ? 35  TRP D CE2 1 
ATOM   1845 C CE3 . TRP B 2 36  ? 15.154  7.814   9.378   1.00 49.50  ? 35  TRP D CE3 1 
ATOM   1846 C CZ2 . TRP B 2 36  ? 13.962  6.968   6.950   1.00 50.49  ? 35  TRP D CZ2 1 
ATOM   1847 C CZ3 . TRP B 2 36  ? 13.915  7.148   9.352   1.00 51.57  ? 35  TRP D CZ3 1 
ATOM   1848 C CH2 . TRP B 2 36  ? 13.336  6.744   8.144   1.00 51.38  ? 35  TRP D CH2 1 
ATOM   1849 N N   . TYR B 2 37  ? 18.296  11.113  11.358  1.00 42.24  ? 36  TYR D N   1 
ATOM   1850 C CA  . TYR B 2 37  ? 19.160  11.363  12.502  1.00 41.98  ? 36  TYR D CA  1 
ATOM   1851 C C   . TYR B 2 37  ? 19.095  10.216  13.497  1.00 45.32  ? 36  TYR D C   1 
ATOM   1852 O O   . TYR B 2 37  ? 18.073  9.534   13.636  1.00 45.76  ? 36  TYR D O   1 
ATOM   1853 C CB  . TYR B 2 37  ? 18.806  12.679  13.246  1.00 44.80  ? 36  TYR D CB  1 
ATOM   1854 C CG  . TYR B 2 37  ? 18.762  13.853  12.309  1.00 45.66  ? 36  TYR D CG  1 
ATOM   1855 C CD1 . TYR B 2 37  ? 17.600  14.152  11.609  1.00 45.84  ? 36  TYR D CD1 1 
ATOM   1856 C CD2 . TYR B 2 37  ? 19.894  14.597  12.047  1.00 43.26  ? 36  TYR D CD2 1 
ATOM   1857 C CE1 . TYR B 2 37  ? 17.561  15.164  10.705  1.00 43.98  ? 36  TYR D CE1 1 
ATOM   1858 C CE2 . TYR B 2 37  ? 19.866  15.610  11.150  1.00 43.44  ? 36  TYR D CE2 1 
ATOM   1859 C CZ  . TYR B 2 37  ? 18.690  15.897  10.479  1.00 46.01  ? 36  TYR D CZ  1 
ATOM   1860 O OH  . TYR B 2 37  ? 18.622  16.940  9.583   1.00 48.89  ? 36  TYR D OH  1 
ATOM   1861 N N   . GLN B 2 38  ? 20.203  10.038  14.210  1.00 43.37  ? 37  GLN D N   1 
ATOM   1862 C CA  . GLN B 2 38  ? 20.289  9.160   15.366  1.00 43.04  ? 37  GLN D CA  1 
ATOM   1863 C C   . GLN B 2 38  ? 20.442  9.994   16.622  1.00 43.74  ? 37  GLN D C   1 
ATOM   1864 O O   . GLN B 2 38  ? 21.289  10.891  16.669  1.00 45.03  ? 37  GLN D O   1 
ATOM   1865 C CB  . GLN B 2 38  ? 21.479  8.215   15.237  1.00 45.08  ? 37  GLN D CB  1 
ATOM   1866 C CG  . GLN B 2 38  ? 21.796  7.370   16.462  1.00 43.59  ? 37  GLN D CG  1 
ATOM   1867 C CD  . GLN B 2 38  ? 23.161  6.714   16.312  1.00 43.59  ? 37  GLN D CD  1 
ATOM   1868 O OE1 . GLN B 2 38  ? 24.195  7.390   16.381  1.00 46.16  ? 37  GLN D OE1 1 
ATOM   1869 N NE2 . GLN B 2 38  ? 23.175  5.406   16.084  1.00 40.21  ? 37  GLN D NE2 1 
ATOM   1870 N N   . GLN B 2 39  ? 19.640  9.680   17.641  1.00 47.35  ? 38  GLN D N   1 
ATOM   1871 C CA  . GLN B 2 39  ? 19.694  10.316  18.954  1.00 43.74  ? 38  GLN D CA  1 
ATOM   1872 C C   . GLN B 2 39  ? 19.737  9.234   20.031  1.00 44.36  ? 38  GLN D C   1 
ATOM   1873 O O   . GLN B 2 39  ? 18.883  8.340   20.045  1.00 44.85  ? 38  GLN D O   1 
ATOM   1874 C CB  . GLN B 2 39  ? 18.473  11.217  19.160  1.00 44.82  ? 38  GLN D CB  1 
ATOM   1875 C CG  . GLN B 2 39  ? 18.652  12.363  20.165  1.00 45.24  ? 38  GLN D CG  1 
ATOM   1876 C CD  . GLN B 2 39  ? 17.304  12.925  20.608  1.00 46.53  ? 38  GLN D CD  1 
ATOM   1877 O OE1 . GLN B 2 39  ? 16.262  12.304  20.346  1.00 47.16  ? 38  GLN D OE1 1 
ATOM   1878 N NE2 . GLN B 2 39  ? 17.309  14.076  21.289  1.00 47.02  ? 38  GLN D NE2 1 
ATOM   1879 N N   . LYS B 2 40  ? 20.764  9.296   20.920  1.00 44.79  ? 39  LYS D N   1 
ATOM   1880 C CA  . LYS B 2 40  ? 20.933  8.647   22.218  1.00 44.13  ? 39  LYS D CA  1 
ATOM   1881 C C   . LYS B 2 40  ? 20.414  9.563   23.321  1.00 45.96  ? 39  LYS D C   1 
ATOM   1882 O O   . LYS B 2 40  ? 20.350  10.785  23.138  1.00 46.74  ? 39  LYS D O   1 
ATOM   1883 C CB  . LYS B 2 40  ? 22.415  8.347   22.457  1.00 43.24  ? 39  LYS D CB  1 
ATOM   1884 C CG  . LYS B 2 40  ? 23.088  7.751   21.255  1.00 42.26  ? 39  LYS D CG  1 
ATOM   1885 C CD  . LYS B 2 40  ? 23.614  6.351   21.481  1.00 42.04  ? 39  LYS D CD  1 
ATOM   1886 C CE  . LYS B 2 40  ? 24.741  6.048   20.508  1.00 42.87  ? 39  LYS D CE  1 
ATOM   1887 N NZ  . LYS B 2 40  ? 25.659  5.013   21.015  1.00 45.51  ? 39  LYS D NZ  1 
ATOM   1888 N N   . PRO B 2 41  ? 20.087  9.040   24.512  1.00 48.94  ? 40  PRO D N   1 
ATOM   1889 C CA  . PRO B 2 41  ? 19.431  9.891   25.525  1.00 46.77  ? 40  PRO D CA  1 
ATOM   1890 C C   . PRO B 2 41  ? 20.376  10.940  26.084  1.00 46.66  ? 40  PRO D C   1 
ATOM   1891 O O   . PRO B 2 41  ? 21.559  10.672  26.310  1.00 48.37  ? 40  PRO D O   1 
ATOM   1892 C CB  . PRO B 2 41  ? 19.014  8.889   26.608  1.00 47.57  ? 40  PRO D CB  1 
ATOM   1893 C CG  . PRO B 2 41  ? 19.038  7.567   25.932  1.00 47.23  ? 40  PRO D CG  1 
ATOM   1894 C CD  . PRO B 2 41  ? 20.242  7.677   25.029  1.00 45.91  ? 40  PRO D CD  1 
ATOM   1895 N N   . GLY B 2 42  ? 19.842  12.146  26.308  1.00 47.39  ? 41  GLY D N   1 
ATOM   1896 C CA  . GLY B 2 42  ? 20.644  13.266  26.766  1.00 46.91  ? 41  GLY D CA  1 
ATOM   1897 C C   . GLY B 2 42  ? 21.560  13.863  25.717  1.00 49.30  ? 41  GLY D C   1 
ATOM   1898 O O   . GLY B 2 42  ? 22.468  14.634  26.054  1.00 49.93  ? 41  GLY D O   1 
ATOM   1899 N N   . LYS B 2 43  ? 21.377  13.546  24.452  1.00 45.40  ? 42  LYS D N   1 
ATOM   1900 C CA  . LYS B 2 43  ? 22.326  14.027  23.477  1.00 44.46  ? 42  LYS D CA  1 
ATOM   1901 C C   . LYS B 2 43  ? 21.556  14.608  22.305  1.00 44.57  ? 42  LYS D C   1 
ATOM   1902 O O   . LYS B 2 43  ? 20.410  14.215  22.055  1.00 45.12  ? 42  LYS D O   1 
ATOM   1903 C CB  . LYS B 2 43  ? 23.262  12.901  23.050  1.00 49.63  ? 42  LYS D CB  1 
ATOM   1904 C CG  . LYS B 2 43  ? 24.047  12.274  24.197  1.00 48.21  ? 42  LYS D CG  1 
ATOM   1905 C CD  . LYS B 2 43  ? 25.116  13.239  24.718  1.00 54.28  ? 42  LYS D CD  1 
ATOM   1906 C CE  . LYS B 2 43  ? 25.754  12.736  26.032  1.00 61.47  ? 42  LYS D CE  1 
ATOM   1907 N NZ  . LYS B 2 43  ? 27.215  12.411  25.892  1.00 62.09  ? 42  LYS D NZ  1 
ATOM   1908 N N   . ALA B 2 44  ? 22.169  15.581  21.627  1.00 44.15  ? 43  ALA D N   1 
ATOM   1909 C CA  . ALA B 2 44  ? 21.536  16.154  20.456  1.00 44.65  ? 43  ALA D CA  1 
ATOM   1910 C C   . ALA B 2 44  ? 21.559  15.133  19.330  1.00 43.86  ? 43  ALA D C   1 
ATOM   1911 O O   . ALA B 2 44  ? 22.476  14.315  19.251  1.00 42.94  ? 43  ALA D O   1 
ATOM   1912 C CB  . ALA B 2 44  ? 22.244  17.421  19.996  1.00 45.60  ? 43  ALA D CB  1 
ATOM   1913 N N   . PRO B 2 45  ? 20.536  15.136  18.482  1.00 45.22  ? 44  PRO D N   1 
ATOM   1914 C CA  . PRO B 2 45  ? 20.555  14.298  17.274  1.00 43.18  ? 44  PRO D CA  1 
ATOM   1915 C C   . PRO B 2 45  ? 21.846  14.412  16.462  1.00 42.41  ? 44  PRO D C   1 
ATOM   1916 O O   . PRO B 2 45  ? 22.504  15.454  16.415  1.00 41.92  ? 44  PRO D O   1 
ATOM   1917 C CB  . PRO B 2 45  ? 19.343  14.816  16.490  1.00 43.87  ? 44  PRO D CB  1 
ATOM   1918 C CG  . PRO B 2 45  ? 18.358  15.148  17.594  1.00 45.06  ? 44  PRO D CG  1 
ATOM   1919 C CD  . PRO B 2 45  ? 19.227  15.794  18.683  1.00 45.00  ? 44  PRO D CD  1 
ATOM   1920 N N   . LYS B 2 46  ? 22.216  13.300  15.835  1.00 41.66  ? 45  LYS D N   1 
ATOM   1921 C CA  . LYS B 2 46  ? 23.315  13.255  14.883  1.00 43.80  ? 45  LYS D CA  1 
ATOM   1922 C C   . LYS B 2 46  ? 22.771  12.916  13.508  1.00 43.21  ? 45  LYS D C   1 
ATOM   1923 O O   . LYS B 2 46  ? 22.018  11.952  13.349  1.00 42.70  ? 45  LYS D O   1 
ATOM   1924 C CB  . LYS B 2 46  ? 24.372  12.227  15.273  1.00 43.79  ? 45  LYS D CB  1 
ATOM   1925 C CG  . LYS B 2 46  ? 24.621  12.236  16.761  1.00 49.04  ? 45  LYS D CG  1 
ATOM   1926 C CD  . LYS B 2 46  ? 25.935  11.552  17.146  1.00 56.78  ? 45  LYS D CD  1 
ATOM   1927 C CE  . LYS B 2 46  ? 27.142  12.279  16.541  1.00 61.02  ? 45  LYS D CE  1 
ATOM   1928 N NZ  . LYS B 2 46  ? 28.405  12.005  17.304  1.00 64.92  ? 45  LYS D NZ  1 
ATOM   1929 N N   . LEU B 2 47  ? 23.162  13.713  12.520  1.00 46.20  ? 46  LEU D N   1 
ATOM   1930 C CA  . LEU B 2 47  ? 22.819  13.416  11.137  1.00 44.81  ? 46  LEU D CA  1 
ATOM   1931 C C   . LEU B 2 47  ? 23.504  12.146  10.647  1.00 38.73  ? 46  LEU D C   1 
ATOM   1932 O O   . LEU B 2 47  ? 24.688  11.914  10.908  1.00 38.87  ? 46  LEU D O   1 
ATOM   1933 C CB  . LEU B 2 47  ? 23.187  14.619  10.264  1.00 45.30  ? 46  LEU D CB  1 
ATOM   1934 C CG  . LEU B 2 47  ? 22.970  14.498  8.758   1.00 44.44  ? 46  LEU D CG  1 
ATOM   1935 C CD1 . LEU B 2 47  ? 21.485  14.758  8.433   1.00 42.71  ? 46  LEU D CD1 1 
ATOM   1936 C CD2 . LEU B 2 47  ? 23.881  15.518  8.105   1.00 44.82  ? 46  LEU D CD2 1 
ATOM   1937 N N   . LEU B 2 48  ? 22.759  11.326  9.916   1.00 38.71  ? 47  LEU D N   1 
ATOM   1938 C CA  . LEU B 2 48  ? 23.368  10.136  9.319   1.00 43.97  ? 47  LEU D CA  1 
ATOM   1939 C C   . LEU B 2 48  ? 23.332  10.139  7.797   1.00 42.48  ? 47  LEU D C   1 
ATOM   1940 O O   . LEU B 2 48  ? 24.371  9.953   7.159   1.00 41.15  ? 47  LEU D O   1 
ATOM   1941 C CB  . LEU B 2 48  ? 22.686  8.859   9.844   1.00 41.79  ? 47  LEU D CB  1 
ATOM   1942 C CG  . LEU B 2 48  ? 22.639  8.686   11.366  1.00 42.17  ? 47  LEU D CG  1 
ATOM   1943 C CD1 . LEU B 2 48  ? 21.548  7.693   11.728  1.00 42.97  ? 47  LEU D CD1 1 
ATOM   1944 C CD2 . LEU B 2 48  ? 23.992  8.272   11.955  1.00 38.17  ? 47  LEU D CD2 1 
ATOM   1945 N N   . ILE B 2 49  ? 22.155  10.344  7.210   1.00 40.87  ? 48  ILE D N   1 
ATOM   1946 C CA  . ILE B 2 49  ? 21.907  10.286  5.780   1.00 38.00  ? 48  ILE D CA  1 
ATOM   1947 C C   . ILE B 2 49  ? 21.236  11.594  5.389   1.00 44.41  ? 48  ILE D C   1 
ATOM   1948 O O   . ILE B 2 49  ? 20.268  12.001  6.039   1.00 46.06  ? 48  ILE D O   1 
ATOM   1949 C CB  . ILE B 2 49  ? 20.979  9.110   5.431   1.00 43.10  ? 48  ILE D CB  1 
ATOM   1950 C CG1 . ILE B 2 49  ? 21.649  7.723   5.625   1.00 42.42  ? 48  ILE D CG1 1 
ATOM   1951 C CG2 . ILE B 2 49  ? 20.420  9.293   4.062   1.00 41.74  ? 48  ILE D CG2 1 
ATOM   1952 C CD1 . ILE B 2 49  ? 23.126  7.662   5.276   1.00 40.95  ? 48  ILE D CD1 1 
ATOM   1953 N N   . TYR B 2 50  ? 21.740  12.262  4.336   1.00 47.01  ? 49  TYR D N   1 
ATOM   1954 C CA  . TYR B 2 50  ? 21.095  13.467  3.808   1.00 43.48  ? 49  TYR D CA  1 
ATOM   1955 C C   . TYR B 2 50  ? 20.642  13.250  2.371   1.00 46.56  ? 49  TYR D C   1 
ATOM   1956 O O   . TYR B 2 50  ? 21.211  12.440  1.623   1.00 46.17  ? 49  TYR D O   1 
ATOM   1957 C CB  . TYR B 2 50  ? 21.997  14.701  3.849   1.00 39.59  ? 49  TYR D CB  1 
ATOM   1958 C CG  . TYR B 2 50  ? 23.313  14.562  3.152   1.00 39.41  ? 49  TYR D CG  1 
ATOM   1959 C CD1 . TYR B 2 50  ? 24.388  14.027  3.817   1.00 41.38  ? 49  TYR D CD1 1 
ATOM   1960 C CD2 . TYR B 2 50  ? 23.499  14.997  1.834   1.00 40.38  ? 49  TYR D CD2 1 
ATOM   1961 C CE1 . TYR B 2 50  ? 25.630  13.902  3.206   1.00 42.34  ? 49  TYR D CE1 1 
ATOM   1962 C CE2 . TYR B 2 50  ? 24.752  14.881  1.205   1.00 40.22  ? 49  TYR D CE2 1 
ATOM   1963 C CZ  . TYR B 2 50  ? 25.808  14.321  1.913   1.00 41.68  ? 49  TYR D CZ  1 
ATOM   1964 O OH  . TYR B 2 50  ? 27.059  14.157  1.361   1.00 45.73  ? 49  TYR D OH  1 
ATOM   1965 N N   . SER B 2 51  ? 19.615  14.008  1.997   1.00 46.74  ? 50  SER D N   1 
ATOM   1966 C CA  . SER B 2 51  ? 19.024  13.949  0.668   1.00 45.75  ? 50  SER D CA  1 
ATOM   1967 C C   . SER B 2 51  ? 18.813  12.497  0.245   1.00 43.66  ? 50  SER D C   1 
ATOM   1968 O O   . SER B 2 51  ? 19.395  12.003  -0.716  1.00 45.03  ? 50  SER D O   1 
ATOM   1969 C CB  . SER B 2 51  ? 19.879  14.706  -0.334  1.00 48.52  ? 50  SER D CB  1 
ATOM   1970 O OG  . SER B 2 51  ? 19.232  14.748  -1.598  1.00 54.47  ? 50  SER D OG  1 
ATOM   1971 N N   . ALA B 2 52  ? 17.998  11.815  1.050   1.00 44.94  ? 51  ALA D N   1 
ATOM   1972 C CA  . ALA B 2 52  ? 17.551  10.423  0.920   1.00 44.55  ? 51  ALA D CA  1 
ATOM   1973 C C   . ALA B 2 52  ? 18.651  9.371   1.012   1.00 42.30  ? 51  ALA D C   1 
ATOM   1974 O O   . ALA B 2 52  ? 18.516  8.444   1.825   1.00 44.83  ? 51  ALA D O   1 
ATOM   1975 C CB  . ALA B 2 52  ? 16.765  10.217  -0.371  1.00 44.67  ? 51  ALA D CB  1 
ATOM   1976 N N   . SER B 2 53  ? 19.741  9.494   0.231   1.00 40.83  ? 52  SER D N   1 
ATOM   1977 C CA  . SER B 2 53  ? 20.707  8.406   0.103   1.00 37.46  ? 52  SER D CA  1 
ATOM   1978 C C   . SER B 2 53  ? 22.169  8.756   0.367   1.00 36.47  ? 52  SER D C   1 
ATOM   1979 O O   . SER B 2 53  ? 23.028  7.895   0.216   1.00 35.76  ? 52  SER D O   1 
ATOM   1980 C CB  . SER B 2 53  ? 20.612  7.796   -1.298  1.00 43.56  ? 52  SER D CB  1 
ATOM   1981 O OG  . SER B 2 53  ? 20.910  8.748   -2.325  1.00 48.36  ? 52  SER D OG  1 
ATOM   1982 N N   . SER B 2 54  ? 22.509  9.964   0.754   1.00 40.80  ? 53  SER D N   1 
ATOM   1983 C CA  . SER B 2 54  ? 23.925  10.301  0.822   1.00 40.38  ? 53  SER D CA  1 
ATOM   1984 C C   . SER B 2 54  ? 24.473  10.107  2.228   1.00 40.10  ? 53  SER D C   1 
ATOM   1985 O O   . SER B 2 54  ? 23.929  10.638  3.207   1.00 40.46  ? 53  SER D O   1 
ATOM   1986 C CB  . SER B 2 54  ? 24.166  11.723  0.312   1.00 40.59  ? 53  SER D CB  1 
ATOM   1987 O OG  . SER B 2 54  ? 23.380  11.962  -0.861  1.00 41.90  ? 53  SER D OG  1 
ATOM   1988 N N   . LEU B 2 55  ? 25.549  9.340   2.318   1.00 37.03  ? 54  LEU D N   1 
ATOM   1989 C CA  . LEU B 2 55  ? 26.165  9.073   3.609   1.00 41.28  ? 54  LEU D CA  1 
ATOM   1990 C C   . LEU B 2 55  ? 26.824  10.339  4.136   1.00 40.60  ? 54  LEU D C   1 
ATOM   1991 O O   . LEU B 2 55  ? 27.849  10.767  3.604   1.00 43.94  ? 54  LEU D O   1 
ATOM   1992 C CB  . LEU B 2 55  ? 27.188  7.951   3.472   1.00 37.04  ? 54  LEU D CB  1 
ATOM   1993 C CG  . LEU B 2 55  ? 27.545  7.327   4.810   1.00 39.34  ? 54  LEU D CG  1 
ATOM   1994 C CD1 . LEU B 2 55  ? 26.402  6.448   5.234   1.00 38.10  ? 54  LEU D CD1 1 
ATOM   1995 C CD2 . LEU B 2 55  ? 28.841  6.541   4.734   1.00 38.29  ? 54  LEU D CD2 1 
ATOM   1996 N N   . TYR B 2 56  ? 26.259  10.942  5.178   1.00 37.85  ? 55  TYR D N   1 
ATOM   1997 C CA  . TYR B 2 56  ? 26.938  12.072  5.807   1.00 42.92  ? 55  TYR D CA  1 
ATOM   1998 C C   . TYR B 2 56  ? 28.323  11.654  6.256   1.00 41.35  ? 55  TYR D C   1 
ATOM   1999 O O   . TYR B 2 56  ? 28.519  10.557  6.779   1.00 41.43  ? 55  TYR D O   1 
ATOM   2000 C CB  . TYR B 2 56  ? 26.158  12.624  7.012   1.00 44.88  ? 55  TYR D CB  1 
ATOM   2001 C CG  . TYR B 2 56  ? 26.765  13.887  7.642   1.00 46.05  ? 55  TYR D CG  1 
ATOM   2002 C CD1 . TYR B 2 56  ? 26.954  15.043  6.892   1.00 46.38  ? 55  TYR D CD1 1 
ATOM   2003 C CD2 . TYR B 2 56  ? 27.094  13.938  8.997   1.00 45.92  ? 55  TYR D CD2 1 
ATOM   2004 C CE1 . TYR B 2 56  ? 27.481  16.205  7.470   1.00 46.92  ? 55  TYR D CE1 1 
ATOM   2005 C CE2 . TYR B 2 56  ? 27.619  15.100  9.578   1.00 45.65  ? 55  TYR D CE2 1 
ATOM   2006 C CZ  . TYR B 2 56  ? 27.812  16.216  8.814   1.00 46.07  ? 55  TYR D CZ  1 
ATOM   2007 O OH  . TYR B 2 56  ? 28.346  17.345  9.387   1.00 47.43  ? 55  TYR D OH  1 
ATOM   2008 N N   . SER B 2 57  ? 29.287  12.538  6.030   1.00 43.10  ? 56  SER D N   1 
ATOM   2009 C CA  . SER B 2 57  ? 30.658  12.240  6.403   1.00 43.77  ? 56  SER D CA  1 
ATOM   2010 C C   . SER B 2 57  ? 30.735  11.809  7.850   1.00 40.52  ? 56  SER D C   1 
ATOM   2011 O O   . SER B 2 57  ? 29.955  12.265  8.693   1.00 44.07  ? 56  SER D O   1 
ATOM   2012 C CB  . SER B 2 57  ? 31.564  13.449  6.229   1.00 45.89  ? 56  SER D CB  1 
ATOM   2013 O OG  . SER B 2 57  ? 32.681  13.227  7.088   1.00 50.40  ? 56  SER D OG  1 
ATOM   2014 N N   . GLY B 2 58  ? 31.712  10.953  8.126   1.00 39.89  ? 57  GLY D N   1 
ATOM   2015 C CA  . GLY B 2 58  ? 31.911  10.395  9.450   1.00 43.91  ? 57  GLY D CA  1 
ATOM   2016 C C   . GLY B 2 58  ? 31.124  9.134   9.734   1.00 41.65  ? 57  GLY D C   1 
ATOM   2017 O O   . GLY B 2 58  ? 31.651  8.232   10.377  1.00 42.19  ? 57  GLY D O   1 
ATOM   2018 N N   . VAL B 2 59  ? 29.883  9.058   9.250   1.00 40.39  ? 58  VAL D N   1 
ATOM   2019 C CA  . VAL B 2 59  ? 28.958  7.939   9.502   1.00 42.04  ? 58  VAL D CA  1 
ATOM   2020 C C   . VAL B 2 59  ? 29.502  6.639   8.908   1.00 40.71  ? 58  VAL D C   1 
ATOM   2021 O O   . VAL B 2 59  ? 30.025  6.650   7.775   1.00 41.94  ? 58  VAL D O   1 
ATOM   2022 C CB  . VAL B 2 59  ? 27.574  8.276   8.919   1.00 41.48  ? 58  VAL D CB  1 
ATOM   2023 C CG1 . VAL B 2 59  ? 26.690  7.059   8.876   1.00 40.84  ? 58  VAL D CG1 1 
ATOM   2024 C CG2 . VAL B 2 59  ? 26.904  9.378   9.762   1.00 40.40  ? 58  VAL D CG2 1 
ATOM   2025 N N   . PRO B 2 60  ? 29.374  5.495   9.593   1.00 40.85  ? 59  PRO D N   1 
ATOM   2026 C CA  . PRO B 2 60  ? 29.851  4.205   9.048   1.00 41.64  ? 59  PRO D CA  1 
ATOM   2027 C C   . PRO B 2 60  ? 29.075  3.703   7.830   1.00 41.11  ? 59  PRO D C   1 
ATOM   2028 O O   . PRO B 2 60  ? 27.887  3.987   7.644   1.00 43.73  ? 59  PRO D O   1 
ATOM   2029 C CB  . PRO B 2 60  ? 29.651  3.245   10.229  1.00 38.90  ? 59  PRO D CB  1 
ATOM   2030 C CG  . PRO B 2 60  ? 29.757  4.127   11.411  1.00 42.24  ? 59  PRO D CG  1 
ATOM   2031 C CD  . PRO B 2 60  ? 28.977  5.349   10.998  1.00 41.32  ? 59  PRO D CD  1 
ATOM   2032 N N   . SER B 2 61  ? 29.748  2.874   7.020   1.00 38.65  ? 60  SER D N   1 
ATOM   2033 C CA  . SER B 2 61  ? 29.089  2.365   5.810   1.00 42.74  ? 60  SER D CA  1 
ATOM   2034 C C   . SER B 2 61  ? 27.915  1.437   6.090   1.00 41.52  ? 60  SER D C   1 
ATOM   2035 O O   . SER B 2 61  ? 27.161  1.160   5.149   1.00 42.10  ? 60  SER D O   1 
ATOM   2036 C CB  . SER B 2 61  ? 30.052  1.607   4.871   1.00 46.11  ? 60  SER D CB  1 
ATOM   2037 O OG  . SER B 2 61  ? 31.331  2.214   4.745   1.00 49.94  ? 60  SER D OG  1 
ATOM   2038 N N   . ARG B 2 62  ? 27.731  0.936   7.325   1.00 42.07  ? 61  ARG D N   1 
ATOM   2039 C CA  . ARG B 2 62  ? 26.572  0.074   7.553   1.00 38.90  ? 61  ARG D CA  1 
ATOM   2040 C C   . ARG B 2 62  ? 25.251  0.835   7.465   1.00 42.55  ? 61  ARG D C   1 
ATOM   2041 O O   . ARG B 2 62  ? 24.186  0.201   7.476   1.00 47.81  ? 61  ARG D O   1 
ATOM   2042 C CB  . ARG B 2 62  ? 26.656  -0.634  8.894   1.00 40.48  ? 61  ARG D CB  1 
ATOM   2043 C CG  . ARG B 2 62  ? 26.784  0.269   10.110  1.00 40.94  ? 61  ARG D CG  1 
ATOM   2044 C CD  . ARG B 2 62  ? 26.885  -0.525  11.364  1.00 40.87  ? 61  ARG D CD  1 
ATOM   2045 N NE  . ARG B 2 62  ? 27.082  0.349   12.506  1.00 42.85  ? 61  ARG D NE  1 
ATOM   2046 C CZ  . ARG B 2 62  ? 28.277  0.737   12.922  1.00 44.48  ? 61  ARG D CZ  1 
ATOM   2047 N NH1 . ARG B 2 62  ? 29.374  0.432   12.243  1.00 43.74  ? 61  ARG D NH1 1 
ATOM   2048 N NH2 . ARG B 2 62  ? 28.375  1.456   14.036  1.00 45.65  ? 61  ARG D NH2 1 
ATOM   2049 N N   . PHE B 2 63  ? 25.287  2.164   7.373   1.00 37.04  ? 62  PHE D N   1 
ATOM   2050 C CA  . PHE B 2 63  ? 24.067  2.938   7.221   1.00 39.52  ? 62  PHE D CA  1 
ATOM   2051 C C   . PHE B 2 63  ? 23.807  3.242   5.747   1.00 41.26  ? 62  PHE D C   1 
ATOM   2052 O O   . PHE B 2 63  ? 24.734  3.376   4.938   1.00 42.45  ? 62  PHE D O   1 
ATOM   2053 C CB  . PHE B 2 63  ? 24.154  4.233   8.033   1.00 42.85  ? 62  PHE D CB  1 
ATOM   2054 C CG  . PHE B 2 63  ? 24.164  4.008   9.523   1.00 38.84  ? 62  PHE D CG  1 
ATOM   2055 C CD1 . PHE B 2 63  ? 22.981  3.920   10.236  1.00 38.87  ? 62  PHE D CD1 1 
ATOM   2056 C CD2 . PHE B 2 63  ? 25.363  3.848   10.200  1.00 38.05  ? 62  PHE D CD2 1 
ATOM   2057 C CE1 . PHE B 2 63  ? 22.995  3.704   11.623  1.00 39.48  ? 62  PHE D CE1 1 
ATOM   2058 C CE2 . PHE B 2 63  ? 25.388  3.643   11.583  1.00 39.18  ? 62  PHE D CE2 1 
ATOM   2059 C CZ  . PHE B 2 63  ? 24.207  3.566   12.294  1.00 38.16  ? 62  PHE D CZ  1 
ATOM   2060 N N   . SER B 2 64  ? 22.530  3.336   5.397   1.00 39.01  ? 63  SER D N   1 
ATOM   2061 C CA  . SER B 2 64  ? 22.188  3.450   3.993   1.00 37.15  ? 63  SER D CA  1 
ATOM   2062 C C   . SER B 2 64  ? 20.731  3.839   3.896   1.00 39.23  ? 63  SER D C   1 
ATOM   2063 O O   . SER B 2 64  ? 19.925  3.481   4.762   1.00 41.67  ? 63  SER D O   1 
ATOM   2064 C CB  . SER B 2 64  ? 22.409  2.123   3.257   1.00 43.86  ? 63  SER D CB  1 
ATOM   2065 O OG  . SER B 2 64  ? 21.264  1.285   3.401   1.00 40.79  ? 63  SER D OG  1 
ATOM   2066 N N   . GLY B 2 65  ? 20.393  4.536   2.812   1.00 40.98  ? 64  GLY D N   1 
ATOM   2067 C CA  . GLY B 2 65  ? 19.054  5.059   2.634   1.00 42.28  ? 64  GLY D CA  1 
ATOM   2068 C C   . GLY B 2 65  ? 18.634  4.966   1.180   1.00 40.48  ? 64  GLY D C   1 
ATOM   2069 O O   . GLY B 2 65  ? 19.467  4.714   0.299   1.00 41.40  ? 64  GLY D O   1 
ATOM   2070 N N   . SER B 2 66  ? 17.333  5.163   0.941   1.00 40.10  ? 65  SER D N   1 
ATOM   2071 C CA  . SER B 2 66  ? 16.806  5.141   -0.416  1.00 43.02  ? 65  SER D CA  1 
ATOM   2072 C C   . SER B 2 66  ? 15.323  5.498   -0.419  1.00 46.83  ? 65  SER D C   1 
ATOM   2073 O O   . SER B 2 66  ? 14.649  5.442   0.608   1.00 47.41  ? 65  SER D O   1 
ATOM   2074 C CB  . SER B 2 66  ? 17.027  3.781   -1.083  1.00 51.93  ? 65  SER D CB  1 
ATOM   2075 O OG  . SER B 2 66  ? 17.746  3.935   -2.308  1.00 50.26  ? 65  SER D OG  1 
ATOM   2076 N N   . ARG B 2 67  ? 14.821  5.874   -1.607  1.00 51.99  ? 66  ARG D N   1 
ATOM   2077 C CA  . ARG B 2 67  ? 13.439  6.309   -1.785  1.00 52.55  ? 66  ARG D CA  1 
ATOM   2078 C C   . ARG B 2 67  ? 12.768  5.438   -2.825  1.00 52.27  ? 66  ARG D C   1 
ATOM   2079 O O   . ARG B 2 67  ? 13.380  5.086   -3.832  1.00 53.14  ? 66  ARG D O   1 
ATOM   2080 C CB  . ARG B 2 67  ? 13.321  7.783   -2.233  1.00 55.72  ? 66  ARG D CB  1 
ATOM   2081 C CG  . ARG B 2 67  ? 11.909  8.186   -2.751  1.00 56.27  ? 66  ARG D CG  1 
ATOM   2082 C CD  . ARG B 2 67  ? 11.903  9.515   -3.481  1.00 55.54  ? 66  ARG D CD  1 
ATOM   2083 N NE  . ARG B 2 67  ? 12.681  9.465   -4.705  1.00 57.52  ? 66  ARG D NE  1 
ATOM   2084 C CZ  . ARG B 2 67  ? 12.162  9.243   -5.906  1.00 62.50  ? 66  ARG D CZ  1 
ATOM   2085 N NH1 . ARG B 2 67  ? 10.863  9.032   -6.071  1.00 65.34  ? 66  ARG D NH1 1 
ATOM   2086 N NH2 . ARG B 2 67  ? 12.965  9.224   -6.965  1.00 62.42  ? 66  ARG D NH2 1 
ATOM   2087 N N   . SER B 2 68  ? 11.511  5.090   -2.571  1.00 55.40  ? 67  SER D N   1 
ATOM   2088 C CA  . SER B 2 68  ? 10.711  4.354   -3.540  1.00 57.91  ? 67  SER D CA  1 
ATOM   2089 C C   . SER B 2 68  ? 9.299   4.924   -3.471  1.00 64.23  ? 67  SER D C   1 
ATOM   2090 O O   . SER B 2 68  ? 8.497   4.522   -2.625  1.00 64.22  ? 67  SER D O   1 
ATOM   2091 C CB  . SER B 2 68  ? 10.736  2.856   -3.270  1.00 56.15  ? 67  SER D CB  1 
ATOM   2092 O OG  . SER B 2 68  ? 9.526   2.263   -3.698  1.00 56.57  ? 67  SER D OG  1 
ATOM   2093 N N   . GLY B 2 69  ? 8.998   5.859   -4.364  1.00 70.48  ? 68  GLY D N   1 
ATOM   2094 C CA  . GLY B 2 69  ? 7.701   6.515   -4.322  1.00 71.31  ? 68  GLY D CA  1 
ATOM   2095 C C   . GLY B 2 69  ? 7.684   7.522   -3.210  1.00 68.61  ? 68  GLY D C   1 
ATOM   2096 O O   . GLY B 2 69  ? 8.601   8.347   -3.093  1.00 66.57  ? 68  GLY D O   1 
ATOM   2097 N N   . THR B 2 70  ? 6.640   7.455   -2.375  1.00 67.32  ? 69  THR D N   1 
ATOM   2098 C CA  . THR B 2 70  ? 6.514   8.340   -1.223  1.00 67.49  ? 69  THR D CA  1 
ATOM   2099 C C   . THR B 2 70  ? 7.284   7.824   -0.008  1.00 68.22  ? 69  THR D C   1 
ATOM   2100 O O   . THR B 2 70  ? 7.479   8.587   0.952   1.00 65.60  ? 69  THR D O   1 
ATOM   2101 C CB  . THR B 2 70  ? 5.035   8.522   -0.840  1.00 68.07  ? 69  THR D CB  1 
ATOM   2102 O OG1 . THR B 2 70  ? 4.590   7.403   -0.057  1.00 70.74  ? 69  THR D OG1 1 
ATOM   2103 C CG2 . THR B 2 70  ? 4.148   8.618   -2.086  1.00 67.23  ? 69  THR D CG2 1 
ATOM   2104 N N   . ASP B 2 71  ? 7.727   6.557   -0.034  1.00 63.72  ? 70  ASP D N   1 
ATOM   2105 C CA  . ASP B 2 71  ? 8.334   5.919   1.123   1.00 60.07  ? 70  ASP D CA  1 
ATOM   2106 C C   . ASP B 2 71  ? 9.848   6.041   1.081   1.00 59.00  ? 70  ASP D C   1 
ATOM   2107 O O   . ASP B 2 71  ? 10.472  5.790   0.048   1.00 58.45  ? 70  ASP D O   1 
ATOM   2108 C CB  . ASP B 2 71  ? 7.952   4.439   1.205   1.00 62.15  ? 70  ASP D CB  1 
ATOM   2109 C CG  . ASP B 2 71  ? 6.445   4.196   1.075   1.00 68.04  ? 70  ASP D CG  1 
ATOM   2110 O OD1 . ASP B 2 71  ? 5.630   5.044   1.512   1.00 68.46  ? 70  ASP D OD1 1 
ATOM   2111 O OD2 . ASP B 2 71  ? 6.072   3.127   0.540   1.00 69.03  ? 70  ASP D OD2 1 
ATOM   2112 N N   . PHE B 2 72  ? 10.435  6.400   2.225   1.00 58.67  ? 71  PHE D N   1 
ATOM   2113 C CA  . PHE B 2 72  ? 11.877  6.490   2.418   1.00 53.37  ? 71  PHE D CA  1 
ATOM   2114 C C   . PHE B 2 72  ? 12.283  5.437   3.443   1.00 52.53  ? 71  PHE D C   1 
ATOM   2115 O O   . PHE B 2 72  ? 11.449  4.962   4.220   1.00 56.40  ? 71  PHE D O   1 
ATOM   2116 C CB  . PHE B 2 72  ? 12.272  7.915   2.855   1.00 50.83  ? 71  PHE D CB  1 
ATOM   2117 C CG  . PHE B 2 72  ? 12.028  8.953   1.786   1.00 49.75  ? 71  PHE D CG  1 
ATOM   2118 C CD1 . PHE B 2 72  ? 10.739  9.336   1.456   1.00 53.14  ? 71  PHE D CD1 1 
ATOM   2119 C CD2 . PHE B 2 72  ? 13.086  9.498   1.061   1.00 52.26  ? 71  PHE D CD2 1 
ATOM   2120 C CE1 . PHE B 2 72  ? 10.504  10.274  0.437   1.00 57.44  ? 71  PHE D CE1 1 
ATOM   2121 C CE2 . PHE B 2 72  ? 12.865  10.436  0.030   1.00 50.98  ? 71  PHE D CE2 1 
ATOM   2122 C CZ  . PHE B 2 72  ? 11.571  10.830  -0.271  1.00 53.30  ? 71  PHE D CZ  1 
ATOM   2123 N N   . THR B 2 73  ? 13.555  5.038   3.431   1.00 44.35  ? 72  THR D N   1 
ATOM   2124 C CA  . THR B 2 73  ? 13.971  3.935   4.282   1.00 43.91  ? 72  THR D CA  1 
ATOM   2125 C C   . THR B 2 73  ? 15.426  4.067   4.696   1.00 46.59  ? 72  THR D C   1 
ATOM   2126 O O   . THR B 2 73  ? 16.297  4.322   3.867   1.00 45.50  ? 72  THR D O   1 
ATOM   2127 C CB  . THR B 2 73  ? 13.818  2.574   3.592   1.00 45.83  ? 72  THR D CB  1 
ATOM   2128 O OG1 . THR B 2 73  ? 14.475  2.604   2.323   1.00 44.23  ? 72  THR D OG1 1 
ATOM   2129 C CG2 . THR B 2 73  ? 12.366  2.167   3.426   1.00 47.74  ? 72  THR D CG2 1 
ATOM   2130 N N   . LEU B 2 74  ? 15.698  3.814   5.969   1.00 47.78  ? 73  LEU D N   1 
ATOM   2131 C CA  . LEU B 2 74  ? 17.061  3.666   6.456   1.00 44.65  ? 73  LEU D CA  1 
ATOM   2132 C C   . LEU B 2 74  ? 17.280  2.212   6.834   1.00 42.79  ? 73  LEU D C   1 
ATOM   2133 O O   . LEU B 2 74  ? 16.397  1.591   7.430   1.00 43.25  ? 73  LEU D O   1 
ATOM   2134 C CB  . LEU B 2 74  ? 17.307  4.585   7.656   1.00 43.80  ? 73  LEU D CB  1 
ATOM   2135 C CG  . LEU B 2 74  ? 18.627  4.507   8.404   1.00 40.86  ? 73  LEU D CG  1 
ATOM   2136 C CD1 . LEU B 2 74  ? 19.647  5.459   7.817   1.00 41.17  ? 73  LEU D CD1 1 
ATOM   2137 C CD2 . LEU B 2 74  ? 18.336  4.906   9.812   1.00 44.05  ? 73  LEU D CD2 1 
ATOM   2138 N N   . THR B 2 75  ? 18.439  1.663   6.465   1.00 40.78  ? 74  THR D N   1 
ATOM   2139 C CA  . THR B 2 75  ? 18.835  0.332   6.901   1.00 40.81  ? 74  THR D CA  1 
ATOM   2140 C C   . THR B 2 75  ? 20.227  0.360   7.504   1.00 39.91  ? 74  THR D C   1 
ATOM   2141 O O   . THR B 2 75  ? 21.098  1.122   7.062   1.00 41.11  ? 74  THR D O   1 
ATOM   2142 C CB  . THR B 2 75  ? 18.855  -0.716  5.752   1.00 45.73  ? 74  THR D CB  1 
ATOM   2143 O OG1 . THR B 2 75  ? 20.002  -0.472  4.911   1.00 43.19  ? 74  THR D OG1 1 
ATOM   2144 C CG2 . THR B 2 75  ? 17.520  -0.793  4.941   1.00 41.63  ? 74  THR D CG2 1 
ATOM   2145 N N   . ILE B 2 76  ? 20.440  -0.508  8.490   1.00 40.19  ? 75  ILE D N   1 
ATOM   2146 C CA  . ILE B 2 76  ? 21.753  -0.733  9.074   1.00 39.43  ? 75  ILE D CA  1 
ATOM   2147 C C   . ILE B 2 76  ? 22.124  -2.163  8.734   1.00 45.42  ? 75  ILE D C   1 
ATOM   2148 O O   . ILE B 2 76  ? 21.438  -3.107  9.140   1.00 44.57  ? 75  ILE D O   1 
ATOM   2149 C CB  . ILE B 2 76  ? 21.789  -0.475  10.592  1.00 39.85  ? 75  ILE D CB  1 
ATOM   2150 C CG1 . ILE B 2 76  ? 21.096  0.832   10.953  1.00 40.21  ? 75  ILE D CG1 1 
ATOM   2151 C CG2 . ILE B 2 76  ? 23.230  -0.346  11.074  1.00 40.24  ? 75  ILE D CG2 1 
ATOM   2152 C CD1 . ILE B 2 76  ? 20.251  0.738   12.138  1.00 41.28  ? 75  ILE D CD1 1 
ATOM   2153 N N   . SER B 2 77  ? 23.189  -2.316  7.958   1.00 42.39  ? 76  SER D N   1 
ATOM   2154 C CA  . SER B 2 77  ? 23.454  -3.596  7.329   1.00 42.09  ? 76  SER D CA  1 
ATOM   2155 C C   . SER B 2 77  ? 23.915  -4.637  8.334   1.00 47.91  ? 76  SER D C   1 
ATOM   2156 O O   . SER B 2 77  ? 23.848  -5.839  8.041   1.00 47.52  ? 76  SER D O   1 
ATOM   2157 C CB  . SER B 2 77  ? 24.480  -3.403  6.218   1.00 39.96  ? 76  SER D CB  1 
ATOM   2158 O OG  . SER B 2 77  ? 25.775  -3.173  6.736   1.00 41.93  ? 76  SER D OG  1 
ATOM   2159 N N   . SER B 2 78  ? 24.369  -4.204  9.509   1.00 47.11  ? 77  SER D N   1 
ATOM   2160 C CA  . SER B 2 78  ? 24.635  -5.137  10.598  1.00 48.61  ? 77  SER D CA  1 
ATOM   2161 C C   . SER B 2 78  ? 24.805  -4.286  11.837  1.00 50.61  ? 77  SER D C   1 
ATOM   2162 O O   . SER B 2 78  ? 25.824  -3.597  11.967  1.00 52.45  ? 77  SER D O   1 
ATOM   2163 C CB  . SER B 2 78  ? 25.873  -5.974  10.346  1.00 50.07  ? 77  SER D CB  1 
ATOM   2164 O OG  . SER B 2 78  ? 26.937  -5.472  11.131  1.00 54.96  ? 77  SER D OG  1 
ATOM   2165 N N   . LEU B 2 79  ? 23.799  -4.314  12.715  1.00 49.23  ? 78  LEU D N   1 
ATOM   2166 C CA  . LEU B 2 79  ? 23.802  -3.554  13.961  1.00 48.07  ? 78  LEU D CA  1 
ATOM   2167 C C   . LEU B 2 79  ? 25.123  -3.673  14.704  1.00 49.10  ? 78  LEU D C   1 
ATOM   2168 O O   . LEU B 2 79  ? 25.921  -4.594  14.485  1.00 51.31  ? 78  LEU D O   1 
ATOM   2169 C CB  . LEU B 2 79  ? 22.685  -4.029  14.883  1.00 45.57  ? 78  LEU D CB  1 
ATOM   2170 C CG  . LEU B 2 79  ? 21.398  -3.229  14.810  1.00 45.22  ? 78  LEU D CG  1 
ATOM   2171 C CD1 . LEU B 2 79  ? 20.624  -3.458  16.096  1.00 46.06  ? 78  LEU D CD1 1 
ATOM   2172 C CD2 . LEU B 2 79  ? 21.659  -1.751  14.573  1.00 42.88  ? 78  LEU D CD2 1 
ATOM   2173 N N   . GLN B 2 80  ? 25.356  -2.734  15.588  1.00 47.58  ? 79  GLN D N   1 
ATOM   2174 C CA  . GLN B 2 80  ? 26.546  -2.721  16.412  1.00 48.71  ? 79  GLN D CA  1 
ATOM   2175 C C   . GLN B 2 80  ? 26.064  -2.333  17.787  1.00 47.86  ? 79  GLN D C   1 
ATOM   2176 O O   . GLN B 2 80  ? 24.918  -1.898  17.937  1.00 45.87  ? 79  GLN D O   1 
ATOM   2177 C CB  . GLN B 2 80  ? 27.568  -1.717  15.880  1.00 49.44  ? 79  GLN D CB  1 
ATOM   2178 C CG  . GLN B 2 80  ? 28.119  -2.157  14.587  1.00 48.57  ? 79  GLN D CG  1 
ATOM   2179 C CD  . GLN B 2 80  ? 29.309  -3.037  14.823  1.00 55.01  ? 79  GLN D CD  1 
ATOM   2180 O OE1 . GLN B 2 80  ? 29.286  -4.239  14.525  1.00 61.03  ? 79  GLN D OE1 1 
ATOM   2181 N NE2 . GLN B 2 80  ? 30.363  -2.451  15.382  1.00 57.10  ? 79  GLN D NE2 1 
ATOM   2182 N N   . PRO B 2 81  ? 26.888  -2.506  18.822  1.00 53.33  ? 80  PRO D N   1 
ATOM   2183 C CA  . PRO B 2 81  ? 26.426  -2.070  20.155  1.00 53.90  ? 80  PRO D CA  1 
ATOM   2184 C C   . PRO B 2 81  ? 26.167  -0.571  20.202  1.00 53.42  ? 80  PRO D C   1 
ATOM   2185 O O   . PRO B 2 81  ? 25.121  -0.130  20.694  1.00 54.30  ? 80  PRO D O   1 
ATOM   2186 C CB  . PRO B 2 81  ? 27.568  -2.511  21.085  1.00 52.04  ? 80  PRO D CB  1 
ATOM   2187 C CG  . PRO B 2 81  ? 28.240  -3.649  20.325  1.00 51.36  ? 80  PRO D CG  1 
ATOM   2188 C CD  . PRO B 2 81  ? 28.205  -3.168  18.897  1.00 53.29  ? 80  PRO D CD  1 
ATOM   2189 N N   . GLU B 2 82  ? 27.060  0.224   19.624  1.00 47.25  ? 81  GLU D N   1 
ATOM   2190 C CA  . GLU B 2 82  ? 26.844  1.661   19.598  1.00 45.84  ? 81  GLU D CA  1 
ATOM   2191 C C   . GLU B 2 82  ? 25.609  2.058   18.795  1.00 46.35  ? 81  GLU D C   1 
ATOM   2192 O O   . GLU B 2 82  ? 25.205  3.225   18.858  1.00 48.95  ? 81  GLU D O   1 
ATOM   2193 C CB  . GLU B 2 82  ? 28.067  2.324   18.994  1.00 44.70  ? 81  GLU D CB  1 
ATOM   2194 C CG  . GLU B 2 82  ? 28.187  1.828   17.591  1.00 47.96  ? 81  GLU D CG  1 
ATOM   2195 C CD  . GLU B 2 82  ? 29.325  0.867   17.382  1.00 53.29  ? 81  GLU D CD  1 
ATOM   2196 O OE1 . GLU B 2 82  ? 30.127  1.186   16.476  1.00 55.88  ? 81  GLU D OE1 1 
ATOM   2197 O OE2 . GLU B 2 82  ? 29.424  -0.180  18.105  1.00 53.86  ? 81  GLU D OE2 1 
ATOM   2198 N N   . ASP B 2 83  ? 25.032  1.153   18.004  1.00 46.70  ? 82  ASP D N   1 
ATOM   2199 C CA  . ASP B 2 83  ? 23.906  1.518   17.157  1.00 44.13  ? 82  ASP D CA  1 
ATOM   2200 C C   . ASP B 2 83  ? 22.563  1.494   17.883  1.00 41.77  ? 82  ASP D C   1 
ATOM   2201 O O   . ASP B 2 83  ? 21.541  1.770   17.262  1.00 44.08  ? 82  ASP D O   1 
ATOM   2202 C CB  . ASP B 2 83  ? 23.819  0.594   15.917  1.00 46.00  ? 82  ASP D CB  1 
ATOM   2203 C CG  . ASP B 2 83  ? 25.006  0.736   14.956  1.00 44.67  ? 82  ASP D CG  1 
ATOM   2204 O OD1 . ASP B 2 83  ? 25.722  1.757   14.999  1.00 42.55  ? 82  ASP D OD1 1 
ATOM   2205 O OD2 . ASP B 2 83  ? 25.204  -0.187  14.134  1.00 46.70  ? 82  ASP D OD2 1 
ATOM   2206 N N   . PHE B 2 84  ? 22.498  1.178   19.165  1.00 46.96  ? 83  PHE D N   1 
ATOM   2207 C CA  . PHE B 2 84  ? 21.190  1.061   19.817  1.00 48.39  ? 83  PHE D CA  1 
ATOM   2208 C C   . PHE B 2 84  ? 20.742  2.436   20.280  1.00 46.01  ? 83  PHE D C   1 
ATOM   2209 O O   . PHE B 2 84  ? 21.314  2.985   21.218  1.00 50.39  ? 83  PHE D O   1 
ATOM   2210 C CB  . PHE B 2 84  ? 21.257  0.069   20.970  1.00 45.33  ? 83  PHE D CB  1 
ATOM   2211 C CG  . PHE B 2 84  ? 21.180  -1.334  20.510  1.00 44.95  ? 83  PHE D CG  1 
ATOM   2212 C CD1 . PHE B 2 84  ? 19.953  -1.940  20.277  1.00 45.70  ? 83  PHE D CD1 1 
ATOM   2213 C CD2 . PHE B 2 84  ? 22.339  -2.012  20.191  1.00 43.72  ? 83  PHE D CD2 1 
ATOM   2214 C CE1 . PHE B 2 84  ? 19.895  -3.213  19.802  1.00 48.00  ? 83  PHE D CE1 1 
ATOM   2215 C CE2 . PHE B 2 84  ? 22.288  -3.285  19.714  1.00 45.57  ? 83  PHE D CE2 1 
ATOM   2216 C CZ  . PHE B 2 84  ? 21.066  -3.889  19.510  1.00 47.05  ? 83  PHE D CZ  1 
ATOM   2217 N N   . ALA B 2 85  ? 19.734  2.996   19.619  1.00 47.29  ? 84  ALA D N   1 
ATOM   2218 C CA  . ALA B 2 85  ? 19.362  4.390   19.837  1.00 45.26  ? 84  ALA D CA  1 
ATOM   2219 C C   . ALA B 2 85  ? 17.950  4.634   19.298  1.00 46.88  ? 84  ALA D C   1 
ATOM   2220 O O   . ALA B 2 85  ? 17.194  3.689   19.053  1.00 50.34  ? 84  ALA D O   1 
ATOM   2221 C CB  . ALA B 2 85  ? 20.407  5.313   19.201  1.00 44.82  ? 84  ALA D CB  1 
ATOM   2222 N N   . THR B 2 86  ? 17.580  5.903   19.156  1.00 45.38  ? 85  THR D N   1 
ATOM   2223 C CA  . THR B 2 86  ? 16.316  6.268   18.533  1.00 48.10  ? 85  THR D CA  1 
ATOM   2224 C C   . THR B 2 86  ? 16.584  6.947   17.195  1.00 46.30  ? 85  THR D C   1 
ATOM   2225 O O   . THR B 2 86  ? 17.585  7.656   17.040  1.00 46.58  ? 85  THR D O   1 
ATOM   2226 C CB  . THR B 2 86  ? 15.497  7.173   19.453  1.00 50.51  ? 85  THR D CB  1 
ATOM   2227 O OG1 . THR B 2 86  ? 15.437  6.585   20.762  1.00 55.51  ? 85  THR D OG1 1 
ATOM   2228 C CG2 . THR B 2 86  ? 14.077  7.336   18.929  1.00 51.75  ? 85  THR D CG2 1 
ATOM   2229 N N   . TYR B 2 87  ? 15.713  6.714   16.215  1.00 46.72  ? 86  TYR D N   1 
ATOM   2230 C CA  . TYR B 2 87  ? 15.960  7.217   14.865  1.00 47.41  ? 86  TYR D CA  1 
ATOM   2231 C C   . TYR B 2 87  ? 14.755  8.002   14.376  1.00 48.89  ? 86  TYR D C   1 
ATOM   2232 O O   . TYR B 2 87  ? 13.603  7.701   14.718  1.00 48.21  ? 86  TYR D O   1 
ATOM   2233 C CB  . TYR B 2 87  ? 16.320  6.084   13.862  1.00 48.35  ? 86  TYR D CB  1 
ATOM   2234 C CG  . TYR B 2 87  ? 17.617  5.373   14.222  1.00 47.10  ? 86  TYR D CG  1 
ATOM   2235 C CD1 . TYR B 2 87  ? 17.618  4.304   15.123  1.00 45.86  ? 86  TYR D CD1 1 
ATOM   2236 C CD2 . TYR B 2 87  ? 18.841  5.801   13.708  1.00 45.41  ? 86  TYR D CD2 1 
ATOM   2237 C CE1 . TYR B 2 87  ? 18.793  3.665   15.482  1.00 44.95  ? 86  TYR D CE1 1 
ATOM   2238 C CE2 . TYR B 2 87  ? 20.022  5.166   14.060  1.00 44.87  ? 86  TYR D CE2 1 
ATOM   2239 C CZ  . TYR B 2 87  ? 19.985  4.096   14.947  1.00 44.68  ? 86  TYR D CZ  1 
ATOM   2240 O OH  . TYR B 2 87  ? 21.146  3.471   15.307  1.00 41.34  ? 86  TYR D OH  1 
ATOM   2241 N N   . TYR B 2 88  ? 15.054  9.038   13.599  1.00 51.31  ? 87  TYR D N   1 
ATOM   2242 C CA  . TYR B 2 88  ? 14.100  10.065  13.215  1.00 51.81  ? 87  TYR D CA  1 
ATOM   2243 C C   . TYR B 2 88  ? 14.348  10.409  11.760  1.00 47.72  ? 87  TYR D C   1 
ATOM   2244 O O   . TYR B 2 88  ? 15.502  10.619  11.359  1.00 44.66  ? 87  TYR D O   1 
ATOM   2245 C CB  . TYR B 2 88  ? 14.243  11.347  14.068  1.00 47.28  ? 87  TYR D CB  1 
ATOM   2246 C CG  . TYR B 2 88  ? 13.776  11.256  15.509  1.00 51.59  ? 87  TYR D CG  1 
ATOM   2247 C CD1 . TYR B 2 88  ? 12.421  11.255  15.824  1.00 55.23  ? 87  TYR D CD1 1 
ATOM   2248 C CD2 . TYR B 2 88  ? 14.687  11.250  16.560  1.00 49.89  ? 87  TYR D CD2 1 
ATOM   2249 C CE1 . TYR B 2 88  ? 11.994  11.208  17.132  1.00 54.15  ? 87  TYR D CE1 1 
ATOM   2250 C CE2 . TYR B 2 88  ? 14.263  11.202  17.859  1.00 49.81  ? 87  TYR D CE2 1 
ATOM   2251 C CZ  . TYR B 2 88  ? 12.922  11.181  18.137  1.00 52.58  ? 87  TYR D CZ  1 
ATOM   2252 O OH  . TYR B 2 88  ? 12.513  11.121  19.439  1.00 59.72  ? 87  TYR D OH  1 
ATOM   2253 N N   . CYS B 2 89  ? 13.268  10.475  10.981  1.00 50.88  ? 88  CYS D N   1 
ATOM   2254 C CA  . CYS B 2 89  ? 13.336  10.952  9.603   1.00 52.77  ? 88  CYS D CA  1 
ATOM   2255 C C   . CYS B 2 89  ? 12.917  12.408  9.565   1.00 48.41  ? 88  CYS D C   1 
ATOM   2256 O O   . CYS B 2 89  ? 12.029  12.833  10.306  1.00 51.61  ? 88  CYS D O   1 
ATOM   2257 C CB  . CYS B 2 89  ? 12.448  10.131  8.658   1.00 49.39  ? 88  CYS D CB  1 
ATOM   2258 S SG  . CYS B 2 89  ? 10.733  9.875   9.250   1.00 60.79  ? 88  CYS D SG  1 
ATOM   2259 N N   . GLN B 2 90  ? 13.549  13.165  8.697   1.00 47.15  ? 89  GLN D N   1 
ATOM   2260 C CA  . GLN B 2 90  ? 13.229  14.573  8.545   1.00 51.11  ? 89  GLN D CA  1 
ATOM   2261 C C   . GLN B 2 90  ? 12.868  14.888  7.106   1.00 54.13  ? 89  GLN D C   1 
ATOM   2262 O O   . GLN B 2 90  ? 13.656  14.612  6.189   1.00 53.57  ? 89  GLN D O   1 
ATOM   2263 C CB  . GLN B 2 90  ? 14.402  15.432  8.941   1.00 47.77  ? 89  GLN D CB  1 
ATOM   2264 C CG  . GLN B 2 90  ? 14.145  16.847  8.643   1.00 48.71  ? 89  GLN D CG  1 
ATOM   2265 C CD  . GLN B 2 90  ? 15.411  17.580  8.645   1.00 49.01  ? 89  GLN D CD  1 
ATOM   2266 O OE1 . GLN B 2 90  ? 16.473  16.961  8.594   1.00 48.00  ? 89  GLN D OE1 1 
ATOM   2267 N NE2 . GLN B 2 90  ? 15.340  18.903  8.794   1.00 53.69  ? 89  GLN D NE2 1 
ATOM   2268 N N   . GLN B 2 91  ? 11.705  15.495  6.911   1.00 54.61  ? 90  GLN D N   1 
ATOM   2269 C CA  . GLN B 2 91  ? 11.313  16.019  5.608   1.00 58.99  ? 90  GLN D CA  1 
ATOM   2270 C C   . GLN B 2 91  ? 11.399  17.539  5.695   1.00 58.47  ? 90  GLN D C   1 
ATOM   2271 O O   . GLN B 2 91  ? 10.608  18.164  6.415   1.00 55.75  ? 90  GLN D O   1 
ATOM   2272 C CB  . GLN B 2 91  ? 9.907   15.550  5.233   1.00 62.39  ? 90  GLN D CB  1 
ATOM   2273 C CG  . GLN B 2 91  ? 9.445   15.913  3.807   1.00 63.79  ? 90  GLN D CG  1 
ATOM   2274 C CD  . GLN B 2 91  ? 7.914   15.938  3.694   1.00 71.80  ? 90  GLN D CD  1 
ATOM   2275 O OE1 . GLN B 2 91  ? 7.204   15.859  4.704   1.00 75.22  ? 90  GLN D OE1 1 
ATOM   2276 N NE2 . GLN B 2 91  ? 7.406   16.036  2.475   1.00 71.68  ? 90  GLN D NE2 1 
ATOM   2277 N N   . ASP B 2 92  ? 12.381  18.118  4.990   1.00 57.50  ? 91  ASP D N   1 
ATOM   2278 C CA  . ASP B 2 92  ? 12.542  19.574  4.860   1.00 60.24  ? 91  ASP D CA  1 
ATOM   2279 C C   . ASP B 2 92  ? 11.737  20.078  3.657   1.00 65.68  ? 91  ASP D C   1 
ATOM   2280 O O   . ASP B 2 92  ? 12.276  20.454  2.612   1.00 68.86  ? 91  ASP D O   1 
ATOM   2281 C CB  . ASP B 2 92  ? 14.018  19.936  4.726   1.00 58.08  ? 91  ASP D CB  1 
ATOM   2282 C CG  . ASP B 2 92  ? 14.266  21.445  4.724   1.00 62.00  ? 91  ASP D CG  1 
ATOM   2283 O OD1 . ASP B 2 92  ? 13.281  22.231  4.727   1.00 62.13  ? 91  ASP D OD1 1 
ATOM   2284 O OD2 . ASP B 2 92  ? 15.458  21.845  4.666   1.00 60.58  ? 91  ASP D OD2 1 
ATOM   2285 N N   . GLY B 2 93  ? 10.415  20.102  3.833   1.00 68.48  ? 92  GLY D N   1 
ATOM   2286 C CA  . GLY B 2 93  ? 9.493   20.309  2.733   1.00 74.29  ? 92  GLY D CA  1 
ATOM   2287 C C   . GLY B 2 93  ? 9.359   21.762  2.319   1.00 81.68  ? 92  GLY D C   1 
ATOM   2288 O O   . GLY B 2 93  ? 10.042  22.656  2.821   1.00 80.42  ? 92  GLY D O   1 
ATOM   2289 N N   . TRP B 2 94  ? 8.421   21.988  1.389   1.00 90.11  ? 93  TRP D N   1 
ATOM   2290 C CA  . TRP B 2 94  ? 8.248   23.292  0.745   1.00 93.70  ? 93  TRP D CA  1 
ATOM   2291 C C   . TRP B 2 94  ? 7.985   24.401  1.757   1.00 94.95  ? 93  TRP D C   1 
ATOM   2292 O O   . TRP B 2 94  ? 8.718   25.400  1.824   1.00 91.98  ? 93  TRP D O   1 
ATOM   2293 C CB  . TRP B 2 94  ? 7.096   23.215  -0.255  1.00 96.26  ? 93  TRP D CB  1 
ATOM   2294 C CG  . TRP B 2 94  ? 7.062   24.358  -1.228  1.00 103.57 ? 93  TRP D CG  1 
ATOM   2295 C CD1 . TRP B 2 94  ? 7.919   25.430  -1.281  1.00 102.93 ? 93  TRP D CD1 1 
ATOM   2296 C CD2 . TRP B 2 94  ? 6.107   24.557  -2.279  1.00 106.34 ? 93  TRP D CD2 1 
ATOM   2297 N NE1 . TRP B 2 94  ? 7.561   26.268  -2.311  1.00 104.91 ? 93  TRP D NE1 1 
ATOM   2298 C CE2 . TRP B 2 94  ? 6.452   25.756  -2.937  1.00 107.86 ? 93  TRP D CE2 1 
ATOM   2299 C CE3 . TRP B 2 94  ? 4.995   23.835  -2.731  1.00 105.89 ? 93  TRP D CE3 1 
ATOM   2300 C CZ2 . TRP B 2 94  ? 5.720   26.249  -4.019  1.00 108.29 ? 93  TRP D CZ2 1 
ATOM   2301 C CZ3 . TRP B 2 94  ? 4.273   24.325  -3.806  1.00 105.57 ? 93  TRP D CZ3 1 
ATOM   2302 C CH2 . TRP B 2 94  ? 4.637   25.520  -4.437  1.00 107.71 ? 93  TRP D CH2 1 
ATOM   2303 N N   . SER B 2 95  ? 6.908   24.263  2.525   1.00 88.73  ? 94  SER D N   1 
ATOM   2304 C CA  . SER B 2 95  ? 6.593   25.276  3.518   1.00 87.66  ? 94  SER D CA  1 
ATOM   2305 C C   . SER B 2 95  ? 7.357   25.037  4.824   1.00 85.34  ? 94  SER D C   1 
ATOM   2306 O O   . SER B 2 95  ? 7.947   25.973  5.380   1.00 83.81  ? 94  SER D O   1 
ATOM   2307 C CB  . SER B 2 95  ? 5.075   25.320  3.749   1.00 86.52  ? 94  SER D CB  1 
ATOM   2308 O OG  . SER B 2 95  ? 4.487   24.050  3.518   1.00 87.83  ? 94  SER D OG  1 
ATOM   2309 N N   . LEU B 2 96  ? 7.408   23.788  5.305   1.00 82.35  ? 95  LEU D N   1 
ATOM   2310 C CA  . LEU B 2 96  ? 7.797   23.562  6.692   1.00 72.99  ? 95  LEU D CA  1 
ATOM   2311 C C   . LEU B 2 96  ? 8.516   22.225  6.874   1.00 70.76  ? 95  LEU D C   1 
ATOM   2312 O O   . LEU B 2 96  ? 8.230   21.247  6.179   1.00 72.02  ? 95  LEU D O   1 
ATOM   2313 C CB  . LEU B 2 96  ? 6.558   23.633  7.579   1.00 71.20  ? 95  LEU D CB  1 
ATOM   2314 C CG  . LEU B 2 96  ? 5.379   22.851  7.000   1.00 77.46  ? 95  LEU D CG  1 
ATOM   2315 C CD1 . LEU B 2 96  ? 5.375   21.390  7.487   1.00 75.77  ? 95  LEU D CD1 1 
ATOM   2316 C CD2 . LEU B 2 96  ? 4.072   23.526  7.338   1.00 84.36  ? 95  LEU D CD2 1 
ATOM   2317 N N   . ILE B 2 97  ? 9.449   22.199  7.838   1.00 67.45  ? 96  ILE D N   1 
ATOM   2318 C CA  . ILE B 2 97  ? 10.182  20.996  8.227   1.00 62.02  ? 96  ILE D CA  1 
ATOM   2319 C C   . ILE B 2 97  ? 9.293   20.118  9.095   1.00 61.82  ? 96  ILE D C   1 
ATOM   2320 O O   . ILE B 2 97  ? 8.602   20.612  9.992   1.00 64.75  ? 96  ILE D O   1 
ATOM   2321 C CB  . ILE B 2 97  ? 11.458  21.379  8.991   1.00 58.67  ? 96  ILE D CB  1 
ATOM   2322 C CG1 . ILE B 2 97  ? 12.301  22.340  8.169   1.00 57.74  ? 96  ILE D CG1 1 
ATOM   2323 C CG2 . ILE B 2 97  ? 12.243  20.127  9.393   1.00 55.50  ? 96  ILE D CG2 1 
ATOM   2324 C CD1 . ILE B 2 97  ? 13.636  22.637  8.790   1.00 58.33  ? 96  ILE D CD1 1 
ATOM   2325 N N   . THR B 2 98  ? 9.315   18.809  8.838   1.00 59.04  ? 97  THR D N   1 
ATOM   2326 C CA  . THR B 2 98  ? 8.585   17.815  9.618   1.00 56.82  ? 97  THR D CA  1 
ATOM   2327 C C   . THR B 2 98  ? 9.568   16.774  10.150  1.00 54.26  ? 97  THR D C   1 
ATOM   2328 O O   . THR B 2 98  ? 10.650  16.578  9.590   1.00 54.31  ? 97  THR D O   1 
ATOM   2329 C CB  . THR B 2 98  ? 7.480   17.104  8.779   1.00 59.18  ? 97  THR D CB  1 
ATOM   2330 O OG1 . THR B 2 98  ? 6.794   18.042  7.937   1.00 63.66  ? 97  THR D OG1 1 
ATOM   2331 C CG2 . THR B 2 98  ? 6.469   16.410  9.669   1.00 57.78  ? 97  THR D CG2 1 
ATOM   2332 N N   . PHE B 2 99  ? 9.202   16.112  11.245  1.00 54.58  ? 98  PHE D N   1 
ATOM   2333 C CA  . PHE B 2 99  ? 9.983   14.992  11.745  1.00 52.57  ? 98  PHE D CA  1 
ATOM   2334 C C   . PHE B 2 99  ? 9.061   13.804  11.967  1.00 57.20  ? 98  PHE D C   1 
ATOM   2335 O O   . PHE B 2 99  ? 7.901   13.959  12.359  1.00 62.10  ? 98  PHE D O   1 
ATOM   2336 C CB  . PHE B 2 99  ? 10.688  15.323  13.036  1.00 50.19  ? 98  PHE D CB  1 
ATOM   2337 C CG  . PHE B 2 99  ? 11.990  16.006  12.856  1.00 49.07  ? 98  PHE D CG  1 
ATOM   2338 C CD1 . PHE B 2 99  ? 13.114  15.289  12.573  1.00 47.77  ? 98  PHE D CD1 1 
ATOM   2339 C CD2 . PHE B 2 99  ? 12.103  17.363  13.037  1.00 49.41  ? 98  PHE D CD2 1 
ATOM   2340 C CE1 . PHE B 2 99  ? 14.325  15.908  12.436  1.00 46.82  ? 98  PHE D CE1 1 
ATOM   2341 C CE2 . PHE B 2 99  ? 13.324  17.993  12.907  1.00 48.48  ? 98  PHE D CE2 1 
ATOM   2342 C CZ  . PHE B 2 99  ? 14.435  17.266  12.591  1.00 47.19  ? 98  PHE D CZ  1 
ATOM   2343 N N   . GLY B 2 100 ? 9.566   12.620  11.697  1.00 56.22  ? 99  GLY D N   1 
ATOM   2344 C CA  . GLY B 2 100 ? 8.779   11.443  11.956  1.00 59.72  ? 99  GLY D CA  1 
ATOM   2345 C C   . GLY B 2 100 ? 8.694   11.163  13.435  1.00 59.66  ? 99  GLY D C   1 
ATOM   2346 O O   . GLY B 2 100 ? 9.512   11.632  14.221  1.00 59.22  ? 99  GLY D O   1 
ATOM   2347 N N   . GLN B 2 101 ? 7.695   10.368  13.817  1.00 62.65  ? 100 GLN D N   1 
ATOM   2348 C CA  . GLN B 2 101 ? 7.447   10.134  15.236  1.00 61.17  ? 100 GLN D CA  1 
ATOM   2349 C C   . GLN B 2 101 ? 8.640   9.515   15.954  1.00 59.56  ? 100 GLN D C   1 
ATOM   2350 O O   . GLN B 2 101 ? 8.721   9.622   17.181  1.00 62.33  ? 100 GLN D O   1 
ATOM   2351 C CB  . GLN B 2 101 ? 6.210   9.255   15.406  1.00 63.59  ? 100 GLN D CB  1 
ATOM   2352 C CG  . GLN B 2 101 ? 6.549   7.775   15.278  1.00 68.31  ? 100 GLN D CG  1 
ATOM   2353 C CD  . GLN B 2 101 ? 5.326   6.865   15.241  1.00 73.08  ? 100 GLN D CD  1 
ATOM   2354 O OE1 . GLN B 2 101 ? 5.459   5.643   15.119  1.00 72.54  ? 100 GLN D OE1 1 
ATOM   2355 N NE2 . GLN B 2 101 ? 4.132   7.454   15.375  1.00 76.96  ? 100 GLN D NE2 1 
ATOM   2356 N N   . GLY B 2 102 ? 9.558   8.881   15.232  1.00 58.90  ? 101 GLY D N   1 
ATOM   2357 C CA  . GLY B 2 102 ? 10.738  8.267   15.807  1.00 56.79  ? 101 GLY D CA  1 
ATOM   2358 C C   . GLY B 2 102 ? 10.634  6.749   15.889  1.00 54.13  ? 101 GLY D C   1 
ATOM   2359 O O   . GLY B 2 102 ? 9.550   6.164   15.856  1.00 54.91  ? 101 GLY D O   1 
ATOM   2360 N N   . THR B 2 103 ? 11.800  6.102   16.010  1.00 52.25  ? 102 THR D N   1 
ATOM   2361 C CA  . THR B 2 103 ? 11.899  4.642   16.111  1.00 54.00  ? 102 THR D CA  1 
ATOM   2362 C C   . THR B 2 103 ? 13.006  4.271   17.089  1.00 54.57  ? 102 THR D C   1 
ATOM   2363 O O   . THR B 2 103 ? 14.181  4.547   16.825  1.00 51.86  ? 102 THR D O   1 
ATOM   2364 C CB  . THR B 2 103 ? 12.183  4.001   14.750  1.00 53.82  ? 102 THR D CB  1 
ATOM   2365 O OG1 . THR B 2 103 ? 10.977  3.954   13.985  1.00 57.88  ? 102 THR D OG1 1 
ATOM   2366 C CG2 . THR B 2 103 ? 12.703  2.585   14.917  1.00 55.11  ? 102 THR D CG2 1 
ATOM   2367 N N   . LYS B 2 104 ? 12.641  3.623   18.196  1.00 57.50  ? 103 LYS D N   1 
ATOM   2368 C CA  . LYS B 2 104 ? 13.578  3.276   19.259  1.00 56.24  ? 103 LYS D CA  1 
ATOM   2369 C C   . LYS B 2 104 ? 14.023  1.839   19.066  1.00 57.04  ? 103 LYS D C   1 
ATOM   2370 O O   . LYS B 2 104 ? 13.180  0.943   18.955  1.00 59.94  ? 103 LYS D O   1 
ATOM   2371 C CB  . LYS B 2 104 ? 12.914  3.446   20.633  1.00 59.89  ? 103 LYS D CB  1 
ATOM   2372 C CG  . LYS B 2 104 ? 13.837  3.855   21.825  1.00 64.46  ? 103 LYS D CG  1 
ATOM   2373 C CD  . LYS B 2 104 ? 15.068  2.937   21.972  1.00 66.22  ? 103 LYS D CD  1 
ATOM   2374 C CE  . LYS B 2 104 ? 16.205  3.572   22.795  1.00 66.21  ? 103 LYS D CE  1 
ATOM   2375 N NZ  . LYS B 2 104 ? 17.449  2.723   22.736  1.00 65.14  ? 103 LYS D NZ  1 
ATOM   2376 N N   . VAL B 2 105 ? 15.329  1.606   19.047  1.00 50.86  ? 104 VAL D N   1 
ATOM   2377 C CA  . VAL B 2 105 ? 15.853  0.285   18.713  1.00 54.28  ? 104 VAL D CA  1 
ATOM   2378 C C   . VAL B 2 105 ? 16.548  -0.264  19.951  1.00 52.88  ? 104 VAL D C   1 
ATOM   2379 O O   . VAL B 2 105 ? 17.713  0.052   20.206  1.00 52.71  ? 104 VAL D O   1 
ATOM   2380 C CB  . VAL B 2 105 ? 16.794  0.320   17.496  1.00 56.03  ? 104 VAL D CB  1 
ATOM   2381 C CG1 . VAL B 2 105 ? 17.450  -1.058  17.271  1.00 54.09  ? 104 VAL D CG1 1 
ATOM   2382 C CG2 . VAL B 2 105 ? 16.042  0.751   16.239  1.00 48.76  ? 104 VAL D CG2 1 
ATOM   2383 N N   . GLU B 2 106 ? 15.843  -1.106  20.707  1.00 57.16  ? 105 GLU D N   1 
ATOM   2384 C CA  . GLU B 2 106 ? 16.331  -1.688  21.951  1.00 60.76  ? 105 GLU D CA  1 
ATOM   2385 C C   . GLU B 2 106 ? 16.952  -3.063  21.699  1.00 57.59  ? 105 GLU D C   1 
ATOM   2386 O O   . GLU B 2 106 ? 16.698  -3.699  20.678  1.00 57.03  ? 105 GLU D O   1 
ATOM   2387 C CB  . GLU B 2 106 ? 15.187  -1.820  22.960  1.00 64.02  ? 105 GLU D CB  1 
ATOM   2388 C CG  . GLU B 2 106 ? 14.249  -0.602  23.060  1.00 66.20  ? 105 GLU D CG  1 
ATOM   2389 C CD  . GLU B 2 106 ? 14.103  -0.018  24.487  1.00 74.13  ? 105 GLU D CD  1 
ATOM   2390 O OE1 . GLU B 2 106 ? 15.090  0.490   25.093  1.00 73.35  ? 105 GLU D OE1 1 
ATOM   2391 O OE2 . GLU B 2 106 ? 12.980  -0.114  25.027  1.00 77.25  ? 105 GLU D OE2 1 
ATOM   2392 N N   . ILE B 2 107 ? 17.766  -3.531  22.661  1.00 54.30  ? 106 ILE D N   1 
ATOM   2393 C CA  . ILE B 2 107 ? 18.425  -4.833  22.551  1.00 53.78  ? 106 ILE D CA  1 
ATOM   2394 C C   . ILE B 2 107 ? 17.451  -5.939  22.935  1.00 54.07  ? 106 ILE D C   1 
ATOM   2395 O O   . ILE B 2 107 ? 16.541  -5.758  23.751  1.00 56.17  ? 106 ILE D O   1 
ATOM   2396 C CB  . ILE B 2 107 ? 19.691  -4.902  23.432  1.00 56.64  ? 106 ILE D CB  1 
ATOM   2397 C CG1 . ILE B 2 107 ? 20.681  -3.795  23.074  1.00 53.39  ? 106 ILE D CG1 1 
ATOM   2398 C CG2 . ILE B 2 107 ? 20.389  -6.248  23.284  1.00 51.14  ? 106 ILE D CG2 1 
ATOM   2399 C CD1 . ILE B 2 107 ? 22.108  -4.037  23.583  1.00 54.21  ? 106 ILE D CD1 1 
ATOM   2400 N N   . LYS B 2 108 ? 17.645  -7.103  22.338  1.00 54.43  ? 107 LYS D N   1 
ATOM   2401 C CA  . LYS B 2 108 ? 16.938  -8.304  22.742  1.00 60.75  ? 107 LYS D CA  1 
ATOM   2402 C C   . LYS B 2 108 ? 17.847  -9.149  23.628  1.00 61.57  ? 107 LYS D C   1 
ATOM   2403 O O   . LYS B 2 108 ? 19.059  -9.229  23.391  1.00 61.25  ? 107 LYS D O   1 
ATOM   2404 C CB  . LYS B 2 108 ? 16.485  -9.102  21.519  1.00 56.92  ? 107 LYS D CB  1 
ATOM   2405 C CG  . LYS B 2 108 ? 16.011  -10.497 21.833  1.00 57.48  ? 107 LYS D CG  1 
ATOM   2406 C CD  . LYS B 2 108 ? 14.679  -10.785 21.183  1.00 56.90  ? 107 LYS D CD  1 
ATOM   2407 C CE  . LYS B 2 108 ? 13.602  -9.902  21.769  1.00 55.73  ? 107 LYS D CE  1 
ATOM   2408 N NZ  . LYS B 2 108 ? 12.252  -10.346 21.350  1.00 57.20  ? 107 LYS D NZ  1 
ATOM   2409 N N   . ARG B 2 109 ? 17.267  -9.756  24.660  1.00 56.02  ? 108 ARG D N   1 
ATOM   2410 C CA  . ARG B 2 109 ? 18.017  -10.687 25.484  1.00 61.08  ? 108 ARG D CA  1 
ATOM   2411 C C   . ARG B 2 109 ? 17.051  -11.719 26.039  1.00 60.19  ? 108 ARG D C   1 
ATOM   2412 O O   . ARG B 2 109 ? 15.867  -11.742 25.698  1.00 61.52  ? 108 ARG D O   1 
ATOM   2413 C CB  . ARG B 2 109 ? 18.791  -9.950  26.586  1.00 65.63  ? 108 ARG D CB  1 
ATOM   2414 C CG  . ARG B 2 109 ? 18.038  -8.763  27.190  1.00 64.74  ? 108 ARG D CG  1 
ATOM   2415 C CD  . ARG B 2 109 ? 18.362  -8.536  28.648  1.00 61.72  ? 108 ARG D CD  1 
ATOM   2416 N NE  . ARG B 2 109 ? 17.768  -9.580  29.468  1.00 67.22  ? 108 ARG D NE  1 
ATOM   2417 C CZ  . ARG B 2 109 ? 18.432  -10.333 30.335  1.00 66.62  ? 108 ARG D CZ  1 
ATOM   2418 N NH1 . ARG B 2 109 ? 19.701  -10.098 30.630  1.00 68.26  ? 108 ARG D NH1 1 
ATOM   2419 N NH2 . ARG B 2 109 ? 17.809  -11.353 30.912  1.00 64.16  ? 108 ARG D NH2 1 
ATOM   2420 N N   . THR B 2 110 ? 17.564  -12.597 26.880  1.00 61.39  ? 109 THR D N   1 
ATOM   2421 C CA  . THR B 2 110 ? 16.679  -13.567 27.499  1.00 66.50  ? 109 THR D CA  1 
ATOM   2422 C C   . THR B 2 110 ? 15.808  -12.898 28.559  1.00 65.82  ? 109 THR D C   1 
ATOM   2423 O O   . THR B 2 110 ? 16.145  -11.854 29.121  1.00 65.05  ? 109 THR D O   1 
ATOM   2424 C CB  . THR B 2 110 ? 17.486  -14.710 28.106  1.00 62.99  ? 109 THR D CB  1 
ATOM   2425 O OG1 . THR B 2 110 ? 18.407  -14.181 29.068  1.00 61.55  ? 109 THR D OG1 1 
ATOM   2426 C CG2 . THR B 2 110 ? 18.262  -15.422 27.021  1.00 64.51  ? 109 THR D CG2 1 
ATOM   2427 N N   . VAL B 2 111 ? 14.677  -13.533 28.846  1.00 68.96  ? 110 VAL D N   1 
ATOM   2428 C CA  . VAL B 2 111 ? 13.702  -12.948 29.760  1.00 72.31  ? 110 VAL D CA  1 
ATOM   2429 C C   . VAL B 2 111 ? 14.220  -12.997 31.197  1.00 70.90  ? 110 VAL D C   1 
ATOM   2430 O O   . VAL B 2 111 ? 14.506  -14.070 31.737  1.00 66.97  ? 110 VAL D O   1 
ATOM   2431 C CB  . VAL B 2 111 ? 12.359  -13.675 29.620  1.00 73.98  ? 110 VAL D CB  1 
ATOM   2432 C CG1 . VAL B 2 111 ? 11.545  -13.536 30.886  1.00 71.87  ? 110 VAL D CG1 1 
ATOM   2433 C CG2 . VAL B 2 111 ? 11.623  -13.108 28.440  1.00 79.08  ? 110 VAL D CG2 1 
ATOM   2434 N N   . ALA B 2 112 ? 14.355  -11.829 31.824  1.00 73.96  ? 111 ALA D N   1 
ATOM   2435 C CA  . ALA B 2 112 ? 14.844  -11.722 33.191  1.00 65.33  ? 111 ALA D CA  1 
ATOM   2436 C C   . ALA B 2 112 ? 13.691  -11.424 34.125  1.00 66.42  ? 111 ALA D C   1 
ATOM   2437 O O   . ALA B 2 112 ? 12.746  -10.717 33.763  1.00 64.34  ? 111 ALA D O   1 
ATOM   2438 C CB  . ALA B 2 112 ? 15.894  -10.625 33.346  1.00 67.92  ? 111 ALA D CB  1 
ATOM   2439 N N   . ALA B 2 113 ? 13.790  -11.957 35.315  1.00 70.00  ? 112 ALA D N   1 
ATOM   2440 C CA  . ALA B 2 113 ? 12.805  -11.766 36.353  1.00 66.45  ? 112 ALA D CA  1 
ATOM   2441 C C   . ALA B 2 113 ? 13.155  -10.524 37.169  1.00 65.74  ? 112 ALA D C   1 
ATOM   2442 O O   . ALA B 2 113 ? 14.339  -10.216 37.357  1.00 64.48  ? 112 ALA D O   1 
ATOM   2443 C CB  . ALA B 2 113 ? 12.757  -12.990 37.246  1.00 70.10  ? 112 ALA D CB  1 
ATOM   2444 N N   . PRO B 2 114 ? 12.153  -9.769  37.617  1.00 66.53  ? 113 PRO D N   1 
ATOM   2445 C CA  . PRO B 2 114 ? 12.438  -8.593  38.444  1.00 66.02  ? 113 PRO D CA  1 
ATOM   2446 C C   . PRO B 2 114 ? 12.547  -8.967  39.922  1.00 68.83  ? 113 PRO D C   1 
ATOM   2447 O O   . PRO B 2 114 ? 11.747  -9.740  40.454  1.00 68.94  ? 113 PRO D O   1 
ATOM   2448 C CB  . PRO B 2 114 ? 11.221  -7.695  38.183  1.00 66.51  ? 113 PRO D CB  1 
ATOM   2449 C CG  . PRO B 2 114 ? 10.101  -8.668  37.975  1.00 68.20  ? 113 PRO D CG  1 
ATOM   2450 C CD  . PRO B 2 114 ? 10.740  -9.801  37.181  1.00 67.75  ? 113 PRO D CD  1 
ATOM   2451 N N   . SER B 2 115 ? 13.552  -8.414  40.594  1.00 67.66  ? 114 SER D N   1 
ATOM   2452 C CA  . SER B 2 115 ? 13.581  -8.424  42.053  1.00 68.28  ? 114 SER D CA  1 
ATOM   2453 C C   . SER B 2 115 ? 12.590  -7.374  42.542  1.00 68.94  ? 114 SER D C   1 
ATOM   2454 O O   . SER B 2 115 ? 12.782  -6.175  42.305  1.00 69.52  ? 114 SER D O   1 
ATOM   2455 C CB  . SER B 2 115 ? 14.989  -8.125  42.563  1.00 68.57  ? 114 SER D CB  1 
ATOM   2456 O OG  . SER B 2 115 ? 15.951  -8.882  41.849  1.00 73.83  ? 114 SER D OG  1 
ATOM   2457 N N   . VAL B 2 116 ? 11.531  -7.807  43.206  1.00 69.87  ? 115 VAL D N   1 
ATOM   2458 C CA  . VAL B 2 116 ? 10.478  -6.903  43.655  1.00 70.72  ? 115 VAL D CA  1 
ATOM   2459 C C   . VAL B 2 116 ? 10.705  -6.544  45.122  1.00 75.01  ? 115 VAL D C   1 
ATOM   2460 O O   . VAL B 2 116 ? 10.665  -7.420  45.995  1.00 75.88  ? 115 VAL D O   1 
ATOM   2461 C CB  . VAL B 2 116 ? 9.100   -7.540  43.445  1.00 72.46  ? 115 VAL D CB  1 
ATOM   2462 C CG1 . VAL B 2 116 ? 8.014   -6.691  44.055  1.00 74.88  ? 115 VAL D CG1 1 
ATOM   2463 C CG2 . VAL B 2 116 ? 8.862   -7.693  41.981  1.00 73.48  ? 115 VAL D CG2 1 
ATOM   2464 N N   . PHE B 2 117 ? 10.931  -5.249  45.400  1.00 73.80  ? 116 PHE D N   1 
ATOM   2465 C CA  . PHE B 2 117 ? 11.148  -4.753  46.758  1.00 71.10  ? 116 PHE D CA  1 
ATOM   2466 C C   . PHE B 2 117 ? 10.109  -3.697  47.110  1.00 71.86  ? 116 PHE D C   1 
ATOM   2467 O O   . PHE B 2 117 ? 9.751   -2.867  46.274  1.00 72.20  ? 116 PHE D O   1 
ATOM   2468 C CB  . PHE B 2 117 ? 12.531  -4.152  46.902  1.00 69.50  ? 116 PHE D CB  1 
ATOM   2469 C CG  . PHE B 2 117 ? 13.648  -5.070  46.503  1.00 70.73  ? 116 PHE D CG  1 
ATOM   2470 C CD1 . PHE B 2 117 ? 13.595  -6.435  46.721  1.00 78.73  ? 116 PHE D CD1 1 
ATOM   2471 C CD2 . PHE B 2 117 ? 14.714  -4.566  45.799  1.00 73.25  ? 116 PHE D CD2 1 
ATOM   2472 C CE1 . PHE B 2 117 ? 14.646  -7.266  46.311  1.00 81.25  ? 116 PHE D CE1 1 
ATOM   2473 C CE2 . PHE B 2 117 ? 15.754  -5.374  45.387  1.00 75.38  ? 116 PHE D CE2 1 
ATOM   2474 C CZ  . PHE B 2 117 ? 15.723  -6.728  45.644  1.00 77.53  ? 116 PHE D CZ  1 
ATOM   2475 N N   . ILE B 2 118 ? 9.643   -3.721  48.356  1.00 73.34  ? 117 ILE D N   1 
ATOM   2476 C CA  . ILE B 2 118 ? 8.657   -2.769  48.858  1.00 74.28  ? 117 ILE D CA  1 
ATOM   2477 C C   . ILE B 2 118 ? 9.314   -1.929  49.947  1.00 74.02  ? 117 ILE D C   1 
ATOM   2478 O O   . ILE B 2 118 ? 10.224  -2.394  50.640  1.00 73.87  ? 117 ILE D O   1 
ATOM   2479 C CB  . ILE B 2 118 ? 7.403   -3.489  49.393  1.00 76.54  ? 117 ILE D CB  1 
ATOM   2480 C CG1 . ILE B 2 118 ? 6.444   -2.498  50.040  1.00 78.37  ? 117 ILE D CG1 1 
ATOM   2481 C CG2 . ILE B 2 118 ? 7.796   -4.608  50.355  1.00 77.47  ? 117 ILE D CG2 1 
ATOM   2482 C CD1 . ILE B 2 118 ? 5.652   -1.733  49.050  1.00 77.28  ? 117 ILE D CD1 1 
ATOM   2483 N N   . PHE B 2 119 ? 8.856   -0.674  50.085  1.00 75.23  ? 118 PHE D N   1 
ATOM   2484 C CA  . PHE B 2 119 ? 9.501   0.370   50.911  1.00 73.89  ? 118 PHE D CA  1 
ATOM   2485 C C   . PHE B 2 119 ? 8.432   1.172   51.651  1.00 78.15  ? 118 PHE D C   1 
ATOM   2486 O O   . PHE B 2 119 ? 7.469   1.622   51.012  1.00 80.61  ? 118 PHE D O   1 
ATOM   2487 C CB  . PHE B 2 119 ? 10.319  1.327   50.052  1.00 71.65  ? 118 PHE D CB  1 
ATOM   2488 C CG  . PHE B 2 119 ? 11.581  0.759   49.486  1.00 70.61  ? 118 PHE D CG  1 
ATOM   2489 C CD1 . PHE B 2 119 ? 12.714  0.637   50.268  1.00 70.75  ? 118 PHE D CD1 1 
ATOM   2490 C CD2 . PHE B 2 119 ? 11.674  0.455   48.137  1.00 70.31  ? 118 PHE D CD2 1 
ATOM   2491 C CE1 . PHE B 2 119 ? 13.908  0.171   49.728  1.00 72.09  ? 118 PHE D CE1 1 
ATOM   2492 C CE2 . PHE B 2 119 ? 12.863  -0.021  47.600  1.00 69.31  ? 118 PHE D CE2 1 
ATOM   2493 C CZ  . PHE B 2 119 ? 13.980  -0.164  48.398  1.00 68.50  ? 118 PHE D CZ  1 
ATOM   2494 N N   . PRO B 2 120 ? 8.581   1.426   52.954  1.00 78.76  ? 119 PRO D N   1 
ATOM   2495 C CA  . PRO B 2 120 ? 7.526   2.142   53.697  1.00 84.19  ? 119 PRO D CA  1 
ATOM   2496 C C   . PRO B 2 120 ? 7.757   3.646   53.713  1.00 83.97  ? 119 PRO D C   1 
ATOM   2497 O O   . PRO B 2 120 ? 8.878   4.123   53.481  1.00 76.56  ? 119 PRO D O   1 
ATOM   2498 C CB  . PRO B 2 120 ? 7.633   1.545   55.108  1.00 82.66  ? 119 PRO D CB  1 
ATOM   2499 C CG  . PRO B 2 120 ? 9.096   1.301   55.259  1.00 81.07  ? 119 PRO D CG  1 
ATOM   2500 C CD  . PRO B 2 120 ? 9.619   0.906   53.865  1.00 78.06  ? 119 PRO D CD  1 
ATOM   2501 N N   . PRO B 2 121 ? 6.709   4.417   54.017  1.00 88.20  ? 120 PRO D N   1 
ATOM   2502 C CA  . PRO B 2 121 ? 6.779   5.882   53.897  1.00 90.18  ? 120 PRO D CA  1 
ATOM   2503 C C   . PRO B 2 121 ? 7.898   6.596   54.653  1.00 93.02  ? 120 PRO D C   1 
ATOM   2504 O O   . PRO B 2 121 ? 8.224   7.728   54.268  1.00 95.66  ? 120 PRO D O   1 
ATOM   2505 C CB  . PRO B 2 121 ? 5.407   6.317   54.425  1.00 92.01  ? 120 PRO D CB  1 
ATOM   2506 C CG  . PRO B 2 121 ? 4.508   5.212   54.032  1.00 93.65  ? 120 PRO D CG  1 
ATOM   2507 C CD  . PRO B 2 121 ? 5.316   3.941   54.077  1.00 92.96  ? 120 PRO D CD  1 
ATOM   2508 N N   . SER B 2 122 ? 8.475   6.017   55.706  1.00 85.75  ? 121 SER D N   1 
ATOM   2509 C CA  . SER B 2 122 ? 9.447   6.734   56.535  1.00 82.06  ? 121 SER D CA  1 
ATOM   2510 C C   . SER B 2 122 ? 8.830   7.914   57.266  1.00 81.61  ? 121 SER D C   1 
ATOM   2511 O O   . SER B 2 122 ? 8.009   8.659   56.720  1.00 80.97  ? 121 SER D O   1 
ATOM   2512 C CB  . SER B 2 122 ? 10.635  7.264   55.736  1.00 80.38  ? 121 SER D CB  1 
ATOM   2513 O OG  . SER B 2 122 ? 10.631  8.690   55.754  1.00 74.36  ? 121 SER D OG  1 
ATOM   2514 N N   . ASP B 2 123 ? 9.283   8.120   58.493  1.00 79.46  ? 122 ASP D N   1 
ATOM   2515 C CA  . ASP B 2 123 ? 8.609   9.028   59.395  1.00 79.07  ? 122 ASP D CA  1 
ATOM   2516 C C   . ASP B 2 123 ? 8.961   10.486  59.135  1.00 78.29  ? 122 ASP D C   1 
ATOM   2517 O O   . ASP B 2 123 ? 8.183   11.368  59.518  1.00 79.30  ? 122 ASP D O   1 
ATOM   2518 C CB  . ASP B 2 123 ? 8.925   8.598   60.831  1.00 81.42  ? 122 ASP D CB  1 
ATOM   2519 C CG  . ASP B 2 123 ? 9.292   7.104   60.928  1.00 82.30  ? 122 ASP D CG  1 
ATOM   2520 O OD1 . ASP B 2 123 ? 8.423   6.248   60.634  1.00 80.96  ? 122 ASP D OD1 1 
ATOM   2521 O OD2 . ASP B 2 123 ? 10.453  6.788   61.283  1.00 82.12  ? 122 ASP D OD2 1 
ATOM   2522 N N   . GLU B 2 124 ? 10.099  10.766  58.491  1.00 76.61  ? 123 GLU D N   1 
ATOM   2523 C CA  . GLU B 2 124 ? 10.359  12.135  58.049  1.00 76.76  ? 123 GLU D CA  1 
ATOM   2524 C C   . GLU B 2 124 ? 9.181   12.661  57.257  1.00 78.78  ? 123 GLU D C   1 
ATOM   2525 O O   . GLU B 2 124 ? 8.704   13.775  57.486  1.00 81.18  ? 123 GLU D O   1 
ATOM   2526 C CB  . GLU B 2 124 ? 11.613  12.204  57.189  1.00 74.01  ? 123 GLU D CB  1 
ATOM   2527 C CG  . GLU B 2 124 ? 12.874  11.975  57.932  1.00 73.54  ? 123 GLU D CG  1 
ATOM   2528 C CD  . GLU B 2 124 ? 13.285  10.543  57.837  1.00 73.20  ? 123 GLU D CD  1 
ATOM   2529 O OE1 . GLU B 2 124 ? 12.393  9.690   58.009  1.00 74.20  ? 123 GLU D OE1 1 
ATOM   2530 O OE2 . GLU B 2 124 ? 14.475  10.273  57.576  1.00 72.00  ? 123 GLU D OE2 1 
ATOM   2531 N N   . GLN B 2 125 ? 8.673   11.847  56.339  1.00 77.88  ? 124 GLN D N   1 
ATOM   2532 C CA  . GLN B 2 125 ? 7.581   12.295  55.491  1.00 79.48  ? 124 GLN D CA  1 
ATOM   2533 C C   . GLN B 2 125 ? 6.273   12.391  56.268  1.00 79.95  ? 124 GLN D C   1 
ATOM   2534 O O   . GLN B 2 125 ? 5.563   13.400  56.176  1.00 80.77  ? 124 GLN D O   1 
ATOM   2535 C CB  . GLN B 2 125 ? 7.442   11.361  54.295  1.00 79.49  ? 124 GLN D CB  1 
ATOM   2536 C CG  . GLN B 2 125 ? 6.568   11.927  53.196  1.00 82.58  ? 124 GLN D CG  1 
ATOM   2537 C CD  . GLN B 2 125 ? 6.231   10.907  52.126  1.00 84.09  ? 124 GLN D CD  1 
ATOM   2538 O OE1 . GLN B 2 125 ? 6.774   9.793   52.122  1.00 83.16  ? 124 GLN D OE1 1 
ATOM   2539 N NE2 . GLN B 2 125 ? 5.334   11.282  51.206  1.00 81.92  ? 124 GLN D NE2 1 
ATOM   2540 N N   . LEU B 2 126 ? 5.945   11.363  57.059  1.00 80.50  ? 125 LEU D N   1 
ATOM   2541 C CA  . LEU B 2 126 ? 4.669   11.359  57.773  1.00 82.68  ? 125 LEU D CA  1 
ATOM   2542 C C   . LEU B 2 126 ? 4.556   12.476  58.800  1.00 85.83  ? 125 LEU D C   1 
ATOM   2543 O O   . LEU B 2 126 ? 3.518   12.583  59.470  1.00 85.34  ? 125 LEU D O   1 
ATOM   2544 C CB  . LEU B 2 126 ? 4.450   10.033  58.477  1.00 82.53  ? 125 LEU D CB  1 
ATOM   2545 C CG  . LEU B 2 126 ? 4.568   8.806   57.604  1.00 82.04  ? 125 LEU D CG  1 
ATOM   2546 C CD1 . LEU B 2 126 ? 5.475   7.805   58.294  1.00 83.82  ? 125 LEU D CD1 1 
ATOM   2547 C CD2 . LEU B 2 126 ? 3.178   8.257   57.365  1.00 84.60  ? 125 LEU D CD2 1 
ATOM   2548 N N   . LYS B 2 127 ? 5.605   13.282  58.961  1.00 84.77  ? 126 LYS D N   1 
ATOM   2549 C CA  . LYS B 2 127 ? 5.493   14.488  59.765  1.00 84.45  ? 126 LYS D CA  1 
ATOM   2550 C C   . LYS B 2 127 ? 4.596   15.518  59.088  1.00 83.67  ? 126 LYS D C   1 
ATOM   2551 O O   . LYS B 2 127 ? 3.773   16.160  59.747  1.00 86.64  ? 126 LYS D O   1 
ATOM   2552 C CB  . LYS B 2 127 ? 6.883   15.063  60.025  1.00 83.74  ? 126 LYS D CB  1 
ATOM   2553 C CG  . LYS B 2 127 ? 6.851   16.444  60.618  1.00 87.45  ? 126 LYS D CG  1 
ATOM   2554 C CD  . LYS B 2 127 ? 7.870   16.591  61.742  1.00 95.09  ? 126 LYS D CD  1 
ATOM   2555 C CE  . LYS B 2 127 ? 7.601   17.869  62.530  1.00 97.88  ? 126 LYS D CE  1 
ATOM   2556 N NZ  . LYS B 2 127 ? 8.706   18.242  63.441  1.00 99.16  ? 126 LYS D NZ  1 
ATOM   2557 N N   . SER B 2 128 ? 4.713   15.669  57.773  1.00 84.66  ? 127 SER D N   1 
ATOM   2558 C CA  . SER B 2 128 ? 4.015   16.724  57.049  1.00 86.12  ? 127 SER D CA  1 
ATOM   2559 C C   . SER B 2 128 ? 2.689   16.272  56.439  1.00 89.35  ? 127 SER D C   1 
ATOM   2560 O O   . SER B 2 128 ? 2.112   17.019  55.638  1.00 90.21  ? 127 SER D O   1 
ATOM   2561 C CB  . SER B 2 128 ? 4.912   17.298  55.949  1.00 81.15  ? 127 SER D CB  1 
ATOM   2562 O OG  . SER B 2 128 ? 6.257   16.882  56.110  1.00 81.94  ? 127 SER D OG  1 
ATOM   2563 N N   . GLY B 2 129 ? 2.212   15.069  56.764  1.00 91.23  ? 128 GLY D N   1 
ATOM   2564 C CA  . GLY B 2 129 ? 0.834   14.696  56.486  1.00 96.01  ? 128 GLY D CA  1 
ATOM   2565 C C   . GLY B 2 129 ? 0.555   13.934  55.205  1.00 97.31  ? 128 GLY D C   1 
ATOM   2566 O O   . GLY B 2 129 ? -0.618  13.806  54.830  1.00 100.37 ? 128 GLY D O   1 
ATOM   2567 N N   . THR B 2 130 ? 1.574   13.414  54.527  1.00 92.29  ? 129 THR D N   1 
ATOM   2568 C CA  . THR B 2 130 ? 1.367   12.626  53.316  1.00 93.49  ? 129 THR D CA  1 
ATOM   2569 C C   . THR B 2 130 ? 2.390   11.496  53.270  1.00 92.22  ? 129 THR D C   1 
ATOM   2570 O O   . THR B 2 130 ? 3.561   11.694  53.605  1.00 90.20  ? 129 THR D O   1 
ATOM   2571 C CB  . THR B 2 130 ? 1.459   13.508  52.056  1.00 90.94  ? 129 THR D CB  1 
ATOM   2572 O OG1 . THR B 2 130 ? 0.456   14.530  52.122  1.00 89.93  ? 129 THR D OG1 1 
ATOM   2573 C CG2 . THR B 2 130 ? 1.273   12.690  50.787  1.00 88.09  ? 129 THR D CG2 1 
ATOM   2574 N N   . ALA B 2 131 ? 1.941   10.309  52.863  1.00 89.86  ? 130 ALA D N   1 
ATOM   2575 C CA  . ALA B 2 131 ? 2.751   9.097   52.913  1.00 87.51  ? 130 ALA D CA  1 
ATOM   2576 C C   . ALA B 2 131 ? 2.876   8.472   51.525  1.00 84.08  ? 130 ALA D C   1 
ATOM   2577 O O   . ALA B 2 131 ? 1.863   8.209   50.869  1.00 85.15  ? 130 ALA D O   1 
ATOM   2578 C CB  . ALA B 2 131 ? 2.137   8.094   53.897  1.00 90.60  ? 130 ALA D CB  1 
ATOM   2579 N N   . SER B 2 132 ? 4.114   8.216   51.089  1.00 83.29  ? 131 SER D N   1 
ATOM   2580 C CA  . SER B 2 132 ? 4.392   7.605   49.788  1.00 84.37  ? 131 SER D CA  1 
ATOM   2581 C C   . SER B 2 132 ? 5.126   6.281   49.973  1.00 81.68  ? 131 SER D C   1 
ATOM   2582 O O   . SER B 2 132 ? 6.247   6.251   50.491  1.00 82.45  ? 131 SER D O   1 
ATOM   2583 C CB  . SER B 2 132 ? 5.222   8.530   48.881  1.00 83.52  ? 131 SER D CB  1 
ATOM   2584 O OG  . SER B 2 132 ? 4.578   9.764   48.599  1.00 84.09  ? 131 SER D OG  1 
ATOM   2585 N N   . VAL B 2 133 ? 4.508   5.198   49.519  1.00 79.40  ? 132 VAL D N   1 
ATOM   2586 C CA  . VAL B 2 133 ? 5.118   3.875   49.504  1.00 80.64  ? 132 VAL D CA  1 
ATOM   2587 C C   . VAL B 2 133 ? 5.410   3.497   48.054  1.00 83.09  ? 132 VAL D C   1 
ATOM   2588 O O   . VAL B 2 133 ? 4.559   3.672   47.172  1.00 82.43  ? 132 VAL D O   1 
ATOM   2589 C CB  . VAL B 2 133 ? 4.214   2.843   50.204  1.00 80.61  ? 132 VAL D CB  1 
ATOM   2590 C CG1 . VAL B 2 133 ? 2.771   3.034   49.804  1.00 79.23  ? 132 VAL D CG1 1 
ATOM   2591 C CG2 . VAL B 2 133 ? 4.648   1.442   49.866  1.00 79.26  ? 132 VAL D CG2 1 
ATOM   2592 N N   . VAL B 2 134 ? 6.622   3.006   47.798  1.00 81.42  ? 133 VAL D N   1 
ATOM   2593 C CA  . VAL B 2 134 ? 7.045   2.675   46.444  1.00 80.45  ? 133 VAL D CA  1 
ATOM   2594 C C   . VAL B 2 134 ? 7.413   1.200   46.379  1.00 81.90  ? 133 VAL D C   1 
ATOM   2595 O O   . VAL B 2 134 ? 7.981   0.642   47.326  1.00 77.38  ? 133 VAL D O   1 
ATOM   2596 C CB  . VAL B 2 134 ? 8.222   3.555   45.962  1.00 76.41  ? 133 VAL D CB  1 
ATOM   2597 C CG1 . VAL B 2 134 ? 8.238   4.880   46.684  1.00 71.45  ? 133 VAL D CG1 1 
ATOM   2598 C CG2 . VAL B 2 134 ? 9.560   2.850   46.113  1.00 73.98  ? 133 VAL D CG2 1 
ATOM   2599 N N   . CYS B 2 135 ? 7.067   0.571   45.258  1.00 84.31  ? 134 CYS D N   1 
ATOM   2600 C CA  . CYS B 2 135 ? 7.548   -0.757  44.918  1.00 84.09  ? 134 CYS D CA  1 
ATOM   2601 C C   . CYS B 2 135 ? 8.596   -0.627  43.825  1.00 82.08  ? 134 CYS D C   1 
ATOM   2602 O O   . CYS B 2 135 ? 8.435   0.165   42.890  1.00 81.63  ? 134 CYS D O   1 
ATOM   2603 C CB  . CYS B 2 135 ? 6.412   -1.670  44.450  1.00 85.45  ? 134 CYS D CB  1 
ATOM   2604 S SG  . CYS B 2 135 ? 6.874   -3.424  44.481  1.00 96.73  ? 134 CYS D SG  1 
ATOM   2605 N N   . LEU B 2 136 ? 9.670   -1.392  43.947  1.00 74.29  ? 135 LEU D N   1 
ATOM   2606 C CA  . LEU B 2 136 ? 10.752  -1.377  42.977  1.00 70.09  ? 135 LEU D CA  1 
ATOM   2607 C C   . LEU B 2 136 ? 10.747  -2.690  42.198  1.00 70.00  ? 135 LEU D C   1 
ATOM   2608 O O   . LEU B 2 136 ? 10.550  -3.762  42.783  1.00 71.10  ? 135 LEU D O   1 
ATOM   2609 C CB  . LEU B 2 136 ? 12.087  -1.186  43.690  1.00 66.06  ? 135 LEU D CB  1 
ATOM   2610 C CG  . LEU B 2 136 ? 13.399  -1.173  42.911  1.00 66.33  ? 135 LEU D CG  1 
ATOM   2611 C CD1 . LEU B 2 136 ? 14.436  -0.634  43.837  1.00 66.23  ? 135 LEU D CD1 1 
ATOM   2612 C CD2 . LEU B 2 136 ? 13.844  -2.509  42.416  1.00 69.39  ? 135 LEU D CD2 1 
ATOM   2613 N N   . LEU B 2 137 ? 10.996  -2.611  40.885  1.00 65.89  ? 136 LEU D N   1 
ATOM   2614 C CA  . LEU B 2 137 ? 11.132  -3.791  40.025  1.00 66.35  ? 136 LEU D CA  1 
ATOM   2615 C C   . LEU B 2 137 ? 12.526  -3.775  39.398  1.00 64.77  ? 136 LEU D C   1 
ATOM   2616 O O   . LEU B 2 137 ? 12.738  -3.097  38.390  1.00 68.00  ? 136 LEU D O   1 
ATOM   2617 C CB  . LEU B 2 137 ? 10.043  -3.811  38.953  1.00 66.05  ? 136 LEU D CB  1 
ATOM   2618 C CG  . LEU B 2 137 ? 8.674   -4.366  39.381  1.00 68.17  ? 136 LEU D CG  1 
ATOM   2619 C CD1 . LEU B 2 137 ? 8.016   -3.529  40.465  1.00 69.15  ? 136 LEU D CD1 1 
ATOM   2620 C CD2 . LEU B 2 137 ? 7.753   -4.483  38.201  1.00 68.41  ? 136 LEU D CD2 1 
ATOM   2621 N N   . ASN B 2 138 ? 13.474  -4.534  39.958  1.00 63.65  ? 137 ASN D N   1 
ATOM   2622 C CA  . ASN B 2 138 ? 14.884  -4.416  39.586  1.00 63.84  ? 137 ASN D CA  1 
ATOM   2623 C C   . ASN B 2 138 ? 15.259  -5.429  38.509  1.00 64.65  ? 137 ASN D C   1 
ATOM   2624 O O   . ASN B 2 138 ? 15.040  -6.638  38.672  1.00 64.42  ? 137 ASN D O   1 
ATOM   2625 C CB  . ASN B 2 138 ? 15.797  -4.589  40.805  1.00 65.93  ? 137 ASN D CB  1 
ATOM   2626 C CG  . ASN B 2 138 ? 17.179  -3.968  40.596  1.00 64.59  ? 137 ASN D CG  1 
ATOM   2627 O OD1 . ASN B 2 138 ? 18.206  -4.579  40.873  1.00 65.95  ? 137 ASN D OD1 1 
ATOM   2628 N ND2 . ASN B 2 138 ? 17.199  -2.764  40.063  1.00 65.46  ? 137 ASN D ND2 1 
ATOM   2629 N N   . ASN B 2 139 ? 15.800  -4.916  37.404  1.00 63.65  ? 138 ASN D N   1 
ATOM   2630 C CA  . ASN B 2 139 ? 16.411  -5.685  36.315  1.00 64.78  ? 138 ASN D CA  1 
ATOM   2631 C C   . ASN B 2 139 ? 15.465  -6.742  35.745  1.00 64.50  ? 138 ASN D C   1 
ATOM   2632 O O   . ASN B 2 139 ? 15.561  -7.926  36.034  1.00 66.24  ? 138 ASN D O   1 
ATOM   2633 C CB  . ASN B 2 139 ? 17.723  -6.325  36.771  1.00 63.79  ? 138 ASN D CB  1 
ATOM   2634 C CG  . ASN B 2 139 ? 18.725  -5.299  37.233  1.00 66.15  ? 138 ASN D CG  1 
ATOM   2635 O OD1 . ASN B 2 139 ? 18.354  -4.249  37.761  1.00 66.36  ? 138 ASN D OD1 1 
ATOM   2636 N ND2 . ASN B 2 139 ? 20.000  -5.563  36.984  1.00 70.37  ? 138 ASN D ND2 1 
ATOM   2637 N N   . PHE B 2 140 ? 14.568  -6.293  34.884  1.00 65.00  ? 139 PHE D N   1 
ATOM   2638 C CA  . PHE B 2 140 ? 13.655  -7.217  34.230  1.00 66.05  ? 139 PHE D CA  1 
ATOM   2639 C C   . PHE B 2 140 ? 13.583  -6.946  32.731  1.00 68.95  ? 139 PHE D C   1 
ATOM   2640 O O   . PHE B 2 140 ? 13.446  -5.796  32.307  1.00 65.89  ? 139 PHE D O   1 
ATOM   2641 C CB  . PHE B 2 140 ? 12.265  -7.143  34.853  1.00 65.51  ? 139 PHE D CB  1 
ATOM   2642 C CG  . PHE B 2 140 ? 11.633  -5.792  34.769  1.00 67.15  ? 139 PHE D CG  1 
ATOM   2643 C CD1 . PHE B 2 140 ? 10.509  -5.594  33.982  1.00 68.78  ? 139 PHE D CD1 1 
ATOM   2644 C CD2 . PHE B 2 140 ? 12.139  -4.726  35.504  1.00 64.34  ? 139 PHE D CD2 1 
ATOM   2645 C CE1 . PHE B 2 140 ? 9.911   -4.359  33.906  1.00 68.67  ? 139 PHE D CE1 1 
ATOM   2646 C CE2 . PHE B 2 140 ? 11.550  -3.488  35.433  1.00 67.15  ? 139 PHE D CE2 1 
ATOM   2647 C CZ  . PHE B 2 140 ? 10.427  -3.303  34.631  1.00 68.62  ? 139 PHE D CZ  1 
ATOM   2648 N N   . TYR B 2 141 ? 13.693  -8.012  31.940  1.00 71.40  ? 140 TYR D N   1 
ATOM   2649 C CA  . TYR B 2 141 ? 13.400  -8.020  30.525  1.00 71.98  ? 140 TYR D CA  1 
ATOM   2650 C C   . TYR B 2 141 ? 12.220  -8.953  30.294  1.00 72.85  ? 140 TYR D C   1 
ATOM   2651 O O   . TYR B 2 141 ? 12.187  -10.032 30.894  1.00 74.75  ? 140 TYR D O   1 
ATOM   2652 C CB  . TYR B 2 141 ? 14.593  -8.526  29.721  1.00 71.30  ? 140 TYR D CB  1 
ATOM   2653 C CG  . TYR B 2 141 ? 14.518  -8.225  28.236  1.00 68.62  ? 140 TYR D CG  1 
ATOM   2654 C CD1 . TYR B 2 141 ? 14.075  -6.991  27.755  1.00 69.60  ? 140 TYR D CD1 1 
ATOM   2655 C CD2 . TYR B 2 141 ? 14.752  -9.227  27.321  1.00 67.78  ? 140 TYR D CD2 1 
ATOM   2656 C CE1 . TYR B 2 141 ? 13.970  -6.752  26.390  1.00 69.16  ? 140 TYR D CE1 1 
ATOM   2657 C CE2 . TYR B 2 141 ? 14.642  -9.011  25.962  1.00 64.92  ? 140 TYR D CE2 1 
ATOM   2658 C CZ  . TYR B 2 141 ? 14.253  -7.780  25.497  1.00 66.59  ? 140 TYR D CZ  1 
ATOM   2659 O OH  . TYR B 2 141 ? 14.156  -7.602  24.143  1.00 64.96  ? 140 TYR D OH  1 
ATOM   2660 N N   . PRO B 2 142 ? 11.232  -8.596  29.452  1.00 74.88  ? 141 PRO D N   1 
ATOM   2661 C CA  . PRO B 2 142 ? 11.053  -7.343  28.715  1.00 74.13  ? 141 PRO D CA  1 
ATOM   2662 C C   . PRO B 2 142 ? 10.411  -6.281  29.583  1.00 75.63  ? 141 PRO D C   1 
ATOM   2663 O O   . PRO B 2 142 ? 10.097  -6.509  30.754  1.00 76.47  ? 141 PRO D O   1 
ATOM   2664 C CB  . PRO B 2 142 ? 10.127  -7.750  27.570  1.00 72.20  ? 141 PRO D CB  1 
ATOM   2665 C CG  . PRO B 2 142 ? 9.244   -8.792  28.190  1.00 76.01  ? 141 PRO D CG  1 
ATOM   2666 C CD  . PRO B 2 142 ? 10.089  -9.501  29.238  1.00 76.72  ? 141 PRO D CD  1 
ATOM   2667 N N   . ARG B 2 143 ? 10.181  -5.112  28.993  1.00 70.93  ? 142 ARG D N   1 
ATOM   2668 C CA  . ARG B 2 143 ? 9.488   -4.046  29.698  1.00 71.64  ? 142 ARG D CA  1 
ATOM   2669 C C   . ARG B 2 143 ? 8.064   -4.433  30.070  1.00 72.53  ? 142 ARG D C   1 
ATOM   2670 O O   . ARG B 2 143 ? 7.489   -3.851  30.995  1.00 73.93  ? 142 ARG D O   1 
ATOM   2671 C CB  . ARG B 2 143 ? 9.492   -2.794  28.828  1.00 73.36  ? 142 ARG D CB  1 
ATOM   2672 C CG  . ARG B 2 143 ? 8.555   -1.694  29.255  1.00 72.48  ? 142 ARG D CG  1 
ATOM   2673 C CD  . ARG B 2 143 ? 8.846   -0.510  28.407  1.00 70.16  ? 142 ARG D CD  1 
ATOM   2674 N NE  . ARG B 2 143 ? 10.287  -0.362  28.264  1.00 70.40  ? 142 ARG D NE  1 
ATOM   2675 C CZ  . ARG B 2 143 ? 10.923  0.799   28.312  1.00 70.97  ? 142 ARG D CZ  1 
ATOM   2676 N NH1 . ARG B 2 143 ? 10.273  1.932   28.525  1.00 70.23  ? 142 ARG D NH1 1 
ATOM   2677 N NH2 . ARG B 2 143 ? 12.244  0.825   28.146  1.00 72.55  ? 142 ARG D NH2 1 
ATOM   2678 N N   . GLU B 2 144 ? 7.468   -5.386  29.359  1.00 73.25  ? 143 GLU D N   1 
ATOM   2679 C CA  . GLU B 2 144 ? 6.100   -5.773  29.678  1.00 76.84  ? 143 GLU D CA  1 
ATOM   2680 C C   . GLU B 2 144 ? 5.982   -6.124  31.157  1.00 74.87  ? 143 GLU D C   1 
ATOM   2681 O O   . GLU B 2 144 ? 6.437   -7.185  31.598  1.00 75.01  ? 143 GLU D O   1 
ATOM   2682 C CB  . GLU B 2 144 ? 5.635   -6.942  28.790  1.00 79.75  ? 143 GLU D CB  1 
ATOM   2683 C CG  . GLU B 2 144 ? 4.176   -7.430  29.028  1.00 81.09  ? 143 GLU D CG  1 
ATOM   2684 C CD  . GLU B 2 144 ? 3.078   -6.392  28.758  1.00 84.62  ? 143 GLU D CD  1 
ATOM   2685 O OE1 . GLU B 2 144 ? 1.911   -6.810  28.610  1.00 87.82  ? 143 GLU D OE1 1 
ATOM   2686 O OE2 . GLU B 2 144 ? 3.361   -5.179  28.661  1.00 86.69  ? 143 GLU D OE2 1 
ATOM   2687 N N   . ALA B 2 145 ? 5.388   -5.224  31.933  1.00 78.73  ? 144 ALA D N   1 
ATOM   2688 C CA  . ALA B 2 145 ? 5.284   -5.429  33.369  1.00 79.89  ? 144 ALA D CA  1 
ATOM   2689 C C   . ALA B 2 145 ? 4.083   -4.677  33.913  1.00 83.45  ? 144 ALA D C   1 
ATOM   2690 O O   . ALA B 2 145 ? 3.874   -3.513  33.569  1.00 87.91  ? 144 ALA D O   1 
ATOM   2691 C CB  . ALA B 2 145 ? 6.559   -4.970  34.072  1.00 73.17  ? 144 ALA D CB  1 
ATOM   2692 N N   . LYS B 2 146 ? 3.304   -5.332  34.763  1.00 87.98  ? 145 LYS D N   1 
ATOM   2693 C CA  . LYS B 2 146 ? 2.226   -4.656  35.472  1.00 91.42  ? 145 LYS D CA  1 
ATOM   2694 C C   . LYS B 2 146 ? 2.309   -4.959  36.957  1.00 91.82  ? 145 LYS D C   1 
ATOM   2695 O O   . LYS B 2 146 ? 2.258   -6.124  37.363  1.00 93.68  ? 145 LYS D O   1 
ATOM   2696 C CB  . LYS B 2 146 ? 0.841   -5.054  34.953  1.00 94.03  ? 145 LYS D CB  1 
ATOM   2697 C CG  . LYS B 2 146 ? -0.203  -3.956  35.175  1.00 93.44  ? 145 LYS D CG  1 
ATOM   2698 C CD  . LYS B 2 146 ? 0.274   -2.607  34.598  1.00 93.30  ? 145 LYS D CD  1 
ATOM   2699 C CE  . LYS B 2 146 ? 0.652   -2.702  33.118  1.00 92.74  ? 145 LYS D CE  1 
ATOM   2700 N NZ  . LYS B 2 146 ? 0.559   -1.382  32.427  1.00 94.08  ? 145 LYS D NZ  1 
ATOM   2701 N N   . VAL B 2 147 ? 2.423   -3.914  37.755  1.00 91.50  ? 146 VAL D N   1 
ATOM   2702 C CA  . VAL B 2 147 ? 2.361   -4.021  39.199  1.00 88.82  ? 146 VAL D CA  1 
ATOM   2703 C C   . VAL B 2 147 ? 0.944   -3.685  39.613  1.00 92.67  ? 146 VAL D C   1 
ATOM   2704 O O   . VAL B 2 147 ? 0.296   -2.836  38.992  1.00 93.34  ? 146 VAL D O   1 
ATOM   2705 C CB  . VAL B 2 147 ? 3.372   -3.075  39.861  1.00 85.19  ? 146 VAL D CB  1 
ATOM   2706 C CG1 . VAL B 2 147 ? 4.747   -3.449  39.441  1.00 82.92  ? 146 VAL D CG1 1 
ATOM   2707 C CG2 . VAL B 2 147 ? 3.081   -1.648  39.475  1.00 86.96  ? 146 VAL D CG2 1 
ATOM   2708 N N   . GLN B 2 148 ? 0.447   -4.364  40.645  1.00 91.78  ? 147 GLN D N   1 
ATOM   2709 C CA  . GLN B 2 148 ? -0.862  -4.082  41.221  1.00 95.00  ? 147 GLN D CA  1 
ATOM   2710 C C   . GLN B 2 148 ? -0.714  -3.727  42.696  1.00 98.36  ? 147 GLN D C   1 
ATOM   2711 O O   . GLN B 2 148 ? -0.161  -4.512  43.474  1.00 98.00  ? 147 GLN D O   1 
ATOM   2712 C CB  . GLN B 2 148 ? -1.809  -5.278  41.067  1.00 99.09  ? 147 GLN D CB  1 
ATOM   2713 C CG  . GLN B 2 148 ? -3.087  -5.030  40.245  1.00 102.90 ? 147 GLN D CG  1 
ATOM   2714 C CD  . GLN B 2 148 ? -3.985  -3.883  40.747  1.00 105.11 ? 147 GLN D CD  1 
ATOM   2715 O OE1 . GLN B 2 148 ? -3.628  -3.114  41.639  1.00 104.78 ? 147 GLN D OE1 1 
ATOM   2716 N NE2 . GLN B 2 148 ? -5.167  -3.780  40.158  1.00 110.02 ? 147 GLN D NE2 1 
ATOM   2717 N N   . TRP B 2 149 ? -1.222  -2.555  43.084  1.00 100.18 ? 148 TRP D N   1 
ATOM   2718 C CA  . TRP B 2 149 ? -1.130  -2.085  44.463  1.00 97.92  ? 148 TRP D CA  1 
ATOM   2719 C C   . TRP B 2 149 ? -2.324  -2.590  45.255  1.00 98.95  ? 148 TRP D C   1 
ATOM   2720 O O   . TRP B 2 149 ? -3.471  -2.418  44.833  1.00 102.50 ? 148 TRP D O   1 
ATOM   2721 C CB  . TRP B 2 149 ? -1.079  -0.559  44.517  1.00 97.74  ? 148 TRP D CB  1 
ATOM   2722 C CG  . TRP B 2 149 ? 0.300   -0.018  44.344  1.00 93.78  ? 148 TRP D CG  1 
ATOM   2723 C CD1 . TRP B 2 149 ? 0.838   0.475   43.196  1.00 95.17  ? 148 TRP D CD1 1 
ATOM   2724 C CD2 . TRP B 2 149 ? 1.325   0.082   45.342  1.00 91.75  ? 148 TRP D CD2 1 
ATOM   2725 N NE1 . TRP B 2 149 ? 2.134   0.880   43.410  1.00 91.40  ? 148 TRP D NE1 1 
ATOM   2726 C CE2 . TRP B 2 149 ? 2.458   0.650   44.720  1.00 88.69  ? 148 TRP D CE2 1 
ATOM   2727 C CE3 . TRP B 2 149 ? 1.395   -0.248  46.700  1.00 90.74  ? 148 TRP D CE3 1 
ATOM   2728 C CZ2 . TRP B 2 149 ? 3.645   0.892   45.403  1.00 84.39  ? 148 TRP D CZ2 1 
ATOM   2729 C CZ3 . TRP B 2 149 ? 2.576   -0.007  47.379  1.00 86.34  ? 148 TRP D CZ3 1 
ATOM   2730 C CH2 . TRP B 2 149 ? 3.687   0.557   46.727  1.00 84.59  ? 148 TRP D CH2 1 
ATOM   2731 N N   . LYS B 2 150 ? -2.054  -3.195  46.410  1.00 101.13 ? 149 LYS D N   1 
ATOM   2732 C CA  . LYS B 2 150 ? -3.085  -3.791  47.256  1.00 101.39 ? 149 LYS D CA  1 
ATOM   2733 C C   . LYS B 2 150 ? -2.850  -3.359  48.696  1.00 98.29  ? 149 LYS D C   1 
ATOM   2734 O O   . LYS B 2 150 ? -1.750  -3.553  49.225  1.00 95.81  ? 149 LYS D O   1 
ATOM   2735 C CB  . LYS B 2 150 ? -3.059  -5.322  47.140  1.00 99.42  ? 149 LYS D CB  1 
ATOM   2736 C CG  . LYS B 2 150 ? -4.023  -5.890  46.102  1.00 103.97 ? 149 LYS D CG  1 
ATOM   2737 C CD  . LYS B 2 150 ? -3.466  -7.133  45.374  1.00 107.44 ? 149 LYS D CD  1 
ATOM   2738 C CE  . LYS B 2 150 ? -2.574  -8.023  46.252  1.00 107.71 ? 149 LYS D CE  1 
ATOM   2739 N NZ  . LYS B 2 150 ? -2.394  -9.407  45.683  1.00 105.64 ? 149 LYS D NZ  1 
ATOM   2740 N N   . VAL B 2 151 ? -3.870  -2.772  49.328  1.00 105.99 ? 150 VAL D N   1 
ATOM   2741 C CA  . VAL B 2 151 ? -3.839  -2.464  50.759  1.00 107.20 ? 150 VAL D CA  1 
ATOM   2742 C C   . VAL B 2 151 ? -4.979  -3.206  51.450  1.00 108.83 ? 150 VAL D C   1 
ATOM   2743 O O   . VAL B 2 151 ? -6.155  -3.016  51.116  1.00 108.04 ? 150 VAL D O   1 
ATOM   2744 C CB  . VAL B 2 151 ? -3.890  -0.951  51.044  1.00 104.19 ? 150 VAL D CB  1 
ATOM   2745 C CG1 . VAL B 2 151 ? -5.187  -0.318  50.576  1.00 102.34 ? 150 VAL D CG1 1 
ATOM   2746 C CG2 . VAL B 2 151 ? -3.739  -0.730  52.519  1.00 104.32 ? 150 VAL D CG2 1 
ATOM   2747 N N   . ASP B 2 152 ? -4.620  -4.066  52.402  1.00 115.08 ? 151 ASP D N   1 
ATOM   2748 C CA  . ASP B 2 152 ? -5.582  -4.904  53.123  1.00 116.68 ? 151 ASP D CA  1 
ATOM   2749 C C   . ASP B 2 152 ? -6.443  -5.730  52.154  1.00 118.87 ? 151 ASP D C   1 
ATOM   2750 O O   . ASP B 2 152 ? -7.616  -6.006  52.420  1.00 121.95 ? 151 ASP D O   1 
ATOM   2751 C CB  . ASP B 2 152 ? -6.455  -4.053  54.060  1.00 118.12 ? 151 ASP D CB  1 
ATOM   2752 C CG  . ASP B 2 152 ? -5.684  -3.495  55.275  1.00 117.90 ? 151 ASP D CG  1 
ATOM   2753 O OD1 . ASP B 2 152 ? -4.448  -3.655  55.355  1.00 116.89 ? 151 ASP D OD1 1 
ATOM   2754 O OD2 . ASP B 2 152 ? -6.328  -2.885  56.161  1.00 118.82 ? 151 ASP D OD2 1 
ATOM   2755 N N   . ASN B 2 153 ? -5.836  -6.145  51.025  1.00 108.00 ? 152 ASN D N   1 
ATOM   2756 C CA  . ASN B 2 153 ? -6.465  -6.866  49.899  1.00 104.95 ? 152 ASN D CA  1 
ATOM   2757 C C   . ASN B 2 153 ? -7.522  -6.054  49.165  1.00 104.16 ? 152 ASN D C   1 
ATOM   2758 O O   . ASN B 2 153 ? -8.401  -6.633  48.518  1.00 103.02 ? 152 ASN D O   1 
ATOM   2759 C CB  . ASN B 2 153 ? -7.117  -8.212  50.275  1.00 107.66 ? 152 ASN D CB  1 
ATOM   2760 C CG  . ASN B 2 153 ? -6.185  -9.166  50.981  1.00 106.22 ? 152 ASN D CG  1 
ATOM   2761 O OD1 . ASN B 2 153 ? -5.701  -8.878  52.066  1.00 108.15 ? 152 ASN D OD1 1 
ATOM   2762 N ND2 . ASN B 2 153 ? -5.920  -10.314 50.356  1.00 99.97  ? 152 ASN D ND2 1 
ATOM   2763 N N   . ALA B 2 154 ? -7.485  -4.734  49.227  1.00 109.02 ? 153 ALA D N   1 
ATOM   2764 C CA  . ALA B 2 154 ? -8.368  -3.913  48.406  1.00 110.01 ? 153 ALA D CA  1 
ATOM   2765 C C   . ALA B 2 154 ? -7.538  -3.326  47.270  1.00 111.55 ? 153 ALA D C   1 
ATOM   2766 O O   . ALA B 2 154 ? -6.666  -2.480  47.502  1.00 108.70 ? 153 ALA D O   1 
ATOM   2767 C CB  . ALA B 2 154 ? -9.041  -2.824  49.234  1.00 106.58 ? 153 ALA D CB  1 
ATOM   2768 N N   . LEU B 2 155 ? -7.791  -3.803  46.050  1.00 112.98 ? 154 LEU D N   1 
ATOM   2769 C CA  . LEU B 2 155 ? -7.073  -3.315  44.881  1.00 115.82 ? 154 LEU D CA  1 
ATOM   2770 C C   . LEU B 2 155 ? -7.118  -1.795  44.839  1.00 117.95 ? 154 LEU D C   1 
ATOM   2771 O O   . LEU B 2 155 ? -8.112  -1.178  45.232  1.00 117.57 ? 154 LEU D O   1 
ATOM   2772 C CB  . LEU B 2 155 ? -7.684  -3.896  43.605  1.00 120.11 ? 154 LEU D CB  1 
ATOM   2773 C CG  . LEU B 2 155 ? -7.915  -5.407  43.590  1.00 121.21 ? 154 LEU D CG  1 
ATOM   2774 C CD1 . LEU B 2 155 ? -8.942  -5.792  42.532  1.00 121.78 ? 154 LEU D CD1 1 
ATOM   2775 C CD2 . LEU B 2 155 ? -6.603  -6.130  43.345  1.00 120.54 ? 154 LEU D CD2 1 
ATOM   2776 N N   . GLN B 2 156 ? -6.029  -1.188  44.380  1.00 112.21 ? 155 GLN D N   1 
ATOM   2777 C CA  . GLN B 2 156 ? -5.854  0.255   44.451  1.00 110.72 ? 155 GLN D CA  1 
ATOM   2778 C C   . GLN B 2 156 ? -5.764  0.827   43.047  1.00 111.39 ? 155 GLN D C   1 
ATOM   2779 O O   . GLN B 2 156 ? -4.905  0.416   42.261  1.00 109.00 ? 155 GLN D O   1 
ATOM   2780 C CB  . GLN B 2 156 ? -4.597  0.615   45.245  1.00 109.16 ? 155 GLN D CB  1 
ATOM   2781 C CG  . GLN B 2 156 ? -4.606  0.169   46.698  1.00 107.34 ? 155 GLN D CG  1 
ATOM   2782 C CD  . GLN B 2 156 ? -5.767  0.734   47.483  1.00 108.40 ? 155 GLN D CD  1 
ATOM   2783 O OE1 . GLN B 2 156 ? -5.755  1.902   47.875  1.00 109.72 ? 155 GLN D OE1 1 
ATOM   2784 N NE2 . GLN B 2 156 ? -6.763  -0.106  47.756  1.00 107.38 ? 155 GLN D NE2 1 
ATOM   2785 N N   . SER B 2 157 ? -6.638  1.786   42.745  1.00 113.27 ? 156 SER D N   1 
ATOM   2786 C CA  . SER B 2 157 ? -6.655  2.464   41.458  1.00 113.83 ? 156 SER D CA  1 
ATOM   2787 C C   . SER B 2 157 ? -6.612  3.973   41.673  1.00 115.07 ? 156 SER D C   1 
ATOM   2788 O O   . SER B 2 157 ? -7.144  4.487   42.661  1.00 116.47 ? 156 SER D O   1 
ATOM   2789 C CB  . SER B 2 157 ? -7.906  2.077   40.641  1.00 117.38 ? 156 SER D CB  1 
ATOM   2790 O OG  . SER B 2 157 ? -7.930  2.710   39.367  1.00 121.50 ? 156 SER D OG  1 
ATOM   2791 N N   . GLY B 2 158 ? -5.959  4.682   40.739  1.00 115.69 ? 157 GLY D N   1 
ATOM   2792 C CA  . GLY B 2 158 ? -5.921  6.133   40.730  1.00 112.26 ? 157 GLY D CA  1 
ATOM   2793 C C   . GLY B 2 158 ? -4.795  6.770   41.524  1.00 110.99 ? 157 GLY D C   1 
ATOM   2794 O O   . GLY B 2 158 ? -4.548  7.972   41.363  1.00 110.16 ? 157 GLY D O   1 
ATOM   2795 N N   . ASN B 2 159 ? -4.106  6.005   42.372  1.00 108.22 ? 158 ASN D N   1 
ATOM   2796 C CA  . ASN B 2 159 ? -3.056  6.524   43.244  1.00 105.59 ? 158 ASN D CA  1 
ATOM   2797 C C   . ASN B 2 159 ? -1.638  6.298   42.727  1.00 100.81 ? 158 ASN D C   1 
ATOM   2798 O O   . ASN B 2 159 ? -0.751  7.104   43.023  1.00 99.34  ? 158 ASN D O   1 
ATOM   2799 C CB  . ASN B 2 159 ? -3.193  5.912   44.647  1.00 103.88 ? 158 ASN D CB  1 
ATOM   2800 C CG  . ASN B 2 159 ? -4.013  4.623   44.647  1.00 108.79 ? 158 ASN D CG  1 
ATOM   2801 O OD1 . ASN B 2 159 ? -5.213  4.644   44.929  1.00 112.91 ? 158 ASN D OD1 1 
ATOM   2802 N ND2 . ASN B 2 159 ? -3.389  3.513   44.291  1.00 107.73 ? 158 ASN D ND2 1 
ATOM   2803 N N   . SER B 2 160 ? -1.397  5.254   41.945  1.00 100.01 ? 159 SER D N   1 
ATOM   2804 C CA  . SER B 2 160 ? -0.036  4.868   41.613  1.00 95.87  ? 159 SER D CA  1 
ATOM   2805 C C   . SER B 2 160 ? 0.541   5.760   40.521  1.00 94.12  ? 159 SER D C   1 
ATOM   2806 O O   . SER B 2 160 ? -0.187  6.346   39.715  1.00 96.70  ? 159 SER D O   1 
ATOM   2807 C CB  . SER B 2 160 ? -0.000  3.408   41.166  1.00 100.11 ? 159 SER D CB  1 
ATOM   2808 O OG  . SER B 2 160 ? -0.892  2.628   41.944  1.00 104.51 ? 159 SER D OG  1 
ATOM   2809 N N   . GLN B 2 161 ? 1.869   5.858   40.502  1.00 88.18  ? 160 GLN D N   1 
ATOM   2810 C CA  . GLN B 2 161 ? 2.571   6.623   39.475  1.00 83.78  ? 160 GLN D CA  1 
ATOM   2811 C C   . GLN B 2 161 ? 3.952   6.020   39.280  1.00 80.60  ? 160 GLN D C   1 
ATOM   2812 O O   . GLN B 2 161 ? 4.803   6.111   40.170  1.00 78.48  ? 160 GLN D O   1 
ATOM   2813 C CB  . GLN B 2 161 ? 2.675   8.102   39.847  1.00 80.05  ? 160 GLN D CB  1 
ATOM   2814 C CG  . GLN B 2 161 ? 1.757   9.001   39.055  1.00 77.49  ? 160 GLN D CG  1 
ATOM   2815 C CD  . GLN B 2 161 ? 2.086   10.467  39.262  1.00 82.17  ? 160 GLN D CD  1 
ATOM   2816 O OE1 . GLN B 2 161 ? 2.922   10.808  40.100  1.00 83.58  ? 160 GLN D OE1 1 
ATOM   2817 N NE2 . GLN B 2 161 ? 1.474   11.340  38.461  1.00 80.76  ? 160 GLN D NE2 1 
ATOM   2818 N N   . GLU B 2 162 ? 4.175   5.420   38.115  1.00 78.83  ? 161 GLU D N   1 
ATOM   2819 C CA  . GLU B 2 162 ? 5.399   4.690   37.816  1.00 75.36  ? 161 GLU D CA  1 
ATOM   2820 C C   . GLU B 2 162 ? 6.240   5.418   36.775  1.00 68.79  ? 161 GLU D C   1 
ATOM   2821 O O   . GLU B 2 162 ? 5.721   6.146   35.927  1.00 69.00  ? 161 GLU D O   1 
ATOM   2822 C CB  . GLU B 2 162 ? 5.093   3.263   37.327  1.00 75.60  ? 161 GLU D CB  1 
ATOM   2823 C CG  . GLU B 2 162 ? 3.713   3.092   36.676  1.00 80.15  ? 161 GLU D CG  1 
ATOM   2824 C CD  . GLU B 2 162 ? 3.354   1.633   36.364  1.00 81.77  ? 161 GLU D CD  1 
ATOM   2825 O OE1 . GLU B 2 162 ? 4.266   0.859   35.987  1.00 79.00  ? 161 GLU D OE1 1 
ATOM   2826 O OE2 . GLU B 2 162 ? 2.162   1.264   36.508  1.00 89.06  ? 161 GLU D OE2 1 
ATOM   2827 N N   . SER B 2 163 ? 7.553   5.236   36.874  1.00 64.16  ? 162 SER D N   1 
ATOM   2828 C CA  . SER B 2 163 ? 8.485   5.657   35.845  1.00 66.24  ? 162 SER D CA  1 
ATOM   2829 C C   . SER B 2 163 ? 9.430   4.491   35.563  1.00 67.93  ? 162 SER D C   1 
ATOM   2830 O O   . SER B 2 163 ? 9.645   3.629   36.425  1.00 65.29  ? 162 SER D O   1 
ATOM   2831 C CB  . SER B 2 163 ? 9.254   6.916   36.255  1.00 61.61  ? 162 SER D CB  1 
ATOM   2832 O OG  . SER B 2 163 ? 10.127  6.650   37.331  1.00 65.23  ? 162 SER D OG  1 
ATOM   2833 N N   . VAL B 2 164 ? 9.966   4.431   34.339  1.00 64.14  ? 163 VAL D N   1 
ATOM   2834 C CA  . VAL B 2 164 ? 10.761  3.282   33.926  1.00 64.21  ? 163 VAL D CA  1 
ATOM   2835 C C   . VAL B 2 164 ? 12.150  3.736   33.516  1.00 60.16  ? 163 VAL D C   1 
ATOM   2836 O O   . VAL B 2 164 ? 12.313  4.794   32.903  1.00 62.65  ? 163 VAL D O   1 
ATOM   2837 C CB  . VAL B 2 164 ? 10.081  2.485   32.798  1.00 63.88  ? 163 VAL D CB  1 
ATOM   2838 C CG1 . VAL B 2 164 ? 10.812  1.178   32.582  1.00 62.27  ? 163 VAL D CG1 1 
ATOM   2839 C CG2 . VAL B 2 164 ? 8.633   2.192   33.191  1.00 63.87  ? 163 VAL D CG2 1 
ATOM   2840 N N   . THR B 2 165 ? 13.149  2.950   33.894  1.00 60.87  ? 164 THR D N   1 
ATOM   2841 C CA  . THR B 2 165 ? 14.524  3.233   33.529  1.00 61.71  ? 164 THR D CA  1 
ATOM   2842 C C   . THR B 2 165 ? 14.724  2.923   32.051  1.00 61.74  ? 164 THR D C   1 
ATOM   2843 O O   . THR B 2 165 ? 13.955  2.169   31.448  1.00 65.40  ? 164 THR D O   1 
ATOM   2844 C CB  . THR B 2 165 ? 15.475  2.414   34.414  1.00 61.88  ? 164 THR D CB  1 
ATOM   2845 O OG1 . THR B 2 165 ? 16.603  3.212   34.790  1.00 59.78  ? 164 THR D OG1 1 
ATOM   2846 C CG2 . THR B 2 165 ? 15.961  1.145   33.725  1.00 59.84  ? 164 THR D CG2 1 
ATOM   2847 N N   . GLU B 2 166 ? 15.735  3.535   31.450  1.00 56.34  ? 165 GLU D N   1 
ATOM   2848 C CA  . GLU B 2 166 ? 16.042  3.077   30.103  1.00 63.29  ? 165 GLU D CA  1 
ATOM   2849 C C   . GLU B 2 166 ? 16.837  1.781   30.191  1.00 64.17  ? 165 GLU D C   1 
ATOM   2850 O O   . GLU B 2 166 ? 17.422  1.462   31.229  1.00 67.52  ? 165 GLU D O   1 
ATOM   2851 C CB  . GLU B 2 166 ? 16.818  4.138   29.320  1.00 64.26  ? 165 GLU D CB  1 
ATOM   2852 C CG  . GLU B 2 166 ? 15.920  5.153   28.611  1.00 61.74  ? 165 GLU D CG  1 
ATOM   2853 C CD  . GLU B 2 166 ? 14.842  4.496   27.762  1.00 67.04  ? 165 GLU D CD  1 
ATOM   2854 O OE1 . GLU B 2 166 ? 15.197  3.905   26.712  1.00 75.37  ? 165 GLU D OE1 1 
ATOM   2855 O OE2 . GLU B 2 166 ? 13.652  4.531   28.162  1.00 62.04  ? 165 GLU D OE2 1 
ATOM   2856 N N   . GLN B 2 167 ? 16.825  1.013   29.104  1.00 64.79  ? 166 GLN D N   1 
ATOM   2857 C CA  . GLN B 2 167 ? 17.596  -0.224  29.042  1.00 65.32  ? 166 GLN D CA  1 
ATOM   2858 C C   . GLN B 2 167 ? 18.985  -0.004  29.620  1.00 65.26  ? 166 GLN D C   1 
ATOM   2859 O O   . GLN B 2 167 ? 19.642  0.993   29.313  1.00 64.42  ? 166 GLN D O   1 
ATOM   2860 C CB  . GLN B 2 167 ? 17.695  -0.713  27.587  1.00 65.65  ? 166 GLN D CB  1 
ATOM   2861 C CG  . GLN B 2 167 ? 17.698  -2.219  27.421  1.00 64.60  ? 166 GLN D CG  1 
ATOM   2862 C CD  . GLN B 2 167 ? 17.293  -2.698  26.026  1.00 65.46  ? 166 GLN D CD  1 
ATOM   2863 O OE1 . GLN B 2 167 ? 17.832  -2.236  25.018  1.00 67.08  ? 166 GLN D OE1 1 
ATOM   2864 N NE2 . GLN B 2 167 ? 16.371  -3.655  25.965  1.00 64.64  ? 166 GLN D NE2 1 
ATOM   2865 N N   . ASP B 2 168 ? 19.403  -0.900  30.507  1.00 66.00  ? 167 ASP D N   1 
ATOM   2866 C CA  . ASP B 2 168 ? 20.725  -0.757  31.086  1.00 70.00  ? 167 ASP D CA  1 
ATOM   2867 C C   . ASP B 2 168 ? 21.788  -1.163  30.076  1.00 75.38  ? 167 ASP D C   1 
ATOM   2868 O O   . ASP B 2 168 ? 21.522  -1.902  29.124  1.00 76.45  ? 167 ASP D O   1 
ATOM   2869 C CB  . ASP B 2 168 ? 20.858  -1.590  32.352  1.00 73.60  ? 167 ASP D CB  1 
ATOM   2870 C CG  . ASP B 2 168 ? 22.232  -1.476  32.974  1.00 81.50  ? 167 ASP D CG  1 
ATOM   2871 O OD1 . ASP B 2 168 ? 22.714  -0.342  33.175  1.00 83.44  ? 167 ASP D OD1 1 
ATOM   2872 O OD2 . ASP B 2 168 ? 22.832  -2.526  33.263  1.00 84.09  ? 167 ASP D OD2 1 
ATOM   2873 N N   . SER B 2 169 ? 23.004  -0.649  30.276  1.00 84.04  ? 168 SER D N   1 
ATOM   2874 C CA  . SER B 2 169 ? 24.086  -0.942  29.340  1.00 86.91  ? 168 SER D CA  1 
ATOM   2875 C C   . SER B 2 169 ? 24.699  -2.313  29.596  1.00 86.86  ? 168 SER D C   1 
ATOM   2876 O O   . SER B 2 169 ? 25.151  -2.978  28.655  1.00 86.71  ? 168 SER D O   1 
ATOM   2877 C CB  . SER B 2 169 ? 25.171  0.127   29.421  1.00 87.33  ? 168 SER D CB  1 
ATOM   2878 O OG  . SER B 2 169 ? 26.361  -0.359  28.829  1.00 88.58  ? 168 SER D OG  1 
ATOM   2879 N N   . LYS B 2 170 ? 24.721  -2.749  30.856  1.00 82.61  ? 169 LYS D N   1 
ATOM   2880 C CA  . LYS B 2 170 ? 25.358  -4.013  31.211  1.00 83.20  ? 169 LYS D CA  1 
ATOM   2881 C C   . LYS B 2 170 ? 24.377  -5.178  31.126  1.00 79.27  ? 169 LYS D C   1 
ATOM   2882 O O   . LYS B 2 170 ? 24.610  -6.143  30.395  1.00 79.22  ? 169 LYS D O   1 
ATOM   2883 C CB  . LYS B 2 170 ? 25.948  -3.916  32.619  1.00 89.52  ? 169 LYS D CB  1 
ATOM   2884 C CG  . LYS B 2 170 ? 26.783  -2.655  32.849  1.00 90.26  ? 169 LYS D CG  1 
ATOM   2885 C CD  . LYS B 2 170 ? 26.343  -1.909  34.115  1.00 92.72  ? 169 LYS D CD  1 
ATOM   2886 C CE  . LYS B 2 170 ? 26.442  -0.380  33.948  1.00 96.43  ? 169 LYS D CE  1 
ATOM   2887 N NZ  . LYS B 2 170 ? 25.621  0.398   34.951  1.00 93.62  ? 169 LYS D NZ  1 
ATOM   2888 N N   . ASP B 2 171 ? 23.277  -5.108  31.876  1.00 76.24  ? 170 ASP D N   1 
ATOM   2889 C CA  . ASP B 2 171 ? 22.307  -6.195  31.878  1.00 71.96  ? 170 ASP D CA  1 
ATOM   2890 C C   . ASP B 2 171 ? 21.412  -6.228  30.648  1.00 69.92  ? 170 ASP D C   1 
ATOM   2891 O O   . ASP B 2 171 ? 20.833  -7.281  30.365  1.00 68.44  ? 170 ASP D O   1 
ATOM   2892 C CB  . ASP B 2 171 ? 21.418  -6.086  33.090  1.00 69.01  ? 170 ASP D CB  1 
ATOM   2893 C CG  . ASP B 2 171 ? 22.136  -5.556  34.267  1.00 81.76  ? 170 ASP D CG  1 
ATOM   2894 O OD1 . ASP B 2 171 ? 23.128  -6.194  34.687  1.00 93.83  ? 170 ASP D OD1 1 
ATOM   2895 O OD2 . ASP B 2 171 ? 21.723  -4.487  34.767  1.00 90.23  ? 170 ASP D OD2 1 
ATOM   2896 N N   . SER B 2 172 ? 21.283  -5.115  29.919  1.00 71.76  ? 171 SER D N   1 
ATOM   2897 C CA  . SER B 2 172 ? 20.199  -4.897  28.951  1.00 67.61  ? 171 SER D CA  1 
ATOM   2898 C C   . SER B 2 172 ? 18.826  -5.025  29.608  1.00 64.72  ? 171 SER D C   1 
ATOM   2899 O O   . SER B 2 172 ? 17.848  -5.396  28.954  1.00 63.92  ? 171 SER D O   1 
ATOM   2900 C CB  . SER B 2 172 ? 20.287  -5.835  27.737  1.00 62.08  ? 171 SER D CB  1 
ATOM   2901 O OG  . SER B 2 172 ? 21.466  -5.641  26.976  1.00 58.19  ? 171 SER D OG  1 
ATOM   2902 N N   . THR B 2 173 ? 18.731  -4.715  30.898  1.00 63.92  ? 172 THR D N   1 
ATOM   2903 C CA  . THR B 2 173 ? 17.473  -4.834  31.623  1.00 68.13  ? 172 THR D CA  1 
ATOM   2904 C C   . THR B 2 173 ? 16.821  -3.476  31.873  1.00 65.96  ? 172 THR D C   1 
ATOM   2905 O O   . THR B 2 173 ? 17.344  -2.408  31.538  1.00 65.13  ? 172 THR D O   1 
ATOM   2906 C CB  . THR B 2 173 ? 17.654  -5.543  32.966  1.00 63.78  ? 172 THR D CB  1 
ATOM   2907 O OG1 . THR B 2 173 ? 18.853  -5.082  33.580  1.00 64.02  ? 172 THR D OG1 1 
ATOM   2908 C CG2 . THR B 2 173 ? 17.675  -7.035  32.802  1.00 65.29  ? 172 THR D CG2 1 
ATOM   2909 N N   . TYR B 2 174 ? 15.662  -3.544  32.504  1.00 60.85  ? 173 TYR D N   1 
ATOM   2910 C CA  . TYR B 2 174 ? 14.832  -2.410  32.827  1.00 60.56  ? 173 TYR D CA  1 
ATOM   2911 C C   . TYR B 2 174 ? 14.628  -2.394  34.329  1.00 63.38  ? 173 TYR D C   1 
ATOM   2912 O O   . TYR B 2 174 ? 14.698  -3.433  34.988  1.00 66.46  ? 173 TYR D O   1 
ATOM   2913 C CB  . TYR B 2 174 ? 13.490  -2.534  32.114  1.00 63.80  ? 173 TYR D CB  1 
ATOM   2914 C CG  . TYR B 2 174 ? 13.576  -2.427  30.604  1.00 66.72  ? 173 TYR D CG  1 
ATOM   2915 C CD1 . TYR B 2 174 ? 14.528  -1.622  29.994  1.00 68.15  ? 173 TYR D CD1 1 
ATOM   2916 C CD2 . TYR B 2 174 ? 12.774  -3.218  29.787  1.00 67.91  ? 173 TYR D CD2 1 
ATOM   2917 C CE1 . TYR B 2 174 ? 14.610  -1.539  28.611  1.00 66.94  ? 173 TYR D CE1 1 
ATOM   2918 C CE2 . TYR B 2 174 ? 12.863  -3.151  28.407  1.00 68.22  ? 173 TYR D CE2 1 
ATOM   2919 C CZ  . TYR B 2 174 ? 13.790  -2.309  27.834  1.00 67.55  ? 173 TYR D CZ  1 
ATOM   2920 O OH  . TYR B 2 174 ? 13.917  -2.215  26.477  1.00 69.53  ? 173 TYR D OH  1 
ATOM   2921 N N   . SER B 2 175 ? 14.374  -1.210  34.873  1.00 65.33  ? 174 SER D N   1 
ATOM   2922 C CA  . SER B 2 175 ? 13.890  -1.079  36.237  1.00 60.80  ? 174 SER D CA  1 
ATOM   2923 C C   . SER B 2 175 ? 12.638  -0.217  36.231  1.00 60.96  ? 174 SER D C   1 
ATOM   2924 O O   . SER B 2 175 ? 12.508  0.714   35.428  1.00 61.90  ? 174 SER D O   1 
ATOM   2925 C CB  . SER B 2 175 ? 14.950  -0.479  37.154  1.00 63.18  ? 174 SER D CB  1 
ATOM   2926 O OG  . SER B 2 175 ? 16.083  -1.327  37.256  1.00 61.85  ? 174 SER D OG  1 
ATOM   2927 N N   . LEU B 2 176 ? 11.713  -0.542  37.123  1.00 61.65  ? 175 LEU D N   1 
ATOM   2928 C CA  . LEU B 2 176 ? 10.465  0.193   37.268  1.00 64.10  ? 175 LEU D CA  1 
ATOM   2929 C C   . LEU B 2 176 ? 10.279  0.579   38.724  1.00 64.72  ? 175 LEU D C   1 
ATOM   2930 O O   . LEU B 2 176 ? 10.587  -0.206  39.622  1.00 65.96  ? 175 LEU D O   1 
ATOM   2931 C CB  . LEU B 2 176 ? 9.254   -0.635  36.798  1.00 64.01  ? 175 LEU D CB  1 
ATOM   2932 C CG  . LEU B 2 176 ? 7.856   0.002   36.853  1.00 65.32  ? 175 LEU D CG  1 
ATOM   2933 C CD1 . LEU B 2 176 ? 7.003   -0.489  35.704  1.00 67.76  ? 175 LEU D CD1 1 
ATOM   2934 C CD2 . LEU B 2 176 ? 7.152   -0.297  38.159  1.00 68.73  ? 175 LEU D CD2 1 
ATOM   2935 N N   . SER B 2 177 ? 9.752   1.780   38.955  1.00 65.03  ? 176 SER D N   1 
ATOM   2936 C CA  . SER B 2 177 ? 9.423   2.243   40.301  1.00 69.03  ? 176 SER D CA  1 
ATOM   2937 C C   . SER B 2 177 ? 7.998   2.772   40.288  1.00 72.43  ? 176 SER D C   1 
ATOM   2938 O O   . SER B 2 177 ? 7.724   3.806   39.669  1.00 70.80  ? 176 SER D O   1 
ATOM   2939 C CB  . SER B 2 177 ? 10.390  3.328   40.780  1.00 66.13  ? 176 SER D CB  1 
ATOM   2940 O OG  . SER B 2 177 ? 9.815   4.613   40.618  1.00 68.08  ? 176 SER D OG  1 
ATOM   2941 N N   . SER B 2 178 ? 7.098   2.071   40.973  1.00 73.18  ? 177 SER D N   1 
ATOM   2942 C CA  . SER B 2 178 ? 5.714   2.502   41.139  1.00 75.81  ? 177 SER D CA  1 
ATOM   2943 C C   . SER B 2 178 ? 5.531   3.075   42.538  1.00 78.03  ? 177 SER D C   1 
ATOM   2944 O O   . SER B 2 178 ? 5.697   2.350   43.527  1.00 81.37  ? 177 SER D O   1 
ATOM   2945 C CB  . SER B 2 178 ? 4.759   1.329   40.924  1.00 77.65  ? 177 SER D CB  1 
ATOM   2946 O OG  . SER B 2 178 ? 3.419   1.769   40.770  1.00 82.80  ? 177 SER D OG  1 
ATOM   2947 N N   . THR B 2 179 ? 5.169   4.353   42.635  1.00 75.82  ? 178 THR D N   1 
ATOM   2948 C CA  . THR B 2 179 ? 4.974   4.964   43.944  1.00 80.95  ? 178 THR D CA  1 
ATOM   2949 C C   . THR B 2 179 ? 3.484   5.097   44.231  1.00 84.98  ? 178 THR D C   1 
ATOM   2950 O O   . THR B 2 179 ? 2.705   5.506   43.359  1.00 83.94  ? 178 THR D O   1 
ATOM   2951 C CB  . THR B 2 179 ? 5.619   6.340   44.057  1.00 79.78  ? 178 THR D CB  1 
ATOM   2952 O OG1 . THR B 2 179 ? 4.676   7.322   43.617  1.00 85.51  ? 178 THR D OG1 1 
ATOM   2953 C CG2 . THR B 2 179 ? 6.873   6.415   43.171  1.00 80.09  ? 178 THR D CG2 1 
ATOM   2954 N N   . LEU B 2 180 ? 3.109   4.768   45.464  1.00 83.65  ? 179 LEU D N   1 
ATOM   2955 C CA  . LEU B 2 180 ? 1.746   4.855   45.958  1.00 83.39  ? 179 LEU D CA  1 
ATOM   2956 C C   . LEU B 2 180 ? 1.709   5.983   46.980  1.00 82.93  ? 179 LEU D C   1 
ATOM   2957 O O   . LEU B 2 180 ? 2.447   5.942   47.969  1.00 83.39  ? 179 LEU D O   1 
ATOM   2958 C CB  . LEU B 2 180 ? 1.353   3.522   46.586  1.00 86.12  ? 179 LEU D CB  1 
ATOM   2959 C CG  . LEU B 2 180 ? -0.122  3.184   46.701  1.00 93.36  ? 179 LEU D CG  1 
ATOM   2960 C CD1 . LEU B 2 180 ? -0.857  4.097   47.676  1.00 98.14  ? 179 LEU D CD1 1 
ATOM   2961 C CD2 . LEU B 2 180 ? -0.642  3.347   45.317  1.00 95.56  ? 179 LEU D CD2 1 
ATOM   2962 N N   . THR B 2 181 ? 0.892   7.003   46.739  1.00 83.88  ? 180 THR D N   1 
ATOM   2963 C CA  . THR B 2 181 ? 0.840   8.158   47.628  1.00 87.33  ? 180 THR D CA  1 
ATOM   2964 C C   . THR B 2 181 ? -0.556  8.260   48.225  1.00 93.91  ? 180 THR D C   1 
ATOM   2965 O O   . THR B 2 181 ? -1.548  8.190   47.491  1.00 96.96  ? 180 THR D O   1 
ATOM   2966 C CB  . THR B 2 181 ? 1.210   9.454   46.901  1.00 87.66  ? 180 THR D CB  1 
ATOM   2967 O OG1 . THR B 2 181 ? 0.155   9.814   46.003  1.00 91.79  ? 180 THR D OG1 1 
ATOM   2968 C CG2 . THR B 2 181 ? 2.520   9.290   46.121  1.00 84.66  ? 180 THR D CG2 1 
ATOM   2969 N N   . LEU B 2 182 ? -0.618  8.415   49.556  1.00 95.67  ? 181 LEU D N   1 
ATOM   2970 C CA  . LEU B 2 182 ? -1.847  8.438   50.344  1.00 97.91  ? 181 LEU D CA  1 
ATOM   2971 C C   . LEU B 2 182 ? -1.713  9.477   51.450  1.00 100.09 ? 181 LEU D C   1 
ATOM   2972 O O   . LEU B 2 182 ? -0.610  9.745   51.926  1.00 97.06  ? 181 LEU D O   1 
ATOM   2973 C CB  . LEU B 2 182 ? -2.125  7.076   50.980  1.00 98.73  ? 181 LEU D CB  1 
ATOM   2974 C CG  . LEU B 2 182 ? -3.364  6.321   50.522  1.00 103.54 ? 181 LEU D CG  1 
ATOM   2975 C CD1 . LEU B 2 182 ? -3.554  5.054   51.355  1.00 105.65 ? 181 LEU D CD1 1 
ATOM   2976 C CD2 . LEU B 2 182 ? -4.584  7.224   50.605  1.00 107.90 ? 181 LEU D CD2 1 
ATOM   2977 N N   . SER B 2 183 ? -2.838  10.051  51.873  1.00 105.70 ? 182 SER D N   1 
ATOM   2978 C CA  . SER B 2 183 ? -2.803  10.960  53.013  1.00 110.50 ? 182 SER D CA  1 
ATOM   2979 C C   . SER B 2 183 ? -2.538  10.182  54.302  1.00 112.55 ? 182 SER D C   1 
ATOM   2980 O O   . SER B 2 183 ? -3.078  9.086   54.501  1.00 112.64 ? 182 SER D O   1 
ATOM   2981 C CB  . SER B 2 183 ? -4.117  11.734  53.126  1.00 113.20 ? 182 SER D CB  1 
ATOM   2982 O OG  . SER B 2 183 ? -5.064  11.016  53.896  1.00 117.36 ? 182 SER D OG  1 
ATOM   2983 N N   . LYS B 2 184 ? -1.710  10.765  55.191  1.00 119.10 ? 183 LYS D N   1 
ATOM   2984 C CA  . LYS B 2 184 ? -1.220  10.034  56.365  1.00 119.07 ? 183 LYS D CA  1 
ATOM   2985 C C   . LYS B 2 184 ? -2.361  9.394   57.147  1.00 124.60 ? 183 LYS D C   1 
ATOM   2986 O O   . LYS B 2 184 ? -2.202  8.295   57.693  1.00 124.70 ? 183 LYS D O   1 
ATOM   2987 C CB  . LYS B 2 184 ? -0.374  10.947  57.285  1.00 115.80 ? 183 LYS D CB  1 
ATOM   2988 C CG  . LYS B 2 184 ? -1.120  11.889  58.267  1.00 118.31 ? 183 LYS D CG  1 
ATOM   2989 C CD  . LYS B 2 184 ? -2.183  12.727  57.582  1.00 117.43 ? 183 LYS D CD  1 
ATOM   2990 C CE  . LYS B 2 184 ? -2.629  13.912  58.394  1.00 119.12 ? 183 LYS D CE  1 
ATOM   2991 N NZ  . LYS B 2 184 ? -3.537  14.706  57.524  1.00 120.68 ? 183 LYS D NZ  1 
ATOM   2992 N N   . ALA B 2 185 ? -3.527  10.042  57.175  1.00 119.68 ? 184 ALA D N   1 
ATOM   2993 C CA  . ALA B 2 185 ? -4.682  9.456   57.840  1.00 117.32 ? 184 ALA D CA  1 
ATOM   2994 C C   . ALA B 2 185 ? -5.044  8.119   57.209  1.00 111.85 ? 184 ALA D C   1 
ATOM   2995 O O   . ALA B 2 185 ? -5.180  7.107   57.906  1.00 112.61 ? 184 ALA D O   1 
ATOM   2996 C CB  . ALA B 2 185 ? -5.863  10.423  57.786  1.00 118.20 ? 184 ALA D CB  1 
ATOM   2997 N N   . ASP B 2 186 ? -5.171  8.089   55.881  1.00 113.82 ? 185 ASP D N   1 
ATOM   2998 C CA  . ASP B 2 186 ? -5.562  6.852   55.216  1.00 114.04 ? 185 ASP D CA  1 
ATOM   2999 C C   . ASP B 2 186 ? -4.436  5.825   55.222  1.00 114.51 ? 185 ASP D C   1 
ATOM   3000 O O   . ASP B 2 186 ? -4.700  4.620   55.117  1.00 115.06 ? 185 ASP D O   1 
ATOM   3001 C CB  . ASP B 2 186 ? -6.022  7.132   53.785  1.00 116.17 ? 185 ASP D CB  1 
ATOM   3002 C CG  . ASP B 2 186 ? -7.020  8.274   53.701  1.00 118.81 ? 185 ASP D CG  1 
ATOM   3003 O OD1 . ASP B 2 186 ? -6.665  9.402   54.103  1.00 120.35 ? 185 ASP D OD1 1 
ATOM   3004 O OD2 . ASP B 2 186 ? -8.164  8.041   53.247  1.00 121.61 ? 185 ASP D OD2 1 
ATOM   3005 N N   . TYR B 2 187 ? -3.183  6.269   55.336  1.00 113.32 ? 186 TYR D N   1 
ATOM   3006 C CA  . TYR B 2 187 ? -2.111  5.319   55.607  1.00 108.25 ? 186 TYR D CA  1 
ATOM   3007 C C   . TYR B 2 187 ? -2.303  4.684   56.979  1.00 109.00 ? 186 TYR D C   1 
ATOM   3008 O O   . TYR B 2 187 ? -2.326  3.454   57.115  1.00 107.33 ? 186 TYR D O   1 
ATOM   3009 C CB  . TYR B 2 187 ? -0.752  6.006   55.510  1.00 103.35 ? 186 TYR D CB  1 
ATOM   3010 C CG  . TYR B 2 187 ? 0.414   5.097   55.826  1.00 97.32  ? 186 TYR D CG  1 
ATOM   3011 C CD1 . TYR B 2 187 ? 0.600   3.907   55.139  1.00 95.73  ? 186 TYR D CD1 1 
ATOM   3012 C CD2 . TYR B 2 187 ? 1.331   5.432   56.812  1.00 95.56  ? 186 TYR D CD2 1 
ATOM   3013 C CE1 . TYR B 2 187 ? 1.674   3.078   55.424  1.00 95.79  ? 186 TYR D CE1 1 
ATOM   3014 C CE2 . TYR B 2 187 ? 2.404   4.612   57.106  1.00 92.16  ? 186 TYR D CE2 1 
ATOM   3015 C CZ  . TYR B 2 187 ? 2.571   3.437   56.411  1.00 93.57  ? 186 TYR D CZ  1 
ATOM   3016 O OH  . TYR B 2 187 ? 3.638   2.622   56.707  1.00 90.63  ? 186 TYR D OH  1 
ATOM   3017 N N   . GLU B 2 188 ? -2.483  5.514   58.008  1.00 106.27 ? 187 GLU D N   1 
ATOM   3018 C CA  . GLU B 2 188 ? -2.647  4.995   59.357  1.00 105.81 ? 187 GLU D CA  1 
ATOM   3019 C C   . GLU B 2 188 ? -3.920  4.176   59.511  1.00 104.25 ? 187 GLU D C   1 
ATOM   3020 O O   . GLU B 2 188 ? -3.985  3.333   60.413  1.00 106.33 ? 187 GLU D O   1 
ATOM   3021 C CB  . GLU B 2 188 ? -2.638  6.145   60.364  1.00 106.37 ? 187 GLU D CB  1 
ATOM   3022 C CG  . GLU B 2 188 ? -1.274  6.798   60.528  1.00 106.89 ? 187 GLU D CG  1 
ATOM   3023 C CD  . GLU B 2 188 ? -1.306  8.000   61.461  1.00 115.76 ? 187 GLU D CD  1 
ATOM   3024 O OE1 . GLU B 2 188 ? -2.414  8.457   61.826  1.00 114.07 ? 187 GLU D OE1 1 
ATOM   3025 O OE2 . GLU B 2 188 ? -0.219  8.506   61.812  1.00 120.98 ? 187 GLU D OE2 1 
ATOM   3026 N N   . LYS B 2 189 ? -4.925  4.393   58.654  1.00 106.62 ? 188 LYS D N   1 
ATOM   3027 C CA  . LYS B 2 189 ? -6.181  3.660   58.798  1.00 106.96 ? 188 LYS D CA  1 
ATOM   3028 C C   . LYS B 2 189 ? -5.975  2.167   58.558  1.00 107.07 ? 188 LYS D C   1 
ATOM   3029 O O   . LYS B 2 189 ? -6.336  1.333   59.402  1.00 106.16 ? 188 LYS D O   1 
ATOM   3030 C CB  . LYS B 2 189 ? -7.246  4.218   57.848  1.00 101.70 ? 188 LYS D CB  1 
ATOM   3031 C CG  . LYS B 2 189 ? -7.839  5.574   58.247  1.00 101.82 ? 188 LYS D CG  1 
ATOM   3032 C CD  . LYS B 2 189 ? -7.625  5.933   59.726  1.00 100.52 ? 188 LYS D CD  1 
ATOM   3033 C CE  . LYS B 2 189 ? -8.728  5.347   60.627  1.00 103.20 ? 188 LYS D CE  1 
ATOM   3034 N NZ  . LYS B 2 189 ? -8.391  5.288   62.094  1.00 104.01 ? 188 LYS D NZ  1 
ATOM   3035 N N   . HIS B 2 190 ? -5.383  1.813   57.418  1.00 103.97 ? 189 HIS D N   1 
ATOM   3036 C CA  . HIS B 2 190 ? -5.143  0.421   57.070  1.00 102.06 ? 189 HIS D CA  1 
ATOM   3037 C C   . HIS B 2 190 ? -3.755  -0.018  57.527  1.00 101.24 ? 189 HIS D C   1 
ATOM   3038 O O   . HIS B 2 190 ? -2.866  0.800   57.775  1.00 101.18 ? 189 HIS D O   1 
ATOM   3039 C CB  . HIS B 2 190 ? -5.303  0.200   55.569  1.00 104.17 ? 189 HIS D CB  1 
ATOM   3040 C CG  . HIS B 2 190 ? -6.694  0.440   55.070  1.00 104.56 ? 189 HIS D CG  1 
ATOM   3041 N ND1 . HIS B 2 190 ? -7.663  -0.541  55.076  1.00 101.69 ? 189 HIS D ND1 1 
ATOM   3042 C CD2 . HIS B 2 190 ? -7.266  1.532   54.507  1.00 102.58 ? 189 HIS D CD2 1 
ATOM   3043 C CE1 . HIS B 2 190 ? -8.783  -0.054  54.574  1.00 101.33 ? 189 HIS D CE1 1 
ATOM   3044 N NE2 . HIS B 2 190 ? -8.567  1.200   54.213  1.00 103.85 ? 189 HIS D NE2 1 
ATOM   3045 N N   . LYS B 2 191 ? -3.575  -1.334  57.629  1.00 100.56 ? 190 LYS D N   1 
ATOM   3046 C CA  . LYS B 2 191 ? -2.445  -1.895  58.360  1.00 103.38 ? 190 LYS D CA  1 
ATOM   3047 C C   . LYS B 2 191 ? -1.372  -2.489  57.463  1.00 103.10 ? 190 LYS D C   1 
ATOM   3048 O O   . LYS B 2 191 ? -0.191  -2.150  57.601  1.00 101.97 ? 190 LYS D O   1 
ATOM   3049 C CB  . LYS B 2 191 ? -2.934  -2.969  59.347  1.00 101.90 ? 190 LYS D CB  1 
ATOM   3050 C CG  . LYS B 2 191 ? -1.844  -3.471  60.279  1.00 97.41  ? 190 LYS D CG  1 
ATOM   3051 C CD  . LYS B 2 191 ? -1.792  -2.652  61.560  1.00 98.11  ? 190 LYS D CD  1 
ATOM   3052 C CE  . LYS B 2 191 ? -3.186  -2.375  62.106  1.00 100.28 ? 190 LYS D CE  1 
ATOM   3053 N NZ  . LYS B 2 191 ? -3.148  -1.449  63.271  1.00 100.76 ? 190 LYS D NZ  1 
ATOM   3054 N N   . VAL B 2 192 ? -1.752  -3.385  56.558  1.00 101.93 ? 191 VAL D N   1 
ATOM   3055 C CA  . VAL B 2 192 ? -0.811  -4.114  55.714  1.00 103.25 ? 191 VAL D CA  1 
ATOM   3056 C C   . VAL B 2 192 ? -0.946  -3.625  54.274  1.00 103.04 ? 191 VAL D C   1 
ATOM   3057 O O   . VAL B 2 192 ? -2.061  -3.476  53.756  1.00 104.92 ? 191 VAL D O   1 
ATOM   3058 C CB  . VAL B 2 192 ? -1.029  -5.634  55.836  1.00 101.87 ? 191 VAL D CB  1 
ATOM   3059 C CG1 . VAL B 2 192 ? -2.377  -6.034  55.292  1.00 101.13 ? 191 VAL D CG1 1 
ATOM   3060 C CG2 . VAL B 2 192 ? 0.066   -6.397  55.112  1.00 101.04 ? 191 VAL D CG2 1 
ATOM   3061 N N   . TYR B 2 193 ? 0.193   -3.343  53.639  1.00 102.73 ? 192 TYR D N   1 
ATOM   3062 C CA  . TYR B 2 193 ? 0.242   -2.860  52.263  1.00 100.55 ? 192 TYR D CA  1 
ATOM   3063 C C   . TYR B 2 193 ? 1.173   -3.767  51.472  1.00 96.46  ? 192 TYR D C   1 
ATOM   3064 O O   . TYR B 2 193 ? 2.256   -4.111  51.956  1.00 94.15  ? 192 TYR D O   1 
ATOM   3065 C CB  . TYR B 2 193 ? 0.740   -1.399  52.191  1.00 100.57 ? 192 TYR D CB  1 
ATOM   3066 C CG  . TYR B 2 193 ? -0.157  -0.368  52.863  1.00 101.04 ? 192 TYR D CG  1 
ATOM   3067 C CD1 . TYR B 2 193 ? -0.516  -0.497  54.200  1.00 98.63  ? 192 TYR D CD1 1 
ATOM   3068 C CD2 . TYR B 2 193 ? -0.608  0.751   52.169  1.00 96.16  ? 192 TYR D CD2 1 
ATOM   3069 C CE1 . TYR B 2 193 ? -1.324  0.425   54.810  1.00 99.98  ? 192 TYR D CE1 1 
ATOM   3070 C CE2 . TYR B 2 193 ? -1.407  1.693   52.778  1.00 95.60  ? 192 TYR D CE2 1 
ATOM   3071 C CZ  . TYR B 2 193 ? -1.764  1.522   54.100  1.00 100.78 ? 192 TYR D CZ  1 
ATOM   3072 O OH  . TYR B 2 193 ? -2.571  2.442   54.726  1.00 103.89 ? 192 TYR D OH  1 
ATOM   3073 N N   . ALA B 2 194 ? 0.757   -4.151  50.259  1.00 95.10  ? 193 ALA D N   1 
ATOM   3074 C CA  . ALA B 2 194 ? 1.518   -5.096  49.444  1.00 92.18  ? 193 ALA D CA  1 
ATOM   3075 C C   . ALA B 2 194 ? 1.573   -4.661  47.983  1.00 94.08  ? 193 ALA D C   1 
ATOM   3076 O O   . ALA B 2 194 ? 0.720   -3.916  47.491  1.00 95.61  ? 193 ALA D O   1 
ATOM   3077 C CB  . ALA B 2 194 ? 0.939   -6.510  49.517  1.00 92.91  ? 193 ALA D CB  1 
ATOM   3078 N N   . CYS B 2 195 ? 2.589   -5.174  47.287  1.00 92.75  ? 194 CYS D N   1 
ATOM   3079 C CA  . CYS B 2 195 ? 2.831   -4.892  45.878  1.00 89.95  ? 194 CYS D CA  1 
ATOM   3080 C C   . CYS B 2 195 ? 2.895   -6.227  45.143  1.00 91.73  ? 194 CYS D C   1 
ATOM   3081 O O   . CYS B 2 195 ? 3.686   -7.097  45.519  1.00 90.52  ? 194 CYS D O   1 
ATOM   3082 C CB  . CYS B 2 195 ? 4.130   -4.086  45.713  1.00 87.82  ? 194 CYS D CB  1 
ATOM   3083 S SG  . CYS B 2 195 ? 5.135   -4.451  44.247  1.00 96.71  ? 194 CYS D SG  1 
ATOM   3084 N N   . GLU B 2 196 ? 2.050   -6.395  44.120  1.00 100.76 ? 195 GLU D N   1 
ATOM   3085 C CA  . GLU B 2 196 ? 1.927   -7.631  43.343  1.00 97.43  ? 195 GLU D CA  1 
ATOM   3086 C C   . GLU B 2 196 ? 2.379   -7.401  41.904  1.00 95.57  ? 195 GLU D C   1 
ATOM   3087 O O   . GLU B 2 196 ? 1.892   -6.485  41.227  1.00 94.55  ? 195 GLU D O   1 
ATOM   3088 C CB  . GLU B 2 196 ? 0.484   -8.136  43.366  1.00 99.08  ? 195 GLU D CB  1 
ATOM   3089 C CG  . GLU B 2 196 ? 0.003   -8.763  42.066  1.00 101.18 ? 195 GLU D CG  1 
ATOM   3090 C CD  . GLU B 2 196 ? -1.096  -9.786  42.290  1.00 107.69 ? 195 GLU D CD  1 
ATOM   3091 O OE1 . GLU B 2 196 ? -1.889  -9.603  43.244  1.00 109.61 ? 195 GLU D OE1 1 
ATOM   3092 O OE2 . GLU B 2 196 ? -1.194  -10.744 41.489  1.00 105.17 ? 195 GLU D OE2 1 
ATOM   3093 N N   . VAL B 2 197 ? 3.299   -8.235  41.433  1.00 92.44  ? 196 VAL D N   1 
ATOM   3094 C CA  . VAL B 2 197 ? 3.972   -8.013  40.159  1.00 91.19  ? 196 VAL D CA  1 
ATOM   3095 C C   . VAL B 2 197 ? 3.730   -9.206  39.245  1.00 94.39  ? 196 VAL D C   1 
ATOM   3096 O O   . VAL B 2 197 ? 4.043   -10.347 39.598  1.00 91.85  ? 196 VAL D O   1 
ATOM   3097 C CB  . VAL B 2 197 ? 5.473   -7.765  40.362  1.00 85.26  ? 196 VAL D CB  1 
ATOM   3098 C CG1 . VAL B 2 197 ? 6.175   -7.645  39.025  1.00 84.22  ? 196 VAL D CG1 1 
ATOM   3099 C CG2 . VAL B 2 197 ? 5.662   -6.507  41.198  1.00 85.06  ? 196 VAL D CG2 1 
ATOM   3100 N N   . THR B 2 198 ? 3.168   -8.938  38.072  1.00 101.18 ? 197 THR D N   1 
ATOM   3101 C CA  . THR B 2 198 ? 2.904   -9.985  37.098  1.00 97.79  ? 197 THR D CA  1 
ATOM   3102 C C   . THR B 2 198 ? 3.750   -9.771  35.855  1.00 99.28  ? 197 THR D C   1 
ATOM   3103 O O   . THR B 2 198 ? 3.218   -9.582  34.758  1.00 104.43 ? 197 THR D O   1 
ATOM   3104 C CB  . THR B 2 198 ? 1.429   -10.003 36.724  1.00 99.21  ? 197 THR D CB  1 
ATOM   3105 O OG1 . THR B 2 198 ? 1.221   -9.082  35.646  1.00 102.88 ? 197 THR D OG1 1 
ATOM   3106 C CG2 . THR B 2 198 ? 0.584   -9.587  37.912  1.00 104.22 ? 197 THR D CG2 1 
ATOM   3107 N N   . HIS B 2 199 ? 5.067   -9.759  36.019  1.00 91.77  ? 198 HIS D N   1 
ATOM   3108 C CA  . HIS B 2 199 ? 5.943   -9.843  34.864  1.00 86.26  ? 198 HIS D CA  1 
ATOM   3109 C C   . HIS B 2 199 ? 5.738   -11.184 34.178  1.00 88.35  ? 198 HIS D C   1 
ATOM   3110 O O   . HIS B 2 199 ? 5.315   -12.169 34.793  1.00 91.44  ? 198 HIS D O   1 
ATOM   3111 C CB  . HIS B 2 199 ? 7.400   -9.683  35.281  1.00 81.57  ? 198 HIS D CB  1 
ATOM   3112 C CG  . HIS B 2 199 ? 8.344   -9.520  34.133  1.00 78.83  ? 198 HIS D CG  1 
ATOM   3113 N ND1 . HIS B 2 199 ? 9.436   -10.338 33.944  1.00 75.96  ? 198 HIS D ND1 1 
ATOM   3114 C CD2 . HIS B 2 199 ? 8.352   -8.636  33.108  1.00 76.13  ? 198 HIS D CD2 1 
ATOM   3115 C CE1 . HIS B 2 199 ? 10.083  -9.952  32.859  1.00 74.71  ? 198 HIS D CE1 1 
ATOM   3116 N NE2 . HIS B 2 199 ? 9.447   -8.920  32.335  1.00 74.90  ? 198 HIS D NE2 1 
ATOM   3117 N N   . GLN B 2 200 ? 6.014   -11.218 32.883  1.00 90.14  ? 199 GLN D N   1 
ATOM   3118 C CA  . GLN B 2 200 ? 5.860   -12.483 32.189  1.00 91.01  ? 199 GLN D CA  1 
ATOM   3119 C C   . GLN B 2 200 ? 6.964   -13.463 32.558  1.00 90.28  ? 199 GLN D C   1 
ATOM   3120 O O   . GLN B 2 200 ? 6.799   -14.668 32.351  1.00 93.00  ? 199 GLN D O   1 
ATOM   3121 C CB  . GLN B 2 200 ? 5.805   -12.234 30.681  1.00 101.32 ? 199 GLN D CB  1 
ATOM   3122 C CG  . GLN B 2 200 ? 7.144   -12.147 29.985  1.00 97.65  ? 199 GLN D CG  1 
ATOM   3123 C CD  . GLN B 2 200 ? 7.485   -13.444 29.283  1.00 104.97 ? 199 GLN D CD  1 
ATOM   3124 O OE1 . GLN B 2 200 ? 6.598   -14.208 28.880  1.00 107.36 ? 199 GLN D OE1 1 
ATOM   3125 N NE2 . GLN B 2 200 ? 8.769   -13.710 29.147  1.00 105.08 ? 199 GLN D NE2 1 
ATOM   3126 N N   . GLY B 2 201 ? 8.071   -12.979 33.115  1.00 84.75  ? 200 GLY D N   1 
ATOM   3127 C CA  . GLY B 2 201 ? 9.120   -13.845 33.609  1.00 82.28  ? 200 GLY D CA  1 
ATOM   3128 C C   . GLY B 2 201 ? 8.820   -14.345 35.011  1.00 84.87  ? 200 GLY D C   1 
ATOM   3129 O O   . GLY B 2 201 ? 9.694   -14.887 35.696  1.00 81.39  ? 200 GLY D O   1 
ATOM   3130 N N   . LEU B 2 202 ? 7.579   -14.145 35.456  1.00 83.13  ? 201 LEU D N   1 
ATOM   3131 C CA  . LEU B 2 202 ? 7.095   -14.637 36.737  1.00 76.88  ? 201 LEU D CA  1 
ATOM   3132 C C   . LEU B 2 202 ? 5.953   -15.581 36.427  1.00 83.88  ? 201 LEU D C   1 
ATOM   3133 O O   . LEU B 2 202 ? 4.913   -15.149 35.914  1.00 82.79  ? 201 LEU D O   1 
ATOM   3134 C CB  . LEU B 2 202 ? 6.624   -13.508 37.655  1.00 80.57  ? 201 LEU D CB  1 
ATOM   3135 C CG  . LEU B 2 202 ? 7.603   -12.416 38.078  1.00 75.46  ? 201 LEU D CG  1 
ATOM   3136 C CD1 . LEU B 2 202 ? 6.873   -11.419 38.922  1.00 79.34  ? 201 LEU D CD1 1 
ATOM   3137 C CD2 . LEU B 2 202 ? 8.788   -13.001 38.819  1.00 73.52  ? 201 LEU D CD2 1 
ATOM   3138 N N   . SER B 2 203 ? 6.163   -16.869 36.716  1.00 84.35  ? 202 SER D N   1 
ATOM   3139 C CA  . SER B 2 203 ? 5.092   -17.854 36.621  1.00 85.35  ? 202 SER D CA  1 
ATOM   3140 C C   . SER B 2 203 ? 3.864   -17.390 37.396  1.00 88.28  ? 202 SER D C   1 
ATOM   3141 O O   . SER B 2 203 ? 2.818   -17.087 36.809  1.00 91.51  ? 202 SER D O   1 
ATOM   3142 C CB  . SER B 2 203 ? 5.581   -19.213 37.135  1.00 82.88  ? 202 SER D CB  1 
ATOM   3143 O OG  . SER B 2 203 ? 6.981   -19.205 37.354  1.00 80.45  ? 202 SER D OG  1 
ATOM   3144 N N   . SER B 2 204 ? 3.979   -17.328 38.751  1.00 87.71  ? 203 SER D N   1 
ATOM   3145 C CA  . SER B 2 204 ? 2.907   -16.722 39.516  1.00 89.08  ? 203 SER D CA  1 
ATOM   3146 C C   . SER B 2 204 ? 3.262   -15.278 39.820  1.00 90.03  ? 203 SER D C   1 
ATOM   3147 O O   . SER B 2 204 ? 4.444   -14.922 39.847  1.00 89.96  ? 203 SER D O   1 
ATOM   3148 C CB  . SER B 2 204 ? 2.679   -17.447 40.844  1.00 91.10  ? 203 SER D CB  1 
ATOM   3149 O OG  . SER B 2 204 ? 3.908   -17.761 41.479  1.00 93.34  ? 203 SER D OG  1 
ATOM   3150 N N   . PRO B 2 205 ? 2.272   -14.419 40.054  1.00 89.81  ? 204 PRO D N   1 
ATOM   3151 C CA  . PRO B 2 205 ? 2.589   -13.069 40.527  1.00 89.82  ? 204 PRO D CA  1 
ATOM   3152 C C   . PRO B 2 205 ? 3.237   -13.125 41.903  1.00 83.49  ? 204 PRO D C   1 
ATOM   3153 O O   . PRO B 2 205 ? 2.737   -13.773 42.825  1.00 85.03  ? 204 PRO D O   1 
ATOM   3154 C CB  . PRO B 2 205 ? 1.225   -12.372 40.555  1.00 91.19  ? 204 PRO D CB  1 
ATOM   3155 C CG  . PRO B 2 205 ? 0.420   -13.100 39.543  1.00 88.32  ? 204 PRO D CG  1 
ATOM   3156 C CD  . PRO B 2 205 ? 0.851   -14.543 39.687  1.00 88.11  ? 204 PRO D CD  1 
ATOM   3157 N N   . VAL B 2 206 ? 4.384   -12.482 42.012  1.00 80.73  ? 205 VAL D N   1 
ATOM   3158 C CA  . VAL B 2 206 ? 5.092   -12.355 43.271  1.00 81.45  ? 205 VAL D CA  1 
ATOM   3159 C C   . VAL B 2 206 ? 4.544   -11.133 43.980  1.00 85.76  ? 205 VAL D C   1 
ATOM   3160 O O   . VAL B 2 206 ? 4.332   -10.086 43.353  1.00 86.86  ? 205 VAL D O   1 
ATOM   3161 C CB  . VAL B 2 206 ? 6.606   -12.231 43.040  1.00 79.60  ? 205 VAL D CB  1 
ATOM   3162 C CG1 . VAL B 2 206 ? 7.280   -11.516 44.205  1.00 78.04  ? 205 VAL D CG1 1 
ATOM   3163 C CG2 . VAL B 2 206 ? 7.207   -13.600 42.825  1.00 80.74  ? 205 VAL D CG2 1 
ATOM   3164 N N   . THR B 2 207 ? 4.287   -11.268 45.277  1.00 83.88  ? 206 THR D N   1 
ATOM   3165 C CA  . THR B 2 207 ? 3.789   -10.160 46.075  1.00 84.41  ? 206 THR D CA  1 
ATOM   3166 C C   . THR B 2 207 ? 4.784   -9.841  47.183  1.00 82.05  ? 206 THR D C   1 
ATOM   3167 O O   . THR B 2 207 ? 5.348   -10.746 47.801  1.00 82.72  ? 206 THR D O   1 
ATOM   3168 C CB  . THR B 2 207 ? 2.413   -10.477 46.665  1.00 85.17  ? 206 THR D CB  1 
ATOM   3169 O OG1 . THR B 2 207 ? 1.685   -11.324 45.765  1.00 86.14  ? 206 THR D OG1 1 
ATOM   3170 C CG2 . THR B 2 207 ? 1.631   -9.193  46.849  1.00 87.24  ? 206 THR D CG2 1 
ATOM   3171 N N   . LYS B 2 208 ? 5.011   -8.553  47.417  1.00 82.04  ? 207 LYS D N   1 
ATOM   3172 C CA  . LYS B 2 208 ? 5.856   -8.083  48.505  1.00 83.51  ? 207 LYS D CA  1 
ATOM   3173 C C   . LYS B 2 208 ? 5.051   -7.128  49.374  1.00 88.36  ? 207 LYS D C   1 
ATOM   3174 O O   . LYS B 2 208 ? 4.360   -6.250  48.849  1.00 89.40  ? 207 LYS D O   1 
ATOM   3175 C CB  . LYS B 2 208 ? 7.104   -7.383  47.987  1.00 78.12  ? 207 LYS D CB  1 
ATOM   3176 C CG  . LYS B 2 208 ? 8.184   -8.322  47.464  1.00 80.39  ? 207 LYS D CG  1 
ATOM   3177 C CD  . LYS B 2 208 ? 8.181   -9.693  48.117  1.00 79.44  ? 207 LYS D CD  1 
ATOM   3178 C CE  . LYS B 2 208 ? 9.460   -10.450 47.801  1.00 78.83  ? 207 LYS D CE  1 
ATOM   3179 N NZ  . LYS B 2 208 ? 10.670  -9.674  48.204  1.00 83.22  ? 207 LYS D NZ  1 
ATOM   3180 N N   . SER B 2 209 ? 5.154   -7.295  50.703  1.00 90.77  ? 208 SER D N   1 
ATOM   3181 C CA  . SER B 2 209 ? 4.278   -6.617  51.657  1.00 90.20  ? 208 SER D CA  1 
ATOM   3182 C C   . SER B 2 209 ? 5.048   -6.131  52.890  1.00 95.08  ? 208 SER D C   1 
ATOM   3183 O O   . SER B 2 209 ? 6.220   -6.462  53.092  1.00 92.38  ? 208 SER D O   1 
ATOM   3184 C CB  . SER B 2 209 ? 3.149   -7.543  52.097  1.00 94.18  ? 208 SER D CB  1 
ATOM   3185 O OG  . SER B 2 209 ? 3.554   -8.898  52.026  1.00 94.95  ? 208 SER D OG  1 
ATOM   3186 N N   . PHE B 2 210 ? 4.352   -5.343  53.726  1.00 104.24 ? 209 PHE D N   1 
ATOM   3187 C CA  . PHE B 2 210 ? 4.857   -4.843  55.009  1.00 104.57 ? 209 PHE D CA  1 
ATOM   3188 C C   . PHE B 2 210 ? 3.679   -4.597  55.958  1.00 106.20 ? 209 PHE D C   1 
ATOM   3189 O O   . PHE B 2 210 ? 2.516   -4.676  55.556  1.00 107.58 ? 209 PHE D O   1 
ATOM   3190 C CB  . PHE B 2 210 ? 5.700   -3.566  54.822  1.00 103.77 ? 209 PHE D CB  1 
ATOM   3191 C CG  . PHE B 2 210 ? 4.893   -2.330  54.480  1.00 103.00 ? 209 PHE D CG  1 
ATOM   3192 C CD1 . PHE B 2 210 ? 4.322   -1.553  55.479  1.00 104.28 ? 209 PHE D CD1 1 
ATOM   3193 C CD2 . PHE B 2 210 ? 4.743   -1.923  53.168  1.00 101.04 ? 209 PHE D CD2 1 
ATOM   3194 C CE1 . PHE B 2 210 ? 3.589   -0.423  55.179  1.00 103.64 ? 209 PHE D CE1 1 
ATOM   3195 C CE2 . PHE B 2 210 ? 4.019   -0.785  52.865  1.00 100.94 ? 209 PHE D CE2 1 
ATOM   3196 C CZ  . PHE B 2 210 ? 3.440   -0.035  53.873  1.00 102.08 ? 209 PHE D CZ  1 
ATOM   3197 N N   . ASN B 2 211 ? 3.978   -4.283  57.219  1.00 102.35 ? 210 ASN D N   1 
ATOM   3198 C CA  . ASN B 2 211 ? 2.935   -4.034  58.218  1.00 100.39 ? 210 ASN D CA  1 
ATOM   3199 C C   . ASN B 2 211 ? 3.288   -2.798  59.051  1.00 100.78 ? 210 ASN D C   1 
ATOM   3200 O O   . ASN B 2 211 ? 4.054   -1.925  58.637  1.00 100.19 ? 210 ASN D O   1 
ATOM   3201 C CB  . ASN B 2 211 ? 2.729   -5.278  59.096  1.00 106.42 ? 210 ASN D CB  1 
ATOM   3202 C CG  . ASN B 2 211 ? 3.984   -5.663  59.874  1.00 108.64 ? 210 ASN D CG  1 
ATOM   3203 O OD1 . ASN B 2 211 ? 5.095   -5.221  59.537  1.00 111.59 ? 210 ASN D OD1 1 
ATOM   3204 N ND2 . ASN B 2 211 ? 3.814   -6.481  60.927  1.00 93.99  ? 210 ASN D ND2 1 
ATOM   3205 N N   . ARG B 2 212 ? 2.745   -2.715  60.275  1.00 103.60 ? 211 ARG D N   1 
ATOM   3206 C CA  . ARG B 2 212 ? 2.857   -1.516  61.124  1.00 102.21 ? 211 ARG D CA  1 
ATOM   3207 C C   . ARG B 2 212 ? 2.366   -0.271  60.385  1.00 103.42 ? 211 ARG D C   1 
ATOM   3208 O O   . ARG B 2 212 ? 2.888   0.830   60.588  1.00 103.18 ? 211 ARG D O   1 
ATOM   3209 C CB  . ARG B 2 212 ? 4.293   -1.292  61.625  1.00 102.19 ? 211 ARG D CB  1 
ATOM   3210 C CG  . ARG B 2 212 ? 4.634   -1.864  63.001  1.00 100.11 ? 211 ARG D CG  1 
ATOM   3211 C CD  . ARG B 2 212 ? 6.139   -2.094  63.090  1.00 101.45 ? 211 ARG D CD  1 
ATOM   3212 N NE  . ARG B 2 212 ? 6.556   -3.191  62.223  1.00 101.47 ? 211 ARG D NE  1 
ATOM   3213 C CZ  . ARG B 2 212 ? 7.792   -3.668  62.143  1.00 100.37 ? 211 ARG D CZ  1 
ATOM   3214 N NH1 . ARG B 2 212 ? 8.791   -3.129  62.823  1.00 99.95  ? 211 ARG D NH1 1 
ATOM   3215 N NH2 . ARG B 2 212 ? 8.035   -4.699  61.343  1.00 98.34  ? 211 ARG D NH2 1 
ATOM   3216 N N   . GLY B 2 213 ? 1.371   -0.446  59.512  1.00 101.79 ? 212 GLY D N   1 
ATOM   3217 C CA  . GLY B 2 213 ? 0.860   0.620   58.662  1.00 95.96  ? 212 GLY D CA  1 
ATOM   3218 C C   . GLY B 2 213 ? 0.602   1.961   59.327  1.00 97.44  ? 212 GLY D C   1 
ATOM   3219 O O   . GLY B 2 213 ? -0.533  2.439   59.370  1.00 100.18 ? 212 GLY D O   1 
ATOM   3220 N N   . SER C 3 2   ? 36.390  28.889  1.864   1.00 91.68  ? 2   SER A N   1 
ATOM   3221 C CA  . SER C 3 2   ? 36.215  30.017  2.777   1.00 95.84  ? 2   SER A CA  1 
ATOM   3222 C C   . SER C 3 2   ? 36.596  31.334  2.095   1.00 94.87  ? 2   SER A C   1 
ATOM   3223 O O   . SER C 3 2   ? 36.150  32.411  2.529   1.00 89.24  ? 2   SER A O   1 
ATOM   3224 C CB  . SER C 3 2   ? 37.032  29.811  4.073   1.00 93.04  ? 2   SER A CB  1 
ATOM   3225 O OG  . SER C 3 2   ? 38.404  30.148  3.908   1.00 94.68  ? 2   SER A OG  1 
ATOM   3226 N N   . ILE C 3 3   ? 37.386  31.238  1.014   1.00 94.19  ? 3   ILE A N   1 
ATOM   3227 C CA  . ILE C 3 3   ? 37.958  32.442  0.403   1.00 97.58  ? 3   ILE A CA  1 
ATOM   3228 C C   . ILE C 3 3   ? 36.871  33.273  -0.281  1.00 95.07  ? 3   ILE A C   1 
ATOM   3229 O O   . ILE C 3 3   ? 36.944  34.509  -0.323  1.00 94.31  ? 3   ILE A O   1 
ATOM   3230 C CB  . ILE C 3 3   ? 39.092  32.066  -0.576  1.00 96.29  ? 3   ILE A CB  1 
ATOM   3231 C CG1 . ILE C 3 3   ? 40.484  32.135  0.079   1.00 94.44  ? 3   ILE A CG1 1 
ATOM   3232 C CG2 . ILE C 3 3   ? 39.063  32.946  -1.801  1.00 96.07  ? 3   ILE A CG2 1 
ATOM   3233 C CD1 . ILE C 3 3   ? 40.670  31.237  1.296   1.00 92.95  ? 3   ILE A CD1 1 
ATOM   3234 N N   . VAL C 3 4   ? 35.840  32.619  -0.802  1.00 92.86  ? 4   VAL A N   1 
ATOM   3235 C CA  . VAL C 3 4   ? 34.703  33.280  -1.429  1.00 91.74  ? 4   VAL A CA  1 
ATOM   3236 C C   . VAL C 3 4   ? 33.440  32.869  -0.675  1.00 89.80  ? 4   VAL A C   1 
ATOM   3237 O O   . VAL C 3 4   ? 33.285  31.701  -0.295  1.00 90.17  ? 4   VAL A O   1 
ATOM   3238 C CB  . VAL C 3 4   ? 34.614  32.920  -2.934  1.00 90.17  ? 4   VAL A CB  1 
ATOM   3239 C CG1 . VAL C 3 4   ? 33.326  33.439  -3.572  1.00 89.30  ? 4   VAL A CG1 1 
ATOM   3240 C CG2 . VAL C 3 4   ? 35.823  33.454  -3.692  1.00 93.01  ? 4   VAL A CG2 1 
ATOM   3241 N N   . SER C 3 5   ? 32.545  33.830  -0.451  1.00 88.58  ? 5   SER A N   1 
ATOM   3242 C CA  . SER C 3 5   ? 31.262  33.570  0.177   1.00 86.92  ? 5   SER A CA  1 
ATOM   3243 C C   . SER C 3 5   ? 30.177  34.320  -0.581  1.00 87.64  ? 5   SER A C   1 
ATOM   3244 O O   . SER C 3 5   ? 30.465  35.207  -1.380  1.00 95.66  ? 5   SER A O   1 
ATOM   3245 C CB  . SER C 3 5   ? 31.300  33.986  1.640   1.00 92.23  ? 5   SER A CB  1 
ATOM   3246 O OG  . SER C 3 5   ? 32.524  33.556  2.213   1.00 96.68  ? 5   SER A OG  1 
ATOM   3247 N N   . LEU C 3 6   ? 28.923  33.970  -0.333  1.00 86.09  ? 6   LEU A N   1 
ATOM   3248 C CA  . LEU C 3 6   ? 27.804  34.541  -1.075  1.00 86.66  ? 6   LEU A CA  1 
ATOM   3249 C C   . LEU C 3 6   ? 27.063  35.564  -0.219  1.00 88.73  ? 6   LEU A C   1 
ATOM   3250 O O   . LEU C 3 6   ? 26.587  35.222  0.874   1.00 89.28  ? 6   LEU A O   1 
ATOM   3251 C CB  . LEU C 3 6   ? 26.838  33.443  -1.514  1.00 84.32  ? 6   LEU A CB  1 
ATOM   3252 C CG  . LEU C 3 6   ? 26.913  32.898  -2.954  1.00 85.95  ? 6   LEU A CG  1 
ATOM   3253 C CD1 . LEU C 3 6   ? 26.298  31.513  -2.993  1.00 82.49  ? 6   LEU A CD1 1 
ATOM   3254 C CD2 . LEU C 3 6   ? 26.270  33.820  -4.023  1.00 85.67  ? 6   LEU A CD2 1 
ATOM   3255 N N   . LEU C 3 7   ? 26.952  36.816  -0.712  1.00 90.37  ? 7   LEU A N   1 
ATOM   3256 C CA  . LEU C 3 7   ? 25.999  37.746  -0.104  1.00 91.52  ? 7   LEU A CA  1 
ATOM   3257 C C   . LEU C 3 7   ? 24.577  37.502  -0.576  1.00 90.55  ? 7   LEU A C   1 
ATOM   3258 O O   . LEU C 3 7   ? 23.632  37.685  0.189   1.00 90.30  ? 7   LEU A O   1 
ATOM   3259 C CB  . LEU C 3 7   ? 26.317  39.203  -0.410  1.00 94.71  ? 7   LEU A CB  1 
ATOM   3260 C CG  . LEU C 3 7   ? 27.619  39.909  -0.076  1.00 96.84  ? 7   LEU A CG  1 
ATOM   3261 C CD1 . LEU C 3 7   ? 28.011  39.690  1.366   1.00 96.27  ? 7   LEU A CD1 1 
ATOM   3262 C CD2 . LEU C 3 7   ? 28.705  39.495  -1.047  1.00 96.96  ? 7   LEU A CD2 1 
ATOM   3263 N N   . GLY C 3 8   ? 24.378  37.152  -1.831  1.00 90.25  ? 8   GLY A N   1 
ATOM   3264 C CA  . GLY C 3 8   ? 23.013  37.005  -2.281  1.00 89.73  ? 8   GLY A CA  1 
ATOM   3265 C C   . GLY C 3 8   ? 22.912  36.340  -3.630  1.00 89.04  ? 8   GLY A C   1 
ATOM   3266 O O   . GLY C 3 8   ? 23.880  36.265  -4.390  1.00 89.50  ? 8   GLY A O   1 
ATOM   3267 N N   . ILE C 3 9   ? 21.714  35.841  -3.897  1.00 88.03  ? 9   ILE A N   1 
ATOM   3268 C CA  . ILE C 3 9   ? 21.285  35.402  -5.211  1.00 87.86  ? 9   ILE A CA  1 
ATOM   3269 C C   . ILE C 3 9   ? 19.862  35.903  -5.415  1.00 88.83  ? 9   ILE A C   1 
ATOM   3270 O O   . ILE C 3 9   ? 19.017  35.750  -4.528  1.00 88.07  ? 9   ILE A O   1 
ATOM   3271 C CB  . ILE C 3 9   ? 21.363  33.867  -5.350  1.00 86.07  ? 9   ILE A CB  1 
ATOM   3272 C CG1 . ILE C 3 9   ? 22.708  33.345  -4.828  1.00 84.20  ? 9   ILE A CG1 1 
ATOM   3273 C CG2 . ILE C 3 9   ? 21.089  33.447  -6.785  1.00 86.21  ? 9   ILE A CG2 1 
ATOM   3274 C CD1 . ILE C 3 9   ? 22.805  31.867  -4.743  1.00 81.69  ? 9   ILE A CD1 1 
ATOM   3275 N N   . LYS C 3 10  ? 19.599  36.519  -6.563  1.00 90.65  ? 10  LYS A N   1 
ATOM   3276 C CA  . LYS C 3 10  ? 18.262  36.994  -6.886  1.00 91.84  ? 10  LYS A CA  1 
ATOM   3277 C C   . LYS C 3 10  ? 17.854  36.435  -8.243  1.00 91.79  ? 10  LYS A C   1 
ATOM   3278 O O   . LYS C 3 10  ? 18.634  36.478  -9.203  1.00 92.44  ? 10  LYS A O   1 
ATOM   3279 C CB  . LYS C 3 10  ? 18.203  38.530  -6.865  1.00 94.76  ? 10  LYS A CB  1 
ATOM   3280 C CG  . LYS C 3 10  ? 16.794  39.114  -6.781  1.00 96.05  ? 10  LYS A CG  1 
ATOM   3281 C CD  . LYS C 3 10  ? 16.812  40.647  -6.740  1.00 99.09  ? 10  LYS A CD  1 
ATOM   3282 C CE  . LYS C 3 10  ? 15.609  41.193  -5.966  1.00 99.92  ? 10  LYS A CE  1 
ATOM   3283 N NZ  . LYS C 3 10  ? 15.935  42.094  -4.801  1.00 100.97 ? 10  LYS A NZ  1 
ATOM   3284 N N   . VAL C 3 11  ? 16.635  35.911  -8.314  1.00 91.15  ? 11  VAL A N   1 
ATOM   3285 C CA  . VAL C 3 11  ? 16.136  35.212  -9.499  1.00 91.28  ? 11  VAL A CA  1 
ATOM   3286 C C   . VAL C 3 11  ? 15.239  36.176  -10.284 1.00 95.70  ? 11  VAL A C   1 
ATOM   3287 O O   . VAL C 3 11  ? 14.017  36.235  -10.106 1.00 94.96  ? 11  VAL A O   1 
ATOM   3288 C CB  . VAL C 3 11  ? 15.431  33.910  -9.118  1.00 88.65  ? 11  VAL A CB  1 
ATOM   3289 C CG1 . VAL C 3 11  ? 14.312  34.169  -8.156  1.00 88.80  ? 11  VAL A CG1 1 
ATOM   3290 C CG2 . VAL C 3 11  ? 14.892  33.217  -10.346 1.00 94.21  ? 11  VAL A CG2 1 
ATOM   3291 N N   . LEU C 3 12  ? 15.850  36.922  -11.211 1.00 95.50  ? 12  LEU A N   1 
ATOM   3292 C CA  . LEU C 3 12  ? 15.153  38.057  -11.815 1.00 98.40  ? 12  LEU A CA  1 
ATOM   3293 C C   . LEU C 3 12  ? 13.894  37.630  -12.546 1.00 99.00  ? 12  LEU A C   1 
ATOM   3294 O O   . LEU C 3 12  ? 12.907  38.380  -12.575 1.00 100.73 ? 12  LEU A O   1 
ATOM   3295 C CB  . LEU C 3 12  ? 16.056  38.813  -12.790 1.00 100.41 ? 12  LEU A CB  1 
ATOM   3296 C CG  . LEU C 3 12  ? 17.310  39.540  -12.315 1.00 101.08 ? 12  LEU A CG  1 
ATOM   3297 C CD1 . LEU C 3 12  ? 18.326  38.569  -11.798 1.00 99.29  ? 12  LEU A CD1 1 
ATOM   3298 C CD2 . LEU C 3 12  ? 17.884  40.359  -13.449 1.00 103.63 ? 12  LEU A CD2 1 
ATOM   3299 N N   . ASN C 3 13  ? 13.907  36.439  -13.126 1.00 97.14  ? 13  ASN A N   1 
ATOM   3300 C CA  . ASN C 3 13  ? 12.836  35.980  -14.004 1.00 97.75  ? 13  ASN A CA  1 
ATOM   3301 C C   . ASN C 3 13  ? 11.831  35.133  -13.244 1.00 96.15  ? 13  ASN A C   1 
ATOM   3302 O O   . ASN C 3 13  ? 11.527  34.027  -13.653 1.00 96.75  ? 13  ASN A O   1 
ATOM   3303 C CB  . ASN C 3 13  ? 13.433  35.202  -15.172 1.00 101.60 ? 13  ASN A CB  1 
ATOM   3304 C CG  . ASN C 3 13  ? 14.616  34.328  -14.751 1.00 103.04 ? 13  ASN A CG  1 
ATOM   3305 O OD1 . ASN C 3 13  ? 15.745  34.803  -14.688 1.00 104.08 ? 13  ASN A OD1 1 
ATOM   3306 N ND2 . ASN C 3 13  ? 14.360  33.045  -14.479 1.00 102.26 ? 13  ASN A ND2 1 
ATOM   3307 N N   . ASN C 3 14  ? 11.284  35.606  -12.136 1.00 96.27  ? 14  ASN A N   1 
ATOM   3308 C CA  . ASN C 3 14  ? 10.483  34.711  -11.327 1.00 94.55  ? 14  ASN A CA  1 
ATOM   3309 C C   . ASN C 3 14  ? 9.108   35.297  -11.045 1.00 96.30  ? 14  ASN A C   1 
ATOM   3310 O O   . ASN C 3 14  ? 9.015   36.398  -10.480 1.00 97.73  ? 14  ASN A O   1 
ATOM   3311 C CB  . ASN C 3 14  ? 11.186  34.414  -10.008 1.00 96.14  ? 14  ASN A CB  1 
ATOM   3312 C CG  . ASN C 3 14  ? 10.699  33.131  -9.362  1.00 92.07  ? 14  ASN A CG  1 
ATOM   3313 O OD1 . ASN C 3 14  ? 9.507   32.802  -9.356  1.00 90.45  ? 14  ASN A OD1 1 
ATOM   3314 N ND2 . ASN C 3 14  ? 11.631  32.398  -8.813  1.00 90.67  ? 14  ASN A ND2 1 
ATOM   3315 N N   . PRO C 3 15  ? 8.020   34.570  -11.345 1.00 96.29  ? 15  PRO A N   1 
ATOM   3316 C CA  . PRO C 3 15  ? 7.952   33.249  -12.001 1.00 94.89  ? 15  PRO A CA  1 
ATOM   3317 C C   . PRO C 3 15  ? 8.241   33.301  -13.494 1.00 96.20  ? 15  PRO A C   1 
ATOM   3318 O O   . PRO C 3 15  ? 8.300   34.395  -14.070 1.00 98.50  ? 15  PRO A O   1 
ATOM   3319 C CB  . PRO C 3 15  ? 6.502   32.809  -11.736 1.00 95.33  ? 15  PRO A CB  1 
ATOM   3320 C CG  . PRO C 3 15  ? 6.135   33.510  -10.483 1.00 95.55  ? 15  PRO A CG  1 
ATOM   3321 C CD  . PRO C 3 15  ? 6.757   34.867  -10.649 1.00 97.26  ? 15  PRO A CD  1 
ATOM   3322 N N   . ALA C 3 16  ? 8.407   32.128  -14.122 1.00 94.89  ? 16  ALA A N   1 
ATOM   3323 C CA  . ALA C 3 16  ? 8.740   32.029  -15.537 1.00 95.94  ? 16  ALA A CA  1 
ATOM   3324 C C   . ALA C 3 16  ? 8.175   30.732  -16.110 1.00 97.85  ? 16  ALA A C   1 
ATOM   3325 O O   . ALA C 3 16  ? 7.696   29.859  -15.381 1.00 96.22  ? 16  ALA A O   1 
ATOM   3326 C CB  . ALA C 3 16  ? 10.254  32.104  -15.756 1.00 94.96  ? 16  ALA A CB  1 
ATOM   3327 N N   . LYS C 3 17  ? 8.230   30.627  -17.444 1.00 103.32 ? 17  LYS A N   1 
ATOM   3328 C CA  . LYS C 3 17  ? 7.844   29.437  -18.196 1.00 102.74 ? 17  LYS A CA  1 
ATOM   3329 C C   . LYS C 3 17  ? 8.905   28.353  -18.052 1.00 100.86 ? 17  LYS A C   1 
ATOM   3330 O O   . LYS C 3 17  ? 10.081  28.639  -17.805 1.00 100.01 ? 17  LYS A O   1 
ATOM   3331 C CB  . LYS C 3 17  ? 7.682   29.753  -19.690 1.00 103.32 ? 17  LYS A CB  1 
ATOM   3332 C CG  . LYS C 3 17  ? 6.506   30.647  -20.085 1.00 109.43 ? 17  LYS A CG  1 
ATOM   3333 C CD  . LYS C 3 17  ? 5.351   29.862  -20.711 1.00 113.80 ? 17  LYS A CD  1 
ATOM   3334 C CE  . LYS C 3 17  ? 4.034   30.170  -19.989 1.00 118.66 ? 17  LYS A CE  1 
ATOM   3335 N NZ  . LYS C 3 17  ? 2.824   29.689  -20.717 1.00 123.71 ? 17  LYS A NZ  1 
ATOM   3336 N N   . PHE C 3 18  ? 8.484   27.095  -18.235 1.00 98.11  ? 18  PHE A N   1 
ATOM   3337 C CA  . PHE C 3 18  ? 9.448   25.995  -18.275 1.00 99.36  ? 18  PHE A CA  1 
ATOM   3338 C C   . PHE C 3 18  ? 10.594  26.326  -19.214 1.00 97.75  ? 18  PHE A C   1 
ATOM   3339 O O   . PHE C 3 18  ? 11.763  26.353  -18.811 1.00 96.06  ? 18  PHE A O   1 
ATOM   3340 C CB  . PHE C 3 18  ? 8.765   24.686  -18.696 1.00 98.66  ? 18  PHE A CB  1 
ATOM   3341 C CG  . PHE C 3 18  ? 9.371   23.455  -18.060 1.00 100.58 ? 18  PHE A CG  1 
ATOM   3342 C CD1 . PHE C 3 18  ? 8.583   22.568  -17.339 1.00 98.94  ? 18  PHE A CD1 1 
ATOM   3343 C CD2 . PHE C 3 18  ? 10.721  23.155  -18.222 1.00 98.47  ? 18  PHE A CD2 1 
ATOM   3344 C CE1 . PHE C 3 18  ? 9.128   21.443  -16.737 1.00 92.19  ? 18  PHE A CE1 1 
ATOM   3345 C CE2 . PHE C 3 18  ? 11.270  22.015  -17.634 1.00 94.14  ? 18  PHE A CE2 1 
ATOM   3346 C CZ  . PHE C 3 18  ? 10.468  21.160  -16.895 1.00 91.03  ? 18  PHE A CZ  1 
ATOM   3347 N N   . THR C 3 19  ? 10.258  26.649  -20.459 1.00 98.38  ? 19  THR A N   1 
ATOM   3348 C CA  . THR C 3 19  ? 11.222  26.917  -21.513 1.00 98.35  ? 19  THR A CA  1 
ATOM   3349 C C   . THR C 3 19  ? 12.070  28.168  -21.256 1.00 99.30  ? 19  THR A C   1 
ATOM   3350 O O   . THR C 3 19  ? 13.089  28.345  -21.932 1.00 99.07  ? 19  THR A O   1 
ATOM   3351 C CB  . THR C 3 19  ? 10.458  27.032  -22.842 1.00 97.50  ? 19  THR A CB  1 
ATOM   3352 O OG1 . THR C 3 19  ? 10.512  28.375  -23.328 1.00 98.36  ? 19  THR A OG1 1 
ATOM   3353 C CG2 . THR C 3 19  ? 8.982   26.675  -22.627 1.00 98.73  ? 19  THR A CG2 1 
ATOM   3354 N N   . ASP C 3 20  ? 11.695  29.021  -20.297 1.00 97.97  ? 20  ASP A N   1 
ATOM   3355 C CA  . ASP C 3 20  ? 12.382  30.295  -20.114 1.00 96.66  ? 20  ASP A CA  1 
ATOM   3356 C C   . ASP C 3 20  ? 13.750  30.087  -19.465 1.00 96.01  ? 20  ASP A C   1 
ATOM   3357 O O   . ASP C 3 20  ? 13.882  29.275  -18.548 1.00 98.79  ? 20  ASP A O   1 
ATOM   3358 C CB  . ASP C 3 20  ? 11.537  31.234  -19.250 1.00 99.25  ? 20  ASP A CB  1 
ATOM   3359 C CG  . ASP C 3 20  ? 10.468  31.977  -20.048 1.00 102.50 ? 20  ASP A CG  1 
ATOM   3360 O OD1 . ASP C 3 20  ? 10.438  31.876  -21.301 1.00 101.04 ? 20  ASP A OD1 1 
ATOM   3361 O OD2 . ASP C 3 20  ? 9.644   32.657  -19.404 1.00 100.52 ? 20  ASP A OD2 1 
ATOM   3362 N N   . PRO C 3 21  ? 14.778  30.813  -19.905 1.00 96.08  ? 21  PRO A N   1 
ATOM   3363 C CA  . PRO C 3 21  ? 16.101  30.706  -19.271 1.00 94.57  ? 21  PRO A CA  1 
ATOM   3364 C C   . PRO C 3 21  ? 16.089  31.170  -17.819 1.00 98.07  ? 21  PRO A C   1 
ATOM   3365 O O   . PRO C 3 21  ? 15.115  31.738  -17.313 1.00 98.01  ? 21  PRO A O   1 
ATOM   3366 C CB  . PRO C 3 21  ? 16.970  31.638  -20.121 1.00 97.74  ? 21  PRO A CB  1 
ATOM   3367 C CG  . PRO C 3 21  ? 15.961  32.632  -20.718 1.00 97.94  ? 21  PRO A CG  1 
ATOM   3368 C CD  . PRO C 3 21  ? 14.797  31.744  -21.047 1.00 98.40  ? 21  PRO A CD  1 
ATOM   3369 N N   . TYR C 3 22  ? 17.230  30.932  -17.152 1.00 99.32  ? 22  TYR A N   1 
ATOM   3370 C CA  . TYR C 3 22  ? 17.486  31.340  -15.769 1.00 96.64  ? 22  TYR A CA  1 
ATOM   3371 C C   . TYR C 3 22  ? 18.442  32.525  -15.820 1.00 98.68  ? 22  TYR A C   1 
ATOM   3372 O O   . TYR C 3 22  ? 19.598  32.369  -16.232 1.00 94.29  ? 22  TYR A O   1 
ATOM   3373 C CB  . TYR C 3 22  ? 18.143  30.222  -14.949 1.00 93.73  ? 22  TYR A CB  1 
ATOM   3374 C CG  . TYR C 3 22  ? 17.425  28.886  -14.833 1.00 93.64  ? 22  TYR A CG  1 
ATOM   3375 C CD1 . TYR C 3 22  ? 17.103  28.355  -13.595 1.00 91.52  ? 22  TYR A CD1 1 
ATOM   3376 C CD2 . TYR C 3 22  ? 17.103  28.139  -15.962 1.00 91.41  ? 22  TYR A CD2 1 
ATOM   3377 C CE1 . TYR C 3 22  ? 16.467  27.123  -13.503 1.00 88.88  ? 22  TYR A CE1 1 
ATOM   3378 C CE2 . TYR C 3 22  ? 16.458  26.923  -15.864 1.00 85.39  ? 22  TYR A CE2 1 
ATOM   3379 C CZ  . TYR C 3 22  ? 16.141  26.431  -14.647 1.00 81.88  ? 22  TYR A CZ  1 
ATOM   3380 O OH  . TYR C 3 22  ? 15.495  25.234  -14.566 1.00 82.25  ? 22  TYR A OH  1 
ATOM   3381 N N   . GLU C 3 23  ? 17.980  33.700  -15.393 1.00 108.66 ? 23  GLU A N   1 
ATOM   3382 C CA  . GLU C 3 23  ? 18.866  34.830  -15.124 1.00 109.65 ? 23  GLU A CA  1 
ATOM   3383 C C   . GLU C 3 23  ? 19.016  34.942  -13.614 1.00 106.01 ? 23  GLU A C   1 
ATOM   3384 O O   . GLU C 3 23  ? 18.032  35.180  -12.906 1.00 106.03 ? 23  GLU A O   1 
ATOM   3385 C CB  . GLU C 3 23  ? 18.344  36.141  -15.730 1.00 110.28 ? 23  GLU A CB  1 
ATOM   3386 C CG  . GLU C 3 23  ? 17.359  35.984  -16.891 1.00 111.44 ? 23  GLU A CG  1 
ATOM   3387 C CD  . GLU C 3 23  ? 17.985  35.384  -18.139 1.00 111.67 ? 23  GLU A CD  1 
ATOM   3388 O OE1 . GLU C 3 23  ? 19.227  35.236  -18.186 1.00 111.88 ? 23  GLU A OE1 1 
ATOM   3389 O OE2 . GLU C 3 23  ? 17.222  35.027  -19.064 1.00 112.04 ? 23  GLU A OE2 1 
ATOM   3390 N N   . PHE C 3 24  ? 20.237  34.748  -13.126 1.00 95.26  ? 24  PHE A N   1 
ATOM   3391 C CA  . PHE C 3 24  ? 20.524  34.717  -11.694 1.00 95.05  ? 24  PHE A CA  1 
ATOM   3392 C C   . PHE C 3 24  ? 21.461  35.871  -11.373 1.00 92.74  ? 24  PHE A C   1 
ATOM   3393 O O   . PHE C 3 24  ? 22.662  35.783  -11.655 1.00 92.84  ? 24  PHE A O   1 
ATOM   3394 C CB  . PHE C 3 24  ? 21.169  33.393  -11.287 1.00 92.83  ? 24  PHE A CB  1 
ATOM   3395 C CG  . PHE C 3 24  ? 20.194  32.332  -10.825 1.00 94.55  ? 24  PHE A CG  1 
ATOM   3396 C CD1 . PHE C 3 24  ? 18.936  32.199  -11.390 1.00 98.04  ? 24  PHE A CD1 1 
ATOM   3397 C CD2 . PHE C 3 24  ? 20.552  31.453  -9.820  1.00 83.98  ? 24  PHE A CD2 1 
ATOM   3398 C CE1 . PHE C 3 24  ? 18.066  31.189  -10.941 1.00 94.85  ? 24  PHE A CE1 1 
ATOM   3399 C CE2 . PHE C 3 24  ? 19.702  30.464  -9.380  1.00 82.21  ? 24  PHE A CE2 1 
ATOM   3400 C CZ  . PHE C 3 24  ? 18.457  30.336  -9.927  1.00 82.63  ? 24  PHE A CZ  1 
ATOM   3401 N N   . GLU C 3 25  ? 20.925  36.942  -10.778 1.00 96.66  ? 25  GLU A N   1 
ATOM   3402 C CA  . GLU C 3 25  ? 21.777  38.015  -10.260 1.00 98.39  ? 25  GLU A CA  1 
ATOM   3403 C C   . GLU C 3 25  ? 22.451  37.497  -8.998  1.00 97.32  ? 25  GLU A C   1 
ATOM   3404 O O   . GLU C 3 25  ? 21.793  37.265  -7.973  1.00 96.10  ? 25  GLU A O   1 
ATOM   3405 C CB  . GLU C 3 25  ? 20.986  39.290  -9.969  1.00 100.69 ? 25  GLU A CB  1 
ATOM   3406 C CG  . GLU C 3 25  ? 21.814  40.574  -10.012 1.00 103.45 ? 25  GLU A CG  1 
ATOM   3407 C CD  . GLU C 3 25  ? 21.710  41.426  -8.740  1.00 109.05 ? 25  GLU A CD  1 
ATOM   3408 O OE1 . GLU C 3 25  ? 20.800  41.174  -7.905  1.00 107.21 ? 25  GLU A OE1 1 
ATOM   3409 O OE2 . GLU C 3 25  ? 22.526  42.374  -8.598  1.00 109.03 ? 25  GLU A OE2 1 
ATOM   3410 N N   . ILE C 3 26  ? 23.759  37.296  -9.078  1.00 94.10  ? 26  ILE A N   1 
ATOM   3411 C CA  . ILE C 3 26  ? 24.510  36.591  -8.051  1.00 92.27  ? 26  ILE A CA  1 
ATOM   3412 C C   . ILE C 3 26  ? 25.477  37.585  -7.431  1.00 94.15  ? 26  ILE A C   1 
ATOM   3413 O O   . ILE C 3 26  ? 26.515  37.921  -8.018  1.00 95.55  ? 26  ILE A O   1 
ATOM   3414 C CB  . ILE C 3 26  ? 25.246  35.375  -8.616  1.00 90.50  ? 26  ILE A CB  1 
ATOM   3415 C CG1 . ILE C 3 26  ? 24.265  34.229  -8.864  1.00 88.31  ? 26  ILE A CG1 1 
ATOM   3416 C CG2 . ILE C 3 26  ? 26.391  34.984  -7.714  1.00 89.63  ? 26  ILE A CG2 1 
ATOM   3417 C CD1 . ILE C 3 26  ? 24.643  33.369  -10.015 1.00 87.59  ? 26  ILE A CD1 1 
ATOM   3418 N N   . THR C 3 27  ? 25.134  38.063  -6.244  1.00 94.33  ? 27  THR A N   1 
ATOM   3419 C CA  . THR C 3 27  ? 26.045  38.892  -5.480  1.00 95.98  ? 27  THR A CA  1 
ATOM   3420 C C   . THR C 3 27  ? 26.925  37.983  -4.624  1.00 94.13  ? 27  THR A C   1 
ATOM   3421 O O   . THR C 3 27  ? 26.424  37.104  -3.904  1.00 91.83  ? 27  THR A O   1 
ATOM   3422 C CB  . THR C 3 27  ? 25.268  39.902  -4.631  1.00 97.34  ? 27  THR A CB  1 
ATOM   3423 O OG1 . THR C 3 27  ? 24.094  40.309  -5.348  1.00 98.66  ? 27  THR A OG1 1 
ATOM   3424 C CG2 . THR C 3 27  ? 26.111  41.146  -4.369  1.00 100.26 ? 27  THR A CG2 1 
ATOM   3425 N N   . PHE C 3 28  ? 28.238  38.169  -4.740  1.00 95.26  ? 28  PHE A N   1 
ATOM   3426 C CA  . PHE C 3 28  ? 29.198  37.354  -4.013  1.00 93.90  ? 28  PHE A CA  1 
ATOM   3427 C C   . PHE C 3 28  ? 30.403  38.206  -3.653  1.00 96.33  ? 28  PHE A C   1 
ATOM   3428 O O   . PHE C 3 28  ? 30.563  39.332  -4.128  1.00 98.98  ? 28  PHE A O   1 
ATOM   3429 C CB  . PHE C 3 28  ? 29.578  36.109  -4.822  1.00 95.27  ? 28  PHE A CB  1 
ATOM   3430 C CG  . PHE C 3 28  ? 30.744  36.297  -5.773  1.00 94.60  ? 28  PHE A CG  1 
ATOM   3431 C CD1 . PHE C 3 28  ? 32.041  35.978  -5.389  1.00 93.71  ? 28  PHE A CD1 1 
ATOM   3432 C CD2 . PHE C 3 28  ? 30.533  36.752  -7.062  1.00 94.87  ? 28  PHE A CD2 1 
ATOM   3433 C CE1 . PHE C 3 28  ? 33.105  36.122  -6.269  1.00 95.21  ? 28  PHE A CE1 1 
ATOM   3434 C CE2 . PHE C 3 28  ? 31.594  36.901  -7.941  1.00 96.34  ? 28  PHE A CE2 1 
ATOM   3435 C CZ  . PHE C 3 28  ? 32.881  36.589  -7.541  1.00 96.51  ? 28  PHE A CZ  1 
ATOM   3436 N N   . GLU C 3 29  ? 31.239  37.662  -2.777  1.00 95.55  ? 29  GLU A N   1 
ATOM   3437 C CA  . GLU C 3 29  ? 32.368  38.383  -2.216  1.00 97.82  ? 29  GLU A CA  1 
ATOM   3438 C C   . GLU C 3 29  ? 33.596  37.493  -2.270  1.00 97.12  ? 29  GLU A C   1 
ATOM   3439 O O   . GLU C 3 29  ? 33.499  36.277  -2.123  1.00 94.52  ? 29  GLU A O   1 
ATOM   3440 C CB  . GLU C 3 29  ? 32.119  38.772  -0.763  1.00 98.05  ? 29  GLU A CB  1 
ATOM   3441 C CG  . GLU C 3 29  ? 31.374  37.685  -0.012  1.00 97.96  ? 29  GLU A CG  1 
ATOM   3442 C CD  . GLU C 3 29  ? 31.544  37.774  1.475   1.00 100.80 ? 29  GLU A CD  1 
ATOM   3443 O OE1 . GLU C 3 29  ? 30.520  37.812  2.191   1.00 105.29 ? 29  GLU A OE1 1 
ATOM   3444 O OE2 . GLU C 3 29  ? 32.710  37.823  1.926   1.00 104.44 ? 29  GLU A OE2 1 
ATOM   3445 N N   . CYS C 3 30  ? 34.758  38.110  -2.442  1.00 99.60  ? 30  CYS A N   1 
ATOM   3446 C CA  . CYS C 3 30  ? 36.021  37.387  -2.541  1.00 103.15 ? 30  CYS A CA  1 
ATOM   3447 C C   . CYS C 3 30  ? 37.055  38.001  -1.607  1.00 108.68 ? 30  CYS A C   1 
ATOM   3448 O O   . CYS C 3 30  ? 37.333  39.203  -1.687  1.00 105.27 ? 30  CYS A O   1 
ATOM   3449 C CB  . CYS C 3 30  ? 36.544  37.399  -3.983  1.00 105.25 ? 30  CYS A CB  1 
ATOM   3450 S SG  . CYS C 3 30  ? 38.343  37.278  -4.152  1.00 107.56 ? 30  CYS A SG  1 
ATOM   3451 N N   . LEU C 3 31  ? 37.630  37.171  -0.737  1.00 108.47 ? 31  LEU A N   1 
ATOM   3452 C CA  . LEU C 3 31  ? 38.689  37.577  0.183   1.00 109.33 ? 31  LEU A CA  1 
ATOM   3453 C C   . LEU C 3 31  ? 39.979  36.870  -0.209  1.00 111.89 ? 31  LEU A C   1 
ATOM   3454 O O   . LEU C 3 31  ? 40.001  35.638  -0.287  1.00 114.92 ? 31  LEU A O   1 
ATOM   3455 C CB  . LEU C 3 31  ? 38.329  37.232  1.631   1.00 106.37 ? 31  LEU A CB  1 
ATOM   3456 C CG  . LEU C 3 31  ? 37.007  37.748  2.214   1.00 106.43 ? 31  LEU A CG  1 
ATOM   3457 C CD1 . LEU C 3 31  ? 36.649  39.092  1.607   1.00 107.35 ? 31  LEU A CD1 1 
ATOM   3458 C CD2 . LEU C 3 31  ? 35.858  36.766  2.089   1.00 102.71 ? 31  LEU A CD2 1 
ATOM   3459 N N   . GLU C 3 32  ? 41.045  37.646  -0.451  1.00 112.53 ? 32  GLU A N   1 
ATOM   3460 C CA  . GLU C 3 32  ? 42.329  37.110  -0.906  1.00 119.75 ? 32  GLU A CA  1 
ATOM   3461 C C   . GLU C 3 32  ? 42.163  36.500  -2.303  1.00 124.22 ? 32  GLU A C   1 
ATOM   3462 O O   . GLU C 3 32  ? 41.885  35.305  -2.439  1.00 122.31 ? 32  GLU A O   1 
ATOM   3463 C CB  . GLU C 3 32  ? 42.883  36.084  0.111   1.00 116.66 ? 32  GLU A CB  1 
ATOM   3464 C CG  . GLU C 3 32  ? 44.421  36.026  0.304   1.00 119.58 ? 32  GLU A CG  1 
ATOM   3465 C CD  . GLU C 3 32  ? 45.209  35.599  -0.948  1.00 123.07 ? 32  GLU A CD  1 
ATOM   3466 O OE1 . GLU C 3 32  ? 46.416  35.923  -1.042  1.00 121.35 ? 32  GLU A OE1 1 
ATOM   3467 O OE2 . GLU C 3 32  ? 44.638  34.931  -1.836  1.00 125.84 ? 32  GLU A OE2 1 
ATOM   3468 N N   . SER C 3 33  ? 42.333  37.307  -3.351  1.00 132.46 ? 33  SER A N   1 
ATOM   3469 C CA  . SER C 3 33  ? 42.067  36.851  -4.712  1.00 134.16 ? 33  SER A CA  1 
ATOM   3470 C C   . SER C 3 33  ? 43.113  35.838  -5.179  1.00 136.05 ? 33  SER A C   1 
ATOM   3471 O O   . SER C 3 33  ? 44.263  35.840  -4.731  1.00 136.06 ? 33  SER A O   1 
ATOM   3472 C CB  . SER C 3 33  ? 42.027  38.038  -5.681  1.00 136.53 ? 33  SER A CB  1 
ATOM   3473 O OG  . SER C 3 33  ? 42.028  37.597  -7.033  1.00 136.55 ? 33  SER A OG  1 
ATOM   3474 N N   . LEU C 3 34  ? 42.696  34.963  -6.097  1.00 131.72 ? 34  LEU A N   1 
ATOM   3475 C CA  . LEU C 3 34  ? 43.572  33.950  -6.667  1.00 128.02 ? 34  LEU A CA  1 
ATOM   3476 C C   . LEU C 3 34  ? 43.169  33.761  -8.127  1.00 123.30 ? 34  LEU A C   1 
ATOM   3477 O O   . LEU C 3 34  ? 42.142  34.267  -8.580  1.00 122.61 ? 34  LEU A O   1 
ATOM   3478 C CB  . LEU C 3 34  ? 43.530  32.639  -5.846  1.00 125.31 ? 34  LEU A CB  1 
ATOM   3479 C CG  . LEU C 3 34  ? 44.791  31.762  -5.888  1.00 123.97 ? 34  LEU A CG  1 
ATOM   3480 C CD1 . LEU C 3 34  ? 45.780  32.279  -4.862  1.00 129.99 ? 34  LEU A CD1 1 
ATOM   3481 C CD2 . LEU C 3 34  ? 44.509  30.309  -5.590  1.00 123.12 ? 34  LEU A CD2 1 
ATOM   3482 N N   . LYS C 3 35  ? 44.002  33.043  -8.873  1.00 120.19 ? 35  LYS A N   1 
ATOM   3483 C CA  . LYS C 3 35  ? 43.979  33.117  -10.329 1.00 117.22 ? 35  LYS A CA  1 
ATOM   3484 C C   . LYS C 3 35  ? 43.130  32.046  -11.003 1.00 115.01 ? 35  LYS A C   1 
ATOM   3485 O O   . LYS C 3 35  ? 42.551  32.311  -12.063 1.00 114.87 ? 35  LYS A O   1 
ATOM   3486 C CB  . LYS C 3 35  ? 45.411  33.030  -10.874 1.00 120.75 ? 35  LYS A CB  1 
ATOM   3487 C CG  . LYS C 3 35  ? 46.082  31.643  -10.783 1.00 119.29 ? 35  LYS A CG  1 
ATOM   3488 C CD  . LYS C 3 35  ? 46.476  31.286  -9.343  1.00 120.41 ? 35  LYS A CD  1 
ATOM   3489 C CE  . LYS C 3 35  ? 47.711  30.400  -9.266  1.00 119.47 ? 35  LYS A CE  1 
ATOM   3490 N NZ  . LYS C 3 35  ? 48.284  30.426  -7.885  1.00 119.00 ? 35  LYS A NZ  1 
ATOM   3491 N N   . HIS C 3 36  ? 43.036  30.847  -10.427 1.00 112.64 ? 36  HIS A N   1 
ATOM   3492 C CA  . HIS C 3 36  ? 42.528  29.713  -11.190 1.00 109.25 ? 36  HIS A CA  1 
ATOM   3493 C C   . HIS C 3 36  ? 41.079  29.871  -11.642 1.00 107.11 ? 36  HIS A C   1 
ATOM   3494 O O   . HIS C 3 36  ? 40.619  29.033  -12.422 1.00 109.69 ? 36  HIS A O   1 
ATOM   3495 C CB  . HIS C 3 36  ? 42.677  28.416  -10.390 1.00 108.90 ? 36  HIS A CB  1 
ATOM   3496 C CG  . HIS C 3 36  ? 44.033  27.781  -10.506 1.00 111.99 ? 36  HIS A CG  1 
ATOM   3497 N ND1 . HIS C 3 36  ? 45.120  28.435  -11.046 1.00 113.27 ? 36  HIS A ND1 1 
ATOM   3498 C CD2 . HIS C 3 36  ? 44.462  26.533  -10.197 1.00 109.13 ? 36  HIS A CD2 1 
ATOM   3499 C CE1 . HIS C 3 36  ? 46.167  27.626  -11.035 1.00 115.33 ? 36  HIS A CE1 1 
ATOM   3500 N NE2 . HIS C 3 36  ? 45.792  26.463  -10.531 1.00 109.71 ? 36  HIS A NE2 1 
ATOM   3501 N N   . ASP C 3 37  ? 40.356  30.897  -11.173 1.00 105.23 ? 37  ASP A N   1 
ATOM   3502 C CA  . ASP C 3 37  ? 39.024  31.274  -11.661 1.00 101.53 ? 37  ASP A CA  1 
ATOM   3503 C C   . ASP C 3 37  ? 37.876  30.376  -11.173 1.00 100.87 ? 37  ASP A C   1 
ATOM   3504 O O   . ASP C 3 37  ? 38.093  29.221  -10.778 1.00 95.55  ? 37  ASP A O   1 
ATOM   3505 C CB  . ASP C 3 37  ? 39.013  31.316  -13.188 1.00 105.70 ? 37  ASP A CB  1 
ATOM   3506 C CG  . ASP C 3 37  ? 38.028  32.305  -13.718 1.00 104.93 ? 37  ASP A CG  1 
ATOM   3507 O OD1 . ASP C 3 37  ? 38.192  33.505  -13.398 1.00 105.60 ? 37  ASP A OD1 1 
ATOM   3508 O OD2 . ASP C 3 37  ? 37.085  31.873  -14.419 1.00 99.80  ? 37  ASP A OD2 1 
ATOM   3509 N N   . LEU C 3 38  ? 36.645  30.904  -11.248 1.00 99.81  ? 38  LEU A N   1 
ATOM   3510 C CA  . LEU C 3 38  ? 35.455  30.365  -10.584 1.00 94.15  ? 38  LEU A CA  1 
ATOM   3511 C C   . LEU C 3 38  ? 34.488  29.740  -11.589 1.00 93.50  ? 38  LEU A C   1 
ATOM   3512 O O   . LEU C 3 38  ? 34.099  30.395  -12.565 1.00 95.08  ? 38  LEU A O   1 
ATOM   3513 C CB  . LEU C 3 38  ? 34.737  31.481  -9.816  1.00 89.39  ? 38  LEU A CB  1 
ATOM   3514 C CG  . LEU C 3 38  ? 34.811  31.498  -8.291  1.00 89.97  ? 38  LEU A CG  1 
ATOM   3515 C CD1 . LEU C 3 38  ? 36.209  31.868  -7.842  1.00 93.20  ? 38  LEU A CD1 1 
ATOM   3516 C CD2 . LEU C 3 38  ? 33.795  32.483  -7.719  1.00 89.45  ? 38  LEU A CD2 1 
ATOM   3517 N N   . GLU C 3 39  ? 34.056  28.495  -11.321 1.00 92.60  ? 39  GLU A N   1 
ATOM   3518 C CA  . GLU C 3 39  ? 33.163  27.747  -12.211 1.00 88.00  ? 39  GLU A CA  1 
ATOM   3519 C C   . GLU C 3 39  ? 31.768  27.674  -11.591 1.00 86.17  ? 39  GLU A C   1 
ATOM   3520 O O   . GLU C 3 39  ? 31.501  26.827  -10.737 1.00 84.25  ? 39  GLU A O   1 
ATOM   3521 C CB  . GLU C 3 39  ? 33.740  26.356  -12.492 1.00 91.09  ? 39  GLU A CB  1 
ATOM   3522 C CG  . GLU C 3 39  ? 32.756  25.314  -13.067 1.00 88.62  ? 39  GLU A CG  1 
ATOM   3523 C CD  . GLU C 3 39  ? 32.410  25.570  -14.529 1.00 91.94  ? 39  GLU A CD  1 
ATOM   3524 O OE1 . GLU C 3 39  ? 31.615  26.505  -14.789 1.00 92.50  ? 39  GLU A OE1 1 
ATOM   3525 O OE2 . GLU C 3 39  ? 32.910  24.842  -15.420 1.00 93.45  ? 39  GLU A OE2 1 
ATOM   3526 N N   . TRP C 3 40  ? 30.874  28.542  -12.048 1.00 83.05  ? 40  TRP A N   1 
ATOM   3527 C CA  . TRP C 3 40  ? 29.508  28.601  -11.545 1.00 82.18  ? 40  TRP A CA  1 
ATOM   3528 C C   . TRP C 3 40  ? 28.640  27.655  -12.351 1.00 80.89  ? 40  TRP A C   1 
ATOM   3529 O O   . TRP C 3 40  ? 28.372  27.920  -13.525 1.00 82.00  ? 40  TRP A O   1 
ATOM   3530 C CB  . TRP C 3 40  ? 28.941  30.000  -11.669 1.00 84.26  ? 40  TRP A CB  1 
ATOM   3531 C CG  . TRP C 3 40  ? 29.425  30.931  -10.661 1.00 85.41  ? 40  TRP A CG  1 
ATOM   3532 C CD1 . TRP C 3 40  ? 30.593  31.632  -10.686 1.00 88.39  ? 40  TRP A CD1 1 
ATOM   3533 C CD2 . TRP C 3 40  ? 28.771  31.275  -9.442  1.00 84.98  ? 40  TRP A CD2 1 
ATOM   3534 N NE1 . TRP C 3 40  ? 30.696  32.411  -9.564  1.00 88.28  ? 40  TRP A NE1 1 
ATOM   3535 C CE2 . TRP C 3 40  ? 29.590  32.205  -8.781  1.00 86.63  ? 40  TRP A CE2 1 
ATOM   3536 C CE3 . TRP C 3 40  ? 27.570  30.888  -8.847  1.00 83.50  ? 40  TRP A CE3 1 
ATOM   3537 C CZ2 . TRP C 3 40  ? 29.246  32.754  -7.557  1.00 87.71  ? 40  TRP A CZ2 1 
ATOM   3538 C CZ3 . TRP C 3 40  ? 27.232  31.431  -7.653  1.00 83.63  ? 40  TRP A CZ3 1 
ATOM   3539 C CH2 . TRP C 3 40  ? 28.071  32.340  -7.003  1.00 88.38  ? 40  TRP A CH2 1 
ATOM   3540 N N   . LYS C 3 41  ? 28.135  26.602  -11.713 1.00 78.75  ? 41  LYS A N   1 
ATOM   3541 C CA  . LYS C 3 41  ? 27.388  25.561  -12.397 1.00 77.51  ? 41  LYS A CA  1 
ATOM   3542 C C   . LYS C 3 41  ? 25.969  25.474  -11.861 1.00 76.74  ? 41  LYS A C   1 
ATOM   3543 O O   . LYS C 3 41  ? 25.769  25.479  -10.651 1.00 75.93  ? 41  LYS A O   1 
ATOM   3544 C CB  . LYS C 3 41  ? 28.128  24.243  -12.221 1.00 75.82  ? 41  LYS A CB  1 
ATOM   3545 C CG  . LYS C 3 41  ? 27.411  22.990  -12.661 1.00 74.32  ? 41  LYS A CG  1 
ATOM   3546 C CD  . LYS C 3 41  ? 28.368  21.804  -12.544 1.00 73.03  ? 41  LYS A CD  1 
ATOM   3547 C CE  . LYS C 3 41  ? 29.847  22.245  -12.546 1.00 74.03  ? 41  LYS A CE  1 
ATOM   3548 N NZ  . LYS C 3 41  ? 30.792  21.167  -12.101 1.00 72.83  ? 41  LYS A NZ  1 
ATOM   3549 N N   . LEU C 3 42  ? 24.985  25.378  -12.746 1.00 77.10  ? 42  LEU A N   1 
ATOM   3550 C CA  . LEU C 3 42  ? 23.595  25.180  -12.340 1.00 76.48  ? 42  LEU A CA  1 
ATOM   3551 C C   . LEU C 3 42  ? 23.098  23.799  -12.776 1.00 75.12  ? 42  LEU A C   1 
ATOM   3552 O O   . LEU C 3 42  ? 23.131  23.457  -13.966 1.00 75.53  ? 42  LEU A O   1 
ATOM   3553 C CB  . LEU C 3 42  ? 22.706  26.296  -12.883 1.00 78.40  ? 42  LEU A CB  1 
ATOM   3554 C CG  . LEU C 3 42  ? 21.195  26.141  -12.720 1.00 78.22  ? 42  LEU A CG  1 
ATOM   3555 C CD1 . LEU C 3 42  ? 20.641  27.371  -12.075 1.00 79.49  ? 42  LEU A CD1 1 
ATOM   3556 C CD2 . LEU C 3 42  ? 20.560  26.047  -14.072 1.00 79.30  ? 42  LEU A CD2 1 
ATOM   3557 N N   . THR C 3 43  ? 22.616  23.014  -11.808 1.00 73.43  ? 43  THR A N   1 
ATOM   3558 C CA  . THR C 3 43  ? 22.354  21.592  -11.999 1.00 71.96  ? 43  THR A CA  1 
ATOM   3559 C C   . THR C 3 43  ? 20.894  21.293  -11.698 1.00 71.66  ? 43  THR A C   1 
ATOM   3560 O O   . THR C 3 43  ? 20.425  21.576  -10.594 1.00 72.49  ? 43  THR A O   1 
ATOM   3561 C CB  . THR C 3 43  ? 23.242  20.768  -11.071 1.00 70.35  ? 43  THR A CB  1 
ATOM   3562 O OG1 . THR C 3 43  ? 24.374  21.552  -10.678 1.00 71.88  ? 43  THR A OG1 1 
ATOM   3563 C CG2 . THR C 3 43  ? 23.728  19.535  -11.772 1.00 71.75  ? 43  THR A CG2 1 
ATOM   3564 N N   . TYR C 3 44  ? 20.186  20.696  -12.652 1.00 71.91  ? 44  TYR A N   1 
ATOM   3565 C CA  . TYR C 3 44  ? 18.810  20.269  -12.417 1.00 71.74  ? 44  TYR A CA  1 
ATOM   3566 C C   . TYR C 3 44  ? 18.817  18.943  -11.665 1.00 69.89  ? 44  TYR A C   1 
ATOM   3567 O O   . TYR C 3 44  ? 19.560  18.029  -12.029 1.00 72.24  ? 44  TYR A O   1 
ATOM   3568 C CB  . TYR C 3 44  ? 18.067  20.138  -13.751 1.00 72.99  ? 44  TYR A CB  1 
ATOM   3569 C CG  . TYR C 3 44  ? 16.643  19.606  -13.697 1.00 73.13  ? 44  TYR A CG  1 
ATOM   3570 C CD1 . TYR C 3 44  ? 16.399  18.244  -13.569 1.00 71.93  ? 44  TYR A CD1 1 
ATOM   3571 C CD2 . TYR C 3 44  ? 15.546  20.453  -13.828 1.00 74.68  ? 44  TYR A CD2 1 
ATOM   3572 C CE1 . TYR C 3 44  ? 15.117  17.737  -13.535 1.00 72.26  ? 44  TYR A CE1 1 
ATOM   3573 C CE2 . TYR C 3 44  ? 14.245  19.950  -13.796 1.00 75.01  ? 44  TYR A CE2 1 
ATOM   3574 C CZ  . TYR C 3 44  ? 14.045  18.582  -13.648 1.00 73.80  ? 44  TYR A CZ  1 
ATOM   3575 O OH  . TYR C 3 44  ? 12.783  18.029  -13.612 1.00 74.27  ? 44  TYR A OH  1 
ATOM   3576 N N   . VAL C 3 45  ? 18.000  18.830  -10.616 1.00 69.34  ? 45  VAL A N   1 
ATOM   3577 C CA  . VAL C 3 45  ? 17.902  17.599  -9.836  1.00 67.76  ? 45  VAL A CA  1 
ATOM   3578 C C   . VAL C 3 45  ? 16.449  17.164  -9.780  1.00 68.05  ? 45  VAL A C   1 
ATOM   3579 O O   . VAL C 3 45  ? 15.602  17.891  -9.251  1.00 68.71  ? 45  VAL A O   1 
ATOM   3580 C CB  . VAL C 3 45  ? 18.451  17.753  -8.413  1.00 66.72  ? 45  VAL A CB  1 
ATOM   3581 C CG1 . VAL C 3 45  ? 18.634  16.397  -7.800  1.00 68.71  ? 45  VAL A CG1 1 
ATOM   3582 C CG2 . VAL C 3 45  ? 19.760  18.475  -8.434  1.00 68.83  ? 45  VAL A CG2 1 
ATOM   3583 N N   . GLY C 3 46  ? 16.170  15.961  -10.285 1.00 69.31  ? 46  GLY A N   1 
ATOM   3584 C CA  . GLY C 3 46  ? 14.820  15.443  -10.331 1.00 68.14  ? 46  GLY A CA  1 
ATOM   3585 C C   . GLY C 3 46  ? 14.611  14.205  -9.487  1.00 66.86  ? 46  GLY A C   1 
ATOM   3586 O O   . GLY C 3 46  ? 15.552  13.472  -9.165  1.00 65.59  ? 46  GLY A O   1 
ATOM   3587 N N   . SER C 3 47  ? 13.361  13.975  -9.111  1.00 67.33  ? 47  SER A N   1 
ATOM   3588 C CA  . SER C 3 47  ? 12.979  12.765  -8.408  1.00 66.46  ? 47  SER A CA  1 
ATOM   3589 C C   . SER C 3 47  ? 11.630  12.343  -8.953  1.00 67.76  ? 47  SER A C   1 
ATOM   3590 O O   . SER C 3 47  ? 10.662  13.110  -8.907  1.00 68.97  ? 47  SER A O   1 
ATOM   3591 C CB  . SER C 3 47  ? 12.934  12.972  -6.894  1.00 65.58  ? 47  SER A CB  1 
ATOM   3592 O OG  . SER C 3 47  ? 14.252  12.966  -6.361  1.00 64.31  ? 47  SER A OG  1 
ATOM   3593 N N   . SER C 3 48  ? 11.595  11.132  -9.496  1.00 67.67  ? 48  SER A N   1 
ATOM   3594 C CA  . SER C 3 48  ? 10.431  10.568  -10.150 1.00 71.65  ? 48  SER A CA  1 
ATOM   3595 C C   . SER C 3 48  ? 10.397  9.077   -9.844  1.00 73.71  ? 48  SER A C   1 
ATOM   3596 O O   . SER C 3 48  ? 11.396  8.498   -9.411  1.00 70.63  ? 48  SER A O   1 
ATOM   3597 C CB  . SER C 3 48  ? 10.468  10.813  -11.668 1.00 70.37  ? 48  SER A CB  1 
ATOM   3598 O OG  . SER C 3 48  ? 9.183   10.635  -12.233 1.00 72.60  ? 48  SER A OG  1 
ATOM   3599 N N   . ARG C 3 49  ? 9.242   8.464   -10.124 1.00 85.46  ? 49  ARG A N   1 
ATOM   3600 C CA  . ARG C 3 49  ? 8.879   7.101   -9.740  1.00 86.51  ? 49  ARG A CA  1 
ATOM   3601 C C   . ARG C 3 49  ? 10.025  6.193   -9.297  1.00 82.77  ? 49  ARG A C   1 
ATOM   3602 O O   . ARG C 3 49  ? 10.119  5.812   -8.123  1.00 82.33  ? 49  ARG A O   1 
ATOM   3603 C CB  . ARG C 3 49  ? 8.143   6.430   -10.896 1.00 89.73  ? 49  ARG A CB  1 
ATOM   3604 C CG  . ARG C 3 49  ? 7.845   4.946   -10.651 1.00 93.05  ? 49  ARG A CG  1 
ATOM   3605 C CD  . ARG C 3 49  ? 6.547   4.725   -9.865  1.00 102.81 ? 49  ARG A CD  1 
ATOM   3606 N NE  . ARG C 3 49  ? 5.556   5.769   -10.114 1.00 112.92 ? 49  ARG A NE  1 
ATOM   3607 C CZ  . ARG C 3 49  ? 4.617   6.145   -9.254  1.00 115.94 ? 49  ARG A CZ  1 
ATOM   3608 N NH1 . ARG C 3 49  ? 4.530   5.609   -8.044  1.00 111.42 ? 49  ARG A NH1 1 
ATOM   3609 N NH2 . ARG C 3 49  ? 3.733   7.071   -9.623  1.00 117.84 ? 49  ARG A NH2 1 
ATOM   3610 N N   . SER C 3 50  ? 10.889  5.821   -10.224 1.00 76.23  ? 50  SER A N   1 
ATOM   3611 C CA  . SER C 3 50  ? 11.951  4.869   -9.934  1.00 68.20  ? 50  SER A CA  1 
ATOM   3612 C C   . SER C 3 50  ? 13.310  5.447   -10.286 1.00 65.24  ? 50  SER A C   1 
ATOM   3613 O O   . SER C 3 50  ? 14.235  4.705   -10.635 1.00 64.63  ? 50  SER A O   1 
ATOM   3614 C CB  . SER C 3 50  ? 11.724  3.558   -10.682 1.00 66.90  ? 50  SER A CB  1 
ATOM   3615 O OG  . SER C 3 50  ? 10.355  3.219   -10.722 1.00 68.37  ? 50  SER A OG  1 
ATOM   3616 N N   . LEU C 3 51  ? 13.442  6.770   -10.221 1.00 65.29  ? 51  LEU A N   1 
ATOM   3617 C CA  . LEU C 3 51  ? 14.672  7.363   -10.700 1.00 64.78  ? 51  LEU A CA  1 
ATOM   3618 C C   . LEU C 3 51  ? 14.984  8.618   -9.904  1.00 64.32  ? 51  LEU A C   1 
ATOM   3619 O O   . LEU C 3 51  ? 14.087  9.298   -9.397  1.00 64.85  ? 51  LEU A O   1 
ATOM   3620 C CB  . LEU C 3 51  ? 14.578  7.649   -12.200 1.00 66.08  ? 51  LEU A CB  1 
ATOM   3621 C CG  . LEU C 3 51  ? 15.909  8.102   -12.773 1.00 65.67  ? 51  LEU A CG  1 
ATOM   3622 C CD1 . LEU C 3 51  ? 16.939  7.027   -12.476 1.00 64.43  ? 51  LEU A CD1 1 
ATOM   3623 C CD2 . LEU C 3 51  ? 15.817  8.379   -14.278 1.00 67.06  ? 51  LEU A CD2 1 
ATOM   3624 N N   . ASP C 3 52  ? 16.278  8.881   -9.754  1.00 63.44  ? 52  ASP A N   1 
ATOM   3625 C CA  . ASP C 3 52  ? 16.771  10.112  -9.148  1.00 63.20  ? 52  ASP A CA  1 
ATOM   3626 C C   . ASP C 3 52  ? 17.817  10.663  -10.097 1.00 66.76  ? 52  ASP A C   1 
ATOM   3627 O O   . ASP C 3 52  ? 18.984  10.258  -10.061 1.00 64.51  ? 52  ASP A O   1 
ATOM   3628 C CB  . ASP C 3 52  ? 17.331  9.895   -7.753  1.00 61.92  ? 52  ASP A CB  1 
ATOM   3629 C CG  . ASP C 3 52  ? 16.256  9.896   -6.717  1.00 61.89  ? 52  ASP A CG  1 
ATOM   3630 O OD1 . ASP C 3 52  ? 15.139  10.356  -7.008  1.00 62.92  ? 52  ASP A OD1 1 
ATOM   3631 O OD2 . ASP C 3 52  ? 16.530  9.465   -5.591  1.00 60.94  ? 52  ASP A OD2 1 
ATOM   3632 N N   . HIS C 3 53  ? 17.364  11.575  -10.946 1.00 83.86  ? 53  HIS A N   1 
ATOM   3633 C CA  . HIS C 3 53  ? 18.126  12.083  -12.068 1.00 84.56  ? 53  HIS A CA  1 
ATOM   3634 C C   . HIS C 3 53  ? 18.794  13.378  -11.650 1.00 85.61  ? 53  HIS A C   1 
ATOM   3635 O O   . HIS C 3 53  ? 18.137  14.266  -11.093 1.00 85.44  ? 53  HIS A O   1 
ATOM   3636 C CB  . HIS C 3 53  ? 17.213  12.356  -13.253 1.00 86.13  ? 53  HIS A CB  1 
ATOM   3637 C CG  . HIS C 3 53  ? 17.953  12.792  -14.474 1.00 89.80  ? 53  HIS A CG  1 
ATOM   3638 N ND1 . HIS C 3 53  ? 17.321  13.225  -15.621 1.00 94.78  ? 53  HIS A ND1 1 
ATOM   3639 C CD2 . HIS C 3 53  ? 19.280  12.800  -14.753 1.00 91.92  ? 53  HIS A CD2 1 
ATOM   3640 C CE1 . HIS C 3 53  ? 18.227  13.494  -16.548 1.00 90.14  ? 53  HIS A CE1 1 
ATOM   3641 N NE2 . HIS C 3 53  ? 19.424  13.238  -16.048 1.00 92.12  ? 53  HIS A NE2 1 
ATOM   3642 N N   . ASP C 3 54  ? 20.089  13.488  -11.913 1.00 78.68  ? 54  ASP A N   1 
ATOM   3643 C CA  . ASP C 3 54  ? 20.745  14.781  -11.844 1.00 76.82  ? 54  ASP A CA  1 
ATOM   3644 C C   . ASP C 3 54  ? 21.455  15.031  -13.171 1.00 79.72  ? 54  ASP A C   1 
ATOM   3645 O O   . ASP C 3 54  ? 22.190  14.167  -13.677 1.00 79.58  ? 54  ASP A O   1 
ATOM   3646 C CB  . ASP C 3 54  ? 21.654  14.890  -10.605 1.00 68.96  ? 54  ASP A CB  1 
ATOM   3647 C CG  . ASP C 3 54  ? 23.128  14.810  -10.913 1.00 73.77  ? 54  ASP A CG  1 
ATOM   3648 O OD1 . ASP C 3 54  ? 23.667  15.709  -11.598 1.00 76.88  ? 54  ASP A OD1 1 
ATOM   3649 O OD2 . ASP C 3 54  ? 23.774  13.881  -10.390 1.00 74.82  ? 54  ASP A OD2 1 
ATOM   3650 N N   . GLN C 3 55  ? 21.164  16.187  -13.759 1.00 73.56  ? 55  GLN A N   1 
ATOM   3651 C CA  . GLN C 3 55  ? 21.776  16.645  -14.989 1.00 72.89  ? 55  GLN A CA  1 
ATOM   3652 C C   . GLN C 3 55  ? 22.166  18.108  -14.889 1.00 72.87  ? 55  GLN A C   1 
ATOM   3653 O O   . GLN C 3 55  ? 21.404  18.942  -14.392 1.00 74.15  ? 55  GLN A O   1 
ATOM   3654 C CB  . GLN C 3 55  ? 20.840  16.485  -16.174 1.00 81.47  ? 55  GLN A CB  1 
ATOM   3655 C CG  . GLN C 3 55  ? 19.428  17.052  -15.982 1.00 79.97  ? 55  GLN A CG  1 
ATOM   3656 C CD  . GLN C 3 55  ? 18.647  17.114  -17.313 1.00 85.22  ? 55  GLN A CD  1 
ATOM   3657 O OE1 . GLN C 3 55  ? 17.761  16.290  -17.556 1.00 88.26  ? 55  GLN A OE1 1 
ATOM   3658 N NE2 . GLN C 3 55  ? 18.948  18.115  -18.155 1.00 79.49  ? 55  GLN A NE2 1 
ATOM   3659 N N   . GLU C 3 56  ? 23.332  18.418  -15.425 1.00 73.05  ? 56  GLU A N   1 
ATOM   3660 C CA  . GLU C 3 56  ? 23.815  19.783  -15.465 1.00 72.51  ? 56  GLU A CA  1 
ATOM   3661 C C   . GLU C 3 56  ? 22.993  20.588  -16.469 1.00 74.30  ? 56  GLU A C   1 
ATOM   3662 O O   . GLU C 3 56  ? 22.603  20.067  -17.512 1.00 74.74  ? 56  GLU A O   1 
ATOM   3663 C CB  . GLU C 3 56  ? 25.304  19.744  -15.795 1.00 72.65  ? 56  GLU A CB  1 
ATOM   3664 C CG  . GLU C 3 56  ? 26.023  21.059  -15.906 1.00 74.20  ? 56  GLU A CG  1 
ATOM   3665 C CD  . GLU C 3 56  ? 27.524  20.862  -15.733 1.00 75.55  ? 56  GLU A CD  1 
ATOM   3666 O OE1 . GLU C 3 56  ? 27.883  19.994  -14.887 1.00 78.33  ? 56  GLU A OE1 1 
ATOM   3667 O OE2 . GLU C 3 56  ? 28.327  21.552  -16.414 1.00 75.47  ? 56  GLU A OE2 1 
ATOM   3668 N N   . LEU C 3 57  ? 22.658  21.840  -16.116 1.00 75.44  ? 57  LEU A N   1 
ATOM   3669 C CA  . LEU C 3 57  ? 21.873  22.706  -17.005 1.00 77.37  ? 57  LEU A CA  1 
ATOM   3670 C C   . LEU C 3 57  ? 22.719  23.716  -17.778 1.00 79.14  ? 57  LEU A C   1 
ATOM   3671 O O   . LEU C 3 57  ? 22.521  23.875  -18.989 1.00 80.76  ? 57  LEU A O   1 
ATOM   3672 C CB  . LEU C 3 57  ? 20.766  23.447  -16.234 1.00 77.82  ? 57  LEU A CB  1 
ATOM   3673 C CG  . LEU C 3 57  ? 19.373  22.804  -16.188 1.00 77.45  ? 57  LEU A CG  1 
ATOM   3674 C CD1 . LEU C 3 57  ? 18.475  23.335  -15.104 1.00 77.43  ? 57  LEU A CD1 1 
ATOM   3675 C CD2 . LEU C 3 57  ? 18.714  23.000  -17.530 1.00 79.20  ? 57  LEU A CD2 1 
ATOM   3676 N N   . ASP C 3 58  ? 23.649  24.404  -17.116 1.00 79.31  ? 58  ASP A N   1 
ATOM   3677 C CA  . ASP C 3 58  ? 24.501  25.385  -17.780 1.00 81.16  ? 58  ASP A CA  1 
ATOM   3678 C C   . ASP C 3 58  ? 25.720  25.613  -16.898 1.00 80.73  ? 58  ASP A C   1 
ATOM   3679 O O   . ASP C 3 58  ? 25.782  25.145  -15.764 1.00 79.16  ? 58  ASP A O   1 
ATOM   3680 C CB  . ASP C 3 58  ? 23.737  26.693  -18.047 1.00 83.25  ? 58  ASP A CB  1 
ATOM   3681 C CG  . ASP C 3 58  ? 24.270  27.452  -19.233 1.00 85.44  ? 58  ASP A CG  1 
ATOM   3682 O OD1 . ASP C 3 58  ? 25.486  27.378  -19.496 1.00 85.59  ? 58  ASP A OD1 1 
ATOM   3683 O OD2 . ASP C 3 58  ? 23.459  28.103  -19.918 1.00 87.13  ? 58  ASP A OD2 1 
ATOM   3684 N N   . SER C 3 59  ? 26.696  26.339  -17.427 1.00 82.31  ? 59  SER A N   1 
ATOM   3685 C CA  . SER C 3 59  ? 27.919  26.581  -16.678 1.00 82.26  ? 59  SER A CA  1 
ATOM   3686 C C   . SER C 3 59  ? 28.591  27.826  -17.222 1.00 84.74  ? 59  SER A C   1 
ATOM   3687 O O   . SER C 3 59  ? 28.838  27.916  -18.426 1.00 85.97  ? 59  SER A O   1 
ATOM   3688 C CB  . SER C 3 59  ? 28.864  25.387  -16.762 1.00 80.86  ? 59  SER A CB  1 
ATOM   3689 O OG  . SER C 3 59  ? 30.212  25.817  -16.704 1.00 84.15  ? 59  SER A OG  1 
ATOM   3690 N N   . ILE C 3 60  ? 28.884  28.774  -16.330 1.00 85.59  ? 60  ILE A N   1 
ATOM   3691 C CA  . ILE C 3 60  ? 29.479  30.059  -16.678 1.00 88.16  ? 60  ILE A CA  1 
ATOM   3692 C C   . ILE C 3 60  ? 30.819  30.160  -15.963 1.00 88.34  ? 60  ILE A C   1 
ATOM   3693 O O   . ILE C 3 60  ? 30.988  29.635  -14.858 1.00 88.52  ? 60  ILE A O   1 
ATOM   3694 C CB  . ILE C 3 60  ? 28.575  31.245  -16.280 1.00 89.53  ? 60  ILE A CB  1 
ATOM   3695 C CG1 . ILE C 3 60  ? 29.133  32.567  -16.808 1.00 92.48  ? 60  ILE A CG1 1 
ATOM   3696 C CG2 . ILE C 3 60  ? 28.531  31.406  -14.775 1.00 88.62  ? 60  ILE A CG2 1 
ATOM   3697 C CD1 . ILE C 3 60  ? 28.052  33.517  -17.289 1.00 94.23  ? 60  ILE A CD1 1 
ATOM   3698 N N   . LEU C 3 61  ? 31.773  30.824  -16.592 1.00 90.44  ? 61  LEU A N   1 
ATOM   3699 C CA  . LEU C 3 61  ? 33.053  31.100  -15.967 1.00 91.20  ? 61  LEU A CA  1 
ATOM   3700 C C   . LEU C 3 61  ? 33.193  32.606  -15.828 1.00 93.90  ? 61  LEU A C   1 
ATOM   3701 O O   . LEU C 3 61  ? 33.047  33.338  -16.814 1.00 95.90  ? 61  LEU A O   1 
ATOM   3702 C CB  . LEU C 3 61  ? 34.200  30.513  -16.787 1.00 91.52  ? 61  LEU A CB  1 
ATOM   3703 C CG  . LEU C 3 61  ? 35.326  29.893  -15.971 1.00 90.68  ? 61  LEU A CG  1 
ATOM   3704 C CD1 . LEU C 3 61  ? 34.874  28.564  -15.375 1.00 92.30  ? 61  LEU A CD1 1 
ATOM   3705 C CD2 . LEU C 3 61  ? 36.563  29.707  -16.829 1.00 91.93  ? 61  LEU A CD2 1 
ATOM   3706 N N   . VAL C 3 62  ? 33.454  33.070  -14.607 1.00 94.08  ? 62  VAL A N   1 
ATOM   3707 C CA  . VAL C 3 62  ? 33.619  34.492  -14.327 1.00 96.72  ? 62  VAL A CA  1 
ATOM   3708 C C   . VAL C 3 62  ? 35.104  34.794  -14.142 1.00 98.36  ? 62  VAL A C   1 
ATOM   3709 O O   . VAL C 3 62  ? 35.753  34.246  -13.243 1.00 99.34  ? 62  VAL A O   1 
ATOM   3710 C CB  . VAL C 3 62  ? 32.770  34.929  -13.126 1.00 96.18  ? 62  VAL A CB  1 
ATOM   3711 C CG1 . VAL C 3 62  ? 31.335  34.579  -13.386 1.00 94.74  ? 62  VAL A CG1 1 
ATOM   3712 C CG2 . VAL C 3 62  ? 33.212  34.233  -11.846 1.00 95.61  ? 62  VAL A CG2 1 
ATOM   3713 N N   . GLY C 3 63  ? 35.638  35.663  -15.012 1.00 101.12 ? 63  GLY A N   1 
ATOM   3714 C CA  . GLY C 3 63  ? 37.055  35.943  -15.078 1.00 104.25 ? 63  GLY A CA  1 
ATOM   3715 C C   . GLY C 3 63  ? 37.356  37.317  -15.650 1.00 108.31 ? 63  GLY A C   1 
ATOM   3716 O O   . GLY C 3 63  ? 36.774  37.736  -16.657 1.00 107.64 ? 63  GLY A O   1 
ATOM   3717 N N   . PRO C 3 64  ? 38.271  38.061  -14.998 1.00 112.36 ? 64  PRO A N   1 
ATOM   3718 C CA  . PRO C 3 64  ? 39.062  37.690  -13.818 1.00 112.12 ? 64  PRO A CA  1 
ATOM   3719 C C   . PRO C 3 64  ? 38.279  37.836  -12.513 1.00 111.64 ? 64  PRO A C   1 
ATOM   3720 O O   . PRO C 3 64  ? 37.199  38.419  -12.487 1.00 112.19 ? 64  PRO A O   1 
ATOM   3721 C CB  . PRO C 3 64  ? 40.241  38.673  -13.893 1.00 115.30 ? 64  PRO A CB  1 
ATOM   3722 C CG  . PRO C 3 64  ? 39.721  39.878  -14.732 1.00 117.91 ? 64  PRO A CG  1 
ATOM   3723 C CD  . PRO C 3 64  ? 38.312  39.522  -15.169 1.00 115.78 ? 64  PRO A CD  1 
ATOM   3724 N N   . VAL C 3 65  ? 38.777  37.321  -11.396 1.00 115.03 ? 65  VAL A N   1 
ATOM   3725 C CA  . VAL C 3 65  ? 38.060  37.376  -10.128 1.00 115.08 ? 65  VAL A CA  1 
ATOM   3726 C C   . VAL C 3 65  ? 38.642  38.516  -9.284  1.00 118.30 ? 65  VAL A C   1 
ATOM   3727 O O   . VAL C 3 65  ? 39.834  38.475  -8.948  1.00 115.50 ? 65  VAL A O   1 
ATOM   3728 C CB  . VAL C 3 65  ? 38.102  36.034  -9.384  1.00 115.14 ? 65  VAL A CB  1 
ATOM   3729 C CG1 . VAL C 3 65  ? 39.520  35.605  -9.093  1.00 116.66 ? 65  VAL A CG1 1 
ATOM   3730 C CG2 . VAL C 3 65  ? 37.285  36.127  -8.103  1.00 110.98 ? 65  VAL A CG2 1 
ATOM   3731 N N   . PRO C 3 66  ? 37.863  39.551  -8.986  1.00 121.14 ? 66  PRO A N   1 
ATOM   3732 C CA  . PRO C 3 66  ? 38.365  40.634  -8.128  1.00 119.52 ? 66  PRO A CA  1 
ATOM   3733 C C   . PRO C 3 66  ? 38.005  40.448  -6.660  1.00 117.60 ? 66  PRO A C   1 
ATOM   3734 O O   . PRO C 3 66  ? 37.159  39.616  -6.305  1.00 114.60 ? 66  PRO A O   1 
ATOM   3735 C CB  . PRO C 3 66  ? 37.698  41.890  -8.720  1.00 121.41 ? 66  PRO A CB  1 
ATOM   3736 C CG  . PRO C 3 66  ? 36.882  41.406  -9.938  1.00 122.49 ? 66  PRO A CG  1 
ATOM   3737 C CD  . PRO C 3 66  ? 36.646  39.949  -9.706  1.00 122.14 ? 66  PRO A CD  1 
ATOM   3738 N N   . VAL C 3 67  ? 38.674  41.226  -5.800  1.00 115.29 ? 67  VAL A N   1 
ATOM   3739 C CA  . VAL C 3 67  ? 38.357  41.258  -4.374  1.00 111.58 ? 67  VAL A CA  1 
ATOM   3740 C C   . VAL C 3 67  ? 37.156  42.172  -4.144  1.00 111.83 ? 67  VAL A C   1 
ATOM   3741 O O   . VAL C 3 67  ? 36.819  43.017  -4.980  1.00 113.70 ? 67  VAL A O   1 
ATOM   3742 C CB  . VAL C 3 67  ? 39.579  41.707  -3.544  1.00 113.70 ? 67  VAL A CB  1 
ATOM   3743 C CG1 . VAL C 3 67  ? 39.411  41.357  -2.083  1.00 112.35 ? 67  VAL A CG1 1 
ATOM   3744 C CG2 . VAL C 3 67  ? 40.847  41.065  -4.067  1.00 114.09 ? 67  VAL A CG2 1 
ATOM   3745 N N   . GLY C 3 68  ? 36.491  41.984  -3.011  1.00 110.29 ? 68  GLY A N   1 
ATOM   3746 C CA  . GLY C 3 68  ? 35.335  42.784  -2.660  1.00 110.75 ? 68  GLY A CA  1 
ATOM   3747 C C   . GLY C 3 68  ? 34.029  42.116  -3.029  1.00 107.88 ? 68  GLY A C   1 
ATOM   3748 O O   . GLY C 3 68  ? 33.946  40.899  -3.180  1.00 105.06 ? 68  GLY A O   1 
ATOM   3749 N N   . VAL C 3 69  ? 32.989  42.935  -3.175  1.00 108.81 ? 69  VAL A N   1 
ATOM   3750 C CA  . VAL C 3 69  ? 31.672  42.465  -3.605  1.00 106.65 ? 69  VAL A CA  1 
ATOM   3751 C C   . VAL C 3 69  ? 31.550  42.616  -5.122  1.00 107.47 ? 69  VAL A C   1 
ATOM   3752 O O   . VAL C 3 69  ? 31.590  43.733  -5.656  1.00 110.36 ? 69  VAL A O   1 
ATOM   3753 C CB  . VAL C 3 69  ? 30.543  43.219  -2.885  1.00 107.20 ? 69  VAL A CB  1 
ATOM   3754 C CG1 . VAL C 3 69  ? 30.926  44.659  -2.695  1.00 110.88 ? 69  VAL A CG1 1 
ATOM   3755 C CG2 . VAL C 3 69  ? 29.221  43.110  -3.653  1.00 106.22 ? 69  VAL A CG2 1 
ATOM   3756 N N   . ASN C 3 70  ? 31.404  41.487  -5.819  1.00 105.06 ? 70  ASN A N   1 
ATOM   3757 C CA  . ASN C 3 70  ? 31.142  41.458  -7.249  1.00 105.44 ? 70  ASN A CA  1 
ATOM   3758 C C   . ASN C 3 70  ? 29.712  40.991  -7.461  1.00 103.48 ? 70  ASN A C   1 
ATOM   3759 O O   . ASN C 3 70  ? 29.283  40.017  -6.840  1.00 102.99 ? 70  ASN A O   1 
ATOM   3760 C CB  . ASN C 3 70  ? 32.122  40.526  -7.959  1.00 104.46 ? 70  ASN A CB  1 
ATOM   3761 C CG  . ASN C 3 70  ? 33.462  40.457  -7.259  1.00 105.13 ? 70  ASN A CG  1 
ATOM   3762 O OD1 . ASN C 3 70  ? 33.616  39.785  -6.239  1.00 103.34 ? 70  ASN A OD1 1 
ATOM   3763 N ND2 . ASN C 3 70  ? 34.436  41.177  -7.794  1.00 109.00 ? 70  ASN A ND2 1 
ATOM   3764 N N   . LYS C 3 71  ? 28.964  41.706  -8.292  1.00 105.05 ? 71  LYS A N   1 
ATOM   3765 C CA  . LYS C 3 71  ? 27.648  41.275  -8.746  1.00 103.60 ? 71  LYS A CA  1 
ATOM   3766 C C   . LYS C 3 71  ? 27.718  41.019  -10.252 1.00 104.00 ? 71  LYS A C   1 
ATOM   3767 O O   . LYS C 3 71  ? 27.972  41.945  -11.040 1.00 106.71 ? 71  LYS A O   1 
ATOM   3768 C CB  . LYS C 3 71  ? 26.566  42.304  -8.410  1.00 105.18 ? 71  LYS A CB  1 
ATOM   3769 N N   . PHE C 3 72  ? 27.516  39.753  -10.636 1.00 102.82 ? 72  PHE A N   1 
ATOM   3770 C CA  . PHE C 3 72  ? 27.474  39.299  -12.019 1.00 101.35 ? 72  PHE A CA  1 
ATOM   3771 C C   . PHE C 3 72  ? 26.176  38.542  -12.242 1.00 99.43  ? 72  PHE A C   1 
ATOM   3772 O O   . PHE C 3 72  ? 25.692  37.839  -11.350 1.00 97.21  ? 72  PHE A O   1 
ATOM   3773 C CB  . PHE C 3 72  ? 28.672  38.403  -12.349 1.00 100.24 ? 72  PHE A CB  1 
ATOM   3774 C CG  . PHE C 3 72  ? 28.408  36.924  -12.183 1.00 96.98  ? 72  PHE A CG  1 
ATOM   3775 C CD1 . PHE C 3 72  ? 28.410  36.339  -10.923 1.00 94.98  ? 72  PHE A CD1 1 
ATOM   3776 C CD2 . PHE C 3 72  ? 28.207  36.103  -13.293 1.00 96.04  ? 72  PHE A CD2 1 
ATOM   3777 C CE1 . PHE C 3 72  ? 28.197  34.973  -10.774 1.00 92.15  ? 72  PHE A CE1 1 
ATOM   3778 C CE2 . PHE C 3 72  ? 27.992  34.736  -13.146 1.00 93.22  ? 72  PHE A CE2 1 
ATOM   3779 C CZ  . PHE C 3 72  ? 27.992  34.171  -11.889 1.00 91.29  ? 72  PHE A CZ  1 
ATOM   3780 N N   . VAL C 3 73  ? 25.598  38.682  -13.429 1.00 100.47 ? 73  VAL A N   1 
ATOM   3781 C CA  . VAL C 3 73  ? 24.361  37.907  -13.730 1.00 99.03  ? 73  VAL A CA  1 
ATOM   3782 C C   . VAL C 3 73  ? 24.736  36.652  -14.533 1.00 97.26  ? 73  VAL A C   1 
ATOM   3783 O O   . VAL C 3 73  ? 25.403  36.801  -15.571 1.00 98.46  ? 73  VAL A O   1 
ATOM   3784 C CB  . VAL C 3 73  ? 23.291  38.737  -14.458 1.00 101.35 ? 73  VAL A CB  1 
ATOM   3785 C CG1 . VAL C 3 73  ? 22.112  37.877  -14.899 1.00 100.29 ? 73  VAL A CG1 1 
ATOM   3786 C CG2 . VAL C 3 73  ? 22.811  39.900  -13.602 1.00 102.27 ? 73  VAL A CG2 1 
ATOM   3787 N N   . PHE C 3 74  ? 24.340  35.469  -14.050 1.00 94.53  ? 74  PHE A N   1 
ATOM   3788 C CA  . PHE C 3 74  ? 24.596  34.207  -14.789 1.00 92.74  ? 74  PHE A CA  1 
ATOM   3789 C C   . PHE C 3 74  ? 23.340  33.854  -15.547 1.00 92.67  ? 74  PHE A C   1 
ATOM   3790 O O   . PHE C 3 74  ? 22.329  33.453  -14.941 1.00 91.52  ? 74  PHE A O   1 
ATOM   3791 C CB  . PHE C 3 74  ? 25.028  33.091  -13.835 1.00 90.05  ? 74  PHE A CB  1 
ATOM   3792 C CG  . PHE C 3 74  ? 25.019  31.652  -14.340 1.00 87.98  ? 74  PHE A CG  1 
ATOM   3793 C CD1 . PHE C 3 74  ? 25.192  31.347  -15.686 1.00 89.92  ? 74  PHE A CD1 1 
ATOM   3794 C CD2 . PHE C 3 74  ? 24.862  30.596  -13.450 1.00 85.52  ? 74  PHE A CD2 1 
ATOM   3795 C CE1 . PHE C 3 74  ? 25.192  30.033  -16.125 1.00 86.78  ? 74  PHE A CE1 1 
ATOM   3796 C CE2 . PHE C 3 74  ? 24.865  29.284  -13.895 1.00 83.76  ? 74  PHE A CE2 1 
ATOM   3797 C CZ  . PHE C 3 74  ? 25.030  29.006  -15.229 1.00 84.39  ? 74  PHE A CZ  1 
ATOM   3798 N N   . SER C 3 75  ? 23.390  34.038  -16.862 1.00 94.04  ? 75  SER A N   1 
ATOM   3799 C CA  . SER C 3 75  ? 22.250  33.601  -17.698 1.00 94.00  ? 75  SER A CA  1 
ATOM   3800 C C   . SER C 3 75  ? 22.440  32.101  -17.949 1.00 91.67  ? 75  SER A C   1 
ATOM   3801 O O   . SER C 3 75  ? 23.535  31.718  -18.405 1.00 91.21  ? 75  SER A O   1 
ATOM   3802 C CB  . SER C 3 75  ? 22.193  34.397  -18.959 1.00 96.72  ? 75  SER A CB  1 
ATOM   3803 O OG  . SER C 3 75  ? 22.304  35.785  -18.680 1.00 98.98  ? 75  SER A OG  1 
ATOM   3804 N N   . ALA C 3 76  ? 21.437  31.283  -17.634 1.00 90.31  ? 76  ALA A N   1 
ATOM   3805 C CA  . ALA C 3 76  ? 21.633  29.819  -17.726 1.00 87.98  ? 76  ALA A CA  1 
ATOM   3806 C C   . ALA C 3 76  ? 20.582  29.198  -18.638 1.00 89.11  ? 76  ALA A C   1 
ATOM   3807 O O   . ALA C 3 76  ? 19.462  29.742  -18.721 1.00 89.32  ? 76  ALA A O   1 
ATOM   3808 C CB  . ALA C 3 76  ? 21.594  29.222  -16.345 1.00 85.75  ? 76  ALA A CB  1 
ATOM   3809 N N   . ASP C 3 77  ? 20.927  28.075  -19.271 1.00 86.87  ? 77  ASP A N   1 
ATOM   3810 C CA  . ASP C 3 77  ? 19.997  27.492  -20.270 1.00 87.23  ? 77  ASP A CA  1 
ATOM   3811 C C   . ASP C 3 77  ? 18.869  26.745  -19.564 1.00 85.75  ? 77  ASP A C   1 
ATOM   3812 O O   . ASP C 3 77  ? 19.120  26.098  -18.540 1.00 83.74  ? 77  ASP A O   1 
ATOM   3813 C CB  . ASP C 3 77  ? 20.752  26.657  -21.289 1.00 90.25  ? 77  ASP A CB  1 
ATOM   3814 C CG  . ASP C 3 77  ? 21.188  27.406  -22.538 1.00 89.89  ? 77  ASP A CG  1 
ATOM   3815 O OD1 . ASP C 3 77  ? 20.298  27.875  -23.273 1.00 96.58  ? 77  ASP A OD1 1 
ATOM   3816 O OD2 . ASP C 3 77  ? 22.411  27.515  -22.758 1.00 88.76  ? 77  ASP A OD2 1 
ATOM   3817 N N   . PRO C 3 78  ? 17.637  26.816  -20.095 1.00 87.68  ? 78  PRO A N   1 
ATOM   3818 C CA  . PRO C 3 78  ? 16.502  26.140  -19.489 1.00 87.08  ? 78  PRO A CA  1 
ATOM   3819 C C   . PRO C 3 78  ? 16.523  24.626  -19.611 1.00 85.31  ? 78  PRO A C   1 
ATOM   3820 O O   . PRO C 3 78  ? 17.384  24.057  -20.310 1.00 83.78  ? 78  PRO A O   1 
ATOM   3821 C CB  . PRO C 3 78  ? 15.371  26.756  -20.319 1.00 90.88  ? 78  PRO A CB  1 
ATOM   3822 C CG  . PRO C 3 78  ? 15.984  26.951  -21.674 1.00 88.80  ? 78  PRO A CG  1 
ATOM   3823 C CD  . PRO C 3 78  ? 17.306  27.568  -21.291 1.00 89.56  ? 78  PRO A CD  1 
ATOM   3824 N N   . PRO C 3 79  ? 15.580  23.916  -18.959 1.00 84.56  ? 79  PRO A N   1 
ATOM   3825 C CA  . PRO C 3 79  ? 15.517  22.470  -19.061 1.00 81.75  ? 79  PRO A CA  1 
ATOM   3826 C C   . PRO C 3 79  ? 15.003  21.977  -20.398 1.00 84.55  ? 79  PRO A C   1 
ATOM   3827 O O   . PRO C 3 79  ? 14.532  22.784  -21.218 1.00 89.13  ? 79  PRO A O   1 
ATOM   3828 C CB  . PRO C 3 79  ? 14.560  22.100  -17.927 1.00 81.69  ? 79  PRO A CB  1 
ATOM   3829 C CG  . PRO C 3 79  ? 14.511  23.326  -17.057 1.00 82.98  ? 79  PRO A CG  1 
ATOM   3830 C CD  . PRO C 3 79  ? 14.582  24.454  -18.059 1.00 88.61  ? 79  PRO A CD  1 
ATOM   3831 N N   . SER C 3 80  ? 15.075  20.663  -20.608 1.00 82.95  ? 80  SER A N   1 
ATOM   3832 C CA  . SER C 3 80  ? 14.613  20.059  -21.876 1.00 83.26  ? 80  SER A CA  1 
ATOM   3833 C C   . SER C 3 80  ? 13.558  18.996  -21.569 1.00 82.86  ? 80  SER A C   1 
ATOM   3834 O O   . SER C 3 80  ? 13.941  17.898  -21.172 1.00 81.00  ? 80  SER A O   1 
ATOM   3835 C CB  . SER C 3 80  ? 15.773  19.479  -22.611 1.00 82.74  ? 80  SER A CB  1 
ATOM   3836 O OG  . SER C 3 80  ? 17.003  19.862  -22.011 1.00 81.46  ? 80  SER A OG  1 
ATOM   3837 N N   . ALA C 3 81  ? 12.285  19.309  -21.776 1.00 84.74  ? 81  ALA A N   1 
ATOM   3838 C CA  . ALA C 3 81  ? 11.186  18.367  -21.462 1.00 84.71  ? 81  ALA A CA  1 
ATOM   3839 C C   . ALA C 3 81  ? 11.405  17.013  -22.128 1.00 84.08  ? 81  ALA A C   1 
ATOM   3840 O O   . ALA C 3 81  ? 10.835  16.016  -21.653 1.00 84.40  ? 81  ALA A O   1 
ATOM   3841 C CB  . ALA C 3 81  ? 9.886   18.956  -21.924 1.00 87.27  ? 81  ALA A CB  1 
ATOM   3842 N N   . GLU C 3 82  ? 12.161  16.988  -23.222 1.00 84.51  ? 82  GLU A N   1 
ATOM   3843 C CA  . GLU C 3 82  ? 12.435  15.723  -23.943 1.00 84.08  ? 82  GLU A CA  1 
ATOM   3844 C C   . GLU C 3 82  ? 13.347  14.844  -23.082 1.00 81.54  ? 82  GLU A C   1 
ATOM   3845 O O   . GLU C 3 82  ? 13.337  13.619  -23.283 1.00 80.99  ? 82  GLU A O   1 
ATOM   3846 C CB  . GLU C 3 82  ? 13.100  16.063  -25.274 1.00 85.22  ? 82  GLU A CB  1 
ATOM   3847 C CG  . GLU C 3 82  ? 12.128  16.626  -26.304 1.00 87.91  ? 82  GLU A CG  1 
ATOM   3848 C CD  . GLU C 3 82  ? 12.795  16.867  -27.643 1.00 88.86  ? 82  GLU A CD  1 
ATOM   3849 O OE1 . GLU C 3 82  ? 14.043  16.824  -27.694 1.00 87.37  ? 82  GLU A OE1 1 
ATOM   3850 O OE2 . GLU C 3 82  ? 12.068  17.097  -28.630 1.00 94.75  ? 82  GLU A OE2 1 
ATOM   3851 N N   . LEU C 3 83  ? 14.097  15.454  -22.166 1.00 80.13  ? 83  LEU A N   1 
ATOM   3852 C CA  . LEU C 3 83  ? 15.027  14.701  -21.344 1.00 77.86  ? 83  LEU A CA  1 
ATOM   3853 C C   . LEU C 3 83  ? 14.568  14.583  -19.895 1.00 76.85  ? 83  LEU A C   1 
ATOM   3854 O O   . LEU C 3 83  ? 15.354  14.163  -19.034 1.00 76.08  ? 83  LEU A O   1 
ATOM   3855 C CB  . LEU C 3 83  ? 16.417  15.332  -21.413 1.00 77.32  ? 83  LEU A CB  1 
ATOM   3856 C CG  . LEU C 3 83  ? 17.042  15.346  -22.797 1.00 78.45  ? 83  LEU A CG  1 
ATOM   3857 C CD1 . LEU C 3 83  ? 18.538  15.559  -22.672 1.00 77.50  ? 83  LEU A CD1 1 
ATOM   3858 C CD2 . LEU C 3 83  ? 16.724  14.055  -23.517 1.00 78.61  ? 83  LEU A CD2 1 
ATOM   3859 N N   . ILE C 3 84  ? 13.320  14.950  -19.606 1.00 77.56  ? 84  ILE A N   1 
ATOM   3860 C CA  . ILE C 3 84  ? 12.776  14.922  -18.247 1.00 76.56  ? 84  ILE A CA  1 
ATOM   3861 C C   . ILE C 3 84  ? 11.470  14.126  -18.286 1.00 77.36  ? 84  ILE A C   1 
ATOM   3862 O O   . ILE C 3 84  ? 10.669  14.325  -19.211 1.00 79.44  ? 84  ILE A O   1 
ATOM   3863 C CB  . ILE C 3 84  ? 12.470  16.330  -17.708 1.00 77.24  ? 84  ILE A CB  1 
ATOM   3864 C CG1 . ILE C 3 84  ? 13.680  17.160  -17.233 1.00 76.34  ? 84  ILE A CG1 1 
ATOM   3865 C CG2 . ILE C 3 84  ? 11.568  16.216  -16.505 1.00 77.83  ? 84  ILE A CG2 1 
ATOM   3866 C CD1 . ILE C 3 84  ? 14.835  17.379  -18.165 1.00 76.57  ? 84  ILE A CD1 1 
ATOM   3867 N N   . PRO C 3 85  ? 11.189  13.253  -17.313 1.00 78.09  ? 85  PRO A N   1 
ATOM   3868 C CA  . PRO C 3 85  ? 9.870   12.595  -17.243 1.00 80.19  ? 85  PRO A CA  1 
ATOM   3869 C C   . PRO C 3 85  ? 8.715   13.587  -17.141 1.00 80.95  ? 85  PRO A C   1 
ATOM   3870 O O   . PRO C 3 85  ? 8.865   14.708  -16.660 1.00 80.95  ? 85  PRO A O   1 
ATOM   3871 C CB  . PRO C 3 85  ? 9.970   11.766  -15.960 1.00 75.28  ? 85  PRO A CB  1 
ATOM   3872 C CG  . PRO C 3 85  ? 11.427  11.517  -15.820 1.00 73.50  ? 85  PRO A CG  1 
ATOM   3873 C CD  . PRO C 3 85  ? 12.070  12.796  -16.227 1.00 73.89  ? 85  PRO A CD  1 
ATOM   3874 N N   . ALA C 3 86  ? 7.526   13.134  -17.552 1.00 80.59  ? 86  ALA A N   1 
ATOM   3875 C CA  . ALA C 3 86  ? 6.370   14.028  -17.589 1.00 82.49  ? 86  ALA A CA  1 
ATOM   3876 C C   . ALA C 3 86  ? 5.963   14.500  -16.203 1.00 81.74  ? 86  ALA A C   1 
ATOM   3877 O O   . ALA C 3 86  ? 5.365   15.573  -16.070 1.00 86.51  ? 86  ALA A O   1 
ATOM   3878 C CB  . ALA C 3 86  ? 5.185   13.343  -18.262 1.00 84.55  ? 86  ALA A CB  1 
ATOM   3879 N N   . SER C 3 87  ? 6.263   13.723  -15.164 1.00 81.03  ? 87  SER A N   1 
ATOM   3880 C CA  . SER C 3 87  ? 5.829   14.097  -13.823 1.00 80.83  ? 87  SER A CA  1 
ATOM   3881 C C   . SER C 3 87  ? 6.591   15.309  -13.305 1.00 84.06  ? 87  SER A C   1 
ATOM   3882 O O   . SER C 3 87  ? 5.992   16.239  -12.753 1.00 87.66  ? 87  SER A O   1 
ATOM   3883 C CB  . SER C 3 87  ? 5.991   12.909  -12.882 1.00 80.70  ? 87  SER A CB  1 
ATOM   3884 O OG  . SER C 3 87  ? 5.401   11.767  -13.467 1.00 78.38  ? 87  SER A OG  1 
ATOM   3885 N N   . GLU C 3 88  ? 7.909   15.324  -13.488 1.00 80.44  ? 88  GLU A N   1 
ATOM   3886 C CA  . GLU C 3 88  ? 8.731   16.444  -13.053 1.00 81.12  ? 88  GLU A CA  1 
ATOM   3887 C C   . GLU C 3 88  ? 8.380   17.741  -13.778 1.00 84.95  ? 88  GLU A C   1 
ATOM   3888 O O   . GLU C 3 88  ? 8.782   18.826  -13.331 1.00 84.36  ? 88  GLU A O   1 
ATOM   3889 C CB  . GLU C 3 88  ? 10.201  16.072  -13.248 1.00 77.14  ? 88  GLU A CB  1 
ATOM   3890 C CG  . GLU C 3 88  ? 10.490  14.577  -12.969 1.00 74.33  ? 88  GLU A CG  1 
ATOM   3891 C CD  . GLU C 3 88  ? 11.979  14.264  -12.923 1.00 71.70  ? 88  GLU A CD  1 
ATOM   3892 O OE1 . GLU C 3 88  ? 12.782  15.221  -12.906 1.00 72.93  ? 88  GLU A OE1 1 
ATOM   3893 O OE2 . GLU C 3 88  ? 12.355  13.072  -12.935 1.00 70.71  ? 88  GLU A OE2 1 
ATOM   3894 N N   . LEU C 3 89  ? 7.622   17.648  -14.873 1.00 87.64  ? 89  LEU A N   1 
ATOM   3895 C CA  . LEU C 3 89  ? 7.124   18.834  -15.563 1.00 90.03  ? 89  LEU A CA  1 
ATOM   3896 C C   . LEU C 3 89  ? 6.096   19.577  -14.714 1.00 91.35  ? 89  LEU A C   1 
ATOM   3897 O O   . LEU C 3 89  ? 6.084   20.810  -14.680 1.00 94.27  ? 89  LEU A O   1 
ATOM   3898 C CB  . LEU C 3 89  ? 6.517   18.423  -16.911 1.00 89.26  ? 89  LEU A CB  1 
ATOM   3899 C CG  . LEU C 3 89  ? 7.281   18.359  -18.244 1.00 86.87  ? 89  LEU A CG  1 
ATOM   3900 C CD1 . LEU C 3 89  ? 7.319   19.701  -18.963 1.00 92.85  ? 89  LEU A CD1 1 
ATOM   3901 C CD2 . LEU C 3 89  ? 8.689   17.858  -18.037 1.00 83.23  ? 89  LEU A CD2 1 
ATOM   3902 N N   . VAL C 3 90  ? 5.229   18.848  -14.024 1.00 90.25  ? 90  VAL A N   1 
ATOM   3903 C CA  . VAL C 3 90  ? 4.090   19.441  -13.339 1.00 93.88  ? 90  VAL A CA  1 
ATOM   3904 C C   . VAL C 3 90  ? 4.241   19.354  -11.824 1.00 95.10  ? 90  VAL A C   1 
ATOM   3905 O O   . VAL C 3 90  ? 3.276   19.562  -11.089 1.00 97.11  ? 90  VAL A O   1 
ATOM   3906 C CB  . VAL C 3 90  ? 2.777   18.793  -13.799 1.00 94.19  ? 90  VAL A CB  1 
ATOM   3907 C CG1 . VAL C 3 90  ? 2.693   18.804  -15.313 1.00 97.43  ? 90  VAL A CG1 1 
ATOM   3908 C CG2 . VAL C 3 90  ? 2.691   17.364  -13.265 1.00 87.51  ? 90  VAL A CG2 1 
ATOM   3909 N N   . SER C 3 91  ? 5.439   19.057  -11.342 1.00 94.52  ? 91  SER A N   1 
ATOM   3910 C CA  . SER C 3 91  ? 5.642   18.776  -9.932  1.00 91.71  ? 91  SER A CA  1 
ATOM   3911 C C   . SER C 3 91  ? 6.782   19.631  -9.410  1.00 88.48  ? 91  SER A C   1 
ATOM   3912 O O   . SER C 3 91  ? 7.380   20.431  -10.138 1.00 89.82  ? 91  SER A O   1 
ATOM   3913 C CB  . SER C 3 91  ? 5.940   17.291  -9.705  1.00 91.59  ? 91  SER A CB  1 
ATOM   3914 O OG  . SER C 3 91  ? 4.996   16.461  -10.366 1.00 91.14  ? 91  SER A OG  1 
ATOM   3915 N N   . VAL C 3 92  ? 7.079   19.454  -8.127  1.00 83.27  ? 92  VAL A N   1 
ATOM   3916 C CA  . VAL C 3 92  ? 8.191   20.161  -7.516  1.00 80.69  ? 92  VAL A CA  1 
ATOM   3917 C C   . VAL C 3 92  ? 9.493   19.553  -8.010  1.00 74.78  ? 92  VAL A C   1 
ATOM   3918 O O   . VAL C 3 92  ? 9.602   18.332  -8.180  1.00 77.38  ? 92  VAL A O   1 
ATOM   3919 C CB  . VAL C 3 92  ? 8.099   20.089  -5.981  1.00 78.69  ? 92  VAL A CB  1 
ATOM   3920 C CG1 . VAL C 3 92  ? 8.974   21.162  -5.336  1.00 78.05  ? 92  VAL A CG1 1 
ATOM   3921 C CG2 . VAL C 3 92  ? 6.644   20.166  -5.509  1.00 80.00  ? 92  VAL A CG2 1 
ATOM   3922 N N   . THR C 3 93  ? 10.492  20.398  -8.231  1.00 73.66  ? 93  THR A N   1 
ATOM   3923 C CA  . THR C 3 93  ? 11.819  19.938  -8.614  1.00 72.48  ? 93  THR A CA  1 
ATOM   3924 C C   . THR C 3 93  ? 12.819  20.747  -7.819  1.00 71.90  ? 93  THR A C   1 
ATOM   3925 O O   . THR C 3 93  ? 12.441  21.505  -6.925  1.00 72.25  ? 93  THR A O   1 
ATOM   3926 C CB  . THR C 3 93  ? 12.056  20.079  -10.118 1.00 73.59  ? 93  THR A CB  1 
ATOM   3927 O OG1 . THR C 3 93  ? 11.454  21.301  -10.571 1.00 75.57  ? 93  THR A OG1 1 
ATOM   3928 C CG2 . THR C 3 93  ? 11.441  18.900  -10.853 1.00 73.67  ? 93  THR A CG2 1 
ATOM   3929 N N   . VAL C 3 94  ? 14.098  20.602  -8.140  1.00 71.18  ? 94  VAL A N   1 
ATOM   3930 C CA  . VAL C 3 94  ? 15.146  21.249  -7.358  1.00 70.68  ? 94  VAL A CA  1 
ATOM   3931 C C   . VAL C 3 94  ? 16.257  21.620  -8.320  1.00 71.16  ? 94  VAL A C   1 
ATOM   3932 O O   . VAL C 3 94  ? 16.471  20.938  -9.318  1.00 71.07  ? 94  VAL A O   1 
ATOM   3933 C CB  . VAL C 3 94  ? 15.638  20.336  -6.199  1.00 68.82  ? 94  VAL A CB  1 
ATOM   3934 C CG1 . VAL C 3 94  ? 17.041  20.719  -5.695  1.00 68.28  ? 94  VAL A CG1 1 
ATOM   3935 C CG2 . VAL C 3 94  ? 14.656  20.358  -5.045  1.00 68.63  ? 94  VAL A CG2 1 
ATOM   3936 N N   . ILE C 3 95  ? 16.922  22.732  -8.055  1.00 71.87  ? 95  ILE A N   1 
ATOM   3937 C CA  . ILE C 3 95  ? 18.075  23.163  -8.826  1.00 72.45  ? 95  ILE A CA  1 
ATOM   3938 C C   . ILE C 3 95  ? 19.187  23.548  -7.872  1.00 71.96  ? 95  ILE A C   1 
ATOM   3939 O O   . ILE C 3 95  ? 18.945  24.166  -6.828  1.00 72.10  ? 95  ILE A O   1 
ATOM   3940 C CB  . ILE C 3 95  ? 17.732  24.327  -9.766  1.00 74.57  ? 95  ILE A CB  1 
ATOM   3941 C CG1 . ILE C 3 95  ? 16.917  23.813  -10.943 1.00 75.16  ? 95  ILE A CG1 1 
ATOM   3942 C CG2 . ILE C 3 95  ? 18.977  24.904  -10.324 1.00 75.29  ? 95  ILE A CG2 1 
ATOM   3943 C CD1 . ILE C 3 95  ? 15.460  23.859  -10.738 1.00 80.64  ? 95  ILE A CD1 1 
ATOM   3944 N N   . LEU C 3 96  ? 20.400  23.157  -8.220  1.00 71.48  ? 96  LEU A N   1 
ATOM   3945 C CA  . LEU C 3 96  ? 21.584  23.370  -7.397  1.00 71.10  ? 96  LEU A CA  1 
ATOM   3946 C C   . LEU C 3 96  ? 22.484  24.337  -8.130  1.00 72.65  ? 96  LEU A C   1 
ATOM   3947 O O   . LEU C 3 96  ? 23.190  23.941  -9.071  1.00 73.63  ? 96  LEU A O   1 
ATOM   3948 C CB  . LEU C 3 96  ? 22.314  22.067  -7.145  1.00 69.42  ? 96  LEU A CB  1 
ATOM   3949 C CG  . LEU C 3 96  ? 22.006  21.268  -5.905  1.00 67.91  ? 96  LEU A CG  1 
ATOM   3950 C CD1 . LEU C 3 96  ? 20.564  21.480  -5.481  1.00 68.05  ? 96  LEU A CD1 1 
ATOM   3951 C CD2 . LEU C 3 96  ? 22.254  19.813  -6.360  1.00 66.63  ? 96  LEU A CD2 1 
ATOM   3952 N N   . LEU C 3 97  ? 22.441  25.594  -7.713  1.00 74.01  ? 97  LEU A N   1 
ATOM   3953 C CA  . LEU C 3 97  ? 23.475  26.530  -8.119  1.00 75.54  ? 97  LEU A CA  1 
ATOM   3954 C C   . LEU C 3 97  ? 24.744  26.210  -7.346  1.00 74.83  ? 97  LEU A C   1 
ATOM   3955 O O   . LEU C 3 97  ? 24.757  26.221  -6.112  1.00 74.21  ? 97  LEU A O   1 
ATOM   3956 C CB  . LEU C 3 97  ? 23.019  27.966  -7.886  1.00 77.39  ? 97  LEU A CB  1 
ATOM   3957 C CG  . LEU C 3 97  ? 23.955  29.093  -8.291  1.00 79.39  ? 97  LEU A CG  1 
ATOM   3958 C CD1 . LEU C 3 97  ? 23.188  30.311  -8.594  1.00 81.37  ? 97  LEU A CD1 1 
ATOM   3959 C CD2 . LEU C 3 97  ? 24.779  29.384  -7.100  1.00 79.31  ? 97  LEU A CD2 1 
ATOM   3960 N N   . SER C 3 98  ? 25.805  25.935  -8.075  1.00 75.05  ? 98  SER A N   1 
ATOM   3961 C CA  . SER C 3 98  ? 27.031  25.379  -7.536  1.00 74.33  ? 98  SER A CA  1 
ATOM   3962 C C   . SER C 3 98  ? 28.179  26.225  -8.053  1.00 76.14  ? 98  SER A C   1 
ATOM   3963 O O   . SER C 3 98  ? 28.179  26.627  -9.218  1.00 77.33  ? 98  SER A O   1 
ATOM   3964 C CB  . SER C 3 98  ? 27.162  23.872  -7.955  1.00 72.60  ? 98  SER A CB  1 
ATOM   3965 O OG  . SER C 3 98  ? 28.146  23.605  -8.950  1.00 73.07  ? 98  SER A OG  1 
ATOM   3966 N N   . CYS C 3 99  ? 29.142  26.522  -7.203  1.00 76.56  ? 99  CYS A N   1 
ATOM   3967 C CA  . CYS C 3 99  ? 30.322  27.193  -7.703  1.00 78.35  ? 99  CYS A CA  1 
ATOM   3968 C C   . CYS C 3 99  ? 31.528  26.393  -7.269  1.00 77.67  ? 99  CYS A C   1 
ATOM   3969 O O   . CYS C 3 99  ? 31.566  25.842  -6.172  1.00 76.45  ? 99  CYS A O   1 
ATOM   3970 C CB  . CYS C 3 99  ? 30.400  28.651  -7.244  1.00 80.41  ? 99  CYS A CB  1 
ATOM   3971 S SG  . CYS C 3 99  ? 31.631  29.648  -8.108  1.00 83.15  ? 99  CYS A SG  1 
ATOM   3972 N N   . SER C 3 100 ? 32.476  26.275  -8.170  1.00 78.48  ? 100 SER A N   1 
ATOM   3973 C CA  . SER C 3 100 ? 33.597  25.371  -8.013  1.00 82.22  ? 100 SER A CA  1 
ATOM   3974 C C   . SER C 3 100 ? 34.864  26.133  -8.374  1.00 85.05  ? 100 SER A C   1 
ATOM   3975 O O   . SER C 3 100 ? 34.824  27.090  -9.154  1.00 86.70  ? 100 SER A O   1 
ATOM   3976 C CB  . SER C 3 100 ? 33.436  24.083  -8.894  1.00 79.50  ? 100 SER A CB  1 
ATOM   3977 O OG  . SER C 3 100 ? 32.114  23.543  -8.858  1.00 74.76  ? 100 SER A OG  1 
ATOM   3978 N N   . TYR C 3 101 ? 35.987  25.713  -7.786  1.00 84.52  ? 101 TYR A N   1 
ATOM   3979 C CA  . TYR C 3 101 ? 37.271  26.386  -7.966  1.00 87.43  ? 101 TYR A CA  1 
ATOM   3980 C C   . TYR C 3 101 ? 38.319  25.366  -8.399  1.00 90.55  ? 101 TYR A C   1 
ATOM   3981 O O   . TYR C 3 101 ? 38.736  24.528  -7.592  1.00 88.33  ? 101 TYR A O   1 
ATOM   3982 C CB  . TYR C 3 101 ? 37.706  27.105  -6.687  1.00 91.09  ? 101 TYR A CB  1 
ATOM   3983 C CG  . TYR C 3 101 ? 38.926  27.963  -6.923  1.00 99.20  ? 101 TYR A CG  1 
ATOM   3984 C CD1 . TYR C 3 101 ? 38.807  29.259  -7.439  1.00 97.82  ? 101 TYR A CD1 1 
ATOM   3985 C CD2 . TYR C 3 101 ? 40.202  27.480  -6.649  1.00 102.23 ? 101 TYR A CD2 1 
ATOM   3986 C CE1 . TYR C 3 101 ? 39.921  30.041  -7.673  1.00 101.51 ? 101 TYR A CE1 1 
ATOM   3987 C CE2 . TYR C 3 101 ? 41.327  28.261  -6.885  1.00 105.67 ? 101 TYR A CE2 1 
ATOM   3988 C CZ  . TYR C 3 101 ? 41.177  29.537  -7.395  1.00 107.43 ? 101 TYR A CZ  1 
ATOM   3989 O OH  . TYR C 3 101 ? 42.290  30.310  -7.628  1.00 115.70 ? 101 TYR A OH  1 
ATOM   3990 N N   . ASP C 3 102 ? 38.758  25.455  -9.659  1.00 93.49  ? 102 ASP A N   1 
ATOM   3991 C CA  . ASP C 3 102 ? 39.698  24.506  -10.257 1.00 90.94  ? 102 ASP A CA  1 
ATOM   3992 C C   . ASP C 3 102 ? 39.338  23.067  -9.876  1.00 92.47  ? 102 ASP A C   1 
ATOM   3993 O O   . ASP C 3 102 ? 40.077  22.354  -9.189  1.00 90.04  ? 102 ASP A O   1 
ATOM   3994 C CB  . ASP C 3 102 ? 41.138  24.826  -9.871  1.00 94.46  ? 102 ASP A CB  1 
ATOM   3995 C CG  . ASP C 3 102 ? 42.105  24.632  -11.026 1.00 102.16 ? 102 ASP A CG  1 
ATOM   3996 O OD1 . ASP C 3 102 ? 41.852  25.178  -12.124 1.00 104.02 ? 102 ASP A OD1 1 
ATOM   3997 O OD2 . ASP C 3 102 ? 43.108  23.902  -10.848 1.00 107.94 ? 102 ASP A OD2 1 
ATOM   3998 N N   . GLY C 3 103 ? 38.160  22.659  -10.345 1.00 90.17  ? 103 GLY A N   1 
ATOM   3999 C CA  . GLY C 3 103 ? 37.648  21.327  -10.126 1.00 87.59  ? 103 GLY A CA  1 
ATOM   4000 C C   . GLY C 3 103 ? 36.929  21.129  -8.817  1.00 86.47  ? 103 GLY A C   1 
ATOM   4001 O O   . GLY C 3 103 ? 36.270  20.097  -8.638  1.00 85.69  ? 103 GLY A O   1 
ATOM   4002 N N   . ARG C 3 104 ? 37.017  22.079  -7.898  1.00 86.88  ? 104 ARG A N   1 
ATOM   4003 C CA  . ARG C 3 104 ? 36.604  21.842  -6.522  1.00 84.25  ? 104 ARG A CA  1 
ATOM   4004 C C   . ARG C 3 104 ? 35.360  22.668  -6.229  1.00 82.30  ? 104 ARG A C   1 
ATOM   4005 O O   . ARG C 3 104 ? 35.408  23.901  -6.228  1.00 84.49  ? 104 ARG A O   1 
ATOM   4006 C CB  . ARG C 3 104 ? 37.758  22.138  -5.563  1.00 86.99  ? 104 ARG A CB  1 
ATOM   4007 C CG  . ARG C 3 104 ? 39.060  21.434  -5.987  1.00 88.59  ? 104 ARG A CG  1 
ATOM   4008 C CD  . ARG C 3 104 ? 40.294  21.842  -5.170  1.00 95.11  ? 104 ARG A CD  1 
ATOM   4009 N NE  . ARG C 3 104 ? 40.663  23.249  -5.296  1.00 95.59  ? 104 ARG A NE  1 
ATOM   4010 C CZ  . ARG C 3 104 ? 41.442  23.734  -6.254  1.00 95.60  ? 104 ARG A CZ  1 
ATOM   4011 N NH1 . ARG C 3 104 ? 41.839  22.982  -7.271  1.00 97.63  ? 104 ARG A NH1 1 
ATOM   4012 N NH2 . ARG C 3 104 ? 41.830  25.005  -6.193  1.00 96.38  ? 104 ARG A NH2 1 
ATOM   4013 N N   . GLU C 3 105 ? 34.244  21.973  -6.013  1.00 80.85  ? 105 GLU A N   1 
ATOM   4014 C CA  . GLU C 3 105 ? 32.994  22.596  -5.600  1.00 78.04  ? 105 GLU A CA  1 
ATOM   4015 C C   . GLU C 3 105 ? 33.116  23.006  -4.141  1.00 78.16  ? 105 GLU A C   1 
ATOM   4016 O O   . GLU C 3 105 ? 33.421  22.167  -3.290  1.00 75.85  ? 105 GLU A O   1 
ATOM   4017 C CB  . GLU C 3 105 ? 31.835  21.616  -5.801  1.00 72.59  ? 105 GLU A CB  1 
ATOM   4018 C CG  . GLU C 3 105 ? 30.440  22.184  -5.574  1.00 70.76  ? 105 GLU A CG  1 
ATOM   4019 C CD  . GLU C 3 105 ? 29.358  21.102  -5.513  1.00 68.95  ? 105 GLU A CD  1 
ATOM   4020 O OE1 . GLU C 3 105 ? 29.703  19.902  -5.480  1.00 70.78  ? 105 GLU A OE1 1 
ATOM   4021 O OE2 . GLU C 3 105 ? 28.158  21.447  -5.454  1.00 68.85  ? 105 GLU A OE2 1 
ATOM   4022 N N   . PHE C 3 106 ? 32.909  24.296  -3.848  1.00 74.43  ? 106 PHE A N   1 
ATOM   4023 C CA  . PHE C 3 106 ? 33.011  24.772  -2.478  1.00 74.81  ? 106 PHE A CA  1 
ATOM   4024 C C   . PHE C 3 106 ? 31.712  25.291  -1.904  1.00 74.45  ? 106 PHE A C   1 
ATOM   4025 O O   . PHE C 3 106 ? 31.647  25.492  -0.693  1.00 74.43  ? 106 PHE A O   1 
ATOM   4026 C CB  . PHE C 3 106 ? 34.054  25.890  -2.346  1.00 80.52  ? 106 PHE A CB  1 
ATOM   4027 C CG  . PHE C 3 106 ? 33.858  27.020  -3.311  1.00 83.13  ? 106 PHE A CG  1 
ATOM   4028 C CD1 . PHE C 3 106 ? 34.294  26.903  -4.637  1.00 84.81  ? 106 PHE A CD1 1 
ATOM   4029 C CD2 . PHE C 3 106 ? 33.245  28.197  -2.904  1.00 80.12  ? 106 PHE A CD2 1 
ATOM   4030 C CE1 . PHE C 3 106 ? 34.115  27.949  -5.534  1.00 84.56  ? 106 PHE A CE1 1 
ATOM   4031 C CE2 . PHE C 3 106 ? 33.067  29.241  -3.790  1.00 81.88  ? 106 PHE A CE2 1 
ATOM   4032 C CZ  . PHE C 3 106 ? 33.498  29.124  -5.098  1.00 83.78  ? 106 PHE A CZ  1 
ATOM   4033 N N   . VAL C 3 107 ? 30.694  25.525  -2.719  1.00 74.32  ? 107 VAL A N   1 
ATOM   4034 C CA  . VAL C 3 107 ? 29.422  26.015  -2.205  1.00 74.12  ? 107 VAL A CA  1 
ATOM   4035 C C   . VAL C 3 107 ? 28.346  25.547  -3.158  1.00 73.23  ? 107 VAL A C   1 
ATOM   4036 O O   . VAL C 3 107 ? 28.551  25.492  -4.369  1.00 73.67  ? 107 VAL A O   1 
ATOM   4037 C CB  . VAL C 3 107 ? 29.408  27.560  -2.031  1.00 76.29  ? 107 VAL A CB  1 
ATOM   4038 C CG1 . VAL C 3 107 ? 27.975  28.137  -2.026  1.00 76.39  ? 107 VAL A CG1 1 
ATOM   4039 C CG2 . VAL C 3 107 ? 30.089  27.963  -0.756  1.00 76.97  ? 107 VAL A CG2 1 
ATOM   4040 N N   . ARG C 3 108 ? 27.200  25.207  -2.605  1.00 72.11  ? 108 ARG A N   1 
ATOM   4041 C CA  . ARG C 3 108 ? 26.117  24.641  -3.380  1.00 71.27  ? 108 ARG A CA  1 
ATOM   4042 C C   . ARG C 3 108 ? 24.836  25.165  -2.782  1.00 71.39  ? 108 ARG A C   1 
ATOM   4043 O O   . ARG C 3 108 ? 24.586  24.974  -1.592  1.00 70.68  ? 108 ARG A O   1 
ATOM   4044 C CB  . ARG C 3 108 ? 26.162  23.108  -3.336  1.00 69.36  ? 108 ARG A CB  1 
ATOM   4045 C CG  . ARG C 3 108 ? 24.964  22.400  -3.938  1.00 68.48  ? 108 ARG A CG  1 
ATOM   4046 C CD  . ARG C 3 108 ? 24.888  20.990  -3.395  1.00 67.72  ? 108 ARG A CD  1 
ATOM   4047 N NE  . ARG C 3 108 ? 26.219  20.418  -3.213  1.00 70.84  ? 108 ARG A NE  1 
ATOM   4048 C CZ  . ARG C 3 108 ? 26.572  19.203  -3.618  1.00 71.17  ? 108 ARG A CZ  1 
ATOM   4049 N NH1 . ARG C 3 108 ? 25.697  18.380  -4.166  1.00 71.79  ? 108 ARG A NH1 1 
ATOM   4050 N NH2 . ARG C 3 108 ? 27.838  18.810  -3.486  1.00 69.92  ? 108 ARG A NH2 1 
ATOM   4051 N N   . VAL C 3 109 ? 24.038  25.841  -3.578  1.00 72.43  ? 109 VAL A N   1 
ATOM   4052 C CA  . VAL C 3 109 ? 22.826  26.447  -3.069  1.00 72.86  ? 109 VAL A CA  1 
ATOM   4053 C C   . VAL C 3 109 ? 21.661  25.766  -3.768  1.00 72.19  ? 109 VAL A C   1 
ATOM   4054 O O   . VAL C 3 109 ? 21.524  25.849  -4.995  1.00 72.88  ? 109 VAL A O   1 
ATOM   4055 C CB  . VAL C 3 109 ? 22.826  27.985  -3.249  1.00 75.06  ? 109 VAL A CB  1 
ATOM   4056 C CG1 . VAL C 3 109 ? 21.658  28.604  -2.534  1.00 75.53  ? 109 VAL A CG1 1 
ATOM   4057 C CG2 . VAL C 3 109 ? 24.137  28.619  -2.710  1.00 75.99  ? 109 VAL A CG2 1 
ATOM   4058 N N   . GLY C 3 110 ? 20.841  25.075  -2.987  1.00 70.97  ? 110 GLY A N   1 
ATOM   4059 C CA  . GLY C 3 110 ? 19.716  24.329  -3.511  1.00 70.39  ? 110 GLY A CA  1 
ATOM   4060 C C   . GLY C 3 110 ? 18.400  25.086  -3.324  1.00 71.42  ? 110 GLY A C   1 
ATOM   4061 O O   . GLY C 3 110 ? 18.166  25.682  -2.281  1.00 71.71  ? 110 GLY A O   1 
ATOM   4062 N N   . TYR C 3 111 ? 17.567  25.040  -4.349  1.00 72.08  ? 111 TYR A N   1 
ATOM   4063 C CA  . TYR C 3 111 ? 16.315  25.778  -4.329  1.00 74.22  ? 111 TYR A CA  1 
ATOM   4064 C C   . TYR C 3 111 ? 15.168  24.870  -4.704  1.00 76.02  ? 111 TYR A C   1 
ATOM   4065 O O   . TYR C 3 111 ? 15.223  24.186  -5.732  1.00 72.72  ? 111 TYR A O   1 
ATOM   4066 C CB  . TYR C 3 111 ? 16.336  26.948  -5.304  1.00 75.39  ? 111 TYR A CB  1 
ATOM   4067 C CG  . TYR C 3 111 ? 17.308  28.023  -4.945  1.00 76.32  ? 111 TYR A CG  1 
ATOM   4068 C CD1 . TYR C 3 111 ? 16.976  29.020  -4.031  1.00 77.28  ? 111 TYR A CD1 1 
ATOM   4069 C CD2 . TYR C 3 111 ? 18.567  28.047  -5.511  1.00 76.40  ? 111 TYR A CD2 1 
ATOM   4070 C CE1 . TYR C 3 111 ? 17.875  30.024  -3.712  1.00 78.37  ? 111 TYR A CE1 1 
ATOM   4071 C CE2 . TYR C 3 111 ? 19.470  29.046  -5.196  1.00 77.51  ? 111 TYR A CE2 1 
ATOM   4072 C CZ  . TYR C 3 111 ? 19.120  30.027  -4.295  1.00 78.50  ? 111 TYR A CZ  1 
ATOM   4073 O OH  . TYR C 3 111 ? 20.033  31.000  -3.994  1.00 79.77  ? 111 TYR A OH  1 
ATOM   4074 N N   . TYR C 3 112 ? 14.116  24.902  -3.893  1.00 86.92  ? 112 TYR A N   1 
ATOM   4075 C CA  . TYR C 3 112 ? 12.850  24.341  -4.332  1.00 89.50  ? 112 TYR A CA  1 
ATOM   4076 C C   . TYR C 3 112 ? 12.369  25.050  -5.596  1.00 93.62  ? 112 TYR A C   1 
ATOM   4077 O O   . TYR C 3 112 ? 12.614  26.243  -5.800  1.00 94.75  ? 112 TYR A O   1 
ATOM   4078 C CB  . TYR C 3 112 ? 11.797  24.463  -3.236  1.00 87.63  ? 112 TYR A CB  1 
ATOM   4079 C CG  . TYR C 3 112 ? 11.708  23.219  -2.394  1.00 89.88  ? 112 TYR A CG  1 
ATOM   4080 C CD1 . TYR C 3 112 ? 10.541  22.469  -2.349  1.00 93.66  ? 112 TYR A CD1 1 
ATOM   4081 C CD2 . TYR C 3 112 ? 12.789  22.791  -1.637  1.00 90.62  ? 112 TYR A CD2 1 
ATOM   4082 C CE1 . TYR C 3 112 ? 10.460  21.309  -1.578  1.00 90.37  ? 112 TYR A CE1 1 
ATOM   4083 C CE2 . TYR C 3 112 ? 12.714  21.645  -0.861  1.00 87.11  ? 112 TYR A CE2 1 
ATOM   4084 C CZ  . TYR C 3 112 ? 11.554  20.902  -0.835  1.00 82.75  ? 112 TYR A CZ  1 
ATOM   4085 O OH  . TYR C 3 112 ? 11.479  19.760  -0.066  1.00 77.82  ? 112 TYR A OH  1 
ATOM   4086 N N   . VAL C 3 113 ? 11.683  24.298  -6.455  1.00 82.23  ? 113 VAL A N   1 
ATOM   4087 C CA  . VAL C 3 113 ? 11.083  24.835  -7.667  1.00 83.80  ? 113 VAL A CA  1 
ATOM   4088 C C   . VAL C 3 113 ? 9.758   24.129  -7.913  1.00 86.41  ? 113 VAL A C   1 
ATOM   4089 O O   . VAL C 3 113 ? 9.699   22.897  -7.925  1.00 86.73  ? 113 VAL A O   1 
ATOM   4090 C CB  . VAL C 3 113 ? 12.007  24.667  -8.887  1.00 83.33  ? 113 VAL A CB  1 
ATOM   4091 C CG1 . VAL C 3 113 ? 11.304  25.164  -10.144 1.00 87.91  ? 113 VAL A CG1 1 
ATOM   4092 C CG2 . VAL C 3 113 ? 13.302  25.425  -8.677  1.00 79.25  ? 113 VAL A CG2 1 
ATOM   4093 N N   . ASN C 3 114 ? 8.704   24.904  -8.140  1.00 87.44  ? 114 ASN A N   1 
ATOM   4094 C CA  . ASN C 3 114 ? 7.401   24.360  -8.496  1.00 92.41  ? 114 ASN A CA  1 
ATOM   4095 C C   . ASN C 3 114 ? 7.122   24.571  -9.987  1.00 95.62  ? 114 ASN A C   1 
ATOM   4096 O O   . ASN C 3 114 ? 7.600   25.531  -10.602 1.00 93.75  ? 114 ASN A O   1 
ATOM   4097 C CB  . ASN C 3 114 ? 6.307   25.013  -7.644  1.00 95.13  ? 114 ASN A CB  1 
ATOM   4098 C CG  . ASN C 3 114 ? 4.925   24.454  -7.928  1.00 102.98 ? 114 ASN A CG  1 
ATOM   4099 O OD1 . ASN C 3 114 ? 4.775   23.285  -8.309  1.00 101.38 ? 114 ASN A OD1 1 
ATOM   4100 N ND2 . ASN C 3 114 ? 3.901   25.273  -7.693  1.00 103.84 ? 114 ASN A ND2 1 
ATOM   4101 N N   . ASN C 3 115 ? 6.357   23.651  -10.577 1.00 98.90  ? 115 ASN A N   1 
ATOM   4102 C CA  . ASN C 3 115 ? 5.948   23.791  -11.969 1.00 104.11 ? 115 ASN A CA  1 
ATOM   4103 C C   . ASN C 3 115 ? 4.509   23.304  -12.101 1.00 107.12 ? 115 ASN A C   1 
ATOM   4104 O O   . ASN C 3 115 ? 4.125   22.322  -11.453 1.00 103.63 ? 115 ASN A O   1 
ATOM   4105 C CB  . ASN C 3 115 ? 6.864   22.999  -12.927 1.00 100.64 ? 115 ASN A CB  1 
ATOM   4106 C CG  . ASN C 3 115 ? 8.343   23.164  -12.617 1.00 98.07  ? 115 ASN A CG  1 
ATOM   4107 O OD1 . ASN C 3 115 ? 9.041   23.984  -13.218 1.00 94.41  ? 115 ASN A OD1 1 
ATOM   4108 N ND2 . ASN C 3 115 ? 8.840   22.337  -11.701 1.00 94.86  ? 115 ASN A ND2 1 
ATOM   4109 N N   . GLU C 3 116 ? 3.718   23.995  -12.930 1.00 112.88 ? 116 GLU A N   1 
ATOM   4110 C CA  . GLU C 3 116 ? 2.315   23.641  -13.137 1.00 116.12 ? 116 GLU A CA  1 
ATOM   4111 C C   . GLU C 3 116 ? 1.765   24.372  -14.360 1.00 121.10 ? 116 GLU A C   1 
ATOM   4112 O O   . GLU C 3 116 ? 2.442   25.196  -14.982 1.00 118.34 ? 116 GLU A O   1 
ATOM   4113 C CB  . GLU C 3 116 ? 1.470   23.969  -11.906 1.00 119.26 ? 116 GLU A CB  1 
ATOM   4114 C CG  . GLU C 3 116 ? 1.591   25.397  -11.402 1.00 120.01 ? 116 GLU A CG  1 
ATOM   4115 C CD  . GLU C 3 116 ? 0.945   25.554  -10.036 1.00 125.36 ? 116 GLU A CD  1 
ATOM   4116 O OE1 . GLU C 3 116 ? -0.072  24.871  -9.794  1.00 132.96 ? 116 GLU A OE1 1 
ATOM   4117 O OE2 . GLU C 3 116 ? 1.440   26.349  -9.208  1.00 123.64 ? 116 GLU A OE2 1 
ATOM   4118 N N   . TYR C 3 117 ? 0.503   24.070  -14.672 1.00 127.89 ? 117 TYR A N   1 
ATOM   4119 C CA  . TYR C 3 117 ? -0.216  24.673  -15.787 1.00 132.07 ? 117 TYR A CA  1 
ATOM   4120 C C   . TYR C 3 117 ? -0.751  26.049  -15.401 1.00 136.24 ? 117 TYR A C   1 
ATOM   4121 O O   . TYR C 3 117 ? -1.261  26.241  -14.292 1.00 136.33 ? 117 TYR A O   1 
ATOM   4122 C CB  . TYR C 3 117 ? -1.388  23.775  -16.191 1.00 138.92 ? 117 TYR A CB  1 
ATOM   4123 C CG  . TYR C 3 117 ? -1.025  22.502  -16.933 1.00 138.12 ? 117 TYR A CG  1 
ATOM   4124 C CD1 . TYR C 3 117 ? -0.191  22.520  -18.047 1.00 132.21 ? 117 TYR A CD1 1 
ATOM   4125 C CD2 . TYR C 3 117 ? -1.503  21.273  -16.494 1.00 141.23 ? 117 TYR A CD2 1 
ATOM   4126 C CE1 . TYR C 3 117 ? 0.130   21.346  -18.717 1.00 129.21 ? 117 TYR A CE1 1 
ATOM   4127 C CE2 . TYR C 3 117 ? -1.176  20.099  -17.147 1.00 138.47 ? 117 TYR A CE2 1 
ATOM   4128 C CZ  . TYR C 3 117 ? -0.359  20.138  -18.256 1.00 133.61 ? 117 TYR A CZ  1 
ATOM   4129 O OH  . TYR C 3 117 ? -0.034  18.969  -18.909 1.00 129.48 ? 117 TYR A OH  1 
ATOM   4130 N N   . ASP C 3 118 ? -0.652  27.008  -16.334 1.00 139.12 ? 118 ASP A N   1 
ATOM   4131 C CA  . ASP C 3 118 ? -1.244  28.327  -16.110 1.00 139.55 ? 118 ASP A CA  1 
ATOM   4132 C C   . ASP C 3 118 ? -2.761  28.285  -16.249 1.00 142.73 ? 118 ASP A C   1 
ATOM   4133 O O   . ASP C 3 118 ? -3.475  28.956  -15.495 1.00 142.78 ? 118 ASP A O   1 
ATOM   4134 C CB  . ASP C 3 118 ? -0.657  29.364  -17.081 1.00 139.97 ? 118 ASP A CB  1 
ATOM   4135 C CG  . ASP C 3 118 ? -0.654  28.894  -18.542 1.00 140.02 ? 118 ASP A CG  1 
ATOM   4136 O OD1 . ASP C 3 118 ? -1.461  28.008  -18.901 1.00 141.17 ? 118 ASP A OD1 1 
ATOM   4137 O OD2 . ASP C 3 118 ? 0.145   29.434  -19.343 1.00 135.44 ? 118 ASP A OD2 1 
ATOM   4138 N N   . GLU C 3 119 ? -3.259  27.507  -17.208 1.00 145.03 ? 119 GLU A N   1 
ATOM   4139 C CA  . GLU C 3 119 ? -4.691  27.402  -17.444 1.00 147.43 ? 119 GLU A CA  1 
ATOM   4140 C C   . GLU C 3 119 ? -5.392  26.821  -16.219 1.00 148.77 ? 119 GLU A C   1 
ATOM   4141 O O   . GLU C 3 119 ? -4.849  25.961  -15.520 1.00 151.25 ? 119 GLU A O   1 
ATOM   4142 C CB  . GLU C 3 119 ? -4.951  26.535  -18.679 1.00 149.12 ? 119 GLU A CB  1 
ATOM   4143 C CG  . GLU C 3 119 ? -6.256  26.821  -19.405 1.00 150.67 ? 119 GLU A CG  1 
ATOM   4144 C CD  . GLU C 3 119 ? -6.623  28.285  -19.393 1.00 150.01 ? 119 GLU A CD  1 
ATOM   4145 O OE1 . GLU C 3 119 ? -7.756  28.600  -18.974 1.00 150.17 ? 119 GLU A OE1 1 
ATOM   4146 O OE2 . GLU C 3 119 ? -5.794  29.114  -19.830 1.00 150.25 ? 119 GLU A OE2 1 
ATOM   4147 N N   . GLU C 3 120 ? -6.604  27.311  -15.951 1.00 151.75 ? 120 GLU A N   1 
ATOM   4148 C CA  . GLU C 3 120 ? -7.338  26.888  -14.761 1.00 151.74 ? 120 GLU A CA  1 
ATOM   4149 C C   . GLU C 3 120 ? -7.888  25.477  -14.921 1.00 159.71 ? 120 GLU A C   1 
ATOM   4150 O O   . GLU C 3 120 ? -7.628  24.598  -14.090 1.00 159.53 ? 120 GLU A O   1 
ATOM   4151 C CB  . GLU C 3 120 ? -8.464  27.878  -14.478 1.00 146.13 ? 120 GLU A CB  1 
ATOM   4152 C CG  . GLU C 3 120 ? -7.972  29.299  -14.429 1.00 145.05 ? 120 GLU A CG  1 
ATOM   4153 C CD  . GLU C 3 120 ? -7.209  29.579  -13.156 1.00 139.60 ? 120 GLU A CD  1 
ATOM   4154 O OE1 . GLU C 3 120 ? -5.994  29.276  -13.101 1.00 140.87 ? 120 GLU A OE1 1 
ATOM   4155 O OE2 . GLU C 3 120 ? -7.830  30.116  -12.214 1.00 131.81 ? 120 GLU A OE2 1 
ATOM   4156 N N   . GLU C 3 121 ? -8.670  25.252  -15.981 1.00 168.51 ? 121 GLU A N   1 
ATOM   4157 C CA  . GLU C 3 121 ? -9.216  23.925  -16.257 1.00 170.96 ? 121 GLU A CA  1 
ATOM   4158 C C   . GLU C 3 121 ? -8.096  22.903  -16.417 1.00 170.00 ? 121 GLU A C   1 
ATOM   4159 O O   . GLU C 3 121 ? -8.105  21.850  -15.770 1.00 169.56 ? 121 GLU A O   1 
ATOM   4160 C CB  . GLU C 3 121 ? -10.104 23.993  -17.508 1.00 171.32 ? 121 GLU A CB  1 
ATOM   4161 C CG  . GLU C 3 121 ? -10.595 22.675  -18.147 1.00 176.23 ? 121 GLU A CG  1 
ATOM   4162 C CD  . GLU C 3 121 ? -10.789 21.520  -17.171 1.00 177.13 ? 121 GLU A CD  1 
ATOM   4163 O OE1 . GLU C 3 121 ? -9.963  20.582  -17.188 1.00 175.56 ? 121 GLU A OE1 1 
ATOM   4164 O OE2 . GLU C 3 121 ? -11.757 21.552  -16.383 1.00 182.07 ? 121 GLU A OE2 1 
ATOM   4165 N N   . LEU C 3 122 ? -7.101  23.218  -17.252 1.00 161.48 ? 122 LEU A N   1 
ATOM   4166 C CA  . LEU C 3 122 ? -5.975  22.314  -17.456 1.00 157.98 ? 122 LEU A CA  1 
ATOM   4167 C C   . LEU C 3 122 ? -5.345  21.892  -16.139 1.00 158.17 ? 122 LEU A C   1 
ATOM   4168 O O   . LEU C 3 122 ? -4.797  20.789  -16.034 1.00 157.14 ? 122 LEU A O   1 
ATOM   4169 C CB  . LEU C 3 122 ? -4.929  22.983  -18.339 1.00 151.95 ? 122 LEU A CB  1 
ATOM   4170 C CG  . LEU C 3 122 ? -4.444  22.167  -19.528 1.00 149.96 ? 122 LEU A CG  1 
ATOM   4171 C CD1 . LEU C 3 122 ? -5.616  21.499  -20.241 1.00 150.42 ? 122 LEU A CD1 1 
ATOM   4172 C CD2 . LEU C 3 122 ? -3.667  23.069  -20.466 1.00 145.15 ? 122 LEU A CD2 1 
ATOM   4173 N N   . ARG C 3 123 ? -5.416  22.752  -15.124 1.00 162.20 ? 123 ARG A N   1 
ATOM   4174 C CA  . ARG C 3 123 ? -4.924  22.385  -13.804 1.00 163.14 ? 123 ARG A CA  1 
ATOM   4175 C C   . ARG C 3 123 ? -5.887  21.442  -13.084 1.00 166.29 ? 123 ARG A C   1 
ATOM   4176 O O   . ARG C 3 123 ? -5.444  20.520  -12.389 1.00 167.78 ? 123 ARG A O   1 
ATOM   4177 C CB  . ARG C 3 123 ? -4.652  23.652  -12.987 1.00 161.75 ? 123 ARG A CB  1 
ATOM   4178 C CG  . ARG C 3 123 ? -3.628  23.449  -11.886 1.00 159.62 ? 123 ARG A CG  1 
ATOM   4179 C CD  . ARG C 3 123 ? -4.043  24.142  -10.587 1.00 160.69 ? 123 ARG A CD  1 
ATOM   4180 N NE  . ARG C 3 123 ? -2.895  24.472  -9.744  1.00 156.78 ? 123 ARG A NE  1 
ATOM   4181 C CZ  . ARG C 3 123 ? -2.974  25.075  -8.561  1.00 154.92 ? 123 ARG A CZ  1 
ATOM   4182 N NH1 . ARG C 3 123 ? -4.132  25.504  -8.080  1.00 157.08 ? 123 ARG A NH1 1 
ATOM   4183 N NH2 . ARG C 3 123 ? -1.866  25.252  -7.842  1.00 150.88 ? 123 ARG A NH2 1 
ATOM   4184 N N   . GLU C 3 124 ? -7.201  21.632  -13.257 1.00 161.21 ? 124 GLU A N   1 
ATOM   4185 C CA  . GLU C 3 124 ? -8.181  20.734  -12.641 1.00 157.36 ? 124 GLU A CA  1 
ATOM   4186 C C   . GLU C 3 124 ? -8.170  19.359  -13.304 1.00 158.60 ? 124 GLU A C   1 
ATOM   4187 O O   . GLU C 3 124 ? -8.137  18.328  -12.622 1.00 156.36 ? 124 GLU A O   1 
ATOM   4188 C CB  . GLU C 3 124 ? -9.578  21.357  -12.717 1.00 153.81 ? 124 GLU A CB  1 
ATOM   4189 C CG  . GLU C 3 124 ? -10.003 22.129  -11.473 1.00 142.96 ? 124 GLU A CG  1 
ATOM   4190 C CD  . GLU C 3 124 ? -10.862 21.312  -10.527 1.00 133.79 ? 124 GLU A CD  1 
ATOM   4191 O OE1 . GLU C 3 124 ? -10.302 20.576  -9.685  1.00 129.83 ? 124 GLU A OE1 1 
ATOM   4192 O OE2 . GLU C 3 124 ? -12.105 21.422  -10.626 1.00 129.05 ? 124 GLU A OE2 1 
ATOM   4193 N N   . ASN C 3 125 ? -8.216  19.325  -14.634 1.00 159.61 ? 125 ASN A N   1 
ATOM   4194 C CA  . ASN C 3 125 ? -8.126  18.084  -15.396 1.00 158.62 ? 125 ASN A CA  1 
ATOM   4195 C C   . ASN C 3 125 ? -6.979  18.209  -16.391 1.00 157.60 ? 125 ASN A C   1 
ATOM   4196 O O   . ASN C 3 125 ? -7.016  19.093  -17.268 1.00 157.71 ? 125 ASN A O   1 
ATOM   4197 C CB  . ASN C 3 125 ? -9.441  17.775  -16.119 1.00 160.73 ? 125 ASN A CB  1 
ATOM   4198 C CG  . ASN C 3 125 ? -10.294 16.760  -15.379 1.00 158.69 ? 125 ASN A CG  1 
ATOM   4199 O OD1 . ASN C 3 125 ? -10.281 15.573  -15.701 1.00 156.54 ? 125 ASN A OD1 1 
ATOM   4200 N ND2 . ASN C 3 125 ? -11.049 17.226  -14.390 1.00 160.62 ? 125 ASN A ND2 1 
ATOM   4201 N N   . PRO C 3 126 ? -5.957  17.361  -16.306 1.00 156.52 ? 126 PRO A N   1 
ATOM   4202 C CA  . PRO C 3 126 ? -4.759  17.547  -17.126 1.00 155.30 ? 126 PRO A CA  1 
ATOM   4203 C C   . PRO C 3 126 ? -5.007  17.135  -18.563 1.00 156.39 ? 126 PRO A C   1 
ATOM   4204 O O   . PRO C 3 126 ? -5.890  16.309  -18.836 1.00 155.40 ? 126 PRO A O   1 
ATOM   4205 C CB  . PRO C 3 126 ? -3.742  16.617  -16.456 1.00 153.01 ? 126 PRO A CB  1 
ATOM   4206 C CG  . PRO C 3 126 ? -4.592  15.483  -15.967 1.00 148.51 ? 126 PRO A CG  1 
ATOM   4207 C CD  . PRO C 3 126 ? -5.874  16.137  -15.486 1.00 151.35 ? 126 PRO A CD  1 
ATOM   4208 N N   . PRO C 3 127 ? -4.253  17.688  -19.510 1.00 163.88 ? 127 PRO A N   1 
ATOM   4209 C CA  . PRO C 3 127 ? -4.223  17.109  -20.856 1.00 163.74 ? 127 PRO A CA  1 
ATOM   4210 C C   . PRO C 3 127 ? -3.462  15.793  -20.840 1.00 162.42 ? 127 PRO A C   1 
ATOM   4211 O O   . PRO C 3 127 ? -2.610  15.546  -19.983 1.00 160.94 ? 127 PRO A O   1 
ATOM   4212 C CB  . PRO C 3 127 ? -3.495  18.167  -21.694 1.00 161.17 ? 127 PRO A CB  1 
ATOM   4213 C CG  . PRO C 3 127 ? -2.668  18.924  -20.716 1.00 158.24 ? 127 PRO A CG  1 
ATOM   4214 C CD  . PRO C 3 127 ? -3.395  18.878  -19.394 1.00 160.75 ? 127 PRO A CD  1 
ATOM   4215 N N   . ALA C 3 128 ? -3.795  14.932  -21.806 1.00 153.54 ? 128 ALA A N   1 
ATOM   4216 C CA  . ALA C 3 128 ? -3.162  13.618  -21.878 1.00 150.33 ? 128 ALA A CA  1 
ATOM   4217 C C   . ALA C 3 128 ? -1.645  13.728  -21.959 1.00 143.76 ? 128 ALA A C   1 
ATOM   4218 O O   . ALA C 3 128 ? -0.927  12.866  -21.435 1.00 140.54 ? 128 ALA A O   1 
ATOM   4219 C CB  . ALA C 3 128 ? -3.709  12.839  -23.079 1.00 150.14 ? 128 ALA A CB  1 
ATOM   4220 N N   . LYS C 3 129 ? -1.144  14.790  -22.587 1.00 141.76 ? 129 LYS A N   1 
ATOM   4221 C CA  . LYS C 3 129 ? 0.277   15.000  -22.814 1.00 131.69 ? 129 LYS A CA  1 
ATOM   4222 C C   . LYS C 3 129 ? 0.671   16.345  -22.226 1.00 123.56 ? 129 LYS A C   1 
ATOM   4223 O O   . LYS C 3 129 ? -0.100  17.309  -22.286 1.00 127.72 ? 129 LYS A O   1 
ATOM   4224 C CB  . LYS C 3 129 ? 0.599   14.955  -24.319 1.00 129.35 ? 129 LYS A CB  1 
ATOM   4225 C CG  . LYS C 3 129 ? 0.427   13.574  -24.966 1.00 132.26 ? 129 LYS A CG  1 
ATOM   4226 C CD  . LYS C 3 129 ? 1.767   12.926  -25.291 1.00 130.56 ? 129 LYS A CD  1 
ATOM   4227 C CE  . LYS C 3 129 ? 2.120   11.846  -24.285 1.00 125.98 ? 129 LYS A CE  1 
ATOM   4228 N NZ  . LYS C 3 129 ? 3.561   11.500  -24.358 1.00 117.31 ? 129 LYS A NZ  1 
ATOM   4229 N N   . VAL C 3 130 ? 1.868   16.415  -21.656 1.00 119.18 ? 130 VAL A N   1 
ATOM   4230 C CA  . VAL C 3 130 ? 2.280   17.649  -21.003 1.00 115.42 ? 130 VAL A CA  1 
ATOM   4231 C C   . VAL C 3 130 ? 2.585   18.688  -22.071 1.00 112.87 ? 130 VAL A C   1 
ATOM   4232 O O   . VAL C 3 130 ? 3.459   18.489  -22.921 1.00 108.44 ? 130 VAL A O   1 
ATOM   4233 C CB  . VAL C 3 130 ? 3.488   17.415  -20.087 1.00 110.56 ? 130 VAL A CB  1 
ATOM   4234 C CG1 . VAL C 3 130 ? 3.819   18.686  -19.319 1.00 109.11 ? 130 VAL A CG1 1 
ATOM   4235 C CG2 . VAL C 3 130 ? 3.217   16.264  -19.128 1.00 105.01 ? 130 VAL A CG2 1 
ATOM   4236 N N   . GLN C 3 131 ? 1.850   19.795  -22.041 1.00 110.15 ? 131 GLN A N   1 
ATOM   4237 C CA  . GLN C 3 131 ? 2.082   20.912  -22.955 1.00 113.76 ? 131 GLN A CA  1 
ATOM   4238 C C   . GLN C 3 131 ? 3.028   21.882  -22.259 1.00 113.15 ? 131 GLN A C   1 
ATOM   4239 O O   . GLN C 3 131 ? 2.601   22.784  -21.539 1.00 117.29 ? 131 GLN A O   1 
ATOM   4240 C CB  . GLN C 3 131 ? 0.767   21.582  -23.346 1.00 119.19 ? 131 GLN A CB  1 
ATOM   4241 C CG  . GLN C 3 131 ? 0.275   21.283  -24.772 1.00 119.26 ? 131 GLN A CG  1 
ATOM   4242 C CD  . GLN C 3 131 ? -1.007  22.030  -25.131 1.00 118.07 ? 131 GLN A CD  1 
ATOM   4243 O OE1 . GLN C 3 131 ? -1.404  22.970  -24.444 1.00 120.44 ? 131 GLN A OE1 1 
ATOM   4244 N NE2 . GLN C 3 131 ? -1.655  21.613  -26.217 1.00 117.66 ? 131 GLN A NE2 1 
ATOM   4245 N N   . VAL C 3 132 ? 4.332   21.702  -22.499 1.00 114.21 ? 132 VAL A N   1 
ATOM   4246 C CA  . VAL C 3 132 ? 5.365   22.519  -21.860 1.00 112.93 ? 132 VAL A CA  1 
ATOM   4247 C C   . VAL C 3 132 ? 5.112   24.011  -22.058 1.00 117.39 ? 132 VAL A C   1 
ATOM   4248 O O   . VAL C 3 132 ? 5.511   24.833  -21.223 1.00 115.47 ? 132 VAL A O   1 
ATOM   4249 C CB  . VAL C 3 132 ? 6.749   22.103  -22.397 1.00 102.00 ? 132 VAL A CB  1 
ATOM   4250 C CG1 . VAL C 3 132 ? 6.707   21.999  -23.898 1.00 107.87 ? 132 VAL A CG1 1 
ATOM   4251 C CG2 . VAL C 3 132 ? 7.823   23.089  -21.975 1.00 102.42 ? 132 VAL A CG2 1 
ATOM   4252 N N   . ASP C 3 133 ? 4.439   24.389  -23.151 1.00 120.54 ? 133 ASP A N   1 
ATOM   4253 C CA  . ASP C 3 133 ? 4.196   25.805  -23.424 1.00 121.76 ? 133 ASP A CA  1 
ATOM   4254 C C   . ASP C 3 133 ? 3.330   26.454  -22.350 1.00 121.95 ? 133 ASP A C   1 
ATOM   4255 O O   . ASP C 3 133 ? 3.444   27.662  -22.109 1.00 122.06 ? 133 ASP A O   1 
ATOM   4256 C CB  . ASP C 3 133 ? 3.545   25.980  -24.800 1.00 123.70 ? 133 ASP A CB  1 
ATOM   4257 C CG  . ASP C 3 133 ? 2.571   24.860  -25.141 1.00 123.45 ? 133 ASP A CG  1 
ATOM   4258 O OD1 . ASP C 3 133 ? 1.950   24.922  -26.225 1.00 126.30 ? 133 ASP A OD1 1 
ATOM   4259 O OD2 . ASP C 3 133 ? 2.443   23.909  -24.343 1.00 120.57 ? 133 ASP A OD2 1 
ATOM   4260 N N   . HIS C 3 134 ? 2.460   25.680  -21.705 1.00 128.81 ? 134 HIS A N   1 
ATOM   4261 C CA  . HIS C 3 134 ? 1.555   26.192  -20.686 1.00 129.30 ? 134 HIS A CA  1 
ATOM   4262 C C   . HIS C 3 134 ? 2.010   25.839  -19.273 1.00 127.75 ? 134 HIS A C   1 
ATOM   4263 O O   . HIS C 3 134 ? 1.250   26.030  -18.317 1.00 130.66 ? 134 HIS A O   1 
ATOM   4264 C CB  . HIS C 3 134 ? 0.133   25.675  -20.934 1.00 133.45 ? 134 HIS A CB  1 
ATOM   4265 C CG  . HIS C 3 134 ? -0.527  26.257  -22.151 1.00 135.54 ? 134 HIS A CG  1 
ATOM   4266 N ND1 . HIS C 3 134 ? 0.181   26.796  -23.206 1.00 133.04 ? 134 HIS A ND1 1 
ATOM   4267 C CD2 . HIS C 3 134 ? -1.836  26.376  -22.480 1.00 139.13 ? 134 HIS A CD2 1 
ATOM   4268 C CE1 . HIS C 3 134 ? -0.662  27.221  -24.131 1.00 133.31 ? 134 HIS A CE1 1 
ATOM   4269 N NE2 . HIS C 3 134 ? -1.892  26.979  -23.715 1.00 138.52 ? 134 HIS A NE2 1 
ATOM   4270 N N   . ILE C 3 135 ? 3.225   25.320  -19.123 1.00 119.25 ? 135 ILE A N   1 
ATOM   4271 C CA  . ILE C 3 135 ? 3.816   25.122  -17.807 1.00 114.29 ? 135 ILE A CA  1 
ATOM   4272 C C   . ILE C 3 135 ? 4.475   26.418  -17.359 1.00 109.86 ? 135 ILE A C   1 
ATOM   4273 O O   . ILE C 3 135 ? 5.114   27.116  -18.158 1.00 108.12 ? 135 ILE A O   1 
ATOM   4274 C CB  . ILE C 3 135 ? 4.838   23.974  -17.826 1.00 111.34 ? 135 ILE A CB  1 
ATOM   4275 C CG1 . ILE C 3 135 ? 4.167   22.633  -17.566 1.00 110.95 ? 135 ILE A CG1 1 
ATOM   4276 C CG2 . ILE C 3 135 ? 5.858   24.175  -16.739 1.00 108.07 ? 135 ILE A CG2 1 
ATOM   4277 C CD1 . ILE C 3 135 ? 3.361   22.153  -18.687 1.00 114.87 ? 135 ILE A CD1 1 
ATOM   4278 N N   . VAL C 3 136 ? 4.340   26.736  -16.072 1.00 109.02 ? 136 VAL A N   1 
ATOM   4279 C CA  . VAL C 3 136 ? 4.998   27.893  -15.486 1.00 103.12 ? 136 VAL A CA  1 
ATOM   4280 C C   . VAL C 3 136 ? 5.729   27.466  -14.218 1.00 100.73 ? 136 VAL A C   1 
ATOM   4281 O O   . VAL C 3 136 ? 5.191   26.720  -13.391 1.00 101.44 ? 136 VAL A O   1 
ATOM   4282 C CB  . VAL C 3 136 ? 3.988   29.022  -15.208 1.00 99.61  ? 136 VAL A CB  1 
ATOM   4283 C CG1 . VAL C 3 136 ? 2.750   28.469  -14.513 1.00 111.76 ? 136 VAL A CG1 1 
ATOM   4284 C CG2 . VAL C 3 136 ? 4.639   30.110  -14.392 1.00 96.77  ? 136 VAL A CG2 1 
ATOM   4285 N N   . ARG C 3 137 ? 6.961   27.944  -14.072 1.00 96.41  ? 137 ARG A N   1 
ATOM   4286 C CA  . ARG C 3 137 ? 7.862   27.561  -12.998 1.00 93.27  ? 137 ARG A CA  1 
ATOM   4287 C C   . ARG C 3 137 ? 8.001   28.685  -11.977 1.00 90.49  ? 137 ARG A C   1 
ATOM   4288 O O   . ARG C 3 137 ? 7.889   29.868  -12.312 1.00 91.03  ? 137 ARG A O   1 
ATOM   4289 C CB  . ARG C 3 137 ? 9.231   27.192  -13.574 1.00 91.65  ? 137 ARG A CB  1 
ATOM   4290 C CG  . ARG C 3 137 ? 10.007  28.398  -14.037 1.00 88.49  ? 137 ARG A CG  1 
ATOM   4291 C CD  . ARG C 3 137 ? 11.489  28.303  -13.815 1.00 86.51  ? 137 ARG A CD  1 
ATOM   4292 N NE  . ARG C 3 137 ? 12.227  29.027  -14.844 1.00 94.89  ? 137 ARG A NE  1 
ATOM   4293 C CZ  . ARG C 3 137 ? 13.510  29.345  -14.745 1.00 95.67  ? 137 ARG A CZ  1 
ATOM   4294 N NH1 . ARG C 3 137 ? 14.206  29.038  -13.663 1.00 91.27  ? 137 ARG A NH1 1 
ATOM   4295 N NH2 . ARG C 3 137 ? 14.095  30.028  -15.733 1.00 92.25  ? 137 ARG A NH2 1 
ATOM   4296 N N   . ASN C 3 138 ? 8.259   28.293  -10.726 1.00 88.92  ? 138 ASN A N   1 
ATOM   4297 C CA  . ASN C 3 138 ? 8.340   29.208  -9.585  1.00 87.91  ? 138 ASN A CA  1 
ATOM   4298 C C   . ASN C 3 138 ? 9.471   28.748  -8.665  1.00 88.62  ? 138 ASN A C   1 
ATOM   4299 O O   . ASN C 3 138 ? 9.364   27.703  -8.004  1.00 86.94  ? 138 ASN A O   1 
ATOM   4300 C CB  . ASN C 3 138 ? 7.005   29.266  -8.836  1.00 87.11  ? 138 ASN A CB  1 
ATOM   4301 C CG  . ASN C 3 138 ? 7.083   30.082  -7.554  1.00 88.03  ? 138 ASN A CG  1 
ATOM   4302 O OD1 . ASN C 3 138 ? 7.946   30.949  -7.409  1.00 92.27  ? 138 ASN A OD1 1 
ATOM   4303 N ND2 . ASN C 3 138 ? 6.160   29.825  -6.627  1.00 86.82  ? 138 ASN A ND2 1 
ATOM   4304 N N   . ILE C 3 139 ? 10.556  29.529  -8.629  1.00 85.13  ? 139 ILE A N   1 
ATOM   4305 C CA  . ILE C 3 139 ? 11.736  29.214  -7.830  1.00 84.66  ? 139 ILE A CA  1 
ATOM   4306 C C   . ILE C 3 139 ? 11.529  29.785  -6.434  1.00 91.86  ? 139 ILE A C   1 
ATOM   4307 O O   . ILE C 3 139 ? 11.171  30.963  -6.278  1.00 91.52  ? 139 ILE A O   1 
ATOM   4308 C CB  . ILE C 3 139 ? 13.010  29.796  -8.471  1.00 82.92  ? 139 ILE A CB  1 
ATOM   4309 C CG1 . ILE C 3 139 ? 13.448  29.003  -9.692  1.00 82.90  ? 139 ILE A CG1 1 
ATOM   4310 C CG2 . ILE C 3 139 ? 14.152  29.839  -7.474  1.00 83.53  ? 139 ILE A CG2 1 
ATOM   4311 C CD1 . ILE C 3 139 ? 14.884  29.262  -10.048 1.00 82.51  ? 139 ILE A CD1 1 
ATOM   4312 N N   . LEU C 3 140 ? 11.751  28.961  -5.410  1.00 89.54  ? 140 LEU A N   1 
ATOM   4313 C CA  . LEU C 3 140 ? 11.700  29.447  -4.031  1.00 88.39  ? 140 LEU A CA  1 
ATOM   4314 C C   . LEU C 3 140 ? 13.086  29.946  -3.609  1.00 85.92  ? 140 LEU A C   1 
ATOM   4315 O O   . LEU C 3 140 ? 13.802  29.328  -2.819  1.00 86.72  ? 140 LEU A O   1 
ATOM   4316 C CB  . LEU C 3 140 ? 11.173  28.357  -3.113  1.00 90.58  ? 140 LEU A CB  1 
ATOM   4317 C CG  . LEU C 3 140 ? 10.940  28.841  -1.691  1.00 90.90  ? 140 LEU A CG  1 
ATOM   4318 C CD1 . LEU C 3 140 ? 9.490   29.187  -1.482  1.00 94.88  ? 140 LEU A CD1 1 
ATOM   4319 C CD2 . LEU C 3 140 ? 11.368  27.730  -0.751  1.00 94.72  ? 140 LEU A CD2 1 
ATOM   4320 N N   . ALA C 3 141 ? 13.454  31.108  -4.154  1.00 88.43  ? 141 ALA A N   1 
ATOM   4321 C CA  . ALA C 3 141 ? 14.804  31.641  -4.002  1.00 89.36  ? 141 ALA A CA  1 
ATOM   4322 C C   . ALA C 3 141 ? 14.978  32.498  -2.760  1.00 85.05  ? 141 ALA A C   1 
ATOM   4323 O O   . ALA C 3 141 ? 16.114  32.867  -2.431  1.00 82.45  ? 141 ALA A O   1 
ATOM   4324 C CB  . ALA C 3 141 ? 15.189  32.462  -5.230  1.00 90.81  ? 141 ALA A CB  1 
ATOM   4325 N N   . GLU C 3 142 ? 13.872  32.826  -2.093  1.00 95.33  ? 142 GLU A N   1 
ATOM   4326 C CA  . GLU C 3 142 ? 13.841  33.495  -0.802  1.00 95.73  ? 142 GLU A CA  1 
ATOM   4327 C C   . GLU C 3 142 ? 14.255  32.569  0.340   1.00 93.59  ? 142 GLU A C   1 
ATOM   4328 O O   . GLU C 3 142 ? 14.471  33.048  1.460   1.00 94.20  ? 142 GLU A O   1 
ATOM   4329 C CB  . GLU C 3 142 ? 12.421  34.032  -0.549  1.00 97.03  ? 142 GLU A CB  1 
ATOM   4330 C CG  . GLU C 3 142 ? 11.323  32.944  -0.696  1.00 97.98  ? 142 GLU A CG  1 
ATOM   4331 C CD  . GLU C 3 142 ? 10.548  32.982  -2.022  1.00 104.08 ? 142 GLU A CD  1 
ATOM   4332 O OE1 . GLU C 3 142 ? 11.172  33.104  -3.102  1.00 100.07 ? 142 GLU A OE1 1 
ATOM   4333 O OE2 . GLU C 3 142 ? 9.307   32.822  -1.986  1.00 109.90 ? 142 GLU A OE2 1 
ATOM   4334 N N   . LYS C 3 143 ? 14.353  31.262  0.099   1.00 80.43  ? 143 LYS A N   1 
ATOM   4335 C CA  . LYS C 3 143 ? 14.731  30.302  1.133   1.00 79.53  ? 143 LYS A CA  1 
ATOM   4336 C C   . LYS C 3 143 ? 15.779  29.329  0.596   1.00 77.61  ? 143 LYS A C   1 
ATOM   4337 O O   . LYS C 3 143 ? 15.543  28.110  0.521   1.00 75.85  ? 143 LYS A O   1 
ATOM   4338 C CB  . LYS C 3 143 ? 13.501  29.565  1.678   1.00 80.16  ? 143 LYS A CB  1 
ATOM   4339 C CG  . LYS C 3 143 ? 12.703  30.397  2.713   1.00 79.49  ? 143 LYS A CG  1 
ATOM   4340 C CD  . LYS C 3 143 ? 11.206  30.450  2.416   1.00 81.69  ? 143 LYS A CD  1 
ATOM   4341 C CE  . LYS C 3 143 ? 10.426  29.355  3.118   1.00 77.03  ? 143 LYS A CE  1 
ATOM   4342 N NZ  . LYS C 3 143 ? 9.007   29.248  2.655   1.00 77.95  ? 143 LYS A NZ  1 
ATOM   4343 N N   . PRO C 3 144 ? 16.974  29.832  0.261   1.00 76.41  ? 144 PRO A N   1 
ATOM   4344 C CA  . PRO C 3 144 ? 18.065  28.941  -0.169  1.00 75.15  ? 144 PRO A CA  1 
ATOM   4345 C C   . PRO C 3 144 ? 18.334  27.809  0.822   1.00 73.19  ? 144 PRO A C   1 
ATOM   4346 O O   . PRO C 3 144 ? 18.133  27.949  2.029   1.00 73.00  ? 144 PRO A O   1 
ATOM   4347 C CB  . PRO C 3 144 ? 19.268  29.890  -0.270  1.00 76.46  ? 144 PRO A CB  1 
ATOM   4348 C CG  . PRO C 3 144 ? 18.912  31.038  0.592   1.00 77.88  ? 144 PRO A CG  1 
ATOM   4349 C CD  . PRO C 3 144 ? 17.440  31.221  0.408   1.00 78.34  ? 144 PRO A CD  1 
ATOM   4350 N N   . ARG C 3 145 ? 18.780  26.668  0.301   1.00 71.82  ? 145 ARG A N   1 
ATOM   4351 C CA  . ARG C 3 145 ? 19.290  25.572  1.121   1.00 70.12  ? 145 ARG A CA  1 
ATOM   4352 C C   . ARG C 3 145 ? 20.752  25.388  0.752   1.00 69.97  ? 145 ARG A C   1 
ATOM   4353 O O   . ARG C 3 145 ? 21.064  24.939  -0.345  1.00 69.78  ? 145 ARG A O   1 
ATOM   4354 C CB  . ARG C 3 145 ? 18.468  24.300  0.920   1.00 68.74  ? 145 ARG A CB  1 
ATOM   4355 C CG  . ARG C 3 145 ? 16.960  24.558  0.848   1.00 69.34  ? 145 ARG A CG  1 
ATOM   4356 C CD  . ARG C 3 145 ? 16.371  24.643  2.233   1.00 69.11  ? 145 ARG A CD  1 
ATOM   4357 N NE  . ARG C 3 145 ? 15.048  24.039  2.346   1.00 68.78  ? 145 ARG A NE  1 
ATOM   4358 C CZ  . ARG C 3 145 ? 13.900  24.706  2.385   1.00 69.93  ? 145 ARG A CZ  1 
ATOM   4359 N NH1 . ARG C 3 145 ? 13.857  26.030  2.295   1.00 74.66  ? 145 ARG A NH1 1 
ATOM   4360 N NH2 . ARG C 3 145 ? 12.767  24.031  2.552   1.00 69.64  ? 145 ARG A NH2 1 
ATOM   4361 N N   . VAL C 3 146 ? 21.648  25.755  1.649   1.00 70.23  ? 146 VAL A N   1 
ATOM   4362 C CA  . VAL C 3 146 ? 23.037  26.029  1.311   1.00 70.87  ? 146 VAL A CA  1 
ATOM   4363 C C   . VAL C 3 146 ? 23.924  24.968  1.927   1.00 69.55  ? 146 VAL A C   1 
ATOM   4364 O O   . VAL C 3 146 ? 23.752  24.594  3.087   1.00 68.82  ? 146 VAL A O   1 
ATOM   4365 C CB  . VAL C 3 146 ? 23.468  27.427  1.801   1.00 72.72  ? 146 VAL A CB  1 
ATOM   4366 C CG1 . VAL C 3 146 ? 24.969  27.624  1.647   1.00 73.46  ? 146 VAL A CG1 1 
ATOM   4367 C CG2 . VAL C 3 146 ? 22.684  28.510  1.100   1.00 74.26  ? 146 VAL A CG2 1 
ATOM   4368 N N   . THR C 3 147 ? 24.893  24.508  1.158   1.00 69.40  ? 147 THR A N   1 
ATOM   4369 C CA  . THR C 3 147 ? 25.907  23.571  1.622   1.00 68.47  ? 147 THR A CA  1 
ATOM   4370 C C   . THR C 3 147 ? 27.264  24.151  1.277   1.00 69.78  ? 147 THR A C   1 
ATOM   4371 O O   . THR C 3 147 ? 27.478  24.567  0.137   1.00 70.64  ? 147 THR A O   1 
ATOM   4372 C CB  . THR C 3 147 ? 25.738  22.200  0.952   1.00 66.95  ? 147 THR A CB  1 
ATOM   4373 O OG1 . THR C 3 147 ? 24.353  21.843  0.913   1.00 66.19  ? 147 THR A OG1 1 
ATOM   4374 C CG2 . THR C 3 147 ? 26.547  21.156  1.653   1.00 65.92  ? 147 THR A CG2 1 
ATOM   4375 N N   . ARG C 3 148 ? 28.178  24.175  2.233   1.00 70.09  ? 148 ARG A N   1 
ATOM   4376 C CA  . ARG C 3 148 ? 29.498  24.722  1.976   1.00 71.56  ? 148 ARG A CA  1 
ATOM   4377 C C   . ARG C 3 148 ? 30.532  23.629  2.185   1.00 70.78  ? 148 ARG A C   1 
ATOM   4378 O O   . ARG C 3 148 ? 30.416  22.836  3.114   1.00 69.64  ? 148 ARG A O   1 
ATOM   4379 C CB  . ARG C 3 148 ? 29.782  25.933  2.883   1.00 73.26  ? 148 ARG A CB  1 
ATOM   4380 C CG  . ARG C 3 148 ? 28.906  27.164  2.585   1.00 74.48  ? 148 ARG A CG  1 
ATOM   4381 C CD  . ARG C 3 148 ? 29.151  28.385  3.511   1.00 76.33  ? 148 ARG A CD  1 
ATOM   4382 N NE  . ARG C 3 148 ? 30.458  28.363  4.155   1.00 77.15  ? 148 ARG A NE  1 
ATOM   4383 C CZ  . ARG C 3 148 ? 31.331  29.358  4.118   1.00 79.36  ? 148 ARG A CZ  1 
ATOM   4384 N NH1 . ARG C 3 148 ? 31.096  30.456  3.418   1.00 80.98  ? 148 ARG A NH1 1 
ATOM   4385 N NH2 . ARG C 3 148 ? 32.486  29.233  4.764   1.00 80.13  ? 148 ARG A NH2 1 
ATOM   4386 N N   . PHE C 3 149 ? 31.525  23.568  1.302   1.00 71.47  ? 149 PHE A N   1 
ATOM   4387 C CA  . PHE C 3 149 ? 32.592  22.569  1.370   1.00 75.13  ? 149 PHE A CA  1 
ATOM   4388 C C   . PHE C 3 149 ? 33.936  23.272  1.392   1.00 78.94  ? 149 PHE A C   1 
ATOM   4389 O O   . PHE C 3 149 ? 34.222  24.087  0.510   1.00 79.85  ? 149 PHE A O   1 
ATOM   4390 C CB  . PHE C 3 149 ? 32.578  21.586  0.180   1.00 69.93  ? 149 PHE A CB  1 
ATOM   4391 C CG  . PHE C 3 149 ? 31.215  21.127  -0.216  1.00 68.52  ? 149 PHE A CG  1 
ATOM   4392 C CD1 . PHE C 3 149 ? 30.699  19.958  0.284   1.00 66.82  ? 149 PHE A CD1 1 
ATOM   4393 C CD2 . PHE C 3 149 ? 30.442  21.881  -1.088  1.00 69.09  ? 149 PHE A CD2 1 
ATOM   4394 C CE1 . PHE C 3 149 ? 29.441  19.542  -0.080  1.00 65.76  ? 149 PHE A CE1 1 
ATOM   4395 C CE2 . PHE C 3 149 ? 29.176  21.467  -1.461  1.00 68.02  ? 149 PHE A CE2 1 
ATOM   4396 C CZ  . PHE C 3 149 ? 28.679  20.296  -0.956  1.00 66.37  ? 149 PHE A CZ  1 
ATOM   4397 N N   . ASN C 3 150 ? 34.772  22.930  2.369   1.00 82.05  ? 150 ASN A N   1 
ATOM   4398 C CA  . ASN C 3 150 ? 36.083  23.551  2.491   1.00 83.97  ? 150 ASN A CA  1 
ATOM   4399 C C   . ASN C 3 150 ? 37.027  22.921  1.478   1.00 90.77  ? 150 ASN A C   1 
ATOM   4400 O O   . ASN C 3 150 ? 37.420  21.755  1.622   1.00 89.97  ? 150 ASN A O   1 
ATOM   4401 C CB  . ASN C 3 150 ? 36.615  23.404  3.907   1.00 87.43  ? 150 ASN A CB  1 
ATOM   4402 C CG  . ASN C 3 150 ? 36.111  24.509  4.821   1.00 93.16  ? 150 ASN A CG  1 
ATOM   4403 O OD1 . ASN C 3 150 ? 34.930  24.530  5.186   1.00 91.98  ? 150 ASN A OD1 1 
ATOM   4404 N ND2 . ASN C 3 150 ? 36.992  25.453  5.167   1.00 90.46  ? 150 ASN A ND2 1 
ATOM   4405 N N   . ILE C 3 151 ? 37.379  23.700  0.437   1.00 94.33  ? 151 ILE A N   1 
ATOM   4406 C CA  . ILE C 3 151 ? 38.323  23.287  -0.591  1.00 93.65  ? 151 ILE A CA  1 
ATOM   4407 C C   . ILE C 3 151 ? 39.644  23.997  -0.330  1.00 101.80 ? 151 ILE A C   1 
ATOM   4408 O O   . ILE C 3 151 ? 39.702  25.044  0.337   1.00 100.72 ? 151 ILE A O   1 
ATOM   4409 C CB  . ILE C 3 151 ? 37.758  23.536  -2.021  1.00 94.16  ? 151 ILE A CB  1 
ATOM   4410 C CG1 . ILE C 3 151 ? 37.596  25.018  -2.433  1.00 94.63  ? 151 ILE A CG1 1 
ATOM   4411 C CG2 . ILE C 3 151 ? 36.420  22.839  -2.191  1.00 86.31  ? 151 ILE A CG2 1 
ATOM   4412 C CD1 . ILE C 3 151 ? 38.841  25.728  -2.877  1.00 97.66  ? 151 ILE A CD1 1 
ATOM   4413 N N   . VAL C 3 152 ? 40.725  23.385  -0.811  1.00 108.52 ? 152 VAL A N   1 
ATOM   4414 C CA  . VAL C 3 152 ? 42.058  23.964  -0.701  1.00 111.31 ? 152 VAL A CA  1 
ATOM   4415 C C   . VAL C 3 152 ? 42.174  25.066  -1.738  1.00 109.83 ? 152 VAL A C   1 
ATOM   4416 O O   . VAL C 3 152 ? 42.453  24.798  -2.912  1.00 110.17 ? 152 VAL A O   1 
ATOM   4417 C CB  . VAL C 3 152 ? 43.156  22.902  -0.895  1.00 112.34 ? 152 VAL A CB  1 
ATOM   4418 C CG1 . VAL C 3 152 ? 44.536  23.551  -0.834  1.00 117.04 ? 152 VAL A CG1 1 
ATOM   4419 C CG2 . VAL C 3 152 ? 43.022  21.796  0.150   1.00 109.82 ? 152 VAL A CG2 1 
ATOM   4420 N N   . TRP C 3 153 ? 41.945  26.310  -1.322  1.00 105.92 ? 153 TRP A N   1 
ATOM   4421 C CA  . TRP C 3 153 ? 41.958  27.394  -2.292  1.00 106.70 ? 153 TRP A CA  1 
ATOM   4422 C C   . TRP C 3 153 ? 43.350  27.595  -2.874  1.00 117.28 ? 153 TRP A C   1 
ATOM   4423 O O   . TRP C 3 153 ? 43.494  27.791  -4.086  1.00 119.27 ? 153 TRP A O   1 
ATOM   4424 C CB  . TRP C 3 153 ? 41.450  28.672  -1.648  1.00 101.12 ? 153 TRP A CB  1 
ATOM   4425 C CG  . TRP C 3 153 ? 40.008  28.617  -1.328  1.00 98.03  ? 153 TRP A CG  1 
ATOM   4426 C CD1 . TRP C 3 153 ? 39.441  28.154  -0.180  1.00 99.36  ? 153 TRP A CD1 1 
ATOM   4427 C CD2 . TRP C 3 153 ? 38.933  29.044  -2.163  1.00 95.35  ? 153 TRP A CD2 1 
ATOM   4428 N NE1 . TRP C 3 153 ? 38.077  28.275  -0.244  1.00 97.97  ? 153 TRP A NE1 1 
ATOM   4429 C CE2 . TRP C 3 153 ? 37.738  28.817  -1.455  1.00 95.64  ? 153 TRP A CE2 1 
ATOM   4430 C CE3 . TRP C 3 153 ? 38.862  29.598  -3.440  1.00 93.50  ? 153 TRP A CE3 1 
ATOM   4431 C CZ2 . TRP C 3 153 ? 36.484  29.123  -1.987  1.00 92.99  ? 153 TRP A CZ2 1 
ATOM   4432 C CZ3 . TRP C 3 153 ? 37.620  29.903  -3.963  1.00 90.83  ? 153 TRP A CZ3 1 
ATOM   4433 C CH2 . TRP C 3 153 ? 36.448  29.666  -3.240  1.00 88.72  ? 153 TRP A CH2 1 
ATOM   4434 N N   . ASP C 3 154 ? 44.380  27.505  -2.029  1.00 130.06 ? 154 ASP A N   1 
ATOM   4435 C CA  . ASP C 3 154 ? 45.786  27.764  -2.378  1.00 136.65 ? 154 ASP A CA  1 
ATOM   4436 C C   . ASP C 3 154 ? 46.152  27.406  -3.818  1.00 135.91 ? 154 ASP A C   1 
ATOM   4437 O O   . ASP C 3 154 ? 46.732  28.223  -4.535  1.00 134.54 ? 154 ASP A O   1 
ATOM   4438 C CB  . ASP C 3 154 ? 46.692  27.004  -1.395  1.00 139.37 ? 154 ASP A CB  1 
ATOM   4439 C CG  . ASP C 3 154 ? 48.179  27.273  -1.612  1.00 142.92 ? 154 ASP A CG  1 
ATOM   4440 O OD1 . ASP C 3 154 ? 48.867  27.542  -0.606  1.00 145.41 ? 154 ASP A OD1 1 
ATOM   4441 O OD2 . ASP C 3 154 ? 48.681  27.167  -2.751  1.00 141.25 ? 154 ASP A OD2 1 
ATOM   4442 N N   . LEU D 4 9   ? 20.111  28.667  53.889  1.00 83.14  ? 10  LEU C N   1 
ATOM   4443 C CA  . LEU D 4 9   ? 19.883  27.745  55.014  1.00 82.22  ? 10  LEU C CA  1 
ATOM   4444 C C   . LEU D 4 9   ? 20.992  26.714  55.084  1.00 80.28  ? 10  LEU C C   1 
ATOM   4445 O O   . LEU D 4 9   ? 21.188  25.974  54.148  1.00 80.73  ? 10  LEU C O   1 
ATOM   4446 C CB  . LEU D 4 9   ? 18.548  27.004  54.881  1.00 81.07  ? 10  LEU C CB  1 
ATOM   4447 C CG  . LEU D 4 9   ? 17.782  26.496  56.121  1.00 81.67  ? 10  LEU C CG  1 
ATOM   4448 C CD1 . LEU D 4 9   ? 16.525  25.668  55.769  1.00 81.29  ? 10  LEU C CD1 1 
ATOM   4449 C CD2 . LEU D 4 9   ? 18.611  25.853  57.249  1.00 81.62  ? 10  LEU C CD2 1 
ATOM   4450 N N   . VAL D 4 10  ? 21.721  26.660  56.187  1.00 81.03  ? 11  VAL C N   1 
ATOM   4451 C CA  . VAL D 4 10  ? 22.661  25.574  56.435  1.00 80.11  ? 11  VAL C CA  1 
ATOM   4452 C C   . VAL D 4 10  ? 21.928  24.508  57.243  1.00 81.51  ? 11  VAL C C   1 
ATOM   4453 O O   . VAL D 4 10  ? 21.600  24.719  58.417  1.00 80.49  ? 11  VAL C O   1 
ATOM   4454 C CB  . VAL D 4 10  ? 23.914  26.063  57.168  1.00 83.47  ? 11  VAL C CB  1 
ATOM   4455 C CG1 . VAL D 4 10  ? 24.575  24.904  57.945  1.00 81.81  ? 11  VAL C CG1 1 
ATOM   4456 C CG2 . VAL D 4 10  ? 24.887  26.687  56.187  1.00 82.39  ? 11  VAL C CG2 1 
ATOM   4457 N N   . ILE D 4 11  ? 21.667  23.362  56.612  1.00 82.91  ? 12  ILE C N   1 
ATOM   4458 C CA  . ILE D 4 11  ? 21.010  22.235  57.263  1.00 83.91  ? 12  ILE C CA  1 
ATOM   4459 C C   . ILE D 4 11  ? 22.071  21.233  57.685  1.00 86.52  ? 12  ILE C C   1 
ATOM   4460 O O   . ILE D 4 11  ? 22.889  20.808  56.861  1.00 85.39  ? 12  ILE C O   1 
ATOM   4461 C CB  . ILE D 4 11  ? 19.990  21.561  56.334  1.00 80.91  ? 12  ILE C CB  1 
ATOM   4462 C CG1 . ILE D 4 11  ? 18.842  22.511  55.988  1.00 80.06  ? 12  ILE C CG1 1 
ATOM   4463 C CG2 . ILE D 4 11  ? 19.463  20.299  56.987  1.00 84.21  ? 12  ILE C CG2 1 
ATOM   4464 C CD1 . ILE D 4 11  ? 17.657  21.802  55.349  1.00 83.02  ? 12  ILE C CD1 1 
ATOM   4465 N N   . ASN D 4 12  ? 22.050  20.833  58.956  1.00 94.28  ? 13  ASN C N   1 
ATOM   4466 C CA  . ASN D 4 12  ? 22.914  19.748  59.419  1.00 98.38  ? 13  ASN C CA  1 
ATOM   4467 C C   . ASN D 4 12  ? 22.172  18.912  60.458  1.00 100.41 ? 13  ASN C C   1 
ATOM   4468 O O   . ASN D 4 12  ? 21.920  19.370  61.578  1.00 100.52 ? 13  ASN C O   1 
ATOM   4469 C CB  . ASN D 4 12  ? 24.235  20.283  59.976  1.00 100.07 ? 13  ASN C CB  1 
ATOM   4470 C CG  . ASN D 4 12  ? 25.319  19.209  60.015  1.00 105.12 ? 13  ASN C CG  1 
ATOM   4471 O OD1 . ASN D 4 12  ? 26.251  19.225  59.199  1.00 99.67  ? 13  ASN C OD1 1 
ATOM   4472 N ND2 . ASN D 4 12  ? 25.207  18.275  60.969  1.00 108.27 ? 13  ASN C ND2 1 
ATOM   4473 N N   . GLY D 4 13  ? 21.836  17.677  60.083  1.00 102.81 ? 14  GLY C N   1 
ATOM   4474 C CA  . GLY D 4 13  ? 21.156  16.757  60.969  1.00 106.23 ? 14  GLY C CA  1 
ATOM   4475 C C   . GLY D 4 13  ? 21.843  15.405  60.976  1.00 105.41 ? 14  GLY C C   1 
ATOM   4476 O O   . GLY D 4 13  ? 22.839  15.190  60.283  1.00 106.97 ? 14  GLY C O   1 
ATOM   4477 N N   . ARG D 4 14  ? 21.294  14.502  61.793  1.00 101.79 ? 15  ARG C N   1 
ATOM   4478 C CA  . ARG D 4 14  ? 21.802  13.136  61.818  1.00 99.94  ? 15  ARG C CA  1 
ATOM   4479 C C   . ARG D 4 14  ? 21.846  12.565  60.410  1.00 100.26 ? 15  ARG C C   1 
ATOM   4480 O O   . ARG D 4 14  ? 22.885  12.071  59.962  1.00 101.37 ? 15  ARG C O   1 
ATOM   4481 C CB  . ARG D 4 14  ? 20.939  12.269  62.737  1.00 99.31  ? 15  ARG C CB  1 
ATOM   4482 N N   . THR D 4 15  ? 20.740  12.688  59.674  1.00 101.17 ? 16  THR C N   1 
ATOM   4483 C CA  . THR D 4 15  ? 20.603  12.085  58.354  1.00 97.80  ? 16  THR C CA  1 
ATOM   4484 C C   . THR D 4 15  ? 20.833  13.059  57.201  1.00 96.58  ? 16  THR C C   1 
ATOM   4485 O O   . THR D 4 15  ? 21.364  12.649  56.162  1.00 94.70  ? 16  THR C O   1 
ATOM   4486 C CB  . THR D 4 15  ? 19.215  11.448  58.214  1.00 97.03  ? 16  THR C CB  1 
ATOM   4487 O OG1 . THR D 4 15  ? 18.222  12.472  58.079  1.00 96.53  ? 16  THR C OG1 1 
ATOM   4488 C CG2 . THR D 4 15  ? 18.896  10.632  59.436  1.00 100.83 ? 16  THR C CG2 1 
ATOM   4489 N N   . LEU D 4 16  ? 20.472  14.335  57.344  1.00 94.33  ? 17  LEU C N   1 
ATOM   4490 C CA  . LEU D 4 16  ? 20.501  15.262  56.222  1.00 86.15  ? 17  LEU C CA  1 
ATOM   4491 C C   . LEU D 4 16  ? 21.439  16.425  56.486  1.00 85.17  ? 17  LEU C C   1 
ATOM   4492 O O   . LEU D 4 16  ? 21.519  16.932  57.604  1.00 90.01  ? 17  LEU C O   1 
ATOM   4493 C CB  . LEU D 4 16  ? 19.104  15.770  55.903  1.00 83.39  ? 17  LEU C CB  1 
ATOM   4494 C CG  . LEU D 4 16  ? 19.000  16.414  54.536  1.00 83.18  ? 17  LEU C CG  1 
ATOM   4495 C CD1 . LEU D 4 16  ? 20.013  15.779  53.587  1.00 83.38  ? 17  LEU C CD1 1 
ATOM   4496 C CD2 . LEU D 4 16  ? 17.621  16.060  54.056  1.00 85.78  ? 17  LEU C CD2 1 
ATOM   4497 N N   . SER D 4 17  ? 22.132  16.849  55.436  1.00 82.18  ? 18  SER C N   1 
ATOM   4498 C CA  . SER D 4 17  ? 23.145  17.885  55.538  1.00 79.45  ? 18  SER C CA  1 
ATOM   4499 C C   . SER D 4 17  ? 23.275  18.584  54.189  1.00 82.48  ? 18  SER C C   1 
ATOM   4500 O O   . SER D 4 17  ? 23.521  17.917  53.176  1.00 82.20  ? 18  SER C O   1 
ATOM   4501 C CB  . SER D 4 17  ? 24.459  17.256  55.984  1.00 74.93  ? 18  SER C CB  1 
ATOM   4502 O OG  . SER D 4 17  ? 25.489  17.513  55.068  1.00 76.85  ? 18  SER C OG  1 
ATOM   4503 N N   . GLY D 4 18  ? 23.100  19.907  54.168  1.00 77.11  ? 19  GLY C N   1 
ATOM   4504 C CA  . GLY D 4 18  ? 23.119  20.641  52.906  1.00 76.18  ? 19  GLY C CA  1 
ATOM   4505 C C   . GLY D 4 18  ? 22.709  22.101  53.031  1.00 80.26  ? 19  GLY C C   1 
ATOM   4506 O O   . GLY D 4 18  ? 22.857  22.714  54.092  1.00 78.61  ? 19  GLY C O   1 
ATOM   4507 N N   . TYR D 4 19  ? 22.186  22.661  51.923  1.00 83.15  ? 20  TYR C N   1 
ATOM   4508 C CA  . TYR D 4 19  ? 21.876  24.090  51.834  1.00 77.75  ? 20  TYR C CA  1 
ATOM   4509 C C   . TYR D 4 19  ? 20.800  24.399  50.788  1.00 76.92  ? 20  TYR C C   1 
ATOM   4510 O O   . TYR D 4 19  ? 20.680  23.707  49.773  1.00 76.12  ? 20  TYR C O   1 
ATOM   4511 C CB  . TYR D 4 19  ? 23.158  24.883  51.539  1.00 76.78  ? 20  TYR C CB  1 
ATOM   4512 C CG  . TYR D 4 19  ? 23.825  24.673  50.179  1.00 79.22  ? 20  TYR C CG  1 
ATOM   4513 C CD1 . TYR D 4 19  ? 23.271  25.187  48.998  1.00 80.54  ? 20  TYR C CD1 1 
ATOM   4514 C CD2 . TYR D 4 19  ? 25.023  23.969  50.081  1.00 79.25  ? 20  TYR C CD2 1 
ATOM   4515 C CE1 . TYR D 4 19  ? 23.901  25.011  47.766  1.00 79.95  ? 20  TYR C CE1 1 
ATOM   4516 C CE2 . TYR D 4 19  ? 25.654  23.778  48.861  1.00 79.92  ? 20  TYR C CE2 1 
ATOM   4517 C CZ  . TYR D 4 19  ? 25.091  24.296  47.704  1.00 82.89  ? 20  TYR C CZ  1 
ATOM   4518 O OH  . TYR D 4 19  ? 25.722  24.100  46.485  1.00 85.62  ? 20  TYR C OH  1 
ATOM   4519 N N   . THR D 4 20  ? 20.015  25.454  51.055  1.00 77.96  ? 21  THR C N   1 
ATOM   4520 C CA  . THR D 4 20  ? 19.107  26.076  50.086  1.00 79.99  ? 21  THR C CA  1 
ATOM   4521 C C   . THR D 4 20  ? 19.083  27.583  50.322  1.00 82.24  ? 21  THR C C   1 
ATOM   4522 O O   . THR D 4 20  ? 19.576  28.091  51.334  1.00 81.45  ? 21  THR C O   1 
ATOM   4523 C CB  . THR D 4 20  ? 17.669  25.551  50.185  1.00 78.21  ? 21  THR C CB  1 
ATOM   4524 O OG1 . THR D 4 20  ? 17.711  24.160  50.449  1.00 82.06  ? 21  THR C OG1 1 
ATOM   4525 C CG2 . THR D 4 20  ? 16.904  25.752  48.883  1.00 79.16  ? 21  THR C CG2 1 
ATOM   4526 N N   . THR D 4 21  ? 18.481  28.297  49.377  1.00 84.10  ? 22  THR C N   1 
ATOM   4527 C CA  . THR D 4 21  ? 18.385  29.741  49.419  1.00 85.10  ? 22  THR C CA  1 
ATOM   4528 C C   . THR D 4 21  ? 16.948  30.175  49.191  1.00 88.16  ? 22  THR C C   1 
ATOM   4529 O O   . THR D 4 21  ? 16.098  29.406  48.731  1.00 85.40  ? 22  THR C O   1 
ATOM   4530 C CB  . THR D 4 21  ? 19.266  30.399  48.365  1.00 86.96  ? 22  THR C CB  1 
ATOM   4531 O OG1 . THR D 4 21  ? 18.709  30.128  47.076  1.00 87.03  ? 22  THR C OG1 1 
ATOM   4532 C CG2 . THR D 4 21  ? 20.684  29.869  48.431  1.00 85.98  ? 22  THR C CG2 1 
ATOM   4533 N N   . THR D 4 22  ? 16.696  31.427  49.552  1.00 90.81  ? 23  THR C N   1 
ATOM   4534 C CA  . THR D 4 22  ? 15.474  32.130  49.209  1.00 93.20  ? 23  THR C CA  1 
ATOM   4535 C C   . THR D 4 22  ? 15.725  33.586  49.534  1.00 95.18  ? 23  THR C C   1 
ATOM   4536 O O   . THR D 4 22  ? 16.438  33.905  50.488  1.00 96.33  ? 23  THR C O   1 
ATOM   4537 C CB  . THR D 4 22  ? 14.246  31.591  49.957  1.00 92.65  ? 23  THR C CB  1 
ATOM   4538 O OG1 . THR D 4 22  ? 14.034  30.218  49.587  1.00 89.65  ? 23  THR C OG1 1 
ATOM   4539 C CG2 . THR D 4 22  ? 13.002  32.401  49.599  1.00 93.88  ? 23  THR C CG2 1 
ATOM   4540 N N   . THR D 4 23  ? 15.194  34.460  48.698  1.00 99.52  ? 24  THR C N   1 
ATOM   4541 C CA  . THR D 4 23  ? 15.328  35.888  48.903  1.00 102.44 ? 24  THR C CA  1 
ATOM   4542 C C   . THR D 4 23  ? 13.973  36.441  49.302  1.00 104.62 ? 24  THR C C   1 
ATOM   4543 O O   . THR D 4 23  ? 12.933  35.960  48.839  1.00 103.83 ? 24  THR C O   1 
ATOM   4544 C CB  . THR D 4 23  ? 15.837  36.578  47.650  1.00 105.26 ? 24  THR C CB  1 
ATOM   4545 O OG1 . THR D 4 23  ? 16.660  35.659  46.925  1.00 102.58 ? 24  THR C OG1 1 
ATOM   4546 C CG2 . THR D 4 23  ? 16.671  37.771  48.047  1.00 109.35 ? 24  THR C CG2 1 
ATOM   4547 N N   . ALA D 4 24  ? 13.985  37.432  50.177  1.00 107.79 ? 25  ALA C N   1 
ATOM   4548 C CA  . ALA D 4 24  ? 12.736  37.913  50.735  1.00 111.21 ? 25  ALA C CA  1 
ATOM   4549 C C   . ALA D 4 24  ? 12.989  39.256  51.389  1.00 116.15 ? 25  ALA C C   1 
ATOM   4550 O O   . ALA D 4 24  ? 14.074  39.835  51.273  1.00 116.67 ? 25  ALA C O   1 
ATOM   4551 C CB  . ALA D 4 24  ? 12.148  36.911  51.729  1.00 115.94 ? 25  ALA C CB  1 
ATOM   4552 N N   . VAL D 4 25  ? 11.967  39.736  52.092  1.00 124.43 ? 26  VAL C N   1 
ATOM   4553 C CA  . VAL D 4 25  ? 11.987  41.087  52.640  1.00 125.21 ? 26  VAL C CA  1 
ATOM   4554 C C   . VAL D 4 25  ? 12.742  41.127  53.964  1.00 137.58 ? 26  VAL C C   1 
ATOM   4555 O O   . VAL D 4 25  ? 13.652  41.944  54.146  1.00 132.51 ? 26  VAL C O   1 
ATOM   4556 C CB  . VAL D 4 25  ? 10.549  41.636  52.758  1.00 126.14 ? 26  VAL C CB  1 
ATOM   4557 C CG1 . VAL D 4 25  ? 9.807   41.382  51.477  1.00 125.49 ? 26  VAL C CG1 1 
ATOM   4558 C CG2 . VAL D 4 25  ? 9.775   40.961  53.872  1.00 130.23 ? 26  VAL C CG2 1 
ATOM   4559 N N   . ASP D 4 26  ? 12.413  40.220  54.887  1.00 154.94 ? 27  ASP C N   1 
ATOM   4560 C CA  . ASP D 4 26  ? 13.033  40.163  56.201  1.00 154.58 ? 27  ASP C CA  1 
ATOM   4561 C C   . ASP D 4 26  ? 13.398  38.726  56.537  1.00 149.65 ? 27  ASP C C   1 
ATOM   4562 O O   . ASP D 4 26  ? 12.787  37.778  56.035  1.00 145.97 ? 27  ASP C O   1 
ATOM   4563 C CB  . ASP D 4 26  ? 12.114  40.747  57.296  1.00 155.47 ? 27  ASP C CB  1 
ATOM   4564 C CG  . ASP D 4 26  ? 10.780  40.025  57.400  1.00 152.09 ? 27  ASP C CG  1 
ATOM   4565 O OD1 . ASP D 4 26  ? 10.769  38.810  57.710  1.00 148.21 ? 27  ASP C OD1 1 
ATOM   4566 O OD2 . ASP D 4 26  ? 9.737   40.687  57.198  1.00 155.49 ? 27  ASP C OD2 1 
ATOM   4567 N N   . ALA D 4 27  ? 14.397  38.576  57.408  1.00 131.27 ? 28  ALA C N   1 
ATOM   4568 C CA  . ALA D 4 27  ? 14.885  37.245  57.745  1.00 125.44 ? 28  ALA C CA  1 
ATOM   4569 C C   . ALA D 4 27  ? 13.796  36.381  58.369  1.00 122.87 ? 28  ALA C C   1 
ATOM   4570 O O   . ALA D 4 27  ? 13.860  35.150  58.278  1.00 119.76 ? 28  ALA C O   1 
ATOM   4571 C CB  . ALA D 4 27  ? 16.095  37.343  58.676  1.00 118.26 ? 28  ALA C CB  1 
ATOM   4572 N N   . ALA D 4 28  ? 12.786  36.995  58.993  1.00 121.72 ? 29  ALA C N   1 
ATOM   4573 C CA  . ALA D 4 28  ? 11.708  36.204  59.579  1.00 118.92 ? 29  ALA C CA  1 
ATOM   4574 C C   . ALA D 4 28  ? 10.811  35.597  58.506  1.00 120.11 ? 29  ALA C C   1 
ATOM   4575 O O   . ALA D 4 28  ? 10.273  34.498  58.699  1.00 115.48 ? 29  ALA C O   1 
ATOM   4576 C CB  . ALA D 4 28  ? 10.889  37.053  60.544  1.00 116.86 ? 29  ALA C CB  1 
ATOM   4577 N N   . THR D 4 29  ? 10.635  36.295  57.376  1.00 124.18 ? 30  THR C N   1 
ATOM   4578 C CA  . THR D 4 29  ? 9.917   35.705  56.250  1.00 119.14 ? 30  THR C CA  1 
ATOM   4579 C C   . THR D 4 29  ? 10.752  34.616  55.600  1.00 115.08 ? 30  THR C C   1 
ATOM   4580 O O   . THR D 4 29  ? 10.221  33.579  55.179  1.00 110.39 ? 30  THR C O   1 
ATOM   4581 C CB  . THR D 4 29  ? 9.559   36.775  55.221  1.00 123.48 ? 30  THR C CB  1 
ATOM   4582 O OG1 . THR D 4 29  ? 10.480  37.864  55.332  1.00 130.08 ? 30  THR C OG1 1 
ATOM   4583 C CG2 . THR D 4 29  ? 8.147   37.289  55.452  1.00 118.03 ? 30  THR C CG2 1 
ATOM   4584 N N   . ALA D 4 30  ? 12.064  34.839  55.508  1.00 113.73 ? 31  ALA C N   1 
ATOM   4585 C CA  . ALA D 4 30  ? 12.965  33.780  55.074  1.00 110.17 ? 31  ALA C CA  1 
ATOM   4586 C C   . ALA D 4 30  ? 12.954  32.623  56.065  1.00 107.18 ? 31  ALA C C   1 
ATOM   4587 O O   . ALA D 4 30  ? 12.847  31.457  55.673  1.00 103.58 ? 31  ALA C O   1 
ATOM   4588 C CB  . ALA D 4 30  ? 14.379  34.333  54.896  1.00 108.58 ? 31  ALA C CB  1 
ATOM   4589 N N   . GLU D 4 31  ? 13.039  32.924  57.365  1.00 108.14 ? 32  GLU C N   1 
ATOM   4590 C CA  . GLU D 4 31  ? 13.052  31.837  58.335  1.00 106.09 ? 32  GLU C CA  1 
ATOM   4591 C C   . GLU D 4 31  ? 11.719  31.099  58.370  1.00 105.55 ? 32  GLU C C   1 
ATOM   4592 O O   . GLU D 4 31  ? 11.671  29.954  58.829  1.00 104.11 ? 32  GLU C O   1 
ATOM   4593 C CB  . GLU D 4 31  ? 13.422  32.345  59.739  1.00 107.56 ? 32  GLU C CB  1 
ATOM   4594 C CG  . GLU D 4 31  ? 12.257  32.824  60.601  1.00 108.80 ? 32  GLU C CG  1 
ATOM   4595 C CD  . GLU D 4 31  ? 12.570  32.794  62.092  1.00 107.36 ? 32  GLU C CD  1 
ATOM   4596 O OE1 . GLU D 4 31  ? 13.760  32.855  62.470  1.00 105.61 ? 32  GLU C OE1 1 
ATOM   4597 O OE2 . GLU D 4 31  ? 11.618  32.713  62.891  1.00 112.60 ? 32  GLU C OE2 1 
ATOM   4598 N N   . LYS D 4 32  ? 10.642  31.707  57.870  1.00 109.22 ? 33  LYS C N   1 
ATOM   4599 C CA  . LYS D 4 32  ? 9.362   31.006  57.846  1.00 107.73 ? 33  LYS C CA  1 
ATOM   4600 C C   . LYS D 4 32  ? 9.343   29.925  56.766  1.00 106.62 ? 33  LYS C C   1 
ATOM   4601 O O   . LYS D 4 32  ? 8.938   28.786  57.028  1.00 108.98 ? 33  LYS C O   1 
ATOM   4602 C CB  . LYS D 4 32  ? 8.215   31.997  57.649  1.00 107.95 ? 33  LYS C CB  1 
ATOM   4603 N N   . VAL D 4 33  ? 9.773   30.254  55.542  1.00 101.69 ? 34  VAL C N   1 
ATOM   4604 C CA  . VAL D 4 33  ? 9.794   29.233  54.495  1.00 101.47 ? 34  VAL C CA  1 
ATOM   4605 C C   . VAL D 4 33  ? 10.824  28.159  54.823  1.00 98.19  ? 34  VAL C C   1 
ATOM   4606 O O   . VAL D 4 33  ? 10.558  26.959  54.673  1.00 95.78  ? 34  VAL C O   1 
ATOM   4607 C CB  . VAL D 4 33  ? 10.047  29.851  53.100  1.00 103.50 ? 34  VAL C CB  1 
ATOM   4608 C CG1 . VAL D 4 33  ? 8.791   30.535  52.565  1.00 103.63 ? 34  VAL C CG1 1 
ATOM   4609 C CG2 . VAL D 4 33  ? 11.240  30.803  53.094  1.00 102.23 ? 34  VAL C CG2 1 
ATOM   4610 N N   . PHE D 4 34  ? 12.013  28.572  55.275  1.00 98.71  ? 35  PHE C N   1 
ATOM   4611 C CA  . PHE D 4 34  ? 13.037  27.620  55.695  1.00 95.68  ? 35  PHE C CA  1 
ATOM   4612 C C   . PHE D 4 34  ? 12.450  26.585  56.646  1.00 95.43  ? 35  PHE C C   1 
ATOM   4613 O O   . PHE D 4 34  ? 12.708  25.386  56.504  1.00 93.55  ? 35  PHE C O   1 
ATOM   4614 C CB  . PHE D 4 34  ? 14.197  28.369  56.359  1.00 94.29  ? 35  PHE C CB  1 
ATOM   4615 C CG  . PHE D 4 34  ? 15.214  28.937  55.388  1.00 90.46  ? 35  PHE C CG  1 
ATOM   4616 C CD1 . PHE D 4 34  ? 14.982  28.933  54.030  1.00 89.15  ? 35  PHE C CD1 1 
ATOM   4617 C CD2 . PHE D 4 34  ? 16.375  29.541  55.850  1.00 88.46  ? 35  PHE C CD2 1 
ATOM   4618 C CE1 . PHE D 4 34  ? 15.914  29.477  53.146  1.00 88.18  ? 35  PHE C CE1 1 
ATOM   4619 C CE2 . PHE D 4 34  ? 17.303  30.085  54.967  1.00 87.17  ? 35  PHE C CE2 1 
ATOM   4620 C CZ  . PHE D 4 34  ? 17.070  30.046  53.617  1.00 86.45  ? 35  PHE C CZ  1 
ATOM   4621 N N   . LYS D 4 35  ? 11.634  27.042  57.606  1.00 97.77  ? 36  LYS C N   1 
ATOM   4622 C CA  . LYS D 4 35  ? 10.908  26.150  58.512  1.00 96.26  ? 36  LYS C CA  1 
ATOM   4623 C C   . LYS D 4 35  ? 10.025  25.175  57.749  1.00 97.29  ? 36  LYS C C   1 
ATOM   4624 O O   . LYS D 4 35  ? 10.075  23.963  57.982  1.00 96.04  ? 36  LYS C O   1 
ATOM   4625 C CB  . LYS D 4 35  ? 10.042  26.969  59.467  1.00 99.72  ? 36  LYS C CB  1 
ATOM   4626 N N   . GLN D 4 36  ? 9.178   25.695  56.853  1.00 97.43  ? 37  GLN C N   1 
ATOM   4627 C CA  . GLN D 4 36  ? 8.324   24.844  56.031  1.00 95.94  ? 37  GLN C CA  1 
ATOM   4628 C C   . GLN D 4 36  ? 9.145   23.842  55.234  1.00 94.75  ? 37  GLN C C   1 
ATOM   4629 O O   . GLN D 4 36  ? 8.605   22.832  54.767  1.00 94.80  ? 37  GLN C O   1 
ATOM   4630 C CB  . GLN D 4 36  ? 7.486   25.710  55.090  1.00 100.41 ? 37  GLN C CB  1 
ATOM   4631 C CG  . GLN D 4 36  ? 5.990   25.755  55.401  1.00 105.94 ? 37  GLN C CG  1 
ATOM   4632 C CD  . GLN D 4 36  ? 5.162   26.257  54.215  1.00 110.68 ? 37  GLN C CD  1 
ATOM   4633 O OE1 . GLN D 4 36  ? 5.710   26.617  53.168  1.00 111.28 ? 37  GLN C OE1 1 
ATOM   4634 N NE2 . GLN D 4 36  ? 3.840   26.317  54.392  1.00 113.02 ? 37  GLN C NE2 1 
ATOM   4635 N N   . TYR D 4 37  ? 10.439  24.111  55.066  1.00 93.41  ? 38  TYR C N   1 
ATOM   4636 C CA  . TYR D 4 37  ? 11.395  23.169  54.505  1.00 91.18  ? 38  TYR C CA  1 
ATOM   4637 C C   . TYR D 4 37  ? 11.953  22.223  55.568  1.00 91.32  ? 38  TYR C C   1 
ATOM   4638 O O   . TYR D 4 37  ? 13.119  21.820  55.499  1.00 90.18  ? 38  TYR C O   1 
ATOM   4639 C CB  . TYR D 4 37  ? 12.510  23.951  53.801  1.00 89.71  ? 38  TYR C CB  1 
ATOM   4640 C CG  . TYR D 4 37  ? 13.367  23.161  52.849  1.00 84.13  ? 38  TYR C CG  1 
ATOM   4641 C CD1 . TYR D 4 37  ? 12.833  22.624  51.682  1.00 87.79  ? 38  TYR C CD1 1 
ATOM   4642 C CD2 . TYR D 4 37  ? 14.717  22.964  53.104  1.00 82.16  ? 38  TYR C CD2 1 
ATOM   4643 C CE1 . TYR D 4 37  ? 13.623  21.883  50.796  1.00 82.93  ? 38  TYR C CE1 1 
ATOM   4644 C CE2 . TYR D 4 37  ? 15.511  22.235  52.234  1.00 84.19  ? 38  TYR C CE2 1 
ATOM   4645 C CZ  . TYR D 4 37  ? 14.960  21.696  51.080  1.00 81.68  ? 38  TYR C CZ  1 
ATOM   4646 O OH  . TYR D 4 37  ? 15.758  20.980  50.222  1.00 77.99  ? 38  TYR C OH  1 
ATOM   4647 N N   . ALA D 4 38  ? 11.151  21.876  56.573  1.00 90.84  ? 39  ALA C N   1 
ATOM   4648 C CA  . ALA D 4 38  ? 11.532  20.871  57.553  1.00 88.88  ? 39  ALA C CA  1 
ATOM   4649 C C   . ALA D 4 38  ? 10.824  19.568  57.208  1.00 94.71  ? 39  ALA C C   1 
ATOM   4650 O O   . ALA D 4 38  ? 9.873   19.147  57.874  1.00 94.15  ? 39  ALA C O   1 
ATOM   4651 C CB  . ALA D 4 38  ? 11.175  21.322  58.949  1.00 99.33  ? 39  ALA C CB  1 
ATOM   4652 N N   . PHE D 4 39  ? 11.294  18.925  56.137  1.00 92.20  ? 40  PHE C N   1 
ATOM   4653 C CA  . PHE D 4 39  ? 10.945  17.532  55.902  1.00 92.32  ? 40  PHE C CA  1 
ATOM   4654 C C   . PHE D 4 39  ? 11.379  16.700  57.094  1.00 93.57  ? 40  PHE C C   1 
ATOM   4655 O O   . PHE D 4 39  ? 12.306  15.889  56.971  1.00 93.06  ? 40  PHE C O   1 
ATOM   4656 C CB  . PHE D 4 39  ? 11.668  16.983  54.703  1.00 91.67  ? 40  PHE C CB  1 
ATOM   4657 C CG  . PHE D 4 39  ? 12.960  17.651  54.464  1.00 88.53  ? 40  PHE C CG  1 
ATOM   4658 C CD1 . PHE D 4 39  ? 13.972  17.545  55.399  1.00 87.48  ? 40  PHE C CD1 1 
ATOM   4659 C CD2 . PHE D 4 39  ? 13.222  18.268  53.258  1.00 87.93  ? 40  PHE C CD2 1 
ATOM   4660 C CE1 . PHE D 4 39  ? 15.170  18.143  55.198  1.00 88.92  ? 40  PHE C CE1 1 
ATOM   4661 C CE2 . PHE D 4 39  ? 14.438  18.847  53.034  1.00 87.56  ? 40  PHE C CE2 1 
ATOM   4662 C CZ  . PHE D 4 39  ? 15.421  18.779  54.005  1.00 89.28  ? 40  PHE C CZ  1 
ATOM   4663 N N   . GLY D 4 40  ? 10.763  16.914  58.255  1.00 94.64  ? 41  GLY C N   1 
ATOM   4664 C CA  . GLY D 4 40  ? 11.117  16.164  59.431  1.00 96.53  ? 41  GLY C CA  1 
ATOM   4665 C C   . GLY D 4 40  ? 12.451  16.505  60.041  1.00 94.85  ? 41  GLY C C   1 
ATOM   4666 O O   . GLY D 4 40  ? 12.778  15.960  61.102  1.00 102.01 ? 41  GLY C O   1 
ATOM   4667 N N   . ASN D 4 41  ? 13.243  17.379  59.421  1.00 92.67  ? 42  ASN C N   1 
ATOM   4668 C CA  . ASN D 4 41  ? 14.440  17.847  60.108  1.00 100.93 ? 42  ASN C CA  1 
ATOM   4669 C C   . ASN D 4 41  ? 14.075  18.806  61.243  1.00 109.14 ? 42  ASN C C   1 
ATOM   4670 O O   . ASN D 4 41  ? 14.561  18.655  62.374  1.00 111.76 ? 42  ASN C O   1 
ATOM   4671 C CB  . ASN D 4 41  ? 15.406  18.480  59.105  1.00 92.75  ? 42  ASN C CB  1 
ATOM   4672 C CG  . ASN D 4 41  ? 16.789  18.728  59.695  1.00 93.58  ? 42  ASN C CG  1 
ATOM   4673 O OD1 . ASN D 4 41  ? 16.925  19.233  60.809  1.00 92.99  ? 42  ASN C OD1 1 
ATOM   4674 N ND2 . ASN D 4 41  ? 17.820  18.303  58.975  1.00 95.17  ? 42  ASN C ND2 1 
ATOM   4675 N N   . GLY D 4 42  ? 13.172  19.753  60.976  1.00 103.70 ? 43  GLY C N   1 
ATOM   4676 C CA  . GLY D 4 42  ? 12.804  20.801  61.917  1.00 109.90 ? 43  GLY C CA  1 
ATOM   4677 C C   . GLY D 4 42  ? 12.526  20.372  63.343  1.00 114.04 ? 43  GLY C C   1 
ATOM   4678 O O   . GLY D 4 42  ? 12.739  21.156  64.275  1.00 113.75 ? 43  GLY C O   1 
ATOM   4679 N N   . VAL D 4 43  ? 12.054  19.129  63.507  1.00 125.55 ? 44  VAL C N   1 
ATOM   4680 C CA  . VAL D 4 43  ? 11.759  18.571  64.828  1.00 128.28 ? 44  VAL C CA  1 
ATOM   4681 C C   . VAL D 4 43  ? 12.941  18.767  65.768  1.00 132.71 ? 44  VAL C C   1 
ATOM   4682 O O   . VAL D 4 43  ? 12.791  19.256  66.896  1.00 134.71 ? 44  VAL C O   1 
ATOM   4683 C CB  . VAL D 4 43  ? 11.382  17.082  64.710  1.00 128.30 ? 44  VAL C CB  1 
ATOM   4684 N N   . ASP D 4 44  ? 14.135  18.376  65.322  1.00 126.54 ? 45  ASP C N   1 
ATOM   4685 C CA  . ASP D 4 44  ? 15.361  18.628  66.077  1.00 126.89 ? 45  ASP C CA  1 
ATOM   4686 C C   . ASP D 4 44  ? 16.051  19.798  65.382  1.00 122.83 ? 45  ASP C C   1 
ATOM   4687 O O   . ASP D 4 44  ? 16.979  19.635  64.594  1.00 120.18 ? 45  ASP C O   1 
ATOM   4688 C CB  . ASP D 4 44  ? 16.239  17.374  66.142  1.00 124.41 ? 45  ASP C CB  1 
ATOM   4689 C CG  . ASP D 4 44  ? 17.183  17.365  67.343  1.00 123.97 ? 45  ASP C CG  1 
ATOM   4690 O OD1 . ASP D 4 44  ? 17.256  18.375  68.081  1.00 128.07 ? 45  ASP C OD1 1 
ATOM   4691 O OD2 . ASP D 4 44  ? 17.855  16.331  67.547  1.00 122.85 ? 45  ASP C OD2 1 
ATOM   4692 N N   . GLY D 4 45  ? 15.558  21.002  65.674  1.00 125.50 ? 46  GLY C N   1 
ATOM   4693 C CA  . GLY D 4 45  ? 16.064  22.207  65.058  1.00 117.76 ? 46  GLY C CA  1 
ATOM   4694 C C   . GLY D 4 45  ? 16.701  23.185  66.018  1.00 116.75 ? 46  GLY C C   1 
ATOM   4695 O O   . GLY D 4 45  ? 15.997  23.834  66.794  1.00 111.76 ? 46  GLY C O   1 
ATOM   4696 N N   . GLU D 4 46  ? 18.032  23.305  65.973  1.00 126.73 ? 47  GLU C N   1 
ATOM   4697 C CA  . GLU D 4 46  ? 18.707  24.315  66.783  1.00 128.94 ? 47  GLU C CA  1 
ATOM   4698 C C   . GLU D 4 46  ? 18.310  25.716  66.349  1.00 129.26 ? 47  GLU C C   1 
ATOM   4699 O O   . GLU D 4 46  ? 18.091  26.592  67.192  1.00 133.12 ? 47  GLU C O   1 
ATOM   4700 C CB  . GLU D 4 46  ? 20.223  24.149  66.701  1.00 127.35 ? 47  GLU C CB  1 
ATOM   4701 N N   . TRP D 4 47  ? 18.219  25.948  65.039  1.00 106.34 ? 48  TRP C N   1 
ATOM   4702 C CA  . TRP D 4 47  ? 17.691  27.199  64.495  1.00 107.74 ? 48  TRP C CA  1 
ATOM   4703 C C   . TRP D 4 47  ? 18.474  28.414  65.010  1.00 109.39 ? 48  TRP C C   1 
ATOM   4704 O O   . TRP D 4 47  ? 17.952  29.290  65.711  1.00 107.87 ? 48  TRP C O   1 
ATOM   4705 C CB  . TRP D 4 47  ? 16.196  27.325  64.808  1.00 109.91 ? 48  TRP C CB  1 
ATOM   4706 C CG  . TRP D 4 47  ? 15.300  27.067  63.643  1.00 108.61 ? 48  TRP C CG  1 
ATOM   4707 C CD1 . TRP D 4 47  ? 15.589  26.330  62.532  1.00 107.02 ? 48  TRP C CD1 1 
ATOM   4708 C CD2 . TRP D 4 47  ? 13.970  27.570  63.455  1.00 110.28 ? 48  TRP C CD2 1 
ATOM   4709 N NE1 . TRP D 4 47  ? 14.521  26.334  61.663  1.00 105.30 ? 48  TRP C NE1 1 
ATOM   4710 C CE2 . TRP D 4 47  ? 13.513  27.086  62.211  1.00 107.89 ? 48  TRP C CE2 1 
ATOM   4711 C CE3 . TRP D 4 47  ? 13.119  28.385  64.218  1.00 112.07 ? 48  TRP C CE3 1 
ATOM   4712 C CZ2 . TRP D 4 47  ? 12.245  27.384  61.718  1.00 105.25 ? 48  TRP C CZ2 1 
ATOM   4713 C CZ3 . TRP D 4 47  ? 11.854  28.685  63.718  1.00 110.10 ? 48  TRP C CZ3 1 
ATOM   4714 C CH2 . TRP D 4 47  ? 11.431  28.182  62.482  1.00 105.61 ? 48  TRP C CH2 1 
ATOM   4715 N N   . THR D 4 48  ? 19.749  28.458  64.647  1.00 105.32 ? 49  THR C N   1 
ATOM   4716 C CA  . THR D 4 48  ? 20.612  29.550  65.075  1.00 101.99 ? 49  THR C CA  1 
ATOM   4717 C C   . THR D 4 48  ? 20.278  30.801  64.287  1.00 103.11 ? 49  THR C C   1 
ATOM   4718 O O   . THR D 4 48  ? 20.460  30.825  63.066  1.00 99.24  ? 49  THR C O   1 
ATOM   4719 C CB  . THR D 4 48  ? 22.084  29.215  64.861  1.00 99.88  ? 49  THR C CB  1 
ATOM   4720 O OG1 . THR D 4 48  ? 22.465  29.614  63.538  1.00 97.34  ? 49  THR C OG1 1 
ATOM   4721 C CG2 . THR D 4 48  ? 22.299  27.711  64.990  1.00 103.90 ? 49  THR C CG2 1 
ATOM   4722 N N   . ASP D 4 50  ? 22.228  34.180  61.532  1.00 115.49 ? 51  ASP C N   1 
ATOM   4723 C CA  . ASP D 4 50  ? 23.266  35.187  61.331  1.00 126.27 ? 51  ASP C CA  1 
ATOM   4724 C C   . ASP D 4 50  ? 22.823  36.251  60.337  1.00 133.05 ? 51  ASP C C   1 
ATOM   4725 O O   . ASP D 4 50  ? 22.502  35.937  59.197  1.00 129.30 ? 51  ASP C O   1 
ATOM   4726 C CB  . ASP D 4 50  ? 24.561  34.536  60.846  1.00 121.90 ? 51  ASP C CB  1 
ATOM   4727 C CG  . ASP D 4 50  ? 25.761  35.438  61.023  1.00 126.88 ? 51  ASP C CG  1 
ATOM   4728 O OD1 . ASP D 4 50  ? 25.768  36.554  60.464  1.00 130.74 ? 51  ASP C OD1 1 
ATOM   4729 O OD2 . ASP D 4 50  ? 26.690  35.042  61.751  1.00 124.40 ? 51  ASP C OD2 1 
ATOM   4730 N N   . ASP D 4 51  ? 22.832  37.516  60.768  1.00 153.63 ? 52  ASP C N   1 
ATOM   4731 C CA  . ASP D 4 51  ? 22.321  38.598  59.928  1.00 156.24 ? 52  ASP C CA  1 
ATOM   4732 C C   . ASP D 4 51  ? 23.375  39.139  58.967  1.00 157.61 ? 52  ASP C C   1 
ATOM   4733 O O   . ASP D 4 51  ? 23.092  39.331  57.778  1.00 157.70 ? 52  ASP C O   1 
ATOM   4734 C CB  . ASP D 4 51  ? 21.775  39.736  60.788  1.00 160.33 ? 52  ASP C CB  1 
ATOM   4735 C CG  . ASP D 4 51  ? 20.580  40.418  60.149  1.00 166.78 ? 52  ASP C CG  1 
ATOM   4736 O OD1 . ASP D 4 51  ? 20.671  40.778  58.952  1.00 166.73 ? 52  ASP C OD1 1 
ATOM   4737 O OD2 . ASP D 4 51  ? 19.554  40.594  60.841  1.00 169.65 ? 52  ASP C OD2 1 
ATOM   4738 N N   . ALA D 4 52  ? 24.577  39.434  59.472  1.00 140.73 ? 53  ALA C N   1 
ATOM   4739 C CA  . ALA D 4 52  ? 25.656  39.910  58.612  1.00 136.62 ? 53  ALA C CA  1 
ATOM   4740 C C   . ALA D 4 52  ? 25.848  38.983  57.416  1.00 136.32 ? 53  ALA C C   1 
ATOM   4741 O O   . ALA D 4 52  ? 25.616  39.357  56.260  1.00 137.54 ? 53  ALA C O   1 
ATOM   4742 C CB  . ALA D 4 52  ? 26.951  40.019  59.419  1.00 132.40 ? 53  ALA C CB  1 
ATOM   4743 N N   . THR D 4 53  ? 26.241  37.751  57.693  1.00 129.54 ? 54  THR C N   1 
ATOM   4744 C CA  . THR D 4 53  ? 26.480  36.732  56.689  1.00 128.00 ? 54  THR C CA  1 
ATOM   4745 C C   . THR D 4 53  ? 25.205  36.218  56.028  1.00 127.52 ? 54  THR C C   1 
ATOM   4746 O O   . THR D 4 53  ? 25.295  35.478  55.041  1.00 122.19 ? 54  THR C O   1 
ATOM   4747 C CB  . THR D 4 53  ? 27.269  35.600  57.351  1.00 127.82 ? 54  THR C CB  1 
ATOM   4748 O OG1 . THR D 4 53  ? 26.374  34.684  58.014  1.00 124.10 ? 54  THR C OG1 1 
ATOM   4749 C CG2 . THR D 4 53  ? 28.296  36.215  58.347  1.00 123.29 ? 54  THR C CG2 1 
ATOM   4750 N N   . LYS D 4 54  ? 24.033  36.613  56.523  1.00 128.27 ? 55  LYS C N   1 
ATOM   4751 C CA  . LYS D 4 54  ? 22.753  36.153  55.989  1.00 126.35 ? 55  LYS C CA  1 
ATOM   4752 C C   . LYS D 4 54  ? 22.714  34.629  55.847  1.00 119.40 ? 55  LYS C C   1 
ATOM   4753 O O   . LYS D 4 54  ? 22.343  34.092  54.802  1.00 119.85 ? 55  LYS C O   1 
ATOM   4754 C CB  . LYS D 4 54  ? 22.441  36.832  54.655  1.00 123.78 ? 55  LYS C CB  1 
ATOM   4755 N N   . THR D 4 55  ? 23.112  33.927  56.915  1.00 116.40 ? 56  THR C N   1 
ATOM   4756 C CA  . THR D 4 55  ? 22.926  32.480  57.029  1.00 111.80 ? 56  THR C CA  1 
ATOM   4757 C C   . THR D 4 55  ? 22.114  32.125  58.269  1.00 107.32 ? 56  THR C C   1 
ATOM   4758 O O   . THR D 4 55  ? 22.263  32.743  59.331  1.00 112.18 ? 56  THR C O   1 
ATOM   4759 C CB  . THR D 4 55  ? 24.258  31.706  57.078  1.00 112.47 ? 56  THR C CB  1 
ATOM   4760 O OG1 . THR D 4 55  ? 24.753  31.672  58.423  1.00 110.71 ? 56  THR C OG1 1 
ATOM   4761 C CG2 . THR D 4 55  ? 25.301  32.292  56.133  1.00 117.43 ? 56  THR C CG2 1 
ATOM   4762 N N   . PHE D 4 56  ? 21.257  31.121  58.120  1.00 101.14 ? 57  PHE C N   1 
ATOM   4763 C CA  . PHE D 4 56  ? 20.440  30.597  59.206  1.00 95.35  ? 57  PHE C CA  1 
ATOM   4764 C C   . PHE D 4 56  ? 20.622  29.080  59.244  1.00 90.60  ? 57  PHE C C   1 
ATOM   4765 O O   . PHE D 4 56  ? 20.354  28.394  58.251  1.00 86.05  ? 57  PHE C O   1 
ATOM   4766 C CB  . PHE D 4 56  ? 18.973  30.995  59.017  1.00 92.62  ? 57  PHE C CB  1 
ATOM   4767 N N   . THR D 4 57  ? 21.085  28.569  60.390  1.00 94.02  ? 58  THR C N   1 
ATOM   4768 C CA  . THR D 4 57  ? 21.531  27.191  60.568  1.00 87.83  ? 58  THR C CA  1 
ATOM   4769 C C   . THR D 4 57  ? 20.621  26.434  61.528  1.00 92.11  ? 58  THR C C   1 
ATOM   4770 O O   . THR D 4 57  ? 20.230  26.953  62.579  1.00 94.25  ? 58  THR C O   1 
ATOM   4771 C CB  . THR D 4 57  ? 22.972  27.158  61.101  1.00 87.94  ? 58  THR C CB  1 
ATOM   4772 O OG1 . THR D 4 57  ? 23.858  27.735  60.135  1.00 87.94  ? 58  THR C OG1 1 
ATOM   4773 C CG2 . THR D 4 57  ? 23.413  25.746  61.406  1.00 89.10  ? 58  THR C CG2 1 
ATOM   4774 N N   . VAL D 4 58  ? 20.307  25.195  61.164  1.00 93.26  ? 59  VAL C N   1 
ATOM   4775 C CA  . VAL D 4 58  ? 19.540  24.277  61.991  1.00 92.82  ? 59  VAL C CA  1 
ATOM   4776 C C   . VAL D 4 58  ? 20.475  23.145  62.377  1.00 93.62  ? 59  VAL C C   1 
ATOM   4777 O O   . VAL D 4 58  ? 21.267  22.692  61.544  1.00 92.99  ? 59  VAL C O   1 
ATOM   4778 C CB  . VAL D 4 58  ? 18.328  23.736  61.215  1.00 87.58  ? 59  VAL C CB  1 
ATOM   4779 C CG1 . VAL D 4 58  ? 17.470  22.901  62.091  1.00 93.07  ? 59  VAL C CG1 1 
ATOM   4780 C CG2 . VAL D 4 58  ? 17.568  24.849  60.564  1.00 88.84  ? 59  VAL C CG2 1 
ATOM   4781 N N   . THR D 4 59  ? 20.395  22.681  63.626  1.00 98.88  ? 60  THR C N   1 
ATOM   4782 C CA  . THR D 4 59  ? 21.266  21.605  64.093  1.00 96.13  ? 60  THR C CA  1 
ATOM   4783 C C   . THR D 4 59  ? 20.449  20.587  64.879  1.00 102.90 ? 60  THR C C   1 
ATOM   4784 O O   . THR D 4 59  ? 19.389  20.917  65.415  1.00 107.03 ? 60  THR C O   1 
ATOM   4785 C CB  . THR D 4 59  ? 22.414  22.145  64.951  1.00 90.99  ? 60  THR C CB  1 
ATOM   4786 O OG1 . THR D 4 59  ? 22.807  23.440  64.469  1.00 92.86  ? 60  THR C OG1 1 
ATOM   4787 C CG2 . THR D 4 59  ? 23.604  21.217  64.878  1.00 88.41  ? 60  THR C CG2 1 
ATOM   4788 N N   . GLU D 4 60  ? 20.948  19.340  64.941  1.00 102.33 ? 61  GLU C N   1 
ATOM   4789 C CA  . GLU D 4 60  ? 20.197  18.228  65.536  1.00 107.22 ? 61  GLU C CA  1 
ATOM   4790 C C   . GLU D 4 60  ? 20.875  17.550  66.734  1.00 109.51 ? 61  GLU C C   1 
ATOM   4791 O O   . GLU D 4 60  ? 20.427  17.725  67.874  1.00 108.18 ? 61  GLU C O   1 
ATOM   4792 C CB  . GLU D 4 60  ? 19.897  17.153  64.482  1.00 106.39 ? 61  GLU C CB  1 
ATOM   4793 C CG  . GLU D 4 60  ? 18.879  17.538  63.407  1.00 104.26 ? 61  GLU C CG  1 
ATOM   4794 C CD  . GLU D 4 60  ? 17.979  16.370  62.971  1.00 104.56 ? 61  GLU C CD  1 
ATOM   4795 O OE1 . GLU D 4 60  ? 18.495  15.340  62.475  1.00 98.83  ? 61  GLU C OE1 1 
ATOM   4796 O OE2 . GLU D 4 60  ? 16.742  16.494  63.104  1.00 105.09 ? 61  GLU C OE2 1 
ATOM   4797 N N   . LYS D 4 61  ? 21.930  16.735  66.469  1.00 106.73 ? 62  LYS C N   1 
ATOM   4798 C CA  . LYS D 4 61  ? 22.675  15.844  67.375  1.00 103.47 ? 62  LYS C CA  1 
ATOM   4799 C C   . LYS D 4 61  ? 21.920  14.533  67.570  1.00 103.45 ? 62  LYS C C   1 
ATOM   4800 O O   . LYS D 4 61  ? 20.697  14.553  67.758  1.00 107.06 ? 62  LYS C O   1 
ATOM   4801 C CB  . LYS D 4 61  ? 22.951  16.496  68.732  1.00 102.30 ? 62  LYS C CB  1 
ATOM   4802 N N   . PRO D 4 62  ? 22.610  13.370  67.530  1.00 105.32 ? 63  PRO C N   1 
ATOM   4803 C CA  . PRO D 4 62  ? 22.003  12.023  67.580  1.00 105.57 ? 63  PRO C CA  1 
ATOM   4804 C C   . PRO D 4 62  ? 20.983  11.836  68.699  1.00 105.88 ? 63  PRO C C   1 
ATOM   4805 O O   . PRO D 4 62  ? 21.064  10.823  69.389  1.00 109.74 ? 63  PRO C O   1 
ATOM   4806 C CB  . PRO D 4 62  ? 23.207  11.099  67.807  1.00 102.11 ? 63  PRO C CB  1 
ATOM   4807 C CG  . PRO D 4 62  ? 24.339  11.820  67.157  1.00 104.20 ? 63  PRO C CG  1 
ATOM   4808 C CD  . PRO D 4 62  ? 24.078  13.303  67.390  1.00 100.60 ? 63  PRO C CD  1 
HETATM 4809 O O   . HOH E 5 .   ? 16.875  26.083  30.879  1.00 55.78  ? 301 HOH B O   1 
HETATM 4810 O O   . HOH E 5 .   ? 25.886  22.976  7.232   1.00 45.17  ? 302 HOH B O   1 
HETATM 4811 O O   . HOH F 5 .   ? 19.993  1.684   1.511   1.00 42.73  ? 301 HOH D O   1 
HETATM 4812 O O   . HOH F 5 .   ? 17.371  -10.763 17.322  1.00 60.52  ? 302 HOH D O   1 
HETATM 4813 O O   . HOH F 5 .   ? 29.787  -0.016  8.596   1.00 42.87  ? 303 HOH D O   1 
HETATM 4814 O O   . HOH F 5 .   ? 24.552  16.870  22.122  1.00 51.96  ? 304 HOH D O   1 
HETATM 4815 O O   . HOH F 5 .   ? 4.109   11.934  -5.164  1.00 56.21  ? 305 HOH D O   1 
HETATM 4816 O O   . HOH F 5 .   ? 17.194  16.407  3.460   1.00 47.86  ? 306 HOH D O   1 
HETATM 4817 O O   . HOH F 5 .   ? 17.385  12.882  25.011  1.00 47.72  ? 307 HOH D O   1 
HETATM 4818 O O   . HOH F 5 .   ? 26.042  4.862   15.703  1.00 39.80  ? 308 HOH D O   1 
HETATM 4819 O O   . HOH F 5 .   ? 23.434  -7.618  5.068   1.00 50.06  ? 309 HOH D O   1 
HETATM 4820 O O   . HOH F 5 .   ? 28.098  5.380   14.479  1.00 40.53  ? 310 HOH D O   1 
HETATM 4821 O O   . HOH G 5 .   ? 27.638  33.842  66.016  1.00 62.90  ? 101 HOH C O   1 
HETATM 4822 O O   . HOH G 5 .   ? 25.279  32.427  66.582  1.00 60.45  ? 102 HOH C 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   . GLU A 4   ? 1.6518 1.0755 1.1434 -0.0306 0.3615  -0.1275 2   GLU B N   
2    C CA  . GLU A 4   ? 1.6154 1.0393 1.1070 -0.0178 0.3537  -0.1177 2   GLU B CA  
3    C C   . GLU A 4   ? 1.5991 0.9944 1.0744 -0.0127 0.3610  -0.1021 2   GLU B C   
4    O O   . GLU A 4   ? 1.6064 0.9859 1.0747 -0.0157 0.3668  -0.1001 2   GLU B O   
5    C CB  . GLU A 4   ? 1.6409 1.0823 1.1452 -0.0120 0.3407  -0.1236 2   GLU B CB  
6    C CG  . GLU A 4   ? 1.7075 1.1405 1.2071 -0.0013 0.3359  -0.1118 2   GLU B CG  
7    C CD  . GLU A 4   ? 1.7500 1.1896 1.2553 0.0012  0.3280  -0.1159 2   GLU B CD  
8    O OE1 . GLU A 4   ? 1.8360 1.2898 1.3492 0.0062  0.3170  -0.1208 2   GLU B OE1 
9    O OE2 . GLU A 4   ? 1.6883 1.1174 1.1887 -0.0016 0.3327  -0.1144 2   GLU B OE2 
10   N N   . VAL A 5   ? 1.4102 0.7999 0.8795 -0.0045 0.3605  -0.0922 3   VAL B N   
11   C CA  . VAL A 5   ? 1.3446 0.7099 0.7989 0.0026  0.3661  -0.0780 3   VAL B CA  
12   C C   . VAL A 5   ? 1.3434 0.7112 0.8009 0.0112  0.3590  -0.0733 3   VAL B C   
13   O O   . VAL A 5   ? 1.3328 0.7179 0.8000 0.0165  0.3491  -0.0748 3   VAL B O   
14   C CB  . VAL A 5   ? 1.2189 0.5797 0.6662 0.0086  0.3678  -0.0703 3   VAL B CB  
15   C CG1 . VAL A 5   ? 1.2324 0.6192 0.6936 0.0130  0.3570  -0.0747 3   VAL B CG1 
16   C CG2 . VAL A 5   ? 1.2071 0.5490 0.6421 0.0196  0.3699  -0.0565 3   VAL B CG2 
17   N N   . GLN A 6   ? 1.3021 0.6517 0.7501 0.0123  0.3646  -0.0681 4   GLN B N   
18   C CA  . GLN A 6   ? 1.2529 0.6039 0.7018 0.0197  0.3597  -0.0637 4   GLN B CA  
19   C C   . GLN A 6   ? 1.1791 0.5101 0.6140 0.0285  0.3652  -0.0518 4   GLN B C   
20   O O   . GLN A 6   ? 1.2121 0.5240 0.6347 0.0283  0.3735  -0.0472 4   GLN B O   
21   C CB  . GLN A 6   ? 1.2601 0.6132 0.7129 0.0138  0.3597  -0.0713 4   GLN B CB  
22   C CG  . GLN A 6   ? 1.4120 0.7887 0.8796 0.0106  0.3499  -0.0819 4   GLN B CG  
23   C CD  . GLN A 6   ? 1.5152 0.8963 0.9881 0.0005  0.3521  -0.0935 4   GLN B CD  
24   O OE1 . GLN A 6   ? 1.5011 0.8753 0.9710 -0.0012 0.3550  -0.0946 4   GLN B OE1 
25   N NE2 . GLN A 6   ? 1.4979 0.8919 0.9790 -0.0063 0.3508  -0.1032 4   GLN B NE2 
26   N N   . LEU A 7   ? 1.1343 0.4695 0.5701 0.0366  0.3605  -0.0473 5   LEU B N   
27   C CA  . LEU A 7   ? 1.1584 0.4793 0.5828 0.0465  0.3643  -0.0376 5   LEU B CA  
28   C C   . LEU A 7   ? 1.2041 0.5313 0.6310 0.0497  0.3610  -0.0384 5   LEU B C   
29   O O   . LEU A 7   ? 1.2610 0.6053 0.6967 0.0502  0.3534  -0.0407 5   LEU B O   
30   C CB  . LEU A 7   ? 1.1630 0.4879 0.5862 0.0558  0.3613  -0.0299 5   LEU B CB  
31   C CG  . LEU A 7   ? 1.1890 0.5007 0.6030 0.0571  0.3670  -0.0256 5   LEU B CG  
32   C CD1 . LEU A 7   ? 1.1205 0.4341 0.5309 0.0696  0.3645  -0.0167 5   LEU B CD1 
33   C CD2 . LEU A 7   ? 1.1922 0.4768 0.5906 0.0543  0.3777  -0.0241 5   LEU B CD2 
34   N N   . VAL A 8   ? 1.2086 0.5213 0.6265 0.0517  0.3670  -0.0370 6   VAL B N   
35   C CA  . VAL A 8   ? 1.1514 0.4709 0.5718 0.0533  0.3647  -0.0399 6   VAL B CA  
36   C C   . VAL A 8   ? 1.1666 0.4765 0.5769 0.0642  0.3681  -0.0334 6   VAL B C   
37   O O   . VAL A 8   ? 1.2559 0.5452 0.6544 0.0660  0.3756  -0.0313 6   VAL B O   
38   C CB  . VAL A 8   ? 1.1243 0.4401 0.5462 0.0436  0.3678  -0.0487 6   VAL B CB  
39   C CG1 . VAL A 8   ? 1.1232 0.4533 0.5514 0.0439  0.3628  -0.0537 6   VAL B CG1 
40   C CG2 . VAL A 8   ? 1.1277 0.4484 0.5567 0.0330  0.3672  -0.0554 6   VAL B CG2 
41   N N   . GLU A 9   ? 1.1394 0.4635 0.5531 0.0716  0.3631  -0.0308 7   GLU B N   
42   C CA  . GLU A 9   ? 1.1993 0.5204 0.6058 0.0824  0.3653  -0.0270 7   GLU B CA  
43   C C   . GLU A 9   ? 1.2143 0.5363 0.6201 0.0811  0.3669  -0.0331 7   GLU B C   
44   O O   . GLU A 9   ? 1.1959 0.5249 0.6082 0.0725  0.3648  -0.0399 7   GLU B O   
45   C CB  . GLU A 9   ? 1.1773 0.5163 0.5881 0.0900  0.3597  -0.0227 7   GLU B CB  
46   C CG  . GLU A 9   ? 1.1309 0.4710 0.5427 0.0929  0.3577  -0.0170 7   GLU B CG  
47   C CD  . GLU A 9   ? 1.1622 0.5141 0.5837 0.0849  0.3519  -0.0197 7   GLU B CD  
48   O OE1 . GLU A 9   ? 1.1668 0.5198 0.5926 0.0756  0.3508  -0.0262 7   GLU B OE1 
49   O OE2 . GLU A 9   ? 1.1447 0.5047 0.5690 0.0883  0.3482  -0.0159 7   GLU B OE2 
50   N N   . SER A 10  ? 1.2566 0.5726 0.6543 0.0907  0.3702  -0.0314 8   SER B N   
51   C CA  . SER A 10  ? 1.2422 0.5564 0.6374 0.0913  0.3728  -0.0377 8   SER B CA  
52   C C   . SER A 10  ? 1.2551 0.5695 0.6431 0.1049  0.3744  -0.0354 8   SER B C   
53   O O   . SER A 10  ? 1.2509 0.5580 0.6322 0.1136  0.3757  -0.0289 8   SER B O   
54   C CB  . SER A 10  ? 1.2192 0.5113 0.6078 0.0841  0.3792  -0.0417 8   SER B CB  
55   O OG  . SER A 10  ? 1.3288 0.6283 0.7266 0.0718  0.3771  -0.0484 8   SER B OG  
56   N N   . GLY A 11  ? 1.3188 0.6420 0.7079 0.1072  0.3743  -0.0419 9   GLY B N   
57   C CA  . GLY A 11  ? 1.2761 0.6034 0.6598 0.1203  0.3754  -0.0424 9   GLY B CA  
58   C C   . GLY A 11  ? 1.2964 0.6523 0.6869 0.1259  0.3706  -0.0415 9   GLY B C   
59   O O   . GLY A 11  ? 1.2651 0.6286 0.6521 0.1377  0.3712  -0.0419 9   GLY B O   
60   N N   . GLY A 12  ? 1.3516 0.7240 0.7510 0.1177  0.3661  -0.0408 10  GLY B N   
61   C CA  . GLY A 12  ? 1.3338 0.7330 0.7378 0.1210  0.3625  -0.0399 10  GLY B CA  
62   C C   . GLY A 12  ? 1.3410 0.7576 0.7459 0.1220  0.3627  -0.0475 10  GLY B C   
63   O O   . GLY A 12  ? 1.3576 0.7681 0.7622 0.1172  0.3641  -0.0540 10  GLY B O   
64   N N   . GLY A 13  ? 1.1344 0.5750 0.5405 0.1282  0.3615  -0.0472 11  GLY B N   
65   C CA  . GLY A 13  ? 1.1356 0.5976 0.5425 0.1282  0.3617  -0.0542 11  GLY B CA  
66   C C   . GLY A 13  ? 1.1770 0.6660 0.5845 0.1368  0.3617  -0.0542 11  GLY B C   
67   O O   . GLY A 13  ? 1.1307 0.6268 0.5395 0.1395  0.3602  -0.0478 11  GLY B O   
68   N N   . LEU A 14  ? 1.1422 0.6489 0.5492 0.1408  0.3632  -0.0623 12  LEU B N   
69   C CA  . LEU A 14  ? 1.1419 0.6796 0.5501 0.1481  0.3635  -0.0642 12  LEU B CA  
70   C C   . LEU A 14  ? 1.1592 0.6896 0.5645 0.1633  0.3658  -0.0686 12  LEU B C   
71   O O   . LEU A 14  ? 1.1742 0.6811 0.5755 0.1669  0.3676  -0.0729 12  LEU B O   
72   C CB  . LEU A 14  ? 1.1396 0.7060 0.5486 0.1429  0.3638  -0.0709 12  LEU B CB  
73   C CG  . LEU A 14  ? 1.1692 0.7725 0.5794 0.1497  0.3652  -0.0767 12  LEU B CG  
74   C CD1 . LEU A 14  ? 1.1823 0.8058 0.5946 0.1500  0.3641  -0.0697 12  LEU B CD1 
75   C CD2 . LEU A 14  ? 1.2549 0.8839 0.6644 0.1422  0.3657  -0.0830 12  LEU B CD2 
76   N N   . VAL A 15  ? 1.1585 0.7081 0.5650 0.1721  0.3655  -0.0673 13  VAL B N   
77   C CA  . VAL A 15  ? 1.1760 0.7190 0.5788 0.1882  0.3668  -0.0709 13  VAL B CA  
78   C C   . VAL A 15  ? 1.1729 0.7553 0.5798 0.1955  0.3665  -0.0750 13  VAL B C   
79   O O   . VAL A 15  ? 1.1793 0.7865 0.5908 0.1879  0.3654  -0.0706 13  VAL B O   
80   C CB  . VAL A 15  ? 1.2592 0.7701 0.6569 0.1925  0.3665  -0.0618 13  VAL B CB  
81   C CG1 . VAL A 15  ? 1.2864 0.8004 0.6805 0.2094  0.3665  -0.0627 13  VAL B CG1 
82   C CG2 . VAL A 15  ? 1.2934 0.7651 0.6844 0.1895  0.3684  -0.0614 13  VAL B CG2 
83   N N   . GLN A 16  ? 1.2185 0.8075 0.6235 0.2097  0.3676  -0.0843 14  GLN B N   
84   C CA  . GLN A 16  ? 1.2476 0.8749 0.6569 0.2184  0.3676  -0.0903 14  GLN B CA  
85   C C   . GLN A 16  ? 1.2381 0.8638 0.6471 0.2269  0.3661  -0.0835 14  GLN B C   
86   O O   . GLN A 16  ? 1.2796 0.8705 0.6819 0.2340  0.3655  -0.0782 14  GLN B O   
87   C CB  . GLN A 16  ? 1.3194 0.9515 0.7269 0.2327  0.3686  -0.1038 14  GLN B CB  
88   C CG  . GLN A 16  ? 1.4196 1.0539 0.8274 0.2278  0.3700  -0.1128 14  GLN B CG  
89   C CD  . GLN A 16  ? 1.4983 1.1726 0.9108 0.2355  0.3710  -0.1270 14  GLN B CD  
90   O OE1 . GLN A 16  ? 1.4126 1.1212 0.8298 0.2383  0.3711  -0.1286 14  GLN B OE1 
91   N NE2 . GLN A 16  ? 1.6016 1.2723 1.0130 0.2392  0.3719  -0.1385 14  GLN B NE2 
92   N N   . PRO A 17  ? 1.2196 0.8839 0.6348 0.2269  0.3658  -0.0845 15  PRO B N   
93   C CA  . PRO A 17  ? 1.2368 0.9051 0.6524 0.2384  0.3643  -0.0814 15  PRO B CA  
94   C C   . PRO A 17  ? 1.2673 0.9135 0.6758 0.2582  0.3637  -0.0869 15  PRO B C   
95   O O   . PRO A 17  ? 1.2760 0.9247 0.6829 0.2660  0.3646  -0.0979 15  PRO B O   
96   C CB  . PRO A 17  ? 1.2119 0.9325 0.6357 0.2359  0.3651  -0.0871 15  PRO B CB  
97   C CG  . PRO A 17  ? 1.1869 0.9237 0.6132 0.2168  0.3665  -0.0858 15  PRO B CG  
98   C CD  . PRO A 17  ? 1.1809 0.8890 0.6023 0.2168  0.3671  -0.0896 15  PRO B CD  
99   N N   . GLY A 18  ? 1.2889 0.9118 0.6919 0.2668  0.3620  -0.0791 16  GLY B N   
100  C CA  . GLY A 18  ? 1.2916 0.8847 0.6839 0.2846  0.3612  -0.0816 16  GLY B CA  
101  C C   . GLY A 18  ? 1.3036 0.8524 0.6857 0.2819  0.3628  -0.0796 16  GLY B C   
102  O O   . GLY A 18  ? 1.3479 0.8667 0.7183 0.2956  0.3623  -0.0805 16  GLY B O   
103  N N   . GLY A 19  ? 1.2410 0.7841 0.6263 0.2646  0.3644  -0.0771 17  GLY B N   
104  C CA  . GLY A 19  ? 1.2652 0.7701 0.6423 0.2601  0.3663  -0.0765 17  GLY B CA  
105  C C   . GLY A 19  ? 1.3458 0.8095 0.7130 0.2570  0.3670  -0.0642 17  GLY B C   
106  O O   . GLY A 19  ? 1.3447 0.8090 0.7127 0.2560  0.3658  -0.0552 17  GLY B O   
107  N N   . SER A 20  ? 1.3205 0.7487 0.6782 0.2549  0.3694  -0.0647 18  SER B N   
108  C CA  . SER A 20  ? 1.3341 0.7217 0.6803 0.2504  0.3715  -0.0543 18  SER B CA  
109  C C   . SER A 20  ? 1.3153 0.6942 0.6665 0.2306  0.3733  -0.0518 18  SER B C   
110  O O   . SER A 20  ? 1.2755 0.6551 0.6293 0.2250  0.3744  -0.0594 18  SER B O   
111  C CB  . SER A 20  ? 1.3342 0.6849 0.6630 0.2623  0.3734  -0.0565 18  SER B CB  
112  O OG  . SER A 20  ? 1.3355 0.6523 0.6565 0.2501  0.3773  -0.0535 18  SER B OG  
113  N N   . LEU A 21  ? 1.3243 0.6956 0.6770 0.2208  0.3732  -0.0419 19  LEU B N   
114  C CA  . LEU A 21  ? 1.2764 0.6353 0.6326 0.2032  0.3746  -0.0395 19  LEU B CA  
115  C C   . LEU A 21  ? 1.3027 0.6272 0.6476 0.2002  0.3774  -0.0305 19  LEU B C   
116  O O   . LEU A 21  ? 1.3358 0.6510 0.6720 0.2105  0.3775  -0.0246 19  LEU B O   
117  C CB  . LEU A 21  ? 1.2757 0.6638 0.6467 0.1917  0.3711  -0.0379 19  LEU B CB  
118  C CG  . LEU A 21  ? 1.2776 0.6603 0.6541 0.1748  0.3713  -0.0392 19  LEU B CG  
119  C CD1 . LEU A 21  ? 1.2495 0.6246 0.6232 0.1737  0.3738  -0.0482 19  LEU B CD1 
120  C CD2 . LEU A 21  ? 1.2237 0.6346 0.6123 0.1653  0.3674  -0.0384 19  LEU B CD2 
121  N N   . ARG A 22  ? 1.2712 0.5777 0.6155 0.1860  0.3800  -0.0301 20  ARG B N   
122  C CA  . ARG A 22  ? 1.2842 0.5608 0.6183 0.1803  0.3837  -0.0224 20  ARG B CA  
123  C C   . ARG A 22  ? 1.2821 0.5608 0.6261 0.1622  0.3834  -0.0222 20  ARG B C   
124  O O   . ARG A 22  ? 1.2488 0.5220 0.5947 0.1529  0.3852  -0.0281 20  ARG B O   
125  C CB  . ARG A 22  ? 1.3354 0.5758 0.6504 0.1845  0.3896  -0.0231 20  ARG B CB  
126  C CG  . ARG A 22  ? 1.3611 0.5745 0.6593 0.1893  0.3930  -0.0135 20  ARG B CG  
127  C CD  . ARG A 22  ? 1.3997 0.5721 0.6762 0.1886  0.4002  -0.0130 20  ARG B CD  
128  N NE  . ARG A 22  ? 1.4388 0.6029 0.7190 0.1723  0.4039  -0.0183 20  ARG B NE  
129  C CZ  . ARG A 22  ? 1.4884 0.6186 0.7525 0.1642  0.4113  -0.0170 20  ARG B CZ  
130  N NH1 . ARG A 22  ? 1.4694 0.5688 0.7109 0.1696  0.4164  -0.0092 20  ARG B NH1 
131  N NH2 . ARG A 22  ? 1.4281 0.5558 0.6981 0.1499  0.4140  -0.0237 20  ARG B NH2 
132  N N   . LEU A 23  ? 1.3058 0.5907 0.6552 0.1578  0.3810  -0.0159 21  LEU B N   
133  C CA  . LEU A 23  ? 1.2584 0.5448 0.6167 0.1422  0.3800  -0.0160 21  LEU B CA  
134  C C   . LEU A 23  ? 1.2283 0.4844 0.5750 0.1359  0.3859  -0.0125 21  LEU B C   
135  O O   . LEU A 23  ? 1.2516 0.4858 0.5825 0.1440  0.3902  -0.0073 21  LEU B O   
136  C CB  . LEU A 23  ? 1.2195 0.5292 0.5902 0.1404  0.3740  -0.0125 21  LEU B CB  
137  C CG  . LEU A 23  ? 1.2063 0.5437 0.5837 0.1494  0.3696  -0.0132 21  LEU B CG  
138  C CD1 . LEU A 23  ? 1.1772 0.5348 0.5662 0.1440  0.3642  -0.0105 21  LEU B CD1 
139  C CD2 . LEU A 23  ? 1.2655 0.6166 0.6470 0.1485  0.3692  -0.0210 21  LEU B CD2 
140  N N   . SER A 24  ? 1.2190 0.4747 0.5728 0.1212  0.3861  -0.0157 22  SER B N   
141  C CA  . SER A 24  ? 1.2504 0.4813 0.5949 0.1120  0.3923  -0.0144 22  SER B CA  
142  C C   . SER A 24  ? 1.2691 0.5140 0.6272 0.1004  0.3884  -0.0152 22  SER B C   
143  O O   . SER A 24  ? 1.2712 0.5352 0.6434 0.0929  0.3836  -0.0212 22  SER B O   
144  C CB  . SER A 24  ? 1.2515 0.4661 0.5897 0.1054  0.3979  -0.0210 22  SER B CB  
145  O OG  . SER A 24  ? 1.2491 0.4808 0.6027 0.0931  0.3946  -0.0284 22  SER B OG  
146  N N   . CYS A 25  ? 1.2525 0.4884 0.6056 0.0998  0.3900  -0.0098 23  CYS B N   
147  C CA  . CYS A 25  ? 1.2151 0.4638 0.5803 0.0899  0.3862  -0.0114 23  CYS B CA  
148  C C   . CYS A 25  ? 1.2483 0.4784 0.6072 0.0773  0.3933  -0.0150 23  CYS B C   
149  O O   . CYS A 25  ? 1.2895 0.4954 0.6324 0.0779  0.4007  -0.0105 23  CYS B O   
150  C CB  . CYS A 25  ? 1.2075 0.4618 0.5727 0.0975  0.3832  -0.0045 23  CYS B CB  
151  S SG  . CYS A 25  ? 1.1627 0.4338 0.5421 0.0877  0.3779  -0.0070 23  CYS B SG  
152  N N   . ALA A 26  ? 1.2186 0.4593 0.5887 0.0659  0.3916  -0.0235 24  ALA B N   
153  C CA  . ALA A 26  ? 1.2110 0.4376 0.5769 0.0528  0.3985  -0.0291 24  ALA B CA  
154  C C   . ALA A 26  ? 1.2010 0.4400 0.5770 0.0439  0.3958  -0.0322 24  ALA B C   
155  O O   . ALA A 26  ? 1.2126 0.4775 0.6054 0.0422  0.3869  -0.0363 24  ALA B O   
156  C CB  . ALA A 26  ? 1.2030 0.4365 0.5762 0.0459  0.3979  -0.0380 24  ALA B CB  
157  N N   . ALA A 27  ? 1.2086 0.4285 0.5731 0.0378  0.4038  -0.0312 25  ALA B N   
158  C CA  . ALA A 27  ? 1.1975 0.4293 0.5700 0.0309  0.4017  -0.0341 25  ALA B CA  
159  C C   . ALA A 27  ? 1.1983 0.4326 0.5760 0.0151  0.4055  -0.0448 25  ALA B C   
160  O O   . ALA A 27  ? 1.2480 0.4623 0.6150 0.0082  0.4142  -0.0475 25  ALA B O   
161  C CB  . ALA A 27  ? 1.2152 0.4272 0.5715 0.0354  0.4077  -0.0261 25  ALA B CB  
162  N N   . SER A 28  ? 1.1753 0.4347 0.5692 0.0095  0.3989  -0.0516 26  SER B N   
163  C CA  . SER A 28  ? 1.2292 0.4954 0.6294 -0.0050 0.4018  -0.0629 26  SER B CA  
164  C C   . SER A 28  ? 1.2768 0.5617 0.6861 -0.0077 0.3977  -0.0665 26  SER B C   
165  O O   . SER A 28  ? 1.2451 0.5479 0.6636 0.0009  0.3884  -0.0637 26  SER B O   
166  C CB  . SER A 28  ? 1.2233 0.5093 0.6390 -0.0092 0.3955  -0.0726 26  SER B CB  
167  O OG  . SER A 28  ? 1.2425 0.5469 0.6703 -0.0204 0.3938  -0.0848 26  SER B OG  
168  N N   . GLY A 29  ? 1.2566 0.5375 0.6624 -0.0200 0.4051  -0.0734 27  GLY B N   
169  C CA  . GLY A 29  ? 1.2350 0.5331 0.6474 -0.0233 0.4028  -0.0778 27  GLY B CA  
170  C C   . GLY A 29  ? 1.2031 0.4824 0.5989 -0.0194 0.4092  -0.0684 27  GLY B C   
171  O O   . GLY A 29  ? 1.1767 0.4715 0.5773 -0.0219 0.4076  -0.0721 27  GLY B O   
172  N N   . PHE A 30  ? 1.2164 0.4639 0.5924 -0.0126 0.4161  -0.0572 28  PHE B N   
173  C CA  . PHE A 30  ? 1.2258 0.4541 0.5845 -0.0065 0.4213  -0.0478 28  PHE B CA  
174  C C   . PHE A 30  ? 1.2583 0.4470 0.5928 0.0000  0.4301  -0.0376 28  PHE B C   
175  O O   . PHE A 30  ? 1.2568 0.4411 0.5923 0.0046  0.4284  -0.0358 28  PHE B O   
176  C CB  . PHE A 30  ? 1.1994 0.4511 0.5699 0.0063  0.4101  -0.0432 28  PHE B CB  
177  C CG  . PHE A 30  ? 1.1909 0.4406 0.5621 0.0206  0.4042  -0.0346 28  PHE B CG  
178  C CD1 . PHE A 30  ? 1.1673 0.4364 0.5548 0.0221  0.3957  -0.0384 28  PHE B CD1 
179  C CD2 . PHE A 30  ? 1.2066 0.4371 0.5622 0.0330  0.4068  -0.0232 28  PHE B CD2 
180  C CE1 . PHE A 30  ? 1.1600 0.4296 0.5481 0.0343  0.3906  -0.0312 28  PHE B CE1 
181  C CE2 . PHE A 30  ? 1.1983 0.4308 0.5556 0.0461  0.4013  -0.0164 28  PHE B CE2 
182  C CZ  . PHE A 30  ? 1.1751 0.4275 0.5486 0.0461  0.3935  -0.0205 28  PHE B CZ  
183  N N   . ASN A 31  ? 1.2889 0.4495 0.6006 0.0010  0.4392  -0.0312 29  ASN B N   
184  C CA  . ASN A 31  ? 1.3244 0.4441 0.6091 0.0096  0.4475  -0.0209 29  ASN B CA  
185  C C   . ASN A 31  ? 1.3176 0.4399 0.5997 0.0287  0.4410  -0.0103 29  ASN B C   
186  O O   . ASN A 31  ? 1.3429 0.4772 0.6277 0.0319  0.4379  -0.0087 29  ASN B O   
187  C CB  . ASN A 31  ? 1.4066 0.4880 0.6633 -0.0008 0.4623  -0.0208 29  ASN B CB  
188  C CG  . ASN A 31  ? 1.4978 0.5315 0.7226 0.0079  0.4717  -0.0108 29  ASN B CG  
189  O OD1 . ASN A 31  ? 1.5298 0.5471 0.7387 0.0217  0.4721  -0.0014 29  ASN B OD1 
190  N ND2 . ASN A 31  ? 1.5376 0.5512 0.7534 0.0015  0.4786  -0.0129 29  ASN B ND2 
191  N N   . VAL A 32  ? 1.3260 0.4390 0.6032 0.0411  0.4391  -0.0038 30  VAL B N   
192  C CA  . VAL A 32  ? 1.3242 0.4462 0.6031 0.0593  0.4315  0.0048  30  VAL B CA  
193  C C   . VAL A 32  ? 1.4164 0.5091 0.6693 0.0696  0.4378  0.0141  30  VAL B C   
194  O O   . VAL A 32  ? 1.3896 0.4923 0.6442 0.0847  0.4315  0.0206  30  VAL B O   
195  C CB  . VAL A 32  ? 1.3539 0.4776 0.6356 0.0675  0.4282  0.0068  30  VAL B CB  
196  C CG1 . VAL A 32  ? 1.3912 0.4787 0.6504 0.0631  0.4396  0.0072  30  VAL B CG1 
197  C CG2 . VAL A 32  ? 1.3889 0.5170 0.6679 0.0865  0.4226  0.0153  30  VAL B CG2 
198  N N   . SER A 33  ? 1.5353 0.5913 0.7628 0.0618  0.4502  0.0145  31  SER B N   
199  C CA  . SER A 33  ? 1.5616 0.5854 0.7607 0.0723  0.4565  0.0231  31  SER B CA  
200  C C   . SER A 33  ? 1.5553 0.6043 0.7648 0.0743  0.4507  0.0228  31  SER B C   
201  O O   . SER A 33  ? 1.5705 0.6148 0.7698 0.0897  0.4485  0.0306  31  SER B O   
202  C CB  . SER A 33  ? 1.6209 0.5958 0.7878 0.0617  0.4717  0.0223  31  SER B CB  
203  O OG  . SER A 33  ? 1.7115 0.6431 0.8437 0.0762  0.4784  0.0320  31  SER B OG  
204  N N   . TYR A 34  ? 1.4582 0.5358 0.6875 0.0593  0.4481  0.0137  32  TYR B N   
205  C CA  . TYR A 34  ? 1.4449 0.5513 0.6855 0.0603  0.4421  0.0130  32  TYR B CA  
206  C C   . TYR A 34  ? 1.4189 0.5623 0.6834 0.0732  0.4284  0.0153  32  TYR B C   
207  O O   . TYR A 34  ? 1.3658 0.5263 0.6337 0.0797  0.4239  0.0179  32  TYR B O   
208  C CB  . TYR A 34  ? 1.4528 0.5832 0.7086 0.0410  0.4426  0.0018  32  TYR B CB  
209  C CG  . TYR A 34  ? 1.5208 0.6242 0.7607 0.0235  0.4550  -0.0040 32  TYR B CG  
210  C CD1 . TYR A 34  ? 1.6212 0.6795 0.8270 0.0226  0.4672  0.0011  32  TYR B CD1 
211  C CD2 . TYR A 34  ? 1.4928 0.6167 0.7512 0.0074  0.4543  -0.0156 32  TYR B CD2 
212  C CE1 . TYR A 34  ? 1.6607 0.6939 0.8509 0.0048  0.4791  -0.0051 32  TYR B CE1 
213  C CE2 . TYR A 34  ? 1.5349 0.6375 0.7801 -0.0099 0.4658  -0.0219 32  TYR B CE2 
214  C CZ  . TYR A 34  ? 1.6476 0.7042 0.8586 -0.0120 0.4785  -0.0166 32  TYR B CZ  
215  O OH  . TYR A 34  ? 1.7542 0.7879 0.9505 -0.0308 0.4905  -0.0236 32  TYR B OH  
216  N N   . TYR A 35  ? 1.3853 0.5424 0.6658 0.0761  0.4220  0.0139  33  TYR B N   
217  C CA  . TYR A 35  ? 1.2530 0.4479 0.5583 0.0834  0.4091  0.0132  33  TYR B CA  
218  C C   . TYR A 35  ? 1.2549 0.4453 0.5552 0.1011  0.4056  0.0219  33  TYR B C   
219  O O   . TYR A 35  ? 1.3887 0.5486 0.6687 0.1079  0.4121  0.0276  33  TYR B O   
220  C CB  . TYR A 35  ? 1.2246 0.4426 0.5524 0.0734  0.4034  0.0044  33  TYR B CB  
221  C CG  . TYR A 35  ? 1.2131 0.4479 0.5525 0.0577  0.4035  -0.0060 33  TYR B CG  
222  C CD1 . TYR A 35  ? 1.1828 0.4525 0.5421 0.0566  0.3944  -0.0113 33  TYR B CD1 
223  C CD2 . TYR A 35  ? 1.2334 0.4500 0.5638 0.0439  0.4127  -0.0114 33  TYR B CD2 
224  C CE1 . TYR A 35  ? 1.1727 0.4600 0.5429 0.0433  0.3940  -0.0221 33  TYR B CE1 
225  C CE2 . TYR A 35  ? 1.2224 0.4580 0.5646 0.0295  0.4126  -0.0222 33  TYR B CE2 
226  C CZ  . TYR A 35  ? 1.1917 0.4635 0.5541 0.0297  0.4030  -0.0277 33  TYR B CZ  
227  O OH  . TYR A 35  ? 1.1822 0.4742 0.5559 0.0164  0.4028  -0.0395 33  TYR B OH  
228  N N   . SER A 36  ? 1.2271 0.4489 0.5459 0.1084  0.3951  0.0222  34  SER B N   
229  C CA  . SER A 36  ? 1.2268 0.4528 0.5457 0.1236  0.3905  0.0284  34  SER B CA  
230  C C   . SER A 36  ? 1.2281 0.4700 0.5636 0.1197  0.3852  0.0238  34  SER B C   
231  O O   . SER A 36  ? 1.1846 0.4470 0.5380 0.1088  0.3805  0.0164  34  SER B O   
232  C CB  . SER A 36  ? 1.2414 0.4925 0.5698 0.1333  0.3828  0.0310  34  SER B CB  
233  O OG  . SER A 36  ? 1.2465 0.4954 0.5681 0.1495  0.3810  0.0379  34  SER B OG  
234  N N   . ILE A 37  ? 1.2295 0.4620 0.5579 0.1288  0.3861  0.0277  35  ILE B N   
235  C CA  . ILE A 37  ? 1.1929 0.4379 0.5338 0.1254  0.3824  0.0234  35  ILE B CA  
236  C C   . ILE A 37  ? 1.2103 0.4692 0.5547 0.1392  0.3771  0.0271  35  ILE B C   
237  O O   . ILE A 37  ? 1.2061 0.4515 0.5354 0.1523  0.3800  0.0332  35  ILE B O   
238  C CB  . ILE A 37  ? 1.2156 0.4351 0.5443 0.1188  0.3904  0.0215  35  ILE B CB  
239  C CG1 . ILE A 37  ? 1.2302 0.4321 0.5510 0.1058  0.3976  0.0184  35  ILE B CG1 
240  C CG2 . ILE A 37  ? 1.1959 0.4325 0.5402 0.1127  0.3859  0.0153  35  ILE B CG2 
241  C CD1 . ILE A 37  ? 1.2043 0.4288 0.5449 0.0917  0.3932  0.0095  35  ILE B CD1 
242  N N   . HIS A 38  ? 1.2017 0.4874 0.5650 0.1362  0.3697  0.0228  36  HIS B N   
243  C CA  . HIS A 38  ? 1.1705 0.4772 0.5414 0.1464  0.3638  0.0246  36  HIS B CA  
244  C C   . HIS A 38  ? 1.1604 0.4783 0.5403 0.1426  0.3614  0.0201  36  HIS B C   
245  O O   . HIS A 38  ? 1.1455 0.4615 0.5305 0.1310  0.3618  0.0149  36  HIS B O   
246  C CB  . HIS A 38  ? 1.1208 0.4515 0.5051 0.1463  0.3568  0.0242  36  HIS B CB  
247  C CG  . HIS A 38  ? 1.1803 0.5037 0.5589 0.1463  0.3586  0.0264  36  HIS B CG  
248  N ND1 . HIS A 38  ? 1.1317 0.4603 0.5061 0.1577  0.3572  0.0315  36  HIS B ND1 
249  C CD2 . HIS A 38  ? 1.1479 0.4606 0.5240 0.1363  0.3620  0.0237  36  HIS B CD2 
250  C CE1 . HIS A 38  ? 1.1890 0.5095 0.5579 0.1549  0.3597  0.0321  36  HIS B CE1 
251  N NE2 . HIS A 38  ? 1.1564 0.4678 0.5265 0.1416  0.3627  0.0272  36  HIS B NE2 
252  N N   . TRP A 39  ? 1.1576 0.4887 0.5390 0.1527  0.3589  0.0215  37  TRP B N   
253  C CA  . TRP A 39  ? 1.1414 0.4880 0.5316 0.1502  0.3562  0.0173  37  TRP B CA  
254  C C   . TRP A 39  ? 1.1150 0.4894 0.5167 0.1533  0.3499  0.0175  37  TRP B C   
255  O O   . TRP A 39  ? 1.1016 0.4840 0.5012 0.1640  0.3489  0.0212  37  TRP B O   
256  C CB  . TRP A 39  ? 1.1812 0.5195 0.5616 0.1589  0.3601  0.0172  37  TRP B CB  
257  C CG  . TRP A 39  ? 1.1898 0.5012 0.5589 0.1542  0.3665  0.0157  37  TRP B CG  
258  C CD1 . TRP A 39  ? 1.2196 0.5028 0.5707 0.1592  0.3730  0.0197  37  TRP B CD1 
259  C CD2 . TRP A 39  ? 1.2438 0.5529 0.6168 0.1438  0.3677  0.0098  37  TRP B CD2 
260  N NE1 . TRP A 39  ? 1.2025 0.4656 0.5463 0.1516  0.3785  0.0165  37  TRP B NE1 
261  C CE2 . TRP A 39  ? 1.2638 0.5437 0.6220 0.1421  0.3751  0.0100  37  TRP B CE2 
262  C CE3 . TRP A 39  ? 1.1866 0.5146 0.5727 0.1358  0.3635  0.0043  37  TRP B CE3 
263  C CZ2 . TRP A 39  ? 1.2634 0.5351 0.6217 0.1325  0.3780  0.0043  37  TRP B CZ2 
264  C CZ3 . TRP A 39  ? 1.1806 0.5003 0.5664 0.1270  0.3660  -0.0012 37  TRP B CZ3 
265  C CH2 . TRP A 39  ? 1.2197 0.5128 0.5928 0.1254  0.3731  -0.0015 37  TRP B CH2 
266  N N   . VAL A 40  ? 1.1358 0.5238 0.5480 0.1438  0.3460  0.0135  38  VAL B N   
267  C CA  . VAL A 40  ? 1.1078 0.5196 0.5290 0.1437  0.3408  0.0134  38  VAL B CA  
268  C C   . VAL A 40  ? 1.0838 0.5060 0.5082 0.1386  0.3400  0.0096  38  VAL B C   
269  O O   . VAL A 40  ? 1.0621 0.4746 0.4860 0.1305  0.3410  0.0059  38  VAL B O   
270  C CB  . VAL A 40  ? 1.0871 0.5025 0.5149 0.1364  0.3366  0.0125  38  VAL B CB  
271  C CG1 . VAL A 40  ? 1.0955 0.5281 0.5271 0.1425  0.3331  0.0154  38  VAL B CG1 
272  C CG2 . VAL A 40  ? 1.0566 0.4540 0.4808 0.1332  0.3389  0.0124  38  VAL B CG2 
273  N N   . ARG A 41  ? 1.1136 0.5568 0.5408 0.1425  0.3383  0.0104  39  ARG B N   
274  C CA  . ARG A 41  ? 1.1102 0.5657 0.5385 0.1383  0.3383  0.0073  39  ARG B CA  
275  C C   . ARG A 41  ? 1.1204 0.5951 0.5528 0.1332  0.3346  0.0082  39  ARG B C   
276  O O   . ARG A 41  ? 1.1418 0.6253 0.5767 0.1363  0.3325  0.0112  39  ARG B O   
277  C CB  . ARG A 41  ? 1.0804 0.5444 0.5053 0.1480  0.3415  0.0065  39  ARG B CB  
278  C CG  . ARG A 41  ? 1.1098 0.5906 0.5355 0.1589  0.3410  0.0094  39  ARG B CG  
279  C CD  . ARG A 41  ? 1.1156 0.6161 0.5405 0.1652  0.3429  0.0063  39  ARG B CD  
280  N NE  . ARG A 41  ? 1.1290 0.6451 0.5539 0.1775  0.3429  0.0076  39  ARG B NE  
281  C CZ  . ARG A 41  ? 1.2478 0.7669 0.6680 0.1898  0.3453  0.0052  39  ARG B CZ  
282  N NH1 . ARG A 41  ? 1.2306 0.7361 0.6450 0.1918  0.3483  0.0015  39  ARG B NH1 
283  N NH2 . ARG A 41  ? 1.2916 0.8281 0.7126 0.2008  0.3446  0.0057  39  ARG B NH2 
284  N N   . GLN A 42  ? 1.0982 0.5786 0.5297 0.1249  0.3340  0.0059  40  GLN B N   
285  C CA  . GLN A 42  ? 1.0936 0.5876 0.5248 0.1177  0.3311  0.0074  40  GLN B CA  
286  C C   . GLN A 42  ? 1.0747 0.5857 0.5031 0.1143  0.3327  0.0064  40  GLN B C   
287  O O   . GLN A 42  ? 1.0692 0.5736 0.4943 0.1079  0.3331  0.0035  40  GLN B O   
288  C CB  . GLN A 42  ? 1.0728 0.5514 0.5022 0.1081  0.3279  0.0059  40  GLN B CB  
289  C CG  . GLN A 42  ? 1.0788 0.5631 0.5060 0.1032  0.3244  0.0087  40  GLN B CG  
290  C CD  . GLN A 42  ? 1.0615 0.5287 0.4845 0.0950  0.3211  0.0059  40  GLN B CD  
291  O OE1 . GLN A 42  ? 1.0225 0.4782 0.4443 0.0912  0.3214  0.0018  40  GLN B OE1 
292  N NE2 . GLN A 42  ? 1.0607 0.5256 0.4820 0.0934  0.3177  0.0072  40  GLN B NE2 
293  N N   . ALA A 43  ? 1.0445 0.5794 0.4740 0.1179  0.3336  0.0085  41  ALA B N   
294  C CA  . ALA A 43  ? 1.0351 0.5914 0.4619 0.1128  0.3350  0.0081  41  ALA B CA  
295  C C   . ALA A 43  ? 1.0652 0.6185 0.4856 0.0988  0.3322  0.0107  41  ALA B C   
296  O O   . ALA A 43  ? 1.1412 0.6818 0.5598 0.0947  0.3290  0.0132  41  ALA B O   
297  C CB  . ALA A 43  ? 1.0342 0.6192 0.4639 0.1179  0.3362  0.0098  41  ALA B CB  
298  N N   . PRO A 44  ? 1.1042 0.6679 0.5194 0.0915  0.3332  0.0100  42  PRO B N   
299  C CA  . PRO A 44  ? 1.1218 0.6793 0.5275 0.0780  0.3301  0.0134  42  PRO B CA  
300  C C   . PRO A 44  ? 1.0996 0.6622 0.5013 0.0713  0.3271  0.0204  42  PRO B C   
301  O O   . PRO A 44  ? 1.0881 0.6756 0.4909 0.0697  0.3283  0.0240  42  PRO B O   
302  C CB  . PRO A 44  ? 1.0489 0.6256 0.4502 0.0726  0.3322  0.0126  42  PRO B CB  
303  C CG  . PRO A 44  ? 1.0836 0.6604 0.4919 0.0839  0.3359  0.0055  42  PRO B CG  
304  C CD  . PRO A 44  ? 1.0953 0.6742 0.5115 0.0954  0.3369  0.0056  42  PRO B CD  
305  N N   . GLY A 45  ? 1.1202 0.6593 0.5166 0.0670  0.3232  0.0217  43  GLY B N   
306  C CA  . GLY A 45  ? 1.1787 0.7178 0.5691 0.0600  0.3198  0.0282  43  GLY B CA  
307  C C   . GLY A 45  ? 1.1433 0.6944 0.5427 0.0683  0.3209  0.0292  43  GLY B C   
308  O O   . GLY A 45  ? 1.0854 0.6491 0.4814 0.0623  0.3197  0.0351  43  GLY B O   
309  N N   . LYS A 46  ? 1.1359 0.6833 0.5458 0.0813  0.3229  0.0241  44  LYS B N   
310  C CA  . LYS A 46  ? 1.1522 0.7111 0.5702 0.0907  0.3237  0.0247  44  LYS B CA  
311  C C   . LYS A 46  ? 1.1710 0.7086 0.5930 0.0975  0.3219  0.0219  44  LYS B C   
312  O O   . LYS A 46  ? 1.1480 0.6645 0.5684 0.0958  0.3209  0.0185  44  LYS B O   
313  C CB  . LYS A 46  ? 1.1064 0.6859 0.5317 0.1007  0.3277  0.0222  44  LYS B CB  
314  C CG  . LYS A 46  ? 1.1012 0.7025 0.5231 0.0941  0.3300  0.0228  44  LYS B CG  
315  C CD  . LYS A 46  ? 1.1383 0.7588 0.5550 0.0826  0.3290  0.0290  44  LYS B CD  
316  C CE  . LYS A 46  ? 1.1996 0.8551 0.6223 0.0879  0.3324  0.0282  44  LYS B CE  
317  N NZ  . LYS A 46  ? 1.1761 0.8456 0.6023 0.0954  0.3361  0.0221  44  LYS B NZ  
318  N N   . GLY A 47  ? 1.2601 0.8055 0.6876 0.1049  0.3216  0.0230  45  GLY B N   
319  C CA  . GLY A 47  ? 1.2603 0.7899 0.6920 0.1113  0.3198  0.0208  45  GLY B CA  
320  C C   . GLY A 47  ? 1.2346 0.7533 0.6707 0.1187  0.3219  0.0177  45  GLY B C   
321  O O   . GLY A 47  ? 1.2351 0.7559 0.6707 0.1196  0.3246  0.0164  45  GLY B O   
322  N N   . LEU A 48  ? 1.1759 0.6825 0.6154 0.1234  0.3206  0.0166  46  LEU B N   
323  C CA  . LEU A 48  ? 1.1107 0.6045 0.5520 0.1291  0.3227  0.0151  46  LEU B CA  
324  C C   . LEU A 48  ? 1.0923 0.5960 0.5353 0.1413  0.3247  0.0176  46  LEU B C   
325  O O   . LEU A 48  ? 1.0787 0.5948 0.5242 0.1462  0.3232  0.0196  46  LEU B O   
326  C CB  . LEU A 48  ? 1.0575 0.5348 0.5002 0.1268  0.3207  0.0130  46  LEU B CB  
327  C CG  . LEU A 48  ? 1.0678 0.5323 0.5085 0.1164  0.3185  0.0088  46  LEU B CG  
328  C CD1 . LEU A 48  ? 1.0009 0.4551 0.4447 0.1149  0.3161  0.0056  46  LEU B CD1 
329  C CD2 . LEU A 48  ? 1.0107 0.4676 0.4489 0.1124  0.3212  0.0067  46  LEU B CD2 
330  N N   . GLU A 49  ? 1.1048 0.6022 0.5452 0.1465  0.3282  0.0171  47  GLU B N   
331  C CA  . GLU A 49  ? 1.1230 0.6249 0.5617 0.1594  0.3302  0.0191  47  GLU B CA  
332  C C   . GLU A 49  ? 1.1231 0.6004 0.5559 0.1631  0.3330  0.0195  47  GLU B C   
333  O O   . GLU A 49  ? 1.1199 0.5836 0.5497 0.1583  0.3353  0.0173  47  GLU B O   
334  C CB  . GLU A 49  ? 1.0667 0.5871 0.5048 0.1642  0.3323  0.0179  47  GLU B CB  
335  C CG  . GLU A 49  ? 1.0930 0.6263 0.5307 0.1776  0.3328  0.0194  47  GLU B CG  
336  C CD  . GLU A 49  ? 1.2157 0.7744 0.6545 0.1819  0.3343  0.0169  47  GLU B CD  
337  O OE1 . GLU A 49  ? 1.2285 0.7871 0.6652 0.1796  0.3366  0.0138  47  GLU B OE1 
338  O OE2 . GLU A 49  ? 1.2568 0.8383 0.6992 0.1870  0.3332  0.0173  47  GLU B OE2 
339  N N   . TRP A 50  ? 1.1457 0.6170 0.5756 0.1711  0.3331  0.0225  48  TRP B N   
340  C CA  . TRP A 50  ? 1.1376 0.5844 0.5582 0.1751  0.3368  0.0243  48  TRP B CA  
341  C C   . TRP A 50  ? 1.1301 0.5758 0.5427 0.1875  0.3400  0.0253  48  TRP B C   
342  O O   . TRP A 50  ? 1.1218 0.5883 0.5369 0.1958  0.3386  0.0254  48  TRP B O   
343  C CB  . TRP A 50  ? 1.1491 0.5901 0.5682 0.1779  0.3357  0.0273  48  TRP B CB  
344  C CG  . TRP A 50  ? 1.1637 0.5807 0.5692 0.1850  0.3403  0.0309  48  TRP B CG  
345  C CD1 . TRP A 50  ? 1.1621 0.5547 0.5605 0.1783  0.3442  0.0309  48  TRP B CD1 
346  C CD2 . TRP A 50  ? 1.1322 0.5463 0.5276 0.1999  0.3420  0.0351  48  TRP B CD2 
347  N NE1 . TRP A 50  ? 1.1753 0.5476 0.5581 0.1876  0.3488  0.0354  48  TRP B NE1 
348  C CE2 . TRP A 50  ? 1.1931 0.5773 0.5732 0.2016  0.3473  0.0383  48  TRP B CE2 
349  C CE3 . TRP A 50  ? 1.1377 0.5716 0.5345 0.2120  0.3397  0.0362  48  TRP B CE3 
350  C CZ2 . TRP A 50  ? 1.2329 0.6034 0.5970 0.2159  0.3502  0.0432  48  TRP B CZ2 
351  C CZ3 . TRP A 50  ? 1.2145 0.6380 0.5978 0.2265  0.3419  0.0402  48  TRP B CZ3 
352  C CH2 . TRP A 50  ? 1.2544 0.6450 0.6205 0.2289  0.3471  0.0441  48  TRP B CH2 
353  N N   . VAL A 51  ? 1.1460 0.5678 0.5483 0.1885  0.3445  0.0254  49  VAL B N   
354  C CA  . VAL A 51  ? 1.2110 0.6264 0.6027 0.2012  0.3479  0.0258  49  VAL B CA  
355  C C   . VAL A 51  ? 1.2298 0.6143 0.6046 0.2080  0.3523  0.0303  49  VAL B C   
356  O O   . VAL A 51  ? 1.2751 0.6555 0.6393 0.2227  0.3535  0.0329  49  VAL B O   
357  C CB  . VAL A 51  ? 1.2263 0.6421 0.6182 0.1978  0.3499  0.0208  49  VAL B CB  
358  C CG1 . VAL A 51  ? 1.2389 0.6856 0.6440 0.1922  0.3465  0.0169  49  VAL B CG1 
359  C CG2 . VAL A 51  ? 1.1826 0.5734 0.5705 0.1866  0.3531  0.0195  49  VAL B CG2 
360  N N   . ALA A 52  ? 1.1942 0.5562 0.5648 0.1979  0.3551  0.0311  50  ALA B N   
361  C CA  . ALA A 52  ? 1.2141 0.5439 0.5652 0.2033  0.3610  0.0355  50  ALA B CA  
362  C C   . ALA A 52  ? 1.2373 0.5521 0.5870 0.1920  0.3629  0.0368  50  ALA B C   
363  O O   . ALA A 52  ? 1.1919 0.5132 0.5535 0.1781  0.3612  0.0326  50  ALA B O   
364  C CB  . ALA A 52  ? 1.2321 0.5406 0.5710 0.2046  0.3663  0.0337  50  ALA B CB  
365  N N   . SER A 53  ? 1.2492 0.5436 0.5827 0.1988  0.3667  0.0423  51  SER B N   
366  C CA  . SER A 53  ? 1.2102 0.4872 0.5383 0.1893  0.3704  0.0433  51  SER B CA  
367  C C   . SER A 53  ? 1.2560 0.4935 0.5570 0.1939  0.3795  0.0479  51  SER B C   
368  O O   . SER A 53  ? 1.2923 0.5178 0.5768 0.2094  0.3813  0.0527  51  SER B O   
369  C CB  . SER A 53  ? 1.2591 0.5512 0.5927 0.1926  0.3663  0.0456  51  SER B CB  
370  O OG  . SER A 53  ? 1.2179 0.5405 0.5742 0.1844  0.3590  0.0408  51  SER B OG  
371  N N   . ILE A 54  ? 1.2766 0.4934 0.5717 0.1807  0.3854  0.0459  52  ILE B N   
372  C CA  . ILE A 54  ? 1.3102 0.4864 0.5773 0.1822  0.3952  0.0505  52  ILE B CA  
373  C C   . ILE A 54  ? 1.3537 0.5270 0.6209 0.1732  0.3971  0.0504  52  ILE B C   
374  O O   . ILE A 54  ? 1.3380 0.5303 0.6245 0.1591  0.3939  0.0441  52  ILE B O   
375  C CB  . ILE A 54  ? 1.3101 0.4626 0.5674 0.1736  0.4022  0.0476  52  ILE B CB  
376  C CG1 . ILE A 54  ? 1.3763 0.4820 0.5992 0.1766  0.4134  0.0534  52  ILE B CG1 
377  C CG2 . ILE A 54  ? 1.2880 0.4518 0.5630 0.1542  0.4016  0.0401  52  ILE B CG2 
378  C CD1 . ILE A 54  ? 1.3875 0.4764 0.5884 0.1962  0.4146  0.0595  52  ILE B CD1 
379  N N   . TYR A 55  ? 1.3871 0.5393 0.6331 0.1824  0.4015  0.0568  53  TYR B N   
380  C CA  . TYR A 55  ? 1.3485 0.4987 0.5930 0.1747  0.4036  0.0561  53  TYR B CA  
381  C C   . TYR A 55  ? 1.3680 0.4764 0.5877 0.1659  0.4156  0.0565  53  TYR B C   
382  O O   . TYR A 55  ? 1.4761 0.5540 0.6761 0.1688  0.4222  0.0591  53  TYR B O   
383  C CB  . TYR A 55  ? 1.3790 0.5372 0.6178 0.1897  0.4001  0.0619  53  TYR B CB  
384  C CG  . TYR A 55  ? 1.3849 0.5881 0.6520 0.1936  0.3886  0.0593  53  TYR B CG  
385  C CD1 . TYR A 55  ? 1.3154 0.5492 0.6055 0.1830  0.3825  0.0537  53  TYR B CD1 
386  C CD2 . TYR A 55  ? 1.3805 0.5953 0.6505 0.2070  0.3840  0.0615  53  TYR B CD2 
387  C CE1 . TYR A 55  ? 1.3060 0.5765 0.6188 0.1859  0.3728  0.0513  53  TYR B CE1 
388  C CE2 . TYR A 55  ? 1.3335 0.5873 0.6276 0.2091  0.3745  0.0586  53  TYR B CE2 
389  C CZ  . TYR A 55  ? 1.3364 0.6160 0.6509 0.1985  0.3692  0.0539  53  TYR B CZ  
390  O OH  . TYR A 55  ? 1.3095 0.6242 0.6451 0.2006  0.3605  0.0511  53  TYR B OH  
391  N N   . PRO A 56  ? 1.3966 0.5042 0.6170 0.1534  0.4188  0.0528  54  PRO B N   
392  C CA  . PRO A 56  ? 1.4481 0.5172 0.6461 0.1417  0.4308  0.0511  54  PRO B CA  
393  C C   . PRO A 56  ? 1.4892 0.5170 0.6512 0.1513  0.4396  0.0582  54  PRO B C   
394  O O   . PRO A 56  ? 1.4629 0.4871 0.6138 0.1699  0.4368  0.0657  54  PRO B O   
395  C CB  . PRO A 56  ? 1.4416 0.5359 0.6597 0.1229  0.4292  0.0422  54  PRO B CB  
396  C CG  . PRO A 56  ? 1.3925 0.5235 0.6283 0.1296  0.4195  0.0429  54  PRO B CG  
397  C CD  . PRO A 56  ? 1.3983 0.5431 0.6419 0.1464  0.4116  0.0480  54  PRO B CD  
398  N N   . TYR A 57  ? 1.5451 0.5408 0.6873 0.1383  0.4504  0.0552  55  TYR B N   
399  C CA  . TYR A 57  ? 1.5976 0.5498 0.7023 0.1440  0.4600  0.0597  55  TYR B CA  
400  C C   . TYR A 57  ? 1.5668 0.4779 0.6410 0.1644  0.4638  0.0679  55  TYR B C   
401  O O   . TYR A 57  ? 1.6027 0.4776 0.6513 0.1609  0.4724  0.0664  55  TYR B O   
402  C CB  . TYR A 57  ? 1.5758 0.5513 0.6840 0.1473  0.4555  0.0621  55  TYR B CB  
403  C CG  . TYR A 57  ? 1.5465 0.5636 0.6840 0.1277  0.4513  0.0541  55  TYR B CG  
404  C CD1 . TYR A 57  ? 1.5350 0.5476 0.6765 0.1065  0.4574  0.0457  55  TYR B CD1 
405  C CD2 . TYR A 57  ? 1.5437 0.6049 0.7044 0.1309  0.4414  0.0543  55  TYR B CD2 
406  C CE1 . TYR A 57  ? 1.5419 0.5927 0.7088 0.0901  0.4535  0.0378  55  TYR B CE1 
407  C CE2 . TYR A 57  ? 1.5220 0.6204 0.7078 0.1144  0.4375  0.0461  55  TYR B CE2 
408  C CZ  . TYR A 57  ? 1.5593 0.6527 0.7480 0.0945  0.4435  0.0379  55  TYR B CZ  
409  O OH  . TYR A 57  ? 1.4730 0.6040 0.6858 0.0794  0.4394  0.0289  55  TYR B OH  
410  N N   . TYR A 58  ? 1.5480 0.4779 0.6287 0.1838  0.4551  0.0748  56  TYR B N   
411  C CA  . TYR A 58  ? 1.5827 0.4879 0.6359 0.2046  0.4557  0.0827  56  TYR B CA  
412  C C   . TYR A 58  ? 1.6079 0.5317 0.6729 0.2131  0.4494  0.0862  56  TYR B C   
413  O O   . TYR A 58  ? 1.5886 0.5104 0.6396 0.2331  0.4458  0.0929  56  TYR B O   
414  C CB  . TYR A 58  ? 1.5943 0.4996 0.6362 0.2232  0.4525  0.0888  56  TYR B CB  
415  C CG  . TYR A 58  ? 1.7227 0.6156 0.7512 0.2143  0.4586  0.0857  56  TYR B CG  
416  C CD1 . TYR A 58  ? 1.7285 0.5879 0.7362 0.1982  0.4697  0.0799  56  TYR B CD1 
417  C CD2 . TYR A 58  ? 1.6899 0.6147 0.7291 0.2185  0.4518  0.0887  56  TYR B CD2 
418  C CE1 . TYR A 58  ? 1.7506 0.6110 0.7492 0.1852  0.4729  0.0797  56  TYR B CE1 
419  C CE2 . TYR A 58  ? 1.6684 0.5913 0.6974 0.2070  0.4554  0.0886  56  TYR B CE2 
420  C CZ  . TYR A 58  ? 1.7093 0.6014 0.7187 0.1896  0.4656  0.0849  56  TYR B CZ  
421  O OH  . TYR A 58  ? 1.7392 0.6327 0.7390 0.1754  0.4684  0.0866  56  TYR B OH  
422  N N   . GLY A 59  ? 1.5833 0.5256 0.6720 0.1987  0.4482  0.0808  57  GLY B N   
423  C CA  . GLY A 59  ? 1.5065 0.4794 0.6144 0.2052  0.4401  0.0792  57  GLY B CA  
424  C C   . GLY A 59  ? 1.4697 0.4857 0.6024 0.2168  0.4283  0.0793  57  GLY B C   
425  O O   . GLY A 59  ? 1.4768 0.5234 0.6356 0.2072  0.4231  0.0746  57  GLY B O   
426  N N   . SER A 60  ? 1.4790 0.4992 0.6030 0.2371  0.4238  0.0838  58  SER B N   
427  C CA  . SER A 60  ? 1.4850 0.5411 0.6263 0.2500  0.4139  0.0848  58  SER B CA  
428  C C   . SER A 60  ? 1.4460 0.5528 0.6286 0.2416  0.4041  0.0769  58  SER B C   
429  O O   . SER A 60  ? 1.4341 0.5551 0.6369 0.2237  0.4034  0.0713  58  SER B O   
430  C CB  . SER A 60  ? 1.5751 0.6263 0.7100 0.2505  0.4152  0.0883  58  SER B CB  
431  O OG  . SER A 60  ? 1.5955 0.6651 0.7304 0.2692  0.4084  0.0923  58  SER B OG  
432  N N   . THR A 61  ? 1.4284 0.5623 0.6225 0.2547  0.3965  0.0758  59  THR B N   
433  C CA  . THR A 61  ? 1.3470 0.5196 0.5729 0.2474  0.3892  0.0682  59  THR B CA  
434  C C   . THR A 61  ? 1.3471 0.5590 0.5918 0.2571  0.3801  0.0674  59  THR B C   
435  O O   . THR A 61  ? 1.4248 0.6348 0.6574 0.2724  0.3788  0.0722  59  THR B O   
436  C CB  . THR A 61  ? 1.3806 0.5468 0.6021 0.2515  0.3903  0.0649  59  THR B CB  
437  O OG1 . THR A 61  ? 1.3768 0.5407 0.5838 0.2730  0.3882  0.0675  59  THR B OG1 
438  C CG2 . THR A 61  ? 1.3868 0.5119 0.5866 0.2427  0.4000  0.0657  59  THR B CG2 
439  N N   . SER A 62  ? 1.3494 0.5965 0.6226 0.2480  0.3739  0.0610  60  SER B N   
440  C CA  . SER A 62  ? 1.3326 0.6184 0.6243 0.2551  0.3658  0.0589  60  SER B CA  
441  C C   . SER A 62  ? 1.3098 0.6195 0.6202 0.2494  0.3624  0.0521  60  SER B C   
442  O O   . SER A 62  ? 1.2782 0.5832 0.5954 0.2351  0.3641  0.0485  60  SER B O   
443  C CB  . SER A 62  ? 1.3141 0.6202 0.6209 0.2477  0.3616  0.0588  60  SER B CB  
444  O OG  . SER A 62  ? 1.3822 0.6647 0.6715 0.2503  0.3657  0.0643  60  SER B OG  
445  N N   . TYR A 63  ? 1.2627 0.5984 0.5805 0.2606  0.3578  0.0498  61  TYR B N   
446  C CA  . TYR A 63  ? 1.3413 0.6992 0.6733 0.2573  0.3556  0.0432  61  TYR B CA  
447  C C   . TYR A 63  ? 1.3975 0.7959 0.7477 0.2600  0.3494  0.0404  61  TYR B C   
448  O O   . TYR A 63  ? 1.4599 0.8681 0.8065 0.2732  0.3471  0.0425  61  TYR B O   
449  C CB  . TYR A 63  ? 1.3639 0.7086 0.6816 0.2700  0.3584  0.0414  61  TYR B CB  
450  C CG  . TYR A 63  ? 1.3341 0.6371 0.6317 0.2670  0.3652  0.0436  61  TYR B CG  
451  C CD1 . TYR A 63  ? 1.3439 0.6387 0.6477 0.2500  0.3679  0.0406  61  TYR B CD1 
452  C CD2 . TYR A 63  ? 1.3355 0.6069 0.6067 0.2811  0.3691  0.0484  61  TYR B CD2 
453  C CE1 . TYR A 63  ? 1.3277 0.5859 0.6136 0.2461  0.3747  0.0419  61  TYR B CE1 
454  C CE2 . TYR A 63  ? 1.4089 0.6401 0.6595 0.2772  0.3763  0.0504  61  TYR B CE2 
455  C CZ  . TYR A 63  ? 1.3867 0.6123 0.6455 0.2590  0.3793  0.0469  61  TYR B CZ  
456  O OH  . TYR A 63  ? 1.3503 0.5374 0.5890 0.2539  0.3869  0.0482  61  TYR B OH  
457  N N   . ALA A 64  ? 1.3508 0.7717 0.7190 0.2472  0.3468  0.0357  62  ALA B N   
458  C CA  . ALA A 64  ? 1.4279 0.8865 0.8113 0.2484  0.3423  0.0324  62  ALA B CA  
459  C C   . ALA A 64  ? 1.6329 1.1052 1.0118 0.2647  0.3421  0.0297  62  ALA B C   
460  O O   . ALA A 64  ? 1.6590 1.1174 1.0282 0.2708  0.3450  0.0276  62  ALA B O   
461  C CB  . ALA A 64  ? 1.4118 0.8866 0.8095 0.2330  0.3411  0.0279  62  ALA B CB  
462  N N   . ASP A 65  ? 1.8255 1.3261 1.2116 0.2723  0.3386  0.0288  63  ASP B N   
463  C CA  . ASP A 65  ? 1.8388 1.3562 1.2217 0.2889  0.3378  0.0250  63  ASP B CA  
464  C C   . ASP A 65  ? 1.7922 1.3245 1.1804 0.2865  0.3392  0.0178  63  ASP B C   
465  O O   . ASP A 65  ? 1.7872 1.3181 1.1674 0.3002  0.3400  0.0141  63  ASP B O   
466  C CB  . ASP A 65  ? 1.8345 1.3857 1.2277 0.2941  0.3337  0.0238  63  ASP B CB  
467  C CG  . ASP A 65  ? 1.8683 1.4068 1.2551 0.2993  0.3320  0.0301  63  ASP B CG  
468  O OD1 . ASP A 65  ? 1.8803 1.3849 1.2556 0.2963  0.3344  0.0357  63  ASP B OD1 
469  O OD2 . ASP A 65  ? 1.8782 1.4420 1.2716 0.3056  0.3286  0.0292  63  ASP B OD2 
470  N N   . SER A 66  ? 1.6566 1.2027 1.0572 0.2698  0.3394  0.0154  64  SER B N   
471  C CA  . SER A 66  ? 1.6111 1.1758 1.0170 0.2668  0.3408  0.0084  64  SER B CA  
472  C C   . SER A 66  ? 1.6216 1.1578 1.0162 0.2694  0.3441  0.0068  64  SER B C   
473  O O   . SER A 66  ? 1.5640 1.1115 0.9577 0.2765  0.3452  0.0001  64  SER B O   
474  C CB  . SER A 66  ? 1.5608 1.1438 0.9794 0.2480  0.3403  0.0075  64  SER B CB  
475  O OG  . SER A 66  ? 1.5308 1.0868 0.9468 0.2360  0.3417  0.0099  64  SER B OG  
476  N N   . VAL A 67  ? 1.5937 1.0942 0.9798 0.2637  0.3460  0.0122  65  VAL B N   
477  C CA  . VAL A 67  ? 1.5997 1.0720 0.9752 0.2633  0.3496  0.0108  65  VAL B CA  
478  C C   . VAL A 67  ? 1.6498 1.0932 1.0059 0.2799  0.3514  0.0137  65  VAL B C   
479  O O   . VAL A 67  ? 1.6313 1.0429 0.9744 0.2796  0.3551  0.0144  65  VAL B O   
480  C CB  . VAL A 67  ? 1.5319 0.9829 0.9088 0.2459  0.3512  0.0139  65  VAL B CB  
481  C CG1 . VAL A 67  ? 1.4739 0.9510 0.8673 0.2314  0.3484  0.0125  65  VAL B CG1 
482  C CG2 . VAL A 67  ? 1.5079 0.9322 0.8756 0.2460  0.3520  0.0214  65  VAL B CG2 
483  N N   . LYS A 68  ? 1.7908 1.2450 1.1437 0.2947  0.3489  0.0150  66  LYS B N   
484  C CA  . LYS A 68  ? 1.8243 1.2494 1.1560 0.3116  0.3499  0.0190  66  LYS B CA  
485  C C   . LYS A 68  ? 1.8478 1.2593 1.1680 0.3223  0.3516  0.0133  66  LYS B C   
486  O O   . LYS A 68  ? 1.8047 1.2436 1.1357 0.3244  0.3502  0.0043  66  LYS B O   
487  C CB  . LYS A 68  ? 1.8473 1.2928 1.1795 0.3266  0.3457  0.0200  66  LYS B CB  
488  C CG  . LYS A 68  ? 1.8814 1.3630 1.2223 0.3391  0.3425  0.0106  66  LYS B CG  
489  C CD  . LYS A 68  ? 1.9059 1.3802 1.2312 0.3632  0.3399  0.0105  66  LYS B CD  
490  C CE  . LYS A 68  ? 1.8899 1.3159 1.1892 0.3726  0.3428  0.0143  66  LYS B CE  
491  N NZ  . LYS A 68  ? 1.8996 1.3231 1.1848 0.3976  0.3390  0.0110  66  LYS B NZ  
492  N N   . GLY A 69  ? 1.7569 1.1255 1.0543 0.3284  0.3550  0.0181  67  GLY B N   
493  C CA  . GLY A 69  ? 1.7276 1.0785 1.0114 0.3403  0.3561  0.0128  67  GLY B CA  
494  C C   . GLY A 69  ? 1.6249 0.9786 0.9173 0.3285  0.3584  0.0056  67  GLY B C   
495  O O   . GLY A 69  ? 1.6139 0.9361 0.8915 0.3302  0.3615  0.0044  67  GLY B O   
496  N N   . ARG A 70  ? 1.6235 1.0145 0.9389 0.3164  0.3568  0.0005  68  ARG B N   
497  C CA  . ARG A 70  ? 1.5263 0.9215 0.8502 0.3037  0.3589  -0.0058 68  ARG B CA  
498  C C   . ARG A 70  ? 1.5344 0.8981 0.8531 0.2870  0.3631  -0.0001 68  ARG B C   
499  O O   . ARG A 70  ? 1.4704 0.8197 0.7861 0.2812  0.3659  -0.0043 68  ARG B O   
500  C CB  . ARG A 70  ? 1.4966 0.9378 0.8430 0.2945  0.3565  -0.0111 68  ARG B CB  
501  C CG  . ARG A 70  ? 1.5243 1.0010 0.8779 0.3074  0.3527  -0.0150 68  ARG B CG  
502  C CD  . ARG A 70  ? 1.4393 0.9601 0.8107 0.3002  0.3520  -0.0238 68  ARG B CD  
503  N NE  . ARG A 70  ? 1.4076 0.9638 0.7906 0.2999  0.3493  -0.0231 68  ARG B NE  
504  C CZ  . ARG A 70  ? 1.4435 1.0129 0.8371 0.2841  0.3489  -0.0185 68  ARG B CZ  
505  N NH1 . ARG A 70  ? 1.4162 0.9698 0.8115 0.2676  0.3504  -0.0150 68  ARG B NH1 
506  N NH2 . ARG A 70  ? 1.4737 1.0723 0.8760 0.2851  0.3465  -0.0178 68  ARG B NH2 
507  N N   . PHE A 71  ? 1.5357 0.8896 0.8538 0.2792  0.3635  0.0085  69  PHE B N   
508  C CA  . PHE A 71  ? 1.4959 0.8275 0.8131 0.2617  0.3670  0.0125  69  PHE B CA  
509  C C   . PHE A 71  ? 1.4893 0.7786 0.7836 0.2651  0.3715  0.0202  69  PHE B C   
510  O O   . PHE A 71  ? 1.4857 0.7685 0.7691 0.2775  0.3707  0.0255  69  PHE B O   
511  C CB  . PHE A 71  ? 1.4907 0.8453 0.8259 0.2482  0.3638  0.0149  69  PHE B CB  
512  C CG  . PHE A 71  ? 1.4944 0.8835 0.8488 0.2395  0.3609  0.0082  69  PHE B CG  
513  C CD1 . PHE A 71  ? 1.5297 0.9434 0.8884 0.2486  0.3596  0.0011  69  PHE B CD1 
514  C CD2 . PHE A 71  ? 1.4364 0.8334 0.8031 0.2226  0.3595  0.0087  69  PHE B CD2 
515  C CE1 . PHE A 71  ? 1.4890 0.9341 0.8627 0.2398  0.3578  -0.0046 69  PHE B CE1 
516  C CE2 . PHE A 71  ? 1.4338 0.8594 0.8143 0.2148  0.3572  0.0035  69  PHE B CE2 
517  C CZ  . PHE A 71  ? 1.4489 0.8987 0.8324 0.2229  0.3568  -0.0028 69  PHE B CZ  
518  N N   . THR A 72  ? 1.3930 0.6538 0.6789 0.2537  0.3768  0.0206  70  THR B N   
519  C CA  . THR A 72  ? 1.3870 0.6070 0.6502 0.2527  0.3827  0.0279  70  THR B CA  
520  C C   . THR A 72  ? 1.3720 0.5833 0.6415 0.2316  0.3862  0.0289  70  THR B C   
521  O O   . THR A 72  ? 1.3619 0.5674 0.6346 0.2212  0.3886  0.0237  70  THR B O   
522  C CB  . THR A 72  ? 1.4432 0.6299 0.6827 0.2629  0.3870  0.0266  70  THR B CB  
523  O OG1 . THR A 72  ? 1.4522 0.6326 0.6763 0.2838  0.3849  0.0298  70  THR B OG1 
524  C CG2 . THR A 72  ? 1.4154 0.5596 0.6344 0.2520  0.3955  0.0312  70  THR B CG2 
525  N N   . ILE A 73  ? 1.3546 0.5674 0.6272 0.2258  0.3857  0.0344  71  ILE B N   
526  C CA  . ILE A 73  ? 1.3395 0.5399 0.6144 0.2077  0.3894  0.0351  71  ILE B CA  
527  C C   . ILE A 73  ? 1.3424 0.4988 0.5890 0.2077  0.3986  0.0400  71  ILE B C   
528  O O   . ILE A 73  ? 1.3873 0.5241 0.6125 0.2220  0.4008  0.0457  71  ILE B O   
529  C CB  . ILE A 73  ? 1.3175 0.5384 0.6077 0.2016  0.3849  0.0373  71  ILE B CB  
530  C CG1 . ILE A 73  ? 1.2716 0.4882 0.5699 0.1823  0.3869  0.0347  71  ILE B CG1 
531  C CG2 . ILE A 73  ? 1.3439 0.5501 0.6183 0.2115  0.3867  0.0449  71  ILE B CG2 
532  C CD1 . ILE A 73  ? 1.2801 0.5190 0.5951 0.1761  0.3814  0.0348  71  ILE B CD1 
533  N N   . SER A 74  ? 1.3462 0.4866 0.5912 0.1914  0.4040  0.0374  72  SER B N   
534  C CA  . SER A 74  ? 1.3858 0.4830 0.6027 0.1878  0.4143  0.0410  72  SER B CA  
535  C C   . SER A 74  ? 1.3766 0.4700 0.6017 0.1665  0.4185  0.0361  72  SER B C   
536  O O   . SER A 74  ? 1.3610 0.4842 0.6121 0.1569  0.4126  0.0300  72  SER B O   
537  C CB  . SER A 74  ? 1.4217 0.4954 0.6177 0.1994  0.4177  0.0403  72  SER B CB  
538  O OG  . SER A 74  ? 1.4768 0.5405 0.6549 0.2187  0.4165  0.0466  72  SER B OG  
539  N N   . ALA A 75  ? 1.4106 0.4666 0.6117 0.1592  0.4289  0.0384  73  ALA B N   
540  C CA  . ALA A 75  ? 1.4042 0.4564 0.6121 0.1385  0.4337  0.0332  73  ALA B CA  
541  C C   . ALA A 75  ? 1.4649 0.4730 0.6422 0.1323  0.4464  0.0343  73  ALA B C   
542  O O   . ALA A 75  ? 1.4890 0.4644 0.6358 0.1418  0.4528  0.0416  73  ALA B O   
543  C CB  . ALA A 75  ? 1.3843 0.4481 0.6031 0.1302  0.4320  0.0341  73  ALA B CB  
544  N N   . ASP A 76  ? 1.4659 0.4733 0.6505 0.1162  0.4500  0.0265  74  ASP B N   
545  C CA  . ASP A 76  ? 1.5273 0.4954 0.6851 0.1068  0.4626  0.0256  74  ASP B CA  
546  C C   . ASP A 76  ? 1.5642 0.5316 0.7285 0.0857  0.4681  0.0213  74  ASP B C   
547  O O   . ASP A 76  ? 1.5381 0.5313 0.7279 0.0739  0.4640  0.0123  74  ASP B O   
548  C CB  . ASP A 76  ? 1.5853 0.5529 0.7458 0.1068  0.4622  0.0182  74  ASP B CB  
549  C CG  . ASP A 76  ? 1.6992 0.6232 0.8279 0.1006  0.4745  0.0176  74  ASP B CG  
550  O OD1 . ASP A 76  ? 1.7157 0.6120 0.8176 0.1145  0.4770  0.0223  74  ASP B OD1 
551  O OD2 . ASP A 76  ? 1.7150 0.6324 0.8449 0.0813  0.4817  0.0122  74  ASP B OD2 
552  N N   . THR A 77  ? 1.6328 0.5704 0.7731 0.0817  0.4773  0.0270  75  THR B N   
553  C CA  . THR A 77  ? 1.6308 0.5714 0.7799 0.0634  0.4809  0.0220  75  THR B CA  
554  C C   . THR A 77  ? 1.6657 0.5945 0.8119 0.0437  0.4898  0.0133  75  THR B C   
555  O O   . THR A 77  ? 1.6146 0.5658 0.7835 0.0284  0.4877  0.0041  75  THR B O   
556  C CB  . THR A 77  ? 1.6610 0.5699 0.7838 0.0652  0.4882  0.0291  75  THR B CB  
557  O OG1 . THR A 77  ? 1.6052 0.5332 0.7373 0.0827  0.4783  0.0353  75  THR B OG1 
558  C CG2 . THR A 77  ? 1.6937 0.6042 0.8246 0.0453  0.4924  0.0205  75  THR B CG2 
559  N N   . SER A 78  ? 1.8050 0.6999 0.9224 0.0443  0.4996  0.0151  76  SER B N   
560  C CA  . SER A 78  ? 1.8079 0.6955 0.9248 0.0276  0.5068  0.0056  76  SER B CA  
561  C C   . SER A 78  ? 1.7476 0.6804 0.9055 0.0233  0.4951  -0.0047 76  SER B C   
562  O O   . SER A 78  ? 1.7354 0.6819 0.9091 0.0058  0.4966  -0.0140 76  SER B O   
563  C CB  . SER A 78  ? 1.8411 0.6968 0.9288 0.0356  0.5130  0.0072  76  SER B CB  
564  O OG  . SER A 78  ? 1.8760 0.7562 0.9854 0.0477  0.5015  0.0031  76  SER B OG  
565  N N   . LYS A 79  ? 1.6677 0.6254 0.8425 0.0393  0.4833  -0.0036 77  LYS B N   
566  C CA  . LYS A 79  ? 1.6012 0.5985 0.8096 0.0368  0.4726  -0.0126 77  LYS B CA  
567  C C   . LYS A 79  ? 1.5232 0.5601 0.7605 0.0376  0.4610  -0.0134 77  LYS B C   
568  O O   . LYS A 79  ? 1.4563 0.5266 0.7192 0.0383  0.4510  -0.0194 77  LYS B O   
569  C CB  . LYS A 79  ? 1.5488 0.5510 0.7589 0.0521  0.4666  -0.0128 77  LYS B CB  
570  N N   . ASN A 80  ? 1.4967 0.5302 0.7295 0.0372  0.4621  -0.0083 78  ASN B N   
571  C CA  . ASN A 80  ? 1.3785 0.4486 0.6375 0.0367  0.4514  -0.0104 78  ASN B CA  
572  C C   . ASN A 80  ? 1.3574 0.4611 0.6384 0.0485  0.4383  -0.0104 78  ASN B C   
573  O O   . ASN A 80  ? 1.2995 0.4330 0.6040 0.0429  0.4305  -0.0181 78  ASN B O   
574  C CB  . ASN A 80  ? 1.3494 0.4363 0.6248 0.0183  0.4517  -0.0213 78  ASN B CB  
575  C CG  . ASN A 80  ? 1.3585 0.4710 0.6499 0.0166  0.4448  -0.0228 78  ASN B CG  
576  O OD1 . ASN A 80  ? 1.3507 0.4718 0.6443 0.0293  0.4386  -0.0158 78  ASN B OD1 
577  N ND2 . ASN A 80  ? 1.3235 0.4500 0.6265 0.0011  0.4457  -0.0327 78  ASN B ND2 
578  N N   . THR A 81  ? 1.3411 0.4385 0.6125 0.0652  0.4361  -0.0021 79  THR B N   
579  C CA  . THR A 81  ? 1.3136 0.4370 0.6009 0.0759  0.4262  -0.0028 79  THR B CA  
580  C C   . THR A 81  ? 1.3322 0.4510 0.6091 0.0938  0.4240  0.0064  79  THR B C   
581  O O   . THR A 81  ? 1.3949 0.4827 0.6468 0.0996  0.4316  0.0131  79  THR B O   
582  C CB  . THR A 81  ? 1.3847 0.5020 0.6696 0.0752  0.4284  -0.0082 79  THR B CB  
583  O OG1 . THR A 81  ? 1.3714 0.4906 0.6638 0.0583  0.4315  -0.0172 79  THR B OG1 
584  C CG2 . THR A 81  ? 1.3617 0.5081 0.6640 0.0848  0.4183  -0.0105 79  THR B CG2 
585  N N   . ALA A 82  ? 1.2921 0.4413 0.5869 0.1023  0.4138  0.0064  80  ALA B N   
586  C CA  . ALA A 82  ? 1.2967 0.4473 0.5849 0.1198  0.4108  0.0134  80  ALA B CA  
587  C C   . ALA A 82  ? 1.2872 0.4555 0.5844 0.1281  0.4054  0.0098  80  ALA B C   
588  O O   . ALA A 82  ? 1.2757 0.4554 0.5845 0.1202  0.4037  0.0026  80  ALA B O   
589  C CB  . ALA A 82  ? 1.2721 0.4441 0.5724 0.1229  0.4040  0.0168  80  ALA B CB  
590  N N   . TYR A 83  ? 1.2931 0.4647 0.5847 0.1444  0.4027  0.0143  81  TYR B N   
591  C CA  . TYR A 83  ? 1.2913 0.4767 0.5876 0.1540  0.3991  0.0103  81  TYR B CA  
592  C C   . TYR A 83  ? 1.3203 0.5267 0.6221 0.1683  0.3929  0.0141  81  TYR B C   
593  O O   . TYR A 83  ? 1.3274 0.5192 0.6139 0.1798  0.3948  0.0204  81  TYR B O   
594  C CB  . TYR A 83  ? 1.3297 0.4853 0.6045 0.1611  0.4056  0.0094  81  TYR B CB  
595  C CG  . TYR A 83  ? 1.3456 0.4783 0.6130 0.1466  0.4128  0.0056  81  TYR B CG  
596  C CD1 . TYR A 83  ? 1.3309 0.4780 0.6131 0.1369  0.4110  -0.0031 81  TYR B CD1 
597  C CD2 . TYR A 83  ? 1.3753 0.4732 0.6207 0.1417  0.4218  0.0104  81  TYR B CD2 
598  C CE1 . TYR A 83  ? 1.3454 0.4750 0.6229 0.1233  0.4173  -0.0076 81  TYR B CE1 
599  C CE2 . TYR A 83  ? 1.4085 0.4876 0.6479 0.1267  0.4290  0.0060  81  TYR B CE2 
600  C CZ  . TYR A 83  ? 1.3849 0.4812 0.6416 0.1177  0.4264  -0.0034 81  TYR B CZ  
601  O OH  . TYR A 83  ? 1.4483 0.5293 0.7011 0.1029  0.4331  -0.0091 81  TYR B OH  
602  N N   . LEU A 84  ? 1.2821 0.5220 0.6039 0.1675  0.3858  0.0101  82  LEU B N   
603  C CA  . LEU A 84  ? 1.2703 0.5322 0.5968 0.1815  0.3809  0.0112  82  LEU B CA  
604  C C   . LEU A 84  ? 1.3336 0.5987 0.6571 0.1900  0.3813  0.0053  82  LEU B C   
605  O O   . LEU A 84  ? 1.3194 0.5924 0.6511 0.1821  0.3810  -0.0014 82  LEU B O   
606  C CB  . LEU A 84  ? 1.2662 0.5620 0.6134 0.1762  0.3739  0.0101  82  LEU B CB  
607  C CG  . LEU A 84  ? 1.3229 0.6427 0.6741 0.1901  0.3698  0.0106  82  LEU B CG  
608  C CD1 . LEU A 84  ? 1.3029 0.6123 0.6432 0.2014  0.3704  0.0176  82  LEU B CD1 
609  C CD2 . LEU A 84  ? 1.2270 0.5811 0.5968 0.1844  0.3639  0.0083  82  LEU B CD2 
610  N N   . GLN A 85  ? 1.3560 0.6140 0.6669 0.2066  0.3819  0.0070  83  GLN B N   
611  C CA  . GLN A 85  ? 1.3580 0.6187 0.6650 0.2176  0.3818  0.0004  83  GLN B CA  
612  C C   . GLN A 85  ? 1.3823 0.6773 0.6998 0.2296  0.3762  -0.0015 83  GLN B C   
613  O O   . GLN A 85  ? 1.4089 0.7049 0.7212 0.2400  0.3747  0.0039  83  GLN B O   
614  C CB  . GLN A 85  ? 1.3798 0.6025 0.6618 0.2281  0.3868  0.0026  83  GLN B CB  
615  C CG  . GLN A 85  ? 1.4110 0.6370 0.6876 0.2448  0.3850  -0.0043 83  GLN B CG  
616  C CD  . GLN A 85  ? 1.4148 0.6484 0.6999 0.2388  0.3852  -0.0146 83  GLN B CD  
617  O OE1 . GLN A 85  ? 1.4200 0.6272 0.6961 0.2309  0.3898  -0.0165 83  GLN B OE1 
618  N NE2 . GLN A 85  ? 1.4055 0.6768 0.7078 0.2417  0.3806  -0.0219 83  GLN B NE2 
619  N N   . MET A 86  ? 1.3772 0.7014 0.7090 0.2276  0.3734  -0.0093 84  MET B N   
620  C CA  . MET A 86  ? 1.3964 0.7564 0.7383 0.2372  0.3690  -0.0123 84  MET B CA  
621  C C   . MET A 86  ? 1.3805 0.7492 0.7200 0.2493  0.3690  -0.0218 84  MET B C   
622  O O   . MET A 86  ? 1.3598 0.7286 0.7019 0.2434  0.3704  -0.0287 84  MET B O   
623  C CB  . MET A 86  ? 1.3947 0.7869 0.7552 0.2243  0.3659  -0.0134 84  MET B CB  
624  C CG  . MET A 86  ? 1.3743 0.7558 0.7383 0.2108  0.3655  -0.0066 84  MET B CG  
625  S SD  . MET A 86  ? 1.2837 0.6929 0.6654 0.1938  0.3622  -0.0096 84  MET B SD  
626  C CE  . MET A 86  ? 1.1849 0.5632 0.5630 0.1795  0.3649  -0.0088 84  MET B CE  
627  N N   . ASN A 87  ? 1.3989 0.7754 0.7334 0.2667  0.3671  -0.0228 85  ASN B N   
628  C CA  . ASN A 87  ? 1.3611 0.7522 0.6947 0.2817  0.3656  -0.0327 85  ASN B CA  
629  C C   . ASN A 87  ? 1.3741 0.8092 0.7212 0.2872  0.3620  -0.0355 85  ASN B C   
630  O O   . ASN A 87  ? 1.4387 0.8850 0.7921 0.2817  0.3605  -0.0286 85  ASN B O   
631  C CB  . ASN A 87  ? 1.3314 0.6887 0.6444 0.2989  0.3662  -0.0316 85  ASN B CB  
632  C CG  . ASN A 87  ? 1.3871 0.6974 0.6838 0.2911  0.3710  -0.0258 85  ASN B CG  
633  O OD1 . ASN A 87  ? 1.3728 0.6777 0.6745 0.2758  0.3736  -0.0278 85  ASN B OD1 
634  N ND2 . ASN A 87  ? 1.4485 0.7254 0.7248 0.3010  0.3722  -0.0188 85  ASN B ND2 
635  N N   . SER A 88  ? 1.3725 0.8346 0.7248 0.2970  0.3606  -0.0466 86  SER B N   
636  C CA  . SER A 88  ? 1.3878 0.8943 0.7523 0.3024  0.3578  -0.0506 86  SER B CA  
637  C C   . SER A 88  ? 1.3909 0.9243 0.7700 0.2839  0.3579  -0.0468 86  SER B C   
638  O O   . SER A 88  ? 1.3675 0.9294 0.7548 0.2842  0.3560  -0.0452 86  SER B O   
639  C CB  . SER A 88  ? 1.3829 0.8835 0.7396 0.3187  0.3552  -0.0461 86  SER B CB  
640  O OG  . SER A 88  ? 1.4392 0.9838 0.8074 0.3257  0.3526  -0.0520 86  SER B OG  
641  N N   . LEU A 89  ? 1.3701 0.8936 0.7517 0.2677  0.3598  -0.0456 87  LEU B N   
642  C CA  . LEU A 89  ? 1.3906 0.9314 0.7830 0.2498  0.3593  -0.0412 87  LEU B CA  
643  C C   . LEU A 89  ? 1.3754 0.9644 0.7792 0.2471  0.3586  -0.0474 87  LEU B C   
644  O O   . LEU A 89  ? 1.3752 0.9847 0.7809 0.2518  0.3597  -0.0575 87  LEU B O   
645  C CB  . LEU A 89  ? 1.4049 0.9274 0.7967 0.2356  0.3611  -0.0413 87  LEU B CB  
646  C CG  . LEU A 89  ? 1.4060 0.8900 0.7918 0.2273  0.3619  -0.0329 87  LEU B CG  
647  C CD1 . LEU A 89  ? 1.4028 0.8702 0.7869 0.2176  0.3641  -0.0367 87  LEU B CD1 
648  C CD2 . LEU A 89  ? 1.3721 0.8637 0.7654 0.2159  0.3596  -0.0252 87  LEU B CD2 
649  N N   . ARG A 90  ? 1.3712 0.9788 0.7823 0.2385  0.3571  -0.0416 88  ARG B N   
650  C CA  . ARG A 90  ? 1.3038 0.9572 0.7242 0.2339  0.3571  -0.0458 88  ARG B CA  
651  C C   . ARG A 90  ? 1.2581 0.9183 0.6830 0.2138  0.3571  -0.0412 88  ARG B C   
652  O O   . ARG A 90  ? 1.2859 0.9166 0.7082 0.2054  0.3563  -0.0350 88  ARG B O   
653  C CB  . ARG A 90  ? 1.3545 1.0254 0.7782 0.2419  0.3552  -0.0433 88  ARG B CB  
654  C CG  . ARG A 90  ? 1.3707 1.0151 0.7860 0.2607  0.3537  -0.0416 88  ARG B CG  
655  C CD  . ARG A 90  ? 1.3815 1.0426 0.7951 0.2787  0.3538  -0.0523 88  ARG B CD  
656  N NE  . ARG A 90  ? 1.4424 1.0965 0.8524 0.2805  0.3558  -0.0605 88  ARG B NE  
657  C CZ  . ARG A 90  ? 1.4152 1.0889 0.8259 0.2933  0.3559  -0.0724 88  ARG B CZ  
658  N NH1 . ARG A 90  ? 1.4352 1.1378 0.8501 0.3054  0.3543  -0.0778 88  ARG B NH1 
659  N NH2 . ARG A 90  ? 1.3741 1.0405 0.7821 0.2937  0.3576  -0.0801 88  ARG B NH2 
660  N N   . ALA A 91  ? 1.2822 0.9816 0.7128 0.2055  0.3579  -0.0443 89  ALA B N   
661  C CA  . ALA A 91  ? 1.3010 1.0061 0.7330 0.1866  0.3576  -0.0395 89  ALA B CA  
662  C C   . ALA A 91  ? 1.3314 1.0222 0.7646 0.1785  0.3549  -0.0291 89  ALA B C   
663  O O   . ALA A 91  ? 1.2598 0.9435 0.6921 0.1641  0.3537  -0.0242 89  ALA B O   
664  C CB  . ALA A 91  ? 1.2087 0.9598 0.6442 0.1788  0.3595  -0.0439 89  ALA B CB  
665  N N   . GLU A 92  ? 1.3055 0.9922 0.7401 0.1880  0.3534  -0.0262 90  GLU B N   
666  C CA  . GLU A 92  ? 1.3156 0.9898 0.7516 0.1816  0.3507  -0.0176 90  GLU B CA  
667  C C   . GLU A 92  ? 1.3209 0.9530 0.7530 0.1797  0.3494  -0.0132 90  GLU B C   
668  O O   . GLU A 92  ? 1.3406 0.9614 0.7739 0.1706  0.3471  -0.0073 90  GLU B O   
669  C CB  . GLU A 92  ? 1.3506 1.0378 0.7896 0.1929  0.3496  -0.0169 90  GLU B CB  
670  C CG  . GLU A 92  ? 1.3778 1.1090 0.8209 0.1962  0.3516  -0.0238 90  GLU B CG  
671  C CD  . GLU A 92  ? 1.4559 1.1945 0.8993 0.2158  0.3515  -0.0292 90  GLU B CD  
672  O OE1 . GLU A 92  ? 1.4485 1.1596 0.8858 0.2283  0.3514  -0.0309 90  GLU B OE1 
673  O OE2 . GLU A 92  ? 1.4595 1.2318 0.9082 0.2185  0.3516  -0.0321 90  GLU B OE2 
674  N N   . ASP A 93  ? 1.2595 0.8689 0.6865 0.1872  0.3511  -0.0166 91  ASP B N   
675  C CA  . ASP A 93  ? 1.2789 0.8496 0.7015 0.1849  0.3507  -0.0130 91  ASP B CA  
676  C C   . ASP A 93  ? 1.2273 0.7876 0.6498 0.1709  0.3508  -0.0137 91  ASP B C   
677  O O   . ASP A 93  ? 1.2235 0.7541 0.6430 0.1677  0.3508  -0.0120 91  ASP B O   
678  C CB  . ASP A 93  ? 1.3263 0.8739 0.7410 0.1984  0.3529  -0.0154 91  ASP B CB  
679  C CG  . ASP A 93  ? 1.3268 0.8769 0.7388 0.2137  0.3523  -0.0137 91  ASP B CG  
680  O OD1 . ASP A 93  ? 1.2759 0.8207 0.6891 0.2130  0.3503  -0.0074 91  ASP B OD1 
681  O OD2 . ASP A 93  ? 1.3297 0.8868 0.7378 0.2269  0.3536  -0.0192 91  ASP B OD2 
682  N N   . THR A 94  ? 1.2205 0.8050 0.6455 0.1620  0.3508  -0.0161 92  THR B N   
683  C CA  . THR A 94  ? 1.1721 0.7467 0.5958 0.1492  0.3504  -0.0166 92  THR B CA  
684  C C   . THR A 94  ? 1.1223 0.6836 0.5471 0.1394  0.3470  -0.0103 92  THR B C   
685  O O   . THR A 94  ? 1.1234 0.7009 0.5504 0.1355  0.3451  -0.0062 92  THR B O   
686  C CB  . THR A 94  ? 1.1328 0.7371 0.5564 0.1423  0.3514  -0.0202 92  THR B CB  
687  O OG1 . THR A 94  ? 1.1007 0.7220 0.5251 0.1316  0.3493  -0.0148 92  THR B OG1 
688  C CG2 . THR A 94  ? 1.1463 0.7768 0.5710 0.1529  0.3540  -0.0263 92  THR B CG2 
689  N N   . ALA A 95  ? 1.0685 0.6013 0.4917 0.1354  0.3464  -0.0101 93  ALA B N   
690  C CA  . ALA A 95  ? 1.0730 0.5925 0.4974 0.1272  0.3431  -0.0059 93  ALA B CA  
691  C C   . ALA A 95  ? 1.0746 0.5668 0.4975 0.1227  0.3432  -0.0082 93  ALA B C   
692  O O   . ALA A 95  ? 1.0716 0.5545 0.4922 0.1255  0.3461  -0.0124 93  ALA B O   
693  C CB  . ALA A 95  ? 1.0988 0.6173 0.5258 0.1336  0.3417  -0.0013 93  ALA B CB  
694  N N   . VAL A 96  ? 1.0541 0.5344 0.4779 0.1153  0.3401  -0.0062 94  VAL B N   
695  C CA  . VAL A 96  ? 1.0736 0.5306 0.4973 0.1107  0.3400  -0.0086 94  VAL B CA  
696  C C   . VAL A 96  ? 1.1175 0.5605 0.5422 0.1169  0.3411  -0.0059 94  VAL B C   
697  O O   . VAL A 96  ? 1.0991 0.5455 0.5260 0.1189  0.3388  -0.0020 94  VAL B O   
698  C CB  . VAL A 96  ? 1.0474 0.5002 0.4710 0.1002  0.3360  -0.0092 94  VAL B CB  
699  C CG1 . VAL A 96  ? 1.0464 0.4795 0.4721 0.0969  0.3354  -0.0112 94  VAL B CG1 
700  C CG2 . VAL A 96  ? 1.0500 0.5081 0.4697 0.0934  0.3358  -0.0127 94  VAL B CG2 
701  N N   . TYR A 97  ? 1.1019 0.5286 0.5234 0.1195  0.3447  -0.0077 95  TYR B N   
702  C CA  . TYR A 97  ? 1.0772 0.4885 0.4958 0.1252  0.3468  -0.0044 95  TYR B CA  
703  C C   . TYR A 97  ? 1.1035 0.4993 0.5236 0.1162  0.3462  -0.0056 95  TYR B C   
704  O O   . TYR A 97  ? 1.1149 0.5028 0.5350 0.1086  0.3473  -0.0102 95  TYR B O   
705  C CB  . TYR A 97  ? 1.0960 0.4967 0.5071 0.1333  0.3518  -0.0054 95  TYR B CB  
706  C CG  . TYR A 97  ? 1.0995 0.5164 0.5093 0.1452  0.3519  -0.0037 95  TYR B CG  
707  C CD1 . TYR A 97  ? 1.0945 0.5355 0.5082 0.1453  0.3507  -0.0067 95  TYR B CD1 
708  C CD2 . TYR A 97  ? 1.1095 0.5197 0.5139 0.1561  0.3534  0.0005  95  TYR B CD2 
709  C CE1 . TYR A 97  ? 1.1030 0.5632 0.5165 0.1558  0.3509  -0.0063 95  TYR B CE1 
710  C CE2 . TYR A 97  ? 1.1127 0.5402 0.5165 0.1677  0.3531  0.0011  95  TYR B CE2 
711  C CZ  . TYR A 97  ? 1.1665 0.6201 0.5757 0.1674  0.3519  -0.0028 95  TYR B CZ  
712  O OH  . TYR A 97  ? 1.2350 0.7090 0.6443 0.1787  0.3518  -0.0034 95  TYR B OH  
713  N N   . TYR A 98  ? 1.0771 0.4714 0.4991 0.1169  0.3443  -0.0022 96  TYR B N   
714  C CA  . TYR A 98  ? 1.0653 0.4484 0.4890 0.1095  0.3439  -0.0035 96  TYR B CA  
715  C C   . TYR A 98  ? 1.0802 0.4460 0.4965 0.1141  0.3488  -0.0002 96  TYR B C   
716  O O   . TYR A 98  ? 1.0878 0.4531 0.4990 0.1245  0.3502  0.0047  96  TYR B O   
717  C CB  . TYR A 98  ? 1.0498 0.4441 0.4798 0.1072  0.3383  -0.0028 96  TYR B CB  
718  C CG  . TYR A 98  ? 1.0389 0.4428 0.4728 0.1001  0.3338  -0.0064 96  TYR B CG  
719  C CD1 . TYR A 98  ? 1.0365 0.4348 0.4723 0.0907  0.3324  -0.0123 96  TYR B CD1 
720  C CD2 . TYR A 98  ? 1.0334 0.4516 0.4672 0.1025  0.3312  -0.0042 96  TYR B CD2 
721  C CE1 . TYR A 98  ? 1.0302 0.4345 0.4664 0.0852  0.3283  -0.0155 96  TYR B CE1 
722  C CE2 . TYR A 98  ? 1.0282 0.4512 0.4613 0.0958  0.3278  -0.0067 96  TYR B CE2 
723  C CZ  . TYR A 98  ? 1.0274 0.4421 0.4609 0.0878  0.3262  -0.0122 96  TYR B CZ  
724  O OH  . TYR A 98  ? 1.0257 0.4422 0.4553 0.0819  0.3227  -0.0146 96  TYR B OH  
725  N N   . CYS A 99  ? 1.0991 0.4507 0.5136 0.1062  0.3516  -0.0030 97  CYS B N   
726  C CA  . CYS A 99  ? 1.1169 0.4506 0.5222 0.1085  0.3567  0.0005  97  CYS B CA  
727  C C   . CYS A 99  ? 1.1376 0.4731 0.5484 0.1002  0.3549  -0.0020 97  CYS B C   
728  O O   . CYS A 99  ? 1.1480 0.4927 0.5679 0.0910  0.3513  -0.0081 97  CYS B O   
729  C CB  . CYS A 99  ? 1.1686 0.4806 0.5630 0.1067  0.3641  -0.0007 97  CYS B CB  
730  S SG  . CYS A 99  ? 1.2156 0.5234 0.6153 0.0903  0.3655  -0.0091 97  CYS B SG  
731  N N   . ALA A 100 ? 1.1008 0.4287 0.5058 0.1039  0.3573  0.0020  98  ALA B N   
732  C CA  . ALA A 100 ? 1.1381 0.4749 0.5507 0.0973  0.3541  -0.0013 98  ALA B CA  
733  C C   . ALA A 100 ? 1.1029 0.4256 0.5056 0.0985  0.3594  0.0018  98  ALA B C   
734  O O   . ALA A 100 ? 1.1176 0.4297 0.5093 0.1086  0.3626  0.0086  98  ALA B O   
735  C CB  . ALA A 100 ? 1.0665 0.4254 0.4896 0.1012  0.3460  -0.0009 98  ALA B CB  
736  N N   . ARG A 101 ? 1.0995 0.4240 0.5063 0.0884  0.3600  -0.0039 99  ARG B N   
737  C CA  . ARG A 101 ? 1.1133 0.4272 0.5114 0.0869  0.3652  -0.0027 99  ARG B CA  
738  C C   . ARG A 101 ? 1.1020 0.4313 0.5046 0.0940  0.3602  0.0000  99  ARG B C   
739  O O   . ARG A 101 ? 1.0792 0.4308 0.4956 0.0942  0.3521  -0.0032 99  ARG B O   
740  C CB  . ARG A 101 ? 1.1117 0.4275 0.5148 0.0727  0.3672  -0.0118 99  ARG B CB  
741  C CG  . ARG A 101 ? 1.1305 0.4329 0.5225 0.0681  0.3748  -0.0118 99  ARG B CG  
742  C CD  . ARG A 101 ? 1.1311 0.4356 0.5278 0.0533  0.3778  -0.0218 99  ARG B CD  
743  N NE  . ARG A 101 ? 1.1119 0.4419 0.5225 0.0483  0.3720  -0.0296 99  ARG B NE  
744  C CZ  . ARG A 101 ? 1.1077 0.4480 0.5260 0.0363  0.3726  -0.0404 99  ARG B CZ  
745  N NH1 . ARG A 101 ? 1.1217 0.4483 0.5352 0.0268  0.3793  -0.0443 99  ARG B NH1 
746  N NH2 . ARG A 101 ? 1.0892 0.4554 0.5210 0.0340  0.3661  -0.0482 99  ARG B NH2 
747  N N   . GLY A 102 ? 1.1395 0.4552 0.5286 0.0998  0.3653  0.0057  100 GLY B N   
748  C CA  . GLY A 102 ? 1.1118 0.4423 0.5042 0.1062  0.3612  0.0077  100 GLY B CA  
749  C C   . GLY A 102 ? 1.1028 0.4465 0.5028 0.0964  0.3600  0.0002  100 GLY B C   
750  O O   . GLY A 102 ? 1.1148 0.4480 0.5097 0.0863  0.3660  -0.0042 100 GLY B O   
751  N N   . TYR A 103 ? 1.0818 0.4499 0.4943 0.0993  0.3522  -0.0024 101 TYR B N   
752  C CA  . TYR A 103 ? 1.0720 0.4575 0.4924 0.0932  0.3497  -0.0098 101 TYR B CA  
753  C C   . TYR A 103 ? 1.0711 0.4654 0.4890 0.1040  0.3473  -0.0044 101 TYR B C   
754  O O   . TYR A 103 ? 1.0547 0.4645 0.4816 0.1108  0.3402  -0.0036 101 TYR B O   
755  C CB  . TYR A 103 ? 1.0476 0.4546 0.4858 0.0873  0.3414  -0.0195 101 TYR B CB  
756  C CG  . TYR A 103 ? 1.0371 0.4644 0.4850 0.0812  0.3381  -0.0299 101 TYR B CG  
757  C CD1 . TYR A 103 ? 1.0249 0.4713 0.4795 0.0872  0.3320  -0.0317 101 TYR B CD1 
758  C CD2 . TYR A 103 ? 1.0391 0.4685 0.4903 0.0696  0.3407  -0.0393 101 TYR B CD2 
759  C CE1 . TYR A 103 ? 1.0158 0.4820 0.4797 0.0822  0.3286  -0.0427 101 TYR B CE1 
760  C CE2 . TYR A 103 ? 1.0296 0.4802 0.4905 0.0645  0.3373  -0.0504 101 TYR B CE2 
761  C CZ  . TYR A 103 ? 1.0181 0.4870 0.4853 0.0710  0.3312  -0.0522 101 TYR B CZ  
762  O OH  . TYR A 103 ? 1.0095 0.5009 0.4866 0.0665  0.3277  -0.0648 101 TYR B OH  
763  N N   . GLY A 104 ? 1.0910 0.4739 0.4952 0.1056  0.3538  -0.0005 102 GLY B N   
764  C CA  . GLY A 104 ? 1.0946 0.4827 0.4934 0.1172  0.3525  0.0058  102 GLY B CA  
765  C C   . GLY A 104 ? 1.0924 0.4779 0.4904 0.1293  0.3494  0.0131  102 GLY B C   
766  O O   . GLY A 104 ? 1.1569 0.5207 0.5439 0.1325  0.3542  0.0184  102 GLY B O   
767  N N   . TRP A 105 ? 1.0735 0.4813 0.4827 0.1359  0.3418  0.0127  103 TRP B N   
768  C CA  . TRP A 105 ? 1.0714 0.4827 0.4829 0.1455  0.3383  0.0176  103 TRP B CA  
769  C C   . TRP A 105 ? 1.0568 0.4779 0.4818 0.1397  0.3331  0.0126  103 TRP B C   
770  O O   . TRP A 105 ? 1.0773 0.5071 0.5065 0.1460  0.3294  0.0151  103 TRP B O   
771  C CB  . TRP A 105 ? 1.0962 0.5260 0.5108 0.1562  0.3335  0.0201  103 TRP B CB  
772  C CG  . TRP A 105 ? 1.1476 0.5702 0.5482 0.1643  0.3375  0.0256  103 TRP B CG  
773  C CD1 . TRP A 105 ? 1.1878 0.6038 0.5772 0.1780  0.3390  0.0335  103 TRP B CD1 
774  C CD2 . TRP A 105 ? 1.1218 0.5448 0.5174 0.1598  0.3403  0.0233  103 TRP B CD2 
775  N NE1 . TRP A 105 ? 1.2316 0.6408 0.6077 0.1827  0.3427  0.0370  103 TRP B NE1 
776  C CE2 . TRP A 105 ? 1.1681 0.5821 0.5478 0.1712  0.3437  0.0310  103 TRP B CE2 
777  C CE3 . TRP A 105 ? 1.1560 0.5874 0.5585 0.1475  0.3403  0.0150  103 TRP B CE3 
778  C CZ2 . TRP A 105 ? 1.1915 0.6037 0.5611 0.1700  0.3474  0.0314  103 TRP B CZ2 
779  C CZ3 . TRP A 105 ? 1.1782 0.6103 0.5718 0.1459  0.3442  0.0146  103 TRP B CZ3 
780  C CH2 . TRP A 105 ? 1.1675 0.5895 0.5444 0.1566  0.3479  0.0232  103 TRP B CH2 
781  N N   . ALA A 106 ? 1.0425 0.4630 0.4735 0.1278  0.3329  0.0054  104 ALA B N   
782  C CA  . ALA A 106 ? 1.0284 0.4545 0.4690 0.1228  0.3285  0.0013  104 ALA B CA  
783  C C   . ALA A 106 ? 1.0391 0.4469 0.4742 0.1164  0.3337  0.0012  104 ALA B C   
784  O O   . ALA A 106 ? 1.0585 0.4477 0.4817 0.1169  0.3408  0.0049  104 ALA B O   
785  C CB  . ALA A 106 ? 1.0113 0.4541 0.4641 0.1160  0.3221  -0.0084 104 ALA B CB  
786  N N   . LEU A 107 ? 1.0281 0.4402 0.4708 0.1106  0.3301  -0.0033 105 LEU B N   
787  C CA  . LEU A 107 ? 1.0352 0.4340 0.4749 0.1047  0.3338  -0.0043 105 LEU B CA  
788  C C   . LEU A 107 ? 1.0241 0.4301 0.4730 0.0939  0.3302  -0.0139 105 LEU B C   
789  O O   . LEU A 107 ? 1.0117 0.4272 0.4672 0.0931  0.3242  -0.0169 105 LEU B O   
790  C CB  . LEU A 107 ? 1.0345 0.4330 0.4729 0.1105  0.3328  0.0003  105 LEU B CB  
791  C CG  . LEU A 107 ? 1.0448 0.4399 0.4753 0.1227  0.3353  0.0085  105 LEU B CG  
792  C CD1 . LEU A 107 ? 1.0375 0.4441 0.4711 0.1289  0.3320  0.0111  105 LEU B CD1 
793  C CD2 . LEU A 107 ? 1.0673 0.4397 0.4847 0.1241  0.3432  0.0119  105 LEU B CD2 
794  N N   . ASP A 108 ? 1.0304 0.4312 0.4786 0.0856  0.3339  -0.0193 106 ASP B N   
795  C CA  . ASP A 108 ? 1.0180 0.4309 0.4769 0.0770  0.3290  -0.0300 106 ASP B CA  
796  C C   . ASP A 108 ? 1.0519 0.4592 0.5122 0.0705  0.3293  -0.0338 106 ASP B C   
797  O O   . ASP A 108 ? 1.0614 0.4793 0.5302 0.0669  0.3227  -0.0412 106 ASP B O   
798  C CB  . ASP A 108 ? 1.0205 0.4391 0.4815 0.0709  0.3311  -0.0369 106 ASP B CB  
799  C CG  . ASP A 108 ? 1.0401 0.4412 0.4910 0.0648  0.3410  -0.0357 106 ASP B CG  
800  O OD1 . ASP A 108 ? 1.0523 0.4355 0.4947 0.0655  0.3460  -0.0301 106 ASP B OD1 
801  O OD2 . ASP A 108 ? 1.0450 0.4502 0.4954 0.0593  0.3442  -0.0407 106 ASP B OD2 
802  N N   . TYR A 109 ? 1.0709 0.4614 0.5225 0.0696  0.3363  -0.0293 107 TYR B N   
803  C CA  . TYR A 109 ? 1.0343 0.4207 0.4872 0.0635  0.3368  -0.0334 107 TYR B CA  
804  C C   . TYR A 109 ? 1.0809 0.4578 0.5271 0.0697  0.3388  -0.0259 107 TYR B C   
805  O O   . TYR A 109 ? 1.0527 0.4188 0.4898 0.0770  0.3435  -0.0181 107 TYR B O   
806  C CB  . TYR A 109 ? 1.0473 0.4236 0.4969 0.0544  0.3439  -0.0382 107 TYR B CB  
807  C CG  . TYR A 109 ? 1.0485 0.4391 0.5081 0.0455  0.3410  -0.0497 107 TYR B CG  
808  C CD1 . TYR A 109 ? 1.0539 0.4500 0.5139 0.0438  0.3426  -0.0522 107 TYR B CD1 
809  C CD2 . TYR A 109 ? 1.0450 0.4447 0.5133 0.0391  0.3367  -0.0591 107 TYR B CD2 
810  C CE1 . TYR A 109 ? 1.0339 0.4459 0.5038 0.0360  0.3400  -0.0643 107 TYR B CE1 
811  C CE2 . TYR A 109 ? 1.0295 0.4446 0.5078 0.0321  0.3334  -0.0712 107 TYR B CE2 
812  C CZ  . TYR A 109 ? 1.0245 0.4464 0.5040 0.0305  0.3351  -0.0740 107 TYR B CZ  
813  O OH  . TYR A 109 ? 1.0322 0.4720 0.5223 0.0239  0.3318  -0.0874 107 TYR B OH  
814  N N   . TRP A 110 ? 1.1400 0.5216 0.5900 0.0674  0.3352  -0.0291 108 TRP B N   
815  C CA  . TRP A 110 ? 1.0756 0.4533 0.5207 0.0730  0.3361  -0.0237 108 TRP B CA  
816  C C   . TRP A 110 ? 1.1143 0.4873 0.5590 0.0670  0.3381  -0.0283 108 TRP B C   
817  O O   . TRP A 110 ? 1.1303 0.5077 0.5807 0.0588  0.3359  -0.0364 108 TRP B O   
818  C CB  . TRP A 110 ? 1.0259 0.4157 0.4741 0.0775  0.3296  -0.0219 108 TRP B CB  
819  C CG  . TRP A 110 ? 1.0212 0.4172 0.4700 0.0843  0.3275  -0.0173 108 TRP B CG  
820  C CD1 . TRP A 110 ? 1.0157 0.4170 0.4686 0.0833  0.3253  -0.0199 108 TRP B CD1 
821  C CD2 . TRP A 110 ? 1.0214 0.4216 0.4671 0.0934  0.3273  -0.0104 108 TRP B CD2 
822  N NE1 . TRP A 110 ? 1.0128 0.4201 0.4650 0.0913  0.3238  -0.0145 108 TRP B NE1 
823  C CE2 . TRP A 110 ? 1.0160 0.4231 0.4640 0.0975  0.3249  -0.0087 108 TRP B CE2 
824  C CE3 . TRP A 110 ? 1.0257 0.4269 0.4675 0.0985  0.3289  -0.0062 108 TRP B CE3 
825  C CZ2 . TRP A 110 ? 1.0147 0.4291 0.4614 0.1064  0.3241  -0.0028 108 TRP B CZ2 
826  C CZ3 . TRP A 110 ? 1.0241 0.4341 0.4650 0.1071  0.3281  -0.0009 108 TRP B CZ3 
827  C CH2 . TRP A 110 ? 1.0186 0.4349 0.4620 0.1109  0.3257  0.0009  108 TRP B CH2 
828  N N   . GLY A 111 ? 1.2095 0.5750 0.6477 0.0717  0.3418  -0.0240 109 GLY B N   
829  C CA  . GLY A 111 ? 1.2121 0.5764 0.6501 0.0677  0.3427  -0.0283 109 GLY B CA  
830  C C   . GLY A 111 ? 1.2276 0.6048 0.6695 0.0674  0.3362  -0.0302 109 GLY B C   
831  O O   . GLY A 111 ? 1.2105 0.5960 0.6549 0.0694  0.3312  -0.0288 109 GLY B O   
832  N N   . GLN A 112 ? 1.1768 0.5545 0.6177 0.0646  0.3366  -0.0339 110 GLN B N   
833  C CA  . GLN A 112 ? 1.0845 0.4715 0.5248 0.0650  0.3319  -0.0345 110 GLN B CA  
834  C C   . GLN A 112 ? 1.0593 0.4496 0.4944 0.0726  0.3341  -0.0286 110 GLN B C   
835  O O   . GLN A 112 ? 1.0824 0.4813 0.5153 0.0742  0.3309  -0.0264 110 GLN B O   
836  C CB  . GLN A 112 ? 1.0910 0.4795 0.5327 0.0579  0.3302  -0.0424 110 GLN B CB  
837  C CG  . GLN A 112 ? 1.2195 0.6134 0.6644 0.0531  0.3231  -0.0477 110 GLN B CG  
838  C CD  . GLN A 112 ? 1.3120 0.7078 0.7613 0.0458  0.3212  -0.0577 110 GLN B CD  
839  O OE1 . GLN A 112 ? 1.2634 0.6567 0.7131 0.0434  0.3255  -0.0607 110 GLN B OE1 
840  N NE2 . GLN A 112 ? 1.2557 0.6565 0.7084 0.0427  0.3141  -0.0639 110 GLN B NE2 
841  N N   . GLY A 113 ? 1.0844 0.4680 0.5164 0.0775  0.3396  -0.0261 111 GLY B N   
842  C CA  . GLY A 113 ? 1.0978 0.4870 0.5259 0.0862  0.3415  -0.0216 111 GLY B CA  
843  C C   . GLY A 113 ? 1.0862 0.4767 0.5115 0.0863  0.3442  -0.0255 111 GLY B C   
844  O O   . GLY A 113 ? 1.0698 0.4582 0.4963 0.0793  0.3439  -0.0314 111 GLY B O   
845  N N   . THR A 114 ? 1.0764 0.4718 0.4982 0.0951  0.3468  -0.0228 112 THR B N   
846  C CA  . THR A 114 ? 1.0852 0.4885 0.5049 0.0963  0.3484  -0.0268 112 THR B CA  
847  C C   . THR A 114 ? 1.0824 0.5048 0.5013 0.1033  0.3476  -0.0238 112 THR B C   
848  O O   . THR A 114 ? 1.1066 0.5321 0.5254 0.1105  0.3477  -0.0189 112 THR B O   
849  C CB  . THR A 114 ? 1.0990 0.4891 0.5143 0.0999  0.3538  -0.0298 112 THR B CB  
850  O OG1 . THR A 114 ? 1.1811 0.5643 0.5916 0.1101  0.3566  -0.0249 112 THR B OG1 
851  C CG2 . THR A 114 ? 1.1734 0.5473 0.5894 0.0912  0.3553  -0.0337 112 THR B CG2 
852  N N   . LEU A 115 ? 1.0790 0.5160 0.4971 0.1006  0.3469  -0.0271 113 LEU B N   
853  C CA  . LEU A 115 ? 1.0775 0.5368 0.4947 0.1053  0.3468  -0.0251 113 LEU B CA  
854  C C   . LEU A 115 ? 1.0896 0.5533 0.5051 0.1154  0.3508  -0.0279 113 LEU B C   
855  O O   . LEU A 115 ? 1.0994 0.5544 0.5130 0.1156  0.3533  -0.0334 113 LEU B O   
856  C CB  . LEU A 115 ? 1.0737 0.5472 0.4886 0.0972  0.3447  -0.0270 113 LEU B CB  
857  C CG  . LEU A 115 ? 1.0720 0.5716 0.4853 0.0991  0.3447  -0.0241 113 LEU B CG  
858  C CD1 . LEU A 115 ? 1.0652 0.5683 0.4809 0.1022  0.3430  -0.0176 113 LEU B CD1 
859  C CD2 . LEU A 115 ? 1.1348 0.6460 0.5427 0.0891  0.3427  -0.0244 113 LEU B CD2 
860  N N   . VAL A 116 ? 1.0901 0.5668 0.5058 0.1241  0.3513  -0.0248 114 VAL B N   
861  C CA  . VAL A 116 ? 1.1028 0.5849 0.5162 0.1357  0.3545  -0.0279 114 VAL B CA  
862  C C   . VAL A 116 ? 1.1102 0.6254 0.5255 0.1379  0.3540  -0.0285 114 VAL B C   
863  O O   . VAL A 116 ? 1.1131 0.6409 0.5308 0.1389  0.3522  -0.0236 114 VAL B O   
864  C CB  . VAL A 116 ? 1.1112 0.5767 0.5217 0.1456  0.3558  -0.0240 114 VAL B CB  
865  C CG1 . VAL A 116 ? 1.1224 0.6012 0.5304 0.1594  0.3577  -0.0264 114 VAL B CG1 
866  C CG2 . VAL A 116 ? 1.1323 0.5664 0.5381 0.1437  0.3583  -0.0246 114 VAL B CG2 
867  N N   . THR A 117 ? 1.1615 0.6926 0.5759 0.1377  0.3556  -0.0350 115 THR B N   
868  C CA  . THR A 117 ? 1.1286 0.6949 0.5441 0.1378  0.3559  -0.0368 115 THR B CA  
869  C C   . THR A 117 ? 1.1333 0.7114 0.5485 0.1514  0.3587  -0.0434 115 THR B C   
870  O O   . THR A 117 ? 1.1248 0.6929 0.5375 0.1559  0.3607  -0.0502 115 THR B O   
871  C CB  . THR A 117 ? 1.1281 0.7058 0.5418 0.1268  0.3556  -0.0398 115 THR B CB  
872  O OG1 . THR A 117 ? 1.1145 0.6650 0.5269 0.1192  0.3541  -0.0389 115 THR B OG1 
873  C CG2 . THR A 117 ? 1.1491 0.7531 0.5622 0.1180  0.3540  -0.0348 115 THR B CG2 
874  N N   . VAL A 118 ? 1.1355 0.7344 0.5530 0.1585  0.3586  -0.0420 116 VAL B N   
875  C CA  . VAL A 118 ? 1.1401 0.7541 0.5573 0.1725  0.3608  -0.0493 116 VAL B CA  
876  C C   . VAL A 118 ? 1.1849 0.8433 0.6058 0.1694  0.3613  -0.0521 116 VAL B C   
877  O O   . VAL A 118 ? 1.2085 0.8827 0.6320 0.1634  0.3600  -0.0459 116 VAL B O   
878  C CB  . VAL A 118 ? 1.1999 0.7976 0.6154 0.1861  0.3604  -0.0465 116 VAL B CB  
879  C CG1 . VAL A 118 ? 1.2188 0.7743 0.6297 0.1845  0.3600  -0.0406 116 VAL B CG1 
880  C CG2 . VAL A 118 ? 1.1818 0.8011 0.6014 0.1875  0.3588  -0.0417 116 VAL B CG2 
881  N N   . SER A 119 ? 1.1871 0.8664 0.6079 0.1722  0.3635  -0.0618 117 SER B N   
882  C CA  . SER A 119 ? 1.1655 0.8894 0.5887 0.1666  0.3650  -0.0658 117 SER B CA  
883  C C   . SER A 119 ? 1.1736 0.9116 0.5965 0.1738  0.3675  -0.0787 117 SER B C   
884  O O   . SER A 119 ? 1.1656 0.8760 0.5858 0.1799  0.3677  -0.0831 117 SER B O   
885  C CB  . SER A 119 ? 1.1847 0.9161 0.6059 0.1480  0.3639  -0.0587 117 SER B CB  
886  O OG  . SER A 119 ? 1.2515 1.0245 0.6724 0.1409  0.3659  -0.0630 117 SER B OG  
887  N N   . SER A 120 ? 1.1895 0.9718 0.6151 0.1726  0.3695  -0.0854 118 SER B N   
888  C CA  . SER A 120 ? 1.2025 1.0034 0.6284 0.1779  0.3719  -0.0990 118 SER B CA  
889  C C   . SER A 120 ? 1.1696 0.9805 0.5923 0.1636  0.3727  -0.0994 118 SER B C   
890  O O   . SER A 120 ? 1.1816 1.0042 0.6041 0.1672  0.3745  -0.1108 118 SER B O   
891  C CB  . SER A 120 ? 1.1487 0.9954 0.5793 0.1841  0.3743  -0.1088 118 SER B CB  
892  O OG  . SER A 120 ? 1.1548 1.0268 0.5876 0.1752  0.3744  -0.1013 118 SER B OG  
893  N N   . ALA A 121 ? 1.1901 0.9962 0.6096 0.1481  0.3711  -0.0879 119 ALA B N   
894  C CA  . ALA A 121 ? 1.1942 1.0062 0.6088 0.1353  0.3712  -0.0876 119 ALA B CA  
895  C C   . ALA A 121 ? 1.2033 0.9801 0.6162 0.1395  0.3706  -0.0922 119 ALA B C   
896  O O   . ALA A 121 ? 1.2379 0.9793 0.6521 0.1483  0.3696  -0.0916 119 ALA B O   
897  C CB  . ALA A 121 ? 1.2201 1.0281 0.6301 0.1188  0.3688  -0.0735 119 ALA B CB  
898  N N   . SER A 122 ? 1.2136 1.0016 0.6230 0.1321  0.3712  -0.0967 120 SER B N   
899  C CA  . SER A 122 ? 1.2254 0.9875 0.6335 0.1347  0.3710  -0.1031 120 SER B CA  
900  C C   . SER A 122 ? 1.2234 0.9660 0.6263 0.1209  0.3686  -0.0948 120 SER B C   
901  O O   . SER A 122 ? 1.2516 1.0080 0.6500 0.1087  0.3673  -0.0860 120 SER B O   
902  C CB  . SER A 122 ? 1.1992 0.9906 0.6079 0.1388  0.3736  -0.1174 120 SER B CB  
903  O OG  . SER A 122 ? 1.1795 0.9477 0.5867 0.1394  0.3731  -0.1235 120 SER B OG  
904  N N   . THR A 123 ? 1.2412 0.9511 0.6440 0.1227  0.3678  -0.0981 121 THR B N   
905  C CA  . THR A 123 ? 1.3089 0.9979 0.7075 0.1111  0.3653  -0.0924 121 THR B CA  
906  C C   . THR A 123 ? 1.3598 1.0733 0.7526 0.1023  0.3655  -0.0959 121 THR B C   
907  O O   . THR A 123 ? 1.3211 1.0496 0.7148 0.1071  0.3674  -0.1073 121 THR B O   
908  C CB  . THR A 123 ? 1.2868 0.9366 0.6879 0.1152  0.3648  -0.0957 121 THR B CB  
909  O OG1 . THR A 123 ? 1.2807 0.9160 0.6784 0.1048  0.3627  -0.0945 121 THR B OG1 
910  C CG2 . THR A 123 ? 1.3325 0.9826 0.7365 0.1267  0.3673  -0.1084 121 THR B CG2 
911  N N   . LYS A 124 ? 1.4495 1.1664 0.8352 0.0894  0.3631  -0.0860 122 LYS B N   
912  C CA  . LYS A 124 ? 1.4520 1.1943 0.8289 0.0793  0.3628  -0.0858 122 LYS B CA  
913  C C   . LYS A 124 ? 1.4664 1.1882 0.8343 0.0669  0.3588  -0.0761 122 LYS B C   
914  O O   . LYS A 124 ? 1.4633 1.1739 0.8294 0.0620  0.3565  -0.0654 122 LYS B O   
915  C CB  . LYS A 124 ? 1.4575 1.2420 0.8322 0.0758  0.3646  -0.0824 122 LYS B CB  
916  C CG  . LYS A 124 ? 1.5073 1.3241 0.8729 0.0668  0.3653  -0.0839 122 LYS B CG  
917  C CD  . LYS A 124 ? 1.5108 1.3530 0.8679 0.0535  0.3643  -0.0710 122 LYS B CD  
918  C CE  . LYS A 124 ? 1.5079 1.3947 0.8698 0.0565  0.3681  -0.0747 122 LYS B CE  
919  N NZ  . LYS A 124 ? 1.5217 1.4249 0.8785 0.0444  0.3668  -0.0605 122 LYS B NZ  
920  N N   . GLY A 125 ? 1.3685 1.0859 0.7302 0.0621  0.3577  -0.0803 123 GLY B N   
921  C CA  . GLY A 125 ? 1.3198 1.0201 0.6704 0.0507  0.3535  -0.0725 123 GLY B CA  
922  C C   . GLY A 125 ? 1.3614 1.0818 0.7001 0.0387  0.3516  -0.0601 123 GLY B C   
923  O O   . GLY A 125 ? 1.3285 1.0825 0.6679 0.0382  0.3541  -0.0585 123 GLY B O   
924  N N   . PRO A 126 ? 1.3536 1.0542 0.6804 0.0284  0.3468  -0.0510 124 PRO B N   
925  C CA  . PRO A 126 ? 1.3422 1.0554 0.6564 0.0156  0.3439  -0.0370 124 PRO B CA  
926  C C   . PRO A 126 ? 1.3801 1.1145 0.6787 0.0051  0.3424  -0.0340 124 PRO B C   
927  O O   . PRO A 126 ? 1.3708 1.0992 0.6640 0.0055  0.3417  -0.0410 124 PRO B O   
928  C CB  . PRO A 126 ? 1.2645 0.9394 0.5726 0.0111  0.3385  -0.0297 124 PRO B CB  
929  C CG  . PRO A 126 ? 1.2502 0.9026 0.5578 0.0152  0.3377  -0.0397 124 PRO B CG  
930  C CD  . PRO A 126 ? 1.3190 0.9829 0.6429 0.0278  0.3433  -0.0531 124 PRO B CD  
931  N N   . SER A 127 ? 1.4075 1.1679 0.6986 -0.0053 0.3417  -0.0230 125 SER B N   
932  C CA  . SER A 127 ? 1.4053 1.1805 0.6779 -0.0190 0.3384  -0.0150 125 SER B CA  
933  C C   . SER A 127 ? 1.3862 1.1290 0.6428 -0.0309 0.3303  -0.0014 125 SER B C   
934  O O   . SER A 127 ? 1.3572 1.0848 0.6171 -0.0326 0.3281  0.0060  125 SER B O   
935  C CB  . SER A 127 ? 1.3839 1.2052 0.6564 -0.0252 0.3413  -0.0095 125 SER B CB  
936  O OG  . SER A 127 ? 1.4253 1.2707 0.7153 -0.0115 0.3482  -0.0223 125 SER B OG  
937  N N   . VAL A 128 ? 1.2899 1.0206 0.5288 -0.0383 0.3253  0.0011  126 VAL B N   
938  C CA  . VAL A 128 ? 1.2724 0.9687 0.4932 -0.0486 0.3161  0.0127  126 VAL B CA  
939  C C   . VAL A 128 ? 1.3030 1.0141 0.5024 -0.0652 0.3102  0.0262  126 VAL B C   
940  O O   . VAL A 128 ? 1.3791 1.0930 0.5658 -0.0675 0.3083  0.0233  126 VAL B O   
941  C CB  . VAL A 128 ? 1.2880 0.9476 0.5047 -0.0415 0.3135  0.0034  126 VAL B CB  
942  C CG1 . VAL A 128 ? 1.3105 0.9366 0.5043 -0.0522 0.3027  0.0153  126 VAL B CG1 
943  C CG2 . VAL A 128 ? 1.3055 0.9495 0.5436 -0.0273 0.3184  -0.0071 126 VAL B CG2 
944  N N   . PHE A 129 ? 1.2565 0.9769 0.4524 -0.0765 0.3070  0.0402  127 PHE B N   
945  C CA  . PHE A 129 ? 1.2782 1.0112 0.4560 -0.0948 0.3001  0.0567  127 PHE B CA  
946  C C   . PHE A 129 ? 1.2953 0.9857 0.4539 -0.1057 0.2871  0.0701  127 PHE B C   
947  O O   . PHE A 129 ? 1.3240 0.9845 0.4877 -0.1006 0.2849  0.0693  127 PHE B O   
948  C CB  . PHE A 129 ? 1.2724 1.0422 0.4617 -0.1003 0.3046  0.0636  127 PHE B CB  
949  C CG  . PHE A 129 ? 1.2572 1.0687 0.4644 -0.0882 0.3163  0.0500  127 PHE B CG  
950  C CD1 . PHE A 129 ? 1.2699 1.0999 0.4744 -0.0829 0.3201  0.0400  127 PHE B CD1 
951  C CD2 . PHE A 129 ? 1.2411 1.0740 0.4666 -0.0820 0.3226  0.0472  127 PHE B CD2 
952  C CE1 . PHE A 129 ? 1.2638 1.1316 0.4837 -0.0715 0.3295  0.0272  127 PHE B CE1 
953  C CE2 . PHE A 129 ? 1.2842 1.1550 0.5244 -0.0702 0.3319  0.0344  127 PHE B CE2 
954  C CZ  . PHE A 129 ? 1.3069 1.1947 0.5443 -0.0648 0.3352  0.0243  127 PHE B CZ  
955  N N   . PRO A 130 ? 1.3215 1.0060 0.4571 -0.1203 0.2772  0.0826  128 PRO B N   
956  C CA  . PRO A 130 ? 1.3406 0.9802 0.4563 -0.1288 0.2626  0.0941  128 PRO B CA  
957  C C   . PRO A 130 ? 1.3485 0.9839 0.4633 -0.1430 0.2551  0.1112  128 PRO B C   
958  O O   . PRO A 130 ? 1.3420 1.0126 0.4692 -0.1488 0.2610  0.1158  128 PRO B O   
959  C CB  . PRO A 130 ? 1.3677 1.0050 0.4589 -0.1378 0.2543  0.0999  128 PRO B CB  
960  C CG  . PRO A 130 ? 1.3657 1.0556 0.4640 -0.1406 0.2640  0.0981  128 PRO B CG  
961  C CD  . PRO A 130 ? 1.3373 1.0573 0.4637 -0.1309 0.2775  0.0890  128 PRO B CD  
962  N N   . LEU A 131 ? 1.3678 0.9588 0.4682 -0.1476 0.2415  0.1194  129 LEU B N   
963  C CA  . LEU A 131 ? 1.3838 0.9615 0.4777 -0.1634 0.2294  0.1374  129 LEU B CA  
964  C C   . LEU A 131 ? 1.4175 0.9605 0.4829 -0.1733 0.2112  0.1487  129 LEU B C   
965  O O   . LEU A 131 ? 1.4391 0.9391 0.4936 -0.1665 0.2018  0.1459  129 LEU B O   
966  C CB  . LEU A 131 ? 1.3684 0.9221 0.4742 -0.1567 0.2289  0.1352  129 LEU B CB  
967  C CG  . LEU A 131 ? 1.3387 0.9251 0.4716 -0.1485 0.2442  0.1271  129 LEU B CG  
968  C CD1 . LEU A 131 ? 1.3220 0.8804 0.4652 -0.1367 0.2449  0.1205  129 LEU B CD1 
969  C CD2 . LEU A 131 ? 1.3441 0.9632 0.4824 -0.1639 0.2446  0.1396  129 LEU B CD2 
970  N N   . ALA A 132 ? 1.4359 0.9968 0.4888 -0.1886 0.2055  0.1612  130 ALA B N   
971  C CA  . ALA A 132 ? 1.4664 0.9966 0.4919 -0.1932 0.1899  0.1675  130 ALA B CA  
972  C C   . ALA A 132 ? 1.4968 0.9934 0.5069 -0.2085 0.1690  0.1867  130 ALA B C   
973  O O   . ALA A 132 ? 1.5026 1.0156 0.5195 -0.2229 0.1676  0.1991  130 ALA B O   
974  C CB  . ALA A 132 ? 1.4786 1.0425 0.4954 -0.1989 0.1941  0.1689  130 ALA B CB  
975  N N   . PRO A 133 ? 1.5188 0.9690 0.5076 -0.2058 0.1516  0.1892  131 PRO B N   
976  C CA  . PRO A 133 ? 1.5499 0.9636 0.5247 -0.2185 0.1291  0.2066  131 PRO B CA  
977  C C   . PRO A 133 ? 1.6796 1.1059 0.6396 -0.2373 0.1198  0.2235  131 PRO B C   
978  O O   . PRO A 133 ? 1.6527 1.1104 0.6079 -0.2395 0.1283  0.2220  131 PRO B O   
979  C CB  . PRO A 133 ? 1.5632 0.9267 0.5190 -0.2060 0.1139  0.2008  131 PRO B CB  
980  C CG  . PRO A 133 ? 1.5848 0.9644 0.5336 -0.1953 0.1247  0.1874  131 PRO B CG  
981  C CD  . PRO A 133 ? 1.5593 0.9873 0.5351 -0.1901 0.1508  0.1754  131 PRO B CD  
982  N N   . SER A 134 ? 1.7981 1.1972 0.7504 -0.2507 0.1012  0.2397  132 SER B N   
983  C CA  . SER A 134 ? 1.8513 1.2585 0.7908 -0.2707 0.0916  0.2575  132 SER B CA  
984  C C   . SER A 134 ? 1.9838 1.3374 0.9008 -0.2752 0.0636  0.2694  132 SER B C   
985  O O   . SER A 134 ? 2.0113 1.3238 0.9272 -0.2648 0.0513  0.2651  132 SER B O   
986  C CB  . SER A 134 ? 1.8904 1.3281 0.8477 -0.2857 0.1001  0.2658  132 SER B CB  
987  O OG  . SER A 134 ? 2.0062 1.4088 0.9624 -0.2947 0.0830  0.2768  132 SER B OG  
988  N N   . SER A 135 ? 2.0086 1.3628 0.9074 -0.2904 0.0531  0.2842  133 SER B N   
989  C CA  . SER A 135 ? 2.0594 1.3637 0.9359 -0.2954 0.0251  0.2966  133 SER B CA  
990  C C   . SER A 135 ? 2.1681 1.4519 1.0506 -0.3095 0.0125  0.3093  133 SER B C   
991  O O   . SER A 135 ? 2.2211 1.4560 1.0928 -0.3075 -0.0111 0.3142  133 SER B O   
992  C CB  . SER A 135 ? 1.9438 1.2550 0.7969 -0.3054 0.0186  0.3072  133 SER B CB  
993  O OG  . SER A 135 ? 1.9441 1.2102 0.7740 -0.2957 -0.0032 0.3073  133 SER B OG  
994  N N   . LYS A 136 ? 2.1847 1.5049 1.0840 -0.3233 0.0269  0.3140  134 LYS B N   
995  C CA  . LYS A 136 ? 2.2165 1.5190 1.1232 -0.3360 0.0168  0.3238  134 LYS B CA  
996  C C   . LYS A 136 ? 2.3345 1.6073 1.2550 -0.3212 0.0114  0.3137  134 LYS B C   
997  O O   . LYS A 136 ? 2.3577 1.5940 1.2768 -0.3261 -0.0073 0.3206  134 LYS B O   
998  C CB  . LYS A 136 ? 2.1373 1.4890 1.0600 -0.3519 0.0356  0.3281  134 LYS B CB  
999  C CG  . LYS A 136 ? 2.1492 1.5281 1.0999 -0.3428 0.0548  0.3153  134 LYS B CG  
1000 C CD  . LYS A 136 ? 2.1220 1.4775 1.0838 -0.3485 0.0454  0.3193  134 LYS B CD  
1001 C CE  . LYS A 136 ? 1.9679 1.3585 0.9563 -0.3434 0.0660  0.3090  134 LYS B CE  
1002 N NZ  . LYS A 136 ? 1.7447 1.1265 0.7422 -0.3568 0.0595  0.3167  134 LYS B NZ  
1003 N N   . SER A 137 ? 2.7241 2.0111 1.6575 -0.3029 0.0271  0.2970  135 SER B N   
1004 C CA  . SER A 137 ? 2.7096 1.9768 1.6587 -0.2892 0.0270  0.2864  135 SER B CA  
1005 C C   . SER A 137 ? 2.7186 1.9298 1.6542 -0.2758 0.0036  0.2831  135 SER B C   
1006 O O   . SER A 137 ? 2.6961 1.8901 1.6415 -0.2597 0.0043  0.2709  135 SER B O   
1007 C CB  . SER A 137 ? 2.6690 1.9702 1.6354 -0.2741 0.0526  0.2693  135 SER B CB  
1008 O OG  . SER A 137 ? 2.6308 1.9600 1.6204 -0.2785 0.0670  0.2678  135 SER B OG  
1009 N N   . THR A 138 ? 2.4792 1.6620 1.3921 -0.2814 -0.0176 0.2933  136 THR B N   
1010 C CA  . THR A 138 ? 2.4336 1.5608 1.3345 -0.2703 -0.0446 0.2919  136 THR B CA  
1011 C C   . THR A 138 ? 2.4714 1.5766 1.3853 -0.2766 -0.0570 0.2969  136 THR B C   
1012 O O   . THR A 138 ? 2.4459 1.5478 1.3562 -0.2952 -0.0664 0.3113  136 THR B O   
1013 C CB  . THR A 138 ? 2.3336 1.4386 1.2068 -0.2747 -0.0640 0.3016  136 THR B CB  
1014 O OG1 . THR A 138 ? 2.2652 1.3196 1.1266 -0.2581 -0.0888 0.2957  136 THR B OG1 
1015 C CG2 . THR A 138 ? 2.2887 1.3945 1.1539 -0.2986 -0.0735 0.3210  136 THR B CG2 
1016 N N   . SER A 139 ? 2.5201 1.6135 1.4502 -0.2616 -0.0548 0.2844  137 SER B N   
1017 C CA  . SER A 139 ? 2.5371 1.6037 1.4789 -0.2637 -0.0700 0.2865  137 SER B CA  
1018 C C   . SER A 139 ? 2.6170 1.6316 1.5421 -0.2588 -0.1028 0.2899  137 SER B C   
1019 O O   . SER A 139 ? 2.6563 1.6620 1.5633 -0.2713 -0.1153 0.3027  137 SER B O   
1020 C CB  . SER A 139 ? 2.4208 1.4885 1.3834 -0.2473 -0.0593 0.2713  137 SER B CB  
1021 O OG  . SER A 139 ? 2.2978 1.4060 1.2686 -0.2418 -0.0305 0.2625  137 SER B OG  
1022 N N   . GLY A 140 ? 2.5364 1.5166 1.4673 -0.2400 -0.1175 0.2781  138 GLY B N   
1023 C CA  . GLY A 140 ? 2.5640 1.4994 1.4777 -0.2286 -0.1465 0.2763  138 GLY B CA  
1024 C C   . GLY A 140 ? 2.5067 1.4461 1.4008 -0.2189 -0.1424 0.2719  138 GLY B C   
1025 O O   . GLY A 140 ? 2.5285 1.4457 1.4012 -0.2193 -0.1614 0.2779  138 GLY B O   
1026 N N   . GLY A 141 ? 2.3451 1.3140 1.2457 -0.2105 -0.1171 0.2615  139 GLY B N   
1027 C CA  . GLY A 141 ? 2.1907 1.1694 1.0742 -0.2017 -0.1089 0.2556  139 GLY B CA  
1028 C C   . GLY A 141 ? 2.0224 1.0427 0.9385 -0.1859 -0.0818 0.2335  139 GLY B C   
1029 O O   . GLY A 141 ? 1.9437 0.9699 0.8715 -0.1653 -0.0811 0.2136  139 GLY B O   
1030 N N   . THR A 142 ? 2.0600 1.1098 0.9918 -0.1954 -0.0597 0.2361  140 THR B N   
1031 C CA  . THR A 142 ? 1.9018 0.9907 0.8649 -0.1816 -0.0335 0.2164  140 THR B CA  
1032 C C   . THR A 142 ? 1.8944 1.0255 0.8539 -0.1966 -0.0063 0.2244  140 THR B C   
1033 O O   . THR A 142 ? 1.9950 1.1302 0.9434 -0.2180 -0.0047 0.2428  140 THR B O   
1034 C CB  . THR A 142 ? 1.8824 0.9661 0.8748 -0.1726 -0.0342 0.2067  140 THR B CB  
1035 O OG1 . THR A 142 ? 1.8755 0.9332 0.8788 -0.1520 -0.0530 0.1904  140 THR B OG1 
1036 C CG2 . THR A 142 ? 1.6915 0.8178 0.7112 -0.1657 -0.0043 0.1936  140 THR B CG2 
1037 N N   . ALA A 143 ? 1.7669 0.9313 0.7380 -0.1849 0.0146  0.2091  141 ALA B N   
1038 C CA  . ALA A 143 ? 1.7022 0.9089 0.6707 -0.1954 0.0403  0.2129  141 ALA B CA  
1039 C C   . ALA A 143 ? 1.6135 0.8514 0.6134 -0.1796 0.0640  0.1931  141 ALA B C   
1040 O O   . ALA A 143 ? 1.5777 0.8063 0.5981 -0.1600 0.0615  0.1753  141 ALA B O   
1041 C CB  . ALA A 143 ? 1.6961 0.9132 0.6412 -0.1985 0.0423  0.2153  141 ALA B CB  
1042 N N   . ALA A 144 ? 1.5729 0.8488 0.5753 -0.1882 0.0869  0.1960  142 ALA B N   
1043 C CA  . ALA A 144 ? 1.4906 0.7965 0.5203 -0.1751 0.1099  0.1797  142 ALA B CA  
1044 C C   . ALA A 144 ? 1.5096 0.8545 0.5343 -0.1766 0.1319  0.1757  142 ALA B C   
1045 O O   . ALA A 144 ? 1.4892 0.8602 0.5069 -0.1928 0.1377  0.1876  142 ALA B O   
1046 C CB  . ALA A 144 ? 1.4762 0.7898 0.5203 -0.1820 0.1155  0.1856  142 ALA B CB  
1047 N N   . LEU A 145 ? 1.4930 0.8484 0.5310 -0.1583 0.1428  0.1563  143 LEU B N   
1048 C CA  . LEU A 145 ? 1.4443 0.8363 0.4827 -0.1558 0.1646  0.1484  143 LEU B CA  
1049 C C   . LEU A 145 ? 1.4102 0.8174 0.4766 -0.1386 0.1824  0.1303  143 LEU B C   
1050 O O   . LEU A 145 ? 1.3955 0.7830 0.4795 -0.1259 0.1770  0.1207  143 LEU B O   
1051 C CB  . LEU A 145 ? 1.4566 0.8464 0.4808 -0.1507 0.1608  0.1417  143 LEU B CB  
1052 C CG  . LEU A 145 ? 1.4869 0.8506 0.5231 -0.1323 0.1500  0.1257  143 LEU B CG  
1053 C CD1 . LEU A 145 ? 1.5708 0.9526 0.6093 -0.1209 0.1626  0.1090  143 LEU B CD1 
1054 C CD2 . LEU A 145 ? 1.5210 0.8494 0.5387 -0.1369 0.1232  0.1354  143 LEU B CD2 
1055 N N   . GLY A 146 ? 1.4035 0.8460 0.4735 -0.1379 0.2036  0.1253  144 GLY B N   
1056 C CA  . GLY A 146 ? 1.3672 0.8229 0.4614 -0.1224 0.2204  0.1098  144 GLY B CA  
1057 C C   . GLY A 146 ? 1.3375 0.8333 0.4441 -0.1162 0.2372  0.0986  144 GLY B C   
1058 O O   . GLY A 146 ? 1.3496 0.8692 0.4487 -0.1251 0.2369  0.1037  144 GLY B O   
1059 N N   . CYS A 147 ? 1.3180 0.8214 0.4456 -0.1000 0.2506  0.0827  145 CYS B N   
1060 C CA  . CYS A 147 ? 1.3221 0.8638 0.4686 -0.0916 0.2654  0.0706  145 CYS B CA  
1061 C C   . CYS A 147 ? 1.2711 0.8410 0.4407 -0.0899 0.2741  0.0715  145 CYS B C   
1062 O O   . CYS A 147 ? 1.2622 0.8166 0.4394 -0.0871 0.2729  0.0734  145 CYS B O   
1063 C CB  . CYS A 147 ? 1.2952 0.8254 0.4510 -0.0740 0.2731  0.0513  145 CYS B CB  
1064 S SG  . CYS A 147 ? 1.3317 0.8545 0.4685 -0.0726 0.2700  0.0430  145 CYS B SG  
1065 N N   . LEU A 148 ? 1.2645 0.8762 0.4445 -0.0904 0.2825  0.0692  146 LEU B N   
1066 C CA  . LEU A 148 ? 1.2451 0.8857 0.4470 -0.0857 0.2913  0.0670  146 LEU B CA  
1067 C C   . LEU A 148 ? 1.2354 0.8923 0.4560 -0.0681 0.3028  0.0490  146 LEU B C   
1068 O O   . LEU A 148 ? 1.2283 0.9087 0.4482 -0.0667 0.3069  0.0430  146 LEU B O   
1069 C CB  . LEU A 148 ? 1.2549 0.9321 0.4542 -0.1006 0.2909  0.0791  146 LEU B CB  
1070 C CG  . LEU A 148 ? 1.2396 0.9456 0.4573 -0.0988 0.2976  0.0797  146 LEU B CG  
1071 C CD1 . LEU A 148 ? 1.2221 0.9626 0.4578 -0.0846 0.3096  0.0653  146 LEU B CD1 
1072 C CD2 . LEU A 148 ? 1.2284 0.9037 0.4535 -0.0922 0.2956  0.0790  146 LEU B CD2 
1073 N N   . VAL A 149 ? 1.2611 0.9038 0.4980 -0.0546 0.3070  0.0404  147 VAL B N   
1074 C CA  . VAL A 149 ? 1.2343 0.8859 0.4896 -0.0380 0.3159  0.0240  147 VAL B CA  
1075 C C   . VAL A 149 ? 1.2436 0.9289 0.5162 -0.0329 0.3228  0.0224  147 VAL B C   
1076 O O   . VAL A 149 ? 1.2207 0.8993 0.5029 -0.0291 0.3232  0.0246  147 VAL B O   
1077 C CB  . VAL A 149 ? 1.1801 0.7954 0.4422 -0.0267 0.3157  0.0157  147 VAL B CB  
1078 C CG1 . VAL A 149 ? 1.1713 0.7945 0.4522 -0.0115 0.3235  0.0004  147 VAL B CG1 
1079 C CG2 . VAL A 149 ? 1.1944 0.7788 0.4378 -0.0313 0.3088  0.0160  147 VAL B CG2 
1080 N N   . LYS A 150 ? 1.2357 0.9580 0.5119 -0.0320 0.3280  0.0177  148 LYS B N   
1081 C CA  . LYS A 150 ? 1.2295 0.9894 0.5176 -0.0297 0.3334  0.0174  148 LYS B CA  
1082 C C   . LYS A 150 ? 1.2702 1.0489 0.5740 -0.0136 0.3409  0.0015  148 LYS B C   
1083 O O   . LYS A 150 ? 1.2793 1.0577 0.5821 -0.0085 0.3426  -0.0080 148 LYS B O   
1084 C CB  . LYS A 150 ? 1.2051 1.0003 0.4823 -0.0451 0.3324  0.0278  148 LYS B CB  
1085 C CG  . LYS A 150 ? 1.1883 1.0197 0.4753 -0.0465 0.3364  0.0311  148 LYS B CG  
1086 C CD  . LYS A 150 ? 1.1942 1.0595 0.4699 -0.0631 0.3352  0.0425  148 LYS B CD  
1087 C CE  . LYS A 150 ? 1.1901 1.0908 0.4745 -0.0661 0.3390  0.0468  148 LYS B CE  
1088 N NZ  . LYS A 150 ? 1.2136 1.1408 0.5157 -0.0485 0.3471  0.0316  148 LYS B NZ  
1089 N N   . ASP A 151 ? 1.2351 1.0302 0.5527 -0.0057 0.3448  -0.0013 149 ASP B N   
1090 C CA  . ASP A 151 ? 1.2361 1.0549 0.5674 0.0086  0.3511  -0.0150 149 ASP B CA  
1091 C C   . ASP A 151 ? 1.2803 1.0704 0.6186 0.0221  0.3522  -0.0273 149 ASP B C   
1092 O O   . ASP A 151 ? 1.3126 1.1122 0.6514 0.0268  0.3545  -0.0373 149 ASP B O   
1093 C CB  . ASP A 151 ? 1.1999 1.0641 0.5267 0.0036  0.3543  -0.0174 149 ASP B CB  
1094 C CG  . ASP A 151 ? 1.2368 1.1401 0.5654 -0.0027 0.3563  -0.0109 149 ASP B CG  
1095 O OD1 . ASP A 151 ? 1.2019 1.0945 0.5315 -0.0075 0.3540  -0.0014 149 ASP B OD1 
1096 O OD2 . ASP A 151 ? 1.3021 1.2485 0.6303 -0.0035 0.3601  -0.0151 149 ASP B OD2 
1097 N N   . TYR A 152 ? 1.2716 1.0271 0.6158 0.0278  0.3503  -0.0261 150 TYR B N   
1098 C CA  . TYR A 152 ? 1.3063 1.0342 0.6591 0.0402  0.3514  -0.0364 150 TYR B CA  
1099 C C   . TYR A 152 ? 1.3125 1.0330 0.6780 0.0517  0.3530  -0.0381 150 TYR B C   
1100 O O   . TYR A 152 ? 1.2837 1.0105 0.6502 0.0491  0.3522  -0.0302 150 TYR B O   
1101 C CB  . TYR A 152 ? 1.2908 0.9808 0.6368 0.0355  0.3470  -0.0339 150 TYR B CB  
1102 C CG  . TYR A 152 ? 1.2605 0.9266 0.6044 0.0312  0.3430  -0.0241 150 TYR B CG  
1103 C CD1 . TYR A 152 ? 1.2599 0.9022 0.6142 0.0403  0.3432  -0.0264 150 TYR B CD1 
1104 C CD2 . TYR A 152 ? 1.2534 0.9207 0.5839 0.0176  0.3387  -0.0123 150 TYR B CD2 
1105 C CE1 . TYR A 152 ? 1.2752 0.8973 0.6275 0.0368  0.3395  -0.0184 150 TYR B CE1 
1106 C CE2 . TYR A 152 ? 1.2546 0.8996 0.5825 0.0138  0.3345  -0.0041 150 TYR B CE2 
1107 C CZ  . TYR A 152 ? 1.2458 0.8694 0.5851 0.0239  0.3352  -0.0078 150 TYR B CZ  
1108 O OH  . TYR A 152 ? 1.2338 0.8370 0.5703 0.0206  0.3312  -0.0006 150 TYR B OH  
1109 N N   . PHE A 153 ? 1.3543 1.0613 0.7285 0.0643  0.3552  -0.0483 151 PHE B N   
1110 C CA  . PHE A 153 ? 1.3486 1.0445 0.7332 0.0764  0.3566  -0.0506 151 PHE B CA  
1111 C C   . PHE A 153 ? 1.3747 1.0398 0.7637 0.0843  0.3569  -0.0582 151 PHE B C   
1112 O O   . PHE A 153 ? 1.3465 1.0140 0.7341 0.0848  0.3581  -0.0663 151 PHE B O   
1113 C CB  . PHE A 153 ? 1.3303 1.0592 0.7203 0.0850  0.3603  -0.0563 151 PHE B CB  
1114 C CG  . PHE A 153 ? 1.3228 1.0449 0.7203 0.0951  0.3607  -0.0549 151 PHE B CG  
1115 C CD1 . PHE A 153 ? 1.3013 1.0375 0.6991 0.0908  0.3598  -0.0465 151 PHE B CD1 
1116 C CD2 . PHE A 153 ? 1.3107 1.0112 0.7138 0.1084  0.3619  -0.0615 151 PHE B CD2 
1117 C CE1 . PHE A 153 ? 1.2714 1.0029 0.6758 0.1007  0.3601  -0.0457 151 PHE B CE1 
1118 C CE2 . PHE A 153 ? 1.2810 0.9746 0.6891 0.1180  0.3620  -0.0596 151 PHE B CE2 
1119 C CZ  . PHE A 153 ? 1.2932 1.0030 0.7023 0.1146  0.3611  -0.0520 151 PHE B CZ  
1120 N N   . PRO A 154 ? 1.5185 1.1554 0.9125 0.0895  0.3559  -0.0556 152 PRO B N   
1121 C CA  . PRO A 154 ? 1.5054 1.1329 0.9007 0.0877  0.3536  -0.0460 152 PRO B CA  
1122 C C   . PRO A 154 ? 1.4929 1.0955 0.8834 0.0780  0.3497  -0.0404 152 PRO B C   
1123 O O   . PRO A 154 ? 1.5050 1.0968 0.8918 0.0735  0.3488  -0.0443 152 PRO B O   
1124 C CB  . PRO A 154 ? 1.5043 1.1144 0.9068 0.1002  0.3551  -0.0485 152 PRO B CB  
1125 C CG  . PRO A 154 ? 1.5096 1.1004 0.9127 0.1029  0.3563  -0.0566 152 PRO B CG  
1126 C CD  . PRO A 154 ? 1.5119 1.1268 0.9113 0.0993  0.3576  -0.0630 152 PRO B CD  
1127 N N   . GLU A 155 ? 1.3288 0.9223 0.7194 0.0753  0.3471  -0.0323 153 GLU B N   
1128 C CA  . GLU A 155 ? 1.2574 0.8257 0.6435 0.0679  0.3432  -0.0287 153 GLU B CA  
1129 C C   . GLU A 155 ? 1.2363 0.7789 0.6269 0.0716  0.3435  -0.0356 153 GLU B C   
1130 O O   . GLU A 155 ? 1.2950 0.8343 0.6923 0.0803  0.3465  -0.0406 153 GLU B O   
1131 C CB  . GLU A 155 ? 1.1717 0.7330 0.5593 0.0675  0.3408  -0.0210 153 GLU B CB  
1132 C CG  . GLU A 155 ? 1.2026 0.7826 0.5824 0.0584  0.3388  -0.0128 153 GLU B CG  
1133 C CD  . GLU A 155 ? 1.2049 0.7691 0.5725 0.0468  0.3341  -0.0081 153 GLU B CD  
1134 O OE1 . GLU A 155 ? 1.2226 0.7861 0.5824 0.0415  0.3335  -0.0109 153 GLU B OE1 
1135 O OE2 . GLU A 155 ? 1.2236 0.7759 0.5880 0.0431  0.3306  -0.0020 153 GLU B OE2 
1136 N N   . PRO A 156 ? 1.1921 0.7164 0.5781 0.0647  0.3403  -0.0362 154 PRO B N   
1137 C CA  . PRO A 156 ? 1.2282 0.7490 0.6033 0.0548  0.3361  -0.0308 154 PRO B CA  
1138 C C   . PRO A 156 ? 1.2115 0.7371 0.5762 0.0477  0.3349  -0.0339 154 PRO B C   
1139 O O   . PRO A 156 ? 1.2322 0.7589 0.6001 0.0503  0.3370  -0.0421 154 PRO B O   
1140 C CB  . PRO A 156 ? 1.1005 0.5944 0.4784 0.0546  0.3332  -0.0317 154 PRO B CB  
1141 C CG  . PRO A 156 ? 1.1208 0.6056 0.5084 0.0599  0.3360  -0.0402 154 PRO B CG  
1142 C CD  . PRO A 156 ? 1.1289 0.6318 0.5202 0.0663  0.3405  -0.0428 154 PRO B CD  
1143 N N   . VAL A 157 ? 1.1981 0.7247 0.5487 0.0384  0.3311  -0.0273 155 VAL B N   
1144 C CA  . VAL A 157 ? 1.2402 0.7639 0.5777 0.0312  0.3286  -0.0295 155 VAL B CA  
1145 C C   . VAL A 157 ? 1.2507 0.7473 0.5782 0.0264  0.3229  -0.0279 155 VAL B C   
1146 O O   . VAL A 157 ? 1.2155 0.7020 0.5421 0.0257  0.3205  -0.0219 155 VAL B O   
1147 C CB  . VAL A 157 ? 1.2414 0.7899 0.5667 0.0231  0.3282  -0.0226 155 VAL B CB  
1148 C CG1 . VAL A 157 ? 1.2355 0.7865 0.5531 0.0158  0.3248  -0.0100 155 VAL B CG1 
1149 C CG2 . VAL A 157 ? 1.2760 0.8205 0.5862 0.0161  0.3252  -0.0246 155 VAL B CG2 
1150 N N   . THR A 158 ? 1.2639 0.7494 0.5840 0.0239  0.3205  -0.0345 156 THR B N   
1151 C CA  . THR A 158 ? 1.2705 0.7315 0.5774 0.0196  0.3141  -0.0348 156 THR B CA  
1152 C C   . THR A 158 ? 1.2991 0.7605 0.5827 0.0109  0.3095  -0.0315 156 THR B C   
1153 O O   . THR A 158 ? 1.3067 0.7838 0.5899 0.0103  0.3119  -0.0354 156 THR B O   
1154 C CB  . THR A 158 ? 1.2649 0.7120 0.5840 0.0245  0.3138  -0.0471 156 THR B CB  
1155 O OG1 . THR A 158 ? 1.2915 0.7335 0.5989 0.0209  0.3101  -0.0535 156 THR B OG1 
1156 C CG2 . THR A 158 ? 1.2922 0.7515 0.6322 0.0313  0.3201  -0.0530 156 THR B CG2 
1157 N N   . VAL A 159 ? 1.3133 0.7565 0.5761 0.0041  0.3022  -0.0240 157 VAL B N   
1158 C CA  . VAL A 159 ? 1.3132 0.7531 0.5495 -0.0055 0.2956  -0.0177 157 VAL B CA  
1159 C C   . VAL A 159 ? 1.3380 0.7479 0.5580 -0.0063 0.2856  -0.0216 157 VAL B C   
1160 O O   . VAL A 159 ? 1.3426 0.7396 0.5705 -0.0062 0.2760  -0.0178 157 VAL B O   
1161 C CB  . VAL A 159 ? 1.3087 0.7589 0.5327 -0.0160 0.2922  -0.0003 157 VAL B CB  
1162 C CG1 . VAL A 159 ? 1.3259 0.7697 0.5214 -0.0275 0.2833  0.0082  157 VAL B CG1 
1163 C CG2 . VAL A 159 ? 1.3067 0.7921 0.5489 -0.0145 0.3005  0.0010  157 VAL B CG2 
1164 N N   . SER A 160 ? 1.3653 0.7731 0.5777 -0.0067 0.2814  -0.0292 158 SER B N   
1165 C CA  . SER A 160 ? 1.3645 0.7548 0.5769 -0.0066 0.2645  -0.0340 158 SER B CA  
1166 C C   . SER A 160 ? 1.4401 0.8314 0.6345 -0.0158 0.2506  -0.0236 158 SER B C   
1167 O O   . SER A 160 ? 1.4331 0.8404 0.6153 -0.0200 0.2573  -0.0209 158 SER B O   
1168 C CB  . SER A 160 ? 1.4194 0.8057 0.6388 0.0016  0.2704  -0.0540 158 SER B CB  
1169 O OG  . SER A 160 ? 1.4554 0.8344 0.6680 0.0004  0.2557  -0.0588 158 SER B OG  
1170 N N   . TRP A 161 ? 1.4746 0.8485 0.6664 -0.0187 0.2305  -0.0181 159 TRP B N   
1171 C CA  . TRP A 161 ? 1.4716 0.8413 0.6444 -0.0275 0.2147  -0.0072 159 TRP B CA  
1172 C C   . TRP A 161 ? 1.5324 0.8919 0.7030 -0.0216 0.2040  -0.0206 159 TRP B C   
1173 O O   . TRP A 161 ? 1.5294 0.8742 0.7119 -0.0144 0.1947  -0.0308 159 TRP B O   
1174 C CB  . TRP A 161 ? 1.4045 0.7599 0.5729 -0.0355 0.1980  0.0095  159 TRP B CB  
1175 C CG  . TRP A 161 ? 1.3585 0.7292 0.5214 -0.0454 0.2070  0.0253  159 TRP B CG  
1176 C CD1 . TRP A 161 ? 1.3451 0.7206 0.5205 -0.0449 0.2151  0.0291  159 TRP B CD1 
1177 C CD2 . TRP A 161 ? 1.3459 0.7324 0.4897 -0.0574 0.2097  0.0382  159 TRP B CD2 
1178 N NE1 . TRP A 161 ? 1.3271 0.7208 0.4931 -0.0557 0.2222  0.0431  159 TRP B NE1 
1179 C CE2 . TRP A 161 ? 1.2950 0.6964 0.4417 -0.0639 0.2194  0.0489  159 TRP B CE2 
1180 C CE3 . TRP A 161 ? 1.3525 0.7436 0.4768 -0.0634 0.2047  0.0414  159 TRP B CE3 
1181 C CZ2 . TRP A 161 ? 1.3083 0.7304 0.4399 -0.0767 0.2248  0.0619  159 TRP B CZ2 
1182 C CZ3 . TRP A 161 ? 1.3439 0.7545 0.4521 -0.0764 0.2101  0.0553  159 TRP B CZ3 
1183 C CH2 . TRP A 161 ? 1.3387 0.7653 0.4509 -0.0832 0.2202  0.0652  159 TRP B CH2 
1184 N N   . ASN A 162 ? 1.5026 0.8726 0.6585 -0.0245 0.2055  -0.0216 160 ASN B N   
1185 C CA  . ASN A 162 ? 1.5172 0.8811 0.6685 -0.0195 0.1954  -0.0340 160 ASN B CA  
1186 C C   . ASN A 162 ? 1.5398 0.9016 0.7110 -0.0079 0.2025  -0.0562 160 ASN B C   
1187 O O   . ASN A 162 ? 1.5617 0.9111 0.7381 -0.0021 0.1890  -0.0668 160 ASN B O   
1188 C CB  . ASN A 162 ? 1.5355 0.8785 0.6751 -0.0226 0.1692  -0.0249 160 ASN B CB  
1189 C CG  . ASN A 162 ? 1.5875 0.9329 0.7016 -0.0352 0.1614  -0.0053 160 ASN B CG  
1190 O OD1 . ASN A 162 ? 1.5734 0.9384 0.6806 -0.0425 0.1760  0.0029  160 ASN B OD1 
1191 N ND2 . ASN A 162 ? 1.5898 0.9154 0.6893 -0.0378 0.1380  0.0024  160 ASN B ND2 
1192 N N   . SER A 163 ? 1.5340 0.9084 0.7158 -0.0048 0.2240  -0.0637 161 SER B N   
1193 C CA  . SER A 163 ? 1.5642 0.9380 0.7627 0.0041  0.2339  -0.0844 161 SER B CA  
1194 C C   . SER A 163 ? 1.6252 0.9837 0.8388 0.0089  0.2245  -0.0898 161 SER B C   
1195 O O   . SER A 163 ? 1.6294 0.9839 0.8528 0.0149  0.2216  -0.1070 161 SER B O   
1196 C CB  . SER A 163 ? 1.5629 0.9419 0.7566 0.0070  0.2323  -0.0994 161 SER B CB  
1197 O OG  . SER A 163 ? 1.6244 0.9914 0.8147 0.0087  0.2108  -0.1020 161 SER B OG  
1198 N N   . GLY A 164 ? 1.8189 1.1707 1.0349 0.0061  0.2201  -0.0760 162 GLY B N   
1199 C CA  . GLY A 164 ? 1.8095 1.1485 1.0397 0.0106  0.2111  -0.0803 162 GLY B CA  
1200 C C   . GLY A 164 ? 1.8226 1.1471 1.0488 0.0114  0.1861  -0.0799 162 GLY B C   
1201 O O   . GLY A 164 ? 1.8205 1.1348 1.0584 0.0155  0.1763  -0.0835 162 GLY B O   
1202 N N   . ALA A 165 ? 1.6241 0.9472 0.8336 0.0082  0.1746  -0.0757 163 ALA B N   
1203 C CA  . ALA A 165 ? 1.5991 0.9058 0.8028 0.0102  0.1492  -0.0752 163 ALA B CA  
1204 C C   . ALA A 165 ? 1.5812 0.8739 0.7743 0.0028  0.1344  -0.0538 163 ALA B C   
1205 O O   . ALA A 165 ? 1.6046 0.8796 0.7931 0.0048  0.1116  -0.0523 163 ALA B O   
1206 C CB  . ALA A 165 ? 1.6271 0.9364 0.8163 0.0108  0.1416  -0.0805 163 ALA B CB  
1207 N N   . LEU A 166 ? 1.5508 0.8505 0.7396 -0.0057 0.1460  -0.0378 164 LEU B N   
1208 C CA  . LEU A 166 ? 1.5045 0.7920 0.6837 -0.0146 0.1332  -0.0173 164 LEU B CA  
1209 C C   . LEU A 166 ? 1.4684 0.7575 0.6639 -0.0142 0.1418  -0.0143 164 LEU B C   
1210 O O   . LEU A 166 ? 1.4214 0.7248 0.6170 -0.0197 0.1582  -0.0057 164 LEU B O   
1211 C CB  . LEU A 166 ? 1.4794 0.7755 0.6369 -0.0272 0.1368  0.0006  164 LEU B CB  
1212 C CG  . LEU A 166 ? 1.4248 0.7075 0.5712 -0.0387 0.1232  0.0221  164 LEU B CG  
1213 C CD1 . LEU A 166 ? 1.4835 0.7381 0.6250 -0.0358 0.0957  0.0226  164 LEU B CD1 
1214 C CD2 . LEU A 166 ? 1.3919 0.6857 0.5158 -0.0529 0.1273  0.0398  164 LEU B CD2 
1215 N N   . THR A 167 ? 1.4556 0.7309 0.6646 -0.0073 0.1295  -0.0217 165 THR B N   
1216 C CA  . THR A 167 ? 1.3582 0.6352 0.5841 -0.0051 0.1366  -0.0216 165 THR B CA  
1217 C C   . THR A 167 ? 1.3325 0.5939 0.5555 -0.0111 0.1198  -0.0067 165 THR B C   
1218 O O   . THR A 167 ? 1.3931 0.6560 0.6296 -0.0096 0.1241  -0.0059 165 THR B O   
1219 C CB  . THR A 167 ? 1.3508 0.6278 0.5965 0.0070  0.1382  -0.0430 165 THR B CB  
1220 O OG1 . THR A 167 ? 1.3498 0.6111 0.5951 0.0124  0.1149  -0.0509 165 THR B OG1 
1221 C CG2 . THR A 167 ? 1.3902 0.6826 0.6394 0.0112  0.1570  -0.0571 165 THR B CG2 
1222 N N   . SER A 168 ? 1.3485 0.5938 0.5538 -0.0180 0.1004  0.0051  166 SER B N   
1223 C CA  . SER A 168 ? 1.3555 0.5829 0.5578 -0.0243 0.0833  0.0189  166 SER B CA  
1224 C C   . SER A 168 ? 1.3385 0.5700 0.5234 -0.0405 0.0871  0.0413  166 SER B C   
1225 O O   . SER A 168 ? 1.3807 0.6219 0.5493 -0.0474 0.0938  0.0477  166 SER B O   
1226 C CB  . SER A 168 ? 1.3409 0.5414 0.5360 -0.0203 0.0546  0.0167  166 SER B CB  
1227 O OG  . SER A 168 ? 1.3659 0.5657 0.5780 -0.0053 0.0504  -0.0055 166 SER B OG  
1228 N N   . GLY A 169 ? 1.3329 0.5583 0.5217 -0.0470 0.0826  0.0525  167 GLY B N   
1229 C CA  . GLY A 169 ? 1.3474 0.5777 0.5219 -0.0638 0.0855  0.0734  167 GLY B CA  
1230 C C   . GLY A 169 ? 1.3309 0.5924 0.5057 -0.0685 0.1118  0.0764  167 GLY B C   
1231 O O   . GLY A 169 ? 1.3453 0.6150 0.5058 -0.0833 0.1147  0.0929  167 GLY B O   
1232 N N   . VAL A 170 ? 1.3189 0.5983 0.5096 -0.0567 0.1308  0.0610  168 VAL B N   
1233 C CA  . VAL A 170 ? 1.2906 0.5984 0.4810 -0.0585 0.1550  0.0612  168 VAL B CA  
1234 C C   . VAL A 170 ? 1.2720 0.5933 0.4793 -0.0556 0.1688  0.0607  168 VAL B C   
1235 O O   . VAL A 170 ? 1.2781 0.5913 0.5022 -0.0459 0.1663  0.0513  168 VAL B O   
1236 C CB  . VAL A 170 ? 1.2952 0.6112 0.4885 -0.0476 0.1662  0.0444  168 VAL B CB  
1237 C CG1 . VAL A 170 ? 1.3352 0.6341 0.5413 -0.0349 0.1555  0.0281  168 VAL B CG1 
1238 C CG2 . VAL A 170 ? 1.2545 0.5950 0.4576 -0.0427 0.1914  0.0380  168 VAL B CG2 
1239 N N   . HIS A 171 ? 1.2636 0.6072 0.4664 -0.0636 0.1831  0.0701  169 HIS B N   
1240 C CA  . HIS A 171 ? 1.2433 0.6030 0.4606 -0.0605 0.1971  0.0699  169 HIS B CA  
1241 C C   . HIS A 171 ? 1.2337 0.6215 0.4490 -0.0590 0.2194  0.0673  169 HIS B C   
1242 O O   . HIS A 171 ? 1.2454 0.6501 0.4482 -0.0706 0.2237  0.0783  169 HIS B O   
1243 C CB  . HIS A 171 ? 1.2533 0.6119 0.4686 -0.0731 0.1885  0.0854  169 HIS B CB  
1244 C CG  . HIS A 171 ? 1.2796 0.6092 0.4953 -0.0754 0.1650  0.0888  169 HIS B CG  
1245 N ND1 . HIS A 171 ? 1.2937 0.6108 0.4948 -0.0912 0.1491  0.1049  169 HIS B ND1 
1246 C CD2 . HIS A 171 ? 1.2627 0.5732 0.4913 -0.0640 0.1544  0.0776  169 HIS B CD2 
1247 C CE1 . HIS A 171 ? 1.3026 0.5920 0.5074 -0.0883 0.1287  0.1033  169 HIS B CE1 
1248 N NE2 . HIS A 171 ? 1.3623 0.6488 0.5843 -0.0716 0.1316  0.0863  169 HIS B NE2 
1249 N N   . THR A 172 ? 1.2506 0.6437 0.4780 -0.0450 0.2334  0.0526  170 THR B N   
1250 C CA  . THR A 172 ? 1.2037 0.6213 0.4323 -0.0406 0.2544  0.0486  170 THR B CA  
1251 C C   . THR A 172 ? 1.1907 0.6212 0.4300 -0.0391 0.2624  0.0527  170 THR B C   
1252 O O   . THR A 172 ? 1.2280 0.6470 0.4800 -0.0333 0.2579  0.0499  170 THR B O   
1253 C CB  . THR A 172 ? 1.1901 0.6043 0.4264 -0.0265 0.2653  0.0314  170 THR B CB  
1254 O OG1 . THR A 172 ? 1.1980 0.5945 0.4302 -0.0253 0.2540  0.0246  170 THR B OG1 
1255 C CG2 . THR A 172 ? 1.2083 0.6446 0.4388 -0.0244 0.2828  0.0278  170 THR B CG2 
1256 N N   . PHE A 173 ? 1.1917 0.6475 0.4264 -0.0434 0.2741  0.0580  171 PHE B N   
1257 C CA  . PHE A 173 ? 1.1834 0.6538 0.4270 -0.0446 0.2784  0.0640  171 PHE B CA  
1258 C C   . PHE A 173 ? 1.1862 0.6772 0.4545 -0.0290 0.2907  0.0522  171 PHE B C   
1259 O O   . PHE A 173 ? 1.1832 0.6833 0.4598 -0.0204 0.2973  0.0418  171 PHE B O   
1260 C CB  . PHE A 173 ? 1.1935 0.6907 0.4333 -0.0597 0.2759  0.0763  171 PHE B CB  
1261 C CG  . PHE A 173 ? 1.2434 0.7223 0.4681 -0.0764 0.2606  0.0914  171 PHE B CG  
1262 C CD1 . PHE A 173 ? 1.2497 0.7172 0.4572 -0.0882 0.2488  0.0988  171 PHE B CD1 
1263 C CD2 . PHE A 173 ? 1.2311 0.7062 0.4658 -0.0791 0.2542  0.0969  171 PHE B CD2 
1264 C CE1 . PHE A 173 ? 1.2562 0.7070 0.4557 -0.1030 0.2307  0.1124  171 PHE B CE1 
1265 C CE2 . PHE A 173 ? 1.2474 0.7071 0.4755 -0.0941 0.2364  0.1096  171 PHE B CE2 
1266 C CZ  . PHE A 173 ? 1.2522 0.6983 0.4622 -0.1061 0.2244  0.1177  171 PHE B CZ  
1267 N N   . PRO A 174 ? 1.2411 0.7376 0.5214 -0.0247 0.2928  0.0536  172 PRO B N   
1268 C CA  . PRO A 174 ? 1.1738 0.6931 0.4762 -0.0112 0.3027  0.0448  172 PRO B CA  
1269 C C   . PRO A 174 ? 1.1454 0.7001 0.4528 -0.0136 0.3078  0.0449  172 PRO B C   
1270 O O   . PRO A 174 ? 1.1709 0.7424 0.4700 -0.0269 0.3049  0.0547  172 PRO B O   
1271 C CB  . PRO A 174 ? 1.1204 0.6420 0.4294 -0.0104 0.3019  0.0499  172 PRO B CB  
1272 C CG  . PRO A 174 ? 1.1369 0.6243 0.4300 -0.0171 0.2927  0.0554  172 PRO B CG  
1273 C CD  . PRO A 174 ? 1.1923 0.6720 0.4663 -0.0308 0.2856  0.0624  172 PRO B CD  
1274 N N   . ALA A 175 ? 1.1508 0.7165 0.4710 -0.0014 0.3148  0.0339  173 ALA B N   
1275 C CA  . ALA A 175 ? 1.1473 0.7482 0.4731 -0.0011 0.3201  0.0320  173 ALA B CA  
1276 C C   . ALA A 175 ? 1.1392 0.7677 0.4744 -0.0004 0.3229  0.0358  173 ALA B C   
1277 O O   . ALA A 175 ? 1.2293 0.8492 0.5715 0.0050  0.3226  0.0366  173 ALA B O   
1278 C CB  . ALA A 175 ? 1.1336 0.7362 0.4707 0.0126  0.3258  0.0191  173 ALA B CB  
1279 N N   . VAL A 176 ? 1.1124 0.7758 0.4474 -0.0059 0.3258  0.0375  174 VAL B N   
1280 C CA  . VAL A 176 ? 1.1420 0.8378 0.4850 -0.0061 0.3292  0.0400  174 VAL B CA  
1281 C C   . VAL A 176 ? 1.1993 0.9252 0.5533 0.0055  0.3363  0.0294  174 VAL B C   
1282 O O   . VAL A 176 ? 1.2422 0.9761 0.5929 0.0055  0.3380  0.0245  174 VAL B O   
1283 C CB  . VAL A 176 ? 1.1636 0.8774 0.4948 -0.0260 0.3256  0.0527  174 VAL B CB  
1284 C CG1 . VAL A 176 ? 1.1911 0.9349 0.5303 -0.0274 0.3286  0.0556  174 VAL B CG1 
1285 C CG2 . VAL A 176 ? 1.1319 0.8095 0.4488 -0.0378 0.3166  0.0627  174 VAL B CG2 
1286 N N   . LEU A 177 ? 1.1723 0.9138 0.5385 0.0162  0.3400  0.0252  175 LEU B N   
1287 C CA  . LEU A 177 ? 1.2174 0.9904 0.5924 0.0266  0.3458  0.0155  175 LEU B CA  
1288 C C   . LEU A 177 ? 1.2484 1.0655 0.6202 0.0153  0.3480  0.0195  175 LEU B C   
1289 O O   . LEU A 177 ? 1.2826 1.1104 0.6530 0.0061  0.3467  0.0278  175 LEU B O   
1290 C CB  . LEU A 177 ? 1.2594 1.0305 0.6473 0.0435  0.3482  0.0089  175 LEU B CB  
1291 C CG  . LEU A 177 ? 1.2906 1.0892 0.6868 0.0566  0.3534  -0.0026 175 LEU B CG  
1292 C CD1 . LEU A 177 ? 1.3008 1.0718 0.7017 0.0714  0.3540  -0.0115 175 LEU B CD1 
1293 C CD2 . LEU A 177 ? 1.2614 1.0865 0.6654 0.0629  0.3557  -0.0041 175 LEU B CD2 
1294 N N   . GLN A 178 ? 1.2852 1.1294 0.6563 0.0158  0.3515  0.0130  176 GLN B N   
1295 C CA  . GLN A 178 ? 1.2960 1.1858 0.6633 0.0042  0.3540  0.0162  176 GLN B CA  
1296 C C   . GLN A 178 ? 1.3000 1.2281 0.6787 0.0166  0.3600  0.0044  176 GLN B C   
1297 O O   . GLN A 178 ? 1.3057 1.2221 0.6937 0.0343  0.3618  -0.0065 176 GLN B O   
1298 C CB  . GLN A 178 ? 1.3048 1.2025 0.6614 -0.0054 0.3535  0.0176  176 GLN B CB  
1299 C CG  . GLN A 178 ? 1.3145 1.1850 0.6565 -0.0223 0.3469  0.0313  176 GLN B CG  
1300 C CD  . GLN A 178 ? 1.3358 1.1985 0.6684 -0.0251 0.3457  0.0291  176 GLN B CD  
1301 O OE1 . GLN A 178 ? 1.3499 1.2035 0.6681 -0.0407 0.3406  0.0399  176 GLN B OE1 
1302 N NE2 . GLN A 178 ? 1.3065 1.1703 0.6465 -0.0101 0.3497  0.0151  176 GLN B NE2 
1303 N N   . SER A 179 ? 1.2411 1.2151 0.6182 0.0069  0.3629  0.0067  177 SER B N   
1304 C CA  . SER A 179 ? 1.2556 1.2714 0.6427 0.0176  0.3686  -0.0061 177 SER B CA  
1305 C C   . SER A 179 ? 1.2585 1.2760 0.6495 0.0316  0.3712  -0.0214 177 SER B C   
1306 O O   . SER A 179 ? 1.2861 1.3083 0.6871 0.0479  0.3739  -0.0343 177 SER B O   
1307 C CB  . SER A 179 ? 1.2523 1.3214 0.6360 0.0040  0.3716  -0.0014 177 SER B CB  
1308 O OG  . SER A 179 ? 1.2522 1.3135 0.6231 -0.0148 0.3681  0.0156  177 SER B OG  
1309 N N   . SER A 180 ? 1.2566 1.2684 0.6394 0.0257  0.3702  -0.0201 178 SER B N   
1310 C CA  . SER A 180 ? 1.2388 1.2498 0.6248 0.0381  0.3725  -0.0345 178 SER B CA  
1311 C C   . SER A 180 ? 1.2419 1.2072 0.6346 0.0549  0.3709  -0.0405 178 SER B C   
1312 O O   . SER A 180 ? 1.2540 1.2177 0.6516 0.0683  0.3730  -0.0537 178 SER B O   
1313 C CB  . SER A 180 ? 1.2421 1.2522 0.6169 0.0276  0.3711  -0.0303 178 SER B CB  
1314 O OG  . SER A 180 ? 1.2525 1.2343 0.6172 0.0133  0.3660  -0.0141 178 SER B OG  
1315 N N   . GLY A 181 ? 1.2492 1.1783 0.6422 0.0546  0.3672  -0.0313 179 GLY B N   
1316 C CA  . GLY A 181 ? 1.2566 1.1419 0.6545 0.0685  0.3655  -0.0350 179 GLY B CA  
1317 C C   . GLY A 181 ? 1.2553 1.1053 0.6466 0.0644  0.3626  -0.0323 179 GLY B C   
1318 O O   . GLY A 181 ? 1.2286 1.0444 0.6236 0.0751  0.3618  -0.0366 179 GLY B O   
1319 N N   . LEU A 182 ? 1.3008 1.1581 0.6818 0.0488  0.3610  -0.0251 180 LEU B N   
1320 C CA  . LEU A 182 ? 1.2819 1.1088 0.6552 0.0439  0.3581  -0.0233 180 LEU B CA  
1321 C C   . LEU A 182 ? 1.2362 1.0342 0.6020 0.0326  0.3529  -0.0103 180 LEU B C   
1322 O O   . LEU A 182 ? 1.2086 1.0182 0.5713 0.0227  0.3513  -0.0004 180 LEU B O   
1323 C CB  . LEU A 182 ? 1.2669 1.1197 0.6317 0.0353  0.3593  -0.0251 180 LEU B CB  
1324 C CG  . LEU A 182 ? 1.2986 1.1764 0.6691 0.0462  0.3639  -0.0400 180 LEU B CG  
1325 C CD1 . LEU A 182 ? 1.3123 1.1516 0.6879 0.0591  0.3635  -0.0486 180 LEU B CD1 
1326 C CD2 . LEU A 182 ? 1.2561 1.1723 0.6354 0.0539  0.3681  -0.0472 180 LEU B CD2 
1327 N N   . TYR A 183 ? 1.2124 0.9733 0.5752 0.0339  0.3501  -0.0111 181 TYR B N   
1328 C CA  . TYR A 183 ? 1.2301 0.9595 0.5854 0.0252  0.3448  -0.0015 181 TYR B CA  
1329 C C   . TYR A 183 ? 1.2549 0.9850 0.5944 0.0098  0.3412  0.0054  181 TYR B C   
1330 O O   . TYR A 183 ? 1.2694 1.0085 0.6049 0.0096  0.3427  -0.0003 181 TYR B O   
1331 C CB  . TYR A 183 ? 1.2496 0.9401 0.6100 0.0353  0.3438  -0.0073 181 TYR B CB  
1332 C CG  . TYR A 183 ? 1.2629 0.9455 0.6358 0.0479  0.3454  -0.0100 181 TYR B CG  
1333 C CD1 . TYR A 183 ? 1.2756 0.9783 0.6529 0.0483  0.3462  -0.0054 181 TYR B CD1 
1334 C CD2 . TYR A 183 ? 1.2763 0.9345 0.6566 0.0594  0.3465  -0.0176 181 TYR B CD2 
1335 C CE1 . TYR A 183 ? 1.3504 1.0462 0.7380 0.0605  0.3474  -0.0079 181 TYR B CE1 
1336 C CE2 . TYR A 183 ? 1.3755 1.0258 0.7654 0.0706  0.3476  -0.0191 181 TYR B CE2 
1337 C CZ  . TYR A 183 ? 1.3514 1.0201 0.7446 0.0718  0.3479  -0.0144 181 TYR B CZ  
1338 O OH  . TYR A 183 ? 1.3216 0.9813 0.7232 0.0839  0.3488  -0.0160 181 TYR B OH  
1339 N N   . SER A 184 ? 1.2377 0.9587 0.5673 -0.0032 0.3361  0.0178  182 SER B N   
1340 C CA  . SER A 184 ? 1.2386 0.9492 0.5505 -0.0178 0.3306  0.0258  182 SER B CA  
1341 C C   . SER A 184 ? 1.1856 0.8606 0.4890 -0.0246 0.3234  0.0349  182 SER B C   
1342 O O   . SER A 184 ? 1.1705 0.8426 0.4793 -0.0245 0.3225  0.0396  182 SER B O   
1343 C CB  . SER A 184 ? 1.2432 0.9905 0.5464 -0.0322 0.3304  0.0341  182 SER B CB  
1344 O OG  . SER A 184 ? 1.2971 1.0743 0.6087 -0.0334 0.3335  0.0373  182 SER B OG  
1345 N N   . LEU A 185 ? 1.2022 0.8509 0.4914 -0.0300 0.3181  0.0365  183 LEU B N   
1346 C CA  . LEU A 185 ? 1.1869 0.7970 0.4655 -0.0342 0.3105  0.0421  183 LEU B CA  
1347 C C   . LEU A 185 ? 1.1917 0.7915 0.4478 -0.0491 0.3024  0.0511  183 LEU B C   
1348 O O   . LEU A 185 ? 1.1943 0.8078 0.4447 -0.0511 0.3040  0.0480  183 LEU B O   
1349 C CB  . LEU A 185 ? 1.1640 0.7467 0.4503 -0.0200 0.3127  0.0300  183 LEU B CB  
1350 C CG  . LEU A 185 ? 1.2074 0.7500 0.4813 -0.0215 0.3058  0.0307  183 LEU B CG  
1351 C CD1 . LEU A 185 ? 1.1896 0.7150 0.4784 -0.0077 0.3093  0.0213  183 LEU B CD1 
1352 C CD2 . LEU A 185 ? 1.2301 0.7632 0.4904 -0.0239 0.3037  0.0261  183 LEU B CD2 
1353 N N   . SER A 186 ? 1.2141 0.7887 0.4564 -0.0595 0.2928  0.0623  184 SER B N   
1354 C CA  . SER A 186 ? 1.2205 0.7793 0.4391 -0.0739 0.2823  0.0725  184 SER B CA  
1355 C C   . SER A 186 ? 1.2284 0.7415 0.4343 -0.0711 0.2739  0.0716  184 SER B C   
1356 O O   . SER A 186 ? 1.2214 0.7172 0.4341 -0.0650 0.2735  0.0700  184 SER B O   
1357 C CB  . SER A 186 ? 1.2348 0.8069 0.4458 -0.0922 0.2754  0.0891  184 SER B CB  
1358 O OG  . SER A 186 ? 1.2438 0.8536 0.4726 -0.0905 0.2844  0.0881  184 SER B OG  
1359 N N   . SER A 187 ? 1.2461 0.7409 0.4327 -0.0748 0.2673  0.0717  185 SER B N   
1360 C CA  . SER A 187 ? 1.2530 0.7090 0.4311 -0.0706 0.2566  0.0685  185 SER B CA  
1361 C C   . SER A 187 ? 1.2794 0.7216 0.4390 -0.0843 0.2385  0.0807  185 SER B C   
1362 O O   . SER A 187 ? 1.2937 0.7469 0.4378 -0.0905 0.2402  0.0830  185 SER B O   
1363 C CB  . SER A 187 ? 1.2422 0.6925 0.4263 -0.0560 0.2639  0.0507  185 SER B CB  
1364 O OG  . SER A 187 ? 1.2437 0.6664 0.4313 -0.0515 0.2493  0.0453  185 SER B OG  
1365 N N   . VAL A 188 ? 1.2874 0.7052 0.4481 -0.0889 0.2208  0.0883  186 VAL B N   
1366 C CA  . VAL A 188 ? 1.3169 0.7186 0.4583 -0.1033 0.2019  0.1026  186 VAL B CA  
1367 C C   . VAL A 188 ? 1.3222 0.6899 0.4665 -0.0961 0.1826  0.0972  186 VAL B C   
1368 O O   . VAL A 188 ? 1.3028 0.6608 0.4658 -0.0835 0.1827  0.0859  186 VAL B O   
1369 C CB  . VAL A 188 ? 1.3295 0.7346 0.4655 -0.1198 0.1966  0.1204  186 VAL B CB  
1370 C CG1 . VAL A 188 ? 1.3293 0.7708 0.4592 -0.1291 0.2137  0.1261  186 VAL B CG1 
1371 C CG2 . VAL A 188 ? 1.3125 0.7083 0.4682 -0.1135 0.1943  0.1178  186 VAL B CG2 
1372 N N   . VAL A 189 ? 1.3497 0.7000 0.4751 -0.1038 0.1656  0.1050  187 VAL B N   
1373 C CA  . VAL A 189 ? 1.3589 0.6769 0.4854 -0.0969 0.1446  0.1001  187 VAL B CA  
1374 C C   . VAL A 189 ? 1.3959 0.6926 0.4995 -0.1118 0.1231  0.1180  187 VAL B C   
1375 O O   . VAL A 189 ? 1.4166 0.7221 0.4990 -0.1232 0.1241  0.1281  187 VAL B O   
1376 C CB  . VAL A 189 ? 1.3513 0.6677 0.4807 -0.0829 0.1465  0.0823  187 VAL B CB  
1377 C CG1 . VAL A 189 ? 1.3652 0.6975 0.4757 -0.0889 0.1531  0.0851  187 VAL B CG1 
1378 C CG2 . VAL A 189 ? 1.3631 0.6485 0.4929 -0.0758 0.1233  0.0767  187 VAL B CG2 
1379 N N   . THR A 190 ? 1.4062 0.6747 0.5130 -0.1122 0.1036  0.1222  188 THR B N   
1380 C CA  . THR A 190 ? 1.4452 0.6852 0.5297 -0.1240 0.0795  0.1376  188 THR B CA  
1381 C C   . THR A 190 ? 1.4576 0.6755 0.5361 -0.1124 0.0630  0.1274  188 THR B C   
1382 O O   . THR A 190 ? 1.4368 0.6507 0.5341 -0.0951 0.0623  0.1087  188 THR B O   
1383 C CB  . THR A 190 ? 1.4553 0.6724 0.5445 -0.1300 0.0638  0.1468  188 THR B CB  
1384 O OG1 . THR A 190 ? 1.4718 0.6858 0.5879 -0.1136 0.0649  0.1305  188 THR B OG1 
1385 C CG2 . THR A 190 ? 1.4623 0.6950 0.5449 -0.1495 0.0725  0.1646  188 THR B CG2 
1386 N N   . VAL A 191 ? 1.4927 0.6972 0.5445 -0.1221 0.0493  0.1395  189 VAL B N   
1387 C CA  . VAL A 191 ? 1.5160 0.7042 0.5615 -0.1100 0.0352  0.1285  189 VAL B CA  
1388 C C   . VAL A 191 ? 1.6291 0.7848 0.6461 -0.1213 0.0090  0.1463  189 VAL B C   
1389 O O   . VAL A 191 ? 1.6874 0.8403 0.6877 -0.1407 0.0073  0.1672  189 VAL B O   
1390 C CB  . VAL A 191 ? 1.5811 0.7978 0.6243 -0.1052 0.0537  0.1183  189 VAL B CB  
1391 C CG1 . VAL A 191 ? 1.6134 0.8373 0.6258 -0.1216 0.0535  0.1355  189 VAL B CG1 
1392 C CG2 . VAL A 191 ? 1.5810 0.7945 0.6378 -0.0850 0.0509  0.0947  189 VAL B CG2 
1393 N N   . PRO A 192 ? 1.6058 0.7356 0.6159 -0.1104 -0.0126 0.1390  190 PRO B N   
1394 C CA  . PRO A 192 ? 1.7145 0.8116 0.6943 -0.1208 -0.0381 0.1568  190 PRO B CA  
1395 C C   . PRO A 192 ? 1.8010 0.9122 0.7521 -0.1385 -0.0304 0.1741  190 PRO B C   
1396 O O   . PRO A 192 ? 1.8504 0.9877 0.7999 -0.1342 -0.0156 0.1656  190 PRO B O   
1397 C CB  . PRO A 192 ? 1.7522 0.8299 0.7332 -0.1014 -0.0571 0.1399  190 PRO B CB  
1398 C CG  . PRO A 192 ? 1.5914 0.6779 0.6065 -0.0843 -0.0499 0.1179  190 PRO B CG  
1399 C CD  . PRO A 192 ? 1.5693 0.6955 0.5992 -0.0881 -0.0174 0.1144  190 PRO B CD  
1400 N N   . SER A 193 ? 1.8543 0.9484 0.7822 -0.1592 -0.0408 0.1984  191 SER B N   
1401 C CA  . SER A 193 ? 1.8731 0.9765 0.7694 -0.1779 -0.0375 0.2168  191 SER B CA  
1402 C C   . SER A 193 ? 1.9524 1.0392 0.8260 -0.1709 -0.0542 0.2152  191 SER B C   
1403 O O   . SER A 193 ? 1.9393 1.0419 0.7898 -0.1817 -0.0476 0.2246  191 SER B O   
1404 C CB  . SER A 193 ? 1.9221 1.0056 0.7967 -0.2025 -0.0482 0.2435  191 SER B CB  
1405 O OG  . SER A 193 ? 1.9728 1.0935 0.8603 -0.2167 -0.0247 0.2492  191 SER B OG  
1406 N N   . SER A 194 ? 1.9534 1.0095 0.8324 -0.1531 -0.0763 0.2032  192 SER B N   
1407 C CA  . SER A 194 ? 1.9809 1.0244 0.8420 -0.1427 -0.0917 0.1975  192 SER B CA  
1408 C C   . SER A 194 ? 2.0117 1.0952 0.8844 -0.1322 -0.0693 0.1790  192 SER B C   
1409 O O   . SER A 194 ? 2.0258 1.1235 0.8763 -0.1394 -0.0644 0.1856  192 SER B O   
1410 C CB  . SER A 194 ? 1.9613 0.9698 0.8321 -0.1229 -0.1180 0.1837  192 SER B CB  
1411 O OG  . SER A 194 ? 1.9602 0.9890 0.8532 -0.1011 -0.1099 0.1563  192 SER B OG  
1412 N N   . SER A 195 ? 2.2509 1.3524 1.1579 -0.1152 -0.0556 0.1555  193 SER B N   
1413 C CA  . SER A 195 ? 2.2298 1.3659 1.1515 -0.1035 -0.0349 0.1350  193 SER B CA  
1414 C C   . SER A 195 ? 2.2002 1.3749 1.1192 -0.1165 -0.0070 0.1415  193 SER B C   
1415 O O   . SER A 195 ? 2.1768 1.3802 1.1069 -0.1077 0.0110  0.1250  193 SER B O   
1416 C CB  . SER A 195 ? 2.2042 1.3478 1.1627 -0.0849 -0.0269 0.1104  193 SER B CB  
1417 O OG  . SER A 195 ? 2.2287 1.3582 1.1918 -0.0667 -0.0435 0.0922  193 SER B OG  
1418 N N   . LEU A 196 ? 2.0069 1.1837 0.9118 -0.1371 -0.0030 0.1638  194 LEU B N   
1419 C CA  . LEU A 196 ? 1.9282 1.1447 0.8309 -0.1491 0.0232  0.1689  194 LEU B CA  
1420 C C   . LEU A 196 ? 1.8942 1.1295 0.7786 -0.1487 0.0280  0.1656  194 LEU B C   
1421 O O   . LEU A 196 ? 1.9406 1.2112 0.8368 -0.1439 0.0507  0.1527  194 LEU B O   
1422 C CB  . LEU A 196 ? 1.8727 1.0870 0.7584 -0.1731 0.0227  0.1945  194 LEU B CB  
1423 C CG  . LEU A 196 ? 1.7584 0.9930 0.6675 -0.1777 0.0417  0.1943  194 LEU B CG  
1424 C CD1 . LEU A 196 ? 1.7593 1.0099 0.6491 -0.2031 0.0492  0.2168  194 LEU B CD1 
1425 C CD2 . LEU A 196 ? 1.6906 0.9603 0.6276 -0.1626 0.0672  0.1721  194 LEU B CD2 
1426 N N   . GLY A 197 ? 1.9145 1.1256 0.7699 -0.1527 0.0060  0.1763  195 GLY B N   
1427 C CA  . GLY A 197 ? 1.9681 1.1970 0.8024 -0.1545 0.0091  0.1759  195 GLY B CA  
1428 C C   . GLY A 197 ? 1.9354 1.1753 0.7842 -0.1329 0.0125  0.1497  195 GLY B C   
1429 O O   . GLY A 197 ? 1.8794 1.1510 0.7253 -0.1323 0.0285  0.1420  195 GLY B O   
1430 N N   . THR A 198 ? 1.9240 1.1395 0.7889 -0.1154 -0.0024 0.1348  196 THR B N   
1431 C CA  . THR A 198 ? 1.9046 1.1266 0.7802 -0.0960 -0.0038 0.1105  196 THR B CA  
1432 C C   . THR A 198 ? 1.9160 1.1598 0.8289 -0.0822 0.0171  0.0861  196 THR B C   
1433 O O   . THR A 198 ? 1.9005 1.1578 0.8242 -0.0684 0.0222  0.0647  196 THR B O   
1434 C CB  . THR A 198 ? 1.9541 1.1374 0.8227 -0.0845 -0.0349 0.1074  196 THR B CB  
1435 O OG1 . THR A 198 ? 2.0000 1.1536 0.8356 -0.0991 -0.0560 0.1339  196 THR B OG1 
1436 C CG2 . THR A 198 ? 1.9483 1.1390 0.8136 -0.0695 -0.0406 0.0887  196 THR B CG2 
1437 N N   . GLN A 199 ? 1.9141 1.1617 0.8462 -0.0859 0.0292  0.0888  197 GLN B N   
1438 C CA  . GLN A 199 ? 1.8654 1.1280 0.8316 -0.0731 0.0467  0.0675  197 GLN B CA  
1439 C C   . GLN A 199 ? 1.8202 1.1159 0.7947 -0.0810 0.0751  0.0695  197 GLN B C   
1440 O O   . GLN A 199 ? 1.8111 1.1088 0.7815 -0.0944 0.0797  0.0868  197 GLN B O   
1441 C CB  . GLN A 199 ? 1.8745 1.1126 0.8584 -0.0676 0.0355  0.0660  197 GLN B CB  
1442 C CG  . GLN A 199 ? 1.8196 1.0745 0.8358 -0.0585 0.0557  0.0491  197 GLN B CG  
1443 C CD  . GLN A 199 ? 1.8268 1.0760 0.8629 -0.0402 0.0501  0.0245  197 GLN B CD  
1444 O OE1 . GLN A 199 ? 1.8821 1.1148 0.9088 -0.0331 0.0296  0.0192  197 GLN B OE1 
1445 N NE2 . GLN A 199 ? 1.8134 1.0765 0.8765 -0.0326 0.0678  0.0090  197 GLN B NE2 
1446 N N   . THR A 200 ? 1.8235 1.1451 0.8103 -0.0724 0.0936  0.0511  198 THR B N   
1447 C CA  . THR A 200 ? 1.7616 1.1146 0.7579 -0.0767 0.1202  0.0495  198 THR B CA  
1448 C C   . THR A 200 ? 1.7084 1.0606 0.7325 -0.0707 0.1314  0.0423  198 THR B C   
1449 O O   . THR A 200 ? 1.7135 1.0504 0.7553 -0.0586 0.1253  0.0285  198 THR B O   
1450 C CB  . THR A 200 ? 1.7372 1.1146 0.7365 -0.0687 0.1343  0.0311  198 THR B CB  
1451 O OG1 . THR A 200 ? 1.7477 1.1241 0.7742 -0.0536 0.1420  0.0086  198 THR B OG1 
1452 C CG2 . THR A 200 ? 1.7453 1.1162 0.7221 -0.0680 0.1177  0.0311  198 THR B CG2 
1453 N N   . TYR A 201 ? 1.6731 1.0439 0.7010 -0.0790 0.1482  0.0511  199 TYR B N   
1454 C CA  . TYR A 201 ? 1.6438 1.0161 0.6961 -0.0741 0.1598  0.0462  199 TYR B CA  
1455 C C   . TYR A 201 ? 1.5985 1.0022 0.6609 -0.0716 0.1860  0.0373  199 TYR B C   
1456 O O   . TYR A 201 ? 1.5877 1.0136 0.6373 -0.0820 0.1953  0.0474  199 TYR B O   
1457 C CB  . TYR A 201 ? 1.6514 1.0122 0.6986 -0.0865 0.1514  0.0667  199 TYR B CB  
1458 C CG  . TYR A 201 ? 1.7306 1.0565 0.7696 -0.0870 0.1244  0.0738  199 TYR B CG  
1459 C CD1 . TYR A 201 ? 1.7515 1.0633 0.7675 -0.1026 0.1091  0.0961  199 TYR B CD1 
1460 C CD2 . TYR A 201 ? 1.7427 1.0493 0.7978 -0.0723 0.1142  0.0581  199 TYR B CD2 
1461 C CE1 . TYR A 201 ? 1.7618 1.0386 0.7693 -0.1024 0.0831  0.1024  199 TYR B CE1 
1462 C CE2 . TYR A 201 ? 1.7506 1.0253 0.7989 -0.0713 0.0884  0.0633  199 TYR B CE2 
1463 C CZ  . TYR A 201 ? 1.7591 1.0177 0.7833 -0.0858 0.0724  0.0855  199 TYR B CZ  
1464 O OH  . TYR A 201 ? 1.8103 1.0345 0.8271 -0.0838 0.0455  0.0901  199 TYR B OH  
1465 N N   . ILE A 202 ? 1.5527 0.9585 0.6372 -0.0581 0.1975  0.0182  200 ILE B N   
1466 C CA  . ILE A 202 ? 1.4899 0.9205 0.5854 -0.0535 0.2214  0.0081  200 ILE B CA  
1467 C C   . ILE A 202 ? 1.4527 0.8779 0.5699 -0.0474 0.2297  0.0045  200 ILE B C   
1468 O O   . ILE A 202 ? 1.4795 0.8847 0.6095 -0.0400 0.2216  -0.0029 200 ILE B O   
1469 C CB  . ILE A 202 ? 1.4870 0.9250 0.5872 -0.0431 0.2291  -0.0128 200 ILE B CB  
1470 C CG1 . ILE A 202 ? 1.5126 0.9276 0.6225 -0.0338 0.2162  -0.0256 200 ILE B CG1 
1471 C CG2 . ILE A 202 ? 1.4638 0.9168 0.5426 -0.0493 0.2269  -0.0097 200 ILE B CG2 
1472 C CD1 . ILE A 202 ? 1.4817 0.9025 0.6054 -0.0225 0.2281  -0.0490 200 ILE B CD1 
1473 N N   . CYS A 203 ? 1.4083 0.8528 0.5295 -0.0500 0.2455  0.0092  201 CYS B N   
1474 C CA  . CYS A 203 ? 1.3875 0.8301 0.5287 -0.0426 0.2560  0.0042  201 CYS B CA  
1475 C C   . CYS A 203 ? 1.4121 0.8676 0.5635 -0.0318 0.2751  -0.0134 201 CYS B C   
1476 O O   . CYS A 203 ? 1.3994 0.8827 0.5554 -0.0328 0.2817  -0.0153 201 CYS B O   
1477 C CB  . CYS A 203 ? 1.3520 0.8064 0.4921 -0.0513 0.2601  0.0200  201 CYS B CB  
1478 S SG  . CYS A 203 ? 1.2959 0.7943 0.4484 -0.0514 0.2774  0.0186  201 CYS B SG  
1479 N N   . ASN A 204 ? 1.4016 0.8435 0.5698 -0.0213 0.2788  -0.0266 202 ASN B N   
1480 C CA  . ASN A 204 ? 1.3723 0.8311 0.5688 -0.0115 0.2895  -0.0419 202 ASN B CA  
1481 C C   . ASN A 204 ? 1.3770 0.8477 0.5973 -0.0075 0.2972  -0.0387 202 ASN B C   
1482 O O   . ASN A 204 ? 1.3646 0.8188 0.5888 -0.0058 0.2957  -0.0356 202 ASN B O   
1483 C CB  . ASN A 204 ? 1.4134 0.8539 0.6181 -0.0040 0.2871  -0.0580 202 ASN B CB  
1484 C CG  . ASN A 204 ? 1.4368 0.8591 0.6159 -0.0072 0.2752  -0.0599 202 ASN B CG  
1485 O OD1 . ASN A 204 ? 1.4830 0.8883 0.6700 -0.0039 0.2644  -0.0655 202 ASN B OD1 
1486 N ND2 . ASN A 204 ? 1.4457 0.8799 0.6080 -0.0133 0.2714  -0.0543 202 ASN B ND2 
1487 N N   . VAL A 205 ? 1.3497 0.8494 0.5844 -0.0056 0.3047  -0.0398 203 VAL B N   
1488 C CA  . VAL A 205 ? 1.3184 0.8329 0.5737 -0.0009 0.3112  -0.0373 203 VAL B CA  
1489 C C   . VAL A 205 ? 1.3426 0.8609 0.6219 0.0096  0.3172  -0.0515 203 VAL B C   
1490 O O   . VAL A 205 ? 1.3591 0.8864 0.6404 0.0114  0.3187  -0.0609 203 VAL B O   
1491 C CB  . VAL A 205 ? 1.2995 0.8454 0.5515 -0.0066 0.3138  -0.0283 203 VAL B CB  
1492 C CG1 . VAL A 205 ? 1.2580 0.8227 0.5320 0.0008  0.3208  -0.0296 203 VAL B CG1 
1493 C CG2 . VAL A 205 ? 1.3063 0.8472 0.5370 -0.0191 0.3067  -0.0119 203 VAL B CG2 
1494 N N   . ASN A 206 ? 1.3517 0.8617 0.6483 0.0159  0.3198  -0.0527 204 ASN B N   
1495 C CA  . ASN A 206 ? 1.3466 0.8576 0.6652 0.0245  0.3244  -0.0633 204 ASN B CA  
1496 C C   . ASN A 206 ? 1.3236 0.8442 0.6557 0.0302  0.3290  -0.0590 204 ASN B C   
1497 O O   . ASN A 206 ? 1.3093 0.8203 0.6425 0.0303  0.3278  -0.0519 204 ASN B O   
1498 C CB  . ASN A 206 ? 1.3609 0.8484 0.6871 0.0263  0.3214  -0.0704 204 ASN B CB  
1499 C CG  . ASN A 206 ? 1.4052 0.8944 0.7514 0.0320  0.3251  -0.0811 204 ASN B CG  
1500 O OD1 . ASN A 206 ? 1.4517 0.9272 0.8076 0.0326  0.3232  -0.0870 204 ASN B OD1 
1501 N ND2 . ASN A 206 ? 1.3849 0.8919 0.7366 0.0358  0.3300  -0.0836 204 ASN B ND2 
1502 N N   . HIS A 207 ? 1.2919 0.8311 0.6334 0.0356  0.3340  -0.0641 205 HIS B N   
1503 C CA  . HIS A 207 ? 1.3012 0.8494 0.6548 0.0429  0.3381  -0.0623 205 HIS B CA  
1504 C C   . HIS A 207 ? 1.3098 0.8538 0.6772 0.0508  0.3415  -0.0727 205 HIS B C   
1505 O O   . HIS A 207 ? 1.2962 0.8571 0.6652 0.0540  0.3444  -0.0793 205 HIS B O   
1506 C CB  . HIS A 207 ? 1.2665 0.8448 0.6152 0.0418  0.3403  -0.0575 205 HIS B CB  
1507 C CG  . HIS A 207 ? 1.2512 0.8407 0.6110 0.0499  0.3440  -0.0564 205 HIS B CG  
1508 N ND1 . HIS A 207 ? 1.2577 0.8685 0.6235 0.0570  0.3482  -0.0632 205 HIS B ND1 
1509 C CD2 . HIS A 207 ? 1.2179 0.8000 0.5832 0.0529  0.3438  -0.0501 205 HIS B CD2 
1510 C CE1 . HIS A 207 ? 1.2843 0.9000 0.6579 0.0642  0.3503  -0.0609 205 HIS B CE1 
1511 N NE2 . HIS A 207 ? 1.2696 0.8684 0.6433 0.0617  0.3477  -0.0528 205 HIS B NE2 
1512 N N   . LYS A 208 ? 1.2936 0.8157 0.6702 0.0535  0.3411  -0.0738 206 LYS B N   
1513 C CA  . LYS A 208 ? 1.2812 0.7942 0.6688 0.0586  0.3437  -0.0821 206 LYS B CA  
1514 C C   . LYS A 208 ? 1.2315 0.7550 0.6245 0.0676  0.3484  -0.0841 206 LYS B C   
1515 O O   . LYS A 208 ? 1.2241 0.7491 0.6207 0.0709  0.3507  -0.0930 206 LYS B O   
1516 C CB  . LYS A 208 ? 1.2866 0.7759 0.6813 0.0578  0.3423  -0.0807 206 LYS B CB  
1517 C CG  . LYS A 208 ? 1.3279 0.8060 0.7319 0.0609  0.3451  -0.0879 206 LYS B CG  
1518 C CD  . LYS A 208 ? 1.3714 0.8556 0.7757 0.0586  0.3453  -0.0987 206 LYS B CD  
1519 C CE  . LYS A 208 ? 1.4081 0.8762 0.8209 0.0565  0.3461  -0.1054 206 LYS B CE  
1520 N NZ  . LYS A 208 ? 1.4432 0.9053 0.8575 0.0486  0.3414  -0.1081 206 LYS B NZ  
1521 N N   . PRO A 209 ? 1.2294 0.7601 0.6230 0.0723  0.3496  -0.0770 207 PRO B N   
1522 C CA  . PRO A 209 ? 1.2288 0.7698 0.6264 0.0822  0.3536  -0.0801 207 PRO B CA  
1523 C C   . PRO A 209 ? 1.3069 0.8679 0.7033 0.0849  0.3558  -0.0896 207 PRO B C   
1524 O O   . PRO A 209 ? 1.3503 0.9091 0.7508 0.0930  0.3586  -0.0966 207 PRO B O   
1525 C CB  . PRO A 209 ? 1.2500 0.8066 0.6460 0.0840  0.3535  -0.0715 207 PRO B CB  
1526 C CG  . PRO A 209 ? 1.2826 0.8217 0.6775 0.0781  0.3500  -0.0635 207 PRO B CG  
1527 C CD  . PRO A 209 ? 1.2436 0.7717 0.6345 0.0695  0.3472  -0.0666 207 PRO B CD  
1528 N N   . SER A 210 ? 1.2732 0.8532 0.6627 0.0784  0.3545  -0.0902 208 SER B N   
1529 C CA  . SER A 210 ? 1.2344 0.8363 0.6221 0.0801  0.3564  -0.0995 208 SER B CA  
1530 C C   . SER A 210 ? 1.2815 0.8758 0.6667 0.0741  0.3545  -0.1061 208 SER B C   
1531 O O   . SER A 210 ? 1.3099 0.9240 0.6918 0.0739  0.3554  -0.1134 208 SER B O   
1532 C CB  . SER A 210 ? 1.2933 0.9286 0.6740 0.0770  0.3569  -0.0953 208 SER B CB  
1533 O OG  . SER A 210 ? 1.3288 0.9611 0.7004 0.0663  0.3534  -0.0858 208 SER B OG  
1534 N N   . ASN A 211 ? 1.2798 0.8480 0.6671 0.0697  0.3520  -0.1045 209 ASN B N   
1535 C CA  . ASN A 211 ? 1.3115 0.8716 0.6973 0.0638  0.3495  -0.1110 209 ASN B CA  
1536 C C   . ASN A 211 ? 1.3085 0.8874 0.6820 0.0574  0.3474  -0.1099 209 ASN B C   
1537 O O   . ASN A 211 ? 1.3119 0.9047 0.6830 0.0572  0.3478  -0.1184 209 ASN B O   
1538 C CB  . ASN A 211 ? 1.3531 0.9103 0.7466 0.0684  0.3518  -0.1234 209 ASN B CB  
1539 C CG  . ASN A 211 ? 1.4179 0.9562 0.8160 0.0631  0.3493  -0.1289 209 ASN B CG  
1540 O OD1 . ASN A 211 ? 1.4224 0.9436 0.8220 0.0587  0.3469  -0.1235 209 ASN B OD1 
1541 N ND2 . ASN A 211 ? 1.4610 1.0048 0.8616 0.0633  0.3497  -0.1405 209 ASN B ND2 
1542 N N   . THR A 212 ? 1.3537 0.9324 0.7180 0.0519  0.3449  -0.0989 210 THR B N   
1543 C CA  . THR A 212 ? 1.3672 0.9607 0.7159 0.0442  0.3426  -0.0946 210 THR B CA  
1544 C C   . THR A 212 ? 1.3556 0.9275 0.6944 0.0368  0.3372  -0.0891 210 THR B C   
1545 O O   . THR A 212 ? 1.3299 0.8854 0.6705 0.0362  0.3356  -0.0822 210 THR B O   
1546 C CB  . THR A 212 ? 1.3597 0.9777 0.7026 0.0430  0.3444  -0.0857 210 THR B CB  
1547 O OG1 . THR A 212 ? 1.3560 0.9892 0.7104 0.0522  0.3490  -0.0909 210 THR B OG1 
1548 C CG2 . THR A 212 ? 1.3325 0.9737 0.6601 0.0355  0.3433  -0.0838 210 THR B CG2 
1549 N N   . LYS A 213 ? 1.3806 0.9532 0.7083 0.0317  0.3341  -0.0931 211 LYS B N   
1550 C CA  . LYS A 213 ? 1.4097 0.9630 0.7235 0.0250  0.3280  -0.0892 211 LYS B CA  
1551 C C   . LYS A 213 ? 1.4053 0.9717 0.6986 0.0184  0.3252  -0.0876 211 LYS B C   
1552 O O   . LYS A 213 ? 1.4020 0.9761 0.6956 0.0195  0.3252  -0.0978 211 LYS B O   
1553 C CB  . LYS A 213 ? 1.4141 0.9470 0.7386 0.0271  0.3255  -0.0994 211 LYS B CB  
1554 C CG  . LYS A 213 ? 1.4396 0.9522 0.7505 0.0219  0.3184  -0.0975 211 LYS B CG  
1555 C CD  . LYS A 213 ? 1.4390 0.9318 0.7646 0.0242  0.3163  -0.1022 211 LYS B CD  
1556 C CE  . LYS A 213 ? 1.5151 1.0014 0.8435 0.0231  0.3111  -0.1144 211 LYS B CE  
1557 N NZ  . LYS A 213 ? 1.4702 0.9372 0.8008 0.0222  0.3053  -0.1149 211 LYS B NZ  
1558 N N   . VAL A 214 ? 1.4060 0.9757 0.6812 0.0108  0.3225  -0.0742 212 VAL B N   
1559 C CA  . VAL A 214 ? 1.3999 0.9809 0.6523 0.0026  0.3189  -0.0695 212 VAL B CA  
1560 C C   . VAL A 214 ? 1.3606 0.9163 0.5898 -0.0054 0.3105  -0.0596 212 VAL B C   
1561 O O   . VAL A 214 ? 1.3811 0.9172 0.6111 -0.0058 0.3083  -0.0534 212 VAL B O   
1562 C CB  . VAL A 214 ? 1.3551 0.9690 0.6040 -0.0016 0.3223  -0.0611 212 VAL B CB  
1563 C CG1 . VAL A 214 ? 1.3700 1.0064 0.6407 0.0080  0.3299  -0.0710 212 VAL B CG1 
1564 C CG2 . VAL A 214 ? 1.3253 0.9358 0.5689 -0.0078 0.3204  -0.0456 212 VAL B CG2 
1565 N N   . ASP A 215 ? 1.3478 0.9036 0.5546 -0.0118 0.3050  -0.0580 213 ASP B N   
1566 C CA  . ASP A 215 ? 1.3902 0.9202 0.5690 -0.0197 0.2947  -0.0483 213 ASP B CA  
1567 C C   . ASP A 215 ? 1.4094 0.9548 0.5643 -0.0319 0.2902  -0.0333 213 ASP B C   
1568 O O   . ASP A 215 ? 1.4058 0.9665 0.5505 -0.0341 0.2893  -0.0367 213 ASP B O   
1569 C CB  . ASP A 215 ? 1.3889 0.8994 0.5606 -0.0156 0.2893  -0.0613 213 ASP B CB  
1570 C CG  . ASP A 215 ? 1.4015 0.8987 0.5984 -0.0060 0.2922  -0.0748 213 ASP B CG  
1571 O OD1 . ASP A 215 ? 1.4792 0.9690 0.6797 -0.0017 0.2892  -0.0885 213 ASP B OD1 
1572 O OD2 . ASP A 215 ? 1.4357 0.9306 0.6491 -0.0033 0.2966  -0.0712 213 ASP B OD2 
1573 N N   . LYS A 216 ? 1.3797 0.9228 0.5270 -0.0405 0.2868  -0.0166 214 LYS B N   
1574 C CA  . LYS A 216 ? 1.4469 1.0055 0.5743 -0.0546 0.2813  -0.0001 214 LYS B CA  
1575 C C   . LYS A 216 ? 1.4707 0.9959 0.5659 -0.0636 0.2663  0.0113  214 LYS B C   
1576 O O   . LYS A 216 ? 1.4765 0.9693 0.5676 -0.0615 0.2600  0.0130  214 LYS B O   
1577 C CB  . LYS A 216 ? 1.4102 0.9883 0.5491 -0.0604 0.2846  0.0121  214 LYS B CB  
1578 C CG  . LYS A 216 ? 1.3961 0.9969 0.5195 -0.0764 0.2796  0.0291  214 LYS B CG  
1579 C CD  . LYS A 216 ? 1.4611 1.0862 0.5749 -0.0786 0.2807  0.0250  214 LYS B CD  
1580 C CE  . LYS A 216 ? 1.4827 1.1511 0.5989 -0.0887 0.2840  0.0349  214 LYS B CE  
1581 N NZ  . LYS A 216 ? 1.4106 1.1051 0.5534 -0.0825 0.2945  0.0310  214 LYS B NZ  
1582 N N   . LYS A 217 ? 1.4800 1.0134 0.5530 -0.0728 0.2594  0.0185  215 LYS B N   
1583 C CA  . LYS A 217 ? 1.5168 1.0223 0.5606 -0.0828 0.2412  0.0327  215 LYS B CA  
1584 C C   . LYS A 217 ? 1.5074 1.0238 0.5407 -0.0999 0.2364  0.0551  215 LYS B C   
1585 O O   . LYS A 217 ? 1.4838 1.0389 0.5239 -0.1061 0.2428  0.0588  215 LYS B O   
1586 C CB  . LYS A 217 ? 1.5505 1.0578 0.5778 -0.0825 0.2337  0.0275  215 LYS B CB  
1587 C CG  . LYS A 217 ? 1.6009 1.0923 0.6037 -0.0954 0.2126  0.0466  215 LYS B CG  
1588 C CD  . LYS A 217 ? 1.7073 1.2023 0.6914 -0.0951 0.2048  0.0424  215 LYS B CD  
1589 C CE  . LYS A 217 ? 1.7490 1.2134 0.7358 -0.0848 0.1865  0.0337  215 LYS B CE  
1590 N NZ  . LYS A 217 ? 1.8103 1.2848 0.7902 -0.0777 0.1865  0.0188  215 LYS B NZ  
1591 N N   . VAL A 218 ? 1.5646 1.0531 0.5922 -0.1064 0.2225  0.0688  216 VAL B N   
1592 C CA  . VAL A 218 ? 1.5957 1.0903 0.6137 -0.1240 0.2167  0.0905  216 VAL B CA  
1593 C C   . VAL A 218 ? 1.6236 1.0945 0.6115 -0.1361 0.1957  0.1061  216 VAL B C   
1594 O O   . VAL A 218 ? 1.6443 1.0817 0.6330 -0.1308 0.1777  0.1057  216 VAL B O   
1595 C CB  . VAL A 218 ? 1.4914 0.9720 0.5238 -0.1239 0.2166  0.0954  216 VAL B CB  
1596 C CG1 . VAL A 218 ? 1.4643 0.9700 0.5034 -0.1400 0.2153  0.1126  216 VAL B CG1 
1597 C CG2 . VAL A 218 ? 1.4399 0.9327 0.5000 -0.1077 0.2337  0.0771  216 VAL B CG2 
1598 N N   . GLU A 219 ? 1.5591 1.0568 0.5376 -0.1496 0.1944  0.1175  217 GLU B N   
1599 C CA  . GLU A 219 ? 1.6142 1.0949 0.5630 -0.1611 0.1760  0.1320  217 GLU B CA  
1600 C C   . GLU A 219 ? 1.6083 1.1092 0.5573 -0.1808 0.1709  0.1529  217 GLU B C   
1601 O O   . GLU A 219 ? 1.5681 1.1088 0.5386 -0.1846 0.1849  0.1529  217 GLU B O   
1602 C CB  . GLU A 219 ? 1.6820 1.1802 0.6190 -0.1563 0.1795  0.1221  217 GLU B CB  
1603 C CG  . GLU A 219 ? 1.7462 1.2176 0.6789 -0.1394 0.1739  0.1047  217 GLU B CG  
1604 C CD  . GLU A 219 ? 1.7479 1.1753 0.6780 -0.1364 0.1491  0.1103  217 GLU B CD  
1605 O OE1 . GLU A 219 ? 1.7453 1.1548 0.6489 -0.1464 0.1303  0.1257  217 GLU B OE1 
1606 O OE2 . GLU A 219 ? 1.7346 1.1457 0.6885 -0.1234 0.1480  0.0985  217 GLU B OE2 
1607 N N   . PRO A 220 ? 1.6778 1.1521 0.6032 -0.1933 0.1503  0.1705  218 PRO B N   
1608 C CA  . PRO A 220 ? 1.6353 1.1284 0.5600 -0.2133 0.1451  0.1905  218 PRO B CA  
1609 C C   . PRO A 220 ? 1.6503 1.1923 0.5753 -0.2190 0.1564  0.1904  218 PRO B C   
1610 O O   . PRO A 220 ? 1.6678 1.2116 0.5770 -0.2142 0.1547  0.1848  218 PRO B O   
1611 C CB  . PRO A 220 ? 1.6272 1.0738 0.5244 -0.2216 0.1188  0.2064  218 PRO B CB  
1612 C CG  . PRO A 220 ? 1.6654 1.0662 0.5555 -0.2050 0.1104  0.1948  218 PRO B CG  
1613 C CD  . PRO A 220 ? 1.7017 1.1252 0.6004 -0.1889 0.1294  0.1728  218 PRO B CD  
1614 N N   . LYS A 221 ? 1.6313 1.2132 0.5737 -0.2287 0.1674  0.1962  219 LYS B N   
1615 C CA  . LYS A 221 ? 1.6383 1.2710 0.5828 -0.2354 0.1783  0.1975  219 LYS B CA  
1616 C C   . LYS A 221 ? 1.6311 1.2712 0.5580 -0.2300 0.1777  0.1908  219 LYS B C   
1617 O O   . LYS A 221 ? 1.6787 1.3529 0.6169 -0.2191 0.1931  0.1750  219 LYS B O   
1618 C CB  . LYS A 221 ? 1.6113 1.2524 0.5482 -0.2573 0.1701  0.2192  219 LYS B CB  
1619 C CG  . LYS A 221 ? 1.6354 1.3095 0.5586 -0.2671 0.1721  0.2257  219 LYS B CG  
1620 C CD  . LYS A 221 ? 1.6767 1.3176 0.5679 -0.2742 0.1523  0.2378  219 LYS B CD  
1621 C CE  . LYS A 221 ? 1.7140 1.3351 0.5919 -0.2953 0.1367  0.2609  219 LYS B CE  
1622 N NZ  . LYS A 221 ? 1.7531 1.3336 0.6006 -0.2985 0.1153  0.2712  219 LYS B NZ  
1623 N N   . MET B 5   ? 1.1481 0.9593 0.8243 0.1590  0.2557  0.0063  4   MET D N   
1624 C CA  . MET B 5   ? 1.1468 0.9958 0.8333 0.1546  0.2647  0.0054  4   MET D CA  
1625 C C   . MET B 5   ? 1.1363 0.9979 0.8264 0.1240  0.2556  0.0065  4   MET D C   
1626 O O   . MET B 5   ? 1.1604 1.0211 0.8430 0.1106  0.2652  0.0065  4   MET D O   
1627 C CB  . MET B 5   ? 1.1086 0.9978 0.8142 0.1749  0.2650  0.0044  4   MET D CB  
1628 C CG  . MET B 5   ? 1.1284 1.0175 0.8305 0.2056  0.2816  0.0032  4   MET D CG  
1629 S SD  . MET B 5   ? 1.2680 1.2131 0.9869 0.2220  0.2936  0.0010  4   MET D SD  
1630 C CE  . MET B 5   ? 1.1931 1.1276 0.9063 0.2617  0.3050  0.0006  4   MET D CE  
1631 N N   . THR B 6   ? 1.0905 0.9636 0.7913 0.1132  0.2375  0.0074  5   THR D N   
1632 C CA  . THR B 6   ? 1.0877 0.9778 0.7940 0.0855  0.2289  0.0085  5   THR D CA  
1633 C C   . THR B 6   ? 1.0622 0.9180 0.7564 0.0652  0.2121  0.0105  5   THR D C   
1634 O O   . THR B 6   ? 1.0467 0.8983 0.7457 0.0666  0.1960  0.0107  5   THR D O   
1635 C CB  . THR B 6   ? 1.0643 0.9998 0.7932 0.0873  0.2219  0.0072  5   THR D CB  
1636 O OG1 . THR B 6   ? 1.1034 1.0733 0.8429 0.1071  0.2375  0.0051  5   THR D OG1 
1637 C CG2 . THR B 6   ? 1.0114 0.9626 0.7449 0.0570  0.2136  0.0084  5   THR D CG2 
1638 N N   . GLN B 7   ? 1.0155 0.8489 0.6939 0.0464  0.2156  0.0119  6   GLN D N   
1639 C CA  . GLN B 7   ? 0.9952 0.7905 0.6573 0.0302  0.2024  0.0137  6   GLN D CA  
1640 C C   . GLN B 7   ? 1.0241 0.8264 0.6859 0.0017  0.1922  0.0159  6   GLN D C   
1641 O O   . GLN B 7   ? 1.0232 0.8409 0.6849 -0.0119 0.2019  0.0167  6   GLN D O   
1642 C CB  . GLN B 7   ? 0.9788 0.7408 0.6209 0.0302  0.2132  0.0133  6   GLN D CB  
1643 C CG  . GLN B 7   ? 0.9477 0.6691 0.5712 0.0180  0.2007  0.0145  6   GLN D CG  
1644 C CD  . GLN B 7   ? 0.9232 0.6142 0.5303 0.0264  0.2114  0.0127  6   GLN D CD  
1645 O OE1 . GLN B 7   ? 0.9549 0.6521 0.5644 0.0431  0.2271  0.0107  6   GLN D OE1 
1646 N NE2 . GLN B 7   ? 0.9095 0.5675 0.4994 0.0155  0.2027  0.0130  6   GLN D NE2 
1647 N N   . SER B 8   ? 0.9990 0.7888 0.6596 -0.0071 0.1731  0.0170  7   SER D N   
1648 C CA  . SER B 8   ? 0.9703 0.7574 0.6263 -0.0345 0.1616  0.0194  7   SER D CA  
1649 C C   . SER B 8   ? 0.9774 0.7215 0.6141 -0.0423 0.1463  0.0209  7   SER D C   
1650 O O   . SER B 8   ? 0.9966 0.7225 0.6303 -0.0256 0.1403  0.0197  7   SER D O   
1651 C CB  . SER B 8   ? 0.9561 0.7766 0.6316 -0.0394 0.1516  0.0188  7   SER D CB  
1652 O OG  . SER B 8   ? 0.9800 0.7787 0.6475 -0.0539 0.1318  0.0203  7   SER D OG  
1653 N N   . PRO B 9   ? 0.9940 0.7206 0.6160 -0.0668 0.1403  0.0237  8   PRO D N   
1654 C CA  . PRO B 9   ? 0.9933 0.7334 0.6131 -0.0879 0.1493  0.0259  8   PRO D CA  
1655 C C   . PRO B 9   ? 0.9944 0.7203 0.6005 -0.0863 0.1651  0.0258  8   PRO D C   
1656 O O   . PRO B 9   ? 0.9838 0.6777 0.5750 -0.0784 0.1636  0.0250  8   PRO D O   
1657 C CB  . PRO B 9   ? 0.9552 0.6729 0.5611 -0.1118 0.1327  0.0290  8   PRO D CB  
1658 C CG  . PRO B 9   ? 0.9686 0.6466 0.5581 -0.1024 0.1210  0.0286  8   PRO D CG  
1659 C CD  . PRO B 9   ? 0.9983 0.6895 0.6038 -0.0755 0.1217  0.0252  8   PRO D CD  
1660 N N   . SER B 10  ? 1.0306 0.7802 0.6412 -0.0941 0.1799  0.0264  9   SER D N   
1661 C CA  . SER B 10  ? 1.0409 0.7778 0.6380 -0.0935 0.1951  0.0260  9   SER D CA  
1662 C C   . SER B 10  ? 1.0283 0.7258 0.6003 -0.1094 0.1880  0.0282  9   SER D C   
1663 O O   . SER B 10  ? 1.0382 0.7167 0.5963 -0.1057 0.1973  0.0269  9   SER D O   
1664 C CB  . SER B 10  ? 1.1108 0.8814 0.7163 -0.1019 0.2104  0.0266  9   SER D CB  
1665 O OG  . SER B 10  ? 1.1991 1.0113 0.8283 -0.0948 0.2123  0.0254  9   SER D OG  
1666 N N   . SER B 11  ? 1.0061 0.6905 0.5713 -0.1263 0.1715  0.0311  10  SER D N   
1667 C CA  . SER B 11  ? 1.0035 0.6538 0.5439 -0.1433 0.1652  0.0338  10  SER D CA  
1668 C C   . SER B 11  ? 0.9495 0.5772 0.4818 -0.1510 0.1437  0.0357  10  SER D C   
1669 O O   . SER B 11  ? 0.9490 0.5939 0.4942 -0.1567 0.1349  0.0367  10  SER D O   
1670 C CB  . SER B 11  ? 0.9837 0.6473 0.5201 -0.1648 0.1740  0.0371  10  SER D CB  
1671 O OG  . SER B 11  ? 1.0074 0.6419 0.5200 -0.1733 0.1767  0.0383  10  SER D OG  
1672 N N   . LEU B 12  ? 0.9553 0.5453 0.4655 -0.1516 0.1351  0.0359  11  LEU D N   
1673 C CA  . LEU B 12  ? 0.9612 0.5261 0.4604 -0.1568 0.1144  0.0375  11  LEU D CA  
1674 C C   . LEU B 12  ? 0.9793 0.5070 0.4493 -0.1693 0.1077  0.0398  11  LEU D C   
1675 O O   . LEU B 12  ? 1.0162 0.5253 0.4738 -0.1602 0.1116  0.0375  11  LEU D O   
1676 C CB  . LEU B 12  ? 0.9662 0.5253 0.4725 -0.1343 0.1067  0.0340  11  LEU D CB  
1677 C CG  . LEU B 12  ? 0.9764 0.5331 0.4862 -0.1388 0.0878  0.0352  11  LEU D CG  
1678 C CD1 . LEU B 12  ? 0.9725 0.5630 0.5004 -0.1515 0.0913  0.0367  11  LEU D CD1 
1679 C CD2 . LEU B 12  ? 1.0064 0.5656 0.5279 -0.1155 0.0819  0.0318  11  LEU D CD2 
1680 N N   . SER B 13  ? 0.9989 0.5148 0.4569 -0.1895 0.0972  0.0440  12  SER D N   
1681 C CA  . SER B 13  ? 1.0261 0.5037 0.4541 -0.1998 0.0880  0.0465  12  SER D CA  
1682 C C   . SER B 13  ? 1.0176 0.4700 0.4364 -0.1920 0.0679  0.0457  12  SER D C   
1683 O O   . SER B 13  ? 1.0247 0.4859 0.4555 -0.1917 0.0575  0.0458  12  SER D O   
1684 C CB  . SER B 13  ? 1.0442 0.5169 0.4593 -0.2259 0.0874  0.0520  12  SER D CB  
1685 O OG  . SER B 13  ? 1.0520 0.5343 0.4637 -0.2327 0.1048  0.0530  12  SER D OG  
1686 N N   . ALA B 14  ? 1.0212 0.4433 0.4185 -0.1855 0.0622  0.0445  13  ALA D N   
1687 C CA  . ALA B 14  ? 1.0200 0.4190 0.4079 -0.1759 0.0434  0.0433  13  ALA D CA  
1688 C C   . ALA B 14  ? 1.0324 0.3972 0.3909 -0.1755 0.0374  0.0431  13  ALA D C   
1689 O O   . ALA B 14  ? 1.0628 0.4240 0.4110 -0.1796 0.0488  0.0430  13  ALA D O   
1690 C CB  . ALA B 14  ? 1.0381 0.4529 0.4469 -0.1531 0.0438  0.0387  13  ALA D CB  
1691 N N   . SER B 15  ? 1.0367 0.3777 0.3818 -0.1692 0.0191  0.0427  14  SER D N   
1692 C CA  . SER B 15  ? 1.0496 0.3579 0.3656 -0.1671 0.0099  0.0423  14  SER D CA  
1693 C C   . SER B 15  ? 1.0300 0.3350 0.3494 -0.1450 0.0043  0.0372  14  SER D C   
1694 O O   . SER B 15  ? 1.0486 0.3722 0.3903 -0.1323 0.0048  0.0349  14  SER D O   
1695 C CB  . SER B 15  ? 1.1062 0.3861 0.3991 -0.1791 -0.0081 0.0465  14  SER D CB  
1696 O OG  . SER B 15  ? 1.1704 0.4600 0.4693 -0.1983 -0.0051 0.0510  14  SER D OG  
1697 N N   . VAL B 16  ? 1.0520 0.3340 0.3482 -0.1405 -0.0005 0.0354  15  VAL D N   
1698 C CA  . VAL B 16  ? 1.0228 0.2990 0.3180 -0.1211 -0.0075 0.0306  15  VAL D CA  
1699 C C   . VAL B 16  ? 1.1019 0.3705 0.3982 -0.1139 -0.0264 0.0313  15  VAL D C   
1700 O O   . VAL B 16  ? 1.1158 0.3758 0.4042 -0.1244 -0.0381 0.0340  15  VAL D O   
1701 C CB  . VAL B 16  ? 1.0272 0.2933 0.3038 -0.1186 -0.0108 0.0254  15  VAL D CB  
1702 C CG1 . VAL B 16  ? 1.0458 0.3105 0.3208 -0.1008 -0.0245 0.0194  15  VAL D CG1 
1703 C CG2 . VAL B 16  ? 1.0596 0.3319 0.3368 -0.1199 0.0083  0.0236  15  VAL D CG2 
1704 N N   . GLY B 17  ? 1.0824 0.3599 0.3922 -0.0952 -0.0293 0.0275  16  GLY D N   
1705 C CA  . GLY B 17  ? 1.0328 0.3074 0.3463 -0.0857 -0.0467 0.0271  16  GLY D CA  
1706 C C   . GLY B 17  ? 1.0550 0.3481 0.3911 -0.0881 -0.0464 0.0292  16  GLY D C   
1707 O O   . GLY B 17  ? 1.0662 0.3619 0.4106 -0.0764 -0.0581 0.0281  16  GLY D O   
1708 N N   . ASP B 18  ? 1.0063 0.3162 0.3541 -0.1021 -0.0333 0.0316  17  ASP D N   
1709 C CA  . ASP B 18  ? 1.0675 0.4019 0.4398 -0.1042 -0.0316 0.0326  17  ASP D CA  
1710 C C   . ASP B 18  ? 1.0566 0.4157 0.4545 -0.0840 -0.0247 0.0290  17  ASP D C   
1711 O O   . ASP B 18  ? 1.0431 0.4027 0.4417 -0.0709 -0.0171 0.0261  17  ASP D O   
1712 C CB  . ASP B 18  ? 1.0563 0.4070 0.4361 -0.1221 -0.0170 0.0354  17  ASP D CB  
1713 C CG  . ASP B 18  ? 1.1699 0.5001 0.5288 -0.1435 -0.0250 0.0398  17  ASP D CG  
1714 O OD1 . ASP B 18  ? 1.2202 0.5203 0.5560 -0.1436 -0.0419 0.0406  17  ASP D OD1 
1715 O OD2 . ASP B 18  ? 1.1708 0.5150 0.5360 -0.1598 -0.0143 0.0425  17  ASP D OD2 
1716 N N   . ARG B 19  ? 1.0260 0.4066 0.4450 -0.0821 -0.0268 0.0292  18  ARG D N   
1717 C CA  . ARG B 19  ? 0.9685 0.3732 0.4118 -0.0625 -0.0212 0.0264  18  ARG D CA  
1718 C C   . ARG B 19  ? 0.9361 0.3737 0.4028 -0.0671 -0.0052 0.0269  18  ARG D C   
1719 O O   . ARG B 19  ? 0.9835 0.4344 0.4594 -0.0776 -0.0096 0.0283  18  ARG D O   
1720 C CB  . ARG B 19  ? 0.9858 0.3887 0.4336 -0.0523 -0.0394 0.0255  18  ARG D CB  
1721 C CG  . ARG B 19  ? 0.9133 0.3289 0.3762 -0.0285 -0.0379 0.0225  18  ARG D CG  
1722 C CD  . ARG B 19  ? 0.9066 0.3337 0.3830 -0.0210 -0.0513 0.0218  18  ARG D CD  
1723 N NE  . ARG B 19  ? 0.9198 0.3461 0.4001 0.0021  -0.0566 0.0195  18  ARG D NE  
1724 C CZ  . ARG B 19  ? 0.9298 0.3806 0.4323 0.0189  -0.0505 0.0179  18  ARG D CZ  
1725 N NH1 . ARG B 19  ? 0.9038 0.3829 0.4270 0.0162  -0.0419 0.0181  18  ARG D NH1 
1726 N NH2 . ARG B 19  ? 0.9189 0.3665 0.4223 0.0392  -0.0526 0.0163  18  ARG D NH2 
1727 N N   . VAL B 20  ? 0.9359 0.3875 0.4122 -0.0585 0.0130  0.0253  19  VAL D N   
1728 C CA  . VAL B 20  ? 0.9602 0.4411 0.4546 -0.0632 0.0303  0.0257  19  VAL D CA  
1729 C C   . VAL B 20  ? 0.8910 0.3983 0.4095 -0.0427 0.0373  0.0233  19  VAL D C   
1730 O O   . VAL B 20  ? 0.8888 0.3886 0.4072 -0.0247 0.0362  0.0213  19  VAL D O   
1731 C CB  . VAL B 20  ? 0.9357 0.4100 0.4195 -0.0692 0.0465  0.0256  19  VAL D CB  
1732 C CG1 . VAL B 20  ? 0.9604 0.4591 0.4555 -0.0809 0.0613  0.0271  19  VAL D CG1 
1733 C CG2 . VAL B 20  ? 0.9789 0.4206 0.4348 -0.0823 0.0370  0.0271  19  VAL D CG2 
1734 N N   . THR B 21  ? 0.8766 0.4154 0.4155 -0.0450 0.0443  0.0236  20  THR D N   
1735 C CA  . THR B 21  ? 0.8994 0.4647 0.4602 -0.0244 0.0537  0.0215  20  THR D CA  
1736 C C   . THR B 21  ? 0.9145 0.5093 0.4894 -0.0282 0.0725  0.0216  20  THR D C   
1737 O O   . THR B 21  ? 0.9265 0.5389 0.5080 -0.0439 0.0719  0.0229  20  THR D O   
1738 C CB  . THR B 21  ? 0.9120 0.4925 0.4877 -0.0153 0.0400  0.0205  20  THR D CB  
1739 O OG1 . THR B 21  ? 0.8737 0.4886 0.4687 -0.0214 0.0451  0.0205  20  THR D OG1 
1740 C CG2 . THR B 21  ? 0.9468 0.5038 0.5082 -0.0261 0.0182  0.0216  20  THR D CG2 
1741 N N   . ILE B 22  ? 0.8985 0.4999 0.4784 -0.0127 0.0890  0.0199  21  ILE D N   
1742 C CA  . ILE B 22  ? 0.9045 0.5340 0.4977 -0.0101 0.1081  0.0194  21  ILE D CA  
1743 C C   . ILE B 22  ? 0.9149 0.5698 0.5283 0.0126  0.1119  0.0176  21  ILE D C   
1744 O O   . ILE B 22  ? 0.8968 0.5406 0.5100 0.0298  0.1061  0.0165  21  ILE D O   
1745 C CB  . ILE B 22  ? 0.8690 0.4832 0.4497 -0.0086 0.1242  0.0185  21  ILE D CB  
1746 C CG1 . ILE B 22  ? 0.9228 0.5069 0.4806 -0.0277 0.1174  0.0199  21  ILE D CG1 
1747 C CG2 . ILE B 22  ? 0.9114 0.5530 0.5033 -0.0070 0.1435  0.0180  21  ILE D CG2 
1748 C CD1 . ILE B 22  ? 0.9424 0.5092 0.4858 -0.0279 0.1312  0.0184  21  ILE D CD1 
1749 N N   . THR B 23  ? 0.8869 0.5769 0.5175 0.0136  0.1220  0.0171  22  THR D N   
1750 C CA  . THR B 23  ? 0.9040 0.6220 0.5543 0.0347  0.1242  0.0154  22  THR D CA  
1751 C C   . THR B 23  ? 0.9602 0.7024 0.6199 0.0464  0.1453  0.0143  22  THR D C   
1752 O O   . THR B 23  ? 0.9612 0.7193 0.6226 0.0331  0.1549  0.0147  22  THR D O   
1753 C CB  . THR B 23  ? 0.9311 0.6741 0.5961 0.0270  0.1103  0.0152  22  THR D CB  
1754 O OG1 . THR B 23  ? 0.9289 0.6474 0.5846 0.0212  0.0901  0.0158  22  THR D OG1 
1755 C CG2 . THR B 23  ? 0.9306 0.7079 0.6170 0.0491  0.1140  0.0129  22  THR D CG2 
1756 N N   . CYS B 24  ? 1.0128 0.7573 0.6776 0.0719  0.1525  0.0129  23  CYS D N   
1757 C CA  . CYS B 24  ? 1.0270 0.7912 0.6990 0.0882  0.1723  0.0117  23  CYS D CA  
1758 C C   . CYS B 24  ? 1.0013 0.7964 0.6923 0.1093  0.1708  0.0104  23  CYS D C   
1759 O O   . CYS B 24  ? 0.9927 0.7794 0.6856 0.1218  0.1599  0.0103  23  CYS D O   
1760 C CB  . CYS B 24  ? 1.0107 0.7440 0.6673 0.0999  0.1842  0.0112  23  CYS D CB  
1761 S SG  . CYS B 24  ? 1.1025 0.8481 0.7592 0.1134  0.2103  0.0098  23  CYS D SG  
1762 N N   . ARG B 25  ? 0.9963 0.8286 0.7013 0.1130  0.1811  0.0093  24  ARG D N   
1763 C CA  . ARG B 25  ? 0.9837 0.8503 0.7070 0.1341  0.1819  0.0076  24  ARG D CA  
1764 C C   . ARG B 25  ? 1.0899 0.9627 0.8121 0.1573  0.2026  0.0067  24  ARG D C   
1765 O O   . ARG B 25  ? 1.1202 1.0048 0.8411 0.1524  0.2169  0.0063  24  ARG D O   
1766 C CB  . ARG B 25  ? 0.9966 0.9052 0.7374 0.1206  0.1768  0.0063  24  ARG D CB  
1767 C CG  . ARG B 25  ? 1.0228 0.9757 0.7812 0.1407  0.1877  0.0039  24  ARG D CG  
1768 C CD  . ARG B 25  ? 1.0562 1.0518 0.8346 0.1302  0.1774  0.0018  24  ARG D CD  
1769 N NE  . ARG B 25  ? 1.0899 1.0810 0.8737 0.1309  0.1576  0.0011  24  ARG D NE  
1770 C CZ  . ARG B 25  ? 1.0267 1.0279 0.8172 0.1088  0.1420  0.0004  24  ARG D CZ  
1771 N NH1 . ARG B 25  ? 0.9879 1.0036 0.7806 0.0831  0.1438  0.0007  24  ARG D NH1 
1772 N NH2 . ARG B 25  ? 0.9471 0.9428 0.7414 0.1124  0.1244  -0.0006 24  ARG D NH2 
1773 N N   . ALA B 26  ? 1.1145 0.9784 0.8361 0.1828  0.2044  0.0066  25  ALA D N   
1774 C CA  . ALA B 26  ? 1.1115 0.9765 0.8297 0.2074  0.2235  0.0061  25  ALA D CA  
1775 C C   . ALA B 26  ? 1.0791 0.9801 0.8139 0.2315  0.2239  0.0047  25  ALA D C   
1776 O O   . ALA B 26  ? 1.0787 0.9945 0.8254 0.2326  0.2084  0.0043  25  ALA D O   
1777 C CB  . ALA B 26  ? 1.1128 0.9338 0.8134 0.2185  0.2277  0.0073  25  ALA D CB  
1778 N N   . SER B 27  ? 1.1387 1.0532 0.8734 0.2517  0.2419  0.0039  26  SER D N   
1779 C CA  . SER B 27  ? 1.1484 1.0952 0.8964 0.2787  0.2440  0.0026  26  SER D CA  
1780 C C   . SER B 27  ? 1.1704 1.0948 0.9139 0.2995  0.2384  0.0040  26  SER D C   
1781 O O   . SER B 27  ? 1.1629 1.1103 0.9198 0.3112  0.2277  0.0032  26  SER D O   
1782 C CB  . SER B 27  ? 1.1644 1.1260 0.9095 0.2971  0.2653  0.0015  26  SER D CB  
1783 O OG  . SER B 27  ? 1.1762 1.0957 0.9002 0.3010  0.2788  0.0029  26  SER D OG  
1784 N N   . GLN B 28  ? 1.1346 1.0153 0.8593 0.3042  0.2456  0.0060  27  GLN D N   
1785 C CA  . GLN B 28  ? 1.0948 0.9532 0.8152 0.3217  0.2404  0.0082  27  GLN D CA  
1786 C C   . GLN B 28  ? 1.0236 0.8654 0.7433 0.3092  0.2216  0.0086  27  GLN D C   
1787 O O   . GLN B 28  ? 1.0310 0.8617 0.7475 0.2827  0.2132  0.0085  27  GLN D O   
1788 C CB  . GLN B 28  ? 1.0905 0.9144 0.8011 0.3159  0.2434  0.0128  27  GLN D CB  
1789 C CG  . GLN B 28  ? 1.1414 0.9779 0.8557 0.3206  0.2535  0.0140  27  GLN D CG  
1790 C CD  . GLN B 28  ? 1.1583 1.0260 0.8876 0.3383  0.2486  0.0154  27  GLN D CD  
1791 O OE1 . GLN B 28  ? 1.1596 1.0159 0.8884 0.3452  0.2422  0.0201  27  GLN D OE1 
1792 N NE2 . GLN B 28  ? 1.1333 1.0420 0.8748 0.3446  0.2521  0.0113  27  GLN D NE2 
1793 N N   . SER B 29  ? 1.0009 0.8413 0.7240 0.3277  0.2133  0.0096  28  SER D N   
1794 C CA  . SER B 29  ? 0.9503 0.7741 0.6728 0.3182  0.1938  0.0104  28  SER D CA  
1795 C C   . SER B 29  ? 0.9381 0.7228 0.6472 0.3195  0.1928  0.0141  28  SER D C   
1796 O O   . SER B 29  ? 0.9424 0.7137 0.6497 0.3184  0.1785  0.0148  28  SER D O   
1797 C CB  . SER B 29  ? 0.9322 0.7855 0.6712 0.3317  0.1796  0.0094  28  SER D CB  
1798 O OG  . SER B 29  ? 0.9259 0.8241 0.6817 0.3348  0.1817  0.0068  28  SER D OG  
1799 N N   . VAL B 30  ? 0.9490 0.7209 0.6531 0.3143  0.2021  0.0179  29  VAL D N   
1800 C CA  . VAL B 30  ? 0.9197 0.6636 0.6160 0.3069  0.1970  0.0229  29  VAL D CA  
1801 C C   . VAL B 30  ? 0.8989 0.6115 0.5802 0.2916  0.1958  0.0207  29  VAL D C   
1802 O O   . VAL B 30  ? 0.9251 0.6249 0.5961 0.2817  0.2072  0.0181  29  VAL D O   
1803 C CB  . VAL B 30  ? 0.9060 0.6444 0.5997 0.3065  0.2075  0.0271  29  VAL D CB  
1804 C CG1 . VAL B 30  ? 0.8816 0.5941 0.5665 0.2979  0.2034  0.0316  29  VAL D CG1 
1805 C CG2 . VAL B 30  ? 0.9237 0.6905 0.6295 0.3217  0.2078  0.0290  29  VAL D CG2 
1806 N N   . SER B 31  ? 0.8676 0.5681 0.5467 0.2887  0.1814  0.0215  30  SER D N   
1807 C CA  . SER B 31  ? 0.9161 0.5863 0.5798 0.2740  0.1788  0.0192  30  SER D CA  
1808 C C   . SER B 31  ? 0.8935 0.5429 0.5476 0.2617  0.1873  0.0219  30  SER D C   
1809 O O   . SER B 31  ? 0.9178 0.5441 0.5581 0.2482  0.1901  0.0192  30  SER D O   
1810 C CB  . SER B 31  ? 0.8683 0.5315 0.5320 0.2730  0.1596  0.0196  30  SER D CB  
1811 O OG  . SER B 31  ? 0.8646 0.5124 0.5229 0.2629  0.1560  0.0230  30  SER D OG  
1812 N N   . SER B 32  ? 0.8898 0.5458 0.5494 0.2657  0.1917  0.0269  31  SER D N   
1813 C CA  . SER B 32  ? 0.9391 0.5748 0.5893 0.2546  0.1988  0.0293  31  SER D CA  
1814 C C   . SER B 32  ? 0.9036 0.5294 0.5460 0.2472  0.2133  0.0266  31  SER D C   
1815 O O   . SER B 32  ? 0.8876 0.4921 0.5193 0.2341  0.2173  0.0263  31  SER D O   
1816 C CB  . SER B 32  ? 0.9171 0.5599 0.5723 0.2614  0.2006  0.0349  31  SER D CB  
1817 O OG  . SER B 32  ? 0.9315 0.5904 0.5957 0.2701  0.1885  0.0366  31  SER D OG  
1818 N N   . ALA B 33  ? 0.8921 0.5355 0.5400 0.2547  0.2208  0.0241  32  ALA D N   
1819 C CA  . ALA B 33  ? 0.9120 0.5547 0.5558 0.2504  0.2355  0.0221  32  ALA D CA  
1820 C C   . ALA B 33  ? 0.9811 0.6106 0.6123 0.2361  0.2405  0.0164  32  ALA D C   
1821 O O   . ALA B 33  ? 0.9646 0.5926 0.5909 0.2294  0.2526  0.0146  32  ALA D O   
1822 C CB  . ALA B 33  ? 0.9513 0.6251 0.6075 0.2649  0.2408  0.0218  32  ALA D CB  
1823 N N   . VAL B 34  ? 0.9502 0.5694 0.5743 0.2307  0.2312  0.0134  33  VAL D N   
1824 C CA  . VAL B 34  ? 0.8926 0.5060 0.5061 0.2141  0.2317  0.0089  33  VAL D CA  
1825 C C   . VAL B 34  ? 0.9035 0.4847 0.5015 0.1981  0.2261  0.0079  33  VAL D C   
1826 O O   . VAL B 34  ? 0.8894 0.4557 0.4842 0.2026  0.2163  0.0086  33  VAL D O   
1827 C CB  . VAL B 34  ? 0.8504 0.4905 0.4794 0.2084  0.2132  0.0101  33  VAL D CB  
1828 C CG1 . VAL B 34  ? 0.8715 0.5063 0.4961 0.1812  0.2014  0.0098  33  VAL D CG1 
1829 C CG2 . VAL B 34  ? 0.8496 0.5266 0.4942 0.2175  0.2196  0.0101  33  VAL D CG2 
1830 N N   . ALA B 35  ? 0.8878 0.4602 0.4763 0.1797  0.2320  0.0061  34  ALA D N   
1831 C CA  . ALA B 35  ? 0.8673 0.4148 0.4421 0.1614  0.2241  0.0048  34  ALA D CA  
1832 C C   . ALA B 35  ? 0.9005 0.4564 0.4743 0.1383  0.2185  0.0047  34  ALA D C   
1833 O O   . ALA B 35  ? 0.9166 0.4967 0.4998 0.1356  0.2232  0.0054  34  ALA D O   
1834 C CB  . ALA B 35  ? 0.8687 0.3920 0.4313 0.1610  0.2367  0.0033  34  ALA D CB  
1835 N N   . TRP B 36  ? 0.8619 0.3977 0.4233 0.1217  0.2091  0.0038  35  TRP D N   
1836 C CA  . TRP B 36  ? 0.8784 0.4162 0.4346 0.0993  0.2046  0.0038  35  TRP D CA  
1837 C C   . TRP B 36  ? 0.8979 0.4104 0.4359 0.0886  0.2122  0.0007  35  TRP D C   
1838 O O   . TRP B 36  ? 0.8855 0.3765 0.4142 0.0930  0.2110  -0.0012 35  TRP D O   
1839 C CB  . TRP B 36  ? 0.8267 0.3651 0.3839 0.0880  0.1827  0.0058  35  TRP D CB  
1840 C CG  . TRP B 36  ? 0.8506 0.4149 0.4251 0.0939  0.1741  0.0082  35  TRP D CG  
1841 C CD1 . TRP B 36  ? 0.8663 0.4359 0.4499 0.1099  0.1654  0.0091  35  TRP D CD1 
1842 C CD2 . TRP B 36  ? 0.8705 0.4603 0.4554 0.0833  0.1725  0.0097  35  TRP D CD2 
1843 N NE1 . TRP B 36  ? 0.8325 0.4296 0.4319 0.1106  0.1585  0.0106  35  TRP D NE1 
1844 C CE2 . TRP B 36  ? 0.8624 0.4726 0.4632 0.0937  0.1625  0.0110  35  TRP D CE2 
1845 C CE3 . TRP B 36  ? 0.9001 0.4982 0.4826 0.0657  0.1783  0.0101  35  TRP D CE3 
1846 C CZ2 . TRP B 36  ? 0.8882 0.5275 0.5028 0.0864  0.1583  0.0121  35  TRP D CZ2 
1847 C CZ3 . TRP B 36  ? 0.9120 0.5391 0.5083 0.0582  0.1745  0.0118  35  TRP D CZ3 
1848 C CH2 . TRP B 36  ? 0.8974 0.5450 0.5097 0.0683  0.1647  0.0125  35  TRP D CH2 
1849 N N   . TYR B 37  ? 0.8519 0.3683 0.3849 0.0739  0.2195  0.0001  36  TYR D N   
1850 C CA  . TYR B 37  ? 0.8617 0.3561 0.3771 0.0616  0.2250  -0.0031 36  TYR D CA  
1851 C C   . TYR B 37  ? 0.9063 0.4009 0.4146 0.0397  0.2150  -0.0018 36  TYR D C   
1852 O O   . TYR B 37  ? 0.9022 0.4170 0.4195 0.0325  0.2112  0.0012  36  TYR D O   
1853 C CB  . TYR B 37  ? 0.8994 0.3923 0.4105 0.0661  0.2473  -0.0062 36  TYR D CB  
1854 C CG  . TYR B 37  ? 0.9091 0.4003 0.4253 0.0881  0.2587  -0.0070 36  TYR D CG  
1855 C CD1 . TYR B 37  ? 0.8986 0.4134 0.4299 0.1028  0.2638  -0.0046 36  TYR D CD1 
1856 C CD2 . TYR B 37  ? 0.8861 0.3582 0.3992 0.0927  0.2591  -0.0081 36  TYR D CD2 
1857 C CE1 . TYR B 37  ? 0.8726 0.3876 0.4109 0.1227  0.2709  -0.0039 36  TYR D CE1 
1858 C CE2 . TYR B 37  ? 0.8806 0.3602 0.4099 0.1079  0.2608  -0.0042 36  TYR D CE2 
1859 C CZ  . TYR B 37  ? 0.9023 0.4023 0.4437 0.1231  0.2662  -0.0020 36  TYR D CZ  
1860 O OH  . TYR B 37  ? 0.9314 0.4391 0.4872 0.1378  0.2672  0.0025  36  TYR D OH  
1861 N N   . GLN B 38  ? 0.8947 0.3669 0.3862 0.0291  0.2116  -0.0044 37  GLN D N   
1862 C CA  . GLN B 38  ? 0.8960 0.3633 0.3759 0.0089  0.2055  -0.0037 37  GLN D CA  
1863 C C   . GLN B 38  ? 0.9115 0.3706 0.3799 0.0027  0.2217  -0.0076 37  GLN D C   
1864 O O   . GLN B 38  ? 0.9357 0.3789 0.3963 0.0089  0.2297  -0.0120 37  GLN D O   
1865 C CB  . GLN B 38  ? 0.9324 0.3805 0.4000 0.0022  0.1875  -0.0039 37  GLN D CB  
1866 C CG  . GLN B 38  ? 0.9224 0.3601 0.3737 -0.0173 0.1813  -0.0037 37  GLN D CG  
1867 C CD  . GLN B 38  ? 0.9343 0.3509 0.3711 -0.0197 0.1659  -0.0052 37  GLN D CD  
1868 O OE1 . GLN B 38  ? 0.9741 0.3771 0.4026 -0.0149 0.1702  -0.0099 37  GLN D OE1 
1869 N NE2 . GLN B 38  ? 0.8935 0.3077 0.3268 -0.0268 0.1479  -0.0016 37  GLN D NE2 
1870 N N   . GLN B 39  ? 0.9541 0.4240 0.4209 -0.0102 0.2262  -0.0060 38  GLN D N   
1871 C CA  . GLN B 39  ? 0.9144 0.3782 0.3694 -0.0179 0.2404  -0.0094 38  GLN D CA  
1872 C C   . GLN B 39  ? 0.9273 0.3876 0.3704 -0.0382 0.2321  -0.0073 38  GLN D C   
1873 O O   . GLN B 39  ? 0.9264 0.4017 0.3761 -0.0465 0.2253  -0.0025 38  GLN D O   
1874 C CB  . GLN B 39  ? 0.9179 0.4017 0.3834 -0.0107 0.2582  -0.0094 38  GLN D CB  
1875 C CG  . GLN B 39  ? 0.9301 0.4045 0.3845 -0.0102 0.2765  -0.0145 38  GLN D CG  
1876 C CD  . GLN B 39  ? 0.9360 0.4333 0.3988 -0.0069 0.2916  -0.0136 38  GLN D CD  
1877 O OE1 . GLN B 39  ? 0.9316 0.4530 0.4075 -0.0089 0.2875  -0.0090 38  GLN D OE1 
1878 N NE2 . GLN B 39  ? 0.9414 0.4376 0.4075 -0.0024 0.3027  -0.0174 38  GLN D NE2 
1879 N N   . LYS B 40  ? 0.9458 0.3858 0.3703 -0.0463 0.2323  -0.0112 39  LYS D N   
1880 C CA  . LYS B 40  ? 0.9451 0.3782 0.3537 -0.0637 0.2299  -0.0109 39  LYS D CA  
1881 C C   . LYS B 40  ? 0.9674 0.4063 0.3725 -0.0663 0.2490  -0.0138 39  LYS D C   
1882 O O   . LYS B 40  ? 0.9748 0.4152 0.3858 -0.0543 0.2627  -0.0178 39  LYS D O   
1883 C CB  . LYS B 40  ? 0.9477 0.3568 0.3385 -0.0675 0.2201  -0.0146 39  LYS D CB  
1884 C CG  . LYS B 40  ? 0.9365 0.3387 0.3306 -0.0604 0.2036  -0.0133 39  LYS D CG  
1885 C CD  . LYS B 40  ? 0.9419 0.3329 0.3226 -0.0717 0.1848  -0.0104 39  LYS D CD  
1886 C CE  . LYS B 40  ? 0.9576 0.3360 0.3354 -0.0631 0.1706  -0.0120 39  LYS D CE  
1887 N NZ  . LYS B 40  ? 1.0032 0.3650 0.3610 -0.0723 0.1555  -0.0121 39  LYS D NZ  
1888 N N   . PRO B 41  ? 1.0078 0.4489 0.4028 -0.0814 0.2503  -0.0121 40  PRO D N   
1889 C CA  . PRO B 41  ? 0.9750 0.4281 0.3740 -0.0824 0.2661  -0.0146 40  PRO D CA  
1890 C C   . PRO B 41  ? 0.9761 0.4190 0.3779 -0.0772 0.2692  -0.0223 40  PRO D C   
1891 O O   . PRO B 41  ? 1.0064 0.4323 0.3990 -0.0814 0.2595  -0.0254 40  PRO D O   
1892 C CB  . PRO B 41  ? 0.9872 0.4443 0.3759 -0.1006 0.2623  -0.0104 40  PRO D CB  
1893 C CG  . PRO B 41  ? 0.9850 0.4384 0.3711 -0.1074 0.2457  -0.0043 40  PRO D CG  
1894 C CD  . PRO B 41  ? 0.9752 0.4103 0.3588 -0.0973 0.2360  -0.0078 40  PRO D CD  
1895 N N   . GLY B 42  ? 0.9774 0.4312 0.3920 -0.0682 0.2825  -0.0252 41  GLY D N   
1896 C CA  . GLY B 42  ? 0.9731 0.4174 0.3918 -0.0634 0.2861  -0.0314 41  GLY D CA  
1897 C C   . GLY B 42  ? 1.0056 0.4374 0.4304 -0.0523 0.2825  -0.0334 41  GLY D C   
1898 O O   . GLY B 42  ? 1.0163 0.4379 0.4428 -0.0516 0.2827  -0.0376 41  GLY D O   
1899 N N   . LYS B 43  ? 0.9545 0.3875 0.3828 -0.0441 0.2791  -0.0301 42  LYS D N   
1900 C CA  . LYS B 43  ? 0.9447 0.3662 0.3784 -0.0345 0.2744  -0.0314 42  LYS D CA  
1901 C C   . LYS B 43  ? 0.9383 0.3697 0.3854 -0.0185 0.2808  -0.0286 42  LYS D C   
1902 O O   . LYS B 43  ? 0.9397 0.3861 0.3888 -0.0160 0.2851  -0.0253 42  LYS D O   
1903 C CB  . LYS B 43  ? 1.0182 0.4274 0.4402 -0.0404 0.2592  -0.0306 42  LYS D CB  
1904 C CG  . LYS B 43  ? 1.0077 0.4079 0.4161 -0.0552 0.2514  -0.0330 42  LYS D CG  
1905 C CD  . LYS B 43  ? 1.0851 0.4787 0.4984 -0.0555 0.2529  -0.0375 42  LYS D CD  
1906 C CE  . LYS B 43  ? 1.1820 0.5704 0.5831 -0.0692 0.2475  -0.0403 42  LYS D CE  
1907 N NZ  . LYS B 43  ? 1.1942 0.5737 0.5912 -0.0719 0.2349  -0.0414 42  LYS D NZ  
1908 N N   . ALA B 44  ? 0.9318 0.3569 0.3889 -0.0080 0.2818  -0.0292 43  ALA D N   
1909 C CA  . ALA B 44  ? 0.9310 0.3646 0.4008 0.0085  0.2865  -0.0260 43  ALA D CA  
1910 C C   . ALA B 44  ? 0.9219 0.3557 0.3888 0.0125  0.2771  -0.0233 43  ALA D C   
1911 O O   . ALA B 44  ? 0.9175 0.3396 0.3743 0.0050  0.2655  -0.0239 43  ALA D O   
1912 C CB  . ALA B 44  ? 0.9423 0.3683 0.4219 0.0170  0.2887  -0.0258 43  ALA D CB  
1913 N N   . PRO B 45  ? 0.9317 0.3797 0.4068 0.0244  0.2813  -0.0203 44  PRO D N   
1914 C CA  . PRO B 45  ? 0.9063 0.3545 0.3797 0.0309  0.2726  -0.0180 44  PRO D CA  
1915 C C   . PRO B 45  ? 0.9008 0.3346 0.3760 0.0355  0.2621  -0.0179 44  PRO D C   
1916 O O   . PRO B 45  ? 0.8933 0.3226 0.3770 0.0391  0.2644  -0.0176 44  PRO D O   
1917 C CB  . PRO B 45  ? 0.9038 0.3716 0.3914 0.0471  0.2812  -0.0153 44  PRO D CB  
1918 C CG  . PRO B 45  ? 0.9137 0.3956 0.4027 0.0415  0.2927  -0.0159 44  PRO D CG  
1919 C CD  . PRO B 45  ? 0.9193 0.3863 0.4043 0.0320  0.2939  -0.0193 44  PRO D CD  
1920 N N   . LYS B 46  ? 0.8964 0.3241 0.3625 0.0342  0.2499  -0.0176 45  LYS D N   
1921 C CA  . LYS B 46  ? 0.9250 0.3444 0.3949 0.0403  0.2382  -0.0166 45  LYS D CA  
1922 C C   . LYS B 46  ? 0.9126 0.3396 0.3896 0.0553  0.2340  -0.0142 45  LYS D C   
1923 O O   . LYS B 46  ? 0.9002 0.3402 0.3818 0.0520  0.2253  -0.0113 45  LYS D O   
1924 C CB  . LYS B 46  ? 0.9346 0.3401 0.3892 0.0275  0.2239  -0.0186 45  LYS D CB  
1925 C CG  . LYS B 46  ? 1.0062 0.4064 0.4508 0.0115  0.2276  -0.0213 45  LYS D CG  
1926 C CD  . LYS B 46  ? 1.1115 0.5005 0.5455 0.0011  0.2134  -0.0226 45  LYS D CD  
1927 C CE  . LYS B 46  ? 1.1603 0.5518 0.6064 0.0070  0.2092  -0.0210 45  LYS D CE  
1928 N NZ  . LYS B 46  ? 1.2136 0.6008 0.6524 -0.0044 0.2007  -0.0228 45  LYS D NZ  
1929 N N   . LEU B 47  ? 0.9437 0.3756 0.4361 0.0681  0.2329  -0.0107 46  LEU D N   
1930 C CA  . LEU B 47  ? 0.9203 0.3605 0.4217 0.0832  0.2265  -0.0081 46  LEU D CA  
1931 C C   . LEU B 47  ? 0.8495 0.2800 0.3420 0.0801  0.2087  -0.0091 46  LEU D C   
1932 O O   . LEU B 47  ? 0.8558 0.2782 0.3429 0.0712  0.1993  -0.0093 46  LEU D O   
1933 C CB  . LEU B 47  ? 0.9179 0.3669 0.4362 0.0951  0.2289  -0.0030 46  LEU D CB  
1934 C CG  . LEU B 47  ? 0.8991 0.3600 0.4295 0.1113  0.2216  0.0009  46  LEU D CG  
1935 C CD1 . LEU B 47  ? 0.8693 0.3451 0.4084 0.1242  0.2310  0.0017  46  LEU D CD1 
1936 C CD2 . LEU B 47  ? 0.8994 0.3643 0.4392 0.1153  0.2207  0.0053  46  LEU D CD2 
1937 N N   . LEU B 48  ? 0.8416 0.2858 0.3434 0.0850  0.1985  -0.0061 47  LEU D N   
1938 C CA  . LEU B 48  ? 0.9094 0.3508 0.4103 0.0822  0.1771  -0.0044 47  LEU D CA  
1939 C C   . LEU B 48  ? 0.8843 0.3330 0.3969 0.1004  0.1703  -0.0021 47  LEU D C   
1940 O O   . LEU B 48  ? 0.8724 0.3105 0.3806 0.1052  0.1608  -0.0026 47  LEU D O   
1941 C CB  . LEU B 48  ? 0.8779 0.3297 0.3801 0.0671  0.1647  -0.0017 47  LEU D CB  
1942 C CG  . LEU B 48  ? 0.8887 0.3346 0.3789 0.0482  0.1699  -0.0032 47  LEU D CG  
1943 C CD1 . LEU B 48  ? 0.8917 0.3535 0.3877 0.0365  0.1629  0.0005  47  LEU D CD1 
1944 C CD2 . LEU B 48  ? 0.8516 0.2754 0.3232 0.0382  0.1615  -0.0060 47  LEU D CD2 
1945 N N   . ILE B 49  ? 0.8520 0.3211 0.3798 0.1109  0.1747  0.0005  48  ILE D N   
1946 C CA  . ILE B 49  ? 0.8078 0.2880 0.3482 0.1287  0.1681  0.0029  48  ILE D CA  
1947 C C   . ILE B 49  ? 0.8837 0.3718 0.4317 0.1459  0.1870  0.0031  48  ILE D C   
1948 O O   . ILE B 49  ? 0.8995 0.3995 0.4513 0.1434  0.1990  0.0030  48  ILE D O   
1949 C CB  . ILE B 49  ? 0.8616 0.3623 0.4137 0.1245  0.1533  0.0058  48  ILE D CB  
1950 C CG1 . ILE B 49  ? 0.8595 0.3498 0.4026 0.1098  0.1325  0.0061  48  ILE D CG1 
1951 C CG2 . ILE B 49  ? 0.8338 0.3512 0.4009 0.1444  0.1511  0.0077  48  ILE D CG2 
1952 C CD1 . ILE B 49  ? 0.8519 0.3208 0.3830 0.1132  0.1245  0.0045  48  ILE D CD1 
1953 N N   . TYR B 50  ? 0.9099 0.4069 0.4692 0.1575  0.1843  0.0072  49  TYR D N   
1954 C CA  . TYR B 50  ? 0.8542 0.3697 0.4282 0.1700  0.1952  0.0113  49  TYR D CA  
1955 C C   . TYR B 50  ? 0.8821 0.4167 0.4703 0.1863  0.1863  0.0144  49  TYR D C   
1956 O O   . TYR B 50  ? 0.8767 0.4116 0.4660 0.1875  0.1708  0.0147  49  TYR D O   
1957 C CB  . TYR B 50  ? 0.8044 0.3188 0.3811 0.1660  0.2003  0.0149  49  TYR D CB  
1958 C CG  . TYR B 50  ? 0.8019 0.3160 0.3795 0.1631  0.1882  0.0167  49  TYR D CG  
1959 C CD1 . TYR B 50  ? 0.8352 0.3356 0.4015 0.1494  0.1819  0.0138  49  TYR D CD1 
1960 C CD2 . TYR B 50  ? 0.8051 0.3346 0.3944 0.1739  0.1832  0.0210  49  TYR D CD2 
1961 C CE1 . TYR B 50  ? 0.8459 0.3493 0.4134 0.1470  0.1712  0.0148  49  TYR D CE1 
1962 C CE2 . TYR B 50  ? 0.8022 0.3337 0.3921 0.1707  0.1730  0.0218  49  TYR D CE2 
1963 C CZ  . TYR B 50  ? 0.8285 0.3473 0.4077 0.1576  0.1672  0.0185  49  TYR D CZ  
1964 O OH  . TYR B 50  ? 0.8785 0.4008 0.4582 0.1547  0.1574  0.0187  49  TYR D OH  
1965 N N   . SER B 51  ? 0.8747 0.4270 0.4741 0.1986  0.1956  0.0166  50  SER D N   
1966 C CA  . SER B 51  ? 0.8500 0.4242 0.4640 0.2148  0.1888  0.0195  50  SER D CA  
1967 C C   . SER B 51  ? 0.8240 0.3981 0.4368 0.2179  0.1752  0.0163  50  SER D C   
1968 O O   . SER B 51  ? 0.8383 0.4165 0.4560 0.2209  0.1603  0.0180  50  SER D O   
1969 C CB  . SER B 51  ? 0.8806 0.4612 0.5017 0.2175  0.1834  0.0246  50  SER D CB  
1970 O OG  . SER B 51  ? 0.9441 0.5470 0.5787 0.2323  0.1778  0.0272  50  SER D OG  
1971 N N   . ALA B 52  ? 0.8438 0.4141 0.4496 0.2142  0.1800  0.0115  51  ALA D N   
1972 C CA  . ALA B 52  ? 0.8303 0.4173 0.4451 0.2027  0.1609  0.0121  51  ALA D CA  
1973 C C   . ALA B 52  ? 0.8115 0.3793 0.4164 0.1887  0.1429  0.0118  51  ALA D C   
1974 O O   . ALA B 52  ? 0.8445 0.4125 0.4463 0.1685  0.1343  0.0115  51  ALA D O   
1975 C CB  . ALA B 52  ? 0.8179 0.4302 0.4490 0.2204  0.1538  0.0133  51  ALA D CB  
1976 N N   . SER B 53  ? 0.8005 0.3516 0.3993 0.1991  0.1373  0.0121  52  SER D N   
1977 C CA  . SER B 53  ? 0.7651 0.3023 0.3560 0.1895  0.1179  0.0119  52  SER D CA  
1978 C C   . SER B 53  ? 0.7625 0.2813 0.3419 0.1834  0.1178  0.0114  52  SER D C   
1979 O O   . SER B 53  ? 0.7576 0.2697 0.3315 0.1764  0.1014  0.0111  52  SER D O   
1980 C CB  . SER B 53  ? 0.8351 0.3840 0.4359 0.2038  0.1023  0.0132  52  SER D CB  
1981 O OG  . SER B 53  ? 0.8855 0.4530 0.4990 0.2163  0.1062  0.0158  52  SER D OG  
1982 N N   . SER B 54  ? 0.8155 0.3381 0.3966 0.1809  0.1323  0.0125  53  SER D N   
1983 C CA  . SER B 54  ? 0.8117 0.3325 0.3901 0.1718  0.1287  0.0132  53  SER D CA  
1984 C C   . SER B 54  ? 0.8210 0.3201 0.3823 0.1552  0.1322  0.0100  53  SER D C   
1985 O O   . SER B 54  ? 0.8305 0.3210 0.3859 0.1505  0.1472  0.0084  53  SER D O   
1986 C CB  . SER B 54  ? 0.8059 0.3412 0.3951 0.1775  0.1396  0.0169  53  SER D CB  
1987 O OG  . SER B 54  ? 0.8110 0.3662 0.4147 0.1925  0.1386  0.0197  53  SER D OG  
1988 N N   . LEU B 55  ? 0.7869 0.2795 0.3406 0.1464  0.1181  0.0087  54  LEU D N   
1989 C CA  . LEU B 55  ? 0.8523 0.3267 0.3897 0.1303  0.1190  0.0056  54  LEU D CA  
1990 C C   . LEU B 55  ? 0.8426 0.3190 0.3810 0.1255  0.1331  0.0059  54  LEU D C   
1991 O O   . LEU B 55  ? 0.8800 0.3658 0.4239 0.1267  0.1299  0.0073  54  LEU D O   
1992 C CB  . LEU B 55  ? 0.8021 0.2730 0.3323 0.1240  0.0992  0.0046  54  LEU D CB  
1993 C CG  . LEU B 55  ? 0.8441 0.2952 0.3554 0.1075  0.0967  0.0016  54  LEU D CG  
1994 C CD1 . LEU B 55  ? 0.8368 0.2717 0.3391 0.1033  0.0938  0.0012  54  LEU D CD1 
1995 C CD2 . LEU B 55  ? 0.8327 0.2846 0.3375 0.1022  0.0797  0.0008  54  LEU D CD2 
1996 N N   . TYR B 56  ? 0.8127 0.2800 0.3454 0.1196  0.1486  0.0045  55  TYR D N   
1997 C CA  . TYR B 56  ? 0.8772 0.3437 0.4097 0.1129  0.1602  0.0047  55  TYR D CA  
1998 C C   . TYR B 56  ? 0.8623 0.3231 0.3857 0.1015  0.1507  0.0026  55  TYR D C   
1999 O O   . TYR B 56  ? 0.8706 0.3215 0.3821 0.0935  0.1402  0.0000  55  TYR D O   
2000 C CB  . TYR B 56  ? 0.9073 0.3644 0.4336 0.1063  0.1765  0.0028  55  TYR D CB  
2001 C CG  . TYR B 56  ? 0.9222 0.3779 0.4497 0.0999  0.1884  0.0033  55  TYR D CG  
2002 C CD1 . TYR B 56  ? 0.9192 0.3845 0.4584 0.1080  0.1945  0.0073  55  TYR D CD1 
2003 C CD2 . TYR B 56  ? 0.9282 0.3721 0.4446 0.0855  0.1936  -0.0003 55  TYR D CD2 
2004 C CE1 . TYR B 56  ? 0.9276 0.3884 0.4666 0.1017  0.2050  0.0075  55  TYR D CE1 
2005 C CE2 . TYR B 56  ? 0.9249 0.3667 0.4430 0.0797  0.2039  -0.0002 55  TYR D CE2 
2006 C CZ  . TYR B 56  ? 0.9241 0.3732 0.4530 0.0877  0.2095  0.0036  55  TYR D CZ  
2007 O OH  . TYR B 56  ? 0.9431 0.3872 0.4719 0.0813  0.2191  0.0034  55  TYR D OH  
2008 N N   . SER B 57  ? 0.8806 0.3477 0.4095 0.1009  0.1541  0.0039  56  SER D N   
2009 C CA  . SER B 57  ? 0.8924 0.3566 0.4142 0.0917  0.1460  0.0017  56  SER D CA  
2010 C C   . SER B 57  ? 0.8608 0.3108 0.3682 0.0776  0.1473  -0.0020 56  SER D C   
2011 O O   . SER B 57  ? 0.9091 0.3519 0.4135 0.0731  0.1599  -0.0030 56  SER D O   
2012 C CB  . SER B 57  ? 0.9156 0.3845 0.4436 0.0907  0.1540  0.0029  56  SER D CB  
2013 O OG  . SER B 57  ? 0.9778 0.4404 0.4968 0.0788  0.1502  -0.0005 56  SER D OG  
2014 N N   . GLY B 58  ? 0.8567 0.3038 0.3553 0.0709  0.1341  -0.0040 57  GLY D N   
2015 C CA  . GLY B 58  ? 0.9164 0.3515 0.4004 0.0574  0.1323  -0.0072 57  GLY D CA  
2016 C C   . GLY B 58  ? 0.8950 0.3200 0.3674 0.0545  0.1233  -0.0079 57  GLY D C   
2017 O O   . GLY B 58  ? 0.9087 0.3263 0.3682 0.0457  0.1125  -0.0094 57  GLY D O   
2018 N N   . VAL B 59  ? 0.8780 0.3021 0.3546 0.0617  0.1271  -0.0067 58  VAL D N   
2019 C CA  . VAL B 59  ? 0.9065 0.3182 0.3725 0.0581  0.1203  -0.0075 58  VAL D CA  
2020 C C   . VAL B 59  ? 0.8914 0.3027 0.3528 0.0592  0.0982  -0.0065 58  VAL D C   
2021 O O   . VAL B 59  ? 0.8989 0.3235 0.3713 0.0700  0.0900  -0.0047 58  VAL D O   
2022 C CB  . VAL B 59  ? 0.8957 0.3094 0.3708 0.0684  0.1298  -0.0064 58  VAL D CB  
2023 C CG1 . VAL B 59  ? 0.8933 0.2969 0.3615 0.0654  0.1195  -0.0059 58  VAL D CG1 
2024 C CG2 . VAL B 59  ? 0.8824 0.2946 0.3579 0.0655  0.1515  -0.0080 58  VAL D CG2 
2025 N N   . PRO B 60  ? 0.9032 0.3002 0.3487 0.0485  0.0876  -0.0072 59  PRO D N   
2026 C CA  . PRO B 60  ? 0.9150 0.3114 0.3556 0.0495  0.0655  -0.0057 59  PRO D CA  
2027 C C   . PRO B 60  ? 0.9034 0.3041 0.3544 0.0601  0.0567  -0.0032 59  PRO D C   
2028 O O   . PRO B 60  ? 0.9359 0.3331 0.3927 0.0634  0.0657  -0.0020 59  PRO D O   
2029 C CB  . PRO B 60  ? 0.8930 0.2713 0.3137 0.0336  0.0596  -0.0062 59  PRO D CB  
2030 C CG  . PRO B 60  ? 0.9383 0.3131 0.3536 0.0248  0.0766  -0.0089 59  PRO D CG  
2031 C CD  . PRO B 60  ? 0.9194 0.3011 0.3495 0.0334  0.0949  -0.0094 59  PRO D CD  
2032 N N   . SER B 61  ? 0.8694 0.2774 0.3217 0.0656  0.0383  -0.0023 60  SER D N   
2033 C CA  . SER B 61  ? 0.9153 0.3300 0.3787 0.0759  0.0285  -0.0001 60  SER D CA  
2034 C C   . SER B 61  ? 0.9077 0.3061 0.3637 0.0681  0.0225  0.0024  60  SER D C   
2035 O O   . SER B 61  ? 0.9104 0.3132 0.3762 0.0767  0.0171  0.0047  60  SER D O   
2036 C CB  . SER B 61  ? 0.9531 0.3800 0.4190 0.0830  0.0095  -0.0005 60  SER D CB  
2037 O OG  . SER B 61  ? 0.9970 0.4355 0.4649 0.0867  0.0118  -0.0020 60  SER D OG  
2038 N N   . ARG B 62  ? 0.9263 0.3068 0.3653 0.0516  0.0229  0.0027  61  ARG D N   
2039 C CA  . ARG B 62  ? 0.8832 0.2691 0.3258 0.0404  0.0174  0.0062  61  ARG D CA  
2040 C C   . ARG B 62  ? 0.9153 0.3230 0.3785 0.0416  0.0331  0.0077  61  ARG D C   
2041 O O   . ARG B 62  ? 0.9762 0.3940 0.4465 0.0337  0.0292  0.0103  61  ARG D O   
2042 C CB  . ARG B 62  ? 0.9141 0.2859 0.3381 0.0212  0.0148  0.0068  61  ARG D CB  
2043 C CG  . ARG B 62  ? 0.9221 0.2924 0.3409 0.0132  0.0328  0.0046  61  ARG D CG  
2044 C CD  . ARG B 62  ? 0.9324 0.2886 0.3318 -0.0045 0.0286  0.0055  61  ARG D CD  
2045 N NE  . ARG B 62  ? 0.9599 0.3147 0.3537 -0.0112 0.0453  0.0028  61  ARG D NE  
2046 C CZ  . ARG B 62  ? 0.9888 0.3321 0.3693 -0.0091 0.0468  -0.0015 61  ARG D CZ  
2047 N NH1 . ARG B 62  ? 0.9808 0.3233 0.3579 0.0005  0.0339  -0.0032 61  ARG D NH1 
2048 N NH2 . ARG B 62  ? 1.0060 0.3480 0.3807 -0.0168 0.0616  -0.0043 61  ARG D NH2 
2049 N N   . PHE B 63  ? 0.8400 0.2553 0.3122 0.0514  0.0505  0.0058  62  PHE D N   
2050 C CA  . PHE B 63  ? 0.8583 0.2945 0.3489 0.0556  0.0654  0.0070  62  PHE D CA  
2051 C C   . PHE B 63  ? 0.8703 0.3200 0.3773 0.0752  0.0628  0.0077  62  PHE D C   
2052 O O   . PHE B 63  ? 0.8888 0.3307 0.3932 0.0878  0.0567  0.0067  62  PHE D O   
2053 C CB  . PHE B 63  ? 0.9013 0.3364 0.3905 0.0552  0.0869  0.0045  62  PHE D CB  
2054 C CG  . PHE B 63  ? 0.8579 0.2843 0.3334 0.0363  0.0915  0.0039  62  PHE D CG  
2055 C CD1 . PHE B 63  ? 0.8521 0.2915 0.3334 0.0253  0.0991  0.0058  62  PHE D CD1 
2056 C CD2 . PHE B 63  ? 0.8609 0.2673 0.3174 0.0297  0.0876  0.0012  62  PHE D CD2 
2057 C CE1 . PHE B 63  ? 0.8669 0.2982 0.3348 0.0081  0.1035  0.0055  62  PHE D CE1 
2058 C CE2 . PHE B 63  ? 0.8824 0.2808 0.3254 0.0130  0.0918  0.0005  62  PHE D CE2 
2059 C CZ  . PHE B 63  ? 0.8638 0.2738 0.3122 0.0023  0.0998  0.0029  62  PHE D CZ  
2060 N N   . SER B 64  ? 0.8290 0.3003 0.3528 0.0779  0.0673  0.0095  63  SER D N   
2061 C CA  . SER B 64  ? 0.7957 0.2813 0.3346 0.0960  0.0627  0.0103  63  SER D CA  
2062 C C   . SER B 64  ? 0.8072 0.3193 0.3642 0.0983  0.0732  0.0115  63  SER D C   
2063 O O   . SER B 64  ? 0.8352 0.3552 0.3931 0.0827  0.0762  0.0122  63  SER D O   
2064 C CB  . SER B 64  ? 0.8827 0.3644 0.4192 0.0952  0.0394  0.0113  63  SER D CB  
2065 O OG  . SER B 64  ? 0.8367 0.3324 0.3808 0.0837  0.0332  0.0128  63  SER D OG  
2066 N N   . GLY B 65  ? 0.8198 0.3463 0.3907 0.1183  0.0782  0.0116  64  GLY D N   
2067 C CA  . GLY B 65  ? 0.8216 0.3751 0.4096 0.1244  0.0894  0.0122  64  GLY D CA  
2068 C C   . GLY B 65  ? 0.7881 0.3590 0.3910 0.1428  0.0816  0.0128  64  GLY D C   
2069 O O   . GLY B 65  ? 0.8044 0.3647 0.4039 0.1531  0.0703  0.0128  64  GLY D O   
2070 N N   . SER B 66  ? 0.7683 0.3676 0.3876 0.1474  0.0876  0.0130  65  SER D N   
2071 C CA  . SER B 66  ? 0.7934 0.4132 0.4280 0.1659  0.0815  0.0131  65  SER D CA  
2072 C C   . SER B 66  ? 0.8247 0.4781 0.4765 0.1694  0.0915  0.0127  65  SER D C   
2073 O O   . SER B 66  ? 0.8290 0.4910 0.4814 0.1539  0.0989  0.0126  65  SER D O   
2074 C CB  . SER B 66  ? 0.9069 0.5246 0.5416 0.1608  0.0579  0.0130  65  SER D CB  
2075 O OG  . SER B 66  ? 0.8877 0.4992 0.5227 0.1808  0.0506  0.0131  65  SER D OG  
2076 N N   . ARG B 67  ? 0.8788 0.5523 0.5442 0.1909  0.0916  0.0125  66  ARG D N   
2077 C CA  . ARG B 67  ? 0.8686 0.5770 0.5509 0.1989  0.1011  0.0118  66  ARG D CA  
2078 C C   . ARG B 67  ? 0.8518 0.5850 0.5491 0.2033  0.0850  0.0106  66  ARG D C   
2079 O O   . ARG B 67  ? 0.8659 0.5908 0.5624 0.2141  0.0721  0.0107  66  ARG D O   
2080 C CB  . ARG B 67  ? 0.9066 0.6194 0.5912 0.2242  0.1196  0.0123  66  ARG D CB  
2081 C CG  . ARG B 67  ? 0.8943 0.6464 0.5972 0.2387  0.1266  0.0112  66  ARG D CG  
2082 C CD  . ARG B 67  ? 0.8846 0.6378 0.5879 0.2676  0.1414  0.0121  66  ARG D CD  
2083 N NE  . ARG B 67  ? 0.9141 0.6557 0.6158 0.2842  0.1317  0.0132  66  ARG D NE  
2084 C CZ  . ARG B 67  ? 0.9651 0.7299 0.6799 0.3011  0.1232  0.0126  66  ARG D CZ  
2085 N NH1 . ARG B 67  ? 0.9831 0.7853 0.7141 0.3034  0.1227  0.0106  66  ARG D NH1 
2086 N NH2 . ARG B 67  ? 0.9695 0.7211 0.6809 0.3161  0.1149  0.0139  66  ARG D NH2 
2087 N N   . SER B 68  ? 0.8766 0.6409 0.5875 0.1946  0.0857  0.0091  67  SER D N   
2088 C CA  . SER B 68  ? 0.8933 0.6864 0.6205 0.1988  0.0721  0.0071  67  SER D CA  
2089 C C   . SER B 68  ? 0.9544 0.7877 0.6984 0.2052  0.0849  0.0054  67  SER D C   
2090 O O   . SER B 68  ? 0.9469 0.7971 0.6960 0.1860  0.0873  0.0046  67  SER D O   
2091 C CB  . SER B 68  ? 0.8739 0.6612 0.5985 0.1739  0.0531  0.0063  67  SER D CB  
2092 O OG  . SER B 68  ? 0.8612 0.6845 0.6036 0.1701  0.0462  0.0036  67  SER D OG  
2093 N N   . GLY B 69  ? 1.0254 0.8748 0.7776 0.2328  0.0932  0.0051  68  GLY D N   
2094 C CA  . GLY B 69  ? 1.0183 0.9061 0.7850 0.2425  0.1065  0.0034  68  GLY D CA  
2095 C C   . GLY B 69  ? 0.9904 0.8688 0.7479 0.2407  0.1273  0.0049  68  GLY D C   
2096 O O   . GLY B 69  ? 0.9794 0.8272 0.7226 0.2504  0.1367  0.0070  68  GLY D O   
2097 N N   . THR B 70  ? 0.9624 0.8674 0.7280 0.2277  0.1347  0.0035  69  THR D N   
2098 C CA  . THR B 70  ? 0.9694 0.8682 0.7266 0.2243  0.1542  0.0045  69  THR D CA  
2099 C C   . THR B 70  ? 0.9944 0.8615 0.7360 0.1972  0.1523  0.0061  69  THR D C   
2100 O O   . THR B 70  ? 0.9695 0.8225 0.7004 0.1946  0.1677  0.0070  69  THR D O   
2101 C CB  . THR B 70  ? 0.9566 0.9005 0.7291 0.2233  0.1636  0.0022  69  THR D CB  
2102 O OG1 . THR B 70  ? 0.9852 0.9404 0.7621 0.1931  0.1551  0.0016  69  THR D OG1 
2103 C CG2 . THR B 70  ? 0.9270 0.9096 0.7178 0.2452  0.1598  -0.0003 69  THR D CG2 
2104 N N   . ASP B 71  ? 0.9423 0.7972 0.6815 0.1778  0.1337  0.0064  70  ASP D N   
2105 C CA  . ASP B 71  ? 0.9098 0.7381 0.6345 0.1512  0.1303  0.0079  70  ASP D CA  
2106 C C   . ASP B 71  ? 0.9170 0.7015 0.6232 0.1538  0.1265  0.0095  70  ASP D C   
2107 O O   . ASP B 71  ? 0.9137 0.6877 0.6195 0.1653  0.1146  0.0096  70  ASP D O   
2108 C CB  . ASP B 71  ? 0.9312 0.7689 0.6611 0.1275  0.1126  0.0074  70  ASP D CB  
2109 C CG  . ASP B 71  ? 0.9833 0.8682 0.7337 0.1241  0.1140  0.0051  70  ASP D CG  
2110 O OD1 . ASP B 71  ? 0.9781 0.8874 0.7356 0.1307  0.1308  0.0044  70  ASP D OD1 
2111 O OD2 . ASP B 71  ? 0.9884 0.8866 0.7477 0.1144  0.0978  0.0036  70  ASP D OD2 
2112 N N   . PHE B 72  ? 0.9261 0.6862 0.6169 0.1426  0.1361  0.0106  71  PHE D N   
2113 C CA  . PHE B 72  ? 0.8786 0.5984 0.5508 0.1411  0.1334  0.0116  71  PHE D CA  
2114 C C   . PHE B 72  ? 0.8780 0.5798 0.5381 0.1133  0.1240  0.0124  71  PHE D C   
2115 O O   . PHE B 72  ? 0.9203 0.6383 0.5844 0.0958  0.1255  0.0126  71  PHE D O   
2116 C CB  . PHE B 72  ? 0.8541 0.5598 0.5174 0.1535  0.1538  0.0114  71  PHE D CB  
2117 C CG  . PHE B 72  ? 0.8341 0.5509 0.5054 0.1823  0.1626  0.0112  71  PHE D CG  
2118 C CD1 . PHE B 72  ? 0.8598 0.6123 0.5469 0.1940  0.1702  0.0104  71  PHE D CD1 
2119 C CD2 . PHE B 72  ? 0.8768 0.5693 0.5397 0.1981  0.1627  0.0117  71  PHE D CD2 
2120 C CE1 . PHE B 72  ? 0.9090 0.6712 0.6021 0.2221  0.1780  0.0103  71  PHE D CE1 
2121 C CE2 . PHE B 72  ? 0.8555 0.5567 0.5246 0.2253  0.1708  0.0121  71  PHE D CE2 
2122 C CZ  . PHE B 72  ? 0.8689 0.6040 0.5524 0.2378  0.1786  0.0114  71  PHE D CZ  
2123 N N   . THR B 73  ? 0.7904 0.4596 0.4351 0.1093  0.1139  0.0130  72  THR D N   
2124 C CA  . THR B 73  ? 0.7953 0.4463 0.4270 0.0848  0.1027  0.0139  72  THR D CA  
2125 C C   . THR B 73  ? 0.8480 0.4626 0.4596 0.0828  0.1013  0.0139  72  THR D C   
2126 O O   . THR B 73  ? 0.8398 0.4409 0.4482 0.0977  0.0965  0.0135  72  THR D O   
2127 C CB  . THR B 73  ? 0.8169 0.4717 0.4527 0.0772  0.0811  0.0142  72  THR D CB  
2128 O OG1 . THR B 73  ? 0.7984 0.4462 0.4360 0.0961  0.0712  0.0136  72  THR D OG1 
2129 C CG2 . THR B 73  ? 0.8230 0.5137 0.4771 0.0713  0.0804  0.0137  72  THR D CG2 
2130 N N   . LEU B 74  ? 0.8727 0.4724 0.4704 0.0638  0.1043  0.0144  73  LEU D N   
2131 C CA  . LEU B 74  ? 0.8508 0.4173 0.4283 0.0582  0.0997  0.0140  73  LEU D CA  
2132 C C   . LEU B 74  ? 0.8352 0.3888 0.4017 0.0387  0.0819  0.0155  73  LEU D C   
2133 O O   . LEU B 74  ? 0.8362 0.4016 0.4056 0.0224  0.0811  0.0169  73  LEU D O   
2134 C CB  . LEU B 74  ? 0.8465 0.4035 0.4141 0.0531  0.1177  0.0129  73  LEU D CB  
2135 C CG  . LEU B 74  ? 0.8267 0.3527 0.3730 0.0449  0.1154  0.0118  73  LEU D CG  
2136 C CD1 . LEU B 74  ? 0.8364 0.3486 0.3791 0.0623  0.1207  0.0096  73  LEU D CD1 
2137 C CD2 . LEU B 74  ? 0.8699 0.3949 0.4089 0.0315  0.1297  0.0113  73  LEU D CD2 
2138 N N   . THR B 75  ? 0.8221 0.3518 0.3756 0.0407  0.0676  0.0152  74  THR D N   
2139 C CA  . THR B 75  ? 0.8338 0.3450 0.3719 0.0235  0.0510  0.0165  74  THR D CA  
2140 C C   . THR B 75  ? 0.8394 0.3211 0.3559 0.0211  0.0488  0.0154  74  THR D C   
2141 O O   . THR B 75  ? 0.8577 0.3318 0.3724 0.0359  0.0526  0.0134  74  THR D O   
2142 C CB  . THR B 75  ? 0.8951 0.4060 0.4365 0.0278  0.0302  0.0169  74  THR D CB  
2143 O OG1 . THR B 75  ? 0.8693 0.3661 0.4055 0.0449  0.0234  0.0155  74  THR D OG1 
2144 C CG2 . THR B 75  ? 0.8250 0.3675 0.3893 0.0323  0.0299  0.0171  74  THR D CG2 
2145 N N   . ILE B 76  ? 0.8540 0.3194 0.3535 0.0024  0.0424  0.0167  75  ILE D N   
2146 C CA  . ILE B 76  ? 0.8611 0.2989 0.3381 -0.0012 0.0369  0.0155  75  ILE D CA  
2147 C C   . ILE B 76  ? 0.9466 0.3680 0.4110 -0.0071 0.0146  0.0170  75  ILE D C   
2148 O O   . ILE B 76  ? 0.9374 0.3580 0.3980 -0.0229 0.0080  0.0196  75  ILE D O   
2149 C CB  . ILE B 76  ? 0.8731 0.3033 0.3375 -0.0164 0.0490  0.0155  75  ILE D CB  
2150 C CG1 . ILE B 76  ? 0.8668 0.3160 0.3450 -0.0123 0.0711  0.0143  75  ILE D CG1 
2151 C CG2 . ILE B 76  ? 0.8929 0.2991 0.3371 -0.0150 0.0466  0.0129  75  ILE D CG2 
2152 C CD1 . ILE B 76  ? 0.8785 0.3350 0.3549 -0.0294 0.0807  0.0160  75  ILE D CD1 
2153 N N   . SER B 77  ? 0.9149 0.3234 0.3725 0.0058  0.0030  0.0154  76  SER D N   
2154 C CA  . SER B 77  ? 0.9182 0.3141 0.3668 0.0051  -0.0188 0.0165  76  SER D CA  
2155 C C   . SER B 77  ? 1.0089 0.3797 0.4320 -0.0116 -0.0286 0.0179  76  SER D C   
2156 O O   . SER B 77  ? 1.0110 0.3699 0.4247 -0.0171 -0.0457 0.0195  76  SER D O   
2157 C CB  . SER B 77  ? 0.8931 0.2838 0.3415 0.0250  -0.0276 0.0143  76  SER D CB  
2158 O OG  . SER B 77  ? 0.9299 0.3026 0.3606 0.0270  -0.0274 0.0122  76  SER D OG  
2159 N N   . SER B 78  ? 1.0058 0.3676 0.4165 -0.0193 -0.0180 0.0172  77  SER D N   
2160 C CA  . SER B 78  ? 1.0401 0.3802 0.4267 -0.0361 -0.0248 0.0190  77  SER D CA  
2161 C C   . SER B 78  ? 1.0670 0.4075 0.4484 -0.0428 -0.0073 0.0178  77  SER D C   
2162 O O   . SER B 78  ? 1.0941 0.4290 0.4696 -0.0340 -0.0028 0.0143  77  SER D O   
2163 C CB  . SER B 78  ? 1.0744 0.3893 0.4386 -0.0306 -0.0433 0.0180  77  SER D CB  
2164 O OG  . SER B 78  ? 1.1421 0.4515 0.4945 -0.0289 -0.0374 0.0146  77  SER D OG  
2165 N N   . LEU B 79  ? 1.0459 0.3944 0.4302 -0.0585 0.0028  0.0204  78  LEU D N   
2166 C CA  . LEU B 79  ? 1.0322 0.3824 0.4117 -0.0662 0.0198  0.0194  78  LEU D CA  
2167 C C   . LEU B 79  ? 1.0613 0.3884 0.4161 -0.0669 0.0159  0.0170  78  LEU D C   
2168 O O   . LEU B 79  ? 1.1017 0.4090 0.4389 -0.0654 -0.0012 0.0173  78  LEU D O   
2169 C CB  . LEU B 79  ? 0.9992 0.3546 0.3776 -0.0858 0.0254  0.0234  78  LEU D CB  
2170 C CG  . LEU B 79  ? 0.9765 0.3619 0.3797 -0.0864 0.0416  0.0240  78  LEU D CG  
2171 C CD1 . LEU B 79  ? 0.9882 0.3765 0.3851 -0.1060 0.0508  0.0270  78  LEU D CD1 
2172 C CD2 . LEU B 79  ? 0.9382 0.3365 0.3547 -0.0706 0.0570  0.0198  78  LEU D CD2 
2173 N N   . GLN B 80  ? 1.0416 0.3717 0.3945 -0.0686 0.0315  0.0143  79  GLN D N   
2174 C CA  . GLN B 80  ? 1.0693 0.3813 0.4000 -0.0700 0.0301  0.0112  79  GLN D CA  
2175 C C   . GLN B 80  ? 1.0593 0.3742 0.3850 -0.0836 0.0454  0.0116  79  GLN D C   
2176 O O   . GLN B 80  ? 1.0229 0.3555 0.3645 -0.0886 0.0577  0.0136  79  GLN D O   
2177 C CB  . GLN B 80  ? 1.0762 0.3907 0.4117 -0.0541 0.0344  0.0056  79  GLN D CB  
2178 C CG  . GLN B 80  ? 1.0653 0.3764 0.4036 -0.0407 0.0188  0.0053  79  GLN D CG  
2179 C CD  . GLN B 80  ? 1.1552 0.4592 0.4756 -0.0398 0.0026  0.0029  79  GLN D CD  
2180 O OE1 . GLN B 80  ? 1.2350 0.5346 0.5491 -0.0417 -0.0142 0.0048  79  GLN D OE1 
2181 N NE2 . GLN B 80  ? 1.1834 0.4896 0.4965 -0.0369 0.0077  -0.0007 79  GLN D NE2 
2182 N N   . PRO B 81  ? 1.1414 0.4403 0.4445 -0.0896 0.0446  0.0098  80  PRO D N   
2183 C CA  . PRO B 81  ? 1.1490 0.4517 0.4474 -0.1019 0.0600  0.0098  80  PRO D CA  
2184 C C   . PRO B 81  ? 1.1309 0.4516 0.4472 -0.0953 0.0799  0.0057  80  PRO D C   
2185 O O   . PRO B 81  ? 1.1337 0.4688 0.4605 -0.1020 0.0937  0.0074  80  PRO D O   
2186 C CB  . PRO B 81  ? 1.1405 0.4242 0.4127 -0.1055 0.0532  0.0068  80  PRO D CB  
2187 C CG  . PRO B 81  ? 1.1368 0.4115 0.4031 -0.0992 0.0308  0.0061  80  PRO D CG  
2188 C CD  . PRO B 81  ? 1.1533 0.4352 0.4362 -0.0854 0.0293  0.0065  80  PRO D CD  
2189 N N   . GLU B 82  ? 1.0513 0.3720 0.3720 -0.0817 0.0817  0.0003  81  GLU D N   
2190 C CA  . GLU B 82  ? 1.0237 0.3583 0.3598 -0.0748 0.1005  -0.0037 81  GLU D CA  
2191 C C   . GLU B 82  ? 1.0153 0.3699 0.3759 -0.0695 0.1077  -0.0006 81  GLU D C   
2192 O O   . GLU B 82  ? 1.0402 0.4066 0.4130 -0.0643 0.1247  -0.0030 81  GLU D O   
2193 C CB  . GLU B 82  ? 1.0113 0.3405 0.3466 -0.0617 0.0994  -0.0096 81  GLU D CB  
2194 C CG  . GLU B 82  ? 1.0491 0.3796 0.3935 -0.0506 0.0854  -0.0073 81  GLU D CG  
2195 C CD  . GLU B 82  ? 1.1280 0.4423 0.4546 -0.0488 0.0662  -0.0081 81  GLU D CD  
2196 O OE1 . GLU B 82  ? 1.1554 0.4769 0.4908 -0.0357 0.0613  -0.0095 81  GLU D OE1 
2197 O OE2 . GLU B 82  ? 1.1455 0.4473 0.4536 -0.0594 0.0561  -0.0057 81  GLU D OE2 
2198 N N   . ASP B 83  ? 1.0161 0.3745 0.3838 -0.0695 0.0952  0.0042  82  ASP D N   
2199 C CA  . ASP B 83  ? 0.9686 0.3482 0.3601 -0.0630 0.1009  0.0065  82  ASP D CA  
2200 C C   . ASP B 83  ? 0.9310 0.3264 0.3297 -0.0751 0.1115  0.0099  82  ASP D C   
2201 O O   . ASP B 83  ? 0.9468 0.3627 0.3652 -0.0704 0.1166  0.0116  82  ASP D O   
2202 C CB  . ASP B 83  ? 0.9900 0.3698 0.3878 -0.0573 0.0830  0.0095  82  ASP D CB  
2203 C CG  . ASP B 83  ? 0.9773 0.3471 0.3728 -0.0421 0.0736  0.0063  82  ASP D CG  
2204 O OD1 . ASP B 83  ? 0.9512 0.3190 0.3464 -0.0337 0.0833  0.0019  82  ASP D OD1 
2205 O OD2 . ASP B 83  ? 1.0055 0.3696 0.3993 -0.0387 0.0563  0.0083  82  ASP D OD2 
2206 N N   . PHE B 84  ? 1.0041 0.3924 0.3878 -0.0901 0.1151  0.0109  83  PHE D N   
2207 C CA  . PHE B 84  ? 1.0143 0.4192 0.4050 -0.1023 0.1243  0.0146  83  PHE D CA  
2208 C C   . PHE B 84  ? 0.9757 0.3959 0.3765 -0.0970 0.1458  0.0114  83  PHE D C   
2209 O O   . PHE B 84  ? 1.0385 0.4492 0.4267 -0.0995 0.1546  0.0080  83  PHE D O   
2210 C CB  . PHE B 84  ? 0.9875 0.3779 0.3569 -0.1207 0.1188  0.0179  83  PHE D CB  
2211 C CG  . PHE B 84  ? 0.9884 0.3685 0.3512 -0.1282 0.1000  0.0225  83  PHE D CG  
2212 C CD1 . PHE B 84  ? 0.9889 0.3842 0.3634 -0.1376 0.0984  0.0272  83  PHE D CD1 
2213 C CD2 . PHE B 84  ? 0.9863 0.3426 0.3322 -0.1243 0.0837  0.0216  83  PHE D CD2 
2214 C CE1 . PHE B 84  ? 1.0239 0.4080 0.3918 -0.1445 0.0809  0.0310  83  PHE D CE1 
2215 C CE2 . PHE B 84  ? 1.0161 0.3607 0.3546 -0.1298 0.0661  0.0255  83  PHE D CE2 
2216 C CZ  . PHE B 84  ? 1.0271 0.3844 0.3763 -0.1402 0.0646  0.0302  83  PHE D CZ  
2217 N N   . ALA B 85  ? 0.9769 0.4206 0.3995 -0.0891 0.1540  0.0121  84  ALA D N   
2218 C CA  . ALA B 85  ? 0.9435 0.4003 0.3757 -0.0798 0.1739  0.0087  84  ALA D CA  
2219 C C   . ALA B 85  ? 0.9467 0.4332 0.4012 -0.0753 0.1810  0.0112  84  ALA D C   
2220 O O   . ALA B 85  ? 0.9845 0.4825 0.4456 -0.0840 0.1721  0.0154  84  ALA D O   
2221 C CB  . ALA B 85  ? 0.9422 0.3871 0.3739 -0.0633 0.1764  0.0036  84  ALA D CB  
2222 N N   . THR B 86  ? 0.9200 0.4190 0.3852 -0.0622 0.1973  0.0082  85  THR D N   
2223 C CA  . THR B 86  ? 0.9377 0.4659 0.4241 -0.0539 0.2044  0.0097  85  THR D CA  
2224 C C   . THR B 86  ? 0.9105 0.4401 0.4084 -0.0326 0.2040  0.0078  85  THR D C   
2225 O O   . THR B 86  ? 0.9230 0.4338 0.4131 -0.0231 0.2072  0.0042  85  THR D O   
2226 C CB  . THR B 86  ? 0.9620 0.5062 0.4509 -0.0545 0.2243  0.0085  85  THR D CB  
2227 O OG1 . THR B 86  ? 1.0316 0.5707 0.5068 -0.0741 0.2249  0.0101  85  THR D OG1 
2228 C CG2 . THR B 86  ? 0.9592 0.5377 0.4693 -0.0485 0.2302  0.0105  85  THR D CG2 
2229 N N   . TYR B 87  ? 0.9024 0.4544 0.4185 -0.0254 0.1998  0.0100  86  TYR D N   
2230 C CA  . TYR B 87  ? 0.9072 0.4605 0.4338 -0.0050 0.1974  0.0088  86  TYR D CA  
2231 C C   . TYR B 87  ? 0.9099 0.4928 0.4551 0.0088  0.2099  0.0088  86  TYR D C   
2232 O O   . TYR B 87  ? 0.8897 0.4978 0.4444 0.0012  0.2131  0.0106  86  TYR D O   
2233 C CB  . TYR B 87  ? 0.9198 0.4682 0.4491 -0.0057 0.1761  0.0109  86  TYR D CB  
2234 C CG  . TYR B 87  ? 0.9206 0.4388 0.4303 -0.0154 0.1633  0.0106  86  TYR D CG  
2235 C CD1 . TYR B 87  ? 0.9116 0.4218 0.4090 -0.0360 0.1550  0.0129  86  TYR D CD1 
2236 C CD2 . TYR B 87  ? 0.9084 0.4063 0.4106 -0.0040 0.1604  0.0078  86  TYR D CD2 
2237 C CE1 . TYR B 87  ? 0.9157 0.3987 0.3937 -0.0435 0.1436  0.0124  86  TYR D CE1 
2238 C CE2 . TYR B 87  ? 0.9159 0.3889 0.4000 -0.0121 0.1489  0.0070  86  TYR D CE2 
2239 C CZ  . TYR B 87  ? 0.9200 0.3857 0.3918 -0.0312 0.1403  0.0093  86  TYR D CZ  
2240 O OH  . TYR B 87  ? 0.8923 0.3336 0.3448 -0.0377 0.1289  0.0084  86  TYR D OH  
2241 N N   . TYR B 88  ? 0.9404 0.5196 0.4895 0.0294  0.2174  0.0065  87  TYR D N   
2242 C CA  . TYR B 88  ? 0.9350 0.5364 0.4970 0.0463  0.2323  0.0058  87  TYR D CA  
2243 C C   . TYR B 88  ? 0.8803 0.4817 0.4512 0.0673  0.2280  0.0057  87  TYR D C   
2244 O O   . TYR B 88  ? 0.8529 0.4293 0.4146 0.0729  0.2240  0.0045  87  TYR D O   
2245 C CB  . TYR B 88  ? 0.8844 0.4757 0.4363 0.0513  0.2525  0.0025  87  TYR D CB  
2246 C CG  . TYR B 88  ? 0.9395 0.5362 0.4844 0.0345  0.2608  0.0023  87  TYR D CG  
2247 C CD1 . TYR B 88  ? 0.9711 0.5997 0.5277 0.0329  0.2682  0.0037  87  TYR D CD1 
2248 C CD2 . TYR B 88  ? 0.9325 0.5040 0.4589 0.0216  0.2623  0.0003  87  TYR D CD2 
2249 C CE1 . TYR B 88  ? 0.9577 0.5921 0.5077 0.0183  0.2765  0.0037  87  TYR D CE1 
2250 C CE2 . TYR B 88  ? 0.9322 0.5088 0.4517 0.0075  0.2703  0.0001  87  TYR D CE2 
2251 C CZ  . TYR B 88  ? 0.9530 0.5605 0.4842 0.0059  0.2774  0.0020  87  TYR D CZ  
2252 O OH  . TYR B 88  ? 1.0440 0.6571 0.5680 -0.0082 0.2855  0.0021  87  TYR D OH  
2253 N N   . CYS B 89  ? 0.9047 0.5354 0.4931 0.0788  0.2289  0.0069  88  CYS D N   
2254 C CA  . CYS B 89  ? 0.9245 0.5586 0.5218 0.1016  0.2275  0.0069  88  CYS D CA  
2255 C C   . CYS B 89  ? 0.8675 0.5063 0.4655 0.1209  0.2479  0.0052  88  CYS D C   
2256 O O   . CYS B 89  ? 0.9016 0.5574 0.5019 0.1192  0.2606  0.0045  88  CYS D O   
2257 C CB  . CYS B 89  ? 0.8658 0.5293 0.4816 0.1046  0.2150  0.0088  88  CYS D CB  
2258 S SG  . CYS B 89  ? 0.9909 0.6971 0.6217 0.0958  0.2215  0.0093  88  CYS D SG  
2259 N N   . GLN B 90  ? 0.8577 0.4810 0.4528 0.1396  0.2512  0.0046  89  GLN D N   
2260 C CA  . GLN B 90  ? 0.9086 0.5314 0.5018 0.1598  0.2703  0.0032  89  GLN D CA  
2261 C C   . GLN B 90  ? 0.9386 0.5747 0.5435 0.1838  0.2686  0.0046  89  GLN D C   
2262 O O   . GLN B 90  ? 0.9360 0.5589 0.5405 0.1895  0.2578  0.0056  89  GLN D O   
2263 C CB  . GLN B 90  ? 0.8845 0.4710 0.4594 0.1607  0.2798  0.0009  89  GLN D CB  
2264 C CG  . GLN B 90  ? 0.8907 0.4829 0.4770 0.1752  0.2864  0.0034  89  GLN D CG  
2265 C CD  . GLN B 90  ? 0.9042 0.4708 0.4870 0.1710  0.2822  0.0053  89  GLN D CD  
2266 O OE1 . GLN B 90  ? 0.9007 0.4484 0.4747 0.1620  0.2738  0.0045  89  GLN D OE1 
2267 N NE2 . GLN B 90  ? 0.9622 0.5277 0.5499 0.1761  0.2884  0.0076  89  GLN D NE2 
2268 N N   . GLN B 91  ? 0.9328 0.5949 0.5470 0.1987  0.2797  0.0046  90  GLN D N   
2269 C CA  . GLN B 91  ? 0.9799 0.6558 0.6055 0.2232  0.2792  0.0062  90  GLN D CA  
2270 C C   . GLN B 91  ? 0.9732 0.6439 0.6044 0.2290  0.2833  0.0095  90  GLN D C   
2271 O O   . GLN B 91  ? 0.9337 0.6176 0.5671 0.2293  0.2934  0.0086  90  GLN D O   
2272 C CB  . GLN B 91  ? 1.0031 0.7217 0.6456 0.2297  0.2776  0.0061  90  GLN D CB  
2273 C CG  . GLN B 91  ? 1.0104 0.7474 0.6658 0.2550  0.2746  0.0076  90  GLN D CG  
2274 C CD  . GLN B 91  ? 1.0923 0.8736 0.7620 0.2657  0.2808  0.0063  90  GLN D CD  
2275 O OE1 . GLN B 91  ? 1.1294 0.9277 0.8010 0.2535  0.2873  0.0051  90  GLN D OE1 
2276 N NE2 . GLN B 91  ? 1.0781 0.8823 0.7632 0.2832  0.2730  0.0076  90  GLN D NE2 
2277 N N   . ASP B 92  ? 0.9674 0.6187 0.5987 0.2323  0.2755  0.0134  91  ASP D N   
2278 C CA  . ASP B 92  ? 1.0039 0.6479 0.6371 0.2379  0.2788  0.0174  91  ASP D CA  
2279 C C   . ASP B 92  ? 1.0605 0.7280 0.7070 0.2570  0.2755  0.0208  91  ASP D C   
2280 O O   . ASP B 92  ? 1.1019 0.7636 0.7506 0.2633  0.2679  0.0253  91  ASP D O   
2281 C CB  . ASP B 92  ? 0.9893 0.6034 0.6140 0.2293  0.2735  0.0203  91  ASP D CB  
2282 C CG  . ASP B 92  ? 1.0433 0.6464 0.6659 0.2323  0.2788  0.0243  91  ASP D CG  
2283 O OD1 . ASP B 92  ? 1.0388 0.6558 0.6661 0.2428  0.2854  0.0251  91  ASP D OD1 
2284 O OD2 . ASP B 92  ? 1.0351 0.6161 0.6505 0.2244  0.2764  0.0267  91  ASP D OD2 
2285 N N   . GLY B 93  ? 1.0838 0.7797 0.7385 0.2653  0.2816  0.0185  92  GLY D N   
2286 C CA  . GLY B 93  ? 1.1436 0.8674 0.8115 0.2831  0.2777  0.0203  92  GLY D CA  
2287 C C   . GLY B 93  ? 1.2388 0.9582 0.9063 0.2930  0.2800  0.0247  92  GLY D C   
2288 O O   . GLY B 93  ? 1.2349 0.9286 0.8920 0.2866  0.2846  0.0268  92  GLY D O   
2289 N N   . TRP B 94  ? 1.3332 1.0789 1.0115 0.3090  0.2770  0.0260  93  TRP D N   
2290 C CA  . TRP B 94  ? 1.3806 1.1226 1.0569 0.3202  0.2778  0.0307  93  TRP D CA  
2291 C C   . TRP B 94  ? 1.4029 1.1341 1.0706 0.3188  0.2894  0.0303  93  TRP D C   
2292 O O   . TRP B 94  ? 1.3784 1.0820 1.0346 0.3160  0.2923  0.0342  93  TRP D O   
2293 C CB  . TRP B 94  ? 1.3973 1.1735 1.0865 0.3371  0.2734  0.0307  93  TRP D CB  
2294 C CG  . TRP B 94  ? 1.4930 1.2637 1.1784 0.3488  0.2715  0.0363  93  TRP D CG  
2295 C CD1 . TRP B 94  ? 1.4998 1.2396 1.1716 0.3457  0.2743  0.0414  93  TRP D CD1 
2296 C CD2 . TRP B 94  ? 1.5163 1.3136 1.2103 0.3651  0.2671  0.0374  93  TRP D CD2 
2297 N NE1 . TRP B 94  ? 1.5240 1.2681 1.1940 0.3591  0.2724  0.0459  93  TRP D NE1 
2298 C CE2 . TRP B 94  ? 1.5453 1.3241 1.2287 0.3712  0.2677  0.0435  93  TRP D CE2 
2299 C CE3 . TRP B 94  ? 1.4928 1.3285 1.2019 0.3748  0.2630  0.0337  93  TRP D CE3 
2300 C CZ2 . TRP B 94  ? 1.5443 1.3399 1.2304 0.3867  0.2643  0.0461  93  TRP D CZ2 
2301 C CZ3 . TRP B 94  ? 1.4815 1.3351 1.1947 0.3902  0.2589  0.0359  93  TRP D CZ3 
2302 C CH2 . TRP B 94  ? 1.5195 1.3523 1.2206 0.3960  0.2595  0.0422  93  TRP D CH2 
2303 N N   . SER B 95  ? 1.3146 1.0690 0.9876 0.3209  0.2965  0.0257  94  SER D N   
2304 C CA  . SER B 95  ? 1.3065 1.0527 0.9715 0.3201  0.3071  0.0247  94  SER D CA  
2305 C C   . SER B 95  ? 1.2879 1.0114 0.9433 0.3018  0.3127  0.0219  94  SER D C   
2306 O O   . SER B 95  ? 1.2814 0.9778 0.9250 0.2969  0.3179  0.0235  94  SER D O   
2307 C CB  . SER B 95  ? 1.2763 1.0599 0.9511 0.3307  0.3122  0.0209  94  SER D CB  
2308 O OG  . SER B 95  ? 1.2779 1.0934 0.9659 0.3306  0.3084  0.0174  94  SER D OG  
2309 N N   . LEU B 96  ? 1.2458 0.9784 0.9047 0.2911  0.3118  0.0180  95  LEU D N   
2310 C CA  . LEU B 96  ? 1.1350 0.8534 0.7848 0.2744  0.3188  0.0145  95  LEU D CA  
2311 C C   . LEU B 96  ? 1.1102 0.8209 0.7574 0.2602  0.3142  0.0126  95  LEU D C   
2312 O O   . LEU B 96  ? 1.1174 0.8464 0.7725 0.2639  0.3083  0.0121  95  LEU D O   
2313 C CB  . LEU B 96  ? 1.1017 0.8479 0.7555 0.2760  0.3281  0.0102  95  LEU D CB  
2314 C CG  . LEU B 96  ? 1.1620 0.9507 0.8306 0.2854  0.3263  0.0084  95  LEU D CG  
2315 C CD1 . LEU B 96  ? 1.1363 0.9369 0.8056 0.2713  0.3268  0.0053  95  LEU D CD1 
2316 C CD2 . LEU B 96  ? 1.2377 1.0554 0.9123 0.2957  0.3337  0.0063  95  LEU D CD2 
2317 N N   . ILE B 97  ? 1.0816 0.7646 0.7166 0.2440  0.3169  0.0113  96  ILE D N   
2318 C CA  . ILE B 97  ? 1.0190 0.6903 0.6473 0.2283  0.3135  0.0091  96  ILE D CA  
2319 C C   . ILE B 97  ? 1.0086 0.7032 0.6370 0.2202  0.3202  0.0050  96  ILE D C   
2320 O O   . ILE B 97  ? 1.0420 0.7478 0.6702 0.2184  0.3292  0.0031  96  ILE D O   
2321 C CB  . ILE B 97  ? 0.9929 0.6283 0.6078 0.2137  0.3141  0.0090  96  ILE D CB  
2322 C CG1 . ILE B 97  ? 0.9882 0.6035 0.6022 0.2201  0.3093  0.0139  96  ILE D CG1 
2323 C CG2 . ILE B 97  ? 0.9603 0.5823 0.5663 0.1973  0.3096  0.0065  96  ILE D CG2 
2324 C CD1 . ILE B 97  ? 1.0103 0.5934 0.6124 0.2054  0.3091  0.0139  96  ILE D CD1 
2325 N N   . THR B 98  ? 0.9714 0.6731 0.5987 0.2144  0.3160  0.0039  97  THR D N   
2326 C CA  . THR B 98  ? 0.9377 0.6596 0.5616 0.2027  0.3223  0.0014  97  THR D CA  
2327 C C   . THR B 98  ? 0.9198 0.6153 0.5265 0.1826  0.3190  0.0003  97  THR D C   
2328 O O   . THR B 98  ? 0.9308 0.6006 0.5320 0.1821  0.3099  0.0009  97  THR D O   
2329 C CB  . THR B 98  ? 0.9506 0.7109 0.5871 0.2137  0.3214  0.0015  97  THR D CB  
2330 O OG1 . THR B 98  ? 0.9953 0.7759 0.6477 0.2348  0.3199  0.0027  97  THR D OG1 
2331 C CG2 . THR B 98  ? 0.9197 0.7122 0.5633 0.1976  0.3232  0.0010  97  THR D CG2 
2332 N N   . PHE B 99  ? 0.9203 0.6270 0.5266 0.1613  0.3181  0.0001  98  PHE D N   
2333 C CA  . PHE B 99  ? 0.9016 0.5928 0.5029 0.1363  0.3034  0.0011  98  PHE D CA  
2334 C C   . PHE B 99  ? 0.9448 0.6686 0.5601 0.1198  0.2929  0.0032  98  PHE D C   
2335 O O   . PHE B 99  ? 0.9935 0.7485 0.6176 0.1206  0.3013  0.0030  98  PHE D O   
2336 C CB  . PHE B 99  ? 0.8866 0.5510 0.4693 0.1226  0.3117  -0.0010 98  PHE D CB  
2337 C CG  . PHE B 99  ? 0.8904 0.5161 0.4578 0.1288  0.3147  -0.0030 98  PHE D CG  
2338 C CD1 . PHE B 99  ? 0.8829 0.4869 0.4452 0.1190  0.2999  -0.0024 98  PHE D CD1 
2339 C CD2 . PHE B 99  ? 0.8960 0.5145 0.4669 0.1390  0.3218  -0.0037 98  PHE D CD2 
2340 C CE1 . PHE B 99  ? 0.8860 0.4574 0.4357 0.1232  0.3021  -0.0045 98  PHE D CE1 
2341 C CE2 . PHE B 99  ? 0.8950 0.4847 0.4624 0.1388  0.3165  -0.0036 98  PHE D CE2 
2342 C CZ  . PHE B 99  ? 0.8888 0.4569 0.4471 0.1309  0.3068  -0.0038 98  PHE D CZ  
2343 N N   . GLY B 100 ? 0.9341 0.6509 0.5510 0.1051  0.2745  0.0050  99  GLY D N   
2344 C CA  . GLY B 100 ? 0.9662 0.7091 0.5939 0.0867  0.2642  0.0070  99  GLY D CA  
2345 C C   . GLY B 100 ? 0.9699 0.7093 0.5876 0.0648  0.2694  0.0072  99  GLY D C   
2346 O O   . GLY B 100 ? 0.9793 0.6905 0.5801 0.0608  0.2762  0.0059  99  GLY D O   
2347 N N   . GLN B 101 ? 0.9944 0.7634 0.6225 0.0498  0.2659  0.0089  100 GLN D N   
2348 C CA  . GLN B 101 ? 0.9781 0.7485 0.5977 0.0297  0.2725  0.0096  100 GLN D CA  
2349 C C   . GLN B 101 ? 0.9765 0.7095 0.5769 0.0115  0.2641  0.0106  100 GLN D C   
2350 O O   . GLN B 101 ? 1.0182 0.7434 0.6066 -0.0009 0.2722  0.0104  100 GLN D O   
2351 C CB  . GLN B 101 ? 0.9910 0.7995 0.6255 0.0151  0.2684  0.0117  100 GLN D CB  
2352 C CG  . GLN B 101 ? 1.0545 0.8534 0.6877 -0.0064 0.2486  0.0146  100 GLN D CG  
2353 C CD  . GLN B 101 ? 1.0970 0.9335 0.7463 -0.0209 0.2433  0.0163  100 GLN D CD  
2354 O OE1 . GLN B 101 ? 1.0924 0.9228 0.7410 -0.0389 0.2277  0.0186  100 GLN D OE1 
2355 N NE2 . GLN B 101 ? 1.1285 1.0040 0.7915 -0.0136 0.2563  0.0150  100 GLN D NE2 
2356 N N   . GLY B 102 ? 0.9768 0.6875 0.5735 0.0105  0.2482  0.0113  101 GLY D N   
2357 C CA  . GLY B 102 ? 0.9679 0.6438 0.5459 -0.0045 0.2390  0.0120  101 GLY D CA  
2358 C C   . GLY B 102 ? 0.9341 0.6109 0.5118 -0.0258 0.2217  0.0154  101 GLY D C   
2359 O O   . GLY B 102 ? 0.9301 0.6357 0.5207 -0.0345 0.2195  0.0174  101 GLY D O   
2360 N N   . THR B 103 ? 0.9263 0.5708 0.4882 -0.0345 0.2093  0.0160  102 THR D N   
2361 C CA  . THR B 103 ? 0.9528 0.5897 0.5093 -0.0541 0.1920  0.0193  102 THR D CA  
2362 C C   . THR B 103 ? 0.9793 0.5823 0.5118 -0.0671 0.1882  0.0196  102 THR D C   
2363 O O   . THR B 103 ? 0.9570 0.5344 0.4790 -0.0586 0.1842  0.0174  102 THR D O   
2364 C CB  . THR B 103 ? 0.9490 0.5830 0.5130 -0.0465 0.1747  0.0197  102 THR D CB  
2365 O OG1 . THR B 103 ? 0.9814 0.6505 0.5673 -0.0409 0.1750  0.0200  102 THR D OG1 
2366 C CG2 . THR B 103 ? 0.9767 0.5897 0.5276 -0.0649 0.1563  0.0224  102 THR D CG2 
2367 N N   . LYS B 104 ? 1.0192 0.6228 0.5428 -0.0877 0.1891  0.0223  103 LYS D N   
2368 C CA  . LYS B 104 ? 1.0210 0.5951 0.5210 -0.1004 0.1869  0.0227  103 LYS D CA  
2369 C C   . LYS B 104 ? 1.0408 0.5963 0.5301 -0.1139 0.1667  0.0259  103 LYS D C   
2370 O O   . LYS B 104 ? 1.0707 0.6400 0.5666 -0.1265 0.1601  0.0295  103 LYS D O   
2371 C CB  . LYS B 104 ? 1.0654 0.6502 0.5600 -0.1141 0.2006  0.0239  103 LYS D CB  
2372 C CG  . LYS B 104 ? 1.1387 0.6988 0.6115 -0.1184 0.2077  0.0218  103 LYS D CG  
2373 C CD  . LYS B 104 ? 1.1794 0.7055 0.6313 -0.1266 0.1916  0.0226  103 LYS D CD  
2374 C CE  . LYS B 104 ? 1.1934 0.6957 0.6264 -0.1241 0.1976  0.0185  103 LYS D CE  
2375 N NZ  . LYS B 104 ? 1.1963 0.6682 0.6104 -0.1282 0.1808  0.0186  103 LYS D NZ  
2376 N N   . VAL B 105 ? 0.9786 0.5030 0.4506 -0.1117 0.1571  0.0247  104 VAL D N   
2377 C CA  . VAL B 105 ? 1.0326 0.5368 0.4931 -0.1207 0.1369  0.0273  104 VAL D CA  
2378 C C   . VAL B 105 ? 1.0320 0.5106 0.4665 -0.1356 0.1345  0.0287  104 VAL D C   
2379 O O   . VAL B 105 ? 1.0420 0.4988 0.4618 -0.1296 0.1334  0.0257  104 VAL D O   
2380 C CB  . VAL B 105 ? 1.0587 0.5495 0.5206 -0.1040 0.1248  0.0249  104 VAL D CB  
2381 C CG1 . VAL B 105 ? 1.0477 0.5140 0.4935 -0.1127 0.1037  0.0273  104 VAL D CG1 
2382 C CG2 . VAL B 105 ? 0.9498 0.4663 0.4366 -0.0893 0.1261  0.0240  104 VAL D CG2 
2383 N N   . GLU B 106 ? 1.0872 0.5688 0.5157 -0.1552 0.1335  0.0332  105 GLU D N   
2384 C CA  . GLU B 106 ? 1.1487 0.6078 0.5520 -0.1706 0.1321  0.0354  105 GLU D CA  
2385 C C   . GLU B 106 ? 1.1238 0.5555 0.5090 -0.1788 0.1115  0.0385  105 GLU D C   
2386 O O   . GLU B 106 ? 1.1129 0.5471 0.5069 -0.1773 0.0992  0.0398  105 GLU D O   
2387 C CB  . GLU B 106 ? 1.1832 0.6606 0.5885 -0.1876 0.1438  0.0391  105 GLU D CB  
2388 C CG  . GLU B 106 ? 1.1927 0.7035 0.6192 -0.1799 0.1632  0.0368  105 GLU D CG  
2389 C CD  . GLU B 106 ? 1.2955 0.8090 0.7120 -0.1870 0.1796  0.0365  105 GLU D CD  
2390 O OE1 . GLU B 106 ? 1.2975 0.7912 0.6984 -0.1820 0.1833  0.0332  105 GLU D OE1 
2391 O OE2 . GLU B 106 ? 1.3249 0.8614 0.7489 -0.1984 0.1886  0.0395  105 GLU D OE2 
2392 N N   . ILE B 107 ? 1.0998 0.5049 0.4586 -0.1871 0.1078  0.0395  106 ILE D N   
2393 C CA  . ILE B 107 ? 1.1103 0.4858 0.4474 -0.1941 0.0887  0.0424  106 ILE D CA  
2394 C C   . ILE B 107 ? 1.1154 0.4914 0.4477 -0.2152 0.0849  0.0489  106 ILE D C   
2395 O O   . ILE B 107 ? 1.1348 0.5277 0.4717 -0.2276 0.0979  0.0514  106 ILE D O   
2396 C CB  . ILE B 107 ? 1.1652 0.5125 0.4744 -0.1934 0.0860  0.0408  106 ILE D CB  
2397 C CG1 . ILE B 107 ? 1.1225 0.4699 0.4363 -0.1742 0.0902  0.0339  106 ILE D CG1 
2398 C CG2 . ILE B 107 ? 1.1140 0.4299 0.3990 -0.1984 0.0658  0.0438  106 ILE D CG2 
2399 C CD1 . ILE B 107 ? 1.1511 0.4704 0.4382 -0.1709 0.0821  0.0313  106 ILE D CD1 
2400 N N   . LYS B 108 ? 1.1296 0.4866 0.4520 -0.2198 0.0669  0.0516  107 LYS D N   
2401 C CA  . LYS B 108 ? 1.2162 0.5647 0.5275 -0.2413 0.0610  0.0578  107 LYS D CA  
2402 C C   . LYS B 108 ? 1.2512 0.5616 0.5265 -0.2492 0.0524  0.0607  107 LYS D C   
2403 O O   . LYS B 108 ? 1.2578 0.5486 0.5208 -0.2356 0.0418  0.0569  107 LYS D O   
2404 C CB  . LYS B 108 ? 1.1634 0.5139 0.4853 -0.2425 0.0465  0.0588  107 LYS D CB  
2405 C CG  . LYS B 108 ? 1.1823 0.5146 0.4872 -0.2644 0.0367  0.0648  107 LYS D CG  
2406 C CD  . LYS B 108 ? 1.1579 0.5176 0.4865 -0.2747 0.0372  0.0661  107 LYS D CD  
2407 C CE  . LYS B 108 ? 1.1231 0.5211 0.4731 -0.2804 0.0578  0.0662  107 LYS D CE  
2408 N NZ  . LYS B 108 ? 1.1264 0.5511 0.4958 -0.2947 0.0584  0.0680  107 LYS D NZ  
2409 N N   . ARG B 109 ? 1.1852 0.4935 0.4500 -0.2679 0.0564  0.0650  108 ARG D N   
2410 C CA  . ARG B 109 ? 1.2629 0.5508 0.5071 -0.2697 0.0453  0.0629  108 ARG D CA  
2411 C C   . ARG B 109 ? 1.2535 0.5410 0.4924 -0.2915 0.0443  0.0685  108 ARG D C   
2412 O O   . ARG B 109 ? 1.2605 0.5641 0.5127 -0.3051 0.0507  0.0734  108 ARG D O   
2413 C CB  . ARG B 109 ? 1.3228 0.6113 0.5597 -0.2618 0.0544  0.0581  108 ARG D CB  
2414 C CG  . ARG B 109 ? 1.2983 0.6123 0.5494 -0.2654 0.0766  0.0589  108 ARG D CG  
2415 C CD  . ARG B 109 ? 1.2634 0.5774 0.5043 -0.2676 0.0846  0.0564  108 ARG D CD  
2416 N NE  . ARG B 109 ? 1.3379 0.6474 0.5686 -0.2850 0.0821  0.0610  108 ARG D NE  
2417 C CZ  . ARG B 109 ? 1.3435 0.6339 0.5538 -0.2867 0.0740  0.0597  108 ARG D CZ  
2418 N NH1 . ARG B 109 ? 1.3728 0.6494 0.5713 -0.2729 0.0690  0.0535  108 ARG D NH1 
2419 N NH2 . ARG B 109 ? 1.3173 0.6023 0.5184 -0.3027 0.0712  0.0647  108 ARG D NH2 
2420 N N   . THR B 110 ? 1.2815 0.5507 0.5002 -0.2950 0.0363  0.0677  109 THR D N   
2421 C CA  . THR B 110 ? 1.3491 0.6166 0.5610 -0.3156 0.0363  0.0730  109 THR D CA  
2422 C C   . THR B 110 ? 1.3297 0.6206 0.5505 -0.3271 0.0561  0.0757  109 THR D C   
2423 O O   . THR B 110 ? 1.3150 0.6165 0.5401 -0.3180 0.0679  0.0725  109 THR D O   
2424 C CB  . THR B 110 ? 1.3229 0.5623 0.5082 -0.3151 0.0226  0.0716  109 THR D CB  
2425 O OG1 . THR B 110 ? 1.3094 0.5445 0.4845 -0.3046 0.0274  0.0671  109 THR D OG1 
2426 C CG2 . THR B 110 ? 1.3516 0.5708 0.5286 -0.3037 0.0030  0.0688  109 THR D CG2 
2427 N N   . VAL B 111 ? 1.3658 0.6651 0.5893 -0.3474 0.0597  0.0813  110 VAL D N   
2428 C CA  . VAL B 111 ? 1.3957 0.7216 0.6300 -0.3594 0.0785  0.0842  110 VAL D CA  
2429 C C   . VAL B 111 ? 1.3863 0.7033 0.6043 -0.3583 0.0825  0.0828  110 VAL D C   
2430 O O   . VAL B 111 ? 1.3505 0.6455 0.5485 -0.3645 0.0729  0.0841  110 VAL D O   
2431 C CB  . VAL B 111 ? 1.4100 0.7489 0.6522 -0.3823 0.0804  0.0902  110 VAL D CB  
2432 C CG1 . VAL B 111 ? 1.3760 0.7343 0.6205 -0.3961 0.0955  0.0933  110 VAL D CG1 
2433 C CG2 . VAL B 111 ? 1.4595 0.8209 0.7244 -0.3836 0.0849  0.0913  110 VAL D CG2 
2434 N N   . ALA B 112 ? 1.4171 0.7505 0.6426 -0.3501 0.0969  0.0800  111 ALA D N   
2435 C CA  . ALA B 112 ? 1.3143 0.6417 0.5261 -0.3482 0.1018  0.0782  111 ALA D CA  
2436 C C   . ALA B 112 ? 1.3163 0.6697 0.5377 -0.3623 0.1184  0.0822  111 ALA D C   
2437 O O   . ALA B 112 ? 1.2732 0.6557 0.5159 -0.3662 0.1306  0.0838  111 ALA D O   
2438 C CB  . ALA B 112 ? 1.3474 0.6739 0.5593 -0.3287 0.1058  0.0712  111 ALA D CB  
2439 N N   . ALA B 113 ? 1.3702 0.7137 0.5757 -0.3689 0.1189  0.0837  112 ALA D N   
2440 C CA  . ALA B 113 ? 1.3158 0.6816 0.5274 -0.3816 0.1336  0.0875  112 ALA D CA  
2441 C C   . ALA B 113 ? 1.3006 0.6803 0.5169 -0.3696 0.1469  0.0830  112 ALA D C   
2442 O O   . ALA B 113 ? 1.2943 0.6565 0.4993 -0.3551 0.1419  0.0774  112 ALA D O   
2443 C CB  . ALA B 113 ? 1.3756 0.7219 0.5661 -0.3944 0.1274  0.0917  112 ALA D CB  
2444 N N   . PRO B 114 ? 1.2942 0.7062 0.5276 -0.3750 0.1637  0.0846  113 PRO D N   
2445 C CA  . PRO B 114 ? 1.2820 0.7071 0.5193 -0.3636 0.1764  0.0800  113 PRO D CA  
2446 C C   . PRO B 114 ? 1.3253 0.7434 0.5465 -0.3693 0.1792  0.0816  113 PRO D C   
2447 O O   . PRO B 114 ? 1.3263 0.7488 0.5442 -0.3853 0.1807  0.0878  113 PRO D O   
2448 C CB  . PRO B 114 ? 1.2667 0.7309 0.5294 -0.3665 0.1927  0.0813  113 PRO D CB  
2449 C CG  . PRO B 114 ? 1.2834 0.7574 0.5505 -0.3867 0.1912  0.0885  113 PRO D CG  
2450 C CD  . PRO B 114 ? 1.2934 0.7346 0.5461 -0.3892 0.1719  0.0896  113 PRO D CD  
2451 N N   . SER B 115 ? 1.3175 0.7246 0.5285 -0.3563 0.1798  0.0760  114 SER D N   
2452 C CA  . SER B 115 ? 1.3291 0.7364 0.5288 -0.3594 0.1863  0.0768  114 SER D CA  
2453 C C   . SER B 115 ? 1.3188 0.7624 0.5381 -0.3603 0.2048  0.0771  114 SER D C   
2454 O O   . SER B 115 ? 1.3175 0.7746 0.5494 -0.3473 0.2128  0.0712  114 SER D O   
2455 C CB  . SER B 115 ? 1.3454 0.7310 0.5288 -0.3451 0.1810  0.0700  114 SER D CB  
2456 O OG  . SER B 115 ? 1.4266 0.7828 0.5958 -0.3404 0.1642  0.0684  114 SER D OG  
2457 N N   . VAL B 116 ? 1.3245 0.7839 0.5462 -0.3750 0.2119  0.0835  115 VAL D N   
2458 C CA  . VAL B 116 ? 1.3166 0.8132 0.5572 -0.3765 0.2293  0.0843  115 VAL D CA  
2459 C C   . VAL B 116 ? 1.3737 0.8719 0.6043 -0.3734 0.2369  0.0832  115 VAL D C   
2460 O O   . VAL B 116 ? 1.3941 0.8804 0.6087 -0.3834 0.2339  0.0879  115 VAL D O   
2461 C CB  . VAL B 116 ? 1.3277 0.8457 0.5797 -0.3949 0.2332  0.0920  115 VAL D CB  
2462 C CG1 . VAL B 116 ? 1.3394 0.8969 0.6090 -0.3964 0.2510  0.0930  115 VAL D CG1 
2463 C CG2 . VAL B 116 ? 1.3357 0.8561 0.5999 -0.3964 0.2273  0.0921  115 VAL D CG2 
2464 N N   . PHE B 117 ? 1.3506 0.8632 0.5902 -0.3592 0.2469  0.0768  116 PHE D N   
2465 C CA  . PHE B 117 ? 1.3178 0.8341 0.5496 -0.3547 0.2548  0.0747  116 PHE D CA  
2466 C C   . PHE B 117 ? 1.3081 0.8626 0.5597 -0.3522 0.2720  0.0743  116 PHE D C   
2467 O O   . PHE B 117 ? 1.3001 0.8728 0.5702 -0.3448 0.2779  0.0711  116 PHE D O   
2468 C CB  . PHE B 117 ? 1.3079 0.8035 0.5293 -0.3389 0.2502  0.0661  116 PHE D CB  
2469 C CG  . PHE B 117 ? 1.3417 0.8016 0.5441 -0.3383 0.2333  0.0653  116 PHE D CG  
2470 C CD1 . PHE B 117 ? 1.4547 0.8961 0.6407 -0.3508 0.2237  0.0719  116 PHE D CD1 
2471 C CD2 . PHE B 117 ? 1.3787 0.8242 0.5804 -0.3248 0.2268  0.0578  116 PHE D CD2 
2472 C CE1 . PHE B 117 ? 1.5037 0.9119 0.6716 -0.3483 0.2077  0.0707  116 PHE D CE1 
2473 C CE2 . PHE B 117 ? 1.4215 0.8362 0.6064 -0.3227 0.2112  0.0567  116 PHE D CE2 
2474 C CZ  . PHE B 117 ? 1.4607 0.8566 0.6284 -0.3340 0.2014  0.0630  116 PHE D CZ  
2475 N N   . ILE B 118 ? 1.3245 0.8907 0.5715 -0.3574 0.2801  0.0775  117 ILE D N   
2476 C CA  . ILE B 118 ? 1.3188 0.9214 0.5823 -0.3545 0.2963  0.0774  117 ILE D CA  
2477 C C   . ILE B 118 ? 1.3192 0.9190 0.5744 -0.3423 0.3018  0.0714  117 ILE D C   
2478 O O   . ILE B 118 ? 1.3326 0.9067 0.5675 -0.3421 0.2945  0.0706  117 ILE D O   
2479 C CB  . ILE B 118 ? 1.3392 0.9629 0.6062 -0.3717 0.3023  0.0866  117 ILE D CB  
2480 C CG1 . ILE B 118 ? 1.3445 1.0065 0.6268 -0.3672 0.3190  0.0863  117 ILE D CG1 
2481 C CG2 . ILE B 118 ? 1.3669 0.9661 0.6103 -0.3821 0.2951  0.0917  117 ILE D CG2 
2482 C CD1 . ILE B 118 ? 1.3128 1.0042 0.6191 -0.3620 0.3266  0.0844  117 ILE D CD1 
2483 N N   . PHE B 119 ? 1.3206 0.9468 0.5911 -0.3315 0.3146  0.0670  118 PHE D N   
2484 C CA  . PHE B 119 ? 1.3057 0.9304 0.5716 -0.3174 0.3202  0.0593  118 PHE D CA  
2485 C C   . PHE B 119 ? 1.3438 1.0039 0.6219 -0.3146 0.3359  0.0603  118 PHE D C   
2486 O O   . PHE B 119 ? 1.3594 1.0467 0.6567 -0.3133 0.3437  0.0614  118 PHE D O   
2487 C CB  . PHE B 119 ? 1.2783 0.8933 0.5506 -0.3019 0.3182  0.0498  118 PHE D CB  
2488 C CG  . PHE B 119 ? 1.2814 0.8614 0.5402 -0.3007 0.3034  0.0469  118 PHE D CG  
2489 C CD1 . PHE B 119 ? 1.2973 0.8537 0.5373 -0.2972 0.2972  0.0429  118 PHE D CD1 
2490 C CD2 . PHE B 119 ? 1.2779 0.8501 0.5434 -0.3013 0.2960  0.0474  118 PHE D CD2 
2491 C CE1 . PHE B 119 ? 1.3283 0.8545 0.5562 -0.2946 0.2837  0.0396  118 PHE D CE1 
2492 C CE2 . PHE B 119 ? 1.2798 0.8208 0.5329 -0.2988 0.2823  0.0444  118 PHE D CE2 
2493 C CZ  . PHE B 119 ? 1.2832 0.8017 0.5176 -0.2953 0.2761  0.0405  118 PHE D CZ  
2494 N N   . PRO B 120 ? 1.3543 1.0161 0.6221 -0.3122 0.3409  0.0594  119 PRO D N   
2495 C CA  . PRO B 120 ? 1.4080 1.1044 0.6866 -0.3094 0.3556  0.0608  119 PRO D CA  
2496 C C   . PRO B 120 ? 1.3991 1.1050 0.6863 -0.2909 0.3634  0.0511  119 PRO D C   
2497 O O   . PRO B 120 ? 1.3150 0.9979 0.5962 -0.2811 0.3578  0.0430  119 PRO D O   
2498 C CB  . PRO B 120 ? 1.3966 1.0869 0.6572 -0.3167 0.3559  0.0652  119 PRO D CB  
2499 C CG  . PRO B 120 ? 1.3951 1.0484 0.6367 -0.3127 0.3444  0.0599  119 PRO D CG  
2500 C CD  . PRO B 120 ? 1.3624 0.9963 0.6071 -0.3136 0.3332  0.0584  119 PRO D CD  
2501 N N   . PRO B 121 ? 1.4369 1.1765 0.7377 -0.2856 0.3766  0.0517  120 PRO D N   
2502 C CA  . PRO B 121 ? 1.4553 1.2054 0.7658 -0.2674 0.3845  0.0426  120 PRO D CA  
2503 C C   . PRO B 121 ? 1.5022 1.2320 0.7999 -0.2567 0.3830  0.0337  120 PRO D C   
2504 O O   . PRO B 121 ? 1.5338 1.2625 0.8384 -0.2423 0.3862  0.0251  120 PRO D O   
2505 C CB  . PRO B 121 ? 1.4611 1.2513 0.7835 -0.2661 0.3983  0.0467  120 PRO D CB  
2506 C CG  . PRO B 121 ? 1.4752 1.2793 0.8037 -0.2825 0.3971  0.0568  120 PRO D CG  
2507 C CD  . PRO B 121 ? 1.4831 1.2542 0.7948 -0.2965 0.3839  0.0607  120 PRO D CD  
2508 N N   . SER B 122 ? 1.4215 1.1357 0.7010 -0.2628 0.3788  0.0351  121 SER D N   
2509 C CA  . SER B 122 ? 1.3835 1.0830 0.6515 -0.2529 0.3786  0.0264  121 SER D CA  
2510 C C   . SER B 122 ? 1.3672 1.0918 0.6420 -0.2416 0.3915  0.0225  121 SER D C   
2511 O O   . SER B 122 ? 1.3460 1.0932 0.6372 -0.2342 0.3997  0.0216  121 SER D O   
2512 C CB  . SER B 122 ? 1.3708 1.0449 0.6385 -0.2438 0.3711  0.0169  121 SER D CB  
2513 O OG  . SER B 122 ? 1.2885 0.9719 0.5652 -0.2288 0.3792  0.0081  121 SER D OG  
2514 N N   . ASP B 123 ? 1.3461 1.0656 0.6073 -0.2392 0.3930  0.0196  122 ASP D N   
2515 C CA  . ASP B 123 ? 1.3318 1.0761 0.5963 -0.2306 0.4050  0.0176  122 ASP D CA  
2516 C C   . ASP B 123 ? 1.3198 1.0633 0.5915 -0.2140 0.4092  0.0062  122 ASP D C   
2517 O O   . ASP B 123 ? 1.3221 1.0898 0.6012 -0.2049 0.4199  0.0045  122 ASP D O   
2518 C CB  . ASP B 123 ? 1.3693 1.1089 0.6155 -0.2351 0.4048  0.0196  122 ASP D CB  
2519 C CG  . ASP B 123 ? 1.3913 1.1120 0.6238 -0.2505 0.3949  0.0276  122 ASP D CG  
2520 O OD1 . ASP B 123 ? 1.3686 1.1012 0.6061 -0.2620 0.3956  0.0376  122 ASP D OD1 
2521 O OD2 . ASP B 123 ? 1.4032 1.0971 0.6198 -0.2511 0.3862  0.0238  122 ASP D OD2 
2522 N N   . GLU B 124 ? 1.3083 1.0246 0.5778 -0.2097 0.4012  -0.0017 123 GLU D N   
2523 C CA  . GLU B 124 ? 1.3079 1.0224 0.5863 -0.1948 0.4052  -0.0119 123 GLU D CA  
2524 C C   . GLU B 124 ? 1.3187 1.0591 0.6154 -0.1886 0.4137  -0.0094 123 GLU D C   
2525 O O   . GLU B 124 ? 1.3419 1.0978 0.6448 -0.1763 0.4228  -0.0142 123 GLU D O   
2526 C CB  . GLU B 124 ? 1.2838 0.9677 0.5605 -0.1930 0.3951  -0.0186 123 GLU D CB  
2527 C CG  . GLU B 124 ? 1.2915 0.9514 0.5514 -0.1955 0.3874  -0.0236 123 GLU D CG  
2528 C CD  . GLU B 124 ? 1.2955 0.9408 0.5448 -0.2086 0.3769  -0.0166 123 GLU D CD  
2529 O OE1 . GLU B 124 ? 1.3035 0.9631 0.5528 -0.2178 0.3788  -0.0066 123 GLU D OE1 
2530 O OE2 . GLU B 124 ? 1.2915 0.9116 0.5326 -0.2096 0.3669  -0.0209 123 GLU D OE2 
2531 N N   . GLN B 125 ? 1.3028 1.0489 0.6076 -0.1967 0.4107  -0.0018 124 GLN D N   
2532 C CA  . GLN B 125 ? 1.3086 1.0802 0.6313 -0.1907 0.4182  0.0005  124 GLN D CA  
2533 C C   . GLN B 125 ? 1.3007 1.1087 0.6281 -0.1905 0.4294  0.0063  124 GLN D C   
2534 O O   . GLN B 125 ? 1.3005 1.1303 0.6379 -0.1776 0.4388  0.0032  124 GLN D O   
2535 C CB  . GLN B 125 ? 1.3076 1.0752 0.6374 -0.2002 0.4114  0.0067  124 GLN D CB  
2536 C CG  . GLN B 125 ? 1.3335 1.1224 0.6818 -0.1917 0.4176  0.0069  124 GLN D CG  
2537 C CD  . GLN B 125 ? 1.3495 1.1403 0.7052 -0.2028 0.4120  0.0142  124 GLN D CD  
2538 O OE1 . GLN B 125 ? 1.3474 1.1188 0.6934 -0.2164 0.4022  0.0184  124 GLN D OE1 
2539 N NE2 . GLN B 125 ? 1.3087 1.1228 0.6809 -0.1965 0.4179  0.0156  124 GLN D NE2 
2540 N N   . LEU B 126 ? 1.3081 1.1231 0.6276 -0.2041 0.4287  0.0147  125 LEU D N   
2541 C CA  . LEU B 126 ? 1.3220 1.1731 0.6464 -0.2051 0.4394  0.0213  125 LEU D CA  
2542 C C   . LEU B 126 ? 1.3594 1.2221 0.6798 -0.1916 0.4481  0.0151  125 LEU D C   
2543 O O   . LEU B 126 ? 1.3416 1.2355 0.6653 -0.1904 0.4576  0.0199  125 LEU D O   
2544 C CB  . LEU B 126 ? 1.3229 1.1750 0.6378 -0.2229 0.4365  0.0314  125 LEU D CB  
2545 C CG  . LEU B 126 ? 1.3208 1.1595 0.6369 -0.2381 0.4270  0.0380  125 LEU D CG  
2546 C CD1 . LEU B 126 ? 1.3595 1.1693 0.6558 -0.2497 0.4175  0.0405  125 LEU D CD1 
2547 C CD2 . LEU B 126 ? 1.3377 1.2098 0.6669 -0.2472 0.4335  0.0479  125 LEU D CD2 
2548 N N   . LYS B 127 ? 1.3565 1.1948 0.6693 -0.1820 0.4449  0.0046  126 LYS D N   
2549 C CA  . LYS B 127 ? 1.3500 1.1982 0.6603 -0.1678 0.4530  -0.0027 126 LYS D CA  
2550 C C   . LYS B 127 ? 1.3270 1.1992 0.6529 -0.1534 0.4617  -0.0054 126 LYS D C   
2551 O O   . LYS B 127 ? 1.3551 1.2540 0.6829 -0.1446 0.4714  -0.0056 126 LYS D O   
2552 C CB  . LYS B 127 ? 1.3561 1.1707 0.6551 -0.1625 0.4469  -0.0135 126 LYS D CB  
2553 C CG  . LYS B 127 ? 1.4016 1.2220 0.6993 -0.1469 0.4543  -0.0228 126 LYS D CG  
2554 C CD  . LYS B 127 ? 1.5107 1.3110 0.7915 -0.1475 0.4509  -0.0291 126 LYS D CD  
2555 C CE  . LYS B 127 ? 1.5427 1.3547 0.8214 -0.1334 0.4597  -0.0368 126 LYS D CE  
2556 N NZ  . LYS B 127 ? 1.5713 1.3612 0.8353 -0.1319 0.4561  -0.0455 126 LYS D NZ  
2557 N N   . SER B 128 ? 1.3386 1.2027 0.6753 -0.1503 0.4584  -0.0072 127 SER D N   
2558 C CA  . SER B 128 ? 1.3467 1.2290 0.6967 -0.1348 0.4656  -0.0111 127 SER D CA  
2559 C C   . SER B 128 ? 1.3707 1.2887 0.7356 -0.1373 0.4711  -0.0021 127 SER D C   
2560 O O   . SER B 128 ? 1.3725 1.3057 0.7494 -0.1247 0.4759  -0.0047 127 SER D O   
2561 C CB  . SER B 128 ? 1.2922 1.1454 0.6456 -0.1277 0.4596  -0.0190 127 SER D CB  
2562 O OG  . SER B 128 ? 1.3183 1.1353 0.6599 -0.1357 0.4495  -0.0224 127 SER D OG  
2563 N N   . GLY B 129 ? 1.3905 1.3213 0.7546 -0.1532 0.4702  0.0082  128 GLY D N   
2564 C CA  . GLY B 129 ? 1.4335 1.4036 0.8109 -0.1560 0.4775  0.0168  128 GLY D CA  
2565 C C   . GLY B 129 ? 1.4450 1.4177 0.8345 -0.1648 0.4730  0.0222  128 GLY D C   
2566 O O   . GLY B 129 ? 1.4677 1.4754 0.8706 -0.1647 0.4798  0.0278  128 GLY D O   
2567 N N   . THR B 130 ? 1.3944 1.3326 0.7795 -0.1723 0.4620  0.0205  129 THR D N   
2568 C CA  . THR B 130 ? 1.4062 1.3448 0.8013 -0.1815 0.4569  0.0255  129 THR D CA  
2569 C C   . THR B 130 ? 1.4058 1.3091 0.7890 -0.1981 0.4443  0.0280  129 THR D C   
2570 O O   . THR B 130 ? 1.3952 1.2664 0.7656 -0.1958 0.4379  0.0219  129 THR D O   
2571 C CB  . THR B 130 ? 1.3711 1.3070 0.7773 -0.1662 0.4573  0.0189  129 THR D CB  
2572 O OG1 . THR B 130 ? 1.3436 1.3136 0.7598 -0.1501 0.4689  0.0167  129 THR D OG1 
2573 C CG2 . THR B 130 ? 1.3315 1.2677 0.7477 -0.1754 0.4519  0.0237  129 THR D CG2 
2574 N N   . ALA B 131 ? 1.3724 1.2823 0.7595 -0.2147 0.4405  0.0367  130 ALA D N   
2575 C CA  . ALA B 131 ? 1.3569 1.2364 0.7315 -0.2315 0.4285  0.0406  130 ALA D CA  
2576 C C   . ALA B 131 ? 1.3145 1.1838 0.6963 -0.2381 0.4205  0.0425  130 ALA D C   
2577 O O   . ALA B 131 ? 1.3144 1.2106 0.7106 -0.2424 0.4246  0.0474  130 ALA D O   
2578 C CB  . ALA B 131 ? 1.3938 1.2864 0.7623 -0.2480 0.4301  0.0500  130 ALA D CB  
2579 N N   . SER B 132 ? 1.3203 1.1521 0.6922 -0.2391 0.4092  0.0385  131 SER D N   
2580 C CA  . SER B 132 ? 1.3372 1.1549 0.7135 -0.2447 0.4003  0.0399  131 SER D CA  
2581 C C   . SER B 132 ? 1.3181 1.1066 0.6788 -0.2614 0.3876  0.0445  131 SER D C   
2582 O O   . SER B 132 ? 1.3427 1.1021 0.6880 -0.2597 0.3809  0.0404  131 SER D O   
2583 C CB  . SER B 132 ? 1.3317 1.1305 0.7110 -0.2287 0.3978  0.0308  131 SER D CB  
2584 O OG  . SER B 132 ? 1.3265 1.1491 0.7194 -0.2119 0.4087  0.0262  131 SER D OG  
2585 N N   . VAL B 133 ? 1.2853 1.0815 0.6499 -0.2771 0.3839  0.0527  132 VAL D N   
2586 C CA  . VAL B 133 ? 1.3152 1.0833 0.6655 -0.2929 0.3709  0.0575  132 VAL D CA  
2587 C C   . VAL B 133 ? 1.3488 1.1036 0.7046 -0.2945 0.3621  0.0571  132 VAL D C   
2588 O O   . VAL B 133 ? 1.3270 1.1056 0.6996 -0.2940 0.3669  0.0586  132 VAL D O   
2589 C CB  . VAL B 133 ? 1.3102 1.0941 0.6584 -0.3112 0.3727  0.0673  132 VAL D CB  
2590 C CG1 . VAL B 133 ? 1.2719 1.0979 0.6407 -0.3140 0.3833  0.0713  132 VAL D CG1 
2591 C CG2 . VAL B 133 ? 1.3060 1.0630 0.6424 -0.3277 0.3591  0.0728  132 VAL D CG2 
2592 N N   . VAL B 134 ? 1.3449 1.0626 0.6862 -0.2956 0.3493  0.0548  133 VAL D N   
2593 C CA  . VAL B 134 ? 1.3369 1.0387 0.6813 -0.2956 0.3399  0.0540  133 VAL D CA  
2594 C C   . VAL B 134 ? 1.3680 1.0455 0.6981 -0.3121 0.3263  0.0602  133 VAL D C   
2595 O O   . VAL B 134 ? 1.3230 0.9815 0.6356 -0.3175 0.3211  0.0615  133 VAL D O   
2596 C CB  . VAL B 134 ? 1.2941 0.9734 0.6357 -0.2786 0.3365  0.0445  133 VAL D CB  
2597 C CG1 . VAL B 134 ? 1.2261 0.9172 0.5713 -0.2638 0.3477  0.0377  133 VAL D CG1 
2598 C CG2 . VAL B 134 ? 1.2828 0.9235 0.6045 -0.2818 0.3223  0.0429  133 VAL D CG2 
2599 N N   . CYS B 135 ? 1.3959 1.0742 0.7331 -0.3198 0.3206  0.0639  134 CYS D N   
2600 C CA  . CYS B 135 ? 1.4069 1.0575 0.7305 -0.3328 0.3057  0.0685  134 CYS D CA  
2601 C C   . CYS B 135 ? 1.3911 1.0160 0.7117 -0.3229 0.2955  0.0632  134 CYS D C   
2602 O O   . CYS B 135 ? 1.3766 1.0133 0.7117 -0.3124 0.3001  0.0595  134 CYS D O   
2603 C CB  . CYS B 135 ? 1.4152 1.0837 0.7478 -0.3504 0.3053  0.0766  134 CYS D CB  
2604 S SG  . CYS B 135 ? 1.5766 1.2103 0.8884 -0.3688 0.2880  0.0832  134 CYS D SG  
2605 N N   . LEU B 136 ? 1.3103 0.9006 0.6116 -0.3252 0.2819  0.0629  135 LEU D N   
2606 C CA  . LEU B 136 ? 1.2675 0.8318 0.5637 -0.3162 0.2709  0.0582  135 LEU D CA  
2607 C C   . LEU B 136 ? 1.2740 0.8217 0.5639 -0.3286 0.2572  0.0640  135 LEU D C   
2608 O O   . LEU B 136 ? 1.2948 0.8337 0.5728 -0.3425 0.2517  0.0699  135 LEU D O   
2609 C CB  . LEU B 136 ? 1.2311 0.7692 0.5099 -0.3073 0.2653  0.0521  135 LEU D CB  
2610 C CG  . LEU B 136 ? 1.2466 0.7564 0.5172 -0.2972 0.2534  0.0464  135 LEU D CG  
2611 C CD1 . LEU B 136 ? 1.2537 0.7503 0.5124 -0.2881 0.2537  0.0395  135 LEU D CD1 
2612 C CD2 . LEU B 136 ? 1.2985 0.7829 0.5552 -0.3058 0.2371  0.0508  135 LEU D CD2 
2613 N N   . LEU B 137 ? 1.2218 0.7634 0.5184 -0.3230 0.2514  0.0623  136 LEU D N   
2614 C CA  . LEU B 137 ? 1.2362 0.7589 0.5261 -0.3324 0.2368  0.0668  136 LEU D CA  
2615 C C   . LEU B 137 ? 1.2301 0.7221 0.5089 -0.3200 0.2243  0.0613  136 LEU D C   
2616 O O   . LEU B 137 ? 1.2665 0.7613 0.5557 -0.3089 0.2252  0.0575  136 LEU D O   
2617 C CB  . LEU B 137 ? 1.2182 0.7643 0.5269 -0.3386 0.2407  0.0705  136 LEU D CB  
2618 C CG  . LEU B 137 ? 1.2338 0.8057 0.5505 -0.3568 0.2476  0.0777  136 LEU D CG  
2619 C CD1 . LEU B 137 ? 1.2339 0.8344 0.5589 -0.3545 0.2640  0.0768  136 LEU D CD1 
2620 C CD2 . LEU B 137 ? 1.2241 0.8169 0.5582 -0.3633 0.2491  0.0806  136 LEU D CD2 
2621 N N   . ASN B 138 ? 1.2325 0.6959 0.4901 -0.3212 0.2126  0.0608  137 ASN D N   
2622 C CA  . ASN B 138 ? 1.2475 0.6845 0.4937 -0.3081 0.2020  0.0545  137 ASN D CA  
2623 C C   . ASN B 138 ? 1.2672 0.6829 0.5064 -0.3107 0.1855  0.0570  137 ASN D C   
2624 O O   . ASN B 138 ? 1.2722 0.6755 0.5000 -0.3231 0.1765  0.0626  137 ASN D O   
2625 C CB  . ASN B 138 ? 1.2864 0.7058 0.5130 -0.3058 0.1987  0.0515  137 ASN D CB  
2626 C CG  . ASN B 138 ? 1.2769 0.6797 0.4974 -0.2899 0.1937  0.0428  137 ASN D CG  
2627 O OD1 . ASN B 138 ? 1.3085 0.6869 0.5104 -0.2876 0.1821  0.0409  137 ASN D OD1 
2628 N ND2 . ASN B 138 ? 1.2782 0.6946 0.5144 -0.2788 0.2024  0.0375  137 ASN D ND2 
2629 N N   . ASN B 139 ? 1.2537 0.6649 0.4997 -0.2987 0.1818  0.0528  138 ASN D N   
2630 C CA  . ASN B 139 ? 1.2777 0.6671 0.5168 -0.2963 0.1653  0.0534  138 ASN D CA  
2631 C C   . ASN B 139 ? 1.2725 0.6639 0.5143 -0.3113 0.1594  0.0612  138 ASN D C   
2632 O O   . ASN B 139 ? 1.3056 0.6791 0.5321 -0.3208 0.1484  0.0648  138 ASN D O   
2633 C CB  . ASN B 139 ? 1.2827 0.6422 0.4988 -0.2914 0.1517  0.0501  138 ASN D CB  
2634 C CG  . ASN B 139 ? 1.3140 0.6714 0.5280 -0.2774 0.1565  0.0418  138 ASN D CG  
2635 O OD1 . ASN B 139 ? 1.3065 0.6833 0.5315 -0.2746 0.1714  0.0392  138 ASN D OD1 
2636 N ND2 . ASN B 139 ? 1.3794 0.7142 0.5800 -0.2680 0.1439  0.0372  138 ASN D ND2 
2637 N N   . PHE B 140 ? 1.2652 0.6782 0.5263 -0.3129 0.1666  0.0633  139 PHE D N   
2638 C CA  . PHE B 140 ? 1.2756 0.6927 0.5414 -0.3276 0.1613  0.0700  139 PHE D CA  
2639 C C   . PHE B 140 ? 1.3071 0.7274 0.5853 -0.3209 0.1578  0.0697  139 PHE D C   
2640 O O   . PHE B 140 ? 1.2577 0.6955 0.5502 -0.3100 0.1691  0.0666  139 PHE D O   
2641 C CB  . PHE B 140 ? 1.2548 0.7017 0.5327 -0.3424 0.1754  0.0749  139 PHE D CB  
2642 C CG  . PHE B 140 ? 1.2581 0.7373 0.5561 -0.3349 0.1934  0.0724  139 PHE D CG  
2643 C CD1 . PHE B 140 ? 1.2634 0.7697 0.5802 -0.3410 0.2009  0.0755  139 PHE D CD1 
2644 C CD2 . PHE B 140 ? 1.2211 0.7044 0.5190 -0.3217 0.2031  0.0666  139 PHE D CD2 
2645 C CE1 . PHE B 140 ? 1.2460 0.7828 0.5803 -0.3325 0.2179  0.0728  139 PHE D CE1 
2646 C CE2 . PHE B 140 ? 1.2413 0.7532 0.5569 -0.3135 0.2196  0.0638  139 PHE D CE2 
2647 C CZ  . PHE B 140 ? 1.2449 0.7838 0.5785 -0.3182 0.2272  0.0669  139 PHE D CZ  
2648 N N   . TYR B 141 ? 1.3463 0.7486 0.6179 -0.3266 0.1421  0.0727  140 TYR D N   
2649 C CA  . TYR B 141 ? 1.3488 0.7547 0.6316 -0.3247 0.1374  0.0742  140 TYR D CA  
2650 C C   . TYR B 141 ? 1.3547 0.7705 0.6427 -0.3456 0.1354  0.0809  140 TYR D C   
2651 O O   . TYR B 141 ? 1.3881 0.7893 0.6626 -0.3578 0.1271  0.0836  140 TYR D O   
2652 C CB  . TYR B 141 ? 1.3545 0.7297 0.6250 -0.3130 0.1186  0.0714  140 TYR D CB  
2653 C CG  . TYR B 141 ? 1.3155 0.6937 0.5980 -0.3052 0.1150  0.0715  140 TYR D CG  
2654 C CD1 . TYR B 141 ? 1.3110 0.7174 0.6162 -0.2945 0.1286  0.0686  140 TYR D CD1 
2655 C CD2 . TYR B 141 ? 1.3134 0.6721 0.5898 -0.3070 0.0969  0.0732  140 TYR D CD2 
2656 C CE1 . TYR B 141 ? 1.2936 0.7131 0.6210 -0.2814 0.1220  0.0650  140 TYR D CE1 
2657 C CE2 . TYR B 141 ? 1.2689 0.6357 0.5621 -0.2974 0.0914  0.0716  140 TYR D CE2 
2658 C CZ  . TYR B 141 ? 1.2694 0.6696 0.5910 -0.2832 0.1032  0.0666  140 TYR D CZ  
2659 O OH  . TYR B 141 ? 1.2377 0.6504 0.5802 -0.2702 0.0959  0.0632  140 TYR D OH  
2660 N N   . PRO B 142 ? 1.3660 0.8066 0.6726 -0.3507 0.1430  0.0834  141 PRO D N   
2661 C CA  . PRO B 142 ? 1.3387 0.8073 0.6706 -0.3325 0.1520  0.0778  141 PRO D CA  
2662 C C   . PRO B 142 ? 1.3439 0.8430 0.6868 -0.3312 0.1731  0.0765  141 PRO D C   
2663 O O   . PRO B 142 ? 1.3588 0.8577 0.6890 -0.3455 0.1812  0.0805  141 PRO D O   
2664 C CB  . PRO B 142 ? 1.2987 0.7902 0.6546 -0.3365 0.1456  0.0781  141 PRO D CB  
2665 C CG  . PRO B 142 ? 1.3491 0.8422 0.6968 -0.3639 0.1461  0.0851  141 PRO D CG  
2666 C CD  . PRO B 142 ? 1.3832 0.8358 0.6959 -0.3727 0.1410  0.0892  141 PRO D CD  
2667 N N   . ARG B 143 ? 1.2670 0.7936 0.6344 -0.3129 0.1817  0.0706  142 ARG D N   
2668 C CA  . ARG B 143 ? 1.2615 0.8193 0.6410 -0.3095 0.2017  0.0688  142 ARG D CA  
2669 C C   . ARG B 143 ? 1.2582 0.8482 0.6496 -0.3283 0.2100  0.0735  142 ARG D C   
2670 O O   . ARG B 143 ? 1.2682 0.8792 0.6617 -0.3316 0.2261  0.0739  142 ARG D O   
2671 C CB  . ARG B 143 ? 1.2687 0.8473 0.6714 -0.2853 0.2078  0.0617  142 ARG D CB  
2672 C CG  . ARG B 143 ? 1.2391 0.8555 0.6593 -0.2796 0.2277  0.0595  142 ARG D CG  
2673 C CD  . ARG B 143 ? 1.2016 0.8268 0.6375 -0.2542 0.2318  0.0526  142 ARG D CD  
2674 N NE  . ARG B 143 ? 1.2225 0.8108 0.6417 -0.2434 0.2235  0.0495  142 ARG D NE  
2675 C CZ  . ARG B 143 ? 1.2315 0.8147 0.6501 -0.2254 0.2319  0.0436  142 ARG D CZ  
2676 N NH1 . ARG B 143 ? 1.2091 0.8184 0.6410 -0.2153 0.2488  0.0404  142 ARG D NH1 
2677 N NH2 . ARG B 143 ? 1.2675 0.8182 0.6710 -0.2175 0.2231  0.0407  142 ARG D NH2 
2678 N N   . GLU B 144 ? 1.2625 0.8586 0.6622 -0.3407 0.1995  0.0766  143 GLU D N   
2679 C CA  . GLU B 144 ? 1.2928 0.9219 0.7049 -0.3600 0.2072  0.0807  143 GLU D CA  
2680 C C   . GLU B 144 ? 1.2782 0.8981 0.6685 -0.3783 0.2161  0.0864  143 GLU D C   
2681 O O   . GLU B 144 ? 1.2997 0.8854 0.6647 -0.3939 0.2066  0.0918  143 GLU D O   
2682 C CB  . GLU B 144 ? 1.3278 0.9562 0.7460 -0.3743 0.1924  0.0835  143 GLU D CB  
2683 C CG  . GLU B 144 ? 1.3278 0.9928 0.7604 -0.3967 0.1995  0.0874  143 GLU D CG  
2684 C CD  . GLU B 144 ? 1.3433 1.0636 0.8082 -0.3867 0.2142  0.0831  143 GLU D CD  
2685 O OE1 . GLU B 144 ? 1.3672 1.1210 0.8485 -0.4023 0.2169  0.0848  143 GLU D OE1 
2686 O OE2 . GLU B 144 ? 1.3632 1.0938 0.8369 -0.3633 0.2229  0.0778  143 GLU D OE2 
2687 N N   . ALA B 145 ? 1.3146 0.9637 0.7132 -0.3755 0.2343  0.0853  144 ALA D N   
2688 C CA  . ALA B 145 ? 1.3352 0.9808 0.7194 -0.3870 0.2415  0.0887  144 ALA D CA  
2689 C C   . ALA B 145 ? 1.3583 1.0511 0.7612 -0.3887 0.2605  0.0884  144 ALA D C   
2690 O O   . ALA B 145 ? 1.4026 1.1185 0.8190 -0.3726 0.2726  0.0837  144 ALA D O   
2691 C CB  . ALA B 145 ? 1.2654 0.8812 0.6334 -0.3706 0.2386  0.0843  144 ALA D CB  
2692 N N   . LYS B 146 ? 1.4106 1.1178 0.8144 -0.4068 0.2629  0.0929  145 LYS D N   
2693 C CA  . LYS B 146 ? 1.4342 1.1854 0.8540 -0.4077 0.2803  0.0927  145 LYS D CA  
2694 C C   . LYS B 146 ? 1.4462 1.1888 0.8536 -0.4139 0.2818  0.0952  145 LYS D C   
2695 O O   . LYS B 146 ? 1.4791 1.2052 0.8753 -0.4317 0.2727  0.1003  145 LYS D O   
2696 C CB  . LYS B 146 ? 1.4469 1.2393 0.8866 -0.4251 0.2852  0.0958  145 LYS D CB  
2697 C CG  . LYS B 146 ? 1.4147 1.2594 0.8762 -0.4167 0.3044  0.0929  145 LYS D CG  
2698 C CD  . LYS B 146 ? 1.4102 1.2578 0.8769 -0.3895 0.3121  0.0859  145 LYS D CD  
2699 C CE  . LYS B 146 ? 1.4020 1.2408 0.8809 -0.3777 0.2980  0.0820  145 LYS D CE  
2700 N NZ  . LYS B 146 ? 1.4045 1.2664 0.9036 -0.3491 0.3050  0.0743  145 LYS D NZ  
2701 N N   . VAL B 147 ? 1.4380 1.1914 0.8471 -0.3989 0.2935  0.0915  146 VAL D N   
2702 C CA  . VAL B 147 ? 1.4073 1.1601 0.8073 -0.4033 0.2978  0.0936  146 VAL D CA  
2703 C C   . VAL B 147 ? 1.4331 1.2354 0.8523 -0.4100 0.3128  0.0956  146 VAL D C   
2704 O O   . VAL B 147 ? 1.4240 1.2602 0.8623 -0.4008 0.3231  0.0924  146 VAL D O   
2705 C CB  . VAL B 147 ? 1.3709 1.1054 0.7606 -0.3829 0.3008  0.0879  146 VAL D CB  
2706 C CG1 . VAL B 147 ? 1.3632 1.0523 0.7351 -0.3768 0.2857  0.0856  146 VAL D CG1 
2707 C CG2 . VAL B 147 ? 1.3786 1.1405 0.7851 -0.3637 0.3143  0.0819  146 VAL D CG2 
2708 N N   . GLN B 148 ? 1.4220 1.2295 0.8358 -0.4255 0.3142  0.1009  147 GLN D N   
2709 C CA  . GLN B 148 ? 1.4417 1.2959 0.8721 -0.4320 0.3284  0.1030  147 GLN D CA  
2710 C C   . GLN B 148 ? 1.4882 1.3404 0.9084 -0.4269 0.3355  0.1036  147 GLN D C   
2711 O O   . GLN B 148 ? 1.5005 1.3221 0.9011 -0.4354 0.3278  0.1071  147 GLN D O   
2712 C CB  . GLN B 148 ? 1.4869 1.3554 0.9227 -0.4582 0.3246  0.1093  147 GLN D CB  
2713 C CG  . GLN B 148 ? 1.5092 1.4286 0.9721 -0.4637 0.3329  0.1086  147 GLN D CG  
2714 C CD  . GLN B 148 ? 1.5148 1.4829 0.9959 -0.4516 0.3509  0.1060  147 GLN D CD  
2715 O OE1 . GLN B 148 ? 1.5143 1.4781 0.9887 -0.4367 0.3579  0.1041  147 GLN D OE1 
2716 N NE2 . GLN B 148 ? 1.5533 1.5692 1.0578 -0.4577 0.3580  0.1055  147 GLN D NE2 
2717 N N   . TRP B 149 ? 1.4960 1.3811 0.9291 -0.4124 0.3501  0.1002  148 TRP D N   
2718 C CA  . TRP B 149 ? 1.4696 1.3563 0.8945 -0.4058 0.3578  0.1003  148 TRP D CA  
2719 C C   . TRP B 149 ? 1.4698 1.3883 0.9014 -0.4225 0.3655  0.1065  148 TRP D C   
2720 O O   . TRP B 149 ? 1.4937 1.4545 0.9461 -0.4268 0.3736  0.1072  148 TRP D O   
2721 C CB  . TRP B 149 ? 1.4584 1.3629 0.8924 -0.3810 0.3694  0.0932  148 TRP D CB  
2722 C CG  . TRP B 149 ? 1.4254 1.2918 0.8461 -0.3643 0.3629  0.0871  148 TRP D CG  
2723 C CD1 . TRP B 149 ? 1.4452 1.3007 0.8702 -0.3518 0.3593  0.0818  148 TRP D CD1 
2724 C CD2 . TRP B 149 ? 1.4166 1.2517 0.8176 -0.3584 0.3593  0.0853  148 TRP D CD2 
2725 N NE1 . TRP B 149 ? 1.4145 1.2340 0.8244 -0.3389 0.3536  0.0767  148 TRP D NE1 
2726 C CE2 . TRP B 149 ? 1.3891 1.1964 0.7844 -0.3428 0.3533  0.0785  148 TRP D CE2 
2727 C CE3 . TRP B 149 ? 1.4104 1.2393 0.7982 -0.3646 0.3607  0.0886  148 TRP D CE3 
2728 C CZ2 . TRP B 149 ? 1.3512 1.1264 0.7289 -0.3341 0.3485  0.0743  148 TRP D CZ2 
2729 C CZ3 . TRP B 149 ? 1.3712 1.1681 0.7410 -0.3553 0.3560  0.0846  148 TRP D CZ3 
2730 C CH2 . TRP B 149 ? 1.3592 1.1303 0.7245 -0.3405 0.3498  0.0773  148 TRP D CH2 
2731 N N   . LYS B 150 ? 1.5096 1.4090 0.9240 -0.4312 0.3631  0.1109  149 LYS D N   
2732 C CA  . LYS B 150 ? 1.5038 1.4276 0.9211 -0.4484 0.3695  0.1175  149 LYS D CA  
2733 C C   . LYS B 150 ? 1.4695 1.3901 0.8748 -0.4405 0.3765  0.1181  149 LYS D C   
2734 O O   . LYS B 150 ? 1.4581 1.3397 0.8424 -0.4362 0.3691  0.1173  149 LYS D O   
2735 C CB  . LYS B 150 ? 1.4908 1.3902 0.8964 -0.4725 0.3574  0.1238  149 LYS D CB  
2736 C CG  . LYS B 150 ? 1.5340 1.4588 0.9575 -0.4888 0.3558  0.1257  149 LYS D CG  
2737 C CD  . LYS B 150 ? 1.5952 1.4813 1.0056 -0.5037 0.3390  0.1281  149 LYS D CD  
2738 C CE  . LYS B 150 ? 1.6240 1.4630 1.0056 -0.5097 0.3294  0.1320  149 LYS D CE  
2739 N NZ  . LYS B 150 ? 1.6117 1.4205 0.9816 -0.5284 0.3147  0.1357  149 LYS D NZ  
2740 N N   . VAL B 151 ? 1.5488 1.5111 0.9673 -0.4380 0.3907  0.1191  150 VAL D N   
2741 C CA  . VAL B 151 ? 1.5671 1.5311 0.9750 -0.4331 0.3983  0.1208  150 VAL D CA  
2742 C C   . VAL B 151 ? 1.5775 1.5680 0.9896 -0.4528 0.4044  0.1286  150 VAL D C   
2743 O O   . VAL B 151 ? 1.5459 1.5799 0.9791 -0.4572 0.4129  0.1294  150 VAL D O   
2744 C CB  . VAL B 151 ? 1.5188 1.5049 0.9352 -0.4086 0.4100  0.1144  150 VAL D CB  
2745 C CG1 . VAL B 151 ? 1.4693 1.5077 0.9113 -0.4047 0.4220  0.1135  150 VAL D CG1 
2746 C CG2 . VAL B 151 ? 1.5259 1.5090 0.9289 -0.4045 0.4160  0.1162  150 VAL D CG2 
2747 N N   . ASP B 152 ? 1.6721 1.6365 1.0640 -0.4645 0.4000  0.1341  151 ASP D N   
2748 C CA  . ASP B 152 ? 1.6863 1.6687 1.0783 -0.4848 0.4047  0.1420  151 ASP D CA  
2749 C C   . ASP B 152 ? 1.7034 1.7030 1.1100 -0.5052 0.4012  0.1449  151 ASP D C   
2750 O O   . ASP B 152 ? 1.7264 1.7617 1.1454 -0.5187 0.4092  0.1490  151 ASP D O   
2751 C CB  . ASP B 152 ? 1.6872 1.7114 1.0896 -0.4765 0.4210  0.1426  151 ASP D CB  
2752 C CG  . ASP B 152 ? 1.6965 1.7022 1.0808 -0.4616 0.4242  0.1415  151 ASP D CG  
2753 O OD1 . ASP B 152 ? 1.7045 1.6673 1.0697 -0.4560 0.4142  0.1392  151 ASP D OD1 
2754 O OD2 . ASP B 152 ? 1.6966 1.7321 1.0859 -0.4551 0.4367  0.1425  151 ASP D OD2 
2755 N N   . ASN B 153 ? 1.5751 1.5488 0.9797 -0.5076 0.3887  0.1424  152 ASN D N   
2756 C CA  . ASN B 153 ? 1.5281 1.5134 0.9460 -0.5248 0.3831  0.1435  152 ASN D CA  
2757 C C   . ASN B 153 ? 1.4904 1.5291 0.9379 -0.5194 0.3932  0.1397  152 ASN D C   
2758 O O   . ASN B 153 ? 1.4631 1.5260 0.9252 -0.5365 0.3924  0.1414  152 ASN D O   
2759 C CB  . ASN B 153 ? 1.5652 1.5486 0.9770 -0.5525 0.3802  0.1512  152 ASN D CB  
2760 C CG  . ASN B 153 ? 1.5742 1.5057 0.9559 -0.5596 0.3702  0.1557  152 ASN D CG  
2761 O OD1 . ASN B 153 ? 1.6079 1.5265 0.9750 -0.5502 0.3739  0.1567  152 ASN D OD1 
2762 N ND2 . ASN B 153 ? 1.5085 1.4100 0.8800 -0.5755 0.3571  0.1580  152 ASN D ND2 
2763 N N   . ALA B 154 ? 1.5421 1.6010 0.9991 -0.4960 0.4026  0.1342  153 ALA D N   
2764 C CA  . ALA B 154 ? 1.5299 1.6362 1.0136 -0.4873 0.4112  0.1297  153 ALA D CA  
2765 C C   . ALA B 154 ? 1.5551 1.6429 1.0405 -0.4707 0.4049  0.1230  153 ALA D C   
2766 O O   . ALA B 154 ? 1.5288 1.5963 1.0049 -0.4499 0.4059  0.1188  153 ALA D O   
2767 C CB  . ALA B 154 ? 1.4703 1.6152 0.9639 -0.4717 0.4271  0.1281  153 ALA D CB  
2768 N N   . LEU B 155 ? 1.5673 1.6613 1.0639 -0.4806 0.3983  0.1222  154 LEU D N   
2769 C CA  . LEU B 155 ? 1.6079 1.6861 1.1069 -0.4662 0.3924  0.1163  154 LEU D CA  
2770 C C   . LEU B 155 ? 1.6235 1.7249 1.1331 -0.4383 0.4040  0.1098  154 LEU D C   
2771 O O   . LEU B 155 ? 1.5988 1.7447 1.1235 -0.4326 0.4169  0.1091  154 LEU D O   
2772 C CB  . LEU B 155 ? 1.6503 1.7477 1.1656 -0.4802 0.3871  0.1161  154 LEU D CB  
2773 C CG  . LEU B 155 ? 1.6715 1.7541 1.1798 -0.5097 0.3768  0.1224  154 LEU D CG  
2774 C CD1 . LEU B 155 ? 1.6582 1.7793 1.1894 -0.5241 0.3763  0.1216  154 LEU D CD1 
2775 C CD2 . LEU B 155 ? 1.6915 1.7129 1.1755 -0.5124 0.3609  0.1235  154 LEU D CD2 
2776 N N   . GLN B 156 ? 1.5641 1.6343 1.0648 -0.4203 0.3995  0.1047  155 GLN D N   
2777 C CA  . GLN B 156 ? 1.5400 1.6213 1.0454 -0.3927 0.4094  0.0982  155 GLN D CA  
2778 C C   . GLN B 156 ? 1.5419 1.6305 1.0598 -0.3796 0.4085  0.0924  155 GLN D C   
2779 O O   . GLN B 156 ? 1.5260 1.5803 1.0354 -0.3819 0.3971  0.0914  155 GLN D O   
2780 C CB  . GLN B 156 ? 1.5420 1.5802 1.0253 -0.3808 0.4058  0.0963  155 GLN D CB  
2781 C CG  . GLN B 156 ? 1.5262 1.5566 0.9956 -0.3904 0.4074  0.1014  155 GLN D CG  
2782 C CD  . GLN B 156 ? 1.5201 1.5966 1.0021 -0.3867 0.4224  0.1027  155 GLN D CD  
2783 O OE1 . GLN B 156 ? 1.5320 1.6205 1.0163 -0.3657 0.4317  0.0981  155 GLN D OE1 
2784 N NE2 . GLN B 156 ? 1.4963 1.5980 0.9857 -0.4073 0.4245  0.1089  155 GLN D NE2 
2785 N N   . SER B 157 ? 1.5446 1.6775 1.0818 -0.3646 0.4207  0.0884  156 SER D N   
2786 C CA  . SER B 157 ? 1.5434 1.6882 1.0934 -0.3488 0.4221  0.0824  156 SER D CA  
2787 C C   . SER B 157 ? 1.5546 1.7104 1.1074 -0.3187 0.4336  0.0760  156 SER D C   
2788 O O   . SER B 157 ? 1.5646 1.7417 1.1189 -0.3122 0.4435  0.0765  156 SER D O   
2789 C CB  . SER B 157 ? 1.5642 1.7579 1.1378 -0.3600 0.4249  0.0831  156 SER D CB  
2790 O OG  . SER B 157 ? 1.6080 1.8146 1.1938 -0.3440 0.4262  0.0770  156 SER D OG  
2791 N N   . GLY B 158 ? 1.5679 1.7073 1.1204 -0.3001 0.4321  0.0699  157 GLY D N   
2792 C CA  . GLY B 158 ? 1.5206 1.6687 1.0762 -0.2705 0.4421  0.0632  157 GLY D CA  
2793 C C   . GLY B 158 ? 1.5243 1.6321 1.0607 -0.2576 0.4408  0.0604  157 GLY D C   
2794 O O   . GLY B 158 ? 1.5143 1.6201 1.0512 -0.2329 0.4467  0.0540  157 GLY D O   
2795 N N   . ASN B 159 ? 1.5054 1.5814 1.0250 -0.2733 0.4328  0.0645  158 ASN D N   
2796 C CA  . ASN B 159 ? 1.4898 1.5307 0.9915 -0.2633 0.4310  0.0615  158 ASN D CA  
2797 C C   . ASN B 159 ? 1.4509 1.4415 0.9381 -0.2627 0.4183  0.0586  158 ASN D C   
2798 O O   . ASN B 159 ? 1.4436 1.4095 0.9212 -0.2473 0.4180  0.0529  158 ASN D O   
2799 C CB  . ASN B 159 ? 1.4718 1.5117 0.9633 -0.2783 0.4313  0.0671  158 ASN D CB  
2800 C CG  . ASN B 159 ? 1.5259 1.5843 1.0234 -0.3042 0.4284  0.0751  158 ASN D CG  
2801 O OD1 . ASN B 159 ? 1.5594 1.6602 1.0706 -0.3080 0.4377  0.0779  158 ASN D OD1 
2802 N ND2 . ASN B 159 ? 1.5261 1.5533 1.0139 -0.3218 0.4153  0.0785  158 ASN D ND2 
2803 N N   . SER B 160 ? 1.4462 1.4217 0.9320 -0.2786 0.4077  0.0621  159 SER D N   
2804 C CA  . SER B 160 ? 1.4154 1.3421 0.8851 -0.2801 0.3946  0.0605  159 SER D CA  
2805 C C   . SER B 160 ? 1.3960 1.3106 0.8695 -0.2599 0.3945  0.0534  159 SER D C   
2806 O O   . SER B 160 ? 1.4138 1.3571 0.9033 -0.2491 0.4022  0.0511  159 SER D O   
2807 C CB  . SER B 160 ? 1.4749 1.3886 0.9404 -0.3038 0.3825  0.0669  159 SER D CB  
2808 O OG  . SER B 160 ? 1.5224 1.4582 0.9902 -0.3226 0.3849  0.0737  159 SER D OG  
2809 N N   . GLN B 161 ? 1.3399 1.2121 0.7985 -0.2542 0.3857  0.0497  160 GLN D N   
2810 C CA  . GLN B 161 ? 1.2893 1.1441 0.7496 -0.2361 0.3841  0.0432  160 GLN D CA  
2811 C C   . GLN B 161 ? 1.2702 1.0785 0.7137 -0.2411 0.3694  0.0426  160 GLN D C   
2812 O O   . GLN B 161 ? 1.2559 1.0402 0.6856 -0.2402 0.3657  0.0403  160 GLN D O   
2813 C CB  . GLN B 161 ? 1.2394 1.0993 0.7026 -0.2130 0.3941  0.0358  160 GLN D CB  
2814 C CG  . GLN B 161 ? 1.1900 1.0830 0.6711 -0.1964 0.4051  0.0330  160 GLN D CG  
2815 C CD  . GLN B 161 ? 1.2509 1.1391 0.7322 -0.1722 0.4120  0.0251  160 GLN D CD  
2816 O OE1 . GLN B 161 ? 1.2810 1.1447 0.7502 -0.1698 0.4095  0.0217  160 GLN D OE1 
2817 N NE2 . GLN B 161 ? 1.2212 1.1313 0.7161 -0.1540 0.4200  0.0216  160 GLN D NE2 
2818 N N   . GLU B 162 ? 1.2513 1.0482 0.6957 -0.2458 0.3612  0.0442  161 GLU D N   
2819 C CA  . GLU B 162 ? 1.2265 0.9818 0.6552 -0.2515 0.3460  0.0446  161 GLU D CA  
2820 C C   . GLU B 162 ? 1.1496 0.8852 0.5789 -0.2335 0.3436  0.0383  161 GLU D C   
2821 O O   . GLU B 162 ? 1.1413 0.8959 0.5844 -0.2206 0.3516  0.0357  161 GLU D O   
2822 C CB  . GLU B 162 ? 1.2311 0.9838 0.6575 -0.2728 0.3358  0.0522  161 GLU D CB  
2823 C CG  . GLU B 162 ? 1.2694 1.0621 0.7140 -0.2798 0.3432  0.0558  161 GLU D CG  
2824 C CD  . GLU B 162 ? 1.2913 1.0821 0.7334 -0.3041 0.3328  0.0633  161 GLU D CD  
2825 O OE1 . GLU B 162 ? 1.2729 1.0276 0.7010 -0.3099 0.3182  0.0649  161 GLU D OE1 
2826 O OE2 . GLU B 162 ? 1.3681 1.1935 0.8222 -0.3171 0.3387  0.0675  161 GLU D OE2 
2827 N N   . SER B 163 ? 1.1084 0.8066 0.5227 -0.2319 0.3327  0.0356  162 SER D N   
2828 C CA  . SER B 163 ? 1.1431 0.8182 0.5557 -0.2184 0.3273  0.0308  162 SER D CA  
2829 C C   . SER B 163 ? 1.1805 0.8229 0.5777 -0.2298 0.3102  0.0339  162 SER D C   
2830 O O   . SER B 163 ? 1.1547 0.7862 0.5398 -0.2437 0.3031  0.0373  162 SER D O   
2831 C CB  . SER B 163 ? 1.0888 0.7523 0.4999 -0.2005 0.3323  0.0223  162 SER D CB  
2832 O OG  . SER B 163 ? 1.1469 0.7887 0.5429 -0.2063 0.3260  0.0206  162 SER D OG  
2833 N N   . VAL B 164 ? 1.1376 0.7646 0.5348 -0.2231 0.3033  0.0328  163 VAL D N   
2834 C CA  . VAL B 164 ? 1.1527 0.7509 0.5360 -0.2329 0.2863  0.0362  163 VAL D CA  
2835 C C   . VAL B 164 ? 1.1139 0.6829 0.4892 -0.2190 0.2791  0.0298  163 VAL D C   
2836 O O   . VAL B 164 ? 1.1414 0.7136 0.5254 -0.2024 0.2862  0.0245  163 VAL D O   
2837 C CB  . VAL B 164 ? 1.1438 0.7503 0.5329 -0.2419 0.2816  0.0424  163 VAL D CB  
2838 C CG1 . VAL B 164 ? 1.1388 0.7152 0.5120 -0.2539 0.2628  0.0466  163 VAL D CG1 
2839 C CG2 . VAL B 164 ? 1.1285 0.7698 0.5286 -0.2553 0.2909  0.0476  163 VAL D CG2 
2840 N N   . THR B 165 ? 1.1376 0.6790 0.4962 -0.2255 0.2653  0.0301  164 THR D N   
2841 C CA  . THR B 165 ? 1.1600 0.6746 0.5101 -0.2142 0.2569  0.0241  164 THR D CA  
2842 C C   . THR B 165 ? 1.1627 0.6683 0.5149 -0.2097 0.2488  0.0261  164 THR D C   
2843 O O   . THR B 165 ? 1.2052 0.7189 0.5608 -0.2190 0.2456  0.0329  164 THR D O   
2844 C CB  . THR B 165 ? 1.1763 0.6672 0.5075 -0.2223 0.2445  0.0238  164 THR D CB  
2845 O OG1 . THR B 165 ? 1.1560 0.6332 0.4822 -0.2109 0.2450  0.0154  164 THR D OG1 
2846 C CG2 . THR B 165 ? 1.1615 0.6310 0.4813 -0.2294 0.2268  0.0284  164 THR D CG2 
2847 N N   . GLU B 166 ? 1.1000 0.5899 0.4509 -0.1954 0.2458  0.0202  165 GLU D N   
2848 C CA  . GLU B 166 ? 1.1923 0.6704 0.5422 -0.1917 0.2356  0.0228  165 GLU D CA  
2849 C C   . GLU B 166 ? 1.2174 0.6705 0.5503 -0.2014 0.2165  0.0258  165 GLU D C   
2850 O O   . GLU B 166 ? 1.2674 0.7095 0.5886 -0.2067 0.2119  0.0237  165 GLU D O   
2851 C CB  . GLU B 166 ? 1.2048 0.6760 0.5606 -0.1725 0.2383  0.0158  165 GLU D CB  
2852 C CG  . GLU B 166 ? 1.1562 0.6535 0.5361 -0.1590 0.2505  0.0139  165 GLU D CG  
2853 C CD  . GLU B 166 ? 1.2097 0.7291 0.6085 -0.1619 0.2446  0.0194  165 GLU D CD  
2854 O OE1 . GLU B 166 ? 1.3163 0.8278 0.7196 -0.1585 0.2300  0.0206  165 GLU D OE1 
2855 O OE2 . GLU B 166 ? 1.1346 0.6797 0.5430 -0.1683 0.2542  0.0223  165 GLU D OE2 
2856 N N   . GLN B 167 ? 1.2261 0.6735 0.5620 -0.2019 0.2034  0.0295  166 GLN D N   
2857 C CA  . GLN B 167 ? 1.2483 0.6686 0.5649 -0.2096 0.1851  0.0327  166 GLN D CA  
2858 C C   . GLN B 167 ? 1.2584 0.6593 0.5619 -0.2023 0.1796  0.0258  166 GLN D C   
2859 O O   . GLN B 167 ? 1.2467 0.6462 0.5545 -0.1885 0.1847  0.0193  166 GLN D O   
2860 C CB  . GLN B 167 ? 1.2491 0.6676 0.5778 -0.2023 0.1703  0.0335  166 GLN D CB  
2861 C CG  . GLN B 167 ? 1.2457 0.6474 0.5615 -0.2154 0.1530  0.0397  166 GLN D CG  
2862 C CD  . GLN B 167 ? 1.2482 0.6576 0.5814 -0.2111 0.1415  0.0413  166 GLN D CD  
2863 O OE1 . GLN B 167 ? 1.2655 0.6744 0.6087 -0.1948 0.1368  0.0371  166 GLN D OE1 
2864 N NE2 . GLN B 167 ? 1.2348 0.6507 0.5707 -0.2262 0.1364  0.0471  166 GLN D NE2 
2865 N N   . ASP B 168 ? 1.2772 0.6648 0.5658 -0.2116 0.1700  0.0266  167 ASP D N   
2866 C CA  . ASP B 168 ? 1.3376 0.7087 0.6136 -0.2050 0.1642  0.0197  167 ASP D CA  
2867 C C   . ASP B 168 ? 1.4143 0.7662 0.6835 -0.1959 0.1485  0.0178  167 ASP D C   
2868 O O   . ASP B 168 ? 1.4293 0.7762 0.6992 -0.1974 0.1383  0.0229  167 ASP D O   
2869 C CB  . ASP B 168 ? 1.3909 0.7538 0.6516 -0.2162 0.1592  0.0210  167 ASP D CB  
2870 C CG  . ASP B 168 ? 1.5008 0.8477 0.7480 -0.2096 0.1532  0.0140  167 ASP D CG  
2871 O OD1 . ASP B 168 ? 1.5217 0.8738 0.7749 -0.2006 0.1624  0.0071  167 ASP D OD1 
2872 O OD2 . ASP B 168 ? 1.5450 0.8742 0.7757 -0.2134 0.1393  0.0151  167 ASP D OD2 
2873 N N   . SER B 169 ? 1.5291 0.8714 0.7925 -0.1861 0.1465  0.0102  168 SER D N   
2874 C CA  . SER B 169 ? 1.5725 0.8991 0.8304 -0.1762 0.1322  0.0077  168 SER D CA  
2875 C C   . SER B 169 ? 1.5842 0.8920 0.8239 -0.1812 0.1138  0.0094  168 SER D C   
2876 O O   . SER B 169 ? 1.5874 0.8839 0.8232 -0.1761 0.0993  0.0105  168 SER D O   
2877 C CB  . SER B 169 ? 1.5776 0.9028 0.8377 -0.1646 0.1371  -0.0012 168 SER D CB  
2878 O OG  . SER B 169 ? 1.6013 0.9111 0.8531 -0.1570 0.1214  -0.0038 168 SER D OG  
2879 N N   . LYS B 170 ? 1.5354 0.8395 0.7638 -0.1901 0.1142  0.0096  169 LYS D N   
2880 C CA  . LYS B 170 ? 1.5556 0.8404 0.7651 -0.1936 0.0977  0.0106  169 LYS D CA  
2881 C C   . LYS B 170 ? 1.5081 0.7902 0.7135 -0.2059 0.0914  0.0187  169 LYS D C   
2882 O O   . LYS B 170 ? 1.5140 0.7831 0.7128 -0.2048 0.0760  0.0209  169 LYS D O   
2883 C CB  . LYS B 170 ? 1.6408 0.9216 0.8391 -0.1960 0.1010  0.0069  169 LYS D CB  
2884 C CG  . LYS B 170 ? 1.6455 0.9326 0.8512 -0.1862 0.1096  -0.0010 169 LYS D CG  
2885 C CD  . LYS B 170 ? 1.6716 0.9711 0.8803 -0.1917 0.1253  -0.0027 169 LYS D CD  
2886 C CE  . LYS B 170 ? 1.7082 1.0221 0.9337 -0.1836 0.1396  -0.0088 169 LYS D CE  
2887 N NZ  . LYS B 170 ? 1.6650 0.9948 0.8975 -0.1889 0.1564  -0.0096 169 LYS D NZ  
2888 N N   . ASP B 171 ? 1.4639 0.7589 0.6739 -0.2179 0.1031  0.0231  170 ASP D N   
2889 C CA  . ASP B 171 ? 1.4111 0.7048 0.6182 -0.2316 0.0982  0.0309  170 ASP D CA  
2890 C C   . ASP B 171 ? 1.3768 0.6805 0.5995 -0.2335 0.0981  0.0358  170 ASP D C   
2891 O O   . ASP B 171 ? 1.3609 0.6591 0.5802 -0.2436 0.0895  0.0415  170 ASP D O   
2892 C CB  . ASP B 171 ? 1.3692 0.6757 0.5772 -0.2441 0.1112  0.0340  170 ASP D CB  
2893 C CG  . ASP B 171 ? 1.5342 0.8386 0.7337 -0.2402 0.1171  0.0285  170 ASP D CG  
2894 O OD1 . ASP B 171 ? 1.6996 0.9843 0.8810 -0.2374 0.1057  0.0260  170 ASP D OD1 
2895 O OD2 . ASP B 171 ? 1.6315 0.9542 0.8425 -0.2394 0.1330  0.0263  170 ASP D OD2 
2896 N N   . SER B 172 ? 1.3901 0.7075 0.6291 -0.2242 0.1077  0.0336  171 SER D N   
2897 C CA  . SER B 172 ? 1.3267 0.6594 0.5828 -0.2269 0.1133  0.0387  171 SER D CA  
2898 C C   . SER B 172 ? 1.2817 0.6327 0.5448 -0.2430 0.1249  0.0445  171 SER D C   
2899 O O   . SER B 172 ? 1.2655 0.6256 0.5376 -0.2514 0.1249  0.0503  171 SER D O   
2900 C CB  . SER B 172 ? 1.2614 0.5813 0.5160 -0.2259 0.0961  0.0419  171 SER D CB  
2901 O OG  . SER B 172 ? 1.2175 0.5247 0.4688 -0.2098 0.0861  0.0367  171 SER D OG  
2902 N N   . THR B 173 ? 1.2705 0.6282 0.5297 -0.2477 0.1348  0.0428  172 THR D N   
2903 C CA  . THR B 173 ? 1.3155 0.6921 0.5809 -0.2626 0.1459  0.0480  172 THR D CA  
2904 C C   . THR B 173 ? 1.2734 0.6769 0.5556 -0.2579 0.1664  0.0457  172 THR D C   
2905 O O   . THR B 173 ? 1.2600 0.6661 0.5484 -0.2433 0.1726  0.0399  172 THR D O   
2906 C CB  . THR B 173 ? 1.2691 0.6360 0.5183 -0.2721 0.1431  0.0488  172 THR D CB  
2907 O OG1 . THR B 173 ? 1.2798 0.6344 0.5183 -0.2610 0.1419  0.0418  172 THR D OG1 
2908 C CG2 . THR B 173 ? 1.2992 0.6467 0.5346 -0.2823 0.1266  0.0536  172 THR D CG2 
2909 N N   . TYR B 174 ? 1.1997 0.6237 0.4888 -0.2704 0.1768  0.0501  173 TYR D N   
2910 C CA  . TYR B 174 ? 1.1811 0.6340 0.4861 -0.2677 0.1962  0.0487  173 TYR D CA  
2911 C C   . TYR B 174 ? 1.2164 0.6758 0.5158 -0.2748 0.2033  0.0485  173 TYR D C   
2912 O O   . TYR B 174 ? 1.2641 0.7110 0.5500 -0.2864 0.1948  0.0521  173 TYR D O   
2913 C CB  . TYR B 174 ? 1.2090 0.6858 0.5295 -0.2764 0.2026  0.0545  173 TYR D CB  
2914 C CG  . TYR B 174 ? 1.2447 0.7184 0.5721 -0.2685 0.1977  0.0549  173 TYR D CG  
2915 C CD1 . TYR B 174 ? 1.2648 0.7293 0.5953 -0.2487 0.1957  0.0481  173 TYR D CD1 
2916 C CD2 . TYR B 174 ? 1.2515 0.7366 0.5921 -0.2767 0.1893  0.0590  173 TYR D CD2 
2917 C CE1 . TYR B 174 ? 1.2423 0.7113 0.5899 -0.2364 0.1870  0.0459  173 TYR D CE1 
2918 C CE2 . TYR B 174 ? 1.2481 0.7379 0.6059 -0.2643 0.1800  0.0563  173 TYR D CE2 
2919 C CZ  . TYR B 174 ? 1.2415 0.7228 0.6022 -0.2437 0.1790  0.0500  173 TYR D CZ  
2920 O OH  . TYR B 174 ? 1.2599 0.7452 0.6365 -0.2305 0.1702  0.0475  173 TYR D OH  
2921 N N   . SER B 175 ? 1.2316 0.7099 0.5408 -0.2670 0.2189  0.0441  174 SER D N   
2922 C CA  . SER B 175 ? 1.1704 0.6618 0.4781 -0.2739 0.2282  0.0448  174 SER D CA  
2923 C C   . SER B 175 ? 1.1541 0.6807 0.4815 -0.2729 0.2457  0.0456  174 SER D C   
2924 O O   . SER B 175 ? 1.1580 0.6956 0.4983 -0.2606 0.2531  0.0421  174 SER D O   
2925 C CB  . SER B 175 ? 1.2084 0.6866 0.5058 -0.2644 0.2292  0.0376  174 SER D CB  
2926 O OG  . SER B 175 ? 1.2078 0.6561 0.4861 -0.2653 0.2134  0.0367  174 SER D OG  
2927 N N   . LEU B 176 ? 1.1562 0.7008 0.4854 -0.2854 0.2522  0.0502  175 LEU D N   
2928 C CA  . LEU B 176 ? 1.1690 0.7502 0.5163 -0.2852 0.2687  0.0511  175 LEU D CA  
2929 C C   . LEU B 176 ? 1.1744 0.7658 0.5186 -0.2862 0.2777  0.0499  175 LEU D C   
2930 O O   . LEU B 176 ? 1.1999 0.7770 0.5293 -0.2960 0.2713  0.0525  175 LEU D O   
2931 C CB  . LEU B 176 ? 1.1582 0.7594 0.5146 -0.3015 0.2689  0.0589  175 LEU D CB  
2932 C CG  . LEU B 176 ? 1.1539 0.7978 0.5301 -0.3026 0.2854  0.0602  175 LEU D CG  
2933 C CD1 . LEU B 176 ? 1.1753 0.8359 0.5634 -0.3114 0.2843  0.0646  175 LEU D CD1 
2934 C CD2 . LEU B 176 ? 1.1921 0.8525 0.5669 -0.3147 0.2917  0.0640  175 LEU D CD2 
2935 N N   . SER B 177 ? 1.1657 0.7818 0.5232 -0.2753 0.2926  0.0459  176 SER D N   
2936 C CA  . SER B 177 ? 1.2121 0.8422 0.5686 -0.2753 0.3025  0.0449  176 SER D CA  
2937 C C   . SER B 177 ? 1.2353 0.9060 0.6105 -0.2754 0.3172  0.0472  176 SER D C   
2938 O O   . SER B 177 ? 1.2052 0.8911 0.5938 -0.2610 0.3260  0.0428  176 SER D O   
2939 C CB  . SER B 177 ? 1.1813 0.7984 0.5331 -0.2591 0.3056  0.0361  176 SER D CB  
2940 O OG  . SER B 177 ? 1.1929 0.8337 0.5603 -0.2453 0.3194  0.0316  176 SER D OG  
2941 N N   . SER B 178 ? 1.2387 0.9272 0.6146 -0.2909 0.3198  0.0539  177 SER D N   
2942 C CA  . SER B 178 ? 1.2523 0.9827 0.6453 -0.2922 0.3339  0.0563  177 SER D CA  
2943 C C   . SER B 178 ? 1.2777 1.0195 0.6677 -0.2885 0.3432  0.0548  177 SER D C   
2944 O O   . SER B 178 ? 1.3278 1.0591 0.7048 -0.3000 0.3391  0.0586  177 SER D O   
2945 C CB  . SER B 178 ? 1.2690 1.0148 0.6665 -0.3131 0.3309  0.0648  177 SER D CB  
2946 O OG  . SER B 178 ? 1.3131 1.1028 0.7301 -0.3133 0.3439  0.0662  177 SER D OG  
2947 N N   . THR B 179 ? 1.2390 1.0019 0.6400 -0.2722 0.3556  0.0496  178 THR D N   
2948 C CA  . THR B 179 ? 1.3011 1.0756 0.6992 -0.2675 0.3645  0.0479  178 THR D CA  
2949 C C   . THR B 179 ? 1.3323 1.1511 0.7454 -0.2713 0.3769  0.0524  178 THR D C   
2950 O O   . THR B 179 ? 1.3050 1.1496 0.7345 -0.2654 0.3833  0.0519  178 THR D O   
2951 C CB  . THR B 179 ? 1.2887 1.0554 0.6870 -0.2463 0.3698  0.0386  178 THR D CB  
2952 O OG1 . THR B 179 ? 1.3448 1.1437 0.7605 -0.2334 0.3821  0.0364  178 THR D OG1 
2953 C CG2 . THR B 179 ? 1.3065 1.0384 0.6983 -0.2393 0.3594  0.0334  178 THR D CG2 
2954 N N   . LEU B 180 ? 1.3144 1.1425 0.7214 -0.2802 0.3804  0.0564  179 LEU D N   
2955 C CA  . LEU B 180 ? 1.2930 1.1631 0.7123 -0.2845 0.3921  0.0609  179 LEU D CA  
2956 C C   . LEU B 180 ? 1.2842 1.1650 0.7019 -0.2692 0.4023  0.0562  179 LEU D C   
2957 O O   . LEU B 180 ? 1.3023 1.1615 0.7045 -0.2698 0.3993  0.0549  179 LEU D O   
2958 C CB  . LEU B 180 ? 1.3298 1.2004 0.7421 -0.3076 0.3875  0.0697  179 LEU D CB  
2959 C CG  . LEU B 180 ? 1.4023 1.3156 0.8295 -0.3189 0.3962  0.0760  179 LEU D CG  
2960 C CD1 . LEU B 180 ? 1.4500 1.3954 0.8834 -0.3084 0.4105  0.0750  179 LEU D CD1 
2961 C CD2 . LEU B 180 ? 1.4181 1.3500 0.8627 -0.3160 0.3973  0.0746  179 LEU D CD2 
2962 N N   . THR B 181 ? 1.2803 1.1934 0.7131 -0.2547 0.4141  0.0532  180 THR D N   
2963 C CA  . THR B 181 ? 1.3213 1.2443 0.7525 -0.2385 0.4236  0.0482  180 THR D CA  
2964 C C   . THR B 181 ? 1.3859 1.3540 0.8281 -0.2402 0.4356  0.0530  180 THR D C   
2965 O O   . THR B 181 ? 1.4089 1.4082 0.8671 -0.2412 0.4406  0.0555  180 THR D O   
2966 C CB  . THR B 181 ? 1.3252 1.2434 0.7623 -0.2158 0.4267  0.0391  180 THR D CB  
2967 O OG1 . THR B 181 ? 1.3600 1.3124 0.8154 -0.2085 0.4343  0.0398  180 THR D OG1 
2968 C CG2 . THR B 181 ? 1.3039 1.1802 0.7327 -0.2148 0.4149  0.0349  180 THR D CG2 
2969 N N   . LEU B 182 ? 1.4099 1.3819 0.8430 -0.2404 0.4402  0.0540  181 LEU D N   
2970 C CA  . LEU B 182 ? 1.4227 1.4347 0.8630 -0.2430 0.4513  0.0591  181 LEU D CA  
2971 C C   . LEU B 182 ? 1.4516 1.4668 0.8845 -0.2275 0.4588  0.0544  181 LEU D C   
2972 O O   . LEU B 182 ? 1.4290 1.4115 0.8473 -0.2232 0.4534  0.0493  181 LEU D O   
2973 C CB  . LEU B 182 ? 1.4352 1.4468 0.8694 -0.2672 0.4474  0.0684  181 LEU D CB  
2974 C CG  . LEU B 182 ? 1.4796 1.5254 0.9292 -0.2819 0.4508  0.0756  181 LEU D CG  
2975 C CD1 . LEU B 182 ? 1.5108 1.5521 0.9513 -0.3054 0.4471  0.0842  181 LEU D CD1 
2976 C CD2 . LEU B 182 ? 1.5135 1.6068 0.9794 -0.2684 0.4653  0.0746  181 LEU D CD2 
2977 N N   . SER B 183 ? 1.5061 1.5613 0.9487 -0.2191 0.4711  0.0558  182 SER D N   
2978 C CA  . SER B 183 ? 1.5677 1.6283 1.0023 -0.2056 0.4783  0.0521  182 SER D CA  
2979 C C   . SER B 183 ? 1.6026 1.6516 1.0222 -0.2204 0.4761  0.0573  182 SER D C   
2980 O O   . SER B 183 ? 1.5999 1.6591 1.0209 -0.2391 0.4753  0.0660  182 SER D O   
2981 C CB  . SER B 183 ? 1.5819 1.6894 1.0300 -0.1919 0.4920  0.0527  182 SER D CB  
2982 O OG  . SER B 183 ? 1.6246 1.7595 1.0752 -0.2051 0.4980  0.0615  182 SER D OG  
2983 N N   . LYS B 184 ? 1.6975 1.7254 1.1024 -0.2119 0.4752  0.0517  183 LYS D N   
2984 C CA  . LYS B 184 ? 1.7086 1.7188 1.0967 -0.2246 0.4714  0.0555  183 LYS D CA  
2985 C C   . LYS B 184 ? 1.7669 1.8093 1.1581 -0.2359 0.4792  0.0653  183 LYS D C   
2986 O O   . LYS B 184 ? 1.7755 1.8057 1.1569 -0.2538 0.4744  0.0720  183 LYS D O   
2987 C CB  . LYS B 184 ? 1.6779 1.6700 1.0520 -0.2112 0.4721  0.0472  183 LYS D CB  
2988 C CG  . LYS B 184 ? 1.6994 1.7217 1.0742 -0.1975 0.4845  0.0457  183 LYS D CG  
2989 C CD  . LYS B 184 ? 1.6705 1.7286 1.0628 -0.1830 0.4940  0.0444  183 LYS D CD  
2990 C CE  . LYS B 184 ? 1.6852 1.7649 1.0758 -0.1645 0.5042  0.0397  183 LYS D CE  
2991 N NZ  . LYS B 184 ? 1.6893 1.7995 1.0964 -0.1492 0.5116  0.0376  183 LYS D NZ  
2992 N N   . ALA B 185 ? 1.6865 1.7697 1.0911 -0.2257 0.4912  0.0663  184 ALA D N   
2993 C CA  . ALA B 185 ? 1.6440 1.7601 1.0534 -0.2364 0.4994  0.0754  184 ALA D CA  
2994 C C   . ALA B 185 ? 1.5723 1.6891 0.9884 -0.2595 0.4938  0.0833  184 ALA D C   
2995 O O   . ALA B 185 ? 1.5855 1.6990 0.9941 -0.2777 0.4920  0.0908  184 ALA D O   
2996 C CB  . ALA B 185 ? 1.6357 1.7957 1.0596 -0.2194 0.5130  0.0743  184 ALA D CB  
2997 N N   . ASP B 186 ? 1.5917 1.7116 1.0212 -0.2594 0.4903  0.0815  185 ASP D N   
2998 C CA  . ASP B 186 ? 1.5912 1.7136 1.0280 -0.2815 0.4847  0.0883  185 ASP D CA  
2999 C C   . ASP B 186 ? 1.6178 1.6950 1.0382 -0.2974 0.4705  0.0901  185 ASP D C   
3000 O O   . ASP B 186 ? 1.6258 1.7002 1.0458 -0.3189 0.4654  0.0972  185 ASP D O   
3001 C CB  . ASP B 186 ? 1.6062 1.7459 1.0617 -0.2761 0.4851  0.0854  185 ASP D CB  
3002 C CG  . ASP B 186 ? 1.6208 1.8022 1.0910 -0.2559 0.4986  0.0822  185 ASP D CG  
3003 O OD1 . ASP B 186 ? 1.6437 1.8210 1.1080 -0.2349 0.5030  0.0760  185 ASP D OD1 
3004 O OD2 . ASP B 186 ? 1.6383 1.8567 1.1256 -0.2611 0.5046  0.0855  185 ASP D OD2 
3005 N N   . TYR B 187 ? 1.6193 1.6606 1.0258 -0.2872 0.4638  0.0836  186 TYR D N   
3006 C CA  . TYR B 187 ? 1.5751 1.5746 0.9631 -0.3004 0.4514  0.0854  186 TYR D CA  
3007 C C   . TYR B 187 ? 1.5886 1.5893 0.9637 -0.3116 0.4540  0.0921  186 TYR D C   
3008 O O   . TYR B 187 ? 1.5737 1.5625 0.9417 -0.3313 0.4478  0.0993  186 TYR D O   
3009 C CB  . TYR B 187 ? 1.5287 1.4928 0.9052 -0.2862 0.4447  0.0761  186 TYR D CB  
3010 C CG  . TYR B 187 ? 1.4732 1.3949 0.8298 -0.2972 0.4320  0.0771  186 TYR D CG  
3011 C CD1 . TYR B 187 ? 1.4598 1.3635 0.8141 -0.3139 0.4216  0.0821  186 TYR D CD1 
3012 C CD2 . TYR B 187 ? 1.4638 1.3636 0.8033 -0.2902 0.4303  0.0727  186 TYR D CD2 
3013 C CE1 . TYR B 187 ? 1.4800 1.3446 0.8148 -0.3222 0.4098  0.0829  186 TYR D CE1 
3014 C CE2 . TYR B 187 ? 1.4396 1.3019 0.7603 -0.2988 0.4188  0.0733  186 TYR D CE2 
3015 C CZ  . TYR B 187 ? 1.4642 1.3089 0.7823 -0.3142 0.4086  0.0785  186 TYR D CZ  
3016 O OH  . TYR B 187 ? 1.4459 1.2533 0.7442 -0.3212 0.3970  0.0790  186 TYR D OH  
3017 N N   . GLU B 188 ? 1.5503 1.5657 0.9217 -0.2990 0.4633  0.0899  187 GLU D N   
3018 C CA  . GLU B 188 ? 1.5483 1.5653 0.9066 -0.3077 0.4666  0.0960  187 GLU D CA  
3019 C C   . GLU B 188 ? 1.5152 1.5628 0.8830 -0.3245 0.4727  0.1060  187 GLU D C   
3020 O O   . GLU B 188 ? 1.5475 1.5890 0.9034 -0.3382 0.4722  0.1129  187 GLU D O   
3021 C CB  . GLU B 188 ? 1.5529 1.5822 0.9065 -0.2892 0.4759  0.0911  187 GLU D CB  
3022 C CG  . GLU B 188 ? 1.5755 1.5706 0.9154 -0.2764 0.4692  0.0815  187 GLU D CG  
3023 C CD  . GLU B 188 ? 1.6846 1.6930 1.0206 -0.2579 0.4783  0.0756  187 GLU D CD  
3024 O OE1 . GLU B 188 ? 1.6477 1.6933 0.9933 -0.2520 0.4902  0.0784  187 GLU D OE1 
3025 O OE2 . GLU B 188 ? 1.7638 1.7455 1.0872 -0.2490 0.4735  0.0677  187 GLU D OE2 
3026 N N   . LYS B 189 ? 1.5272 1.6077 0.9161 -0.3240 0.4784  0.1066  188 LYS D N   
3027 C CA  . LYS B 189 ? 1.5172 1.6301 0.9168 -0.3405 0.4847  0.1151  188 LYS D CA  
3028 C C   . LYS B 189 ? 1.5286 1.6183 0.9211 -0.3658 0.4740  0.1219  188 LYS D C   
3029 O O   . LYS B 189 ? 1.5193 1.6107 0.9037 -0.3814 0.4755  0.1295  188 LYS D O   
3030 C CB  . LYS B 189 ? 1.4290 1.5821 0.8531 -0.3339 0.4924  0.1131  188 LYS D CB  
3031 C CG  . LYS B 189 ? 1.4172 1.6025 0.8491 -0.3105 0.5059  0.1085  188 LYS D CG  
3032 C CD  . LYS B 189 ? 1.4072 1.5888 0.8232 -0.3033 0.5116  0.1094  188 LYS D CD  
3033 C CE  . LYS B 189 ? 1.4303 1.6420 0.8489 -0.3166 0.5208  0.1180  188 LYS D CE  
3034 N NZ  . LYS B 189 ? 1.4507 1.6512 0.8501 -0.3161 0.5236  0.1210  188 LYS D NZ  
3035 N N   . HIS B 190 ? 1.4966 1.5630 0.8907 -0.3698 0.4629  0.1192  189 HIS D N   
3036 C CA  . HIS B 190 ? 1.4831 1.5249 0.8697 -0.3925 0.4516  0.1250  189 HIS D CA  
3037 C C   . HIS B 190 ? 1.4977 1.4898 0.8593 -0.3928 0.4403  0.1240  189 HIS D C   
3038 O O   . HIS B 190 ? 1.5053 1.4804 0.8586 -0.3754 0.4393  0.1172  189 HIS D O   
3039 C CB  . HIS B 190 ? 1.5039 1.5485 0.9055 -0.3972 0.4455  0.1230  189 HIS D CB  
3040 C CG  . HIS B 190 ? 1.4842 1.5782 0.9102 -0.3998 0.4554  0.1242  189 HIS D CG  
3041 N ND1 . HIS B 190 ? 1.4387 1.5531 0.8721 -0.4222 0.4565  0.1313  189 HIS D ND1 
3042 C CD2 . HIS B 190 ? 1.4420 1.5691 0.8865 -0.3828 0.4641  0.1187  189 HIS D CD2 
3043 C CE1 . HIS B 190 ? 1.4111 1.5714 0.8675 -0.4190 0.4657  0.1299  189 HIS D CE1 
3044 N NE2 . HIS B 190 ? 1.4381 1.6066 0.9012 -0.3946 0.4705  0.1224  189 HIS D NE2 
3045 N N   . LYS B 191 ? 1.5009 1.4696 0.8503 -0.4128 0.4316  0.1306  190 LYS D N   
3046 C CA  . LYS B 191 ? 1.5593 1.4858 0.8829 -0.4148 0.4227  0.1315  190 LYS D CA  
3047 C C   . LYS B 191 ? 1.5729 1.4580 0.8865 -0.4177 0.4072  0.1288  190 LYS D C   
3048 O O   . LYS B 191 ? 1.5730 1.4284 0.8730 -0.4056 0.4008  0.1230  190 LYS D O   
3049 C CB  . LYS B 191 ? 1.5447 1.4707 0.8565 -0.4334 0.4245  0.1413  190 LYS D CB  
3050 C CG  . LYS B 191 ? 1.5103 1.3966 0.7943 -0.4332 0.4174  0.1425  190 LYS D CG  
3051 C CD  . LYS B 191 ? 1.5174 1.4159 0.7946 -0.4197 0.4274  0.1411  190 LYS D CD  
3052 C CE  . LYS B 191 ? 1.5247 1.4691 0.8165 -0.4233 0.4423  0.1461  190 LYS D CE  
3053 N NZ  . LYS B 191 ? 1.5279 1.4860 0.8144 -0.4077 0.4522  0.1438  190 LYS D NZ  
3054 N N   . VAL B 192 ? 1.5567 1.4394 0.8766 -0.4337 0.4007  0.1326  191 VAL D N   
3055 C CA  . VAL B 192 ? 1.5902 1.4333 0.8994 -0.4383 0.3853  0.1312  191 VAL D CA  
3056 C C   . VAL B 192 ? 1.5774 1.4317 0.9060 -0.4325 0.3833  0.1260  191 VAL D C   
3057 O O   . VAL B 192 ? 1.5822 1.4728 0.9315 -0.4378 0.3905  0.1276  191 VAL D O   
3058 C CB  . VAL B 192 ? 1.5828 1.4079 0.8798 -0.4616 0.3779  0.1398  191 VAL D CB  
3059 C CG1 . VAL B 192 ? 1.5555 1.4147 0.8722 -0.4778 0.3831  0.1446  191 VAL D CG1 
3060 C CG2 . VAL B 192 ? 1.5924 1.3725 0.8741 -0.4641 0.3614  0.1381  191 VAL D CG2 
3061 N N   . TYR B 193 ? 1.5857 1.4101 0.9075 -0.4209 0.3739  0.1195  192 TYR D N   
3062 C CA  . TYR B 193 ? 1.5512 1.3808 0.8885 -0.4135 0.3711  0.1142  192 TYR D CA  
3063 C C   . TYR B 193 ? 1.5173 1.3060 0.8418 -0.4198 0.3548  0.1140  192 TYR D C   
3064 O O   . TYR B 193 ? 1.5070 1.2598 0.8103 -0.4170 0.3463  0.1129  192 TYR D O   
3065 C CB  . TYR B 193 ? 1.5476 1.3827 0.8909 -0.3894 0.3769  0.1051  192 TYR D CB  
3066 C CG  . TYR B 193 ? 1.5357 1.4113 0.8920 -0.3796 0.3929  0.1041  192 TYR D CG  
3067 C CD1 . TYR B 193 ? 1.5047 1.3899 0.8528 -0.3838 0.3998  0.1085  192 TYR D CD1 
3068 C CD2 . TYR B 193 ? 1.4585 1.3613 0.8339 -0.3648 0.4010  0.0986  192 TYR D CD2 
3069 C CE1 . TYR B 193 ? 1.5061 1.4278 0.8651 -0.3741 0.4139  0.1077  192 TYR D CE1 
3070 C CE2 . TYR B 193 ? 1.4360 1.3746 0.8219 -0.3542 0.4151  0.0975  192 TYR D CE2 
3071 C CZ  . TYR B 193 ? 1.5011 1.4492 0.8788 -0.3590 0.4214  0.1020  192 TYR D CZ  
3072 O OH  . TYR B 193 ? 1.5253 1.5092 0.9127 -0.3479 0.4353  0.1011  192 TYR D OH  
3073 N N   . ALA B 194 ? 1.4937 1.2888 0.8307 -0.4277 0.3503  0.1149  193 ALA D N   
3074 C CA  . ALA B 194 ? 1.4729 1.2312 0.7983 -0.4348 0.3345  0.1154  193 ALA D CA  
3075 C C   . ALA B 194 ? 1.4902 1.2536 0.8308 -0.4277 0.3313  0.1107  193 ALA D C   
3076 O O   . ALA B 194 ? 1.4901 1.2903 0.8525 -0.4232 0.3413  0.1090  193 ALA D O   
3077 C CB  . ALA B 194 ? 1.4862 1.2387 0.8053 -0.4587 0.3289  0.1237  193 ALA D CB  
3078 N N   . CYS B 195 ? 1.4899 1.2160 0.8182 -0.4264 0.3170  0.1088  194 CYS D N   
3079 C CA  . CYS B 195 ? 1.4518 1.1753 0.7906 -0.4196 0.3117  0.1046  194 CYS D CA  
3080 C C   . CYS B 195 ? 1.4844 1.1854 0.8157 -0.4361 0.2978  0.1091  194 CYS D C   
3081 O O   . CYS B 195 ? 1.4885 1.1530 0.7978 -0.4408 0.2865  0.1110  194 CYS D O   
3082 C CB  . CYS B 195 ? 1.4359 1.1344 0.7664 -0.3989 0.3077  0.0968  194 CYS D CB  
3083 S SG  . CYS B 195 ? 1.5612 1.2264 0.8868 -0.3942 0.2917  0.0934  194 CYS D SG  
3084 N N   . GLU B 196 ? 1.5854 1.3088 0.9343 -0.4447 0.2985  0.1106  195 GLU D N   
3085 C CA  . GLU B 196 ? 1.5500 1.2572 0.8947 -0.4618 0.2860  0.1147  195 GLU D CA  
3086 C C   . GLU B 196 ? 1.5271 1.2255 0.8787 -0.4533 0.2785  0.1105  195 GLU D C   
3087 O O   . GLU B 196 ? 1.4974 1.2259 0.8691 -0.4446 0.2872  0.1072  195 GLU D O   
3088 C CB  . GLU B 196 ? 1.5540 1.2966 0.9138 -0.4821 0.2928  0.1201  195 GLU D CB  
3089 C CG  . GLU B 196 ? 1.5752 1.3234 0.9458 -0.4946 0.2855  0.1212  195 GLU D CG  
3090 C CD  . GLU B 196 ? 1.6508 1.4156 1.0255 -0.5200 0.2861  0.1275  195 GLU D CD  
3091 O OE1 . GLU B 196 ? 1.6638 1.4565 1.0445 -0.5257 0.2980  0.1302  195 GLU D OE1 
3092 O OE2 . GLU B 196 ? 1.6241 1.3753 0.9966 -0.5342 0.2750  0.1294  195 GLU D OE2 
3093 N N   . VAL B 197 ? 1.5068 1.1644 0.8411 -0.4550 0.2623  0.1107  196 VAL D N   
3094 C CA  . VAL B 197 ? 1.4952 1.1377 0.8318 -0.4442 0.2536  0.1066  196 VAL D CA  
3095 C C   . VAL B 197 ? 1.5408 1.1703 0.8753 -0.4605 0.2408  0.1103  196 VAL D C   
3096 O O   . VAL B 197 ? 1.5246 1.1249 0.8403 -0.4715 0.2297  0.1139  196 VAL D O   
3097 C CB  . VAL B 197 ? 1.4391 1.0437 0.7568 -0.4269 0.2452  0.1018  196 VAL D CB  
3098 C CG1 . VAL B 197 ? 1.4311 1.0187 0.7502 -0.4167 0.2353  0.0981  196 VAL D CG1 
3099 C CG2 . VAL B 197 ? 1.4302 1.0497 0.7519 -0.4111 0.2584  0.0972  196 VAL D CG2 
3100 N N   . THR B 198 ? 1.6132 1.2645 0.9665 -0.4616 0.2423  0.1094  197 THR D N   
3101 C CA  . THR B 198 ? 1.5736 1.2152 0.9270 -0.4766 0.2302  0.1122  197 THR D CA  
3102 C C   . THR B 198 ? 1.5998 1.2205 0.9518 -0.4631 0.2200  0.1084  197 THR D C   
3103 O O   . THR B 198 ? 1.6529 1.2936 1.0215 -0.4653 0.2210  0.1079  197 THR D O   
3104 C CB  . THR B 198 ? 1.5684 1.2558 0.9455 -0.4927 0.2397  0.1146  197 THR D CB  
3105 O OG1 . THR B 198 ? 1.6001 1.3123 0.9965 -0.4814 0.2454  0.1106  197 THR D OG1 
3106 C CG2 . THR B 198 ? 1.6181 1.3386 1.0032 -0.4971 0.2554  0.1163  197 THR D CG2 
3107 N N   . HIS B 199 ? 1.5237 1.1065 0.8567 -0.4486 0.2106  0.1056  198 HIS D N   
3108 C CA  . HIS B 199 ? 1.4642 1.0213 0.7922 -0.4380 0.1976  0.1028  198 HIS D CA  
3109 C C   . HIS B 199 ? 1.4986 1.0380 0.8202 -0.4545 0.1825  0.1066  198 HIS D C   
3110 O O   . HIS B 199 ? 1.5428 1.0760 0.8555 -0.4715 0.1792  0.1108  198 HIS D O   
3111 C CB  . HIS B 199 ? 1.4234 0.9447 0.7313 -0.4205 0.1897  0.0988  198 HIS D CB  
3112 C CG  . HIS B 199 ? 1.3969 0.8965 0.7019 -0.4059 0.1785  0.0950  198 HIS D CG  
3113 N ND1 . HIS B 199 ? 1.3807 0.8405 0.6651 -0.4014 0.1609  0.0940  198 HIS D ND1 
3114 C CD2 . HIS B 199 ? 1.3534 0.8661 0.6730 -0.3939 0.1828  0.0920  198 HIS D CD2 
3115 C CE1 . HIS B 199 ? 1.3670 0.8172 0.6545 -0.3874 0.1543  0.0906  198 HIS D CE1 
3116 N NE2 . HIS B 199 ? 1.3524 0.8331 0.6606 -0.3829 0.1675  0.0896  198 HIS D NE2 
3117 N N   . GLN B 200 ? 1.5226 1.0537 0.8487 -0.4493 0.1735  0.1051  199 GLN D N   
3118 C CA  . GLN B 200 ? 1.5420 1.0545 0.8616 -0.4639 0.1581  0.1080  199 GLN D CA  
3119 C C   . GLN B 200 ? 1.5578 1.0233 0.8493 -0.4604 0.1415  0.1078  199 GLN D C   
3120 O O   . GLN B 200 ? 1.6017 1.0491 0.8830 -0.4741 0.1295  0.1105  199 GLN D O   
3121 C CB  . GLN B 200 ? 1.6662 1.1844 0.9990 -0.4593 0.1532  0.1065  199 GLN D CB  
3122 C CG  . GLN B 200 ? 1.6357 1.1188 0.9557 -0.4393 0.1396  0.1029  199 GLN D CG  
3123 C CD  . GLN B 200 ? 1.7436 1.1945 1.0504 -0.4463 0.1190  0.1041  199 GLN D CD  
3124 O OE1 . GLN B 200 ? 1.7686 1.2285 1.0820 -0.4656 0.1155  0.1071  199 GLN D OE1 
3125 N NE2 . GLN B 200 ? 1.7632 1.1778 1.0515 -0.4306 0.1051  0.1012  199 GLN D NE2 
3126 N N   . GLY B 201 ? 1.4983 0.9451 0.7768 -0.4422 0.1407  0.1042  200 GLY D N   
3127 C CA  . GLY B 201 ? 1.4893 0.8961 0.7409 -0.4379 0.1268  0.1035  200 GLY D CA  
3128 C C   . GLY B 201 ? 1.5269 0.9318 0.7660 -0.4495 0.1323  0.1068  200 GLY D C   
3129 O O   . GLY B 201 ? 1.5005 0.8758 0.7163 -0.4444 0.1244  0.1060  200 GLY D O   
3130 N N   . LEU B 202 ? 1.4886 0.9267 0.7432 -0.4645 0.1462  0.1105  201 LEU D N   
3131 C CA  . LEU B 202 ? 1.4118 0.8522 0.6570 -0.4778 0.1525  0.1146  201 LEU D CA  
3132 C C   . LEU B 202 ? 1.4950 0.9458 0.7461 -0.5015 0.1510  0.1196  201 LEU D C   
3133 O O   . LEU B 202 ? 1.4612 0.9482 0.7364 -0.5102 0.1600  0.1204  201 LEU D O   
3134 C CB  . LEU B 202 ? 1.4430 0.9165 0.7017 -0.4740 0.1715  0.1141  201 LEU D CB  
3135 C CG  . LEU B 202 ? 1.3806 0.8500 0.6363 -0.4518 0.1761  0.1086  201 LEU D CG  
3136 C CD1 . LEU B 202 ? 1.4128 0.9183 0.6835 -0.4513 0.1951  0.1087  201 LEU D CD1 
3137 C CD2 . LEU B 202 ? 1.3783 0.8090 0.6060 -0.4447 0.1657  0.1074  201 LEU D CD2 
3138 N N   . SER B 203 ? 1.5190 0.9384 0.7477 -0.5117 0.1395  0.1224  202 SER D N   
3139 C CA  . SER B 203 ? 1.5286 0.9549 0.7595 -0.5360 0.1385  0.1272  202 SER D CA  
3140 C C   . SER B 203 ? 1.5457 1.0138 0.7945 -0.5495 0.1567  0.1305  202 SER D C   
3141 O O   . SER B 203 ? 1.5665 1.0707 0.8396 -0.5602 0.1639  0.1309  202 SER D O   
3142 C CB  . SER B 203 ? 1.5217 0.9059 0.7216 -0.5427 0.1262  0.1299  202 SER D CB  
3143 O OG  . SER B 203 ? 1.5094 0.8596 0.6878 -0.5228 0.1169  0.1264  202 SER D OG  
3144 N N   . SER B 204 ? 1.5435 1.0086 0.7804 -0.5489 0.1644  0.1326  203 SER D N   
3145 C CA  . SER B 204 ? 1.5411 1.0479 0.7957 -0.5577 0.1823  0.1350  203 SER D CA  
3146 C C   . SER B 204 ? 1.5425 1.0695 0.8088 -0.5375 0.1936  0.1310  203 SER D C   
3147 O O   . SER B 204 ? 1.5542 1.0560 0.8079 -0.5187 0.1877  0.1271  203 SER D O   
3148 C CB  . SER B 204 ? 1.5762 1.0722 0.8128 -0.5697 0.1858  0.1402  203 SER D CB  
3149 O OG  . SER B 204 ? 1.6276 1.0826 0.8362 -0.5572 0.1776  0.1393  203 SER D OG  
3150 N N   . PRO B 205 ? 1.5167 1.0893 0.8065 -0.5404 0.2098  0.1313  204 PRO D N   
3151 C CA  . PRO B 205 ? 1.5082 1.0983 0.8062 -0.5211 0.2215  0.1274  204 PRO D CA  
3152 C C   . PRO B 205 ? 1.4419 1.0115 0.7190 -0.5153 0.2233  0.1284  204 PRO D C   
3153 O O   . PRO B 205 ? 1.4641 1.0340 0.7326 -0.5294 0.2266  0.1334  204 PRO D O   
3154 C CB  . PRO B 205 ? 1.4982 1.1425 0.8241 -0.5285 0.2381  0.1283  204 PRO D CB  
3155 C CG  . PRO B 205 ? 1.4541 1.1101 0.7915 -0.5465 0.2328  0.1302  204 PRO D CG  
3156 C CD  . PRO B 205 ? 1.4742 1.0870 0.7865 -0.5593 0.2177  0.1339  204 PRO D CD  
3157 N N   . VAL B 206 ? 1.4164 0.9667 0.6844 -0.4949 0.2205  0.1235  205 VAL D N   
3158 C CA  . VAL B 206 ? 1.4372 0.9707 0.6868 -0.4867 0.2226  0.1230  205 VAL D CA  
3159 C C   . VAL B 206 ? 1.4739 1.0447 0.7400 -0.4796 0.2403  0.1216  205 VAL D C   
3160 O O   . VAL B 206 ? 1.4728 1.0686 0.7588 -0.4691 0.2475  0.1174  205 VAL D O   
3161 C CB  . VAL B 206 ? 1.4315 0.9287 0.6641 -0.4682 0.2109  0.1175  205 VAL D CB  
3162 C CG1 . VAL B 206 ? 1.4160 0.9099 0.6392 -0.4548 0.2176  0.1145  205 VAL D CG1 
3163 C CG2 . VAL B 206 ? 1.4675 0.9240 0.6765 -0.4751 0.1939  0.1198  205 VAL D CG2 
3164 N N   . THR B 207 ? 1.4516 1.0265 0.7090 -0.4849 0.2476  0.1251  206 THR D N   
3165 C CA  . THR B 207 ? 1.4426 1.0513 0.7132 -0.4776 0.2640  0.1238  206 THR D CA  
3166 C C   . THR B 207 ? 1.4261 1.0138 0.6777 -0.4647 0.2643  0.1213  206 THR D C   
3167 O O   . THR B 207 ? 1.4528 1.0093 0.6809 -0.4697 0.2561  0.1242  206 THR D O   
3168 C CB  . THR B 207 ? 1.4382 1.0790 0.7190 -0.4956 0.2748  0.1302  206 THR D CB  
3169 O OG1 . THR B 207 ? 1.4459 1.0921 0.7347 -0.5132 0.2694  0.1336  206 THR D OG1 
3170 C CG2 . THR B 207 ? 1.4412 1.1280 0.7457 -0.4872 0.2915  0.1278  206 THR D CG2 
3171 N N   . LYS B 208 ? 1.4172 1.0216 0.6784 -0.4478 0.2736  0.1157  207 LYS D N   
3172 C CA  . LYS B 208 ? 1.4453 1.0362 0.6916 -0.4355 0.2758  0.1125  207 LYS D CA  
3173 C C   . LYS B 208 ? 1.4899 1.1178 0.7496 -0.4320 0.2928  0.1126  207 LYS D C   
3174 O O   . LYS B 208 ? 1.4847 1.1451 0.7668 -0.4269 0.3022  0.1103  207 LYS D O   
3175 C CB  . LYS B 208 ? 1.3848 0.9559 0.6273 -0.4163 0.2694  0.1041  207 LYS D CB  
3176 C CG  . LYS B 208 ? 1.4342 0.9633 0.6569 -0.4163 0.2518  0.1033  207 LYS D CG  
3177 C CD  . LYS B 208 ? 1.4370 0.9431 0.6382 -0.4309 0.2444  0.1101  207 LYS D CD  
3178 C CE  . LYS B 208 ? 1.4512 0.9144 0.6296 -0.4257 0.2276  0.1077  207 LYS D CE  
3179 N NZ  . LYS B 208 ? 1.5140 0.9645 0.6836 -0.4072 0.2265  0.1002  207 LYS D NZ  
3180 N N   . SER B 209 ? 1.5268 1.1500 0.7720 -0.4337 0.2968  0.1153  208 SER D N   
3181 C CA  . SER B 209 ? 1.5046 1.1625 0.7600 -0.4333 0.3125  0.1171  208 SER D CA  
3182 C C   . SER B 209 ? 1.5754 1.2220 0.8151 -0.4216 0.3155  0.1140  208 SER D C   
3183 O O   . SER B 209 ? 1.5596 1.1714 0.7792 -0.4162 0.3054  0.1114  208 SER D O   
3184 C CB  . SER B 209 ? 1.5497 1.2225 0.8061 -0.4541 0.3165  0.1263  208 SER D CB  
3185 O OG  . SER B 209 ? 1.5777 1.2157 0.8143 -0.4670 0.3037  0.1308  208 SER D OG  
3186 N N   . PHE B 210 ? 1.6779 1.3558 0.9270 -0.4177 0.3298  0.1144  209 PHE D N   
3187 C CA  . PHE B 210 ? 1.6876 1.3616 0.9238 -0.4080 0.3349  0.1122  209 PHE D CA  
3188 C C   . PHE B 210 ? 1.6936 1.4033 0.9382 -0.4134 0.3494  0.1175  209 PHE D C   
3189 O O   . PHE B 210 ? 1.6953 1.4347 0.9576 -0.4227 0.3559  0.1217  209 PHE D O   
3190 C CB  . PHE B 210 ? 1.6770 1.3486 0.9171 -0.3870 0.3361  0.1017  209 PHE D CB  
3191 C CG  . PHE B 210 ? 1.6466 1.3560 0.9110 -0.3773 0.3488  0.0980  209 PHE D CG  
3192 C CD1 . PHE B 210 ? 1.6523 1.3886 0.9214 -0.3713 0.3620  0.0978  209 PHE D CD1 
3193 C CD2 . PHE B 210 ? 1.6135 1.3307 0.8948 -0.3728 0.3474  0.0944  209 PHE D CD2 
3194 C CE1 . PHE B 210 ? 1.6259 1.3962 0.9158 -0.3610 0.3733  0.0942  209 PHE D CE1 
3195 C CE2 . PHE B 210 ? 1.5940 1.3451 0.8961 -0.3625 0.3592  0.0909  209 PHE D CE2 
3196 C CZ  . PHE B 210 ? 1.5983 1.3758 0.9046 -0.3563 0.3720  0.0907  209 PHE D CZ  
3197 N N   . ASN B 211 ? 1.6496 1.3578 0.8816 -0.4072 0.3546  0.1171  210 ASN D N   
3198 C CA  . ASN B 211 ? 1.6118 1.3527 0.8498 -0.4108 0.3684  0.1221  210 ASN D CA  
3199 C C   . ASN B 211 ? 1.6135 1.3650 0.8507 -0.3925 0.3767  0.1155  210 ASN D C   
3200 O O   . ASN B 211 ? 1.6080 1.3512 0.8477 -0.3771 0.3744  0.1064  210 ASN D O   
3201 C CB  . ASN B 211 ? 1.6986 1.4264 0.9184 -0.4274 0.3664  0.1316  210 ASN D CB  
3202 C CG  . ASN B 211 ? 1.7487 1.4384 0.9408 -0.4225 0.3581  0.1301  210 ASN D CG  
3203 O OD1 . ASN B 211 ? 1.7951 1.4635 0.9813 -0.4094 0.3508  0.1220  210 ASN D OD1 
3204 N ND2 . ASN B 211 ? 1.5715 1.2534 0.7463 -0.4326 0.3596  0.1377  210 ASN D ND2 
3205 N N   . ARG B 212 ? 1.6449 1.4140 0.8775 -0.3941 0.3865  0.1198  211 ARG D N   
3206 C CA  . ARG B 212 ? 1.6216 1.4066 0.8551 -0.3775 0.3961  0.1141  211 ARG D CA  
3207 C C   . ARG B 212 ? 1.6196 1.4334 0.8766 -0.3644 0.4037  0.1076  211 ARG D C   
3208 O O   . ARG B 212 ? 1.6162 1.4305 0.8737 -0.3473 0.4067  0.0991  211 ARG D O   
3209 C CB  . ARG B 212 ? 1.6391 1.3910 0.8525 -0.3663 0.3886  0.1072  211 ARG D CB  
3210 C CG  . ARG B 212 ? 1.6251 1.3634 0.8154 -0.3701 0.3887  0.1117  211 ARG D CG  
3211 C CD  . ARG B 212 ? 1.6622 1.3606 0.8319 -0.3639 0.3764  0.1059  211 ARG D CD  
3212 N NE  . ARG B 212 ? 1.6743 1.3443 0.8370 -0.3745 0.3635  0.1089  211 ARG D NE  
3213 C CZ  . ARG B 212 ? 1.6786 1.3123 0.8227 -0.3717 0.3512  0.1055  211 ARG D CZ  
3214 N NH1 . ARG B 212 ? 1.6817 1.3028 0.8130 -0.3591 0.3497  0.0985  211 ARG D NH1 
3215 N NH2 . ARG B 212 ? 1.6627 1.2729 0.8009 -0.3816 0.3399  0.1090  211 ARG D NH2 
3216 N N   . GLY B 213 ? 1.5849 1.4220 0.8609 -0.3723 0.4068  0.1113  212 GLY D N   
3217 C CA  . GLY B 213 ? 1.4947 1.3586 0.7929 -0.3605 0.4134  0.1057  212 GLY D CA  
3218 C C   . GLY B 213 ? 1.5032 1.3918 0.8074 -0.3425 0.4254  0.1003  212 GLY D C   
3219 O O   . GLY B 213 ? 1.5199 1.4467 0.8400 -0.3401 0.4368  0.1023  212 GLY D O   
3220 N N   . SER C 2   ? 1.8857 0.8851 0.7127 -0.2636 0.3193  -0.1700 2   SER A N   
3221 C CA  . SER C 2   ? 1.9565 0.9224 0.7625 -0.2746 0.3221  -0.1782 2   SER A CA  
3222 C C   . SER C 2   ? 1.9792 0.8819 0.7437 -0.3035 0.3402  -0.1807 2   SER A C   
3223 O O   . SER C 2   ? 1.9338 0.7867 0.6704 -0.3074 0.3444  -0.1811 2   SER A O   
3224 C CB  . SER C 2   ? 1.8938 0.9174 0.7238 -0.2880 0.3177  -0.1970 2   SER A CB  
3225 O OG  . SER C 2   ? 1.9085 0.9522 0.7366 -0.3260 0.3298  -0.2135 2   SER A OG  
3226 N N   . ILE C 3   ? 1.9724 0.8752 0.7314 -0.3222 0.3519  -0.1813 3   ILE A N   
3227 C CA  . ILE C 3   ? 2.0464 0.8941 0.7670 -0.3547 0.3723  -0.1862 3   ILE A CA  
3228 C C   . ILE C 3   ? 2.0557 0.8217 0.7349 -0.3383 0.3771  -0.1687 3   ILE A C   
3229 O O   . ILE C 3   ? 2.0779 0.7860 0.7194 -0.3573 0.3917  -0.1708 3   ILE A O   
3230 C CB  . ILE C 3   ? 2.0203 0.8917 0.7466 -0.3779 0.3847  -0.1909 3   ILE A CB  
3231 C CG1 . ILE C 3   ? 1.9737 0.8972 0.7175 -0.4153 0.3922  -0.2144 3   ILE A CG1 
3232 C CG2 . ILE C 3   ? 2.0565 0.8546 0.7392 -0.3899 0.4031  -0.1823 3   ILE A CG2 
3233 C CD1 . ILE C 3   ? 1.9148 0.9162 0.7006 -0.4041 0.3748  -0.2242 3   ILE A CD1 
3234 N N   . VAL C 4   ? 2.0276 0.7886 0.7122 -0.3025 0.3651  -0.1514 4   VAL A N   
3235 C CA  . VAL C 4   ? 2.0486 0.7405 0.6965 -0.2810 0.3666  -0.1341 4   VAL A CA  
3236 C C   . VAL C 4   ? 2.0149 0.7183 0.6788 -0.2450 0.3481  -0.1256 4   VAL A C   
3237 O O   . VAL C 4   ? 1.9868 0.7484 0.6907 -0.2282 0.3334  -0.1262 4   VAL A O   
3238 C CB  . VAL C 4   ? 2.0393 0.7114 0.6753 -0.2719 0.3704  -0.1215 4   VAL A CB  
3239 C CG1 . VAL C 4   ? 2.0607 0.6703 0.6621 -0.2432 0.3681  -0.1030 4   VAL A CG1 
3240 C CG2 . VAL C 4   ? 2.0888 0.7411 0.7040 -0.3080 0.3917  -0.1291 4   VAL A CG2 
3241 N N   . SER C 5   ? 2.0287 0.6767 0.6602 -0.2330 0.3501  -0.1174 5   SER A N   
3242 C CA  . SER C 5   ? 2.0033 0.6546 0.6445 -0.1984 0.3349  -0.1081 5   SER A CA  
3243 C C   . SER C 5   ? 2.0484 0.6335 0.6479 -0.1769 0.3382  -0.0906 5   SER A C   
3244 O O   . SER C 5   ? 2.1811 0.7132 0.7402 -0.1907 0.3537  -0.0866 5   SER A O   
3245 C CB  . SER C 5   ? 2.0641 0.7274 0.7127 -0.2046 0.3324  -0.1188 5   SER A CB  
3246 O OG  . SER C 5   ? 2.0935 0.8098 0.7701 -0.2310 0.3333  -0.1368 5   SER A OG  
3247 N N   . LEU C 6   ? 2.0251 0.6133 0.6324 -0.1424 0.3245  -0.0800 6   LEU A N   
3248 C CA  . LEU C 6   ? 2.0627 0.5969 0.6330 -0.1168 0.3251  -0.0630 6   LEU A CA  
3249 C C   . LEU C 6   ? 2.1102 0.6073 0.6539 -0.1065 0.3277  -0.0589 6   LEU A C   
3250 O O   . LEU C 6   ? 2.0986 0.6260 0.6678 -0.0939 0.3173  -0.0621 6   LEU A O   
3251 C CB  . LEU C 6   ? 2.0150 0.5785 0.6102 -0.0840 0.3082  -0.0537 6   LEU A CB  
3252 C CG  . LEU C 6   ? 2.0381 0.5984 0.6293 -0.0789 0.3071  -0.0471 6   LEU A CG  
3253 C CD1 . LEU C 6   ? 1.9624 0.5763 0.5954 -0.0558 0.2892  -0.0451 6   LEU A CD1 
3254 C CD2 . LEU C 6   ? 2.0749 0.5670 0.6131 -0.0648 0.3142  -0.0328 6   LEU A CD2 
3255 N N   . LEU C 7   ? 2.1708 0.6018 0.6610 -0.1107 0.3427  -0.0511 7   LEU A N   
3256 C CA  . LEU C 7   ? 2.2084 0.6010 0.6677 -0.0922 0.3444  -0.0430 7   LEU A CA  
3257 C C   . LEU C 7   ? 2.2020 0.5857 0.6529 -0.0506 0.3331  -0.0268 7   LEU A C   
3258 O O   . LEU C 7   ? 2.1992 0.5823 0.6496 -0.0280 0.3265  -0.0222 7   LEU A O   
3259 C CB  . LEU C 7   ? 2.2909 0.6165 0.6914 -0.1088 0.3656  -0.0399 7   LEU A CB  
3260 C CG  . LEU C 7   ? 2.3261 0.6386 0.7149 -0.1514 0.3829  -0.0544 7   LEU A CG  
3261 C CD1 . LEU C 7   ? 2.2932 0.6469 0.7178 -0.1650 0.3759  -0.0701 7   LEU A CD1 
3262 C CD2 . LEU C 7   ? 2.3216 0.6447 0.7178 -0.1769 0.3908  -0.0601 7   LEU A CD2 
3263 N N   . GLY C 8   ? 2.2044 0.5792 0.6456 -0.0394 0.3312  -0.0182 8   GLY A N   
3264 C CA  . GLY C 8   ? 2.2045 0.5707 0.6341 0.0000  0.3204  -0.0042 8   GLY A CA  
3265 C C   . GLY C 8   ? 2.1946 0.5640 0.6247 0.0105  0.3147  0.0019  8   GLY A C   
3266 O O   . GLY C 8   ? 2.2032 0.5670 0.6306 -0.0118 0.3228  -0.0022 8   GLY A O   
3267 N N   . ILE C 9   ? 2.1725 0.5590 0.6132 0.0455  0.2993  0.0088  9   ILE A N   
3268 C CA  . ILE C 9   ? 2.1687 0.5598 0.6097 0.0644  0.2906  0.0130  9   ILE A CA  
3269 C C   . ILE C 9   ? 2.1910 0.5711 0.6129 0.1023  0.2829  0.0203  9   ILE A C   
3270 O O   . ILE C 9   ? 2.1722 0.5685 0.6055 0.1204  0.2754  0.0224  9   ILE A O   
3271 C CB  . ILE C 9   ? 2.1167 0.5537 0.5998 0.0659  0.2771  0.0110  9   ILE A CB  
3272 C CG1 . ILE C 9   ? 2.0686 0.5422 0.5884 0.0305  0.2821  -0.0030 9   ILE A CG1 
3273 C CG2 . ILE C 9   ? 2.1207 0.5561 0.5987 0.0809  0.2698  0.0146  9   ILE A CG2 
3274 C CD1 . ILE C 9   ? 1.9971 0.5361 0.5708 0.0321  0.2684  -0.0101 9   ILE A CD1 
3275 N N   . LYS C 10  ? 2.2333 0.5862 0.6248 0.1151  0.2856  0.0239  10  LYS A N   
3276 C CA  . LYS C 10  ? 2.2592 0.6020 0.6284 0.1526  0.2789  0.0296  10  LYS A CA  
3277 C C   . LYS C 10  ? 2.2566 0.6066 0.6244 0.1720  0.2681  0.0320  10  LYS A C   
3278 O O   . LYS C 10  ? 2.2732 0.6081 0.6308 0.1574  0.2743  0.0312  10  LYS A O   
3279 C CB  . LYS C 10  ? 2.3279 0.6230 0.6497 0.1540  0.2949  0.0302  10  LYS A CB  
3280 C CG  . LYS C 10  ? 2.3550 0.6399 0.6547 0.1926  0.2900  0.0344  10  LYS A CG  
3281 C CD  . LYS C 10  ? 2.4270 0.6603 0.6779 0.1927  0.3077  0.0347  10  LYS A CD  
3282 C CE  . LYS C 10  ? 2.4430 0.6717 0.6819 0.2220  0.3052  0.0386  10  LYS A CE  
3283 N NZ  . LYS C 10  ? 2.4695 0.6739 0.6929 0.2055  0.3189  0.0377  10  LYS A NZ  
3284 N N   . VAL C 11  ? 2.2379 0.6104 0.6149 0.2048  0.2524  0.0344  11  VAL A N   
3285 C CA  . VAL C 11  ? 2.2350 0.6198 0.6134 0.2253  0.2392  0.0348  11  VAL A CA  
3286 C C   . VAL C 11  ? 2.3163 0.6678 0.6522 0.2573  0.2407  0.0338  11  VAL A C   
3287 O O   . VAL C 11  ? 2.3062 0.6643 0.6376 0.2897  0.2313  0.0368  11  VAL A O   
3288 C CB  . VAL C 11  ? 2.1741 0.6030 0.5914 0.2399  0.2208  0.0357  11  VAL A CB  
3289 C CG1 . VAL C 11  ? 2.1725 0.6110 0.5907 0.2639  0.2168  0.0368  11  VAL A CG1 
3290 C CG2 . VAL C 11  ? 2.2417 0.6811 0.6567 0.2614  0.2068  0.0344  11  VAL A CG2 
3291 N N   . LEU C 12  ? 2.3371 0.6501 0.6412 0.2495  0.2529  0.0316  12  LEU A N   
3292 C CA  . LEU C 12  ? 2.4028 0.6750 0.6610 0.2762  0.2588  0.0347  12  LEU A CA  
3293 C C   . LEU C 12  ? 2.4082 0.6915 0.6620 0.3173  0.2411  0.0378  12  LEU A C   
3294 O O   . LEU C 12  ? 2.4452 0.7113 0.6709 0.3478  0.2411  0.0416  12  LEU A O   
3295 C CB  . LEU C 12  ? 2.4538 0.6827 0.6786 0.2612  0.2750  0.0326  12  LEU A CB  
3296 C CG  . LEU C 12  ? 2.4736 0.6791 0.6880 0.2229  0.2962  0.0292  12  LEU A CG  
3297 C CD1 . LEU C 12  ? 2.4249 0.6663 0.6813 0.1887  0.2944  0.0250  12  LEU A CD1 
3298 C CD2 . LEU C 12  ? 2.5351 0.6933 0.7092 0.2187  0.3116  0.0279  12  LEU A CD2 
3299 N N   . ASN C 13  ? 2.3665 0.6781 0.6463 0.3192  0.2261  0.0363  13  ASN A N   
3300 C CA  . ASN C 13  ? 2.3738 0.6944 0.6457 0.3562  0.2086  0.0386  13  ASN A CA  
3301 C C   . ASN C 13  ? 2.3291 0.6930 0.6313 0.3751  0.1915  0.0393  13  ASN A C   
3302 O O   . ASN C 13  ? 2.3204 0.7124 0.6433 0.3838  0.1749  0.0381  13  ASN A O   
3303 C CB  . ASN C 13  ? 2.4207 0.7424 0.6974 0.3482  0.2023  0.0369  13  ASN A CB  
3304 C CG  . ASN C 13  ? 2.4184 0.7626 0.7340 0.3089  0.2051  0.0336  13  ASN A CG  
3305 O OD1 . ASN C 13  ? 2.4398 0.7638 0.7510 0.2789  0.2218  0.0316  13  ASN A OD1 
3306 N ND2 . ASN C 13  ? 2.3826 0.7681 0.7348 0.3099  0.1892  0.0329  13  ASN A ND2 
3307 N N   . ASN C 14  ? 2.3280 0.6974 0.6323 0.3822  0.1954  0.0412  14  ASN A N   
3308 C CA  . ASN C 14  ? 2.2808 0.6931 0.6184 0.3953  0.1813  0.0416  14  ASN A CA  
3309 C C   . ASN C 14  ? 2.3095 0.7213 0.6283 0.4349  0.1771  0.0452  14  ASN A C   
3310 O O   . ASN C 14  ? 2.3430 0.7304 0.6400 0.4365  0.1909  0.0478  14  ASN A O   
3311 C CB  . ASN C 14  ? 2.2839 0.7149 0.6539 0.3636  0.1888  0.0405  14  ASN A CB  
3312 C CG  . ASN C 14  ? 2.2031 0.6807 0.6144 0.3690  0.1744  0.0399  14  ASN A CG  
3313 O OD1 . ASN C 14  ? 2.1677 0.6720 0.5971 0.3993  0.1594  0.0433  14  ASN A OD1 
3314 N ND2 . ASN C 14  ? 2.1685 0.6651 0.6115 0.3373  0.1771  0.0378  14  ASN A ND2 
3315 N N   . PRO C 15  ? 2.2863 0.7389 0.6335 0.4632  0.1553  0.0496  15  PRO A N   
3316 C CA  . PRO C 15  ? 2.2448 0.7347 0.6258 0.4632  0.1351  0.0497  15  PRO A CA  
3317 C C   . PRO C 15  ? 2.2791 0.7462 0.6298 0.4685  0.1314  0.0484  15  PRO A C   
3318 O O   . PRO C 15  ? 2.3383 0.7615 0.6428 0.4788  0.1433  0.0481  15  PRO A O   
3319 C CB  . PRO C 15  ? 2.2234 0.7609 0.6379 0.4967  0.1148  0.0559  15  PRO A CB  
3320 C CG  . PRO C 15  ? 2.2253 0.7610 0.6443 0.5002  0.1264  0.0576  15  PRO A CG  
3321 C CD  . PRO C 15  ? 2.2858 0.7623 0.6474 0.4926  0.1488  0.0556  15  PRO A CD  
3322 N N   . ALA C 16  ? 2.2445 0.7408 0.6200 0.4620  0.1154  0.0480  16  ALA A N   
3323 C CA  . ALA C 16  ? 2.2708 0.7512 0.6231 0.4644  0.1106  0.0470  16  ALA A CA  
3324 C C   . ALA C 16  ? 2.2678 0.7999 0.6503 0.4741  0.0841  0.0488  16  ALA A C   
3325 O O   . ALA C 16  ? 2.2192 0.7958 0.6408 0.4740  0.0717  0.0502  16  ALA A O   
3326 C CB  . ALA C 16  ? 2.2741 0.7193 0.6146 0.4276  0.1292  0.0414  16  ALA A CB  
3327 N N   . LYS C 17  ? 2.3464 0.8713 0.7081 0.4827  0.0758  0.0482  17  LYS A N   
3328 C CA  . LYS C 17  ? 2.3174 0.8874 0.6990 0.4885  0.0513  0.0472  17  LYS A CA  
3329 C C   . LYS C 17  ? 2.2792 0.8662 0.6868 0.4506  0.0545  0.0416  17  LYS A C   
3330 O O   . LYS C 17  ? 2.2803 0.8365 0.6832 0.4218  0.0754  0.0395  17  LYS A O   
3331 C CB  . LYS C 17  ? 2.3418 0.8943 0.6896 0.5081  0.0438  0.0472  17  LYS A CB  
3332 C CG  . LYS C 17  ? 2.4296 0.9764 0.7519 0.5506  0.0360  0.0515  17  LYS A CG  
3333 C CD  . LYS C 17  ? 2.4610 1.0629 0.7999 0.5784  0.0040  0.0513  17  LYS A CD  
3334 C CE  . LYS C 17  ? 2.5068 1.1400 0.8618 0.6096  -0.0070 0.0559  17  LYS A CE  
3335 N NZ  . LYS C 17  ? 2.5503 1.2344 0.9157 0.6425  -0.0378 0.0553  17  LYS A NZ  
3336 N N   . PHE C 18  ? 2.2148 0.8567 0.6560 0.4497  0.0338  0.0366  18  PHE A N   
3337 C CA  . PHE C 18  ? 2.2119 0.8780 0.6855 0.4147  0.0365  0.0277  18  PHE A CA  
3338 C C   . PHE C 18  ? 2.2190 0.8391 0.6557 0.3997  0.0501  0.0292  18  PHE A C   
3339 O O   . PHE C 18  ? 2.2002 0.8043 0.6454 0.3691  0.0691  0.0276  18  PHE A O   
3340 C CB  . PHE C 18  ? 2.1634 0.8972 0.6881 0.4166  0.0119  0.0179  18  PHE A CB  
3341 C CG  . PHE C 18  ? 2.1542 0.9308 0.7366 0.3833  0.0148  0.0081  18  PHE A CG  
3342 C CD1 . PHE C 18  ? 2.0906 0.9301 0.7386 0.3818  0.0027  0.0007  18  PHE A CD1 
3343 C CD2 . PHE C 18  ? 2.1388 0.8935 0.7092 0.3545  0.0301  0.0064  18  PHE A CD2 
3344 C CE1 . PHE C 18  ? 1.9768 0.8518 0.6741 0.3532  0.0070  -0.0075 18  PHE A CE1 
3345 C CE2 . PHE C 18  ? 2.0538 0.8480 0.6751 0.3268  0.0332  -0.0019 18  PHE A CE2 
3346 C CZ  . PHE C 18  ? 1.9745 0.8269 0.6575 0.3269  0.0218  -0.0087 18  PHE A CZ  
3347 N N   . THR C 19  ? 2.2420 0.8463 0.6497 0.4208  0.0410  0.0312  19  THR A N   
3348 C CA  . THR C 19  ? 2.2615 0.8298 0.6454 0.4093  0.0520  0.0316  19  THR A CA  
3349 C C   . THR C 19  ? 2.3018 0.8118 0.6594 0.3980  0.0794  0.0353  19  THR A C   
3350 O O   . THR C 19  ? 2.3137 0.7940 0.6565 0.3811  0.0926  0.0352  19  THR A O   
3351 C CB  . THR C 19  ? 2.2605 0.8270 0.6172 0.4406  0.0345  0.0325  19  THR A CB  
3352 O OG1 . THR C 19  ? 2.3040 0.8158 0.6174 0.4572  0.0485  0.0377  19  THR A OG1 
3353 C CG2 . THR C 19  ? 2.2566 0.8684 0.6263 0.4704  0.0088  0.0317  19  THR A CG2 
3354 N N   . ASP C 20  ? 2.2927 0.7858 0.6440 0.4059  0.0886  0.0377  20  ASP A N   
3355 C CA  . ASP C 20  ? 2.3059 0.7407 0.6259 0.3976  0.1139  0.0387  20  ASP A CA  
3356 C C   . ASP C 20  ? 2.2934 0.7214 0.6331 0.3560  0.1321  0.0357  20  ASP A C   
3357 O O   . ASP C 20  ? 2.3026 0.7696 0.6814 0.3389  0.1282  0.0338  20  ASP A O   
3358 C CB  . ASP C 20  ? 2.3474 0.7692 0.6546 0.4186  0.1181  0.0405  20  ASP A CB  
3359 C CG  . ASP C 20  ? 2.4051 0.8123 0.6771 0.4594  0.1098  0.0439  20  ASP A CG  
3360 O OD1 . ASP C 20  ? 2.3955 0.7956 0.6482 0.4716  0.1022  0.0446  20  ASP A OD1 
3361 O OD2 . ASP C 20  ? 2.3834 0.7883 0.6475 0.4803  0.1109  0.0459  20  ASP A OD2 
3362 N N   . PRO C 21  ? 2.3187 0.6996 0.6322 0.3394  0.1523  0.0350  21  PRO A N   
3363 C CA  . PRO C 21  ? 2.2950 0.6710 0.6272 0.2997  0.1698  0.0323  21  PRO A CA  
3364 C C   . PRO C 21  ? 2.3357 0.7105 0.6799 0.2895  0.1792  0.0309  21  PRO A C   
3365 O O   . PRO C 21  ? 2.3385 0.7120 0.6734 0.3120  0.1755  0.0322  21  PRO A O   
3366 C CB  . PRO C 21  ? 2.3667 0.6875 0.6596 0.2910  0.1894  0.0318  21  PRO A CB  
3367 C CG  . PRO C 21  ? 2.3936 0.6838 0.6438 0.3275  0.1873  0.0343  21  PRO A CG  
3368 C CD  . PRO C 21  ? 2.3808 0.7121 0.6458 0.3562  0.1604  0.0362  21  PRO A CD  
3369 N N   . TYR C 22  ? 2.3396 0.7250 0.7093 0.2529  0.1912  0.0291  22  TYR A N   
3370 C CA  . TYR C 22  ? 2.2965 0.6908 0.6844 0.2349  0.2011  0.0285  22  TYR A CA  
3371 C C   . TYR C 22  ? 2.3427 0.6995 0.7074 0.2130  0.2233  0.0275  22  TYR A C   
3372 O O   . TYR C 22  ? 2.2885 0.6387 0.6555 0.1869  0.2338  0.0254  22  TYR A O   
3373 C CB  . TYR C 22  ? 2.2324 0.6655 0.6633 0.2093  0.1992  0.0262  22  TYR A CB  
3374 C CG  . TYR C 22  ? 2.1991 0.6920 0.6669 0.2207  0.1787  0.0248  22  TYR A CG  
3375 C CD1 . TYR C 22  ? 2.1473 0.6800 0.6499 0.2173  0.1742  0.0223  22  TYR A CD1 
3376 C CD2 . TYR C 22  ? 2.1643 0.6760 0.6330 0.2334  0.1646  0.0246  22  TYR A CD2 
3377 C CE1 . TYR C 22  ? 2.0846 0.6716 0.6210 0.2263  0.1574  0.0182  22  TYR A CE1 
3378 C CE2 . TYR C 22  ? 2.0592 0.6249 0.5604 0.2416  0.1467  0.0214  22  TYR A CE2 
3379 C CZ  . TYR C 22  ? 1.9917 0.5934 0.5259 0.2379  0.1438  0.0176  22  TYR A CZ  
3380 O OH  . TYR C 22  ? 1.9697 0.6213 0.5343 0.2457  0.1277  0.0121  22  TYR A OH  
3381 N N   . GLU C 23  ? 2.4852 0.8172 0.8263 0.2234  0.2313  0.0282  23  GLU A N   
3382 C CA  . GLU C 23  ? 2.5152 0.8140 0.8368 0.1996  0.2532  0.0257  23  GLU A CA  
3383 C C   . GLU C 23  ? 2.4552 0.7713 0.8014 0.1826  0.2570  0.0245  23  GLU A C   
3384 O O   . GLU C 23  ? 2.4526 0.7770 0.7991 0.2030  0.2507  0.0254  23  GLU A O   
3385 C CB  . GLU C 23  ? 2.5551 0.8088 0.8264 0.2213  0.2624  0.0270  23  GLU A CB  
3386 C CG  . GLU C 23  ? 2.5799 0.8259 0.8283 0.2590  0.2491  0.0310  23  GLU A CG  
3387 C CD  . GLU C 23  ? 2.5857 0.8265 0.8307 0.2533  0.2474  0.0310  23  GLU A CD  
3388 O OE1 . GLU C 23  ? 2.5859 0.8239 0.8413 0.2202  0.2596  0.0282  23  GLU A OE1 
3389 O OE2 . GLU C 23  ? 2.5948 0.8357 0.8264 0.2828  0.2335  0.0334  23  GLU A OE2 
3390 N N   . PHE C 24  ? 2.3105 0.6336 0.6755 0.1460  0.2675  0.0227  24  PHE A N   
3391 C CA  . PHE C 24  ? 2.2937 0.6366 0.6810 0.1266  0.2710  0.0235  24  PHE A CA  
3392 C C   . PHE C 24  ? 2.2836 0.5928 0.6476 0.0990  0.2925  0.0219  24  PHE A C   
3393 O O   . PHE C 24  ? 2.2855 0.5900 0.6522 0.0697  0.3040  0.0164  24  PHE A O   
3394 C CB  . PHE C 24  ? 2.2380 0.6235 0.6655 0.1072  0.2652  0.0196  24  PHE A CB  
3395 C CG  . PHE C 24  ? 2.2371 0.6620 0.6931 0.1289  0.2463  0.0214  24  PHE A CG  
3396 C CD1 . PHE C 24  ? 2.2840 0.7100 0.7311 0.1645  0.2319  0.0254  24  PHE A CD1 
3397 C CD2 . PHE C 24  ? 2.0798 0.5402 0.5708 0.1138  0.2437  0.0182  24  PHE A CD2 
3398 C CE1 . PHE C 24  ? 2.2225 0.6854 0.6958 0.1826  0.2156  0.0261  24  PHE A CE1 
3399 C CE2 . PHE C 24  ? 2.0319 0.5366 0.5549 0.1319  0.2276  0.0172  24  PHE A CE2 
3400 C CZ  . PHE C 24  ? 2.0431 0.5431 0.5535 0.1658  0.2143  0.0224  24  PHE A CZ  
3401 N N   . GLU C 25  ? 2.3489 0.6387 0.6849 0.1075  0.2992  0.0269  25  GLU A N   
3402 C CA  . GLU C 25  ? 2.3887 0.6506 0.6990 0.0800  0.3205  0.0226  25  GLU A CA  
3403 C C   . GLU C 25  ? 2.3552 0.6427 0.6998 0.0530  0.3213  0.0166  25  GLU A C   
3404 O O   . GLU C 25  ? 2.3279 0.6351 0.6884 0.0641  0.3126  0.0174  25  GLU A O   
3405 C CB  . GLU C 25  ? 2.4428 0.6723 0.7107 0.0992  0.3284  0.0226  25  GLU A CB  
3406 C CG  . GLU C 25  ? 2.5067 0.6892 0.7347 0.0762  0.3526  0.0178  25  GLU A CG  
3407 C CD  . GLU C 25  ? 2.5878 0.7524 0.8033 0.0683  0.3613  0.0174  25  GLU A CD  
3408 O OE1 . GLU C 25  ? 2.5525 0.7370 0.7840 0.0879  0.3489  0.0210  25  GLU A OE1 
3409 O OE2 . GLU C 25  ? 2.6087 0.7378 0.7962 0.0430  0.3816  0.0128  25  GLU A OE2 
3410 N N   . ILE C 26  ? 2.3108 0.5995 0.6650 0.0184  0.3323  0.0097  26  ILE A N   
3411 C CA  . ILE C 26  ? 2.2661 0.5861 0.6535 -0.0076 0.3323  0.0024  26  ILE A CA  
3412 C C   . ILE C 26  ? 2.3057 0.5995 0.6720 -0.0410 0.3528  -0.0045 26  ILE A C   
3413 O O   . ILE C 26  ? 2.3333 0.6102 0.6869 -0.0668 0.3678  -0.0096 26  ILE A O   
3414 C CB  . ILE C 26  ? 2.2236 0.5739 0.6412 -0.0206 0.3275  -0.0017 26  ILE A CB  
3415 C CG1 . ILE C 26  ? 2.1763 0.5595 0.6195 0.0098  0.3062  0.0034  26  ILE A CG1 
3416 C CG2 . ILE C 26  ? 2.1982 0.5697 0.6376 -0.0563 0.3356  -0.0109 26  ILE A CG2 
3417 C CD1 . ILE C 26  ? 2.1599 0.5547 0.6134 0.0096  0.3017  0.0028  26  ILE A CD1 
3418 N N   . THR C 27  ? 2.3109 0.6007 0.6726 -0.0408 0.3539  -0.0051 27  THR A N   
3419 C CA  . THR C 27  ? 2.3447 0.6132 0.6891 -0.0743 0.3720  -0.0131 27  THR A CA  
3420 C C   . THR C 27  ? 2.2969 0.6025 0.6772 -0.1020 0.3705  -0.0217 27  THR A C   
3421 O O   . THR C 27  ? 2.2399 0.5898 0.6596 -0.0872 0.3534  -0.0234 27  THR A O   
3422 C CB  . THR C 27  ? 2.3799 0.6214 0.6974 -0.0606 0.3750  -0.0099 27  THR A CB  
3423 O OG1 . THR C 27  ? 2.4096 0.6334 0.7057 -0.0230 0.3686  -0.0004 27  THR A OG1 
3424 C CG2 . THR C 27  ? 2.4428 0.6429 0.7235 -0.0912 0.3980  -0.0169 27  THR A CG2 
3425 N N   . PHE C 28  ? 2.3141 0.6148 0.6906 -0.1403 0.3864  -0.0315 28  PHE A N   
3426 C CA  . PHE C 28  ? 2.2596 0.6204 0.6877 -0.1653 0.3813  -0.0488 28  PHE A CA  
3427 C C   . PHE C 28  ? 2.3017 0.6454 0.7128 -0.2071 0.4019  -0.0619 28  PHE A C   
3428 O O   . PHE C 28  ? 2.3726 0.6568 0.7316 -0.2182 0.4218  -0.0568 28  PHE A O   
3429 C CB  . PHE C 28  ? 2.2513 0.6544 0.7142 -0.1636 0.3722  -0.0507 28  PHE A CB  
3430 C CG  . PHE C 28  ? 2.2542 0.6391 0.7012 -0.1931 0.3898  -0.0552 28  PHE A CG  
3431 C CD1 . PHE C 28  ? 2.2200 0.6457 0.6949 -0.2278 0.3963  -0.0724 28  PHE A CD1 
3432 C CD2 . PHE C 28  ? 2.2885 0.6209 0.6954 -0.1840 0.3989  -0.0432 28  PHE A CD2 
3433 C CE1 . PHE C 28  ? 2.2483 0.6595 0.7098 -0.2549 0.4134  -0.0770 28  PHE A CE1 
3434 C CE2 . PHE C 28  ? 2.3127 0.6358 0.7119 -0.2086 0.4139  -0.0498 28  PHE A CE2 
3435 C CZ  . PHE C 28  ? 2.2985 0.6502 0.7181 -0.2469 0.4240  -0.0642 28  PHE A CZ  
3436 N N   . GLU C 29  ? 2.2593 0.6581 0.7131 -0.2295 0.3973  -0.0795 29  GLU A N   
3437 C CA  . GLU C 29  ? 2.2921 0.6866 0.7381 -0.2700 0.4136  -0.0956 29  GLU A CA  
3438 C C   . GLU C 29  ? 2.2499 0.7034 0.7366 -0.2965 0.4130  -0.1116 29  GLU A C   
3439 O O   . GLU C 29  ? 2.1826 0.6951 0.7135 -0.2814 0.3955  -0.1134 29  GLU A O   
3440 C CB  . GLU C 29  ? 2.2880 0.6940 0.7433 -0.2703 0.4074  -0.1039 29  GLU A CB  
3441 C CG  . GLU C 29  ? 2.2533 0.7145 0.7544 -0.2407 0.3830  -0.1029 29  GLU A CG  
3442 C CD  . GLU C 29  ? 2.2720 0.7635 0.7945 -0.2488 0.3767  -0.1167 29  GLU A CD  
3443 O OE1 . GLU C 29  ? 2.3292 0.8176 0.8536 -0.2215 0.3659  -0.1098 29  GLU A OE1 
3444 O OE2 . GLU C 29  ? 2.3044 0.8231 0.8408 -0.2824 0.3828  -0.1349 29  GLU A OE2 
3445 N N   . CYS C 30  ? 2.2910 0.7312 0.7621 -0.3361 0.4330  -0.1237 30  CYS A N   
3446 C CA  . CYS C 30  ? 2.3064 0.8016 0.8114 -0.3645 0.4357  -0.1400 30  CYS A CA  
3447 C C   . CYS C 30  ? 2.3698 0.8806 0.8788 -0.4046 0.4463  -0.1615 30  CYS A C   
3448 O O   . CYS C 30  ? 2.3577 0.8154 0.8266 -0.4275 0.4664  -0.1637 30  CYS A O   
3449 C CB  . CYS C 30  ? 2.3497 0.8164 0.8328 -0.3759 0.4517  -0.1341 30  CYS A CB  
3450 S SG  . CYS C 30  ? 2.3610 0.8654 0.8605 -0.4271 0.4698  -0.1565 30  CYS A SG  
3451 N N   . LEU C 31  ? 2.3265 0.9122 0.8829 -0.4123 0.4333  -0.1775 31  LEU A N   
3452 C CA  . LEU C 31  ? 2.3236 0.9388 0.8915 -0.4503 0.4399  -0.2008 31  LEU A CA  
3453 C C   . LEU C 31  ? 2.3278 0.9999 0.9236 -0.4778 0.4455  -0.2156 31  LEU A C   
3454 O O   . LEU C 31  ? 2.3344 1.0652 0.9668 -0.4593 0.4309  -0.2136 31  LEU A O   
3455 C CB  . LEU C 31  ? 2.2613 0.9212 0.8593 -0.4357 0.4198  -0.2087 31  LEU A CB  
3456 C CG  . LEU C 31  ? 2.2827 0.9002 0.8612 -0.4045 0.4111  -0.1952 31  LEU A CG  
3457 C CD1 . LEU C 31  ? 2.3418 0.8729 0.8641 -0.4110 0.4306  -0.1844 31  LEU A CD1 
3458 C CD2 . LEU C 31  ? 2.2232 0.8578 0.8213 -0.3587 0.3917  -0.1781 31  LEU A CD2 
3459 N N   . GLU C 32  ? 2.3470 1.0033 0.9254 -0.5216 0.4676  -0.2299 32  GLU A N   
3460 C CA  . GLU C 32  ? 2.4144 1.1209 1.0149 -0.5517 0.4769  -0.2446 32  GLU A CA  
3461 C C   . GLU C 32  ? 2.4782 1.1701 1.0714 -0.5345 0.4813  -0.2276 32  GLU A C   
3462 O O   . GLU C 32  ? 2.4271 1.1680 1.0521 -0.5058 0.4640  -0.2197 32  GLU A O   
3463 C CB  . GLU C 32  ? 2.3250 1.1290 0.9784 -0.5516 0.4581  -0.2610 32  GLU A CB  
3464 C CG  . GLU C 32  ? 2.3350 1.1983 1.0102 -0.5970 0.4691  -0.2871 32  GLU A CG  
3465 C CD  . GLU C 32  ? 2.3750 1.2506 1.0505 -0.6121 0.4853  -0.2856 32  GLU A CD  
3466 O OE1 . GLU C 32  ? 2.3440 1.2436 1.0232 -0.6556 0.5024  -0.3056 32  GLU A OE1 
3467 O OE2 . GLU C 32  ? 2.4145 1.2788 1.0882 -0.5809 0.4810  -0.2649 32  GLU A OE2 
3468 N N   . SER C 33  ? 2.6191 1.2436 1.1700 -0.5509 0.5049  -0.2212 33  SER A N   
3469 C CA  . SER C 33  ? 2.6531 1.2530 1.1913 -0.5314 0.5087  -0.2035 33  SER A CA  
3470 C C   . SER C 33  ? 2.6421 1.3114 1.2157 -0.5442 0.5103  -0.2118 33  SER A C   
3471 O O   . SER C 33  ? 2.6196 1.3375 1.2127 -0.5805 0.5194  -0.2328 33  SER A O   
3472 C CB  . SER C 33  ? 2.7336 1.2408 1.2132 -0.5459 0.5357  -0.1944 33  SER A CB  
3473 O OG  . SER C 33  ? 2.7437 1.2309 1.2138 -0.5332 0.5408  -0.1820 33  SER A OG  
3474 N N   . LEU C 34  ? 2.5812 1.2590 1.1645 -0.5129 0.5010  -0.1945 34  LEU A N   
3475 C CA  . LEU C 34  ? 2.5014 1.2444 1.1186 -0.5174 0.5018  -0.1961 34  LEU A CA  
3476 C C   . LEU C 34  ? 2.4620 1.1625 1.0603 -0.4952 0.5050  -0.1764 34  LEU A C   
3477 O O   . LEU C 34  ? 2.4882 1.1187 1.0518 -0.4724 0.5026  -0.1626 34  LEU A O   
3478 C CB  . LEU C 34  ? 2.4188 1.2528 1.0897 -0.4955 0.4771  -0.1981 34  LEU A CB  
3479 C CG  . LEU C 34  ? 2.3595 1.2796 1.0710 -0.5127 0.4808  -0.2080 34  LEU A CG  
3480 C CD1 . LEU C 34  ? 2.4204 1.3775 1.1411 -0.5534 0.4901  -0.2338 34  LEU A CD1 
3481 C CD2 . LEU C 34  ? 2.3101 1.3016 1.0664 -0.4779 0.4572  -0.2001 34  LEU A CD2 
3482 N N   . LYS C 35  ? 2.4001 1.1447 1.0218 -0.5008 0.5101  -0.1753 35  LYS A N   
3483 C CA  . LYS C 35  ? 2.3843 1.0850 0.9846 -0.4915 0.5195  -0.1620 35  LYS A CA  
3484 C C   . LYS C 35  ? 2.3465 1.0608 0.9623 -0.4459 0.4978  -0.1431 35  LYS A C   
3485 O O   . LYS C 35  ? 2.3740 1.0304 0.9601 -0.4268 0.4994  -0.1304 35  LYS A O   
3486 C CB  . LYS C 35  ? 2.4117 1.1487 1.0277 -0.5243 0.5395  -0.1708 35  LYS A CB  
3487 C CG  . LYS C 35  ? 2.3418 1.1776 1.0129 -0.5171 0.5283  -0.1706 35  LYS A CG  
3488 C CD  . LYS C 35  ? 2.3206 1.2287 1.0257 -0.5305 0.5198  -0.1867 35  LYS A CD  
3489 C CE  . LYS C 35  ? 2.2620 1.2635 1.0137 -0.5447 0.5228  -0.1943 35  LYS A CE  
3490 N NZ  . LYS C 35  ? 2.2278 1.2904 1.0034 -0.5679 0.5207  -0.2153 35  LYS A NZ  
3491 N N   . HIS C 36  ? 2.2771 1.0655 0.9374 -0.4275 0.4779  -0.1419 36  HIS A N   
3492 C CA  . HIS C 36  ? 2.2205 1.0308 0.8996 -0.3917 0.4614  -0.1265 36  HIS A CA  
3493 C C   . HIS C 36  ? 2.2218 0.9735 0.8744 -0.3565 0.4479  -0.1117 36  HIS A C   
3494 O O   . HIS C 36  ? 2.2481 1.0093 0.9104 -0.3286 0.4356  -0.0996 36  HIS A O   
3495 C CB  . HIS C 36  ? 2.1701 1.0676 0.9000 -0.3788 0.4436  -0.1291 36  HIS A CB  
3496 C CG  . HIS C 36  ? 2.1761 1.1413 0.9379 -0.3983 0.4530  -0.1363 36  HIS A CG  
3497 N ND1 . HIS C 36  ? 2.1996 1.1548 0.9493 -0.4319 0.4767  -0.1434 36  HIS A ND1 
3498 C CD2 . HIS C 36  ? 2.0993 1.1428 0.9045 -0.3871 0.4424  -0.1366 36  HIS A CD2 
3499 C CE1 . HIS C 36  ? 2.1890 1.2176 0.9754 -0.4409 0.4798  -0.1478 36  HIS A CE1 
3500 N NE2 . HIS C 36  ? 2.0891 1.1711 0.9083 -0.4130 0.4591  -0.1435 36  HIS A NE2 
3501 N N   . ASP C 37  ? 2.2281 0.9221 0.8481 -0.3568 0.4497  -0.1125 37  ASP A N   
3502 C CA  . ASP C 37  ? 2.2128 0.8440 0.8010 -0.3256 0.4406  -0.0988 37  ASP A CA  
3503 C C   . ASP C 37  ? 2.1851 0.8481 0.7992 -0.2895 0.4140  -0.0904 37  ASP A C   
3504 O O   . ASP C 37  ? 2.0799 0.8130 0.7375 -0.2826 0.4015  -0.0923 37  ASP A O   
3505 C CB  . ASP C 37  ? 2.2867 0.8786 0.8511 -0.3146 0.4470  -0.0890 37  ASP A CB  
3506 C CG  . ASP C 37  ? 2.3216 0.8290 0.8364 -0.2971 0.4494  -0.0810 37  ASP A CG  
3507 O OD1 . ASP C 37  ? 2.3590 0.8135 0.8397 -0.3175 0.4662  -0.0879 37  ASP A OD1 
3508 O OD2 . ASP C 37  ? 2.2623 0.7576 0.7721 -0.2628 0.4345  -0.0687 37  ASP A OD2 
3509 N N   . LEU C 38  ? 2.1987 0.8087 0.7848 -0.2655 0.4064  -0.0810 38  LEU A N   
3510 C CA  . LEU C 38  ? 2.1143 0.7443 0.7188 -0.2350 0.3842  -0.0748 38  LEU A CA  
3511 C C   . LEU C 38  ? 2.1102 0.7305 0.7120 -0.2002 0.3697  -0.0610 38  LEU A C   
3512 O O   . LEU C 38  ? 2.1632 0.7235 0.7259 -0.1908 0.3755  -0.0536 38  LEU A O   
3513 C CB  . LEU C 38  ? 2.0802 0.6606 0.6555 -0.2334 0.3866  -0.0744 38  LEU A CB  
3514 C CG  . LEU C 38  ? 2.0673 0.6844 0.6666 -0.2432 0.3818  -0.0847 38  LEU A CG  
3515 C CD1 . LEU C 38  ? 2.1006 0.7362 0.7044 -0.2843 0.3989  -0.1009 38  LEU A CD1 
3516 C CD2 . LEU C 38  ? 2.0881 0.6533 0.6572 -0.2307 0.3805  -0.0793 38  LEU A CD2 
3517 N N   . GLU C 39  ? 2.0665 0.7440 0.7079 -0.1804 0.3508  -0.0586 39  GLU A N   
3518 C CA  . GLU C 39  ? 2.0074 0.6852 0.6512 -0.1496 0.3357  -0.0476 39  GLU A CA  
3519 C C   . GLU C 39  ? 1.9844 0.6586 0.6311 -0.1223 0.3188  -0.0424 39  GLU A C   
3520 O O   . GLU C 39  ? 1.9307 0.6560 0.6145 -0.1148 0.3066  -0.0453 39  GLU A O   
3521 C CB  . GLU C 39  ? 2.0119 0.7535 0.6957 -0.1486 0.3289  -0.0488 39  GLU A CB  
3522 C CG  . GLU C 39  ? 1.9706 0.7287 0.6680 -0.1176 0.3100  -0.0402 39  GLU A CG  
3523 C CD  . GLU C 39  ? 2.0393 0.7509 0.7030 -0.1044 0.3108  -0.0316 39  GLU A CD  
3524 O OE1 . GLU C 39  ? 2.0770 0.7332 0.7044 -0.0927 0.3111  -0.0268 39  GLU A OE1 
3525 O OE2 . GLU C 39  ? 2.0495 0.7793 0.7219 -0.1039 0.3110  -0.0297 39  GLU A OE2 
3526 N N   . TRP C 40  ? 1.9781 0.5922 0.5853 -0.1062 0.3188  -0.0347 40  TRP A N   
3527 C CA  . TRP C 40  ? 1.9705 0.5765 0.5756 -0.0791 0.3044  -0.0290 40  TRP A CA  
3528 C C   . TRP C 40  ? 1.9453 0.5679 0.5604 -0.0508 0.2872  -0.0218 40  TRP A C   
3529 O O   . TRP C 40  ? 1.9815 0.5669 0.5672 -0.0391 0.2878  -0.0156 40  TRP A O   
3530 C CB  . TRP C 40  ? 2.0376 0.5709 0.5931 -0.0729 0.3128  -0.0236 40  TRP A CB  
3531 C CG  . TRP C 40  ? 2.0616 0.5770 0.6065 -0.0955 0.3262  -0.0297 40  TRP A CG  
3532 C CD1 . TRP C 40  ? 2.1120 0.6058 0.6406 -0.1280 0.3463  -0.0369 40  TRP A CD1 
3533 C CD2 . TRP C 40  ? 2.0537 0.5720 0.6032 -0.0887 0.3211  -0.0301 40  TRP A CD2 
3534 N NE1 . TRP C 40  ? 2.1170 0.5990 0.6383 -0.1427 0.3537  -0.0420 40  TRP A NE1 
3535 C CE2 . TRP C 40  ? 2.0867 0.5838 0.6209 -0.1180 0.3381  -0.0376 40  TRP A CE2 
3536 C CE3 . TRP C 40  ? 2.0234 0.5607 0.5884 -0.0609 0.3043  -0.0255 40  TRP A CE3 
3537 C CZ2 . TRP C 40  ? 2.1014 0.5960 0.6352 -0.1192 0.3379  -0.0401 40  TRP A CZ2 
3538 C CZ3 . TRP C 40  ? 2.0262 0.5602 0.5911 -0.0613 0.3048  -0.0276 40  TRP A CZ3 
3539 C CH2 . TRP C 40  ? 2.0980 0.6119 0.6481 -0.0898 0.3208  -0.0348 40  TRP A CH2 
3540 N N   . LYS C 41  ? 1.8878 0.5630 0.5416 -0.0389 0.2722  -0.0232 41  LYS A N   
3541 C CA  . LYS C 41  ? 1.8600 0.5578 0.5275 -0.0160 0.2563  -0.0186 41  LYS A CA  
3542 C C   . LYS C 41  ? 1.8487 0.5480 0.5191 0.0101  0.2417  -0.0152 41  LYS A C   
3543 O O   . LYS C 41  ? 1.8253 0.5447 0.5149 0.0085  0.2402  -0.0190 41  LYS A O   
3544 C CB  . LYS C 41  ? 1.8030 0.5632 0.5144 -0.0262 0.2532  -0.0239 41  LYS A CB  
3545 C CG  . LYS C 41  ? 1.7664 0.5583 0.4990 -0.0061 0.2372  -0.0212 41  LYS A CG  
3546 C CD  . LYS C 41  ? 1.7193 0.5656 0.4898 -0.0189 0.2386  -0.0261 41  LYS A CD  
3547 C CE  . LYS C 41  ? 1.7322 0.5799 0.5007 -0.0465 0.2558  -0.0306 41  LYS A CE  
3548 N NZ  . LYS C 41  ? 1.6840 0.5910 0.4922 -0.0579 0.2576  -0.0362 41  LYS A NZ  
3549 N N   . LEU C 42  ? 1.8657 0.5461 0.5176 0.0347  0.2308  -0.0088 42  LEU A N   
3550 C CA  . LEU C 42  ? 1.8543 0.5415 0.5103 0.0609  0.2161  -0.0063 42  LEU A CA  
3551 C C   . LEU C 42  ? 1.8138 0.5436 0.4968 0.0738  0.2007  -0.0074 42  LEU A C   
3552 O O   . LEU C 42  ? 1.8254 0.5482 0.4963 0.0793  0.1965  -0.0048 42  LEU A O   
3553 C CB  . LEU C 42  ? 1.9132 0.5432 0.5226 0.0819  0.2152  0.0010  42  LEU A CB  
3554 C CG  . LEU C 42  ? 1.9100 0.5444 0.5175 0.1131  0.1993  0.0041  42  LEU A CG  
3555 C CD1 . LEU C 42  ? 1.9490 0.5427 0.5285 0.1229  0.2050  0.0080  42  LEU A CD1 
3556 C CD2 . LEU C 42  ? 1.9382 0.5543 0.5204 0.1347  0.1892  0.0086  42  LEU A CD2 
3557 N N   . THR C 43  ? 1.7670 0.5384 0.4846 0.0788  0.1928  -0.0116 43  THR A N   
3558 C CA  . THR C 43  ? 1.7232 0.5391 0.4719 0.0846  0.1817  -0.0148 43  THR A CA  
3559 C C   . THR C 43  ? 1.7153 0.5393 0.4680 0.1095  0.1676  -0.0151 43  THR A C   
3560 O O   . THR C 43  ? 1.7208 0.5500 0.4835 0.1144  0.1683  -0.0167 43  THR A O   
3561 C CB  . THR C 43  ? 1.6735 0.5358 0.4635 0.0661  0.1876  -0.0210 43  THR A CB  
3562 O OG1 . THR C 43  ? 1.6986 0.5495 0.4830 0.0442  0.2023  -0.0225 43  THR A OG1 
3563 C CG2 . THR C 43  ? 1.6746 0.5675 0.4841 0.0615  0.1845  -0.0226 43  THR A CG2 
3564 N N   . TYR C 44  ? 1.7198 0.5470 0.4656 0.1252  0.1549  -0.0146 44  TYR A N   
3565 C CA  . TYR C 44  ? 1.7109 0.5519 0.4631 0.1480  0.1408  -0.0173 44  TYR A CA  
3566 C C   . TYR C 44  ? 1.6562 0.5462 0.4532 0.1419  0.1387  -0.0248 44  TYR A C   
3567 O O   . TYR C 44  ? 1.6726 0.5851 0.4871 0.1287  0.1405  -0.0269 44  TYR A O   
3568 C CB  . TYR C 44  ? 1.7401 0.5671 0.4662 0.1664  0.1271  -0.0156 44  TYR A CB  
3569 C CG  . TYR C 44  ? 1.7306 0.5792 0.4689 0.1892  0.1098  -0.0197 44  TYR A CG  
3570 C CD1 . TYR C 44  ? 1.6841 0.5806 0.4683 0.1853  0.1011  -0.0260 44  TYR A CD1 
3571 C CD2 . TYR C 44  ? 1.7622 0.5929 0.4823 0.2131  0.1007  -0.0150 44  TYR A CD2 
3572 C CE1 . TYR C 44  ? 1.6679 0.5954 0.4823 0.2017  0.0843  -0.0285 44  TYR A CE1 
3573 C CE2 . TYR C 44  ? 1.7443 0.6098 0.4958 0.2317  0.0827  -0.0171 44  TYR A CE2 
3574 C CZ  . TYR C 44  ? 1.6965 0.6111 0.4964 0.2244  0.0747  -0.0243 44  TYR A CZ  
3575 O OH  . TYR C 44  ? 1.6785 0.6303 0.5130 0.2394  0.0579  -0.0278 44  TYR A OH  
3576 N N   . VAL C 45  ? 1.6373 0.5433 0.4538 0.1523  0.1359  -0.0282 45  VAL A N   
3577 C CA  . VAL C 45  ? 1.5842 0.5388 0.4516 0.1479  0.1341  -0.0332 45  VAL A CA  
3578 C C   . VAL C 45  ? 1.5705 0.5490 0.4660 0.1672  0.1186  -0.0336 45  VAL A C   
3579 O O   . VAL C 45  ? 1.5813 0.5526 0.4767 0.1816  0.1155  -0.0306 45  VAL A O   
3580 C CB  . VAL C 45  ? 1.5612 0.5273 0.4467 0.1375  0.1466  -0.0351 45  VAL A CB  
3581 C CG1 . VAL C 45  ? 1.5563 0.5678 0.4864 0.1313  0.1477  -0.0397 45  VAL A CG1 
3582 C CG2 . VAL C 45  ? 1.5989 0.5479 0.4686 0.1177  0.1587  -0.0323 45  VAL A CG2 
3583 N N   . GLY C 46  ? 1.5682 0.5762 0.4889 0.1668  0.1098  -0.0377 46  GLY A N   
3584 C CA  . GLY C 46  ? 1.5345 0.5695 0.4850 0.1820  0.0949  -0.0399 46  GLY A CA  
3585 C C   . GLY C 46  ? 1.4871 0.5647 0.4884 0.1762  0.0970  -0.0450 46  GLY A C   
3586 O O   . GLY C 46  ? 1.4640 0.5525 0.4758 0.1611  0.1077  -0.0474 46  GLY A O   
3587 N N   . SER C 47  ? 1.4746 0.5766 0.5071 0.1891  0.0878  -0.0463 47  SER A N   
3588 C CA  . SER C 47  ? 1.4345 0.5754 0.5154 0.1849  0.0896  -0.0513 47  SER A CA  
3589 C C   . SER C 47  ? 1.4355 0.5999 0.5393 0.1965  0.0729  -0.0553 47  SER A C   
3590 O O   . SER C 47  ? 1.4511 0.6152 0.5543 0.2131  0.0641  -0.0525 47  SER A O   
3591 C CB  . SER C 47  ? 1.4126 0.5633 0.5157 0.1864  0.1015  -0.0488 47  SER A CB  
3592 O OG  . SER C 47  ? 1.4037 0.5446 0.4951 0.1724  0.1165  -0.0480 47  SER A OG  
3593 N N   . SER C 48  ? 1.4215 0.6058 0.5439 0.1877  0.0686  -0.0622 48  SER A N   
3594 C CA  . SER C 48  ? 1.4561 0.6653 0.6009 0.1941  0.0521  -0.0688 48  SER A CA  
3595 C C   . SER C 48  ? 1.4598 0.6974 0.6434 0.1807  0.0575  -0.0763 48  SER A C   
3596 O O   . SER C 48  ? 1.4225 0.6553 0.6059 0.1681  0.0725  -0.0757 48  SER A O   
3597 C CB  . SER C 48  ? 1.4582 0.6491 0.5664 0.1980  0.0374  -0.0705 48  SER A CB  
3598 O OG  . SER C 48  ? 1.4722 0.6876 0.5984 0.2091  0.0186  -0.0763 48  SER A OG  
3599 N N   . ARG C 49  ? 1.5884 0.8553 0.8035 0.1838  0.0452  -0.0837 49  ARG A N   
3600 C CA  . ARG C 49  ? 1.5779 0.8735 0.8354 0.1725  0.0503  -0.0916 49  ARG A CA  
3601 C C   . ARG C 49  ? 1.5336 0.8208 0.7905 0.1571  0.0691  -0.0915 49  ARG A C   
3602 O O   . ARG C 49  ? 1.5162 0.8138 0.7981 0.1545  0.0844  -0.0893 49  ARG A O   
3603 C CB  . ARG C 49  ? 1.6107 0.9225 0.8761 0.1698  0.0325  -0.1024 49  ARG A CB  
3604 C CG  . ARG C 49  ? 1.6319 0.9676 0.9362 0.1547  0.0389  -0.1121 49  ARG A CG  
3605 C CD  . ARG C 49  ? 1.7262 1.0987 1.0814 0.1585  0.0377  -0.1158 49  ARG A CD  
3606 N NE  . ARG C 49  ? 1.8492 1.2352 1.2060 0.1763  0.0204  -0.1141 49  ARG A NE  
3607 C CZ  . ARG C 49  ? 1.8684 1.2787 1.2581 0.1866  0.0215  -0.1116 49  ARG A CZ  
3608 N NH1 . ARG C 49  ? 1.7958 1.2184 1.2193 0.1810  0.0395  -0.1100 49  ARG A NH1 
3609 N NH2 . ARG C 49  ? 1.8891 1.3116 1.2765 0.2046  0.0046  -0.1101 49  ARG A NH2 
3610 N N   . SER C 50  ? 1.4666 0.7355 0.6944 0.1485  0.0685  -0.0935 50  SER A N   
3611 C CA  . SER C 50  ? 1.3673 0.6304 0.5936 0.1355  0.0855  -0.0938 50  SER A CA  
3612 C C   . SER C 50  ? 1.3536 0.5880 0.5371 0.1329  0.0920  -0.0873 50  SER A C   
3613 O O   . SER C 50  ? 1.3530 0.5791 0.5234 0.1234  0.1005  -0.0885 50  SER A O   
3614 C CB  . SER C 50  ? 1.3447 0.6159 0.5812 0.1252  0.0819  -0.1039 50  SER A CB  
3615 O OG  . SER C 50  ? 1.3431 0.6404 0.6142 0.1269  0.0705  -0.1118 50  SER A OG  
3616 N N   . LEU C 51  ? 1.3671 0.5856 0.5280 0.1412  0.0889  -0.0806 51  LEU A N   
3617 C CA  . LEU C 51  ? 1.3837 0.5744 0.5033 0.1370  0.0945  -0.0755 51  LEU A CA  
3618 C C   . LEU C 51  ? 1.3863 0.5641 0.4937 0.1421  0.1011  -0.0680 51  LEU A C   
3619 O O   . LEU C 51  ? 1.3875 0.5701 0.5064 0.1530  0.0955  -0.0661 51  LEU A O   
3620 C CB  . LEU C 51  ? 1.4175 0.5893 0.5039 0.1398  0.0799  -0.0773 51  LEU A CB  
3621 C CG  . LEU C 51  ? 1.4360 0.5787 0.4803 0.1335  0.0882  -0.0724 51  LEU A CG  
3622 C CD1 . LEU C 51  ? 1.4150 0.5657 0.4674 0.1208  0.1036  -0.0737 51  LEU A CD1 
3623 C CD2 . LEU C 51  ? 1.4730 0.5939 0.4810 0.1378  0.0748  -0.0735 51  LEU A CD2 
3624 N N   . ASP C 52  ? 1.3875 0.5503 0.4725 0.1335  0.1138  -0.0642 52  ASP A N   
3625 C CA  . ASP C 52  ? 1.3965 0.5419 0.4627 0.1346  0.1207  -0.0585 52  ASP A CA  
3626 C C   . ASP C 52  ? 1.4654 0.5822 0.4890 0.1273  0.1234  -0.0560 52  ASP A C   
3627 O O   . ASP C 52  ? 1.4386 0.5568 0.4559 0.1156  0.1352  -0.0559 52  ASP A O   
3628 C CB  . ASP C 52  ? 1.3681 0.5293 0.4552 0.1298  0.1357  -0.0575 52  ASP A CB  
3629 C CG  . ASP C 52  ? 1.3509 0.5300 0.4706 0.1400  0.1342  -0.0575 52  ASP A CG  
3630 O OD1 . ASP C 52  ? 1.3635 0.5407 0.4865 0.1510  0.1220  -0.0572 52  ASP A OD1 
3631 O OD2 . ASP C 52  ? 1.3263 0.5218 0.4674 0.1382  0.1456  -0.0574 52  ASP A OD2 
3632 N N   . HIS C 53  ? 1.6999 0.7919 0.6946 0.1354  0.1130  -0.0536 53  HIS A N   
3633 C CA  . HIS C 53  ? 1.7334 0.7945 0.6849 0.1310  0.1140  -0.0511 53  HIS A CA  
3634 C C   . HIS C 53  ? 1.7646 0.7989 0.6893 0.1272  0.1245  -0.0460 53  HIS A C   
3635 O O   . HIS C 53  ? 1.7659 0.7911 0.6892 0.1367  0.1220  -0.0435 53  HIS A O   
3636 C CB  . HIS C 53  ? 1.7649 0.8114 0.6962 0.1442  0.0969  -0.0514 53  HIS A CB  
3637 C CG  . HIS C 53  ? 1.8381 0.8511 0.7229 0.1413  0.0983  -0.0485 53  HIS A CG  
3638 N ND1 . HIS C 53  ? 1.9178 0.9101 0.7731 0.1544  0.0845  -0.0476 53  HIS A ND1 
3639 C CD2 . HIS C 53  ? 1.8762 0.8754 0.7409 0.1272  0.1121  -0.0462 53  HIS A CD2 
3640 C CE1 . HIS C 53  ? 1.8822 0.8449 0.6976 0.1487  0.0909  -0.0446 53  HIS A CE1 
3641 N NE2 . HIS C 53  ? 1.8979 0.8715 0.7307 0.1306  0.1067  -0.0420 53  HIS A NE2 
3642 N N   . ASP C 54  ? 1.6850 0.7101 0.5942 0.1126  0.1361  -0.0438 54  ASP A N   
3643 C CA  . ASP C 54  ? 1.6760 0.6770 0.5659 0.1057  0.1437  -0.0376 54  ASP A CA  
3644 C C   . ASP C 54  ? 1.7280 0.7081 0.5931 0.0993  0.1445  -0.0331 54  ASP A C   
3645 O O   . ASP C 54  ? 1.7171 0.7136 0.5931 0.0902  0.1474  -0.0337 54  ASP A O   
3646 C CB  . ASP C 54  ? 1.5617 0.5826 0.4759 0.0915  0.1568  -0.0377 54  ASP A CB  
3647 C CG  . ASP C 54  ? 1.6187 0.6475 0.5369 0.0727  0.1673  -0.0358 54  ASP A CG  
3648 O OD1 . ASP C 54  ? 1.6758 0.6769 0.5684 0.0660  0.1713  -0.0320 54  ASP A OD1 
3649 O OD2 . ASP C 54  ? 1.6108 0.6740 0.5581 0.0651  0.1728  -0.0383 54  ASP A OD2 
3650 N N   . GLN C 55  ? 1.6742 0.6164 0.5044 0.1064  0.1422  -0.0284 55  GLN A N   
3651 C CA  . GLN C 55  ? 1.6842 0.5990 0.4862 0.1023  0.1447  -0.0234 55  GLN A CA  
3652 C C   . GLN C 55  ? 1.7051 0.5829 0.4808 0.0977  0.1547  -0.0182 55  GLN A C   
3653 O O   . GLN C 55  ? 1.7323 0.5909 0.4942 0.1088  0.1523  -0.0167 55  GLN A O   
3654 C CB  . GLN C 55  ? 1.8065 0.7052 0.5837 0.1206  0.1297  -0.0230 55  GLN A CB  
3655 C CG  . GLN C 55  ? 1.7977 0.6824 0.5583 0.1428  0.1175  -0.0237 55  GLN A CG  
3656 C CD  . GLN C 55  ? 1.8812 0.7465 0.6101 0.1615  0.1024  -0.0228 55  GLN A CD  
3657 O OE1 . GLN C 55  ? 1.9110 0.7956 0.6469 0.1729  0.0876  -0.0296 55  GLN A OE1 
3658 N NE2 . GLN C 55  ? 1.8337 0.6598 0.5268 0.1652  0.1061  -0.0153 55  GLN A NE2 
3659 N N   . GLU C 56  ? 1.7145 0.5800 0.4811 0.0820  0.1662  -0.0156 56  GLU A N   
3660 C CA  . GLU C 56  ? 1.7302 0.5561 0.4687 0.0746  0.1779  -0.0118 56  GLU A CA  
3661 C C   . GLU C 56  ? 1.7824 0.5626 0.4781 0.0940  0.1712  -0.0062 56  GLU A C   
3662 O O   . GLU C 56  ? 1.7917 0.5706 0.4773 0.1059  0.1610  -0.0052 56  GLU A O   
3663 C CB  . GLU C 56  ? 1.7292 0.5591 0.4722 0.0519  0.1925  -0.0123 56  GLU A CB  
3664 C CG  . GLU C 56  ? 1.7716 0.5613 0.4864 0.0388  0.2076  -0.0101 56  GLU A CG  
3665 C CD  . GLU C 56  ? 1.7756 0.5867 0.5081 0.0130  0.2224  -0.0138 56  GLU A CD  
3666 O OE1 . GLU C 56  ? 1.7823 0.6411 0.5526 0.0057  0.2216  -0.0186 56  GLU A OE1 
3667 O OE2 . GLU C 56  ? 1.7923 0.5739 0.5012 0.0011  0.2351  -0.0122 56  GLU A OE2 
3668 N N   . LEU C 57  ? 1.8177 0.5609 0.4876 0.0991  0.1762  -0.0029 57  LEU A N   
3669 C CA  . LEU C 57  ? 1.8719 0.5692 0.4986 0.1203  0.1711  0.0028  57  LEU A CA  
3670 C C   . LEU C 57  ? 1.9219 0.5714 0.5138 0.1108  0.1864  0.0069  57  LEU A C   
3671 O O   . LEU C 57  ? 1.9604 0.5840 0.5241 0.1236  0.1827  0.0104  57  LEU A O   
3672 C CB  . LEU C 57  ? 1.8867 0.5685 0.5016 0.1384  0.1661  0.0045  57  LEU A CB  
3673 C CG  . LEU C 57  ? 1.8713 0.5771 0.4946 0.1637  0.1463  0.0028  57  LEU A CG  
3674 C CD1 . LEU C 57  ? 1.8715 0.5750 0.4955 0.1769  0.1441  0.0029  57  LEU A CD1 
3675 C CD2 . LEU C 57  ? 1.9130 0.5942 0.5021 0.1861  0.1352  0.0066  57  LEU A CD2 
3676 N N   . ASP C 58  ? 1.9282 0.5649 0.5202 0.0886  0.2036  0.0055  58  ASP A N   
3677 C CA  . ASP C 58  ? 1.9784 0.5681 0.5371 0.0766  0.2207  0.0076  58  ASP A CA  
3678 C C   . ASP C 58  ? 1.9633 0.5644 0.5398 0.0452  0.2375  0.0025  58  ASP A C   
3679 O O   . ASP C 58  ? 1.9189 0.5595 0.5292 0.0367  0.2350  -0.0019 58  ASP A O   
3680 C CB  . ASP C 58  ? 2.0402 0.5703 0.5526 0.0954  0.2231  0.0125  58  ASP A CB  
3681 C CG  . ASP C 58  ? 2.0983 0.5776 0.5704 0.0944  0.2355  0.0149  58  ASP A CG  
3682 O OD1 . ASP C 58  ? 2.0980 0.5788 0.5751 0.0700  0.2495  0.0122  58  ASP A OD1 
3683 O OD2 . ASP C 58  ? 2.1451 0.5848 0.5805 0.1194  0.2314  0.0189  58  ASP A OD2 
3684 N N   . SER C 59  ? 2.0026 0.5694 0.5554 0.0281  0.2549  0.0022  59  SER A N   
3685 C CA  . SER C 59  ? 1.9931 0.5718 0.5606 -0.0035 0.2714  -0.0040 59  SER A CA  
3686 C C   . SER C 59  ? 2.0581 0.5777 0.5840 -0.0170 0.2915  -0.0040 59  SER A C   
3687 O O   . SER C 59  ? 2.0896 0.5839 0.5929 -0.0127 0.2959  -0.0013 59  SER A O   
3688 C CB  . SER C 59  ? 1.9440 0.5782 0.5500 -0.0187 0.2713  -0.0082 59  SER A CB  
3689 O OG  . SER C 59  ? 1.9876 0.6179 0.5919 -0.0477 0.2906  -0.0132 59  SER A OG  
3690 N N   . ILE C 60  ? 2.0802 0.5767 0.5951 -0.0334 0.3041  -0.0077 60  ILE A N   
3691 C CA  . ILE C 60  ? 2.1473 0.5823 0.6202 -0.0485 0.3253  -0.0096 60  ILE A CA  
3692 C C   . ILE C 60  ? 2.1362 0.5930 0.6274 -0.0863 0.3416  -0.0188 60  ILE A C   
3693 O O   . ILE C 60  ? 2.1099 0.6161 0.6374 -0.0964 0.3361  -0.0234 60  ILE A O   
3694 C CB  . ILE C 60  ? 2.1959 0.5743 0.6315 -0.0342 0.3276  -0.0068 60  ILE A CB  
3695 C CG1 . ILE C 60  ? 2.2675 0.5867 0.6596 -0.0466 0.3495  -0.0098 60  ILE A CG1 
3696 C CG2 . ILE C 60  ? 2.1709 0.5698 0.6263 -0.0466 0.3275  -0.0100 60  ILE A CG2 
3697 C CD1 . ILE C 60  ? 2.3135 0.5961 0.6707 -0.0165 0.3460  -0.0040 60  ILE A CD1 
3698 N N   . LEU C 61  ? 2.1826 0.6048 0.6487 -0.1067 0.3617  -0.0227 61  LEU A N   
3699 C CA  . LEU C 61  ? 2.1837 0.6205 0.6609 -0.1445 0.3794  -0.0327 61  LEU A CA  
3700 C C   . LEU C 61  ? 2.2573 0.6227 0.6879 -0.1587 0.3993  -0.0371 61  LEU A C   
3701 O O   . LEU C 61  ? 2.3165 0.6226 0.7048 -0.1495 0.4091  -0.0354 61  LEU A O   
3702 C CB  . LEU C 61  ? 2.1740 0.6380 0.6654 -0.1606 0.3883  -0.0355 61  LEU A CB  
3703 C CG  . LEU C 61  ? 2.1276 0.6564 0.6613 -0.1893 0.3930  -0.0447 61  LEU A CG  
3704 C CD1 . LEU C 61  ? 2.1096 0.7072 0.6903 -0.1729 0.3710  -0.0427 61  LEU A CD1 
3705 C CD2 . LEU C 61  ? 2.1391 0.6785 0.6753 -0.2088 0.4084  -0.0477 61  LEU A CD2 
3706 N N   . VAL C 62  ? 2.2561 0.6261 0.6926 -0.1798 0.4056  -0.0437 62  VAL A N   
3707 C CA  . VAL C 62  ? 2.3213 0.6347 0.7191 -0.1956 0.4242  -0.0486 62  VAL A CA  
3708 C C   . VAL C 62  ? 2.3412 0.6564 0.7396 -0.2403 0.4470  -0.0625 62  VAL A C   
3709 O O   . VAL C 62  ? 2.3224 0.6943 0.7579 -0.2621 0.4454  -0.0695 62  VAL A O   
3710 C CB  . VAL C 62  ? 2.3125 0.6289 0.7130 -0.1861 0.4152  -0.0452 62  VAL A CB  
3711 C CG1 . VAL C 62  ? 2.2936 0.6114 0.6947 -0.1429 0.3936  -0.0330 62  VAL A CG1 
3712 C CG2 . VAL C 62  ? 2.2762 0.6424 0.7142 -0.2064 0.4107  -0.0516 62  VAL A CG2 
3713 N N   . GLY C 63  ? 2.4004 0.6756 0.7663 -0.2503 0.4662  -0.0668 63  GLY A N   
3714 C CA  . GLY C 63  ? 2.4409 0.7157 0.8045 -0.2917 0.4895  -0.0809 63  GLY A CA  
3715 C C   . GLY C 63  ? 2.5250 0.7460 0.8442 -0.3008 0.5120  -0.0861 63  GLY A C   
3716 O O   . GLY C 63  ? 2.5398 0.7221 0.8280 -0.2739 0.5124  -0.0782 63  GLY A O   
3717 N N   . PRO C 64  ? 2.5795 0.7970 0.8926 -0.3395 0.5319  -0.1004 64  PRO A N   
3718 C CA  . PRO C 64  ? 2.5504 0.8130 0.8965 -0.3754 0.5341  -0.1120 64  PRO A CA  
3719 C C   . PRO C 64  ? 2.5361 0.8120 0.8936 -0.3676 0.5199  -0.1075 64  PRO A C   
3720 O O   . PRO C 64  ? 2.5602 0.8057 0.8968 -0.3382 0.5116  -0.0971 64  PRO A O   
3721 C CB  . PRO C 64  ? 2.6051 0.8471 0.9288 -0.4165 0.5638  -0.1292 64  PRO A CB  
3722 C CG  . PRO C 64  ? 2.6778 0.8539 0.9485 -0.3967 0.5759  -0.1243 64  PRO A CG  
3723 C CD  . PRO C 64  ? 2.6556 0.8206 0.9228 -0.3460 0.5521  -0.1055 64  PRO A CD  
3724 N N   . VAL C 65  ? 2.5536 0.8746 0.9424 -0.3925 0.5172  -0.1151 65  VAL A N   
3725 C CA  . VAL C 65  ? 2.5468 0.8810 0.9447 -0.3848 0.5046  -0.1104 65  VAL A CA  
3726 C C   . VAL C 65  ? 2.5983 0.9188 0.9778 -0.4195 0.5235  -0.1217 65  VAL A C   
3727 O O   . VAL C 65  ? 2.5497 0.8964 0.9424 -0.4608 0.5377  -0.1386 65  VAL A O   
3728 C CB  . VAL C 65  ? 2.5034 0.9169 0.9543 -0.3790 0.4842  -0.1133 65  VAL A CB  
3729 C CG1 . VAL C 65  ? 2.4911 0.9669 0.9747 -0.4156 0.4933  -0.1316 65  VAL A CG1 
3730 C CG2 . VAL C 65  ? 2.4420 0.8711 0.9035 -0.3646 0.4691  -0.1116 65  VAL A CG2 
3731 N N   . PRO C 66  ? 2.6584 0.9397 1.0046 -0.4047 0.5258  -0.1137 66  PRO A N   
3732 C CA  . PRO C 66  ? 2.6509 0.9170 0.9732 -0.4367 0.5447  -0.1256 66  PRO A CA  
3733 C C   . PRO C 66  ? 2.6141 0.9022 0.9520 -0.4398 0.5332  -0.1277 66  PRO A C   
3734 O O   . PRO C 66  ? 2.5616 0.8704 0.9221 -0.4106 0.5107  -0.1174 66  PRO A O   
3735 C CB  . PRO C 66  ? 2.7135 0.9176 0.9820 -0.4158 0.5556  -0.1177 66  PRO A CB  
3736 C CG  . PRO C 66  ? 2.7309 0.9258 0.9974 -0.3730 0.5419  -0.1017 66  PRO A CG  
3737 C CD  . PRO C 66  ? 2.6931 0.9353 1.0123 -0.3611 0.5172  -0.0962 66  PRO A CD  
3738 N N   . VAL C 67  ? 2.5908 0.8744 0.9152 -0.4763 0.5496  -0.1421 67  VAL A N   
3739 C CA  . VAL C 67  ? 2.5253 0.8384 0.8758 -0.4738 0.5331  -0.1507 67  VAL A CA  
3740 C C   . VAL C 67  ? 2.5619 0.8181 0.8691 -0.4449 0.5325  -0.1354 67  VAL A C   
3741 O O   . VAL C 67  ? 2.6218 0.8201 0.8781 -0.4349 0.5482  -0.1249 67  VAL A O   
3742 C CB  . VAL C 67  ? 2.5375 0.8794 0.9032 -0.5215 0.5449  -0.1766 67  VAL A CB  
3743 C CG1 . VAL C 67  ? 2.4895 0.8828 0.8966 -0.5174 0.5224  -0.1886 67  VAL A CG1 
3744 C CG2 . VAL C 67  ? 2.5190 0.9040 0.9117 -0.5538 0.5540  -0.1910 67  VAL A CG2 
3745 N N   . GLY C 68  ? 2.5259 0.8063 0.8582 -0.4270 0.5119  -0.1366 68  GLY A N   
3746 C CA  . GLY C 68  ? 2.5595 0.7926 0.8558 -0.3988 0.5097  -0.1233 68  GLY A CA  
3747 C C   . GLY C 68  ? 2.5217 0.7543 0.8231 -0.3502 0.4895  -0.1030 68  GLY A C   
3748 O O   . GLY C 68  ? 2.4550 0.7363 0.8006 -0.3366 0.4712  -0.1021 68  GLY A O   
3749 N N   . VAL C 69  ? 2.5670 0.7456 0.8216 -0.3232 0.4932  -0.0876 69  VAL A N   
3750 C CA  . VAL C 69  ? 2.5394 0.7165 0.7963 -0.2753 0.4745  -0.0696 69  VAL A CA  
3751 C C   . VAL C 69  ? 2.5614 0.7193 0.8028 -0.2590 0.4782  -0.0633 69  VAL A C   
3752 O O   . VAL C 69  ? 2.6277 0.7393 0.8263 -0.2608 0.4951  -0.0635 69  VAL A O   
3753 C CB  . VAL C 69  ? 2.5649 0.7122 0.7961 -0.2486 0.4699  -0.0614 69  VAL A CB  
3754 C CG1 . VAL C 69  ? 2.6446 0.7407 0.8275 -0.2699 0.4932  -0.0677 69  VAL A CG1 
3755 C CG2 . VAL C 69  ? 2.5566 0.6963 0.7830 -0.1997 0.4550  -0.0462 69  VAL A CG2 
3756 N N   . ASN C 70  ? 2.5087 0.7002 0.7827 -0.2429 0.4631  -0.0581 70  ASN A N   
3757 C CA  . ASN C 70  ? 2.5222 0.6996 0.7845 -0.2221 0.4626  -0.0506 70  ASN A CA  
3758 C C   . ASN C 70  ? 2.4917 0.6774 0.7625 -0.1748 0.4400  -0.0366 70  ASN A C   
3759 O O   . ASN C 70  ? 2.4610 0.6845 0.7676 -0.1633 0.4218  -0.0343 70  ASN A O   
3760 C CB  . ASN C 70  ? 2.4900 0.6977 0.7814 -0.2415 0.4637  -0.0563 70  ASN A CB  
3761 C CG  . ASN C 70  ? 2.4872 0.7143 0.7928 -0.2890 0.4777  -0.0723 70  ASN A CG  
3762 O OD1 . ASN C 70  ? 2.4428 0.7054 0.7782 -0.2996 0.4689  -0.0772 70  ASN A OD1 
3763 N ND2 . ASN C 70  ? 2.5516 0.7561 0.8339 -0.3180 0.5006  -0.0814 70  ASN A ND2 
3764 N N   . LYS C 71  ? 2.5349 0.6857 0.7707 -0.1476 0.4423  -0.0286 71  LYS A N   
3765 C CA  . LYS C 71  ? 2.5118 0.6716 0.7530 -0.1033 0.4223  -0.0167 71  LYS A CA  
3766 C C   . LYS C 71  ? 2.5215 0.6758 0.7543 -0.0913 0.4223  -0.0134 71  LYS A C   
3767 O O   . LYS C 71  ? 2.5831 0.6976 0.7740 -0.0930 0.4394  -0.0175 71  LYS A O   
3768 C CB  . LYS C 71  ? 2.5549 0.6811 0.7603 -0.0768 0.4232  -0.0112 71  LYS A CB  
3769 N N   . PHE C 72  ? 2.4813 0.6720 0.7534 -0.0793 0.4037  -0.0086 72  PHE A N   
3770 C CA  . PHE C 72  ? 2.4639 0.6479 0.7391 -0.0650 0.3982  -0.0042 72  PHE A CA  
3771 C C   . PHE C 72  ? 2.4272 0.6291 0.7217 -0.0245 0.3733  0.0014  72  PHE A C   
3772 O O   . PHE C 72  ? 2.3775 0.6169 0.6990 -0.0177 0.3594  0.0035  72  PHE A O   
3773 C CB  . PHE C 72  ? 2.4328 0.6376 0.7385 -0.0924 0.4010  -0.0165 72  PHE A CB  
3774 C CG  . PHE C 72  ? 2.3606 0.6165 0.7076 -0.0822 0.3810  -0.0151 72  PHE A CG  
3775 C CD1 . PHE C 72  ? 2.3132 0.6060 0.6898 -0.0916 0.3736  -0.0169 72  PHE A CD1 
3776 C CD2 . PHE C 72  ? 2.3432 0.6087 0.6972 -0.0642 0.3708  -0.0129 72  PHE A CD2 
3777 C CE1 . PHE C 72  ? 2.2503 0.5873 0.6638 -0.0825 0.3567  -0.0161 72  PHE A CE1 
3778 C CE2 . PHE C 72  ? 2.2804 0.5911 0.6705 -0.0563 0.3537  -0.0110 72  PHE A CE2 
3779 C CZ  . PHE C 72  ? 2.2341 0.5802 0.6544 -0.0655 0.3471  -0.0128 72  PHE A CZ  
3780 N N   . VAL C 73  ? 2.4554 0.6351 0.7271 0.0044  0.3699  -0.0058 73  VAL A N   
3781 C CA  . VAL C 73  ? 2.4268 0.6267 0.7091 0.0416  0.3482  0.0023  73  VAL A CA  
3782 C C   . VAL C 73  ? 2.3871 0.6147 0.6937 0.0384  0.3391  0.0044  73  VAL A C   
3783 O O   . VAL C 73  ? 2.4149 0.6226 0.7035 0.0310  0.3491  0.0020  73  VAL A O   
3784 C CB  . VAL C 73  ? 2.4838 0.6489 0.7183 0.0753  0.3502  0.0043  73  VAL A CB  
3785 C CG1 . VAL C 73  ? 2.4620 0.6431 0.7053 0.1078  0.3299  0.0114  73  VAL A CG1 
3786 C CG2 . VAL C 73  ? 2.5050 0.6625 0.7184 0.0894  0.3520  0.0064  73  VAL A CG2 
3787 N N   . PHE C 74  ? 2.3248 0.5977 0.6692 0.0448  0.3213  0.0079  74  PHE A N   
3788 C CA  . PHE C 74  ? 2.2846 0.5870 0.6519 0.0457  0.3109  0.0081  74  PHE A CA  
3789 C C   . PHE C 74  ? 2.2865 0.5897 0.6447 0.0853  0.2930  0.0139  74  PHE A C   
3790 O O   . PHE C 74  ? 2.2601 0.5850 0.6324 0.1065  0.2777  0.0172  74  PHE A O   
3791 C CB  . PHE C 74  ? 2.2206 0.5699 0.6309 0.0284  0.3041  0.0058  74  PHE A CB  
3792 C CG  . PHE C 74  ? 2.1745 0.5577 0.6106 0.0369  0.2895  0.0068  74  PHE A CG  
3793 C CD1 . PHE C 74  ? 2.2073 0.5789 0.6302 0.0443  0.2885  0.0079  74  PHE A CD1 
3794 C CD2 . PHE C 74  ? 2.1126 0.5470 0.5897 0.0356  0.2774  0.0054  74  PHE A CD2 
3795 C CE1 . PHE C 74  ? 2.1437 0.5583 0.5953 0.0507  0.2743  0.0085  74  PHE A CE1 
3796 C CE2 . PHE C 74  ? 2.0613 0.5484 0.5726 0.0418  0.2634  0.0042  74  PHE A CE2 
3797 C CZ  . PHE C 74  ? 2.0772 0.5539 0.5752 0.0487  0.2617  0.0063  74  PHE A CZ  
3798 N N   . SER C 75  ? 2.3204 0.5996 0.6533 0.0953  0.2954  0.0148  75  SER A N   
3799 C CA  . SER C 75  ? 2.3214 0.6042 0.6460 0.1304  0.2778  0.0195  75  SER A CA  
3800 C C   . SER C 75  ? 2.2684 0.5895 0.6251 0.1269  0.2645  0.0194  75  SER A C   
3801 O O   . SER C 75  ? 2.2580 0.5835 0.6241 0.1029  0.2732  0.0164  75  SER A O   
3802 C CB  . SER C 75  ? 2.3859 0.6235 0.6654 0.1446  0.2865  0.0209  75  SER A CB  
3803 O OG  . SER C 75  ? 2.4372 0.6369 0.6865 0.1385  0.3047  0.0192  75  SER A OG  
3804 N N   . ALA C 76  ? 2.2366 0.5852 0.6095 0.1510  0.2440  0.0219  76  ALA A N   
3805 C CA  . ALA C 76  ? 2.1786 0.5755 0.5888 0.1470  0.2301  0.0212  76  ALA A CA  
3806 C C   . ALA C 76  ? 2.1878 0.6023 0.5957 0.1804  0.2085  0.0243  76  ALA A C   
3807 O O   . ALA C 76  ? 2.2059 0.5984 0.5893 0.2090  0.2019  0.0266  76  ALA A O   
3808 C CB  . ALA C 76  ? 2.1201 0.5645 0.5734 0.1325  0.2263  0.0188  76  ALA A CB  
3809 N N   . ASP C 77  ? 2.1377 0.5927 0.5702 0.1767  0.1978  0.0233  77  ASP A N   
3810 C CA  . ASP C 77  ? 2.1390 0.6088 0.5666 0.2022  0.1789  0.0250  77  ASP A CA  
3811 C C   . ASP C 77  ? 2.0944 0.6121 0.5517 0.2166  0.1592  0.0234  77  ASP A C   
3812 O O   . ASP C 77  ? 2.0435 0.5999 0.5385 0.2006  0.1589  0.0197  77  ASP A O   
3813 C CB  . ASP C 77  ? 2.1678 0.6558 0.6056 0.1908  0.1774  0.0238  77  ASP A CB  
3814 C CG  . ASP C 77  ? 2.1932 0.6308 0.5913 0.1903  0.1911  0.0262  77  ASP A CG  
3815 O OD1 . ASP C 77  ? 2.3016 0.7055 0.6625 0.2173  0.1863  0.0292  77  ASP A OD1 
3816 O OD2 . ASP C 77  ? 2.1787 0.6116 0.5823 0.1639  0.2070  0.0246  77  ASP A OD2 
3817 N N   . PRO C 78  ? 2.1258 0.6408 0.5648 0.2481  0.1431  0.0254  78  PRO A N   
3818 C CA  . PRO C 78  ? 2.0965 0.6536 0.5584 0.2661  0.1240  0.0233  78  PRO A CA  
3819 C C   . PRO C 78  ? 2.0437 0.6549 0.5428 0.2565  0.1109  0.0173  78  PRO A C   
3820 O O   . PRO C 78  ? 2.0205 0.6366 0.5263 0.2393  0.1153  0.0159  78  PRO A O   
3821 C CB  . PRO C 78  ? 2.1643 0.6991 0.5898 0.3017  0.1117  0.0271  78  PRO A CB  
3822 C CG  . PRO C 78  ? 2.1462 0.6662 0.5615 0.2876  0.1183  0.0270  78  PRO A CG  
3823 C CD  . PRO C 78  ? 2.1777 0.6531 0.5722 0.2763  0.1393  0.0293  78  PRO A CD  
3824 N N   . PRO C 79  ? 2.0125 0.6644 0.5359 0.2668  0.0958  0.0127  79  PRO A N   
3825 C CA  . PRO C 79  ? 1.9500 0.6492 0.5069 0.2566  0.0851  0.0049  79  PRO A CA  
3826 C C   . PRO C 79  ? 1.9895 0.6936 0.5294 0.2754  0.0665  0.0035  79  PRO A C   
3827 O O   . PRO C 79  ? 2.0690 0.7444 0.5732 0.2985  0.0604  0.0087  79  PRO A O   
3828 C CB  . PRO C 79  ? 1.9264 0.6632 0.5141 0.2607  0.0781  -0.0014 79  PRO A CB  
3829 C CG  . PRO C 79  ? 1.9557 0.6666 0.5308 0.2670  0.0884  0.0040  79  PRO A CG  
3830 C CD  . PRO C 79  ? 2.0600 0.7191 0.5878 0.2821  0.0920  0.0130  79  PRO A CD  
3831 N N   . SER C 80  ? 1.9486 0.6891 0.5141 0.2651  0.0578  -0.0042 80  SER A N   
3832 C CA  . SER C 80  ? 1.9544 0.7027 0.5064 0.2795  0.0395  -0.0075 80  SER A CA  
3833 C C   . SER C 80  ? 1.9241 0.7196 0.5045 0.2890  0.0191  -0.0180 80  SER A C   
3834 O O   . SER C 80  ? 1.8715 0.7053 0.5007 0.2700  0.0209  -0.0249 80  SER A O   
3835 C CB  . SER C 80  ? 1.9460 0.6937 0.5039 0.2588  0.0473  -0.0081 80  SER A CB  
3836 O OG  . SER C 80  ? 1.9308 0.6652 0.4992 0.2348  0.0702  -0.0038 80  SER A OG  
3837 N N   . ALA C 81  ? 1.9470 0.7514 0.5212 0.3163  -0.0002 -0.0179 81  ALA A N   
3838 C CA  . ALA C 81  ? 1.9086 0.7727 0.5372 0.3217  -0.0209 -0.0275 81  ALA A CA  
3839 C C   . ALA C 81  ? 1.8839 0.7763 0.5342 0.3065  -0.0294 -0.0380 81  ALA A C   
3840 O O   . ALA C 81  ? 1.8534 0.7950 0.5584 0.2979  -0.0381 -0.0473 81  ALA A O   
3841 C CB  . ALA C 81  ? 1.9439 0.8144 0.5575 0.3550  -0.0417 -0.0262 81  ALA A CB  
3842 N N   . GLU C 82  ? 1.9149 0.7743 0.5219 0.3024  -0.0254 -0.0365 82  GLU A N   
3843 C CA  . GLU C 82  ? 1.8983 0.7780 0.5185 0.2890  -0.0324 -0.0460 82  GLU A CA  
3844 C C   . GLU C 82  ? 1.8463 0.7454 0.5063 0.2601  -0.0165 -0.0497 82  GLU A C   
3845 O O   . GLU C 82  ? 1.8216 0.7482 0.5075 0.2485  -0.0226 -0.0590 82  GLU A O   
3846 C CB  . GLU C 82  ? 1.9450 0.7827 0.5102 0.2924  -0.0291 -0.0416 82  GLU A CB  
3847 C CG  . GLU C 82  ? 1.9972 0.8178 0.5251 0.3211  -0.0452 -0.0382 82  GLU A CG  
3848 C CD  . GLU C 82  ? 2.0270 0.8190 0.5305 0.3187  -0.0392 -0.0327 82  GLU A CD  
3849 O OE1 . GLU C 82  ? 2.0088 0.7885 0.5223 0.2951  -0.0183 -0.0282 82  GLU A OE1 
3850 O OE2 . GLU C 82  ? 2.1141 0.8970 0.5890 0.3408  -0.0547 -0.0328 82  GLU A OE2 
3851 N N   . LEU C 83  ? 1.8333 0.7163 0.4949 0.2485  0.0045  -0.0426 83  LEU A N   
3852 C CA  . LEU C 83  ? 1.7884 0.6877 0.4823 0.2231  0.0209  -0.0449 83  LEU A CA  
3853 C C   . LEU C 83  ? 1.7472 0.6803 0.4926 0.2186  0.0239  -0.0466 83  LEU A C   
3854 O O   . LEU C 83  ? 1.7258 0.6697 0.4952 0.2000  0.0394  -0.0470 83  LEU A O   
3855 C CB  . LEU C 83  ? 1.8005 0.6660 0.4712 0.2089  0.0431  -0.0354 83  LEU A CB  
3856 C CG  . LEU C 83  ? 1.8303 0.6743 0.4762 0.2082  0.0433  -0.0307 83  LEU A CG  
3857 C CD1 . LEU C 83  ? 1.8198 0.6522 0.4726 0.1863  0.0661  -0.0235 83  LEU A CD1 
3858 C CD2 . LEU C 83  ? 1.8219 0.6889 0.4759 0.2084  0.0289  -0.0404 83  LEU A CD2 
3859 N N   . ILE C 84  ? 1.7448 0.6954 0.5066 0.2365  0.0097  -0.0474 84  ILE A N   
3860 C CA  . ILE C 84  ? 1.7068 0.6874 0.5149 0.2352  0.0124  -0.0482 84  ILE A CA  
3861 C C   . ILE C 84  ? 1.6875 0.7144 0.5374 0.2441  -0.0078 -0.0572 84  ILE A C   
3862 O O   . ILE C 84  ? 1.7190 0.7471 0.5521 0.2617  -0.0261 -0.0592 84  ILE A O   
3863 C CB  . ILE C 84  ? 1.7307 0.6862 0.5181 0.2499  0.0175  -0.0392 84  ILE A CB  
3864 C CG1 . ILE C 84  ? 1.7422 0.6579 0.5004 0.2372  0.0403  -0.0318 84  ILE A CG1 
3865 C CG2 . ILE C 84  ? 1.7097 0.7016 0.5458 0.2547  0.0146  -0.0411 84  ILE A CG2 
3866 C CD1 . ILE C 84  ? 1.7736 0.6502 0.4854 0.2274  0.0507  -0.0285 84  ILE A CD1 
3867 N N   . PRO C 85  ? 1.6658 0.7318 0.5695 0.2331  -0.0050 -0.0629 85  PRO A N   
3868 C CA  . PRO C 85  ? 1.6629 0.7740 0.6098 0.2406  -0.0225 -0.0716 85  PRO A CA  
3869 C C   . PRO C 85  ? 1.6711 0.7883 0.6163 0.2654  -0.0347 -0.0677 85  PRO A C   
3870 O O   . PRO C 85  ? 1.6873 0.7781 0.6104 0.2750  -0.0257 -0.0580 85  PRO A O   
3871 C CB  . PRO C 85  ? 1.5738 0.7145 0.5721 0.2245  -0.0098 -0.0747 85  PRO A CB  
3872 C CG  . PRO C 85  ? 1.5652 0.6818 0.5456 0.2063  0.0091  -0.0715 85  PRO A CG  
3873 C CD  . PRO C 85  ? 1.6027 0.6745 0.5304 0.2135  0.0148  -0.0620 85  PRO A CD  
3874 N N   . ALA C 86  ? 1.6454 0.8001 0.6166 0.2756  -0.0551 -0.0760 86  ALA A N   
3875 C CA  . ALA C 86  ? 1.6666 0.8319 0.6358 0.3022  -0.0689 -0.0728 86  ALA A CA  
3876 C C   . ALA C 86  ? 1.6428 0.8207 0.6424 0.3068  -0.0582 -0.0670 86  ALA A C   
3877 O O   . ALA C 86  ? 1.7119 0.8803 0.6949 0.3295  -0.0618 -0.0595 86  ALA A O   
3878 C CB  . ALA C 86  ? 1.6678 0.8793 0.6655 0.3100  -0.0934 -0.0848 86  ALA A CB  
3879 N N   . SER C 87  ? 1.6135 0.8107 0.6548 0.2872  -0.0446 -0.0699 87  SER A N   
3880 C CA  . SER C 87  ? 1.5963 0.8071 0.6677 0.2921  -0.0346 -0.0649 87  SER A CA  
3881 C C   . SER C 87  ? 1.6664 0.8302 0.6975 0.2968  -0.0185 -0.0529 87  SER A C   
3882 O O   . SER C 87  ? 1.7147 0.8737 0.7422 0.3149  -0.0175 -0.0461 87  SER A O   
3883 C CB  . SER C 87  ? 1.5675 0.8085 0.6902 0.2708  -0.0233 -0.0711 87  SER A CB  
3884 O OG  . SER C 87  ? 1.5155 0.7930 0.6696 0.2632  -0.0366 -0.0832 87  SER A OG  
3885 N N   . GLU C 88  ? 1.6426 0.7713 0.6426 0.2804  -0.0053 -0.0505 88  GLU A N   
3886 C CA  . GLU C 88  ? 1.6794 0.7626 0.6403 0.2807  0.0107  -0.0409 88  GLU A CA  
3887 C C   . GLU C 88  ? 1.7569 0.8038 0.6670 0.3039  0.0041  -0.0333 88  GLU A C   
3888 O O   . GLU C 88  ? 1.7730 0.7814 0.6511 0.3081  0.0169  -0.0252 88  GLU A O   
3889 C CB  . GLU C 88  ? 1.6432 0.7032 0.5846 0.2572  0.0247  -0.0416 88  GLU A CB  
3890 C CG  . GLU C 88  ? 1.5811 0.6771 0.5661 0.2374  0.0272  -0.0501 88  GLU A CG  
3891 C CD  . GLU C 88  ? 1.5595 0.6361 0.5287 0.2160  0.0436  -0.0496 88  GLU A CD  
3892 O OE1 . GLU C 88  ? 1.6002 0.6395 0.5314 0.2138  0.0544  -0.0431 88  GLU A OE1 
3893 O OE2 . GLU C 88  ? 1.5318 0.6298 0.5250 0.2014  0.0462  -0.0557 88  GLU A OE2 
3894 N N   . LEU C 89  ? 1.7904 0.8483 0.6913 0.3196  -0.0153 -0.0363 89  LEU A N   
3895 C CA  . LEU C 89  ? 1.8465 0.8740 0.7003 0.3467  -0.0230 -0.0288 89  LEU A CA  
3896 C C   . LEU C 89  ? 1.8545 0.8935 0.7229 0.3685  -0.0243 -0.0235 89  LEU A C   
3897 O O   . LEU C 89  ? 1.9196 0.9173 0.7447 0.3856  -0.0179 -0.0138 89  LEU A O   
3898 C CB  . LEU C 89  ? 1.8342 0.8783 0.6789 0.3591  -0.0454 -0.0347 89  LEU A CB  
3899 C CG  . LEU C 89  ? 1.8311 0.8420 0.6277 0.3551  -0.0482 -0.0352 89  LEU A CG  
3900 C CD1 . LEU C 89  ? 1.9467 0.9047 0.6762 0.3787  -0.0471 -0.0246 89  LEU A CD1 
3901 C CD2 . LEU C 89  ? 1.7926 0.7838 0.5859 0.3250  -0.0295 -0.0360 89  LEU A CD2 
3902 N N   . VAL C 90  ? 1.8028 0.8958 0.7305 0.3684  -0.0311 -0.0294 90  VAL A N   
3903 C CA  . VAL C 90  ? 1.8361 0.9485 0.7823 0.3918  -0.0350 -0.0250 90  VAL A CA  
3904 C C   . VAL C 90  ? 1.8373 0.9583 0.8176 0.3805  -0.0178 -0.0232 90  VAL A C   
3905 O O   . VAL C 90  ? 1.8445 0.9917 0.8537 0.3960  -0.0196 -0.0211 90  VAL A O   
3906 C CB  . VAL C 90  ? 1.8068 0.9781 0.7940 0.4053  -0.0579 -0.0331 90  VAL A CB  
3907 C CG1 . VAL C 90  ? 1.8620 1.0256 0.8141 0.4155  -0.0759 -0.0363 90  VAL A CG1 
3908 C CG2 . VAL C 90  ? 1.6842 0.9051 0.7357 0.3807  -0.0576 -0.0443 90  VAL A CG2 
3909 N N   . SER C 91  ? 1.8382 0.9385 0.8149 0.3551  -0.0010 -0.0238 91  SER A N   
3910 C CA  . SER C 91  ? 1.7865 0.8998 0.7981 0.3428  0.0143  -0.0237 91  SER A CA  
3911 C C   . SER C 91  ? 1.7765 0.8380 0.7474 0.3334  0.0335  -0.0173 91  SER A C   
3912 O O   . SER C 91  ? 1.8265 0.8422 0.7441 0.3355  0.0361  -0.0129 91  SER A O   
3913 C CB  . SER C 91  ? 1.7564 0.9080 0.8156 0.3188  0.0156  -0.0333 91  SER A CB  
3914 O OG  . SER C 91  ? 1.7251 0.9206 0.8173 0.3232  -0.0024 -0.0412 91  SER A OG  
3915 N N   . VAL C 92  ? 1.6995 0.7686 0.6957 0.3226  0.0476  -0.0173 92  VAL A N   
3916 C CA  . VAL C 92  ? 1.6918 0.7185 0.6555 0.3104  0.0656  -0.0135 92  VAL A CA  
3917 C C   . VAL C 92  ? 1.6235 0.6411 0.5768 0.2846  0.0714  -0.0182 92  VAL A C   
3918 O O   . VAL C 92  ? 1.6334 0.6857 0.6209 0.2721  0.0673  -0.0248 92  VAL A O   
3919 C CB  . VAL C 92  ? 1.6514 0.6926 0.6461 0.3078  0.0777  -0.0130 92  VAL A CB  
3920 C CG1 . VAL C 92  ? 1.6726 0.6659 0.6270 0.3019  0.0940  -0.0088 92  VAL A CG1 
3921 C CG2 . VAL C 92  ? 1.6475 0.7188 0.6734 0.3316  0.0700  -0.0105 92  VAL A CG2 
3922 N N   . THR C 93  ? 1.6409 0.6112 0.5466 0.2763  0.0821  -0.0148 93  THR A N   
3923 C CA  . THR C 93  ? 1.6329 0.5937 0.5272 0.2517  0.0902  -0.0185 93  THR A CA  
3924 C C   . THR C 93  ? 1.6450 0.5724 0.5146 0.2385  0.1082  -0.0166 93  THR A C   
3925 O O   . THR C 93  ? 1.6549 0.5698 0.5205 0.2478  0.1138  -0.0133 93  THR A O   
3926 C CB  . THR C 93  ? 1.6674 0.6048 0.5240 0.2536  0.0827  -0.0175 93  THR A CB  
3927 O OG1 . THR C 93  ? 1.7187 0.6192 0.5333 0.2755  0.0791  -0.0104 93  THR A OG1 
3928 C CG2 . THR C 93  ? 1.6445 0.6225 0.5324 0.2565  0.0663  -0.0232 93  THR A CG2 
3929 N N   . VAL C 94  ? 1.6461 0.5596 0.4987 0.2168  0.1176  -0.0190 94  VAL A N   
3930 C CA  . VAL C 94  ? 1.6538 0.5431 0.4886 0.2002  0.1345  -0.0196 94  VAL A CA  
3931 C C   . VAL C 94  ? 1.6847 0.5403 0.4787 0.1848  0.1419  -0.0193 94  VAL A C   
3932 O O   . VAL C 94  ? 1.6804 0.5455 0.4744 0.1813  0.1359  -0.0205 94  VAL A O   
3933 C CB  . VAL C 94  ? 1.6023 0.5313 0.4810 0.1857  0.1411  -0.0252 94  VAL A CB  
3934 C CG1 . VAL C 94  ? 1.6065 0.5195 0.4684 0.1628  0.1569  -0.0283 94  VAL A CG1 
3935 C CG2 . VAL C 94  ? 1.5839 0.5321 0.4918 0.2006  0.1393  -0.0241 94  VAL A CG2 
3936 N N   . ILE C 95  ? 1.7172 0.5343 0.4793 0.1753  0.1546  -0.0167 95  ILE A N   
3937 C CA  . ILE C 95  ? 1.7389 0.5336 0.4804 0.1556  0.1628  -0.0133 95  ILE A CA  
3938 C C   . ILE C 95  ? 1.7276 0.5252 0.4813 0.1310  0.1767  -0.0153 95  ILE A C   
3939 O O   . ILE C 95  ? 1.7318 0.5217 0.4860 0.1333  0.1812  -0.0153 95  ILE A O   
3940 C CB  . ILE C 95  ? 1.8003 0.5416 0.4915 0.1687  0.1631  -0.0054 95  ILE A CB  
3941 C CG1 . ILE C 95  ? 1.8110 0.5548 0.4900 0.1893  0.1483  -0.0046 95  ILE A CG1 
3942 C CG2 . ILE C 95  ? 1.8250 0.5390 0.4968 0.1462  0.1756  -0.0029 95  ILE A CG2 
3943 C CD1 . ILE C 95  ? 1.8796 0.6279 0.5563 0.2191  0.1361  -0.0046 95  ILE A CD1 
3944 N N   . LEU C 96  ? 1.7138 0.5245 0.4777 0.1081  0.1830  -0.0177 96  LEU A N   
3945 C CA  . LEU C 96  ? 1.7005 0.5221 0.4787 0.0831  0.1952  -0.0219 96  LEU A CA  
3946 C C   . LEU C 96  ? 1.7446 0.5262 0.4895 0.0667  0.2064  -0.0194 96  LEU A C   
3947 O O   . LEU C 96  ? 1.7561 0.5416 0.4997 0.0566  0.2083  -0.0193 96  LEU A O   
3948 C CB  . LEU C 96  ? 1.6482 0.5222 0.4673 0.0705  0.1947  -0.0278 96  LEU A CB  
3949 C CG  . LEU C 96  ? 1.6025 0.5182 0.4595 0.0752  0.1918  -0.0326 96  LEU A CG  
3950 C CD1 . LEU C 96  ? 1.6093 0.5144 0.4618 0.0998  0.1841  -0.0303 96  LEU A CD1 
3951 C CD2 . LEU C 96  ? 1.5637 0.5193 0.4487 0.0738  0.1871  -0.0349 96  LEU A CD2 
3952 N N   . LEU C 97  ? 1.7845 0.5260 0.5015 0.0645  0.2146  -0.0172 97  LEU A N   
3953 C CA  . LEU C 97  ? 1.8254 0.5305 0.5144 0.0428  0.2291  -0.0171 97  LEU A CA  
3954 C C   . LEU C 97  ? 1.7949 0.5354 0.5127 0.0147  0.2376  -0.0263 97  LEU A C   
3955 O O   . LEU C 97  ? 1.7737 0.5350 0.5110 0.0109  0.2379  -0.0314 97  LEU A O   
3956 C CB  . LEU C 97  ? 1.8815 0.5299 0.5292 0.0489  0.2364  -0.0119 97  LEU A CB  
3957 C CG  . LEU C 97  ? 1.9352 0.5350 0.5465 0.0272  0.2537  -0.0113 97  LEU A CG  
3958 C CD1 . LEU C 97  ? 1.9975 0.5344 0.5599 0.0438  0.2580  -0.0021 97  LEU A CD1 
3959 C CD2 . LEU C 97  ? 1.9239 0.5389 0.5506 0.0025  0.2631  -0.0199 97  LEU A CD2 
3960 N N   . SER C 98  ? 1.7947 0.5425 0.5142 -0.0036 0.2443  -0.0287 98  SER A N   
3961 C CA  . SER C 98  ? 1.7608 0.5522 0.5110 -0.0273 0.2504  -0.0377 98  SER A CA  
3962 C C   . SER C 98  ? 1.8024 0.5637 0.5270 -0.0531 0.2667  -0.0403 98  SER A C   
3963 O O   . SER C 98  ? 1.8404 0.5631 0.5347 -0.0511 0.2710  -0.0344 98  SER A O   
3964 C CB  . SER C 98  ? 1.7104 0.5526 0.4954 -0.0215 0.2414  -0.0381 98  SER A CB  
3965 O OG  . SER C 98  ? 1.7164 0.5619 0.4982 -0.0357 0.2481  -0.0384 98  SER A OG  
3966 N N   . CYS C 99  ? 1.7989 0.5763 0.5335 -0.0771 0.2763  -0.0496 99  CYS A N   
3967 C CA  . CYS C 99  ? 1.8359 0.5914 0.5498 -0.1046 0.2930  -0.0539 99  CYS A CA  
3968 C C   . CYS C 99  ? 1.7952 0.6105 0.5453 -0.1246 0.2962  -0.0640 99  CYS A C   
3969 O O   . CYS C 99  ? 1.7541 0.6146 0.5360 -0.1233 0.2897  -0.0701 99  CYS A O   
3970 C CB  . CYS C 99  ? 1.8913 0.5946 0.5695 -0.1186 0.3057  -0.0563 99  CYS A CB  
3971 S SG  . CYS C 99  ? 1.9534 0.6113 0.5945 -0.1509 0.3290  -0.0598 99  CYS A SG  
3972 N N   . SER C 100 ? 1.8067 0.6235 0.5519 -0.1402 0.3058  -0.0649 100 SER A N   
3973 C CA  . SER C 100 ? 1.8227 0.6992 0.6019 -0.1547 0.3083  -0.0722 100 SER A CA  
3974 C C   . SER C 100 ? 1.8701 0.7308 0.6305 -0.1867 0.3277  -0.0792 100 SER A C   
3975 O O   . SER C 100 ? 1.9236 0.7255 0.6451 -0.1933 0.3385  -0.0753 100 SER A O   
3976 C CB  . SER C 100 ? 1.7714 0.6777 0.5713 -0.1369 0.2986  -0.0649 100 SER A CB  
3977 O OG  . SER C 100 ? 1.7095 0.6148 0.5164 -0.1079 0.2825  -0.0576 100 SER A OG  
3978 N N   . TYR C 101 ? 1.8367 0.7505 0.6242 -0.2064 0.3330  -0.0898 101 TYR A N   
3979 C CA  . TYR C 101 ? 1.8793 0.7885 0.6542 -0.2404 0.3523  -0.0992 101 TYR A CA  
3980 C C   . TYR C 101 ? 1.8898 0.8564 0.6940 -0.2471 0.3551  -0.1011 101 TYR A C   
3981 O O   . TYR C 101 ? 1.8287 0.8586 0.6690 -0.2459 0.3487  -0.1072 101 TYR A O   
3982 C CB  . TYR C 101 ? 1.9226 0.8402 0.6981 -0.2626 0.3580  -0.1134 101 TYR A CB  
3983 C CG  . TYR C 101 ? 2.0363 0.9398 0.7929 -0.3007 0.3797  -0.1242 101 TYR A CG  
3984 C CD1 . TYR C 101 ? 2.0593 0.8878 0.7697 -0.3149 0.3947  -0.1229 101 TYR A CD1 
3985 C CD2 . TYR C 101 ? 2.0451 1.0100 0.8290 -0.3226 0.3866  -0.1357 101 TYR A CD2 
3986 C CE1 . TYR C 101 ? 2.1171 0.9303 0.8095 -0.3520 0.4167  -0.1335 101 TYR A CE1 
3987 C CE2 . TYR C 101 ? 2.0974 1.0524 0.8653 -0.3599 0.4078  -0.1467 101 TYR A CE2 
3988 C CZ  . TYR C 101 ? 2.1605 1.0386 0.8829 -0.3755 0.4232  -0.1459 101 TYR A CZ  
3989 O OH  . TYR C 101 ? 2.2744 1.1409 0.9807 -0.4147 0.4462  -0.1575 101 TYR A OH  
3990 N N   . ASP C 102 ? 1.9402 0.8841 0.7278 -0.2530 0.3654  -0.0956 102 ASP A N   
3991 C CA  . ASP C 102 ? 1.8837 0.8759 0.6956 -0.2563 0.3688  -0.0949 102 ASP A CA  
3992 C C   . ASP C 102 ? 1.8709 0.9206 0.7221 -0.2307 0.3510  -0.0910 102 ASP A C   
3993 O O   . ASP C 102 ? 1.8084 0.9206 0.6921 -0.2356 0.3502  -0.0977 102 ASP A O   
3994 C CB  . ASP C 102 ? 1.9139 0.9401 0.7350 -0.2907 0.3858  -0.1081 102 ASP A CB  
3995 C CG  . ASP C 102 ? 2.0099 1.0424 0.8294 -0.3022 0.3996  -0.1052 102 ASP A CG  
3996 O OD1 . ASP C 102 ? 2.0632 1.0382 0.8508 -0.3006 0.4067  -0.0974 102 ASP A OD1 
3997 O OD2 . ASP C 102 ? 2.0516 1.1478 0.9020 -0.3106 0.4030  -0.1101 102 ASP A OD2 
3998 N N   . GLY C 103 ? 1.8513 0.8774 0.6974 -0.2028 0.3372  -0.0801 103 GLY A N   
3999 C CA  . GLY C 103 ? 1.7938 0.8625 0.6717 -0.1779 0.3213  -0.0755 103 GLY A CA  
4000 C C   . GLY C 103 ? 1.7670 0.8554 0.6630 -0.1665 0.3095  -0.0791 103 GLY A C   
4001 O O   . GLY C 103 ? 1.7414 0.8548 0.6596 -0.1440 0.2964  -0.0745 103 GLY A O   
4002 N N   . ARG C 104 ? 1.7796 0.8558 0.6658 -0.1813 0.3143  -0.0874 104 ARG A N   
4003 C CA  . ARG C 104 ? 1.7295 0.8346 0.6370 -0.1730 0.3050  -0.0928 104 ARG A CA  
4004 C C   . ARG C 104 ? 1.7298 0.7832 0.6140 -0.1619 0.2990  -0.0892 104 ARG A C   
4005 O O   . ARG C 104 ? 1.7829 0.7909 0.6365 -0.1772 0.3081  -0.0922 104 ARG A O   
4006 C CB  . ARG C 104 ? 1.7476 0.8906 0.6669 -0.1973 0.3138  -0.1069 104 ARG A CB  
4007 C CG  . ARG C 104 ? 1.7449 0.9376 0.6837 -0.2092 0.3220  -0.1099 104 ARG A CG  
4008 C CD  . ARG C 104 ? 1.8120 1.0427 0.7592 -0.2369 0.3325  -0.1253 104 ARG A CD  
4009 N NE  . ARG C 104 ? 1.8436 1.0295 0.7587 -0.2664 0.3467  -0.1331 104 ARG A NE  
4010 C CZ  . ARG C 104 ? 1.8559 1.0230 0.7536 -0.2882 0.3626  -0.1337 104 ARG A CZ  
4011 N NH1 . ARG C 104 ? 1.8729 1.0566 0.7799 -0.2814 0.3651  -0.1254 104 ARG A NH1 
4012 N NH2 . ARG C 104 ? 1.8878 1.0168 0.7575 -0.3176 0.3771  -0.1429 104 ARG A NH2 
4013 N N   . GLU C 105 ? 1.7048 0.7644 0.6027 -0.1351 0.2847  -0.0824 105 GLU A N   
4014 C CA  . GLU C 105 ? 1.6875 0.7084 0.5693 -0.1206 0.2776  -0.0787 105 GLU A CA  
4015 C C   . GLU C 105 ? 1.6805 0.7175 0.5718 -0.1276 0.2779  -0.0881 105 GLU A C   
4016 O O   . GLU C 105 ? 1.6229 0.7127 0.5466 -0.1238 0.2733  -0.0931 105 GLU A O   
4017 C CB  . GLU C 105 ? 1.6103 0.6405 0.5074 -0.0916 0.2632  -0.0701 105 GLU A CB  
4018 C CG  . GLU C 105 ? 1.6060 0.5969 0.4856 -0.0732 0.2556  -0.0646 105 GLU A CG  
4019 C CD  . GLU C 105 ? 1.5690 0.5806 0.4702 -0.0472 0.2420  -0.0591 105 GLU A CD  
4020 O OE1 . GLU C 105 ? 1.5673 0.6237 0.4983 -0.0440 0.2390  -0.0601 105 GLU A OE1 
4021 O OE2 . GLU C 105 ? 1.5814 0.5649 0.4696 -0.0299 0.2351  -0.0542 105 GLU A OE2 
4022 N N   . PHE C 106 ? 1.6585 0.6494 0.5202 -0.1373 0.2838  -0.0906 106 PHE A N   
4023 C CA  . PHE C 106 ? 1.6578 0.6594 0.5251 -0.1446 0.2840  -0.1002 106 PHE A CA  
4024 C C   . PHE C 106 ? 1.6686 0.6364 0.5238 -0.1251 0.2767  -0.0949 106 PHE A C   
4025 O O   . PHE C 106 ? 1.6607 0.6422 0.5251 -0.1255 0.2744  -0.1016 106 PHE A O   
4026 C CB  . PHE C 106 ? 1.7442 0.7261 0.5891 -0.1773 0.2990  -0.1111 106 PHE A CB  
4027 C CG  . PHE C 106 ? 1.8151 0.7273 0.6161 -0.1858 0.3095  -0.1054 106 PHE A CG  
4028 C CD1 . PHE C 106 ? 1.8453 0.7432 0.6340 -0.1920 0.3168  -0.1000 106 PHE A CD1 
4029 C CD2 . PHE C 106 ? 1.8048 0.6641 0.5753 -0.1862 0.3128  -0.1046 106 PHE A CD2 
4030 C CE1 . PHE C 106 ? 1.8789 0.7095 0.6244 -0.1982 0.3276  -0.0942 106 PHE A CE1 
4031 C CE2 . PHE C 106 ? 1.8640 0.6562 0.5909 -0.1922 0.3238  -0.0983 106 PHE A CE2 
4032 C CZ  . PHE C 106 ? 1.8974 0.6745 0.6113 -0.1980 0.3314  -0.0932 106 PHE A CZ  
4033 N N   . VAL C 107 ? 1.6882 0.6135 0.5221 -0.1076 0.2731  -0.0833 107 VAL A N   
4034 C CA  . VAL C 107 ? 1.6998 0.5949 0.5217 -0.0871 0.2666  -0.0775 107 VAL A CA  
4035 C C   . VAL C 107 ? 1.6952 0.5752 0.5121 -0.0620 0.2577  -0.0655 107 VAL A C   
4036 O O   . VAL C 107 ? 1.7112 0.5744 0.5136 -0.0643 0.2604  -0.0608 107 VAL A O   
4037 C CB  . VAL C 107 ? 1.7600 0.5970 0.5416 -0.0994 0.2769  -0.0787 107 VAL A CB  
4038 C CG1 . VAL C 107 ? 1.7836 0.5768 0.5422 -0.0737 0.2713  -0.0679 107 VAL A CG1 
4039 C CG2 . VAL C 107 ? 1.7597 0.6150 0.5499 -0.1177 0.2813  -0.0914 107 VAL A CG2 
4040 N N   . ARG C 108 ? 1.6750 0.5615 0.5034 -0.0379 0.2474  -0.0612 108 ARG A N   
4041 C CA  . ARG C 108 ? 1.6665 0.5471 0.4944 -0.0135 0.2375  -0.0520 108 ARG A CA  
4042 C C   . ARG C 108 ? 1.6797 0.5363 0.4966 0.0080  0.2322  -0.0472 108 ARG A C   
4043 O O   . ARG C 108 ? 1.6561 0.5356 0.4936 0.0130  0.2297  -0.0509 108 ARG A O   
4044 C CB  . ARG C 108 ? 1.6104 0.5465 0.4785 -0.0062 0.2297  -0.0534 108 ARG A CB  
4045 C CG  . ARG C 108 ? 1.5978 0.5341 0.4698 0.0186  0.2186  -0.0463 108 ARG A CG  
4046 C CD  . ARG C 108 ? 1.5569 0.5463 0.4700 0.0258  0.2130  -0.0490 108 ARG A CD  
4047 N NE  . ARG C 108 ? 1.5769 0.6036 0.5112 0.0072  0.2189  -0.0549 108 ARG A NE  
4048 C CZ  . ARG C 108 ? 1.5616 0.6234 0.5190 0.0081  0.2168  -0.0549 108 ARG A CZ  
4049 N NH1 . ARG C 108 ? 1.5661 0.6315 0.5301 0.0248  0.2088  -0.0505 108 ARG A NH1 
4050 N NH2 . ARG C 108 ? 1.5299 0.6238 0.5029 -0.0081 0.2231  -0.0599 108 ARG A NH2 
4051 N N   . VAL C 109 ? 1.7192 0.5302 0.5026 0.0217  0.2308  -0.0389 109 VAL A N   
4052 C CA  . VAL C 109 ? 1.7380 0.5236 0.5067 0.0435  0.2269  -0.0336 109 VAL A CA  
4053 C C   . VAL C 109 ? 1.7264 0.5178 0.4986 0.0702  0.2148  -0.0274 109 VAL A C   
4054 O O   . VAL C 109 ? 1.7501 0.5190 0.5000 0.0753  0.2128  -0.0224 109 VAL A O   
4055 C CB  . VAL C 109 ? 1.8022 0.5261 0.5237 0.0390  0.2368  -0.0292 109 VAL A CB  
4056 C CG1 . VAL C 109 ? 1.8195 0.5223 0.5281 0.0613  0.2337  -0.0239 109 VAL A CG1 
4057 C CG2 . VAL C 109 ? 1.8173 0.5359 0.5341 0.0072  0.2499  -0.0377 109 VAL A CG2 
4058 N N   . GLY C 110 ? 1.6916 0.5136 0.4914 0.0869  0.2071  -0.0285 110 GLY A N   
4059 C CA  . GLY C 110 ? 1.6776 0.5114 0.4855 0.1109  0.1956  -0.0253 110 GLY A CA  
4060 C C   . GLY C 110 ? 1.7079 0.5120 0.4939 0.1369  0.1918  -0.0194 110 GLY A C   
4061 O O   . GLY C 110 ? 1.7142 0.5108 0.4996 0.1399  0.1959  -0.0190 110 GLY A O   
4062 N N   . TYR C 111 ? 1.7272 0.5164 0.4952 0.1561  0.1835  -0.0151 111 TYR A N   
4063 C CA  . TYR C 111 ? 1.7714 0.5328 0.5158 0.1837  0.1793  -0.0093 111 TYR A CA  
4064 C C   . TYR C 111 ? 1.7800 0.5665 0.5422 0.2079  0.1660  -0.0115 111 TYR A C   
4065 O O   . TYR C 111 ? 1.7335 0.5317 0.4978 0.2074  0.1586  -0.0129 111 TYR A O   
4066 C CB  . TYR C 111 ? 1.8218 0.5284 0.5141 0.1880  0.1830  -0.0015 111 TYR A CB  
4067 C CG  . TYR C 111 ? 1.8528 0.5254 0.5216 0.1660  0.1976  0.0005  111 TYR A CG  
4068 C CD1 . TYR C 111 ? 1.8785 0.5269 0.5309 0.1713  0.2042  0.0041  111 TYR A CD1 
4069 C CD2 . TYR C 111 ? 1.8581 0.5234 0.5212 0.1393  0.2054  -0.0019 111 TYR A CD2 
4070 C CE1 . TYR C 111 ? 1.9113 0.5266 0.5397 0.1493  0.2181  0.0045  111 TYR A CE1 
4071 C CE2 . TYR C 111 ? 1.8900 0.5235 0.5314 0.1174  0.2196  -0.0019 111 TYR A CE2 
4072 C CZ  . TYR C 111 ? 1.9170 0.5251 0.5407 0.1219  0.2258  0.0009  111 TYR A CZ  
4073 O OH  . TYR C 111 ? 1.9512 0.5276 0.5521 0.0981  0.2403  -0.0004 111 TYR A OH  
4074 N N   . TYR C 112 ? 1.9083 0.7065 0.6878 0.2283  0.1623  -0.0103 112 TYR A N   
4075 C CA  . TYR C 112 ? 1.9219 0.7507 0.7279 0.2515  0.1468  -0.0066 112 TYR A CA  
4076 C C   . TYR C 112 ? 1.9995 0.7939 0.7638 0.2683  0.1400  -0.0004 112 TYR A C   
4077 O O   . TYR C 112 ? 2.0491 0.7890 0.7618 0.2712  0.1489  0.0038  112 TYR A O   
4078 C CB  . TYR C 112 ? 1.8845 0.7299 0.7152 0.2708  0.1456  -0.0040 112 TYR A CB  
4079 C CG  . TYR C 112 ? 1.8752 0.7757 0.7639 0.2641  0.1441  -0.0089 112 TYR A CG  
4080 C CD1 . TYR C 112 ? 1.8949 0.8378 0.8260 0.2807  0.1331  -0.0078 112 TYR A CD1 
4081 C CD2 . TYR C 112 ? 1.8772 0.7878 0.7780 0.2415  0.1544  -0.0150 112 TYR A CD2 
4082 C CE1 . TYR C 112 ? 1.8206 0.8102 0.8030 0.2741  0.1341  -0.0121 112 TYR A CE1 
4083 C CE2 . TYR C 112 ? 1.8006 0.7583 0.7507 0.2375  0.1545  -0.0187 112 TYR A CE2 
4084 C CZ  . TYR C 112 ? 1.7198 0.7146 0.7097 0.2534  0.1453  -0.0170 112 TYR A CZ  
4085 O OH  . TYR C 112 ? 1.6277 0.6649 0.6642 0.2491  0.1477  -0.0204 112 TYR A OH  
4086 N N   . VAL C 113 ? 1.8379 0.6635 0.6230 0.2796  0.1244  -0.0001 113 VAL A N   
4087 C CA  . VAL C 113 ? 1.8774 0.6792 0.6275 0.2998  0.1148  0.0055  113 VAL A CA  
4088 C C   . VAL C 113 ? 1.8813 0.7312 0.6708 0.3212  0.0961  0.0054  113 VAL A C   
4089 O O   . VAL C 113 ? 1.8537 0.7519 0.6896 0.3113  0.0885  -0.0009 113 VAL A O   
4090 C CB  . VAL C 113 ? 1.8875 0.6696 0.6090 0.2848  0.1153  0.0039  113 VAL A CB  
4091 C CG1 . VAL C 113 ? 1.9652 0.7249 0.6502 0.3089  0.1041  0.0098  113 VAL A CG1 
4092 C CG2 . VAL C 113 ? 1.8643 0.5997 0.5473 0.2626  0.1347  0.0036  113 VAL A CG2 
4093 N N   . ASN C 114 ? 1.9050 0.7419 0.6753 0.3505  0.0892  0.0121  114 ASN A N   
4094 C CA  . ASN C 114 ? 1.9412 0.8244 0.7455 0.3726  0.0704  0.0118  114 ASN A CA  
4095 C C   . ASN C 114 ? 1.9978 0.8672 0.7680 0.3876  0.0570  0.0140  114 ASN A C   
4096 O O   . ASN C 114 ? 2.0125 0.8261 0.7235 0.3921  0.0640  0.0196  114 ASN A O   
4097 C CB  . ASN C 114 ? 1.9714 0.8592 0.7839 0.3983  0.0707  0.0177  114 ASN A CB  
4098 C CG  . ASN C 114 ? 2.0390 0.9813 0.8924 0.4206  0.0517  0.0166  114 ASN A CG  
4099 O OD1 . ASN C 114 ? 1.9890 0.9785 0.8844 0.4100  0.0402  0.0089  114 ASN A OD1 
4100 N ND2 . ASN C 114 ? 2.0550 0.9925 0.8980 0.4511  0.0490  0.0240  114 ASN A ND2 
4101 N N   . ASN C 115 ? 2.0104 0.9301 0.8171 0.3946  0.0382  0.0089  115 ASN A N   
4102 C CA  . ASN C 115 ? 2.0882 1.0017 0.8657 0.4121  0.0226  0.0100  115 ASN A CA  
4103 C C   . ASN C 115 ? 2.0930 1.0642 0.9130 0.4342  0.0020  0.0070  115 ASN A C   
4104 O O   . ASN C 115 ? 2.0110 1.0349 0.8915 0.4237  -0.0017 0.0000  115 ASN A O   
4105 C CB  . ASN C 115 ? 2.0469 0.9593 0.8178 0.3897  0.0198  0.0037  115 ASN A CB  
4106 C CG  . ASN C 115 ? 2.0351 0.9082 0.7828 0.3615  0.0406  0.0041  115 ASN A CG  
4107 O OD1 . ASN C 115 ? 2.0254 0.8446 0.7171 0.3607  0.0498  0.0092  115 ASN A OD1 
4108 N ND2 . ASN C 115 ? 1.9701 0.8722 0.7618 0.3379  0.0482  -0.0018 115 ASN A ND2 
4109 N N   . GLU C 116 ? 2.1798 1.1413 0.9678 0.4651  -0.0105 0.0121  116 GLU A N   
4110 C CA  . GLU C 116 ? 2.1894 1.2078 1.0150 0.4886  -0.0314 0.0091  116 GLU A CA  
4111 C C   . GLU C 116 ? 2.2750 1.2747 1.0517 0.5204  -0.0458 0.0141  116 GLU A C   
4112 O O   . GLU C 116 ? 2.2821 1.2202 0.9940 0.5252  -0.0374 0.0211  116 GLU A O   
4113 C CB  . GLU C 116 ? 2.2108 1.2517 1.0689 0.5029  -0.0262 0.0132  116 GLU A CB  
4114 C CG  . GLU C 116 ? 2.2576 1.2390 1.0634 0.5209  -0.0101 0.0257  116 GLU A CG  
4115 C CD  . GLU C 116 ? 2.3060 1.3092 1.1480 0.5288  -0.0019 0.0287  116 GLU A CD  
4116 O OE1 . GLU C 116 ? 2.3621 1.4290 1.2609 0.5368  -0.0145 0.0241  116 GLU A OE1 
4117 O OE2 . GLU C 116 ? 2.3088 1.2659 1.1229 0.5264  0.0172  0.0352  116 GLU A OE2 
4118 N N   . TYR C 117 ? 2.3320 1.3866 1.1408 0.5429  -0.0669 0.0104  117 TYR A N   
4119 C CA  . TYR C 117 ? 2.3992 1.4494 1.1693 0.5776  -0.0841 0.0142  117 TYR A CA  
4120 C C   . TYR C 117 ? 2.4772 1.4921 1.2074 0.6123  -0.0760 0.0281  117 TYR A C   
4121 O O   . TYR C 117 ? 2.4621 1.4948 1.2231 0.6180  -0.0685 0.0313  117 TYR A O   
4122 C CB  . TYR C 117 ? 2.4407 1.5710 1.2666 0.5871  -0.1106 0.0033  117 TYR A CB  
4123 C CG  . TYR C 117 ? 2.4115 1.5726 1.2637 0.5604  -0.1232 -0.0109 117 TYR A CG  
4124 C CD1 . TYR C 117 ? 2.3674 1.4874 1.1688 0.5543  -0.1249 -0.0113 117 TYR A CD1 
4125 C CD2 . TYR C 117 ? 2.4037 1.6321 1.3303 0.5408  -0.1315 -0.0236 117 TYR A CD2 
4126 C CE1 . TYR C 117 ? 2.3132 1.4595 1.1367 0.5308  -0.1358 -0.0242 117 TYR A CE1 
4127 C CE2 . TYR C 117 ? 2.3535 1.6062 1.3018 0.5161  -0.1416 -0.0368 117 TYR A CE2 
4128 C CZ  . TYR C 117 ? 2.3228 1.5345 1.2191 0.5116  -0.1441 -0.0371 117 TYR A CZ  
4129 O OH  . TYR C 117 ? 2.2570 1.4905 1.1723 0.4880  -0.1537 -0.0502 117 TYR A OH  
4130 N N   . ASP C 118 ? 2.5547 1.5174 1.2136 0.6372  -0.0767 0.0368  118 ASP A N   
4131 C CA  . ASP C 118 ? 2.5869 1.5139 1.2016 0.6750  -0.0700 0.0504  118 ASP A CA  
4132 C C   . ASP C 118 ? 2.5952 1.5862 1.2419 0.7112  -0.0923 0.0498  118 ASP A C   
4133 O O   . ASP C 118 ? 2.5938 1.5874 1.2436 0.7353  -0.0867 0.0578  118 ASP A O   
4134 C CB  . ASP C 118 ? 2.6488 1.4959 1.1735 0.6913  -0.0618 0.0604  118 ASP A CB  
4135 C CG  . ASP C 118 ? 2.6515 1.5106 1.1579 0.6971  -0.0818 0.0548  118 ASP A CG  
4136 O OD1 . ASP C 118 ? 2.6250 1.5570 1.1816 0.7018  -0.1065 0.0446  118 ASP A OD1 
4137 O OD2 . ASP C 118 ? 2.6374 1.4315 1.0773 0.6973  -0.0723 0.0604  118 ASP A OD2 
4138 N N   . GLU C 119 ? 2.5989 1.6425 1.2692 0.7153  -0.1176 0.0398  119 GLU A N   
4139 C CA  . GLU C 119 ? 2.5953 1.7072 1.2990 0.7482  -0.1413 0.0371  119 GLU A CA  
4140 C C   . GLU C 119 ? 2.5643 1.7403 1.3479 0.7385  -0.1405 0.0320  119 GLU A C   
4141 O O   . GLU C 119 ? 2.5753 1.7667 1.4048 0.7003  -0.1313 0.0243  119 GLU A O   
4142 C CB  . GLU C 119 ? 2.5968 1.7543 1.3147 0.7464  -0.1685 0.0241  119 GLU A CB  
4143 C CG  . GLU C 119 ? 2.6011 1.8060 1.3178 0.7904  -0.1944 0.0239  119 GLU A CG  
4144 C CD  . GLU C 119 ? 2.6305 1.7861 1.2831 0.8357  -0.1857 0.0417  119 GLU A CD  
4145 O OE1 . GLU C 119 ? 2.6088 1.8093 1.2877 0.8660  -0.1936 0.0451  119 GLU A OE1 
4146 O OE2 . GLU C 119 ? 2.6872 1.7592 1.2624 0.8415  -0.1703 0.0524  119 GLU A OE2 
4147 N N   . GLU C 120 ? 2.5849 1.7975 1.3833 0.7750  -0.1489 0.0372  120 GLU A N   
4148 C CA  . GLU C 120 ? 2.5416 1.8120 1.4119 0.7703  -0.1458 0.0344  120 GLU A CA  
4149 C C   . GLU C 120 ? 2.5862 1.9451 1.5371 0.7487  -0.1658 0.0166  120 GLU A C   
4150 O O   . GLU C 120 ? 2.5572 1.9409 1.5633 0.7146  -0.1567 0.0091  120 GLU A O   
4151 C CB  . GLU C 120 ? 2.4705 1.7525 1.3293 0.8180  -0.1480 0.0461  120 GLU A CB  
4152 C CG  . GLU C 120 ? 2.5162 1.7063 1.2888 0.8416  -0.1284 0.0633  120 GLU A CG  
4153 C CD  . GLU C 120 ? 2.4645 1.6059 1.2339 0.8181  -0.0993 0.0691  120 GLU A CD  
4154 O OE1 . GLU C 120 ? 2.4993 1.5985 1.2545 0.7811  -0.0866 0.0653  120 GLU A OE1 
4155 O OE2 . GLU C 120 ? 2.3606 1.5068 1.1406 0.8380  -0.0894 0.0772  120 GLU A OE2 
4156 N N   . GLU C 121 ? 2.6796 2.0862 1.6367 0.7689  -0.1930 0.0094  121 GLU A N   
4157 C CA  . GLU C 121 ? 2.6588 2.1484 1.6887 0.7479  -0.2135 -0.0093 121 GLU A CA  
4158 C C   . GLU C 121 ? 2.6496 2.1209 1.6890 0.7006  -0.2076 -0.0200 121 GLU A C   
4159 O O   . GLU C 121 ? 2.6087 2.1211 1.7127 0.6686  -0.2039 -0.0305 121 GLU A O   
4160 C CB  . GLU C 121 ? 2.6519 2.1853 1.6723 0.7791  -0.2443 -0.0153 121 GLU A CB  
4161 C CG  . GLU C 121 ? 2.6677 2.2798 1.7486 0.7582  -0.2698 -0.0369 121 GLU A CG  
4162 C CD  . GLU C 121 ? 2.6319 2.2987 1.7993 0.7206  -0.2631 -0.0488 121 GLU A CD  
4163 O OE1 . GLU C 121 ? 2.6113 2.2659 1.7931 0.6801  -0.2570 -0.0584 121 GLU A OE1 
4164 O OE2 . GLU C 121 ? 2.6596 2.3796 1.8787 0.7324  -0.2626 -0.0480 121 GLU A OE2 
4165 N N   . LEU C 122 ? 2.5852 1.9920 1.5584 0.6966  -0.2047 -0.0165 122 LEU A N   
4166 C CA  . LEU C 122 ? 2.5470 1.9325 1.5231 0.6544  -0.1980 -0.0253 122 LEU A CA  
4167 C C   . LEU C 122 ? 2.5408 1.9163 1.5526 0.6216  -0.1735 -0.0244 122 LEU A C   
4168 O O   . LEU C 122 ? 2.5115 1.9017 1.5575 0.5854  -0.1707 -0.0353 122 LEU A O   
4169 C CB  . LEU C 122 ? 2.5247 1.8311 1.4175 0.6583  -0.1915 -0.0173 122 LEU A CB  
4170 C CG  . LEU C 122 ? 2.5023 1.8116 1.3840 0.6409  -0.2062 -0.0292 122 LEU A CG  
4171 C CD1 . LEU C 122 ? 2.4683 1.8559 1.3909 0.6535  -0.2376 -0.0434 122 LEU A CD1 
4172 C CD2 . LEU C 122 ? 2.4961 1.7291 1.2898 0.6563  -0.2010 -0.0187 122 LEU A CD2 
4173 N N   . ARG C 123 ? 2.6038 1.9531 1.6059 0.6350  -0.1553 -0.0116 123 ARG A N   
4174 C CA  . ARG C 123 ? 2.6059 1.9500 1.6429 0.6076  -0.1330 -0.0108 123 ARG A CA  
4175 C C   . ARG C 123 ? 2.5910 2.0145 1.7128 0.5991  -0.1390 -0.0205 123 ARG A C   
4176 O O   . ARG C 123 ? 2.5915 2.0281 1.7551 0.5662  -0.1279 -0.0272 123 ARG A O   
4177 C CB  . ARG C 123 ? 2.6223 1.9077 1.6157 0.6247  -0.1116 0.0054  123 ARG A CB  
4178 C CG  . ARG C 123 ? 2.6039 1.8562 1.6047 0.5930  -0.0865 0.0070  123 ARG A CG  
4179 C CD  . ARG C 123 ? 2.6171 1.8621 1.6265 0.6075  -0.0703 0.0168  123 ARG A CD  
4180 N NE  . ARG C 123 ? 2.5955 1.7827 1.5789 0.5864  -0.0456 0.0219  123 ARG A NE  
4181 C CZ  . ARG C 123 ? 2.5786 1.7467 1.5611 0.5932  -0.0283 0.0298  123 ARG A CZ  
4182 N NH1 . ARG C 123 ? 2.5901 1.7866 1.5916 0.6230  -0.0311 0.0355  123 ARG A NH1 
4183 N NH2 . ARG C 123 ? 2.5500 1.6707 1.5120 0.5701  -0.0078 0.0317  123 ARG A NH2 
4184 N N   . GLU C 124 ? 2.4997 1.9778 1.6478 0.6283  -0.1560 -0.0215 124 GLU A N   
4185 C CA  . GLU C 124 ? 2.3968 1.9543 1.6277 0.6199  -0.1618 -0.0315 124 GLU A CA  
4186 C C   . GLU C 124 ? 2.3832 1.9866 1.6564 0.5899  -0.1770 -0.0503 124 GLU A C   
4187 O O   . GLU C 124 ? 2.3257 1.9599 1.6555 0.5600  -0.1687 -0.0590 124 GLU A O   
4188 C CB  . GLU C 124 ? 2.3307 1.9366 1.5768 0.6605  -0.1764 -0.0277 124 GLU A CB  
4189 C CG  . GLU C 124 ? 2.1935 1.7917 1.4466 0.6802  -0.1579 -0.0142 124 GLU A CG  
4190 C CD  . GLU C 124 ? 2.0251 1.6952 1.3632 0.6689  -0.1550 -0.0213 124 GLU A CD  
4191 O OE1 . GLU C 124 ? 1.9665 1.6310 1.3356 0.6358  -0.1377 -0.0249 124 GLU A OE1 
4192 O OE2 . GLU C 124 ? 1.9326 1.6652 1.3056 0.6944  -0.1694 -0.0230 124 GLU A OE2 
4193 N N   . ASN C 125 ? 2.4045 2.0111 1.6490 0.5983  -0.1988 -0.0567 125 ASN A N   
4194 C CA  . ASN C 125 ? 2.3707 2.0118 1.6443 0.5706  -0.2140 -0.0749 125 ASN A CA  
4195 C C   . ASN C 125 ? 2.4008 1.9795 1.6079 0.5628  -0.2149 -0.0737 125 ASN A C   
4196 O O   . ASN C 125 ? 2.4307 1.9814 1.5801 0.5919  -0.2256 -0.0669 125 ASN A O   
4197 C CB  . ASN C 125 ? 2.3591 2.0777 1.6703 0.5877  -0.2433 -0.0874 125 ASN A CB  
4198 C CG  . ASN C 125 ? 2.2786 2.0727 1.6782 0.5681  -0.2439 -0.1000 125 ASN A CG  
4199 O OD1 . ASN C 125 ? 2.2279 2.0545 1.6655 0.5377  -0.2514 -0.1169 125 ASN A OD1 
4200 N ND2 . ASN C 125 ? 2.2837 2.1040 1.7150 0.5855  -0.2347 -0.0917 125 ASN A ND2 
4201 N N   . PRO C 126 ? 2.3937 1.9488 1.6047 0.5261  -0.2031 -0.0795 126 PRO A N   
4202 C CA  . PRO C 126 ? 2.4212 1.9121 1.5676 0.5182  -0.1994 -0.0763 126 PRO A CA  
4203 C C   . PRO C 126 ? 2.4337 1.9437 1.5646 0.5228  -0.2255 -0.0880 126 PRO A C   
4204 O O   . PRO C 126 ? 2.3823 1.9582 1.5640 0.5178  -0.2444 -0.1032 126 PRO A O   
4205 C CB  . PRO C 126 ? 2.3902 1.8646 1.5591 0.4776  -0.1792 -0.0802 126 PRO A CB  
4206 C CG  . PRO C 126 ? 2.2832 1.8286 1.5308 0.4609  -0.1852 -0.0942 126 PRO A CG  
4207 C CD  . PRO C 126 ? 2.2959 1.8838 1.5711 0.4906  -0.1925 -0.0897 126 PRO A CD  
4208 N N   . PRO C 127 ? 2.5706 2.0245 1.6316 0.5320  -0.2269 -0.0821 127 PRO A N   
4209 C CA  . PRO C 127 ? 2.5714 2.0352 1.6149 0.5292  -0.2484 -0.0943 127 PRO A CA  
4210 C C   . PRO C 127 ? 2.5449 2.0110 1.6154 0.4870  -0.2417 -0.1065 127 PRO A C   
4211 O O   . PRO C 127 ? 2.5323 1.9710 1.6118 0.4628  -0.2178 -0.1018 127 PRO A O   
4212 C CB  . PRO C 127 ? 2.5916 1.9837 1.5483 0.5505  -0.2449 -0.0812 127 PRO A CB  
4213 C CG  . PRO C 127 ? 2.5812 1.9166 1.5147 0.5456  -0.2153 -0.0653 127 PRO A CG  
4214 C CD  . PRO C 127 ? 2.5790 1.9561 1.5725 0.5449  -0.2079 -0.0642 127 PRO A CD  
4215 N N   . ALA C 128 ? 2.4171 1.9172 1.4997 0.4794  -0.2636 -0.1229 128 ALA A N   
4216 C CA  . ALA C 128 ? 2.3671 1.8707 1.4741 0.4409  -0.2586 -0.1358 128 ALA A CA  
4217 C C   . ALA C 128 ? 2.3247 1.7562 1.3812 0.4254  -0.2368 -0.1262 128 ALA A C   
4218 O O   . ALA C 128 ? 2.2786 1.7031 1.3583 0.3939  -0.2205 -0.1299 128 ALA A O   
4219 C CB  . ALA C 128 ? 2.3499 1.8915 1.4633 0.4389  -0.2868 -0.1544 128 ALA A CB  
4220 N N   . LYS C 129 ? 2.3402 1.7181 1.3278 0.4475  -0.2351 -0.1135 129 LYS A N   
4221 C CA  . LYS C 129 ? 2.2530 1.5628 1.1880 0.4349  -0.2156 -0.1044 129 LYS A CA  
4222 C C   . LYS C 129 ? 2.1791 1.4399 1.0755 0.4521  -0.1968 -0.0854 129 LYS A C   
4223 O O   . LYS C 129 ? 2.2366 1.5001 1.1163 0.4840  -0.2051 -0.0782 129 LYS A O   
4224 C CB  . LYS C 129 ? 2.2498 1.5345 1.1304 0.4431  -0.2304 -0.1084 129 LYS A CB  
4225 C CG  . LYS C 129 ? 2.2644 1.5864 1.1744 0.4221  -0.2465 -0.1280 129 LYS A CG  
4226 C CD  . LYS C 129 ? 2.2656 1.5446 1.1503 0.3951  -0.2309 -0.1286 129 LYS A CD  
4227 C CE  . LYS C 129 ? 2.1821 1.4814 1.1230 0.3606  -0.2148 -0.1349 129 LYS A CE  
4228 N NZ  . LYS C 129 ? 2.0983 1.3489 1.0099 0.3388  -0.1936 -0.1302 129 LYS A NZ  
4229 N N   . VAL C 130 ? 2.1435 1.3598 1.0251 0.4312  -0.1713 -0.0777 130 VAL A N   
4230 C CA  . VAL C 130 ? 2.1227 1.2921 0.9705 0.4430  -0.1519 -0.0614 130 VAL A CA  
4231 C C   . VAL C 130 ? 2.1342 1.2493 0.9051 0.4671  -0.1542 -0.0519 130 VAL A C   
4232 O O   . VAL C 130 ? 2.1025 1.1830 0.8347 0.4571  -0.1512 -0.0525 130 VAL A O   
4233 C CB  . VAL C 130 ? 2.0682 1.2093 0.9234 0.4128  -0.1248 -0.0574 130 VAL A CB  
4234 C CG1 . VAL C 130 ? 2.0746 1.1716 0.8996 0.4235  -0.1056 -0.0425 130 VAL A CG1 
4235 C CG2 . VAL C 130 ? 1.9564 1.1493 0.8843 0.3895  -0.1223 -0.0673 130 VAL A CG2 
4236 N N   . GLN C 131 ? 2.1107 1.2171 0.8575 0.5002  -0.1586 -0.0426 131 GLN A N   
4237 C CA  . GLN C 131 ? 2.2014 1.2503 0.8707 0.5269  -0.1578 -0.0314 131 GLN A CA  
4238 C C   . GLN C 131 ? 2.2276 1.2118 0.8597 0.5207  -0.1283 -0.0173 131 GLN A C   
4239 O O   . GLN C 131 ? 2.2857 1.2584 0.9122 0.5383  -0.1205 -0.0080 131 GLN A O   
4240 C CB  . GLN C 131 ? 2.2655 1.3386 0.9247 0.5687  -0.1784 -0.0290 131 GLN A CB  
4241 C CG  . GLN C 131 ? 2.2681 1.3592 0.9042 0.5873  -0.2052 -0.0370 131 GLN A CG  
4242 C CD  . GLN C 131 ? 2.2490 1.3649 0.8723 0.6321  -0.2253 -0.0336 131 GLN A CD  
4243 O OE1 . GLN C 131 ? 2.2858 1.3892 0.9011 0.6529  -0.2159 -0.0220 131 GLN A OE1 
4244 N NE2 . GLN C 131 ? 2.2331 1.3846 0.8529 0.6480  -0.2531 -0.0439 131 GLN A NE2 
4245 N N   . VAL C 132 ? 2.2643 1.2057 0.8697 0.4953  -0.1116 -0.0160 132 VAL A N   
4246 C CA  . VAL C 132 ? 2.2784 1.1609 0.8517 0.4831  -0.0830 -0.0050 132 VAL A CA  
4247 C C   . VAL C 132 ? 2.3735 1.2025 0.8842 0.5151  -0.0762 0.0090  132 VAL A C   
4248 O O   . VAL C 132 ? 2.3669 1.1584 0.8621 0.5116  -0.0552 0.0176  132 VAL A O   
4249 C CB  . VAL C 132 ? 2.1600 1.0074 0.7080 0.4553  -0.0695 -0.0063 132 VAL A CB  
4250 C CG1 . VAL C 132 ? 2.2536 1.0868 0.7582 0.4700  -0.0841 -0.0080 132 VAL A CG1 
4251 C CG2 . VAL C 132 ? 2.2016 0.9837 0.7063 0.4450  -0.0410 0.0048  132 VAL A CG2 
4252 N N   . ASP C 133 ? 2.4281 1.2516 0.9003 0.5475  -0.0934 0.0111  133 ASP A N   
4253 C CA  . ASP C 133 ? 2.4841 1.2521 0.8902 0.5810  -0.0861 0.0252  133 ASP A CA  
4254 C C   . ASP C 133 ? 2.4743 1.2573 0.9019 0.5995  -0.0837 0.0309  133 ASP A C   
4255 O O   . ASP C 133 ? 2.5088 1.2375 0.8916 0.6148  -0.0663 0.0424  133 ASP A O   
4256 C CB  . ASP C 133 ? 2.5193 1.2900 0.8907 0.6137  -0.1068 0.0246  133 ASP A CB  
4257 C CG  . ASP C 133 ? 2.4732 1.3229 0.8943 0.6194  -0.1390 0.0110  133 ASP A CG  
4258 O OD1 . ASP C 133 ? 2.5155 1.3747 0.9086 0.6477  -0.1601 0.0092  133 ASP A OD1 
4259 O OD2 . ASP C 133 ? 2.3950 1.2990 0.8872 0.5937  -0.1423 0.0007  133 ASP A OD2 
4260 N N   . HIS C 134 ? 2.5128 1.3693 1.0122 0.5971  -0.0990 0.0218  134 HIS A N   
4261 C CA  . HIS C 134 ? 2.5029 1.3814 1.0286 0.6156  -0.0980 0.0266  134 HIS A CA  
4262 C C   . HIS C 134 ? 2.4630 1.3531 1.0379 0.5842  -0.0804 0.0243  134 HIS A C   
4263 O O   . HIS C 134 ? 2.4790 1.3974 1.0882 0.5949  -0.0800 0.0262  134 HIS A O   
4264 C CB  . HIS C 134 ? 2.5146 1.4699 1.0860 0.6394  -0.1273 0.0188  134 HIS A CB  
4265 C CG  . HIS C 134 ? 2.5609 1.5074 1.0816 0.6798  -0.1452 0.0229  134 HIS A CG  
4266 N ND1 . HIS C 134 ? 2.5755 1.4578 1.0216 0.6878  -0.1396 0.0293  134 HIS A ND1 
4267 C CD2 . HIS C 134 ? 2.5856 1.5811 1.1196 0.7156  -0.1687 0.0213  134 HIS A CD2 
4268 C CE1 . HIS C 134 ? 2.5875 1.4774 1.0005 0.7280  -0.1590 0.0319  134 HIS A CE1 
4269 N NE2 . HIS C 134 ? 2.6124 1.5725 1.0783 0.7457  -0.1775 0.0269  134 HIS A NE2 
4270 N N   . ILE C 135 ? 2.3607 1.2310 0.9393 0.5472  -0.0659 0.0204  135 ILE A N   
4271 C CA  . ILE C 135 ? 2.2859 1.1572 0.8994 0.5189  -0.0468 0.0195  135 ILE A CA  
4272 C C   . ILE C 135 ? 2.2727 1.0709 0.8304 0.5216  -0.0222 0.0315  135 ILE A C   
4273 O O   . ILE C 135 ? 2.2921 1.0306 0.7855 0.5258  -0.0134 0.0378  135 ILE A O   
4274 C CB  . ILE C 135 ? 2.2342 1.1197 0.8767 0.4793  -0.0422 0.0098  135 ILE A CB  
4275 C CG1 . ILE C 135 ? 2.1789 1.1412 0.8957 0.4689  -0.0589 -0.0028 135 ILE A CG1 
4276 C CG2 . ILE C 135 ? 2.2011 1.0583 0.8469 0.4526  -0.0171 0.0123  135 ILE A CG2 
4277 C CD1 . ILE C 135 ? 2.2154 1.2126 0.9363 0.4856  -0.0847 -0.0095 135 ILE A CD1 
4278 N N   . VAL C 136 ? 2.2536 1.0542 0.8344 0.5182  -0.0099 0.0341  136 VAL A N   
4279 C CA  . VAL C 136 ? 2.2171 0.9504 0.7505 0.5158  0.0145  0.0433  136 VAL A CA  
4280 C C   . VAL C 136 ? 2.1701 0.9139 0.7433 0.4822  0.0301  0.0384  136 VAL A C   
4281 O O   . VAL C 136 ? 2.1397 0.9396 0.7749 0.4774  0.0236  0.0328  136 VAL A O   
4282 C CB  . VAL C 136 ? 2.1886 0.9022 0.6939 0.5545  0.0148  0.0538  136 VAL A CB  
4283 C CG1 . VAL C 136 ? 2.2968 1.0823 0.8673 0.5690  -0.0006 0.0501  136 VAL A CG1 
4284 C CG2 . VAL C 136 ? 2.1882 0.8361 0.6525 0.5479  0.0411  0.0613  136 VAL A CG2 
4285 N N   . ARG C 137 ? 2.1454 0.8354 0.6824 0.4593  0.0511  0.0402  137 ARG A N   
4286 C CA  . ARG C 137 ? 2.0936 0.7896 0.6608 0.4257  0.0662  0.0348  137 ARG A CA  
4287 C C   . ARG C 137 ? 2.0823 0.7333 0.6225 0.4283  0.0853  0.0408  137 ARG A C   
4288 O O   . ARG C 137 ? 2.1282 0.7215 0.6088 0.4472  0.0934  0.0496  137 ARG A O   
4289 C CB  . ARG C 137 ? 2.0855 0.7606 0.6362 0.3946  0.0756  0.0306  137 ARG A CB  
4290 C CG  . ARG C 137 ? 2.0956 0.6931 0.5736 0.3934  0.0938  0.0378  137 ARG A CG  
4291 C CD  . ARG C 137 ? 2.0789 0.6554 0.5528 0.3557  0.1124  0.0332  137 ARG A CD  
4292 N NE  . ARG C 137 ? 2.2111 0.7423 0.6520 0.3495  0.1225  0.0337  137 ARG A NE  
4293 C CZ  . ARG C 137 ? 2.2312 0.7353 0.6685 0.3190  0.1409  0.0314  137 ARG A CZ  
4294 N NH1 . ARG C 137 ? 2.1607 0.6805 0.6265 0.2922  0.1501  0.0288  137 ARG A NH1 
4295 N NH2 . ARG C 137 ? 2.2132 0.6746 0.6175 0.3161  0.1505  0.0318  137 ARG A NH2 
4296 N N   . ASN C 138 ? 2.0401 0.7159 0.6226 0.4093  0.0929  0.0359  138 ASN A N   
4297 C CA  . ASN C 138 ? 2.0441 0.6859 0.6100 0.4101  0.1096  0.0396  138 ASN A CA  
4298 C C   . ASN C 138 ? 2.0423 0.6917 0.6334 0.3734  0.1229  0.0318  138 ASN A C   
4299 O O   . ASN C 138 ? 1.9825 0.6880 0.6327 0.3626  0.1170  0.0254  138 ASN A O   
4300 C CB  . ASN C 138 ? 2.0127 0.6875 0.6094 0.4380  0.1011  0.0430  138 ASN A CB  
4301 C CG  . ASN C 138 ? 2.0373 0.6841 0.6232 0.4370  0.1181  0.0456  138 ASN A CG  
4302 O OD1 . ASN C 138 ? 2.1160 0.7248 0.6650 0.4178  0.1351  0.0448  138 ASN A OD1 
4303 N ND2 . ASN C 138 ? 1.9960 0.6800 0.6228 0.4524  0.1135  0.0464  138 ASN A ND2 
4304 N N   . ILE C 139 ? 2.0319 0.6251 0.5775 0.3545  0.1413  0.0320  139 ILE A N   
4305 C CA  . ILE C 139 ? 2.0155 0.6189 0.5822 0.3181  0.1537  0.0252  139 ILE A CA  
4306 C C   . ILE C 139 ? 2.1011 0.7090 0.6801 0.3168  0.1623  0.0272  139 ILE A C   
4307 O O   . ILE C 139 ? 2.1192 0.6961 0.6619 0.3286  0.1695  0.0337  139 ILE A O   
4308 C CB  . ILE C 139 ? 2.0191 0.5834 0.5481 0.2919  0.1667  0.0285  139 ILE A CB  
4309 C CG1 . ILE C 139 ? 2.0155 0.5880 0.5465 0.2853  0.1593  0.0249  139 ILE A CG1 
4310 C CG2 . ILE C 139 ? 2.0171 0.5888 0.5679 0.2570  0.1800  0.0251  139 ILE A CG2 
4311 C CD1 . ILE C 139 ? 2.0206 0.5712 0.5434 0.2523  0.1726  0.0255  139 ILE A CD1 
4312 N N   . LEU C 140 ? 2.0422 0.6900 0.6700 0.3028  0.1624  0.0201  140 LEU A N   
4313 C CA  . LEU C 140 ? 2.0224 0.6745 0.6618 0.2987  0.1712  0.0213  140 LEU A CA  
4314 C C   . LEU C 140 ? 2.0025 0.6343 0.6280 0.2642  0.1859  0.0198  140 LEU A C   
4315 O O   . LEU C 140 ? 1.9915 0.6519 0.6516 0.2425  0.1890  0.0129  140 LEU A O   
4316 C CB  . LEU C 140 ? 2.0136 0.7175 0.7106 0.3042  0.1646  0.0153  140 LEU A CB  
4317 C CG  . LEU C 140 ? 2.0121 0.7214 0.7205 0.3055  0.1724  0.0174  140 LEU A CG  
4318 C CD1 . LEU C 140 ? 2.0593 0.7745 0.7711 0.3401  0.1663  0.0241  140 LEU A CD1 
4319 C CD2 . LEU C 140 ? 2.0290 0.7824 0.7877 0.2895  0.1732  0.0090  140 LEU A CD2 
4320 N N   . ALA C 141 ? 2.0682 0.6499 0.6417 0.2599  0.1954  0.0263  141 ALA A N   
4321 C CA  . ALA C 141 ? 2.0936 0.6504 0.6514 0.2264  0.2094  0.0252  141 ALA A CA  
4322 C C   . ALA C 141 ? 2.0460 0.5889 0.5965 0.2175  0.2204  0.0255  141 ALA A C   
4323 O O   . ALA C 141 ? 2.0193 0.5481 0.5651 0.1878  0.2314  0.0220  141 ALA A O   
4324 C CB  . ALA C 141 ? 2.1462 0.6531 0.6510 0.2237  0.2166  0.0318  141 ALA A CB  
4325 N N   . GLU C 142 ? 2.1750 0.7224 0.7249 0.2429  0.2176  0.0288  142 GLU A N   
4326 C CA  . GLU C 142 ? 2.1828 0.7235 0.7311 0.2393  0.2258  0.0287  142 GLU A CA  
4327 C C   . GLU C 142 ? 2.1228 0.7086 0.7245 0.2245  0.2230  0.0204  142 GLU A C   
4328 O O   . GLU C 142 ? 2.1319 0.7130 0.7341 0.2162  0.2300  0.0188  142 GLU A O   
4329 C CB  . GLU C 142 ? 2.2052 0.7419 0.7395 0.2748  0.2228  0.0348  142 GLU A CB  
4330 C CG  . GLU C 142 ? 2.1874 0.7710 0.7645 0.3013  0.2070  0.0340  142 GLU A CG  
4331 C CD  . GLU C 142 ? 2.2742 0.8494 0.8309 0.3268  0.1981  0.0380  142 GLU A CD  
4332 O OE1 . GLU C 142 ? 2.2412 0.7917 0.7694 0.3166  0.1997  0.0381  142 GLU A OE1 
4333 O OE2 . GLU C 142 ? 2.3354 0.9321 0.9082 0.3575  0.1889  0.0409  142 GLU A OE2 
4334 N N   . LYS C 143 ? 1.9276 0.5567 0.5716 0.2222  0.2135  0.0147  143 LYS A N   
4335 C CA  . LYS C 143 ? 1.8846 0.5597 0.5775 0.2104  0.2116  0.0063  143 LYS A CA  
4336 C C   . LYS C 143 ? 1.8436 0.5448 0.5604 0.1871  0.2096  -0.0015 143 LYS A C   
4337 O O   . LYS C 143 ? 1.7948 0.5381 0.5489 0.1925  0.2016  -0.0057 143 LYS A O   
4338 C CB  . LYS C 143 ? 1.8688 0.5805 0.5963 0.2375  0.2030  0.0073  143 LYS A CB  
4339 C CG  . LYS C 143 ? 1.8680 0.5674 0.5849 0.2547  0.2073  0.0128  143 LYS A CG  
4340 C CD  . LYS C 143 ? 1.8936 0.5986 0.6115 0.2901  0.2000  0.0197  143 LYS A CD  
4341 C CE  . LYS C 143 ? 1.8001 0.5554 0.5713 0.3047  0.1936  0.0175  143 LYS A CE  
4342 N NZ  . LYS C 143 ? 1.8045 0.5722 0.5851 0.3376  0.1847  0.0233  143 LYS A NZ  
4343 N N   . PRO C 144 ? 1.8425 0.5212 0.5396 0.1600  0.2180  -0.0042 144 PRO A N   
4344 C CA  . PRO C 144 ? 1.8087 0.5165 0.5300 0.1366  0.2175  -0.0120 144 PRO A CA  
4345 C C   . PRO C 144 ? 1.7489 0.5122 0.5197 0.1310  0.2140  -0.0202 144 PRO A C   
4346 O O   . PRO C 144 ? 1.7392 0.5123 0.5221 0.1344  0.2158  -0.0220 144 PRO A O   
4347 C CB  . PRO C 144 ? 1.8456 0.5202 0.5393 0.1081  0.2299  -0.0145 144 PRO A CB  
4348 C CG  . PRO C 144 ? 1.8830 0.5246 0.5514 0.1128  0.2366  -0.0112 144 PRO A CG  
4349 C CD  . PRO C 144 ? 1.8975 0.5267 0.5524 0.1476  0.2300  -0.0013 144 PRO A CD  
4350 N N   . ARG C 145 ? 1.7107 0.5098 0.5084 0.1235  0.2094  -0.0246 145 ARG A N   
4351 C CA  . ARG C 145 ? 1.6576 0.5082 0.4983 0.1147  0.2083  -0.0322 145 ARG A CA  
4352 C C   . ARG C 145 ? 1.6506 0.5129 0.4950 0.0860  0.2136  -0.0386 145 ARG A C   
4353 O O   . ARG C 145 ? 1.6477 0.5131 0.4903 0.0810  0.2116  -0.0377 145 ARG A O   
4354 C CB  . ARG C 145 ? 1.6183 0.5041 0.4893 0.1331  0.1995  -0.0316 145 ARG A CB  
4355 C CG  . ARG C 145 ? 1.6343 0.5040 0.4963 0.1626  0.1938  -0.0253 145 ARG A CG  
4356 C CD  . ARG C 145 ? 1.6218 0.5032 0.5008 0.1746  0.1959  -0.0250 145 ARG A CD  
4357 N NE  . ARG C 145 ? 1.6051 0.5036 0.5047 0.2010  0.1896  -0.0225 145 ARG A NE  
4358 C CZ  . ARG C 145 ? 1.6312 0.5090 0.5170 0.2245  0.1872  -0.0161 145 ARG A CZ  
4359 N NH1 . ARG C 145 ? 1.7185 0.5537 0.5647 0.2264  0.1908  -0.0105 145 ARG A NH1 
4360 N NH2 . ARG C 145 ? 1.6104 0.5117 0.5238 0.2467  0.1819  -0.0152 145 ARG A NH2 
4361 N N   . VAL C 146 ? 1.6502 0.5193 0.4989 0.0675  0.2202  -0.0454 146 VAL A N   
4362 C CA  . VAL C 146 ? 1.6610 0.5292 0.5024 0.0388  0.2275  -0.0519 146 VAL A CA  
4363 C C   . VAL C 146 ? 1.6128 0.5372 0.4926 0.0274  0.2268  -0.0606 146 VAL A C   
4364 O O   . VAL C 146 ? 1.5871 0.5385 0.4891 0.0343  0.2248  -0.0639 146 VAL A O   
4365 C CB  . VAL C 146 ? 1.7080 0.5366 0.5184 0.0237  0.2369  -0.0548 146 VAL A CB  
4366 C CG1 . VAL C 146 ? 1.7155 0.5516 0.5241 -0.0083 0.2453  -0.0644 146 VAL A CG1 
4367 C CG2 . VAL C 146 ? 1.7614 0.5311 0.5291 0.0352  0.2395  -0.0449 146 VAL A CG2 
4368 N N   . THR C 147 ? 1.6033 0.5445 0.4890 0.0109  0.2292  -0.0637 147 THR A N   
4369 C CA  . THR C 147 ? 1.5633 0.5572 0.4812 -0.0011 0.2299  -0.0717 147 THR A CA  
4370 C C   . THR C 147 ? 1.5860 0.5750 0.4903 -0.0300 0.2389  -0.0791 147 THR A C   
4371 O O   . THR C 147 ? 1.6144 0.5738 0.4957 -0.0383 0.2431  -0.0756 147 THR A O   
4372 C CB  . THR C 147 ? 1.5246 0.5516 0.4674 0.0093  0.2241  -0.0678 147 THR A CB  
4373 O OG1 . THR C 147 ? 1.5165 0.5356 0.4629 0.0346  0.2168  -0.0606 147 THR A OG1 
4374 C CG2 . THR C 147 ? 1.4816 0.5641 0.4590 0.0044  0.2244  -0.0742 147 THR A CG2 
4375 N N   . ARG C 148 ? 1.5759 0.5940 0.4932 -0.0450 0.2424  -0.0897 148 ARG A N   
4376 C CA  . ARG C 148 ? 1.5986 0.6162 0.5042 -0.0742 0.2517  -0.0987 148 ARG A CA  
4377 C C   . ARG C 148 ? 1.5573 0.6366 0.4953 -0.0818 0.2513  -0.1057 148 ARG A C   
4378 O O   . ARG C 148 ? 1.5203 0.6401 0.4856 -0.0693 0.2456  -0.1078 148 ARG A O   
4379 C CB  . ARG C 148 ? 1.6350 0.6284 0.5204 -0.0893 0.2575  -0.1074 148 ARG A CB  
4380 C CG  . ARG C 148 ? 1.6857 0.6118 0.5326 -0.0841 0.2608  -0.0998 148 ARG A CG  
4381 C CD  . ARG C 148 ? 1.7256 0.6240 0.5505 -0.0989 0.2673  -0.1080 148 ARG A CD  
4382 N NE  . ARG C 148 ? 1.7199 0.6541 0.5573 -0.1249 0.2716  -0.1239 148 ARG A NE  
4383 C CZ  . ARG C 148 ? 1.7637 0.6742 0.5775 -0.1543 0.2827  -0.1337 148 ARG A CZ  
4384 N NH1 . ARG C 148 ? 1.8182 0.6657 0.5929 -0.1621 0.2923  -0.1280 148 ARG A NH1 
4385 N NH2 . ARG C 148 ? 1.7549 0.7062 0.5835 -0.1767 0.2851  -0.1496 148 ARG A NH2 
4386 N N   . PHE C 149 ? 1.5651 0.6513 0.4992 -0.1005 0.2580  -0.1083 149 PHE A N   
4387 C CA  . PHE C 149 ? 1.5825 0.7273 0.5447 -0.1077 0.2590  -0.1141 149 PHE A CA  
4388 C C   . PHE C 149 ? 1.6326 0.7833 0.5836 -0.1392 0.2697  -0.1264 149 PHE A C   
4389 O O   . PHE C 149 ? 1.6664 0.7775 0.5903 -0.1564 0.2787  -0.1259 149 PHE A O   
4390 C CB  . PHE C 149 ? 1.5092 0.6658 0.4819 -0.0991 0.2573  -0.1050 149 PHE A CB  
4391 C CG  . PHE C 149 ? 1.4977 0.6343 0.4715 -0.0733 0.2485  -0.0932 149 PHE A CG  
4392 C CD1 . PHE C 149 ? 1.4547 0.6266 0.4578 -0.0528 0.2409  -0.0900 149 PHE A CD1 
4393 C CD2 . PHE C 149 ? 1.5332 0.6149 0.4771 -0.0694 0.2485  -0.0857 149 PHE A CD2 
4394 C CE1 . PHE C 149 ? 1.4467 0.6012 0.4506 -0.0314 0.2336  -0.0808 149 PHE A CE1 
4395 C CE2 . PHE C 149 ? 1.5246 0.5912 0.4688 -0.0457 0.2398  -0.0763 149 PHE A CE2 
4396 C CZ  . PHE C 149 ? 1.4811 0.5849 0.4559 -0.0279 0.2324  -0.0744 149 PHE A CZ  
4397 N N   . ASN C 150 ? 1.6483 0.8494 0.6197 -0.1467 0.2696  -0.1378 150 ASN A N   
4398 C CA  . ASN C 150 ? 1.6707 0.8854 0.6343 -0.1782 0.2795  -0.1521 150 ASN A CA  
4399 C C   . ASN C 150 ? 1.7443 0.9872 0.7174 -0.1885 0.2860  -0.1509 150 ASN A C   
4400 O O   . ASN C 150 ? 1.7062 1.0038 0.7083 -0.1769 0.2820  -0.1499 150 ASN A O   
4401 C CB  . ASN C 150 ? 1.6930 0.9548 0.6742 -0.1809 0.2757  -0.1655 150 ASN A CB  
4402 C CG  . ASN C 150 ? 1.7844 1.0096 0.7457 -0.1852 0.2746  -0.1717 150 ASN A CG  
4403 O OD1 . ASN C 150 ? 1.7788 0.9785 0.7377 -0.1623 0.2675  -0.1628 150 ASN A OD1 
4404 N ND2 . ASN C 150 ? 1.7565 0.9776 0.7028 -0.2155 0.2823  -0.1872 150 ASN A ND2 
4405 N N   . ILE C 151 ? 1.8114 1.0143 0.7583 -0.2091 0.2971  -0.1502 151 ILE A N   
4406 C CA  . ILE C 151 ? 1.7948 1.0176 0.7460 -0.2218 0.3058  -0.1493 151 ILE A CA  
4407 C C   . ILE C 151 ? 1.8944 1.1343 0.8392 -0.2577 0.3188  -0.1659 151 ILE A C   
4408 O O   . ILE C 151 ? 1.8946 1.1105 0.8216 -0.2756 0.3226  -0.1767 151 ILE A O   
4409 C CB  . ILE C 151 ? 1.8276 0.9952 0.7547 -0.2170 0.3095  -0.1357 151 ILE A CB  
4410 C CG1 . ILE C 151 ? 1.8711 0.9684 0.7561 -0.2359 0.3204  -0.1370 151 ILE A CG1 
4411 C CG2 . ILE C 151 ? 1.7296 0.8852 0.6644 -0.1831 0.2957  -0.1218 151 ILE A CG2 
4412 C CD1 . ILE C 151 ? 1.9166 1.0083 0.7858 -0.2716 0.3382  -0.1471 151 ILE A CD1 
4413 N N   . VAL C 152 ? 1.9588 1.2444 0.9200 -0.2683 0.3255  -0.1687 152 VAL A N   
4414 C CA  . VAL C 152 ? 1.9872 1.2967 0.9455 -0.3044 0.3393  -0.1849 152 VAL A CA  
4415 C C   . VAL C 152 ? 2.0019 1.2472 0.9241 -0.3285 0.3550  -0.1836 152 VAL A C   
4416 O O   . VAL C 152 ? 2.0102 1.2474 0.9285 -0.3295 0.3625  -0.1747 152 VAL A O   
4417 C CB  . VAL C 152 ? 1.9654 1.3485 0.9546 -0.3052 0.3420  -0.1870 152 VAL A CB  
4418 C CG1 . VAL C 152 ? 2.0163 1.4271 1.0035 -0.3451 0.3575  -0.2047 152 VAL A CG1 
4419 C CG2 . VAL C 152 ? 1.9026 1.3456 0.9243 -0.2785 0.3275  -0.1872 152 VAL A CG2 
4420 N N   . TRP C 153 ? 1.9779 1.1746 0.8720 -0.3467 0.3604  -0.1919 153 TRP A N   
4421 C CA  . TRP C 153 ? 2.0239 1.1511 0.8790 -0.3670 0.3765  -0.1892 153 TRP A CA  
4422 C C   . TRP C 153 ? 2.1505 1.3004 1.0054 -0.4022 0.3955  -0.1995 153 TRP A C   
4423 O O   . TRP C 153 ? 2.1934 1.3084 1.0298 -0.4080 0.4075  -0.1906 153 TRP A O   
4424 C CB  . TRP C 153 ? 1.9824 1.0528 0.8071 -0.3786 0.3793  -0.1959 153 TRP A CB  
4425 C CG  . TRP C 153 ? 1.9561 0.9932 0.7754 -0.3440 0.3640  -0.1827 153 TRP A CG  
4426 C CD1 . TRP C 153 ? 1.9553 1.0232 0.7968 -0.3230 0.3478  -0.1842 153 TRP A CD1 
4427 C CD2 . TRP C 153 ? 1.9550 0.9233 0.7446 -0.3256 0.3640  -0.1660 153 TRP A CD2 
4428 N NE1 . TRP C 153 ? 1.9567 0.9801 0.7855 -0.2942 0.3385  -0.1697 153 TRP A NE1 
4429 C CE2 . TRP C 153 ? 1.9576 0.9212 0.7549 -0.2949 0.3475  -0.1585 153 TRP A CE2 
4430 C CE3 . TRP C 153 ? 1.9617 0.8726 0.7183 -0.3312 0.3765  -0.1566 153 TRP A CE3 
4431 C CZ2 . TRP C 153 ? 1.9505 0.8580 0.7248 -0.2703 0.3429  -0.1426 153 TRP A CZ2 
4432 C CZ3 . TRP C 153 ? 1.9552 0.8088 0.6873 -0.3053 0.3712  -0.1407 153 TRP A CZ3 
4433 C CH2 . TRP C 153 ? 1.9251 0.7791 0.6667 -0.2756 0.3543  -0.1341 153 TRP A CH2 
4434 N N   . ASP C 154 ? 2.2843 1.4962 1.1613 -0.4246 0.3980  -0.2181 154 ASP A N   
4435 C CA  . ASP C 154 ? 2.3557 1.6000 1.2365 -0.4629 0.4170  -0.2318 154 ASP A CA  
4436 C C   . ASP C 154 ? 2.3501 1.5859 1.2281 -0.4624 0.4288  -0.2184 154 ASP A C   
4437 O O   . ASP C 154 ? 2.3517 1.5535 1.2065 -0.4927 0.4495  -0.2223 154 ASP A O   
4438 C CB  . ASP C 154 ? 2.3443 1.6850 1.2659 -0.4676 0.4099  -0.2468 154 ASP A CB  
4439 C CG  . ASP C 154 ? 2.3681 1.7568 1.3055 -0.5072 0.4266  -0.2622 154 ASP A CG  
4440 O OD1 . ASP C 154 ? 2.3756 1.8143 1.3352 -0.5277 0.4229  -0.2815 154 ASP A OD1 
4441 O OD2 . ASP C 154 ? 2.3499 1.7332 1.2838 -0.5162 0.4414  -0.2544 154 ASP A OD2 
4442 N N   . LEU D 9   ? 1.6186 0.7553 0.7850 -0.2672 0.3222  -0.0738 10  LEU C N   
4443 C CA  . LEU D 9   ? 1.6016 0.7684 0.7540 -0.2915 0.3005  -0.0899 10  LEU C CA  
4444 C C   . LEU D 9   ? 1.5647 0.7469 0.7387 -0.3209 0.2752  -0.0855 10  LEU C C   
4445 O O   . LEU D 9   ? 1.5537 0.7658 0.7477 -0.3125 0.2687  -0.0702 10  LEU C O   
4446 C CB  . LEU D 9   ? 1.5709 0.7955 0.7139 -0.2742 0.3013  -0.0881 10  LEU C CB  
4447 C CG  . LEU D 9   ? 1.5767 0.8305 0.6958 -0.2889 0.2952  -0.1002 10  LEU C CG  
4448 C CD1 . LEU D 9   ? 1.5458 0.8671 0.6759 -0.2788 0.2965  -0.0932 10  LEU C CD1 
4449 C CD2 . LEU D 9   ? 1.5838 0.8260 0.6914 -0.3251 0.2736  -0.1065 10  LEU C CD2 
4450 N N   . VAL D 10  ? 1.5831 0.7463 0.7494 -0.3494 0.2585  -0.1016 11  VAL C N   
4451 C CA  . VAL D 10  ? 1.5616 0.7438 0.7385 -0.3724 0.2309  -0.1007 11  VAL C CA  
4452 C C   . VAL D 10  ? 1.5809 0.7892 0.7270 -0.3794 0.2171  -0.1028 11  VAL C C   
4453 O O   . VAL D 10  ? 1.5820 0.7810 0.6954 -0.3863 0.2167  -0.1169 11  VAL C O   
4454 C CB  . VAL D 10  ? 1.6103 0.7634 0.7977 -0.3969 0.2174  -0.1182 11  VAL C CB  
4455 C CG1 . VAL D 10  ? 1.5867 0.7601 0.7617 -0.4149 0.1852  -0.1257 11  VAL C CG1 
4456 C CG2 . VAL D 10  ? 1.5839 0.7274 0.8190 -0.3994 0.2278  -0.1060 11  VAL C CG2 
4457 N N   . ILE D 11  ? 1.5849 0.8246 0.7407 -0.3764 0.2056  -0.0879 12  ILE C N   
4458 C CA  . ILE D 11  ? 1.5979 0.8576 0.7329 -0.3890 0.1925  -0.0831 12  ILE C CA  
4459 C C   . ILE D 11  ? 1.6371 0.8865 0.7640 -0.4066 0.1617  -0.0824 12  ILE C C   
4460 O O   . ILE D 11  ? 1.6144 0.8667 0.7636 -0.4007 0.1462  -0.0785 12  ILE C O   
4461 C CB  . ILE D 11  ? 1.5418 0.8362 0.6961 -0.3769 0.1939  -0.0709 12  ILE C CB  
4462 C CG1 . ILE D 11  ? 1.5235 0.8369 0.6817 -0.3540 0.2230  -0.0736 12  ILE C CG1 
4463 C CG2 . ILE D 11  ? 1.5830 0.8909 0.7257 -0.3991 0.1780  -0.0620 12  ILE C CG2 
4464 C CD1 . ILE D 11  ? 1.5384 0.8987 0.7174 -0.3456 0.2214  -0.0674 12  ILE C CD1 
4465 N N   . ASN D 12  ? 1.7504 0.9910 0.8407 -0.4223 0.1529  -0.0854 13  ASN C N   
4466 C CA  . ASN D 12  ? 1.8124 1.0411 0.8846 -0.4337 0.1221  -0.0825 13  ASN C CA  
4467 C C   . ASN D 12  ? 1.8519 1.0795 0.8837 -0.4467 0.1204  -0.0688 13  ASN C C   
4468 O O   . ASN D 12  ? 1.8658 1.0916 0.8620 -0.4483 0.1317  -0.0747 13  ASN C O   
4469 C CB  . ASN D 12  ? 1.8407 1.0538 0.9079 -0.4361 0.1084  -0.1028 13  ASN C CB  
4470 C CG  . ASN D 12  ? 1.9082 1.1176 0.9682 -0.4375 0.0741  -0.1016 13  ASN C CG  
4471 O OD1 . ASN D 12  ? 1.8241 1.0447 0.9182 -0.4306 0.0634  -0.1054 13  ASN C OD1 
4472 N ND2 . ASN D 12  ? 1.9685 1.1639 0.9815 -0.4430 0.0581  -0.0942 13  ASN C ND2 
4473 N N   . GLY D 13  ? 1.8809 1.1079 0.9173 -0.4547 0.1058  -0.0498 14  GLY C N   
4474 C CA  . GLY D 13  ? 1.9367 1.1582 0.9412 -0.4724 0.1055  -0.0284 14  GLY C CA  
4475 C C   . GLY D 13  ? 1.9439 1.1302 0.9309 -0.4787 0.0705  -0.0166 14  GLY C C   
4476 O O   . GLY D 13  ? 1.9635 1.1377 0.9630 -0.4655 0.0456  -0.0285 14  GLY C O   
4477 N N   . ARG D 14  ? 1.9140 1.0841 0.8694 -0.4970 0.0705  0.0090  15  ARG C N   
4478 C CA  . ARG D 14  ? 1.9135 1.0370 0.8468 -0.5026 0.0368  0.0241  15  ARG C CA  
4479 C C   . ARG D 14  ? 1.9042 1.0215 0.8835 -0.4974 0.0128  0.0174  15  ARG C C   
4480 O O   . ARG D 14  ? 1.9296 1.0213 0.9008 -0.4794 -0.0199 0.0065  15  ARG C O   
4481 C CB  . ARG D 14  ? 1.9214 1.0272 0.8249 -0.5285 0.0476  0.0610  15  ARG C CB  
4482 N N   . THR D 15  ? 1.8895 1.0377 0.9169 -0.5069 0.0276  0.0199  16  THR C N   
4483 C CA  . THR D 15  ? 1.8339 0.9793 0.9028 -0.4987 0.0024  0.0113  16  THR C CA  
4484 C C   . THR D 15  ? 1.7932 0.9785 0.8978 -0.4683 0.0099  -0.0130 16  THR C C   
4485 O O   . THR D 15  ? 1.7668 0.9455 0.8859 -0.4450 -0.0173 -0.0254 16  THR C O   
4486 C CB  . THR D 15  ? 1.8088 0.9649 0.9132 -0.5281 0.0072  0.0277  16  THR C CB  
4487 O OG1 . THR D 15  ? 1.7699 0.9897 0.9079 -0.5286 0.0442  0.0231  16  THR C OG1 
4488 C CG2 . THR D 15  ? 1.8797 1.0010 0.9503 -0.5619 0.0112  0.0608  16  THR C CG2 
4489 N N   . LEU D 16  ? 1.7488 0.9720 0.8632 -0.4635 0.0458  -0.0189 17  LEU C N   
4490 C CA  . LEU D 16  ? 1.6235 0.8792 0.7706 -0.4352 0.0579  -0.0348 17  LEU C CA  
4491 C C   . LEU D 16  ? 1.6152 0.8709 0.7501 -0.4228 0.0744  -0.0448 17  LEU C C   
4492 O O   . LEU D 16  ? 1.6880 0.9357 0.7962 -0.4359 0.0889  -0.0449 17  LEU C O   
4493 C CB  . LEU D 16  ? 1.5644 0.8625 0.7417 -0.4360 0.0838  -0.0342 17  LEU C CB  
4494 C CG  . LEU D 16  ? 1.5420 0.8688 0.7498 -0.4005 0.0892  -0.0474 17  LEU C CG  
4495 C CD1 . LEU D 16  ? 1.5491 0.8593 0.7597 -0.3775 0.0568  -0.0542 17  LEU C CD1 
4496 C CD2 . LEU D 16  ? 1.5507 0.9154 0.7930 -0.4033 0.0895  -0.0487 17  LEU C CD2 
4497 N N   . SER D 17  ? 1.5665 0.8330 0.7228 -0.3967 0.0720  -0.0534 18  SER C N   
4498 C CA  . SER D 17  ? 1.5316 0.7975 0.6897 -0.3897 0.0850  -0.0611 18  SER C CA  
4499 C C   . SER D 17  ? 1.5514 0.8407 0.7418 -0.3605 0.0998  -0.0610 18  SER C C   
4500 O O   . SER D 17  ? 1.5395 0.8422 0.7416 -0.3378 0.0814  -0.0595 18  SER C O   
4501 C CB  . SER D 17  ? 1.4854 0.7349 0.6265 -0.3934 0.0561  -0.0655 18  SER C CB  
4502 O OG  . SER D 17  ? 1.4948 0.7635 0.6615 -0.3722 0.0519  -0.0693 18  SER C OG  
4503 N N   . GLY D 18  ? 1.4797 0.7705 0.6794 -0.3568 0.1320  -0.0618 19  GLY C N   
4504 C CA  . GLY D 18  ? 1.4544 0.7620 0.6783 -0.3266 0.1519  -0.0551 19  GLY C CA  
4505 C C   . GLY D 18  ? 1.5100 0.8037 0.7358 -0.3239 0.1878  -0.0546 19  GLY C C   
4506 O O   . GLY D 18  ? 1.5016 0.7701 0.7153 -0.3461 0.1947  -0.0638 19  GLY C O   
4507 N N   . TYR D 19  ? 1.5388 0.8457 0.7748 -0.2910 0.2084  -0.0453 20  TYR C N   
4508 C CA  . TYR D 19  ? 1.4786 0.7625 0.7130 -0.2800 0.2426  -0.0414 20  TYR C CA  
4509 C C   . TYR D 19  ? 1.4622 0.7669 0.6934 -0.2377 0.2595  -0.0345 20  TYR C C   
4510 O O   . TYR D 19  ? 1.4382 0.7767 0.6772 -0.2103 0.2478  -0.0296 20  TYR C O   
4511 C CB  . TYR D 19  ? 1.4664 0.7287 0.7222 -0.2854 0.2561  -0.0302 20  TYR C CB  
4512 C CG  . TYR D 19  ? 1.4808 0.7720 0.7573 -0.2564 0.2607  -0.0091 20  TYR C CG  
4513 C CD1 . TYR D 19  ? 1.4960 0.7960 0.7683 -0.2128 0.2849  0.0085  20  TYR C CD1 
4514 C CD2 . TYR D 19  ? 1.4670 0.7815 0.7625 -0.2664 0.2411  -0.0067 20  TYR C CD2 
4515 C CE1 . TYR D 19  ? 1.4739 0.8054 0.7584 -0.1799 0.2914  0.0299  20  TYR C CE1 
4516 C CE2 . TYR D 19  ? 1.4584 0.8085 0.7697 -0.2345 0.2469  0.0130  20  TYR C CE2 
4517 C CZ  . TYR D 19  ? 1.4953 0.8542 0.8000 -0.1910 0.2729  0.0323  20  TYR C CZ  
4518 O OH  . TYR D 19  ? 1.5132 0.9131 0.8271 -0.1525 0.2806  0.0539  20  TYR C OH  
4519 N N   . THR D 20  ? 1.4872 0.7717 0.7032 -0.2273 0.2844  -0.0377 21  THR C N   
4520 C CA  . THR D 20  ? 1.5118 0.8079 0.7194 -0.1804 0.3055  -0.0309 21  THR C CA  
4521 C C   . THR D 20  ? 1.5643 0.8052 0.7553 -0.1721 0.3362  -0.0268 21  THR C C   
4522 O O   . THR D 20  ? 1.5697 0.7681 0.7571 -0.2044 0.3373  -0.0358 21  THR C O   
4523 C CB  . THR D 20  ? 1.4753 0.8185 0.6780 -0.1675 0.2971  -0.0458 21  THR C CB  
4524 O OG1 . THR D 20  ? 1.5083 0.8829 0.7268 -0.1940 0.2653  -0.0528 21  THR C OG1 
4525 C CG2 . THR D 20  ? 1.4768 0.8528 0.6781 -0.1119 0.3055  -0.0416 21  THR C CG2 
4526 N N   . THR D 21  ? 1.5933 0.8314 0.7708 -0.1245 0.3584  -0.0153 22  THR C N   
4527 C CA  . THR D 21  ? 1.6340 0.8091 0.7902 -0.1079 0.3875  -0.0083 22  THR C CA  
4528 C C   . THR D 21  ? 1.6768 0.8698 0.8032 -0.0604 0.3986  -0.0180 22  THR C C   
4529 O O   . THR D 21  ? 1.6177 0.8788 0.7483 -0.0367 0.3864  -0.0260 22  THR C O   
4530 C CB  . THR D 21  ? 1.6665 0.8067 0.8307 -0.0901 0.4109  0.0252  22  THR C CB  
4531 O OG1 . THR D 21  ? 1.6566 0.8408 0.8095 -0.0342 0.4172  0.0395  22  THR C OG1 
4532 C CG2 . THR D 21  ? 1.6400 0.7853 0.8415 -0.1315 0.3999  0.0355  22  THR C CG2 
4533 N N   . THR D 22  ? 1.7406 0.8709 0.8390 -0.0466 0.4191  -0.0202 23  THR C N   
4534 C CA  . THR D 22  ? 1.7816 0.9150 0.8447 0.0097  0.4347  -0.0257 23  THR C CA  
4535 C C   . THR D 22  ? 1.8504 0.8823 0.8838 0.0173  0.4561  -0.0215 23  THR C C   
4536 O O   . THR D 22  ? 1.8802 0.8594 0.9206 -0.0270 0.4501  -0.0318 23  THR C O   
4537 C CB  . THR D 22  ? 1.7528 0.9562 0.8114 0.0124  0.4210  -0.0556 23  THR C CB  
4538 O OG1 . THR D 22  ? 1.6753 0.9633 0.7679 0.0008  0.3990  -0.0581 23  THR C OG1 
4539 C CG2 . THR D 22  ? 1.7769 0.9904 0.7997 0.0763  0.4372  -0.0637 23  THR C CG2 
4540 N N   . THR D 23  ? 1.9272 0.9271 0.9270 0.0752  0.4785  -0.0067 24  THR C N   
4541 C CA  . THR D 23  ? 2.0119 0.9025 0.9780 0.0894  0.4983  -0.0011 24  THR C CA  
4542 C C   . THR D 23  ? 2.0533 0.9503 0.9716 0.1399  0.5000  -0.0284 24  THR C C   
4543 O O   . THR D 23  ? 2.0175 0.9998 0.9277 0.1829  0.4972  -0.0364 24  THR C O   
4544 C CB  . THR D 23  ? 2.0700 0.9028 1.0265 0.1204  0.5267  0.0434  24  THR C CB  
4545 O OG1 . THR D 23  ? 2.0042 0.8914 1.0020 0.0995  0.5241  0.0677  24  THR C OG1 
4546 C CG2 . THR D 23  ? 2.1647 0.8712 1.1189 0.0920  0.5410  0.0556  24  THR C CG2 
4547 N N   . ALA D 24  ? 2.1313 0.9436 1.0205 0.1361  0.5016  -0.0462 25  ALA C N   
4548 C CA  . ALA D 24  ? 2.1857 1.0120 1.0278 0.1842  0.5005  -0.0774 25  ALA C CA  
4549 C C   . ALA D 24  ? 2.3048 1.0013 1.1070 0.1899  0.5042  -0.0900 25  ALA C C   
4550 O O   . ALA D 24  ? 2.3402 0.9361 1.1566 0.1566  0.5095  -0.0712 25  ALA C O   
4551 C CB  . ALA D 24  ? 2.2038 1.1372 1.0641 0.1595  0.4804  -0.1089 25  ALA C CB  
4552 N N   . VAL D 25  ? 2.4231 1.1264 1.1782 0.2326  0.4999  -0.1240 26  VAL C N   
4553 C CA  . VAL D 25  ? 2.4927 1.0685 1.1963 0.2565  0.5001  -0.1422 26  VAL C CA  
4554 C C   . VAL D 25  ? 2.6587 1.1929 1.3759 0.1987  0.4771  -0.1728 26  VAL C C   
4555 O O   . VAL D 25  ? 2.6351 1.0452 1.3545 0.1715  0.4728  -0.1721 26  VAL C O   
4556 C CB  . VAL D 25  ? 2.5167 1.1197 1.1565 0.3398  0.5044  -0.1674 26  VAL C CB  
4557 C CG1 . VAL D 25  ? 2.4873 1.1583 1.1223 0.3947  0.5216  -0.1420 26  VAL C CG1 
4558 C CG2 . VAL D 25  ? 2.5295 1.2487 1.1699 0.3374  0.4899  -0.2058 26  VAL C CG2 
4559 N N   . ASP D 26  ? 2.8398 1.4779 1.5693 0.1777  0.4616  -0.1986 27  ASP C N   
4560 C CA  . ASP D 26  ? 2.8417 1.4567 1.5751 0.1328  0.4381  -0.2305 27  ASP C CA  
4561 C C   . ASP D 26  ? 2.7261 1.4498 1.5100 0.0772  0.4278  -0.2241 27  ASP C C   
4562 O O   . ASP D 26  ? 2.6366 1.4682 1.4415 0.0835  0.4361  -0.2071 27  ASP C O   
4563 C CB  . ASP D 26  ? 2.8740 1.4898 1.5434 0.1815  0.4289  -0.2757 27  ASP C CB  
4564 C CG  . ASP D 26  ? 2.7867 1.5479 1.4441 0.2204  0.4392  -0.2803 27  ASP C CG  
4565 O OD1 . ASP D 26  ? 2.6884 1.5582 1.3849 0.1809  0.4359  -0.2732 27  ASP C OD1 
4566 O OD2 . ASP D 26  ? 2.8438 1.6101 1.4538 0.2908  0.4500  -0.2915 27  ASP C OD2 
4567 N N   . ALA D 27  ? 2.4981 1.1891 1.3004 0.0245  0.4066  -0.2403 28  ALA C N   
4568 C CA  . ALA D 27  ? 2.3814 1.1585 1.2262 -0.0275 0.3947  -0.2327 28  ALA C CA  
4569 C C   . ALA D 27  ? 2.3154 1.2108 1.1424 -0.0105 0.3961  -0.2424 28  ALA C C   
4570 O O   . ALA D 27  ? 2.2362 1.2152 1.0990 -0.0426 0.3933  -0.2248 28  ALA C O   
4571 C CB  . ALA D 27  ? 2.3044 1.0257 1.1633 -0.0772 0.3689  -0.2548 28  ALA C CB  
4572 N N   . ALA D 28  ? 2.3152 1.2206 1.0889 0.0401  0.4009  -0.2687 29  ALA C N   
4573 C CA  . ALA D 28  ? 2.2419 1.2712 1.0052 0.0554  0.4076  -0.2731 29  ALA C CA  
4574 C C   . ALA D 28  ? 2.2164 1.3365 1.0107 0.0736  0.4254  -0.2469 29  ALA C C   
4575 O O   . ALA D 28  ? 2.1122 1.3420 0.9337 0.0553  0.4281  -0.2365 29  ALA C O   
4576 C CB  . ALA D 28  ? 2.2393 1.2645 0.9364 0.1102  0.4089  -0.3094 29  ALA C CB  
4577 N N   . THR D 29  ? 2.2844 1.3590 1.0750 0.1102  0.4366  -0.2359 30  THR C N   
4578 C CA  . THR D 29  ? 2.1823 1.3399 1.0046 0.1292  0.4481  -0.2140 30  THR C CA  
4579 C C   . THR D 29  ? 2.1046 1.2827 0.9851 0.0747  0.4393  -0.1865 30  THR C C   
4580 O O   . THR D 29  ? 1.9998 1.2766 0.9181 0.0661  0.4378  -0.1758 30  THR C O   
4581 C CB  . THR D 29  ? 2.2672 1.3650 1.0593 0.1909  0.4619  -0.2088 30  THR C CB  
4582 O OG1 . THR D 29  ? 2.4085 1.3621 1.1717 0.1878  0.4597  -0.2113 30  THR C OG1 
4583 C CG2 . THR D 29  ? 2.1925 1.3486 0.9434 0.2601  0.4721  -0.2315 30  THR C CG2 
4584 N N   . ALA D 30  ? 2.1144 1.2015 1.0053 0.0383  0.4316  -0.1768 31  ALA C N   
4585 C CA  . ALA D 30  ? 2.0452 1.1540 0.9869 -0.0128 0.4205  -0.1547 31  ALA C CA  
4586 C C   . ALA D 30  ? 1.9781 1.1575 0.9366 -0.0561 0.4052  -0.1620 31  ALA C C   
4587 O O   . ALA D 30  ? 1.8968 1.1462 0.8926 -0.0776 0.3981  -0.1474 31  ALA C O   
4588 C CB  . ALA D 30  ? 2.0556 1.0619 1.0081 -0.0426 0.4169  -0.1448 31  ALA C CB  
4589 N N   . GLU D 31  ? 2.0075 1.1666 0.9349 -0.0657 0.3990  -0.1848 32  GLU C N   
4590 C CA  . GLU D 31  ? 1.9581 1.1797 0.8933 -0.1030 0.3876  -0.1862 32  GLU C CA  
4591 C C   . GLU D 31  ? 1.9102 1.2444 0.8557 -0.0894 0.3987  -0.1800 32  GLU C C   
4592 O O   . GLU D 31  ? 1.8653 1.2585 0.8319 -0.1256 0.3918  -0.1687 32  GLU C O   
4593 C CB  . GLU D 31  ? 2.0052 1.1847 0.8970 -0.1078 0.3780  -0.2134 32  GLU C CB  
4594 C CG  . GLU D 31  ? 2.0229 1.2446 0.8664 -0.0644 0.3905  -0.2344 32  GLU C CG  
4595 C CD  . GLU D 31  ? 2.0201 1.2363 0.8228 -0.0737 0.3782  -0.2563 32  GLU C CD  
4596 O OE1 . GLU D 31  ? 2.0199 1.1695 0.8231 -0.1044 0.3567  -0.2665 32  GLU C OE1 
4597 O OE2 . GLU D 31  ? 2.0744 1.3598 0.8442 -0.0471 0.3903  -0.2638 32  GLU C OE2 
4598 N N   . LYS D 32  ? 1.9495 1.3160 0.8843 -0.0387 0.4152  -0.1860 33  LYS C N   
4599 C CA  . LYS D 32  ? 1.8827 1.3695 0.8409 -0.0285 0.4251  -0.1814 33  LYS C CA  
4600 C C   . LYS D 32  ? 1.8324 1.3679 0.8507 -0.0524 0.4155  -0.1609 33  LYS C C   
4601 O O   . LYS D 32  ? 1.8241 1.4374 0.8792 -0.0863 0.4108  -0.1505 33  LYS C O   
4602 C CB  . LYS D 32  ? 1.8857 1.4013 0.8146 0.0386  0.4429  -0.1984 33  LYS C CB  
4603 N N   . VAL D 33  ? 1.7825 1.2713 0.8100 -0.0335 0.4122  -0.1543 34  VAL C N   
4604 C CA  . VAL D 33  ? 1.7478 1.2813 0.8261 -0.0483 0.3987  -0.1399 34  VAL C CA  
4605 C C   . VAL D 33  ? 1.7050 1.2187 0.8070 -0.1089 0.3788  -0.1268 34  VAL C C   
4606 O O   . VAL D 33  ? 1.6411 1.2143 0.7837 -0.1374 0.3645  -0.1195 34  VAL C O   
4607 C CB  . VAL D 33  ? 1.7892 1.2805 0.8627 -0.0055 0.4018  -0.1335 34  VAL C CB  
4608 C CG1 . VAL D 33  ? 1.7795 1.3193 0.8387 0.0594  0.4159  -0.1456 34  VAL C CG1 
4609 C CG2 . VAL D 33  ? 1.8229 1.1971 0.8644 -0.0064 0.4079  -0.1263 34  VAL C CG2 
4610 N N   . PHE D 34  ? 1.7479 1.1764 0.8262 -0.1287 0.3751  -0.1256 35  PHE C N   
4611 C CA  . PHE D 34  ? 1.7106 1.1207 0.8043 -0.1803 0.3550  -0.1163 35  PHE C CA  
4612 C C   . PHE D 34  ? 1.6831 1.1571 0.7855 -0.2121 0.3500  -0.1133 35  PHE C C   
4613 O O   . PHE D 34  ? 1.6428 1.1372 0.7746 -0.2457 0.3318  -0.1007 35  PHE C O   
4614 C CB  . PHE D 34  ? 1.7310 1.0554 0.7964 -0.1939 0.3527  -0.1236 35  PHE C CB  
4615 C CG  . PHE D 34  ? 1.7001 0.9601 0.7768 -0.1875 0.3527  -0.1147 35  PHE C CG  
4616 C CD1 . PHE D 34  ? 1.6720 0.9478 0.7676 -0.1587 0.3591  -0.1007 35  PHE C CD1 
4617 C CD2 . PHE D 34  ? 1.7015 0.8890 0.7704 -0.2080 0.3476  -0.1205 35  PHE C CD2 
4618 C CE1 . PHE D 34  ? 1.6751 0.8967 0.7786 -0.1505 0.3649  -0.0859 35  PHE C CE1 
4619 C CE2 . PHE D 34  ? 1.6965 0.8319 0.7838 -0.2065 0.3523  -0.1071 35  PHE C CE2 
4620 C CZ  . PHE D 34  ? 1.6764 0.8294 0.7791 -0.1774 0.3635  -0.0867 35  PHE C CZ  
4621 N N   . LYS D 35  ? 1.7116 1.2170 0.7863 -0.1988 0.3669  -0.1232 36  LYS C N   
4622 C CA  . LYS D 35  ? 1.6655 1.2435 0.7483 -0.2246 0.3709  -0.1140 36  LYS C CA  
4623 C C   . LYS D 35  ? 1.6324 1.2911 0.7732 -0.2356 0.3668  -0.1024 36  LYS C C   
4624 O O   . LYS D 35  ? 1.5994 1.2815 0.7683 -0.2788 0.3543  -0.0856 36  LYS C O   
4625 C CB  . LYS D 35  ? 1.7110 1.3238 0.7543 -0.1934 0.3945  -0.1273 36  LYS C CB  
4626 N N   . GLN D 36  ? 1.6141 1.3148 0.7729 -0.1949 0.3754  -0.1129 37  GLN C N   
4627 C CA  . GLN D 36  ? 1.5482 1.3292 0.7678 -0.2008 0.3662  -0.1098 37  GLN C CA  
4628 C C   . GLN D 36  ? 1.5345 1.2802 0.7852 -0.2297 0.3358  -0.1011 37  GLN C C   
4629 O O   . GLN D 36  ? 1.4990 1.2999 0.8028 -0.2500 0.3193  -0.0986 37  GLN C O   
4630 C CB  . GLN D 36  ? 1.5908 1.4101 0.8143 -0.1409 0.3760  -0.1272 37  GLN C CB  
4631 C CG  . GLN D 36  ? 1.6134 1.5488 0.8629 -0.1243 0.3933  -0.1352 37  GLN C CG  
4632 C CD  . GLN D 36  ? 1.6503 1.6370 0.9182 -0.0669 0.3923  -0.1537 37  GLN C CD  
4633 O OE1 . GLN D 36  ? 1.6818 1.6108 0.9354 -0.0363 0.3814  -0.1575 37  GLN C OE1 
4634 N NE2 . GLN D 36  ? 1.6321 1.7326 0.9295 -0.0480 0.4054  -0.1642 37  GLN C NE2 
4635 N N   . TYR D 37  ? 1.5571 1.2141 0.7782 -0.2307 0.3266  -0.0985 38  TYR C N   
4636 C CA  . TYR D 37  ? 1.5349 1.1547 0.7749 -0.2561 0.2981  -0.0900 38  TYR C CA  
4637 C C   . TYR D 37  ? 1.5460 1.1442 0.7797 -0.3082 0.2863  -0.0762 38  TYR C C   
4638 O O   . TYR D 37  ? 1.5538 1.0953 0.7775 -0.3242 0.2673  -0.0711 38  TYR C O   
4639 C CB  . TYR D 37  ? 1.5483 1.0964 0.7639 -0.2299 0.2978  -0.0913 38  TYR C CB  
4640 C CG  . TYR D 37  ? 1.4778 1.0051 0.7136 -0.2347 0.2713  -0.0855 38  TYR C CG  
4641 C CD1 . TYR D 37  ? 1.4988 1.0701 0.7669 -0.2117 0.2554  -0.0912 38  TYR C CD1 
4642 C CD2 . TYR D 37  ? 1.4769 0.9459 0.6988 -0.2569 0.2600  -0.0780 38  TYR C CD2 
4643 C CE1 . TYR D 37  ? 1.4388 0.9929 0.7192 -0.2081 0.2286  -0.0891 38  TYR C CE1 
4644 C CE2 . TYR D 37  ? 1.5014 0.9587 0.7388 -0.2549 0.2359  -0.0736 38  TYR C CE2 
4645 C CZ  . TYR D 37  ? 1.4473 0.9452 0.7109 -0.2288 0.2204  -0.0790 38  TYR C CZ  
4646 O OH  . TYR D 37  ? 1.4012 0.8884 0.6735 -0.2192 0.1947  -0.0777 38  TYR C OH  
4647 N N   . ALA D 38  ? 1.5233 1.1687 0.7595 -0.3315 0.2991  -0.0681 39  ALA C N   
4648 C CA  . ALA D 38  ? 1.5066 1.1358 0.7346 -0.3781 0.2898  -0.0492 39  ALA C CA  
4649 C C   . ALA D 38  ? 1.5461 1.2221 0.8305 -0.4111 0.2737  -0.0369 39  ALA C C   
4650 O O   . ALA D 38  ? 1.5121 1.2478 0.8175 -0.4354 0.2890  -0.0224 39  ALA C O   
4651 C CB  . ALA D 38  ? 1.6463 1.2936 0.8342 -0.3811 0.3166  -0.0432 39  ALA C CB  
4652 N N   . PHE D 39  ? 1.5139 1.1638 0.8255 -0.4115 0.2418  -0.0430 40  PHE C N   
4653 C CA  . PHE D 39  ? 1.4951 1.1590 0.8537 -0.4492 0.2155  -0.0334 40  PHE C CA  
4654 C C   . PHE D 39  ? 1.5325 1.1571 0.8655 -0.4942 0.2137  -0.0063 40  PHE C C   
4655 O O   . PHE D 39  ? 1.5517 1.1122 0.8720 -0.5085 0.1837  -0.0014 40  PHE C O   
4656 C CB  . PHE D 39  ? 1.4958 1.1191 0.8683 -0.4356 0.1768  -0.0471 40  PHE C CB  
4657 C CG  . PHE D 39  ? 1.4918 1.0542 0.8176 -0.4066 0.1754  -0.0528 40  PHE C CG  
4658 C CD1 . PHE D 39  ? 1.5119 1.0177 0.7941 -0.4259 0.1751  -0.0403 40  PHE C CD1 
4659 C CD2 . PHE D 39  ? 1.4829 1.0462 0.8117 -0.3608 0.1713  -0.0693 40  PHE C CD2 
4660 C CE1 . PHE D 39  ? 1.5561 1.0153 0.8072 -0.4045 0.1729  -0.0466 40  PHE C CE1 
4661 C CE2 . PHE D 39  ? 1.5066 1.0188 0.8015 -0.3401 0.1729  -0.0694 40  PHE C CE2 
4662 C CZ  . PHE D 39  ? 1.5562 1.0187 0.8173 -0.3648 0.1728  -0.0593 40  PHE C CZ  
4663 N N   . GLY D 40  ? 1.5388 1.2006 0.8565 -0.5099 0.2459  0.0117  41  GLY C N   
4664 C CA  . GLY D 40  ? 1.5851 1.2128 0.8700 -0.5463 0.2484  0.0416  41  GLY C CA  
4665 C C   . GLY D 40  ? 1.6122 1.1653 0.8263 -0.5325 0.2423  0.0390  41  GLY C C   
4666 O O   . GLY D 40  ? 1.7252 1.2504 0.9002 -0.5542 0.2451  0.0628  41  GLY C O   
4667 N N   . ASN D 41  ? 1.6007 1.1223 0.7981 -0.4971 0.2342  0.0123  42  ASN C N   
4668 C CA  . ASN D 41  ? 1.7440 1.2083 0.8828 -0.4862 0.2308  0.0063  42  ASN C CA  
4669 C C   . ASN D 41  ? 1.8542 1.3422 0.9503 -0.4717 0.2630  0.0038  42  ASN C C   
4670 O O   . ASN D 41  ? 1.9123 1.3757 0.9582 -0.4785 0.2641  0.0127  42  ASN C O   
4671 C CB  . ASN D 41  ? 1.6511 1.0786 0.7943 -0.4585 0.2148  -0.0176 42  ASN C CB  
4672 C CG  . ASN D 41  ? 1.6951 1.0660 0.7945 -0.4557 0.2022  -0.0250 42  ASN C CG  
4673 O OD1 . ASN D 41  ? 1.7038 1.0679 0.7613 -0.4541 0.2151  -0.0277 42  ASN C OD1 
4674 N ND2 . ASN D 41  ? 1.7236 1.0597 0.8329 -0.4533 0.1744  -0.0299 42  ASN C ND2 
4675 N N   . GLY D 42  ? 1.7636 1.3017 0.8747 -0.4466 0.2876  -0.0093 43  GLY C N   
4676 C CA  . GLY D 42  ? 1.8497 1.4086 0.9174 -0.4214 0.3153  -0.0192 43  GLY C CA  
4677 C C   . GLY D 42  ? 1.9085 1.4897 0.9348 -0.4356 0.3313  0.0027  43  GLY C C   
4678 O O   . GLY D 42  ? 1.9267 1.4983 0.8971 -0.4111 0.3421  -0.0107 43  GLY C O   
4679 N N   . VAL D 43  ? 2.0365 1.6448 1.0889 -0.4734 0.3319  0.0366  44  VAL C N   
4680 C CA  . VAL D 43  ? 2.0766 1.7072 1.0900 -0.4896 0.3513  0.0685  44  VAL C CA  
4681 C C   . VAL D 43  ? 2.1802 1.7455 1.1167 -0.4750 0.3380  0.0603  44  VAL C C   
4682 O O   . VAL D 43  ? 2.2180 1.8037 1.0968 -0.4523 0.3579  0.0602  44  VAL C O   
4683 C CB  . VAL D 43  ? 2.0602 1.6983 1.1161 -0.5401 0.3453  0.1089  44  VAL C CB  
4684 N N   . ASP D 44  ? 2.1273 1.6194 1.0613 -0.4838 0.3022  0.0508  45  ASP C N   
4685 C CA  . ASP D 44  ? 2.1718 1.6066 1.0429 -0.4677 0.2832  0.0345  45  ASP C CA  
4686 C C   . ASP D 44  ? 2.1261 1.5313 1.0097 -0.4429 0.2695  -0.0090 45  ASP C C   
4687 O O   . ASP D 44  ? 2.0988 1.4612 1.0062 -0.4492 0.2425  -0.0202 45  ASP C O   
4688 C CB  . ASP D 44  ? 2.1625 1.5431 1.0212 -0.4921 0.2534  0.0551  45  ASP C CB  
4689 C CG  . ASP D 44  ? 2.1949 1.5391 0.9762 -0.4756 0.2410  0.0503  45  ASP C CG  
4690 O OD1 . ASP D 44  ? 2.2565 1.6132 0.9964 -0.4454 0.2508  0.0252  45  ASP C OD1 
4691 O OD2 . ASP D 44  ? 2.2026 1.5036 0.9616 -0.4890 0.2181  0.0692  45  ASP C OD2 
4692 N N   . GLY D 45  ? 2.1574 1.5866 1.0245 -0.4129 0.2902  -0.0317 46  GLY C N   
4693 C CA  . GLY D 45  ? 2.0665 1.4625 0.9454 -0.3905 0.2824  -0.0687 46  GLY C CA  
4694 C C   . GLY D 45  ? 2.0829 1.4457 0.9075 -0.3648 0.2753  -0.1018 46  GLY C C   
4695 O O   . GLY D 45  ? 2.0233 1.4139 0.8091 -0.3376 0.2949  -0.1119 46  GLY C O   
4696 N N   . GLU D 46  ? 2.2280 1.5357 1.0514 -0.3712 0.2454  -0.1218 47  GLU C N   
4697 C CA  . GLU D 46  ? 2.2810 1.5533 1.0648 -0.3494 0.2318  -0.1615 47  GLU C CA  
4698 C C   . GLU D 46  ? 2.2863 1.5422 1.0828 -0.3256 0.2446  -0.1889 47  GLU C C   
4699 O O   . GLU D 46  ? 2.3531 1.6007 1.1043 -0.2960 0.2468  -0.2175 47  GLU C O   
4700 C CB  . GLU D 46  ? 2.2717 1.4986 1.0683 -0.3656 0.1960  -0.1782 47  GLU C CB  
4701 N N   . TRP D 47  ? 1.9804 1.2275 0.8324 -0.3330 0.2516  -0.1812 48  TRP C N   
4702 C CA  . TRP D 47  ? 2.0010 1.2303 0.8624 -0.3070 0.2679  -0.1987 48  TRP C CA  
4703 C C   . TRP D 47  ? 2.0508 1.2142 0.8913 -0.2940 0.2510  -0.2405 48  TRP C C   
4704 O O   . TRP D 47  ? 2.0494 1.2028 0.8464 -0.2614 0.2569  -0.2665 48  TRP C O   
4705 C CB  . TRP D 47  ? 2.0172 1.3054 0.8537 -0.2791 0.2974  -0.1909 48  TRP C CB  
4706 C CG  . TRP D 47  ? 1.9713 1.3017 0.8537 -0.2783 0.3169  -0.1674 48  TRP C CG  
4707 C CD1 . TRP D 47  ? 1.9328 1.2661 0.8672 -0.3026 0.3096  -0.1460 48  TRP C CD1 
4708 C CD2 . TRP D 47  ? 1.9770 1.3571 0.8560 -0.2456 0.3436  -0.1677 48  TRP C CD2 
4709 N NE1 . TRP D 47  ? 1.8853 1.2659 0.8495 -0.2878 0.3282  -0.1346 48  TRP C NE1 
4710 C CE2 . TRP D 47  ? 1.9178 1.3305 0.8511 -0.2539 0.3497  -0.1471 48  TRP C CE2 
4711 C CE3 . TRP D 47  ? 2.0067 1.4115 0.8401 -0.2048 0.3611  -0.1863 48  TRP C CE3 
4712 C CZ2 . TRP D 47  ? 1.8598 1.3320 0.8072 -0.2252 0.3718  -0.1450 48  TRP C CZ2 
4713 C CZ3 . TRP D 47  ? 1.9571 1.4224 0.8037 -0.1753 0.3855  -0.1821 48  TRP C CZ3 
4714 C CH2 . TRP D 47  ? 1.8692 1.3691 0.7744 -0.1868 0.3903  -0.1618 48  TRP C CH2 
4715 N N   . THR D 48  ? 2.0022 1.1224 0.8772 -0.3193 0.2281  -0.2486 49  THR C N   
4716 C CA  . THR D 48  ? 1.9823 1.0391 0.8540 -0.3172 0.2075  -0.2891 49  THR C CA  
4717 C C   . THR D 48  ? 2.0062 1.0141 0.8973 -0.3014 0.2237  -0.2970 49  THR C C   
4718 O O   . THR D 48  ? 1.9439 0.9426 0.8843 -0.3139 0.2355  -0.2729 49  THR C O   
4719 C CB  . THR D 48  ? 1.9474 0.9849 0.8627 -0.3524 0.1799  -0.2933 49  THR C CB  
4720 O OG1 . THR D 48  ? 1.9028 0.9159 0.8799 -0.3675 0.1906  -0.2771 49  THR C OG1 
4721 C CG2 . THR D 48  ? 1.9829 1.0708 0.8940 -0.3686 0.1714  -0.2661 49  THR C CG2 
4722 N N   . ASP D 50  ? 2.1913 0.9701 1.2266 -0.3361 0.2365  -0.3004 51  ASP C N   
4723 C CA  . ASP D 50  ? 2.3384 1.0390 1.4203 -0.3640 0.2265  -0.3135 51  ASP C CA  
4724 C C   . ASP D 50  ? 2.4451 1.0773 1.5330 -0.3450 0.2558  -0.2926 51  ASP C C   
4725 O O   . ASP D 50  ? 2.3832 1.0435 1.4862 -0.3350 0.2843  -0.2495 51  ASP C O   
4726 C CB  . ASP D 50  ? 2.2484 0.9829 1.4005 -0.4102 0.2175  -0.2944 51  ASP C CB  
4727 C CG  . ASP D 50  ? 2.3118 0.9874 1.5216 -0.4476 0.1980  -0.3170 51  ASP C CG  
4728 O OD1 . ASP D 50  ? 2.3724 0.9848 1.6103 -0.4456 0.2123  -0.3062 51  ASP C OD1 
4729 O OD2 . ASP D 50  ? 2.2548 0.9745 1.4975 -0.4689 0.1634  -0.3392 51  ASP C OD2 
4730 N N   . ASP D 51  ? 2.7424 1.2797 1.8153 -0.3372 0.2464  -0.3244 52  ASP C N   
4731 C CA  . ASP D 51  ? 2.8050 1.2623 1.8692 -0.3115 0.2733  -0.3056 52  ASP C CA  
4732 C C   . ASP D 51  ? 2.8162 1.2180 1.9541 -0.3528 0.2863  -0.2740 52  ASP C C   
4733 O O   . ASP D 51  ? 2.8185 1.2090 1.9642 -0.3369 0.3213  -0.2276 52  ASP C O   
4734 C CB  . ASP D 51  ? 2.9049 1.2746 1.9123 -0.2779 0.2570  -0.3533 52  ASP C CB  
4735 C CG  . ASP D 51  ? 3.0168 1.3471 1.9729 -0.2202 0.2865  -0.3366 52  ASP C CG  
4736 O OD1 . ASP D 51  ? 3.0193 1.3129 2.0026 -0.2213 0.3152  -0.2931 52  ASP C OD1 
4737 O OD2 . ASP D 51  ? 3.0729 1.4138 1.9594 -0.1697 0.2818  -0.3661 52  ASP C OD2 
4738 N N   . ALA D 52  ? 2.5762 0.9838 1.7872 -0.3942 0.2535  -0.2911 53  ALA C N   
4739 C CA  . ALA D 52  ? 2.4943 0.8958 1.8008 -0.4312 0.2618  -0.2540 53  ALA C CA  
4740 C C   . ALA D 52  ? 2.4618 0.9276 1.7901 -0.4401 0.2969  -0.1995 53  ALA C C   
4741 O O   . ALA D 52  ? 2.4856 0.9232 1.8173 -0.4253 0.3345  -0.1532 53  ALA C O   
4742 C CB  . ALA D 52  ? 2.4043 0.8349 1.7915 -0.4753 0.2171  -0.2853 53  ALA C CB  
4743 N N   . THR D 53  ? 2.3445 0.8963 1.6811 -0.4580 0.2834  -0.2053 54  THR C N   
4744 C CA  . THR D 53  ? 2.2960 0.9159 1.6513 -0.4641 0.3074  -0.1619 54  THR C CA  
4745 C C   . THR D 53  ? 2.3034 0.9472 1.5948 -0.4143 0.3342  -0.1376 54  THR C C   
4746 O O   . THR D 53  ? 2.2092 0.9156 1.5180 -0.4058 0.3521  -0.0989 54  THR C O   
4747 C CB  . THR D 53  ? 2.2581 0.9611 1.6376 -0.4920 0.2751  -0.1826 54  THR C CB  
4748 O OG1 . THR D 53  ? 2.2221 0.9626 1.5304 -0.4657 0.2631  -0.2027 54  THR C OG1 
4749 C CG2 . THR D 53  ? 2.1832 0.8809 1.6204 -0.5228 0.2346  -0.2217 54  THR C CG2 
4750 N N   . LYS D 54  ? 2.3459 0.9570 1.5710 -0.3750 0.3338  -0.1600 55  LYS C N   
4751 C CA  . LYS D 54  ? 2.3232 0.9791 1.4984 -0.3239 0.3534  -0.1420 55  LYS C CA  
4752 C C   . LYS D 54  ? 2.1968 0.9607 1.3791 -0.3273 0.3450  -0.1308 55  LYS C C   
4753 O O   . LYS D 54  ? 2.1861 0.9966 1.3712 -0.3045 0.3633  -0.0981 55  LYS C O   
4754 C CB  . LYS D 54  ? 2.3037 0.9204 1.4791 -0.2939 0.3907  -0.0992 55  LYS C CB  
4755 N N   . THR D 55  ? 2.1471 0.9463 1.3292 -0.3534 0.3146  -0.1596 56  THR C N   
4756 C CA  . THR D 55  ? 2.0619 0.9487 1.2373 -0.3545 0.3023  -0.1540 56  THR C CA  
4757 C C   . THR D 55  ? 2.0157 0.9239 1.1381 -0.3429 0.2869  -0.1841 56  THR C C   
4758 O O   . THR D 55  ? 2.0980 0.9656 1.1985 -0.3477 0.2712  -0.2188 56  THR C O   
4759 C CB  . THR D 55  ? 2.0430 0.9648 1.2653 -0.3937 0.2813  -0.1511 56  THR C CB  
4760 O OG1 . THR D 55  ? 2.0274 0.9401 1.2392 -0.4162 0.2505  -0.1897 56  THR C OG1 
4761 C CG2 . THR D 55  ? 2.0936 0.9919 1.3762 -0.4132 0.2960  -0.1267 56  THR C CG2 
4762 N N   . PHE D 56  ? 1.9218 0.8961 1.0251 -0.3268 0.2912  -0.1703 57  PHE C N   
4763 C CA  . PHE D 56  ? 1.8511 0.8624 0.9093 -0.3179 0.2829  -0.1873 57  PHE C CA  
4764 C C   . PHE D 56  ? 1.7663 0.8409 0.8350 -0.3378 0.2686  -0.1713 57  PHE C C   
4765 O O   . PHE D 56  ? 1.6888 0.8002 0.7803 -0.3331 0.2757  -0.1458 57  PHE C O   
4766 C CB  . PHE D 56  ? 1.8218 0.8497 0.8477 -0.2766 0.3063  -0.1852 57  PHE C CB  
4767 N N   . THR D 57  ? 1.8139 0.8962 0.8621 -0.3561 0.2462  -0.1878 58  THR C N   
4768 C CA  . THR D 57  ? 1.7207 0.8427 0.7737 -0.3769 0.2271  -0.1748 58  THR C CA  
4769 C C   . THR D 57  ? 1.7771 0.9375 0.7851 -0.3717 0.2278  -0.1719 58  THR C C   
4770 O O   . THR D 57  ? 1.8207 0.9742 0.7861 -0.3587 0.2302  -0.1920 58  THR C O   
4771 C CB  . THR D 57  ? 1.7251 0.8255 0.7908 -0.4008 0.1991  -0.1929 58  THR C CB  
4772 O OG1 . THR D 57  ? 1.7149 0.7926 0.8339 -0.4114 0.2019  -0.1880 58  THR C OG1 
4773 C CG2 . THR D 57  ? 1.7310 0.8657 0.7888 -0.4147 0.1771  -0.1816 58  THR C CG2 
4774 N N   . VAL D 58  ? 1.7752 0.9753 0.7931 -0.3814 0.2251  -0.1461 59  VAL C N   
4775 C CA  . VAL D 58  ? 1.7681 1.0053 0.7534 -0.3857 0.2268  -0.1334 59  VAL C CA  
4776 C C   . VAL D 58  ? 1.7828 1.0139 0.7606 -0.4076 0.1991  -0.1252 59  VAL C C   
4777 O O   . VAL D 58  ? 1.7665 0.9888 0.7779 -0.4170 0.1831  -0.1191 59  VAL C O   
4778 C CB  . VAL D 58  ? 1.6782 0.9618 0.6875 -0.3820 0.2443  -0.1099 59  VAL C CB  
4779 C CG1 . VAL D 58  ? 1.7424 1.0670 0.7268 -0.3915 0.2517  -0.0930 59  VAL C CG1 
4780 C CG2 . VAL D 58  ? 1.6887 0.9771 0.7096 -0.3540 0.2678  -0.1186 59  VAL C CG2 
4781 N N   . THR D 59  ? 1.8635 1.1007 0.7926 -0.4101 0.1937  -0.1242 60  THR C N   
4782 C CA  . THR D 59  ? 1.8388 1.0646 0.7491 -0.4244 0.1665  -0.1160 60  THR C CA  
4783 C C   . THR D 59  ? 1.9299 1.1783 0.8014 -0.4307 0.1753  -0.0867 60  THR C C   
4784 O O   . THR D 59  ? 1.9794 1.2575 0.8298 -0.4216 0.2018  -0.0806 60  THR C O   
4785 C CB  . THR D 59  ? 1.7915 0.9906 0.6752 -0.4183 0.1438  -0.1482 60  THR C CB  
4786 O OG1 . THR D 59  ? 1.8104 0.9894 0.7283 -0.4134 0.1465  -0.1759 60  THR C OG1 
4787 C CG2 . THR D 59  ? 1.7611 0.9488 0.6491 -0.4291 0.1113  -0.1453 60  THR C CG2 
4788 N N   . GLU D 60  ? 1.9306 1.1649 0.7927 -0.4453 0.1539  -0.0666 61  GLU C N   
4789 C CA  . GLU D 60  ? 1.9983 1.2440 0.8315 -0.4583 0.1626  -0.0297 61  GLU C CA  
4790 C C   . GLU D 60  ? 2.0579 1.2788 0.8241 -0.4538 0.1452  -0.0215 61  GLU C C   
4791 O O   . GLU D 60  ? 2.0535 1.2905 0.7662 -0.4418 0.1625  -0.0147 61  GLU C O   
4792 C CB  . GLU D 60  ? 1.9738 1.2160 0.8527 -0.4801 0.1538  -0.0048 61  GLU C CB  
4793 C CG  . GLU D 60  ? 1.9148 1.1936 0.8530 -0.4830 0.1735  -0.0044 61  GLU C CG  
4794 C CD  . GLU D 60  ? 1.9033 1.1963 0.8731 -0.5085 0.1740  0.0266  61  GLU C CD  
4795 O OE1 . GLU D 60  ? 1.8391 1.0969 0.8191 -0.5200 0.1445  0.0352  61  GLU C OE1 
4796 O OE2 . GLU D 60  ? 1.8878 1.2293 0.8758 -0.5163 0.2023  0.0401  61  GLU C OE2 
4797 N N   . LYS D 61  ? 2.0354 1.2203 0.7995 -0.4579 0.1110  -0.0208 62  LYS C N   
4798 C CA  . LYS D 61  ? 2.0253 1.1789 0.7273 -0.4507 0.0873  -0.0097 62  LYS C CA  
4799 C C   . LYS D 61  ? 2.0370 1.1745 0.7194 -0.4703 0.0959  0.0406  62  LYS C C   
4800 O O   . LYS D 61  ? 2.0701 1.2377 0.7602 -0.4842 0.1300  0.0662  62  LYS C O   
4801 C CB  . LYS D 61  ? 2.0296 1.1912 0.6661 -0.4249 0.0894  -0.0291 62  LYS C CB  
4802 N N   . PRO D 62  ? 2.0841 1.1743 0.7433 -0.4723 0.0654  0.0566  63  PRO C N   
4803 C CA  . PRO D 62  ? 2.1029 1.1585 0.7497 -0.4955 0.0670  0.1052  63  PRO C CA  
4804 C C   . PRO D 62  ? 2.1159 1.1882 0.7189 -0.5049 0.1047  0.1465  63  PRO C C   
4805 O O   . PRO D 62  ? 2.1976 1.2267 0.7455 -0.5077 0.1001  0.1842  63  PRO C O   
4806 C CB  . PRO D 62  ? 2.0955 1.0919 0.6923 -0.4780 0.0251  0.1057  63  PRO C CB  
4807 C CG  . PRO D 62  ? 2.1064 1.1187 0.7341 -0.4569 -0.0016 0.0556  63  PRO C CG  
4808 C CD  . PRO D 62  ? 2.0362 1.1025 0.6837 -0.4510 0.0247  0.0261  63  PRO C CD  
# 
